Datasets:

lhallee

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SwissProt

like 0

A0A0N9E2K8

MMP21_DANRE

MLTVIRRIFIIQTFIFITAEKIFHSRDHSDVLNNIHQAELITDTDTAQRFLSKYGFIKAAGSEESQLSESSGDLDFSLSLDLHEGGTTSGSSSSDLQFVSALRDFQRLSDLPVTGVFDDATKAAMNKPRCGVMDDDQELKDVTGSNSTRNHIRTSTNTSHNHEHQAPVRKKRHLSALLKNTSLQKRDVSKWTGHMAFSKSVLKWRLIGEGYSSQLSIQEQKYIFRLAFRMWSEISPLQFIEDLHSPLENIDIRLGFGTGRHLGCSQRFDGAGREFAHAWFLGDIHFDDDEHFTVPNTGSGISLLKVAVHEIGHVLGLPHIYRPGSIMQPSYLPQDAGFEIDWMDRKSIQRLYGVCTGRFSTVFDWIRKEQTPYGEVVVRFNTYFMRDGLYWLYENRNNRTRYGDPVAVQVGWHGLPSGGVDAYVHVWNRKTDAVYFFKGMQYWRYDSENDHVFSHAPDGRLYPRLISEDFPGVSGPLDTAYYDRRDAHIYFFKGSQVFRFDVRMRRLASSSPQEMTEVFPAIVSGDHPVRSLDAAYFSYTHNTVFLLKGSLFWRVLSGKERRRRAFLPMNGLLAHRRVHEQWFDICDVHSSSLRTTRRR

3.4.24.-

collagen catabolic process [GO:0030574]; determination of heart left/right asymmetry [GO:0061371]; determination of left/right symmetry [GO:0007368]; embryonic heart tube left/right pattern formation [GO:0060971]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; regulation of heart looping [GO:1901207]

extracellular matrix [GO:0031012]; extracellular space [GO:0005615]

metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]

PF00045;PF00413;PF01471;

3.40.390.10;2.110.10.10;

Peptidase M10A family

PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.

FUNCTION: Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway. {ECO:0000269|PubMed:26429889, ECO:0000269|PubMed:26437028}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0N9HMN6

POMT3_SINHE

MEMAPTMDLEIRNGNGYGDSGEELLAAQAHIYNHIFNFISSMALKCAVELNIPEILHNHQPKAVTLSELVQALQIPQAKSACLYRLLRILVHSGFFAITKIQSEGDEEGYLPTLSSKLLLKNHPMSMSPCLLGLVNPTMVAPMHFFSDWFKRSDDMTPFEATHGASLWKYFGETPHMAEIFNEAMGCETRLAMSVVLKECKGKLEGISSLVDVGGGTGNVGRAIAEAFPNVKCTVLDLPQVVGNLKGSNNLEFVSGDMFQFIPPADVVFLKWILHDWNDEECIKILKRCKEAIPSKEEGGKLIIIDMVVNDHNKGSYESTETQLFYDLTLMALLTGTERTETEWKKLFVAAGFTSYIISPVLGLKSIIEVFP

2.1.1.323

aromatic compound biosynthetic process [GO:0019438]; melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259]; phenylpropanoid biosynthetic process [GO:0009699]; response to wounding [GO:0009611]

acetylserotonin O-methyltransferase activity [GO:0017096]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

PF08100;PF00891;

3.40.50.150;1.10.10.10;

Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family, COMT subfamily

CATALYTIC ACTIVITY: Reaction=(-)-pluviatolide + S-adenosyl-L-methionine = (-)-bursehernin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:49036, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90893, ChEBI:CHEBI:90896; EC=2.1.1.323; Evidence={ECO:0000269|PubMed:26359402}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49037; Evidence={ECO:0000269|PubMed:26359402};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 uM for (-)-pluviatolide {ECO:0000269|PubMed:26359402}; Vmax=1.7 nmol/min/mg enzyme with (-)-pluviatolide as substrate {ECO:0000269|PubMed:26359402}; Note=kcat is 0.72 sec(-1) with (-)-pluviatolide as substrate. {ECO:0000269|PubMed:26359402};

PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26359402}.

FUNCTION: O-methyltransferase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family (PubMed:26359402). Catalyzes the methylation of (-)-pluviatolide to produce (-)-bursehernin (PubMed:26359402). {ECO:0000269|PubMed:26359402}.

Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum)

A0A0N9HTA1

DOMT1_SINHE

MDTRADAEIKAMELIGIGVLPLAMKAIIELNVLEILSKAGPDTQLTAAQIVTDIPTTNPNAGFQLDRILRLLASHSVLSSSITKSGERVYGLTPMCKYFLPDQDGVSLAPMVVTIHDKVLLQSWHYLKDSVLKQGSLPFTEAFGMSPFEYSVSDTRFNKVFNAGMFDHSTLCMRDVLQRYKGFQGLGELVDVGGGTGGSLKMILSQYPNLKGINFDLPHVVADAPSFPGVKHIGGDMFESVPSGDAIFMKWILHDWDDGRCLTLLKNCWNALPEHGKVIIVEWILPSDAATDPTSRRVFTADLMMLAFSEGGKERTLGDYGALAKEAGFTTVKDFPCANGISVIEFHKK

2.1.1.330

aromatic compound biosynthetic process [GO:0019438]; methylation [GO:0032259]; phenylpropanoid biosynthetic process [GO:0009699]; response to wounding [GO:0009611]

O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

PF08100;PF00891;

3.40.50.150;1.10.10.10;

Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family, COMT subfamily

CATALYTIC ACTIVITY: Reaction=(-)-5'-demethylyatein + S-adenosyl-L-methionine = (-)-yatein + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:49040, ChEBI:CHEBI:4553, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90894; EC=2.1.1.330; Evidence={ECO:0000269|PubMed:26359402}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49041; Evidence={ECO:0000269|PubMed:26359402};

PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26359402}.

FUNCTION: O-methyltransferase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family (PubMed:26359402). Catalyzes the methylation of (-)-5'-demethylyatein to produce (-)-yatein (PubMed:26359402). {ECO:0000269|PubMed:26359402}.

Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum)

A0A0N9NCU6

YOPJ_YERPU

MIGPISQINISGGLSEKETSSLISNEELKNIITQLETDISDGSWFHKNYSRMDVEVMPALVIQANNKYPEMNLNLVTSPLDLSIEIKNVIENGVRSSRFIINMGEGGIHFSVIDYKHINGKTSLILFEPANFNSMGPAMLAIRTKTAIERYQLPDCHFSMVEMDIQRSSSECGIFSFALAKKLYIERDSLLKIHEDNIKGILSDGENPLPHDKLDPYLPVTFYKHTQGKKRLNEYLNTNPQGVGTVVNKKNETIVNRFDNNKSIVDGKELSVSVHKKRIAEYKTLLKV

2.3.1.-

COFACTOR: Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130; Evidence={ECO:0000250|UniProtKB:O68718};

negative regulation of JNK cascade [GO:0046329]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of p38MAPK cascade [GO:1903753]; peptidyl-serine O-acetylation [GO:0030919]; peptidyl-threonine O-acetylation [GO:0120258]

extracellular region [GO:0005576]

O-acetyltransferase activity [GO:0016413]; toxin activity [GO:0090729]

PF03421;

Acetyltransferase YopJ family

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DUD0}. Note=Secreted via type III secretion system (T3SS). {ECO:0000250|UniProtKB:P0DUD0}.

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-threonyl-[protein] = CoA + O-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:65340, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:16780, ChEBI:CHEBI:30013, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:141025; Evidence={ECO:0000269|PubMed:16728640}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65341; Evidence={ECO:0000269|PubMed:16728640}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-seryl-[protein] = CoA + O-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:59392, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15352, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:141128; Evidence={ECO:0000269|PubMed:16728640}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393; Evidence={ECO:0000269|PubMed:16728640};

FUNCTION: Serine/threonine-protein acetyltransferase translocated into infected cells, which inhibits the host immune response and induces cell death by mediating acetylation of target proteins (PubMed:10489373, PubMed:12433923, PubMed:16728640, PubMed:22563435, PubMed:26810037). Inhibits the MAPK and NF-kappa-B signaling pathways by acetylating protein-kinases such as MAP2K1, MAP2K6, MAP3K7/TAK1 and I-kappa-B kinase (CHUK/IKKA and IKBKB) on serine and threonine residues critical for their activation by phosphorylation, thereby preventing protein-kinase activation (PubMed:16728640, PubMed:30361383, Ref.9). Promotes pyroptosis, a programmed cell death, in host cells by mediating acetylation of MAP3K7/TAK1: MAP3K7/TAK1 inactivation triggers activation of caspase-8 (CASP8), followed by CASP8-dependent cleavage of gasdermin-D (GSDMD) and induction of pyroptosis (PubMed:30361383, PubMed:30381458). Also able to induce intestinal barrier dysfunction by acetylating and inhibiting host protein-kinases RIPK2/RICK and MAP3K7/TAK1, thereby promoting cell death (By similarity). {ECO:0000250|UniProtKB:P0DUD0, ECO:0000269|PubMed:10489373, ECO:0000269|PubMed:12433923, ECO:0000269|PubMed:16728640, ECO:0000269|PubMed:22563435, ECO:0000269|PubMed:26810037, ECO:0000269|PubMed:30361383, ECO:0000269|PubMed:30381458, ECO:0000269|Ref.9}.

Yersinia pseudotuberculosis

A0A0P0VIP0

LRSK7_ORYSJ

MPPRCRRLPLLFILLLAVRPLSAAAASSIAAAPASSYRRISWASNLTLLGSASLLPGAAGVALTTPSRDGVGAGRALFSEPVRLLLPQDAAASASASRAATPASFSTRFTFRITPSPTYGDGLAFLLTSSRTFLGASNGFLGLFPSSSASDEGELRDVSTVAVEIDTHLDVALHDPDGNHVALDAGSIFSVASAQPGVDLKAGVPITAWVEYRAPRRRLNVWLSYSPSRRPEKPALSADVDLSGLLRTYMYAGFSASNGNGAALHVVERWTFRTFGFPNSSYAPPPTKYIGPMPPNNQPLPPPPSPSPSPPPPSPPPPPHPNHRRRHLFYKVLGGVLGGMVLLGLVVVGSAVLLGRSVRRKNQEHAVASEDMGEATLSMEVARAATKGFDSGNVIGVGGSGATVYEGVLPSGSRVAVKRFQAIGSCTKAFDSELKAMLNCPHHPNLVPLAGWCRSKDELVLVYEFMPNGNLDSALHTLGGATLPWEARFRAVYGVASALAYLHDECENRIIHRDVKSSNVMLDAEFNARLGDFGLARTVSHGGLPLTTQPAGTLGYLAPEYVHTGVATERSDVYSFGVLALEVATGRRPAERGISVVNWVWTLWGRRRLVDAADRRLQGRFVADEMRRVLLVGLCCVHPDCRKRPGMRRVVSMLDGTAPLILVPDKMPPVLLQPVPNASSMNSADTANTAFFSCR

2.7.11.1

defense response to bacterium [GO:0042742]; defense response to oomycetes [GO:0002229]; pollen aperture formation [GO:0062075]; pollen development [GO:0009555]; protein autophosphorylation [GO:0046777]

cytosol [GO:0005829]; plasma membrane [GO:0005886]; pollen aperture [GO:0062074]

ATP binding [GO:0005524]; carbohydrate binding [GO:0030246]; kinase activity [GO:0016301]; protein serine/threonine kinase activity [GO:0004674]

PF00139;PF00069;

2.60.120.200;1.10.510.10;

Leguminous lectin family; Protein kinase superfamily, Ser/Thr protein kinase family

PTM: Autophosphorylated at Thr-376; Ser-378; Thr-386; Thr-403 and Thr-657. {ECO:0000269|PubMed:31833176}.

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31833176, ECO:0000269|PubMed:32284546}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:32284546}. Note=During meiosis, localizes diffusely in the cytosol and plasma membrane of microspore mother cells (MMCs). During tetrad development, localizes at the corners. At late tetrad stage, accumulates to the four corners of the tetrad, assembled into ring-like structures marking future aperture sites. When microspores are released from tetrads and preliminary aperture structures has formed, remains in a distinctly ring-shaped distribution beneath the aperture in the plasma membrane between the annulus and operculum. {ECO:0000269|PubMed:32284546}.

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:31833176}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:31833176}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:31833176}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000269|PubMed:31833176};

FUNCTION: Legume-lectin receptor-like kinase required for normal pollen development and male fertility (PubMed:31833176, PubMed:32284546). Regulates pollen exine assembly and aperture development (PubMed:31833176, PubMed:32284546). Plays a critical role in annulus formation, and may participate in the formation of the fibrillar-granular layer underneath the operculum (PubMed:32284546). May function by regulating the expression of genes involved in pollen exine development (PubMed:31833176). Kinase activity is required for its function in pollen development (PubMed:31833176). {ECO:0000269|PubMed:31833176, ECO:0000269|PubMed:32284546}.

Oryza sativa subsp. japonica (Rice)

A0A0P0WGX7

ENL1_ORYSJ

MASPPPFDICGDLDDDPTPPAPTPLAAPTPNGLNDRLLRLTRTHQRGPSQNPNPNPNPNPKPPPPPPPQEPEPAKVKLAGRRRLCKLSTAGDESAGDDDSIRDILDDLTTRLDSLSVDRPTARPRPHVSPLPCALHADPDPSQSQLNDGTKPSSSFVDCDDDDDDAGGAYGGFGVKEEVTRKVFKASSSFGGRGNDDKMKAKGAYAFDTVSRKTTTESKASKFFGDYDDEDDIDQDAENGKENHADDVGWEKTEDFKMEPTGTGVTRKPYNLPGRIFNMLYPHQREGLRWLWVLHCRGTGGILGDDMGLGKTMQVSAFLAGLFHSRLIKRVLVVAPKTLLTHWTKELSVVSLKDKIRDYSGPNANARNYELKYAFKEGGILLTTYDIVRNNFKMIKGNFTNDFDDEEETLWNYVILDEGHIIKNPKTQRAQSLFEIPCAHRIVISGTPIQNNLKEMWALFYFCCPEVLGDKEQFKARYEHAIIQGNDKNATNRQKHIGSNVAKELRERIKPYFLRRMKNEVFLDSGTGEDKKLAKKNELIIWLKLTSCQRQLYEAFLNSELVHSSMQGSPLAAITILKKICDHPLLLTKKAAEGVLEGMDAMLNNQEMGMVEKMAMNLADMAHDDDDVELQVGQDVSCKLSFMMSLLQNLVSEGHNVLIFSQTRKMLNIIQEAIILEGYKFLRIDGTTKISERERIVKDFQEGPGAPIFLLTTQVGGLGLTLTKAARVIVVDPAWNPSTDNQSVDRAYRIGQMKDVIVYRLMTSGTIEEKIYKLQVFKGALFRTATEHKEQTRYFSKRDIQELFSLPEQGFDVSLTQKQLQEEHGQQLVMDDSLRKHIQFLEQQGIAGVSHHSLLFSKTAILPTLNDNDGLDSRRAMPMAKHYYKGASSDYVANGAAYAMKPKEFIARTYSPNSTSTESPEEIKAKINRLSQTLANTVLVAKLPDRGDKIRRQINELDEKLTVIESSPEPLERKGPTEVICLDDLSV

3.6.4.-

cell division [GO:0051301]; double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; reciprocal meiotic recombination [GO:0007131]; regulation of endosperm development [GO:2000014]; regulation of mitotic sister chromatid separation [GO:0010965]; transcription-coupled nucleotide-excision repair [GO:0006283]

chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]

ATP binding [GO:0005524]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA translocase activity [GO:0015616]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787]

PF00271;PF00176;

3.40.50.300;3.40.50.10810;

SNF2/RAD54 helicase family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25327517}. Chromosome {ECO:0000269|PubMed:25327517}. Note=Localizes to the cytoplasm during interphase, but moves to the chromosome arms during mitosis. {ECO:0000269|PubMed:25327517}.

FUNCTION: DNA helicase that acts as an essential component of the spindle assembly checkpoint (By similarity). Plays an indispensable role in the development of seed endosperm (PubMed:25327517). Is required to secure sister chromosome separation during endosperm syncytial mitosis, which involves extremely rapid free nuclear cycles (PubMed:25327517). {ECO:0000250|UniProtKB:Q2NKX8, ECO:0000269|PubMed:25327517}.

Oryza sativa subsp. japonica (Rice)

A0A0P0X9Z7

CWZF7_ORYSJ

MLSVRRRQEDARGVGLRGGAAAGGMEDDAELEEGEACGDETAFVDPDVALSYIDEKIQDVLGHFQKDFEGAVSAENLGSKFGGYGSFLPTYQRSPLPQTRSPPKAANVSSRSPYHQPTESMSQNTLAVAAPSVSKHNGSMVPLSDDSSKKEVHQSTKVERASSTQDSLNGLSKSSDHNRFKVRIKVGSDNGLARNNAAIYSGLGLDISSPSSIEDSPDGCGSLSPEFNNVPIESPRTILQIMTCFSVPGGFLLSPLRDDLVQLTQKVVPTSKKWETNANTENVQERYEGYAAKRVKSDAKKKKAVDTKRSKSRNDVSAVMKNEIDIETPAGQKIVLEALNIPLLSNPRTMEAKDGSQFEEDPMRDTLVENKDARLKERTINSDLMAIKYENVKAEAAECLENSGPGSSGMDFSAVKGEVKFKAEKAEIHVEDRNTTSEKDFQSDRKQERKIKTESKCNATGVNFEGNKVMNERTPVVGRSIGKVSSKETLLNDINEENVSKSESRRSQKEQNMNASSSSDFLEDDRGVLSSGAVKERKNDSQSKSSHPGRKPKAKSHRDVREHLPEGSYGGKDDTLENGSGLGELRPKKIWKNDSERDSDMPGTSKREISSSLKNDRHTPAEEQRMHVPPSVSAPTANAAPMLPAPVVIEEHWVCCDICQKWRLLPYKMNPSLLPKKWKCSMLQWLPGMNRCEVSEDETTNALNALYVSPAPGNGVASVGHSHVASSGLTTSNTLNVNGHVEQSRKRKNTLSDGNVSFDVSQQMQGSVYPLSNQHAPIRSKSAADSIQFPVERDSKSVDHFVEKKRSKSKNHGSSSDGGHLVERSKKHSKVKSKREMDHDEYRTSKKIKKEERRQRQSGIDSNPGYDLASGDVPDEAKALPSKSMALQGSSERSDVPPSKYKSVSKYNSSEKSKRSKDGDVFLPEDKNKEHSYPSDAQKPDLSSKKRIVKEWEESQHNSTPPVSKMSIVNQSSSSKETCKDQNLKETKSKLTKSEEPFAMTDSKSIKVAHSNQTSRNLNNELFEDSTPFAVKSGMSEPPENRSSEQALDLAEPASSDLAYFQTTAVTSSSSKASGSQRRKQNFHVAKTSPIESVSSSPPRISNNDKVSHDKILGKDGSTCANTNNMQSLVKNTEVIVDNVRQARKSHESMLASEPVMNGFSQGNSDKDNELPQLTQGHASNGIISGRSLDDDLQHASGRKDSSLKSSNAARSHNHLHYANKNNLLTDGSSIQHRMAVLDTKGDSMVHENKRSVTSLQDRNGSTHYPPDGNPQSEVSFGKEKSHPKSNKHDMQNSKAQMLPSPLKESKVESHSAPLRSNASKLTAQLKRGNVENGGQHGITKQAISNPADTSSPVRKDNNSTGYALKEARDLKHKANRLKEEGKEQESTRLYFESALKYLHVASTLEPPPSIDGFKQCDAAQNLYSDTAKLCNFVGHAYEKSKKMAAAALAYKCVEVAYLKAAYYKYPTASKDRQMLQAIVQNPPGESPSSSASDIDNLNNNGLSKGPSSKDANSPQVTGNNLLLAARNQPHLTRLLAYTNDVNCAFDATRKSQMAIASAASNQENGIDGLSSVKTVLDFNFQSVNDLLRLVRLSMESISC

positive regulation of DNA-templated transcription [GO:0045893]; regulation of seed growth [GO:0080113]

nucleus [GO:0005634]

sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270]

PF07496;

3.30.40.100;

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28818372}. Note=Exhibits a speckle-like distribution in the nucleus. {ECO:0000269|PubMed:28818372}.

FUNCTION: Transcriptional activator that acts as a positive regulator of grain size (PubMed:31830332). Binds directly to the DNA core sequence 5'-CATTTC-3' found in the promoter of MADS1, and activates MADS1 transcription (PubMed:31830332). Increases grain width via direct up-regulation of MADS1 expression (PubMed:31830332). Promotes active chromatin modification at the MADS1 locus by increasing its level of histone H3K4me3 (PubMed:31830332). In GST pull-down assay, binds specifically to histone H3K4me3, but not to H3K4me1 or H3K4me2 (PubMed:28818372). May facilitate the recruitment of effectors to mediate gene expression (PubMed:28818372). {ECO:0000269|PubMed:28818372, ECO:0000269|PubMed:31830332}.

Oryza sativa subsp. japonica (Rice)

A0A0P0XCU3

SSY3A_ORYSJ

MEMALRPQSLLCPRSRLKVVIRPASSASGGGLAQYFLMTRRYTGSRIVRCMVSSSDCPNRKAKRTISLHTEVASSRGYAPRIAAESSIQEREHINSDEETFDTYNRLLRNESTEWKKLDTTEVDLSQDVSSSSMRKVDATDEAKLDILEDDLPRNLLNGVTMGEVDMLDEAGAEDDVFEVDLSALHNSTVGKMDAVNEVGTENDLFEVDLSALHSAAVGKVDVVDGAKAKEDLFEMDSLALHSVTMGKVDAINAAGAEGDKFEVDLSALASNNSMIEAVNVMDEAKAIEDTLEVDLSGNATSSSTYGEVKFEVDSLGNTSSTVMYGPADGAYEPRSDEVTFKVDSSENASNNVMYGRADVVDESWADEGIFEVDFFTNASSGAEYGKVDVVDEAKTDDFTFEIDSLEKDSNNKMHGKAHMVDEAWDDEAIFEVDLFGNASSIPIYGEVNVLDEARADDGKFEVDLLGNTSSNSTHEEVDVVDEAQTGEATFEVDLLGNALSSAIYKEVPVMGGAQDDEVDVDFSINASITETEKEADAVDEARVEDETFDMDLVGKQISIDSMNDDVVEEGTKHHRYPMLSSAFIEVKTIHETPVSLKPELMSVVMDQEQDKPISSVYQQEGSIFNLHAENQSTVDFHEREQMAITFDKQKESVAKLSKEDQQTAGLPEQNMSFDGVHRKSQSIIGLPFQHQSIVSSPEKYRSIVGFHGQNQSIISSHKQDKSIVGVPKKIQSIVGSTKHDDSIVGFRKQDRSIVSVPEQKQSIVGFHKQDLSIVAVSEQNLSIVAIPRESQSKQISIVRRHDPLHLKEVETKDRDGISKKSGGDDDLPHMLFEEELSQVEDVARAIAYKKQHEVDVISLTPDIQESPQDNIDPQELRRMLQELADQNCSMGNKLFVFPEAVKANSTIDVYLNRNLSALANEPDVHIKGAFNSWRWRPFTERLHKSELSGDWWSCKLHIPKEAYRLDFVFFNGRLVYDNNDSNDFVLQVESTMDEDSFEEFLVEEKKRELERVATEEAERRRHAEEQQRMGEQRAAEQAAREQAKKEIELKKNKLQNLLSSARTHVDNLWHIEPSTYRQGDTVRLYYNRNSRPLMHSTEIWMHGGCNSWTDGLSIVERLVECDDENGDWWYANVHIPEKAFVLDWVFADGPPGNARNYDNNGRQDFHAILPNAMTNEEYWVEEENCIYTRLLHEIREREEAIKIKVEKRAKMKSEMKEKTMRMFLLSQKHIVYTEPLEIRAGTTVDVLYNPSNTVLNGKPEVWFRWSFNRWMHPSGVLPPKKMVKTEDGCHLKATVSVPSDAYMMDFVFSESEEGGIYDNRNGTDYHIPVSGSNAKEPPIHIVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQSNVKNLHVRQSFSLGGTEIKVWFGLVEDLSVYFLEPQNGMFGGGWVYGGNDAGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAESRLATARIIFTIHNLEFGAHFIGKAMTYCDKATTVSHTYSKEVAGHGAIAPHRGKFYGILNGIDPDIWDPYTDNFIPMHYTSENVVEGKNAAKRALQQRFGLQQTDVPIVGIITRLTAQKGIHLIKHALHRTLERNGQVVLLGSAPDPRIQSDFCRLADSLHGENHGRVRLCLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGSIPIVRKTGGLYDTVFDVDHDKDRARVLGLEPNGFSFDGADCNGVDYALNRQQSLLGLKPAVGSTPSAKGSWSKTGPGTGLPWTTLNCTIQLTNFEAPIQRWQEKASIGRYYKLNETWLKVKIFYLSCRYKLTQTWFKVKIFYLSYTYICRIKTLYSMHKQLWEYVSAMFPILSFNYEYLI

2.4.1.21

amylopectin biosynthetic process [GO:0010021]; endosperm development [GO:0009960]; starch biosynthetic process [GO:0019252]

amyloplast [GO:0009501]; chloroplast [GO:0009507]

alpha-1,4-glucan synthase activity [GO:0033201]; glycogen (starch) synthase activity [GO:0004373]; starch binding [GO:2001070]; starch synthase activity [GO:0009011]

PF16760;PF08323;PF00534;

3.40.50.2000;2.60.40.10;

Glycosyltransferase 1 family, Bacterial/plant glycogen synthase subfamily

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. Plastid, amyloplast {ECO:0000305}. Note=Amyloplast or chloroplast, soluble. {ECO:0000305}.

CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21; Evidence={ECO:0000305};

PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}.

FUNCTION: Involved in starch synthesis in endosperm amyloplasts (PubMed:17297616, PubMed:17586688, PubMed:21417378, PubMed:21595523, PubMed:21730357). Plays an important role in the elongation of amylopectin B chains (PubMed:17297616, PubMed:17586688, PubMed:21417378, PubMed:21595523, PubMed:21730357). {ECO:0000269|PubMed:17297616, ECO:0000269|PubMed:17586688, ECO:0000269|PubMed:21417378, ECO:0000269|PubMed:21595523, ECO:0000269|PubMed:21730357}.

Oryza sativa subsp. japonica (Rice)

A0A0P0XII1

CERK1_ORYSJ

MEASTSLLVLVLAAAAFAAGTVTEAAGDGCSAGCDLALASFYVTPNQNVTNMADLFGIGAANYRSLAPYNPNIPNLDFINVGGRVNVYFTCGCRSLPGSPGATYLAGAFPFQMSRGQIYTSVAANYNNLTTAEWLQATNSYPANNIPDTAVINATVNCSCGDASISPDYGLFLTYPLRAEDTLASVAATYGLSSQLDVVRRYNPGMESATGSGIVYIPVKDPNGSYLPLKSPGKGASAGAIAGGVVAGVVVLAAIFLYIIFYRRRKAKQATLLQSSEDSTQLGTISMDKVTPSTIVGPSPVAGITVDKSVEFSYEELSNATQGFSIGNKIGQGGFGAVYYAELRGEKAAIKKMDMQATHEFLAELKVLTHVHHLNLVRLIGYCIESSLFLVYEFIENGNLSQHLRGMGYEPLSWAARIQIALDSARGLEYIHEHTVPVYIHRDIKSANILIDKNYRAKVADFGLTKLTEVGGTSMPTGTRVVGTFGYMPPEYARYGDVSPKVDVYAFGVVLYELISAKEAIVRSTESSSDSKGLVYLFEEALNSPDPKEGLRTLIDPKLGEDYPIDSILKLTQLAKVCTQEDPKLRPSMRSVVVALMTLSSTSEFWDMNNLYENQGLVNLMSGR

2.7.11.1

innate immune response [GO:0045087]; phosphorylation [GO:0016310]

plasma membrane [GO:0005886]

ATP binding [GO:0005524]; chitin binding [GO:0008061]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; transmembrane receptor protein kinase activity [GO:0019199]

PF07714;

1.10.510.10;

Protein kinase superfamily, Ser/Thr protein kinase family

PTM: Autophosphorylated; induced by chitin and derivatives. {ECO:0000250}.

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24964058, ECO:0000269|PubMed:25335639}; Single-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23498959}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23498959};

FUNCTION: Lysin motif (LysM) receptor kinase required as a cell surface receptor for chitin elicitor (chitooligosaccharides) signaling leading to innate immunity in response to biotic stresses. Involved in the resistance to pathogenic fungi, probably by sensing microbe-associated molecular patterns (MAMP) and pathogen-associated molecular patterns (PAMP) (PubMed:21070404, PubMed:22891159, PubMed:24964058). Involved in the detection of microbial peptidoglycans (PGNs) and mediates PGN response (PubMed:24964058). Plays dual roles in PGN and chitin signaling during innate immunity. Acts as an adapter for LYP4 and LYP6 and mediates signal transduction from the extracellular to intracellular spaces. Participates in the activation of defense genes during response to PGN and chitin (PubMed:25335639). Phosphorylates the downstream partner RLCK185 in response to chitin elicitation (PubMed:23498959). {ECO:0000269|PubMed:21070404, ECO:0000269|PubMed:22891159, ECO:0000269|PubMed:23498959, ECO:0000269|PubMed:24964058, ECO:0000269|PubMed:25335639}.

Oryza sativa subsp. japonica (Rice)

A0A0P0ZBS7

MENC_GEOSE

MAINIEYVILRHLQMELKAPFTTSFGTFQRKELILVEVVDRDGVSGWGESVAFSAPWYSEETVKTNWHMLEDFLVPLALAEPIHHPEELSKRFSAIRQNNMAKAALEGAVWDLYAKRLGVPLSQALGGAKKDIEVGVSIGIQPTVADLLQVIERYVAQGYRRIKVKIKPSWDVDVIREVRRVFPDVPLMADANSAYTLVDADRLKALDEFGLLMIEQPLAADDLVDHARLQPLLQTPICLDESIRSYDDARKALDLGSCRIINIKIGRVGGLGEAKRIHDLCAERGAPVWCGGMLEAGVGRAHNIAITTLENFTLPGDTAASSHYWERDIITPEVEVHGGLIRVPDAPGIGYDVDRRQVERYTQFAKVFHRTATA

4.2.1.113; 5.1.1.-

COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000269|PubMed:25875730}; Note=Shows highest activity in vitro with Co(2+) and Ni(2+). {ECO:0000269|PubMed:25875730};

menaquinone biosynthetic process [GO:0009234]

isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287]; O-succinylbenzoate synthase activity [GO:0043748]

PF13378;PF02746;

3.20.20.120;3.30.390.10;

Mandelate racemase/muconate lactonizing enzyme family, MenC type 2 subfamily

CATALYTIC ACTIVITY: Reaction=(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O; Xref=Rhea:RHEA:10196, ChEBI:CHEBI:15377, ChEBI:CHEBI:18325, ChEBI:CHEBI:58689; EC=4.2.1.113; Evidence={ECO:0000255|HAMAP-Rule:MF_01933}; CATALYTIC ACTIVITY: Reaction=N(alpha)-acetyl-D-methionine = N(alpha)-acetyl-L-methionine; Xref=Rhea:RHEA:59960, ChEBI:CHEBI:71670, ChEBI:CHEBI:85220; Evidence={ECO:0000269|PubMed:25875730};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.6 mM for N-formyl-D-methionine {ECO:0000269|PubMed:25875730}; KM=9 mM for N-formyl-L-methionine {ECO:0000269|PubMed:25875730}; KM=11.1 mM for N-formyl-D-norleucine {ECO:0000269|PubMed:25875730}; KM=12.5 mM for N-formyl-L-norleucine {ECO:0000269|PubMed:25875730}; KM=19.6 mM for N-formyl-D-aminobutyric acid {ECO:0000269|PubMed:25875730}; KM=17.9 mM for N-formyl-L-aminobutyric acid {ECO:0000269|PubMed:25875730}; KM=9.2 mM for N-formyl-D-norvaline {ECO:0000269|PubMed:25875730}; KM=24.5 mM for N-formyl-L-norvaline {ECO:0000269|PubMed:25875730}; KM=3 mM for N-formyl-D-homophenylalanine {ECO:0000269|PubMed:25875730}; KM=5.7 mM for N-formyl-L-homophenylalanine {ECO:0000269|PubMed:25875730}; Note=kcat is 74.6 sec(-1) with N-formyl-D-methionine as substrate. kcat is 52.9 sec(-1) with N-formyl-L-methionine as substrate. kcat is 12.3 sec(-1) with N-formyl-D-norleucine as substrate. kcat is 8.0 sec(-1) with N-formyl-L-norleucine as substrate. kcat is 15.2 sec(-1) with N-formyl-D-aminobutyric acid as substrate. kcat is 11.6 sec(-1) with N-formyl-L-aminobutyric acid as substrate. kcat is 11.2 sec(-1) with N-formyl-D-norvaline as substrate. kcat is 19.6 sec(-1) with N-formyl-L-norvaline as substrate. kcat is 88.4 sec(-1) with N-formyl-D-homophenylalanine as substrate. kcat is 85.5 sec(-1) with N-formyl-L-homophenylalanine as substrate. {ECO:0000269|PubMed:25875730};

PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_01933}.; PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01933}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:25875730};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55-65 degrees Celsius. {ECO:0000269|PubMed:25875730};

FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (By similarity). Also acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of N-succinyl-D/L-phenylalanine (PubMed:25875730). Can catalyze the racemization of a broad range of N-acylamino acids, including N-acetyl-D-methionine, N-formyl-D/L-methionine, N-formyl-D/L-norleucine, N-formyl-D/L-aminobutyric acid, N-formyl-D/L-norvaline, N-formyl-D/L-homophenylalanine, N-carbamoyl-D-methionine and N-carbamoyl-D-norleucine (PubMed:25875730). May be a bifunctional enzyme involved in menaquinone biosynthesis and in an irreversible pathway for the conversion of D- to L-amino acids, thereby facilitating the survival and/or growth of the organism (By similarity). {ECO:0000250|UniProtKB:Q5L1G9, ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000269|PubMed:25875730}.

Geobacillus stearothermophilus (Bacillus stearothermophilus)

A0A0P6JG37

ASAH1_HETGA

MLGRSRLTFVLLAAAVTCAEAQHAPPWTEDCRKSTYPPSGPTYRGPVPWYTINLDLPPYKRWHELMVDKGPMLKIIVNSFKNMVNTFVPSGKVMQMVDQKLPDLLGQFSGPYEEEMKGIADVTEIPLGEIISFNIFYELFTMCTSIITEDKKGHLLHVRNMDFGIFLGWNINNNTWVITEELKPLTVNLDFQRNSKTVFKATSFAGYVGMLTGFKPGQFSLTLNERFSMNGGYLGLLEWILGKKDASWIGFITRSVLENATSYEEAKNILAKTKLLAPAYFILGGNQSGEGCVITRERKDSLDIYELDPKQGRWYVVQTNYDRWKNPLFLDDRRTPAQTCLKRTTQENLSFATLYDILSTKPVLNKLTVFTALMDVTKNHYEAYLRDCPDPCVGW

3.5.1.23

fatty acid metabolic process [GO:0006631]; sphingolipid metabolic process [GO:0006665]

extracellular region [GO:0005576]; lysosome [GO:0005764]

ceramidase activity [GO:0102121]; fatty acid amide hydrolase activity [GO:0017064]; N-acylsphingosine amidohydrolase activity [GO:0017040]

PF02275;PF15508;

Acid ceramidase family

PTM: N-glycosylated. {ECO:0000269|PubMed:29692406}.; PTM: Proteolytically cleaved into two chains alpha and beta that remain associated via a disulfide bond (PubMed:29692406). Cleavage gives rise to a conformation change that activates the enzyme. The same catalytic Cys residue mediates the autoproteolytic cleavage and subsequent hydrolysis of lipid substrates. The beta chain may undergo an additional C-terminal processing (By similarity). {ECO:0000250|UniProtKB:Q13510, ECO:0000269|PubMed:29692406}.

SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q13510}. Secreted {ECO:0000250|UniProtKB:Q13510}. Note=Secretion is extremely low and localization to lysosomes is mannose-6-phosphate receptor-dependent. {ECO:0000250|UniProtKB:Q13510}.

CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine; Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868, ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoylsphing-4-enine = dodecanoate + sphing-4-enine; Xref=Rhea:RHEA:41291, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:57756, ChEBI:CHEBI:72956; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-tetradecanoylsphing-4-enine = sphing-4-enine + tetradecanoate; Xref=Rhea:RHEA:41287, ChEBI:CHEBI:15377, ChEBI:CHEBI:30807, ChEBI:CHEBI:57756, ChEBI:CHEBI:72957; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoylsphing-4-enine = hexadecanoate + sphing-4-enine; Xref=Rhea:RHEA:38891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:57756, ChEBI:CHEBI:72959; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-octadecanoylsphing-4-enine = octadecanoate + sphing-4-enine; Xref=Rhea:RHEA:41279, ChEBI:CHEBI:15377, ChEBI:CHEBI:25629, ChEBI:CHEBI:57756, ChEBI:CHEBI:72961; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoyl-(4R)-hydroxysphinganine = (4R)-hydroxysphinganine + dodecanoate; Xref=Rhea:RHEA:41303, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:64124, ChEBI:CHEBI:78001; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-(dodecanoyl)-sphinganine = dodecanoate + sphinganine; Xref=Rhea:RHEA:45448, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:57817, ChEBI:CHEBI:85261; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-(acetyl)-sphing-4-enine = acetate + sphing-4-enine; Xref=Rhea:RHEA:58484, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:46979, ChEBI:CHEBI:57756; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-(hexanoyl)sphing-4-enine = hexanoate + sphing-4-enine; Xref=Rhea:RHEA:41295, ChEBI:CHEBI:15377, ChEBI:CHEBI:17120, ChEBI:CHEBI:57756, ChEBI:CHEBI:63867; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-octanoylsphing-4-enine = octanoate + sphing-4-enine; Xref=Rhea:RHEA:45092, ChEBI:CHEBI:15377, ChEBI:CHEBI:25646, ChEBI:CHEBI:45815, ChEBI:CHEBI:57756; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-sphing-4-enine = (9Z)-octadecenoate + sphing-4-enine; Xref=Rhea:RHEA:41299, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57756, ChEBI:CHEBI:77996; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoylethanolamine = dodecanoate + ethanolamine; Xref=Rhea:RHEA:45456, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:57603, ChEBI:CHEBI:85263; Evidence={ECO:0000250|UniProtKB:Q13510};

PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000250|UniProtKB:Q13510}.

FUNCTION: Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (By similarity). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (By similarity). Has a higher catalytic efficiency towards C12-ceramides versus other ceramides (By similarity). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (By similarity). For the reverse synthetic reaction, the natural sphingosine D-erythro isomer is more efficiently utilized as a substrate compared to D-erythro-dihydrosphingosine and D-erythro-phytosphingosine, while the fatty acids with chain lengths of 12 or 14 carbons are the most efficiently used (By similarity). Has also an N-acylethanolamine hydrolase activity (By similarity). By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes (By similarity). Also indirectly regulates tumor necrosis factor/TNF-induced apoptosis (By similarity). By regulating the intracellular balance between ceramides and sphingosine, in adrenocortical cells, probably also acts as a regulator of steroidogenesis (By similarity). {ECO:0000250|UniProtKB:Q13510}.

Heterocephalus glaber (Naked mole rat)

A0A0R4I9Y1

R213B_DANRE

MTRKRKSGKKGKPLAQKKEAQKRGGSTSSSTTQKEGAQKGDGSSSSSTTQKDGAQKRDDSTSSSSTAQKEEGQKSDGSTSSSTTNKEGAQKRDGSTSSRLQKKGPQKRKGSTSSSRAHSRSRSKSKQTSYPSQARSRSHGQHNISTTESGPLSKEAQTQTSASLLVDKDTQTETVGQASQQTQTEINGNTETAEVSQPPQLSHEDVEMEGTVQPRTKGSESDGEKEESVKRKKRKLSEIGEPAKETEDSTKLSHECEEKVGDNQKNEDTNKHYGGDSLKDLKSVTEEPKSYAAAAATGKTGKVSKEQTNQIEANQDSTMESKSTQRKPSPVRAPAGPPMLTFYIYAVLDKRFRFNEQYDSLFLDYGNGNIKLQMKHFNIGKDGYLIEATFSVEDSAVRGGTIQYKYVVQQRQNQKSEIAVRYIEVPSYTTEKEFHLYEGYISCSSTVSITEWMMSLFHSEQKAVYKGWETSAHVLLDRIFLKWHPSNEESNMTFVQHLRSYKNAFESGFVEFPGNYTPFPIKVSELISAKLRMILKKESEALRTSESLDGVKSEALSVALSVFKVCCGCDVDLSLKDWGKLCQVVSECMGSFGEIQTTQTAPFINTVTGLMNLCAKKLITEVVLLVPVLHLLRNSEVNEAGPGSSMDEQRWTGLENISYQSFRERIRGLPDKRRMILKLIKDNLPMTKDNPKLLKSWLSLVAFEDVSEFVQLTGSFPELLIQSLMCRIIEAEKNTDANRTEKNLEVTGKVLNLLLKSIKKDRERIMKTEQLKLILQCCCNVHKSVCKTARLVPQYKVTVLSFQLLLKMAEIVYDGFFKGGEQMKQHQNEVLSKLNIIQEDFRKWRVELLLKPLMQTTGFTYPREMELWNDLYGIESSIPGVTERWKGFLDHDLRRRISQISDTDKIVVYVLVTSAKAVENSHANIQSCLKELCEAAIKNQCQSKKEGTLLCHLFSKTISWPVLSSIIVESAACFGEDHKGRLLDPQSAINFFLSQDKWNEWKLEDGASQLIAESQSFLGRLIQTLCQGSIPLGHLKTIFKYKTQFQKLYNQYKNNNKEMNVSISVSDLLSQREDDLKAFEQQKGYMTNLINMLGKISDVINVPELSSLEEIAKTNVQEVALDKLVEVETYFSKDDLKKNNTRRVLFYSDDQQVQDMAREMHDVNSSNLILSFWQEKAKDYFMAGPELLSLDLTEIYEDIWTPCLTKFLNFGNRIAVGQACFKEVEEALVGCGETGEGDRLKKEFMLMATMLDGHNENWPEQRLKQIREYRCLYDAAESAEVILKLKDRLGLQGDFSHIHSLTLVRDDSFKQNTLGSLSEDLIKARQKLADVERRHTACLEAFLKSDTLIKWIKAEIPSLKELKVFMELATISAGENDADIDRLASFETAVMGYAPLLYSLPQNVGFEEFFDYAKQVLDTLNKDEKLGDKLVDSNRWLDWLKGLRETHGSVEQSSLSLASAINTGGVYHVGWPDDFNGKTGLDNIFYVKVTKNNEEKTYRLNELLELQNKLMLMSSKGEKGKEQVIKFTQVFEGIQRMGRILLQLHRSGNMLFRNWAAEITCNHQNQPCIQVKFPLLSKCIVYQGEVEEELQKLSRSLEDFHKDWCNHLTKMRSQYYPLNHYSSEQIVYLCEWINSINIKKKPVPQQVWHLLTPIKPDCMLNDIKEAFEIATEPQSILQEDTAEELGPNSDFDLPLSFSLLDVSTECLEDLWKQFKENMSGFLTHHVDVETLGRFLSNLSNMNQLHIKRKIPSFLQEGRPNLVQCPAAELMSTTLSFYMESPENPLPTTDEVLMCQEETTEEEVEIFLRRCLGGAASNHKKIYTLVNPGSMSYDVSVALVEYFETQEVCAGPYYRLVMVCPVNQDRYIPSFFSNYKVQTGITISAERSQKYIRHHFKISYELATHSSVYPERLSVWMIASKRPAVGKSLYVRRLFEKFKGEFPRATLLTIRLIDPYIDMDGFVQTLSERLAPLRQQDPVLLHIDVAAVCHGLEEFLFKLLILECISDSKGTIWRRNKAHLVVIETLQRGHKTQTKMEPSHGFLNTLPTIFCRPPKDIKEIMKTNESFRSLDPLMDKEEFESEDIQRPYQYLRRFNRSMNLDRFTYQAHSVEGDPVDCLHHLLSNYGLKDPSWAELKHFTWFLNLQLKDCEKSLFCDSDFCGETLSGFKDFIVKFMIHMARDFASPSIDISDQSPSFFSKNEDEEEILSFRKRWENESHPYIFFNADHVSMSFLGFHVKQNGTILNAVDSKSGKVLMRNVMTQELFSDIQRQMINLSKDFDDLTREDKLQKMSFVVGAEKGCEKGKFDPDPTYELTTDNVMKMLAIHMRFRCEIPVIIMGETGCGKTRLVRFLCDLQREGRDVENMKLVKVHGGTTSETIYKKVREAEELAQKNRQKYKLDTVLFFDEANTTEAIFAIKEVLCDKTVKGYPLKKNSGLKIIAACNPYRRHTTKMVDRLERAGLGYRVKAEETEDRLGKVPMRQLVYRVHPLPPSMVPLVWDFGQLSDSTELSYIRQIVKKKMRDHRLPLSCQNVITNVLAASQKYMRNQADECSFVSLRDVERSMGVLLWFYNHRDIFFPSQDFPRFENVQMVLKCLVLAVGVCYYPSLENKRPYLATISKCFPDQFNSEESLEQEIASCQDFLLKNIQTRETIAKNMALKENVFLMVVCIELRIPLFLVGKPGSSKSLAKTVIADAMQRQASHCDLFKKLKEVHMVSFQCSPHSSPEGIIGTFRNCARFQKDKNLDEYVSVVVLDEIGLAEDSPQMPLKTLHPLLEDGCIDSDNPESYMKVGFVGISNWALDPAKMNRGIFVSRWDPSEKDLVETAEGICSSSQPVLLKIKHLLSKLAKCFLSICKTDSEQFFGLRDYYGLIKMLFDTVKCSDQEPSDKELAEAVLRNFSGQRDGFDPLDYFKDIFQNIQNVQRPNTLNMIEQNLDHHIDKECRYLLLLTTNNAALYIIQHHIFSKENYTQKCPEIVFGSGFPKDQEYAQICRNVSRIKACMETGRTVILLNLLNLYESLYDALNQYYVYFSGQQYVDLGLGSHRVKCRVHRDFRLVVVEDQEKVYKKFPVPLKNRLEKHKVDRSTDLAPWQHRVLEKLKKWAREFSKIQHSDSSEANFSVTDAFVGFHGDACASALLQALKKIDKLHHNKEENREESEAHHIDREFTEFQEKVNKFPDEAQEDDASMEVDKVQDAEIDEEMETLEDDSDLVKMVEGPVFVETRDKIESNKTMDEEEVYEIAKSFLLNCSTPDSVLRLKYSEFGNQETEELQKMYFHLQTHQSLRDLLNNHLNKTNQDKNRFLEVTTFSNLLTGADVRNLGPALGLSTERFLLLSLHQFDTEASFCNKIQSFLRESGPSVHILLIQMDMEESLCKNELIASAKYCTMNEILHLKSDECNIYTVFITKLSRIGEQCTSITGDKYIGFQGGVWLSAHIDDLRDSDDLCLNLKAFCGIPISQLISQTIESDVKESDEMNTNRQQSEKGDSVHLHSLSLLRSCTQKAVSLLRDTDEKTSRSMERMNILLGLLACDPGRTGARFQQVLLKRLVFALIQKEELIPNAKDWVYKVAKNHEALQECGTLRHTLWRYLQDFLTPVLARILEVIDRDCNLYQLYGEGLSEGLTQFWLDIFEDQQLLDLIPSQNTRAPDQEINVQCHLFVGEVEQPCAAPYSWLIKTYCQSLWEESEFVRSSEQDIKARIQQFVSAVSGSRLGSYIQKLSDVENVELGQRYLTDYVLLAFKVNSEDEHWVLQSAVLGCVFTLQTMMSVSPELSPSWIHAAAQIYNPRMDTLSHVLQLNPQLVSLIQQERPKRESPDMCEDILAVGICVEETKLLPVTSLTECLTFLQRVEQLQPCIERVLSPDYSALCSPGCLKYLETIQSVWQGILLVAVFIEKVVIKMKKGDERIIALTLKHCSQLHGLVEGSPDFRSKDNLQQIIRILNDYHEESISSELRYGVKCRVCLMELSEPFALPCEHVFCRSCLRRSMEREEAQHCPVCREPLSNNYQPTVSTTLNYSFALKQHKEIIKCCNTFFLEVVSRFCLTDDQDPPDDLVELLFSLLISAQGDVYKTRELTPFLECVDQSPVVRSVLPKLLMQYSLKQVKKHIQSYLEDLENKLLDKEDRTELYRLFVNCFQDTLLCSDSNGDHKHLRENTNFLSRLARKQTPSRQNDPAEFLMSMARLRMCLDSAAYILSKAICQKNNFVEAEFKFMEQVKAVCDYCDNDWYRVYLLRALNRQAGMDFLQALINSTDYEWIFPAEMMRLHRLIPAEVDRFLCCGQSYRALRDGVGESTQVGTTDGLKEALQASVGSSPLKNALLTLAVFRQVTCHFMSPERTLHPQEQQISILEKVIRDNMSGHAREFCTALLSNHIGGPGSNLRLGTGVPAQRRPVLELLVHACTVFYSGNRLISPLFNIASQPQNMTGAFLPTMPDDHTSEAKQWLSEKKLKMYFCSNSHACFVGECGRPMAKSKCATCGVEIGGEGHIPVPGFTEAYGDYDRTRPGHILGQARTRSEAPNRKLTLAQSCVLRLCLHLAMLQGLIHYQQGIRNMIHPEVSDVYQFLWQHLEKDMEVLGKTLTLNIDDSAIVIHLIFSRFLQTTPVANVDLSTRKSREQWEITVCKTAISPVLQNLDRELNNAQDLIAADNRLSNSPLVKVLRGDPQRMLQLPANCPTEHSAFWSPSSVLAVESISQQIDQAQAPLLTLFVQKVHYIRQLDCLPALAALLSDLIKVLPPGSETQNHTIASLLHCIPAGHQKKLMSERVEIYMKVWNQLRMEISSNASLGLDSTHCEKDITSESSGQFLFPSRKGAGSCLHAVIDVLSETHNSLVREARKLCQQTDSDYKVPLAVLSKSQLALCHPEREFLPLVLANCHYTLEKGQQTVSSYDHQGIERELSRRFFAGKPRIQTDTEKYLRRHHQNFTEVLNEVRAKIPQEMFWNPKQIHQAFSTNYHSTNRHKGLSRFYPDQPLSITTVPDLVIPRRPVGFQTQERHTLTPPGSHLTALNSLPAFSFCAPPISIRSTMELHLEEKDITSFPGLDSLPEELTWAKAAEIWRLAVQFKH

2.3.2.-; 2.3.2.27; 3.6.4.-

defense response to bacterium [GO:0042742]; immune system process [GO:0002376]; lipid droplet formation [GO:0140042]; lipid ubiquitination [GO:0120323]; negative regulation of non-canonical Wnt signaling pathway [GO:2000051]; protein K63-linked ubiquitination [GO:0070534]; regulation of lipid metabolic process [GO:0019216]; sprouting angiogenesis [GO:0002040]; ubiquitin-dependent protein catabolic process [GO:0006511]; xenophagy [GO:0098792]

cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleolus [GO:0005730]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]

PF13923;PF20173;

3.40.50.300;3.30.40.10;

AAA ATPase family

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet {ECO:0000250|UniProtKB:Q63HN8}.

CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q63HN8}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q63HN8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q63HN8};

PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q63HN8}.

FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity. Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS. Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (By similarity). Involved in lipid metabolism by regulating fat storage and lipid droplet formation; act by inhibiting the lipolytic process (By similarity). Also regulates lipotoxicity by inhibiting desaturation of fatty acids. Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger. Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of proteins downstream of rspo3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression. Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (By similarity). {ECO:0000250|UniProtKB:A0A0R4IBK5, ECO:0000250|UniProtKB:Q63HN8}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0R4IBK5

R213A_DANRE

MKCPKCSHEALEKAPKFCSECGHKLQSQSYETTQGTPHDKSQTPSIVPQITNAEMDETGSESKSLEIQNANVSPKRPNENTSPNPKKKKRKKRKKEKKKKSGVSEGPSSLTSDLSDISLTDKEKKMDTDQSSDSDCSSCIVEDTPTPAEPSSHLSPPENETAGPAQLSASALTTGSSKDGEESIGTTQKPVSASASKAPLGVDQQTKEEKVKCKDEGQKSLSAKAQHTPNANVDQNANVQSDANIDKDSQNVEPQKSSSVKTKPSKSTVADPKKTESEKQKSGERDNENSTQPVSSPKLKRNQTEESQKMVFGPNSAPKKNRGSSADSAMKVEKKPAGGKKDSSADQKSKESEDTESQCVTLPKRNTRSTQHISSSDRLTIYFHAVLSKDFKFNPEEDLIFIRAGGPIGNWEENLVELSVSRDLKEHGFLVEGKFICRKIDAEAVSIPYKYVVYKQKKNKYDYEYIYKLDAEVPTNRCLFIKSHLLNDEGEWHQYDDIICAQPAKNMFEWVKKTIWSDEKKNVLQGRKIAGTIMLETIFDLLRSWSKINLNNFFSQLRQFYEIYRNPFVFEKKQTKWYQLDYDEKDVRELLKNFMLMHVTPELQKDSNEKSKFIQEPLKAGLIMLYVWKQYDLKLDYGTLSRLCTAVCLPNLPKDEFLSLWTDITESFSVINSFSDMVEALISKLKAENMPRWIIVIPLLHLLKGTSKPFEQVITKVNSKYEQSWAGLQGLRSNILSPGPQERRAMLNLMKTYGHLVEVDRLLIRSWMYLMPLDDLVECGSIFPVELLDILQLFTMKCPNNISFTSSESTAEALAHIQSQLLQHRYSCPDVDYGIQCIQAACKLLEKICSLVRYFGHSQNFTDIPVACMNLVASVSGFAQTKQEADTFAEKTLVLLNDTKQTVRAWMRQTFKGRLLNSHLFSSHLTGTSFSTETEVWNNIIAIDFVCKDFIKEWRDTFTTDFEGKYQQEDHLDQIEAYCSNIEKLKVSQPYLVNSVEKCALQAVSTICQTKSEWKLFARFNKFRINWRFGNLVSTIILKSWPKDDKGTYFEEEEAVLKHLLGWAAAKNIFQLHGADEKLIDQLSDEAKEKFAMATSLFTNVLNQLVTGKIKMKLLNHILEKKSVFLELLTLDCFSEEEQYKDIDAMKALIQTRQEEVKAIYHERALAGALIAMCHNVEEHVKVDYKYLEDLYSNDMNEMDLDLFMDVHELNQIPTEASLEVPYFELQDDVRSMAEILNIFKDSYIFKLRWGNEAALFVERAEDEELDELDELPITLDVLNEEIFLPCHAAYRNIYTSLKDGSIDFEDIDEIFRAYKGKYEKLAAEVAIMSKQDFNDDQHWVQTRIQQIKQYHELHLAVESAKVVMMVKETLCLQGDFQVLEKLLITTHSDFKSERLDSIDNELIQAKNVLVDITEPRRLCLQELGHRKNFVIWVKEALEDINELKVFVDLASISAGENDLDVDRVACFHDAVLGYSSMLYDLKPDAGFSLFNEMLKKLWKALDNDSNLPKKLCDSARHIEWLKTVKDSHGSVELSSLSLASAINSKGIYVINAQNQKKLALENILKLHIMEEHDGGCETRVYSLEDLRDLQNKLMLMSGKGEQGQCEVDQFAEVFASVQRLVSAFIDLYVAGNPLFRHWEANINCNSKEACIIIDFNLGSVVSVVMVEGDVTEQLPEVCKKMESCLRFWQDFMDKQRSQHYYLNYYTAEQLVYLCHQLAHNNMEEIDDQVLMMLSFIKPSCSTSDLRKAWHILQYDLIRKGPDQNDDLDFQTFVEVSSMTENESTEKSCPTSDDLIQQLGDASGSTKLGVIWNNYMRDMKAFLPDSLDVPSLGYLLEILANSHREDEGDMSQRDKTRTILRELPNGIASGRPNLIICPSEEILISCISIYMNSKNEPLPTYDEVLLCSATTPYEEVELFLRRCLSAGYRGKKIYTMLYVNQLNYEVSYKVEKFFQNQNAHTTNDYRLVLICESNKEHAYLPSAFSQFRLHLIPQQPIPSIQQYLHRHFAVPVGISSAAAVFKDRQNVGVVSSERSGVGKSLYIKRLYEKLKLNSKKPSQLKCIRLTEPKVDENVIIQSLISVLKKNDLSVYHFDVTTMVKKGLHEFLFRLLILGYLMDSKGNMWKSSNKHLYVIEILRPGLSQNDRRAGAKVSFNFLDVFPIVYCRSPKEVLELEMRMEEHPSFGLSDDPLMDDQEFRSEAYQRPYQYLQRFYNGINLDEFLYQGVEGSHVECLQMLFEYCGIIDPSWAELRNFAWFLNLQLQDCEKSVFCDFSFVGDTLLGFKNFVVEFMILMAKDFATPSLSISDQSPGRLHEDFSSANEEDLAPFKIRKRWESEPHPYIFFNDDHDSMTFIGFHLQPNAQKGVDAVDPSNNRVIKQNIMTMELYEGLKLQRVPFNIDFDQLPRWEKIERLSRVLGIQWPLDPDETYELTTDNMLKMLAVHMRFRCGIPVIIMGETGCGKTRLIKFLCEMHRSGVATDNMKLVKVHGGTSSEMIYTKVREAEAMALRNKLDYGFDTVLFFDEANTTEAISSIKEILCDNSAEGQNLTENTGLKIIAACNPYRKHTDVMIKRLESAGLGYRVRAEETDEKLGSIPLRQLVYRVQALPPSMIPLIWDFGQLNDHTEKMYIKQIVERVAETHSIDSGYITVITDVLSASQKYMRTRQDECSFVSLRDVERCMQVFGWFYKKHLMLLSELDKFESIQRTEKTDQHPKDTDERNPILWSLLMAVGVCYHACLEDKEKYRKKICKYFPAAYSPMKVMQEISVIQDIFLEGVPMGENIARNNALKENVFMMVICIELRIPLFLVGKPGSSKSLSKTLVADGMQGQAAHSDLFRKLKQIHLVSFQCSPHSTPEGIINTFKQCARFQEGKNLSEYVSVVVLDEIGLAEDSQKMPLKTLHPLLEEGCIDDQPSPHKKVGFIGISNWALDPAKMNRGIFVSRGDPDENELIESAKGICSSDVMILEKVRECFKPFAHAYLRICKKQEKGFFGLRDYYSLIKMMFAVAKACDQKPSAEQIVKAVLRNFSGKDDVDAVTFFTSRLNIKPELETISAIELVRENVTAIGQDEECRYLLVLTKNYAALRILQQTFFSDQCQPEIIFGSSFPKDQEYTQICRNINRVKICMETGQTIVLLNLQNLYESLYDALNQYYVTLGGQKYVDLGLGTHRVKCRVHKDFRLIVIEEKDIVYKQFPIPLINRLEKHYLDLNTLLKSEQKDIVKNLEQWVQCFTDVKNKHSVAPSARRYSPADAFIGYHTDTCASVVMQVTEQLKGQELSDPRKGILDESKLILLNCATPDAVVRLDCTSLFNVESEHLSRVYFEDQMHNSLAEFILSHIQQEGCSGAFFTEVTTFSRLLTASETQQLQNVVQNIELLSLQQFDTEQSFLKKIKNYLENTTGDKILLIQTDFDEGFQKLNVIASAKYSSINEINKFKKEGSGKIFVYFITKLPRMDGGTSYIGFNGGPWKSIHIDDLRRPKDIVSDIKALQGLTISQLFEEKAEKVDETEAMEVEDMYAGGEDEEDEEKMELEENNGCKDVLDTTALVRSCVQSAVGMLRDQTEGGMRSTKRVEILLMLLAEDQTLQAEFLKTLKTRLHSLLVAHDDNTISAKSWVSREALNVDALHEGGTFRHALWRRVQAVVTPFLAQLVSVVDRDCNLDLLLDRNSGEPLKKLWLEIFRDDKFLSVSPYTRTENNSATKTILVQNYMSVDRNKGCTMPFSWRIKDYLEDLWKHALQQEGHTVKQFEEFFWKTPLGRYISEATNEMQMEFFYRYLQDFISMTMNVTSEVDFEVLRGAFTSSVNEVRIAHEAHESEALSLVWIHVAYHHFKNRIQNLHRMMSLEPQISQMLLENRYASEGKELVLDVLAAVACIEYLEPQNLDGDDQSLAWLRRVKKLQVPVELVCSLESLHNRGDRCRQMVTNIQHGWRRIYSLVLFVEHMLLGVGDLQQKLKPVVLEHTQLLAQVLEQDSNLKKKKPFEAVITVLKTCKDKASQRIIRFGLQLCPVCMGDPRDPLSLPCDHIYCLTCIRQWLVPGQMHCPLCVQEVPDNFELKPSDELRRLISQNASFRMRCNAFFIDLVSTMCFKDNTPPSKDIILHLLSLLMVEASSLPPFKGRDRRFLTKALSPFDDSVDKNPVVRSVVLKLLLNYSFDHVKDYLQQHLTEVEQSKILEETDKAELYCLYMNCLEDSMYDRTQWHTVAEQQNCFLEETRFLLEFLQSDSVSAHTATVEHLQRLARVRLCLDMAADLLVANAGIHDDPSAFIQAFWNNVVNLCRQSRNDWYRVYLIRKLCSLQGVECVKNLLLQETYRWLFPQEILEMNQDDSQIDQYLACGADYKTIRDAVAKFMLDLHINGIQKAIEDCNCTPMKKAVYVLMAFFREVTSLHRTGNPNMHPKPEHCAGLEHFIKNSAIFVNNEMKAFAEKLVRNQLGALRVRPHMPSRDLSLVEVTIHMAAVLLCGNLLLLQPLQKLALSPNNMMASFIPTMPDDMLAVAQQAMGHLQWYFCPNGHPCTVGECGQPMEVSRCPDCDAEIGGSNHRPVDGFRAMQIQADRTQSGHILGDAQRRDLPDMQDTKNMSPAPFALLRLLTHMSMLIGTQNNPQSIMQIIKPAVVHPDAFLMQHLLKDMEQLSKALGKGVDDTVSTIHLAIHSLLEPHQTSQWPDPYDPNLSTKDARNGWENAMNNDVITHHLKVLEHQLKEVNAFIREDERVSSNPVMKLTFGEPGRFLRSLPQNSLIHNSSIWSCRNKVSLMSLTHIVEQNNGRDTLPVLWRFLQREAELRLVRFLPDILVLQRDLVKKFQNITDLTYKTIREFLQDQKAASLTAWYEKRIKIFLTTWNQIRVSLANTGEIKLPADYTEKDLGLDADLQVLLPQRRGLGLCSTALVSYLITIHNDLMYTVEKHTGDDSDYKISPAELTELHVIRYEYDRDLLPLVLANCQYSMECGQETLLEYDLPKIQQQILTRFLQGKPLITINGIPTLVNRQDRNYEIIFKDVKGKVQQELLQPLTQYDLVKELQSYSDVCEALSTVELAVGFLAMTGGEPNMQLGVYLKDVLQMTDHMATHVFKALSRCSLKHCVALWQLLSSLKSETMLRLKRDPFVGISKEYKQPLQEEHKRLLTSFFTKSSADAFLLEMHEFLLLVLKSPKATDTYRPDWRLKHTVVSYMERKDLDVPPEVEEFFPKEILLSEYTSTWNFSVNLRQKRSQS

2.3.2.-; 2.3.2.27; 3.6.4.-

blood circulation [GO:0008015]; defense response to bacterium [GO:0042742]; immune system process [GO:0002376]; lipid droplet formation [GO:0140042]; lipid ubiquitination [GO:0120323]; negative regulation of non-canonical Wnt signaling pathway [GO:2000051]; protein K63-linked ubiquitination [GO:0070534]; regulation of angiogenesis [GO:0045765]; regulation of lipid metabolic process [GO:0019216]; sprouting angiogenesis [GO:0002040]; ubiquitin-dependent protein catabolic process [GO:0006511]; xenophagy [GO:0098792]

cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleolus [GO:0005730]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]

PF00097;PF20173;

3.40.50.300;3.30.40.10;

AAA ATPase family

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet {ECO:0000250|UniProtKB:Q63HN8}.

CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q63HN8}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q63HN8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q63HN8};

PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q63HN8}.

FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (By similarity). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS (By similarity). Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (By similarity). Involved in lipid metabolism by regulating fat storage and lipid droplet formation; act by inhibiting the lipolytic process (PubMed:30705059). Also regulates lipotoxicity by inhibiting desaturation of fatty acids (By similarity). Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger (By similarity). Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of proteins downstream of rspo3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression (By similarity). Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (By similarity). Also involved in neuromuscular regulation (PubMed:26530008). {ECO:0000250|UniProtKB:Q63HN8, ECO:0000269|PubMed:26530008, ECO:0000269|PubMed:30705059}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0R4IDX9

NINJ1_DANRE

MASEAMELNGGVNRRDDPGARPQQGRMSRNTPLNMNHYANKKSAAESMLDIALLMANASQLKTVLELGPSFSFYIPLITLISISLTLQIIVGILLIFIVKWNLNDSSKHYILNLLENIVTALVFIVVVVNVFITAFGVQRPDDKTS

angiogenesis [GO:0001525]; cell adhesion [GO:0007155]; heart development [GO:0007507]; heterotypic cell-cell adhesion [GO:0034113]; killing of cells of another organism [GO:0031640]; leukocyte chemotaxis involved in inflammatory response [GO:0002232]; muscle cell differentiation [GO:0042692]; positive regulation of inflammatory response [GO:0050729]; positive regulation of toll-like receptor 4 signaling pathway [GO:0034145]; programmed cell death [GO:0012501]; regulation of angiogenesis [GO:0045765]; skeletal muscle tissue development [GO:0007519]; tissue regeneration [GO:0042246]

plasma membrane [GO:0005886]; synaptic membrane [GO:0097060]

cell adhesion mediator activity [GO:0098631]; lipopolysaccharide binding [GO:0001530]; membrane destabilizing activity [GO:0140912]

PF04923;

Ninjurin family

SUBCELLULAR LOCATION: [Ninjurin-1]: Cell membrane {ECO:0000250|UniProtKB:Q92982}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q92982}. Synaptic cell membrane {ECO:0000250|UniProtKB:O70131}; Multi-pass membrane protein {ECO:0000255}.

FUNCTION: Effector of necroptotic and pyroptotic programmed cell death that mediates plasma membrane rupture (cytolysis) (By similarity). Acts downstream of Gasdermin (GSDMA, GSDMB, GSDMC, GSDMD, or GSDME) or MLKL during pyroptosis or necroptosis, respectively: oligomerizes in response to death stimuli and promotes plasma membrane rupture by introducing hydrophilic faces of 2 alpha helices into the hydrophobic membrane, leading to release intracellular molecules named damage-associated molecular patterns (DAMPs) that propagate the inflammatory response (By similarity). Acts as a regulator of Toll-like receptor 4 (TLR4) signaling triggered by lipopolysaccharide (LPS) during systemic inflammation; directly binds LPS (By similarity). Involved in leukocyte migration during inflammation by promoting transendothelial migration of macrophages via homotypic binding (By similarity). Promotes the migration of monocytes across the brain endothelium to central nervous system inflammatory lesions (By similarity). Also acts as a homophilic transmembrane adhesion molecule involved in various processes such as axonal growth, cell chemotaxis and angiogenesis (By similarity). Promotes cell adhesion by mediating homophilic interactions via its extracellular N-terminal adhesion motif (N-NAM) (By similarity). Also involved in striated muscle growth and differentiation (PubMed:31091274). {ECO:0000250|UniProtKB:O70131, ECO:0000250|UniProtKB:Q92982, ECO:0000269|PubMed:31091274}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0R4IEW8

ELAV4_DANRE

MFEISRTLNAALLSNEGSTETQWRQADLPQLQGWAEKGLLTQPKMIISNMEPQVTNGPNSATANGPSSNSRSCPSPMQTGGSNDDSKTNLIVNYLPQNMTQEEFRSLFGSIGEIESCKLVRDKITGQSLGYGFVNYIDPKDAEKAINTLNGLRLQTKTIKVSYARPSSASIRDANLYVSGLPKTMTQKELEQLFSQYGRIITSRILVDQVTGPTGGSRGVGFIRFDKRIEAEEAIKGLNGQKPSGAAEPITVKFANNPSQKTSQALLSQLYQSPNRRYPGPLHHQAQRFRLDNLLNMAYGVKRFSPITIDSMTSLVGMNIPGHTGTGWCIFVYNLSPDSDESVLWQLFGPFGAVNNVKVIRDFNTNKCKGFGFVTMTNYDEAAMAIASLNGYRLGDRVLQVSFKTNKTHKS

axonogenesis [GO:0007409]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380]

axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; growth cone [GO:0030426]; perikaryon [GO:0043204]; protein-containing complex [GO:0032991]; ribonucleoprotein complex [GO:1990904]

RNA binding [GO:0003723]

PF00076;

3.30.70.330;

RRM elav family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O09032}. Perikaryon {ECO:0000250|UniProtKB:Q61701}. Cell projection, axon {ECO:0000250|UniProtKB:Q61701}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q61701}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q61701}.

FUNCTION: RNA-binding protein that is involved in the post-transcriptional regulation of mRNAs (By similarity). Plays a role in the regulation of mRNA stability, alternative splicing and translation (By similarity). Binds to AU-rich element (ARE) sequences in the 3' untranslated region (3'UTR) of target mRNAs (By similarity). Mainly plays a role in neuron-specific RNA processing (By similarity). Required for the maturation of motor neuron axonal branches and dendrites (PubMed:29061699). {ECO:0000250|UniProtKB:P26378, ECO:0000250|UniProtKB:Q61701, ECO:0000269|PubMed:29061699}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0R4IFG5

CFA53_DANRE

MLTAQRSRIRCREITGPAHSVALKARPPLSRDIDDIFVRRRKQEATRGEVLEFTKDQSSCDVRMRWERNTQRRVVSATVNRHLQDALDQYQMGIDEKRERLRELLESEELELFKEMEAKKETVLERQAKMHERAKTLRERRESERQRVVADKLDQLFREQSEELRAVQIKRRQDQVCTERESQIRTKEEVRRVQEEEEKLFAQMWESDRLAKEERHNLELQRQRENNLQQKAVLQTQMDMAEQQRIQAKELKQEEAQLLKDQREMLRLEAEREHRQKLQDQEKRRKQLDLSLRLKMKRLTRDRQEELALDMSILEQLLAQEKDEKQDEVLKKLERQEEQRRYREYLSQQLEEQKRLEAETEQLFESELQQAWARREAQWRLEKTARDRLMKDVMDTLRLQIQEKLNENMQKQAEAFKEKEELDRIIQANKLLDEEEKAHFREATKEYQADLLAQMMYRQRIREAEEAEKEYEFQKGLMYEEQYNKKIQDILSRPISSTTAVHPFRRRDRRCSSSGGQMS

cilium assembly [GO:0060271]; cilium movement [GO:0003341]; determination of left/right symmetry [GO:0007368]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]

axonemal microtubule [GO:0005879]; axoneme [GO:0005930]; ciliary base [GO:0097546]; extracellular region [GO:0005576]

PF13868;

CFAP53 family

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:25504577}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25504577}. Note=In cilia of the pronephric kidney tubules, prominent localization along the axonemes and also detected at the ciliary base (PubMed:25504577). In cilia of Kuppfer's vesicle and the spinal canal, localizes exclusively to the ciliary base where it overlaps with the ciliary basal bodies (PubMed:25504577). {ECO:0000269|PubMed:25504577}.

FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity). Regulates motility patterns of both 9+0 and 9+2 motile cilia through differential localization and recruitment of axonemal dynein components (By similarity). Required for cilium motility within the spinal canal and Kuppfer's vesicle and is involved in the establishment of left-right symmetry during embryogenesis (PubMed:25504577, PubMed:26531781, PubMed:26538025). {ECO:0000250|UniProtKB:F1N7G5, ECO:0000250|UniProtKB:Q9D439, ECO:0000269|PubMed:25504577, ECO:0000269|PubMed:26531781, ECO:0000269|PubMed:26538025}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0R4IKJ1

CAPAM_DANRE

MTSENHTTIKADSALVMSPTGSTSQAAPFSPSTSKPIQELPDELIQAGWSKCWSKRENRPYYFNRFTNQSLWEMPVLGQHDVISDPLGLNAAPASGEANADAGLGNGQRKRHPSEDASQAGPNSFKRPKVEIPATPTTPTVPISPSTPGVKPWVNTTTDEKQGQASTPAPAPYRPSVVYWDLDIQTNAVIRERAPADHLPPHPEIELQRAQLTTKLRQHYHELCSQREGIEPPRESFNRWLLERKVVDKGLDPLLPSECDPVISPSMFREIMNDIPIRLSRIKYKEEARKLLFKYAEAAKKMIDSRNATPESRKVVKWNVEDTMNWLRRDHSASKEDYMDRLEHLRKQCGPHVASVAKDSVEGICSKIYHISAEYVRRIRQAHLTLLKECNISVDGTESAEVQDRLVYCYPVRLSIPAPPQTRVELHFENDIACLRFKGEMVKVSRGHFNKLELLYRYSCIDDPRFEKFLSRVWCLIKRYQVMFGSGVNEGSGLQGSLPVPVFEALNKQFGVTFECFASPLNCYFKQFCSAFPDIDGFFGSRGPFLSFSPASGSFEANPPFCEELMDAMVTHFEDLLGRSSEPLSFIIFVPEWRDPPTPALTRMEASRFRRHQMTVPAFEHEYRSGSQHICKREEIYYKAIHGTAVIFLQNNAGFAKWEPTTERIQELLAAYKVSGRSLPSPGPSSTNTGEKDSKPAPERTAPSQDNSSPVDKTAQDTTNT

2.1.1.62

mRNA methylation [GO:0080009]; positive regulation of translation [GO:0045727]

nucleus [GO:0005634]

mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity [GO:0016422]; RNA polymerase II C-terminal domain binding [GO:0099122]; S-adenosyl-L-methionine binding [GO:1904047]

PF12237;PF00397;

1.20.1270.10;2.20.70.10;

CAPAM family

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H4Z3}.

CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenosine) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(N(6),2'-O-dimethyladenosine) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:22744, Rhea:RHEA-COMP:11518, Rhea:RHEA-COMP:11519, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85958, ChEBI:CHEBI:85959; EC=2.1.1.62; Evidence={ECO:0000269|PubMed:30467178}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22745; Evidence={ECO:0000269|PubMed:30467178};

FUNCTION: Cap-specific adenosine methyltransferase that catalyzes formation of N(6),2'-O-dimethyladenosine cap (m6A(m)) by methylating the adenosine at the second transcribed position of capped mRNAs (PubMed:30467178). {ECO:0000269|PubMed:30467178}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0R4IKU3

RECK_DANRE

MSGCLQILTVLLCCRFWALVFSQDQSCCVHHAADIPRCRDACEQLASIRSESRLRHLLHRLPSYCPETLSELWICINNSLPGASRKSDGWVGLGCCELAISAECRRDCKQASSKNDISKVCKKDTENPLYSCITKNEMGSVCCSYAGRHTTCREYCQAIFRTDSSPTVSQISAVKEYCQSVSPPLILCVENYTRLHPTHRPIDSLHCCDRAEEAHCQLACKRILRTLSTEQEIMDGLISECGSQPLPQDPLWQCFLGSAHPPANTDPESPPIAKMDSAKLHCCFKANTSICRNMCVEISTSWGTQSWQEFDQHCEYNPVEMDLITCLADVREPCQLGCKELSYCTNFNNRPTELFRSCNVQSDQGALNDFKLWSNGSIRMPLMNIPVLDIRRCRPEMWKTVACALQIKPCYSRSRGSVICRSDCVEILRQCGDRRRFAEAQTPERICDLLSPTDDPERCIPLNRYLTASELESSVEEVIHPCNPNPCPSSHLCHVNRKGCHVGHDCLPYYCVPGCKLGEASEFLVPADARLQVPVHSAQPGCYEVCVCGQSGRLENCAEMPCFDTSKSCQIAGQRRSHGSSFRVDCNPCSCFAGDAVCSSRQCVRSDSSEEDRRLFTGLPCGCADHFVPVCAGNGRTYPSACVARCVGFTDSQFVFGSCRSFDPCSPNPCQRNQRCVPRRQVCLTDLSEFPCPQYECVSRPSSCDQKLLDPVCDTDNMEHANLCVLNLRGKTLAYSGHCQDACRRPREVCAHNGESYSTVCEAFSERVAVDYQGRCHAVGLESEFGSDSGCNAVPCPPLASDACQPVTPPGACCPVCAGMLRILWNKAQMNIFAKLNRDQPVSLHDILKILRLHVSVPQCDIFGYLSINSEIIILIAPVDQQPTPLQIEACSKEAEKIDSLINSGSPTLVSHVPLSAFLSSELQLSSVRSSSCVSISVCVLLLLCSLILTLTSDL

blood vessel maturation [GO:0001955]; canonical Wnt signaling pathway [GO:0060070]; dorsal root ganglion development [GO:1990791]; extracellular matrix organization [GO:0030198]; negative regulation of metalloendopeptidase activity [GO:1904684]; regulation of angiogenesis [GO:0045765]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of cell cycle [GO:0051726]; regulation of cell migration involved in sprouting angiogenesis [GO:0090049]; regulation of establishment of blood-brain barrier [GO:0090210]; sprouting angiogenesis [GO:0002040]; vasculature development [GO:0001944]; Wnt signaling pathway [GO:0016055]

plasma membrane [GO:0005886]; side of membrane [GO:0098552]; Wnt signalosome [GO:1990909]

coreceptor activity [GO:0015026]; endopeptidase inhibitor activity [GO:0004866]; metalloendopeptidase inhibitor activity [GO:0008191]; serine-type endopeptidase inhibitor activity [GO:0004867]

PF07648;

3.30.60.30;

RECK family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26051822, ECO:0000269|PubMed:27979830}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:A0A1D5PUP4}. Note=Colocalizes with adgra2 at the plasma membrane. {ECO:0000269|PubMed:26051822}.

FUNCTION: Functions together with adgra2 to enable brain endothelial cells to selectively respond to Wnt7 signals (wnt7a or wnt7b) (PubMed:26051822, PubMed:26657775). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (PubMed:26051822, PubMed:26657775). Acts as a Wnt7-specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7. Adgra2 is then required to deliver reck-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex. Also acts as a serine protease inhibitor (By similarity). {ECO:0000250|UniProtKB:O95980, ECO:0000269|PubMed:26051822, ECO:0000269|PubMed:26657775}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0R4IMY7

TRPM2_DANRE

MDEAALEPTLVQTLAVSTAKGGRYLSLSPSFQRCSLASWIKENIKKKECCFYVEDGREGICKCGYPKVQHCDEAIKPEDYMGEQWDKHRHVRETPTDAFGDISFGGLGQKTGKYVRVSSDTSCENLYQLMTEQWKLRSPNLLISVTGGAKNFYIKTHLKDKFRRGLIKVAQTTGAWILTGGTHAGVMKHVGMAVRDYTLSSGSMEGQIVVIGVAPWGVIHNRSTLIHPEGRFPAYYSLDEQGQGRLSCLDINHTHFLLVDDGTQGHYGVEIELRARLEKLISKLSLGNRESGVTIPVVCVVLDGGPGTLNTIYNSMLNHTPCVVLEGSGRLADVIAHVASVPVSKVTMALINRLLKRFFMQEYKNFTELQIIEWTKKIQDILRMPHLLTVFRIDEDKNYDVDVAILQALLKASRSDEHAGRHCWERQLELAVAWNRVDIAESEIFTEESQWTSSDLHPAMFSALVGDKPEFVRLLLENGVCVREFLEREETLCELYSHLPSCFFLRKLAKRVQGGKMRRGQEPLPGSRKVCLSHVSEEVRHLLGSFTQPLYIASRYKPTKDDVRLKVPSKGALDLPCSGEEWSADTVWDPGRDLFLWAVVQNNRELAEIGWEQCRDCIAAALAASKILRKLAQESGEDDSEEATEMLELANHYEKQAIGVFSECHSWDAQRAQKLLIRISPSWGRSTCLWLALEAHDKSFIAHSGVQALLTQIWCGELSVDNPHWKVLLCMIFFPLIYTGFLTFRRDEDIQRQAERTEQQKLAMESVFAGQSDGKIKRHLRGFSQKSELKPLNCSSRLMSFLKSPQVKFYWNIASYFGFLWLFAVVLMIDFQTSPSWRELLLYVWLTSLVCEEIRQLYHDFDGSGFRRKAKMYIKDLWNILDVLSIVLFIAGLICRLQASDTVFYIGKVILCIDFIIFCLRLMAIFSISRTLGPKIIIVRRMMLDLFFFMFLLSIWVVAYGVAKQGILIENEERLNWIIRGAVYEPYITIFGNFPTNIDNTLFDISSCSVNASDPLKPKCPMLNADNTPVFPEWLTIMMLCVYLLFANILLLNLLIAIFNYTFQEVQDNTDTIWKFQRYELIKEYHSRPALPPPFILLSHLILFIRGVFLRDLPQRHKNFRQELEQTEEEELLSWEAYMKDNYLASTRQDESQSVEHRIHDTAEKVGAMSELLEREQEMVSATMAKRLARLEEQVSESAKALRWIIDALKSQGCKSKVQPPLMRSKSSDRDDGDSSGQETDDEEAPHMFARQLQYPDSTVRRFPVPEEKVSWEVNFSPYQPPVYNQQDSSESDTSALDKHRNPGGRTGIRGKGALNTLGPNHILHPIFTRWRDAEHKVLEFLAVWEDAEKRWALLGGPAQPDEPLAQVLERILGKKLNEKTKTLLKAGEEVYKGYVDDSRNTDNAWVETSIITLHCDKNTPLMADLNHMVESSLSSHQPLQWREVSSDACRCSYQREALRQIAHHHNTYF

calcium ion transmembrane transport [GO:0070588]; protein homotetramerization [GO:0051289]; release of sequestered calcium ion into cytosol [GO:0051209]

plasma membrane [GO:0005886]

ADP-D-ribose binding [GO:0072570]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; ligand-gated calcium channel activity [GO:0099604]; ligand-gated monoatomic cation channel activity [GO:0099094]; mono-ADP-D-ribose binding [GO:0072571]; monoatomic ion channel activity [GO:0005216]

PF00520;PF18139;

3.90.79.10;

Transient receptor (TC 1.A.4) family, LTrpC subfamily, TRPM2 sub-subfamily

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30250252}; Multi-pass membrane protein {ECO:0000269|PubMed:30250252}.

FUNCTION: Nonselective, voltage-independent cation channel that mediates Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels. Functions as a ligand-gated ion channel. Binding of ADP-ribose to the cytoplasmic N-terminal region causes a conformation change; the channel is primed but still requires Ca(2+) binding to trigger channel opening. {ECO:0000269|PubMed:30250252}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0R4IVA4

CC14A_DANRE

MTLDNLKHSAILSTLFKMADDNDLLGASEFIKDRLYFATLRSKPKSTANTHYFSTDEEFVYENFYADFGPLNLAMLYRYCCKLNKKLKSFTLTRKRIVHYTSFDQRKRANAAVLIGAYAVIYLKKTPEEAYRALISGSNASYLPFRDASFGNCTYNLTVLDCLQGIRKALQHGFLNFETFDVNEYEHYERVENGDLNWITPGKLLAFSGPHPKSKVENGYPLHAPEAYFPYFRKHNVTTIVRLNKKIYDAKRFTDAGFDHYDLFFVDGSTPSDIITRRFLHICESTSGAVAVHCKAGLGRTGTLIGCYLMKHYRFTSAEAIAWIRICRPGSIIGPQQHYLEEKQASLWAHGDSLRSKQRQYQDRSVPQLISSMDNLSISTSIFKSHSLDRMEENDYAENDLGMTQGDKLRALKGRRQPRSATTGAIRVEDVKVHTRSPSQPLSRMKPPASSQGSISPLKSSKVPASSSSSSSSSSVSASAKRIGRSSSSSTNLKSTRLASSLGNLYEPNTESISSGKPPSPSSFTPHPVRTTYNYHYEVNNNNNQYSTTSSPSKSLGYNLNHSGPSGASANARLSAGEQGHQRNPPAGLSGLSTRHLSRSIPSLQSEYVQY

3.1.3.16; 3.1.3.48

cell cycle [GO:0007049]; cell division [GO:0051301]; cilium assembly [GO:0060271]; dephosphorylation [GO:0016311]; microtubule cytoskeleton organization [GO:0000226]; positive regulation of cytokinesis [GO:0032467]; regulation of exit from mitosis [GO:0007096]

centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinocilium [GO:0060091]; mitotic spindle [GO:0072686]; nucleolus [GO:0005730]; spindle pole [GO:0000922]

myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]

PF00782;PF14671;

3.90.190.10;

Protein-tyrosine phosphatase family, Non-receptor class CDC14 subfamily

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UNH5}. Cell projection, kinocilium {ECO:0000250|UniProtKB:Q6GQT0}. Note=Centrosomal during interphase, released into the cytoplasm at the onset of mitosis. Subsequently localizes to the mitotic spindle pole and at the central spindle (By similarity). Present along both the transient kinocilia of developing cochlear hair cells and the persistent kinocilia of vestibular hair cells (By similarity). {ECO:0000250|UniProtKB:Q6GQT0, ECO:0000250|UniProtKB:Q9UNH5}.

CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:Q9UNH5}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:Q9UNH5};

FUNCTION: Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis. {ECO:0000250|UniProtKB:Q9UNH5}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0R4IVV0

MTP_DANRE

MMPVAGLLLCVTAVLCTSALGAGPRLDNGKLYRYSYSTEVGLNRPTGSPGGNVGFRISSDVDINLAWRNPEIQDEQLLQVKISNIQVESAGKHSRKNNIFHGSSAESILGKVRLEALQRPFLVLWKMGKIRSLYAQKAEPATVKNLKRGVASMLMMQLKSGKMSEADASGKCLVEYKVNKHQVIRTKHLETCKSQETGFTTHSPVLGISGKCAAETVITLENGIIKSADAKETHVLSINARHKAATKVLSRQSLTLKAIEAGPAEVAGKDVAGVVKALDDKFLSVGVIVEKTKPKCKGCPNLMETWKAVRSQLEPNSLSKAEAPRSFLTLVHSLRKSSKSEILTVLQNCSKTALPQLVDAVTSAQTPSSLSAILEFLDFSKKDGLILQERFLYACGFASHPTESMLQSLLEVSQGKIGSTEIKESVVIIMGALLRKLCLKGACDLPAVLKVKELLLAGPDSTQEESEVQMYLLALKNALLPEGIPVLAKYAESEVGAYSTIAITALQRYDPALITAEVKKALNRIYHQNQRIYEKNVRAAAADVIMSSNPSYMEVKNLLLSIGHLPHEMNKYMLSKIQDVLRFQMPAYKLVRQVMKDMISHNYDRFSKTGSSSAYSGFMAETVDVTCTYNLDILYSGSGVLRRSNMNIYGQSNNALLHGLQVTIEAQGLESLIAATPDEGEEELESFAGMSALLFDVQLRPVTFFKGYSDLMSKMFSMSGDPINVVKGLILLTDHSQVIPLQSGLRASAEFQAGLSIDISGGMEFSLWYRESKTSVNNRGALVIIGNMTVDTDFVSAGVEVGFETEATLDFITTVQFSEYPFLVCMQMDKTTFPFRETVSKQEKLPTGQMFSRKRSRDQVVPGSEFPLHQENSNMCKKVFEPAW

cholesterol homeostasis [GO:0042632]; digestion [GO:0007586]; lipid metabolic process [GO:0006629]; lipid transport [GO:0006869]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein metabolic process [GO:0042157]; lipoprotein transport [GO:0042953]; long-chain fatty acid transport [GO:0015909]; medium-chain fatty acid transport [GO:0001579]; plasma lipoprotein particle assembly [GO:0034377]; protein secretion [GO:0009306]; sprouting angiogenesis [GO:0002040]

basolateral plasma membrane [GO:0016323]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]

lipid binding [GO:0008289]; lipid transfer activity [GO:0120013]; lipid transporter activity [GO:0005319]; phosphatidylethanolamine transfer activity [GO:1904121]; phospholipid transporter activity [GO:0005548]

PF19444;PF01347;

1.25.10.20;

SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:17924655}. Golgi apparatus {ECO:0000250|UniProtKB:P55157}. Note=Colocalizes with P4HB/PDI in the endoplasmic reticulum. {ECO:0000269|PubMed:17924655}.

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:P55157}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572; Evidence={ECO:0000250|UniProtKB:P55157}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895, ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:P55157}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38896; Evidence={ECO:0000250|UniProtKB:P55157}; CATALYTIC ACTIVITY: Reaction=a cholesterol ester(in) = a cholesterol ester(out); Xref=Rhea:RHEA:39007, ChEBI:CHEBI:17002; Evidence={ECO:0000250|UniProtKB:P55157}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39008; Evidence={ECO:0000250|UniProtKB:P55157}; CATALYTIC ACTIVITY: Reaction=a triacyl-sn-glycerol(in) = a triacyl-sn-glycerol(out); Xref=Rhea:RHEA:39011, ChEBI:CHEBI:64615; Evidence={ECO:0000250|UniProtKB:P55157}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39012; Evidence={ECO:0000250|UniProtKB:P55157};

FUNCTION: Catalyzes the transport of triglyceride between phospholipid surfaces (PubMed:17924655). Catalyzes the transport of cholesteryl ester, and phospholipid between phospholipid surfaces (By similarity). Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B (PubMed:17924655, PubMed:22581286). Required for yolk lipid utilization and absorption of dietary lipids in larvae (PubMed:17176039). {ECO:0000250|UniProtKB:P55157, ECO:0000269|PubMed:17176039, ECO:0000269|PubMed:17924655, ECO:0000269|PubMed:22581286}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0R4IXF6

KAT2A_DANRE

MADPAAQSSAQPRLQQAQSSGPTGSNSNPGAGSSDPARPGLSQQQWSSQKKAQVRSFPRAKKLEKLGVFSSCKANDACKCNGWKNPNPPTAARMELQQQAASLTETCRSCGHSLAEHVSHLENVSEEEINRLLGMVVDVENLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMGKPVVEGSLGSPPFEKPNIEQGVLNFVQYKFSHLAPKERQTMYELSKMFLLCLNYWKLETPSQFRQRAQKEDAAAYKVDYTRWLCYCHVPQSNDSLPRYETCQVFGRSLLKSIFTVTRRQLLEKFRVEKDKLPPEKRTLILTHFPKFLSMLEEEIYGENSPIWEADFTMPASEGTQLGHQTVLSPVSISGSPHSKGSSASALGVTGLDVASSEPTIGEKRKLPEALTLEDAKRIRVMGDIPMELVNEVMKTITDPAAMLGPETSLLSANAARDETARLEERRGIIEFHVIGNSLSQKSNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPTQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHGILYFLTYADEYAIGYFKKQGFSKDIKVPKSRYLGYIKDYEGATLMECELNPRIPYTELSHIIKRQKEIIKKLIERKQNQIRKVYPGLTCFKEGVRQIPVESIPGIRETGWKPSAKEKSKELKDPDLLYNMLKNLLAQIKTHPDAWPFMEPVKKSEAPDYYEVIRFPIDLKTMTERLKNRYYVTKKLFIADLQRVITNCREYNPPDSEYCKSANTLEKFFYFKLKEAGLIDK

2.3.1.-; 2.3.1.48

bone morphogenesis [GO:0060349]; chromatin remodeling [GO:0006338]; epigenetic regulation of gene expression [GO:0040029]; heart development [GO:0007507]; histone succinylation [GO:0106077]; internal peptidyl-lysine acetylation [GO:0018393]; limb development [GO:0060173]; long-term memory [GO:0007616]; peptidyl-lysine glutarylation [GO:0106227]; positive regulation of cytokine production [GO:0001819]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of bone development [GO:1903010]; regulation of cartilage development [GO:0061035]; regulation of regulatory T cell differentiation [GO:0045589]; regulation of synaptic plasticity [GO:0048167]; regulation of T cell activation [GO:0050863]

ATAC complex [GO:0140672]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; histone acetyltransferase complex [GO:0000123]; nucleus [GO:0005634]

chromatin binding [GO:0003682]; histone acetyltransferase activity [GO:0004402]; histone glutaryltransferase activity [GO:0106229]; histone H3 acetyltransferase activity [GO:0010484]; histone H3K9 acetyltransferase activity [GO:0043992]; histone succinyltransferase activity [GO:0106078]; peptide-lysine-N-acetyltransferase activity [GO:0061733]; transcription coactivator activity [GO:0003713]

PF00583;PF00439;PF06466;

3.40.630.30;1.20.920.10;

Acetyltransferase family, GCN5 subfamily

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92830}. Chromosome {ECO:0000250|UniProtKB:Q92830}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q92830}.

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000250|UniProtKB:Q92830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; Evidence={ECO:0000250|UniProtKB:Q92830}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000250|UniProtKB:Q92830}; CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + succinyl-CoA = CoA + H(+) + N(6)-succinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:16261, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:87830; Evidence={ECO:0000250|UniProtKB:Q92830}; CATALYTIC ACTIVITY: Reaction=glutaryl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-glutaryl-L-lysyl-[protein]; Xref=Rhea:RHEA:18009, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11875, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57378, ChEBI:CHEBI:87828; Evidence={ECO:0000250|UniProtKB:Q92830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18010; Evidence={ECO:0000250|UniProtKB:Q92830};

FUNCTION: Protein lysine acyltransferase that can act as a acetyltransferase, glutaryltransferasesucc, succinyltransferase or malonyltransferase, depending on the context (By similarity). Acts as a histone lysine succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79' (H3K79succ), with a maximum frequency around the transcription start sites of genes (By similarity). Succinylation of histones gives a specific tag for epigenetic transcription activation (By similarity). Association with the 2-oxoglutarate dehydrogenase complex, which provides succinyl-CoA, is required for histone succinylation (By similarity). In different complexes, functions either as an acetyltransferase (HAT) or as a succinyltransferase: in the SAGA and ATAC complexes, acts as a histone acetyltransferase (By similarity). Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles (By similarity). Has a a strong preference for acetylation of H3 at 'Lys-9' (H3K9ac) (By similarity). Acetylation of histones gives a specific tag for epigenetic transcription activation (By similarity). Also acetylates non-histone proteins, such as tbx5 (PubMed:29174768). Involved in heart and limb development by mediating acetylation of tbx5 (PubMed:29174768). Together with kat2b, required for growth and differentiation of craniofacial cartilage and bone by regulating acetylation of histone H3 at 'Lys-9' (H3K9ac) (PubMed:30424580). Also acts as a histone glutaryltransferase: catalyzes glutarylation of histone H4 on 'Lys-91' (H4K91glu), a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes (By similarity). {ECO:0000250|UniProtKB:Q92830, ECO:0000269|PubMed:29174768, ECO:0000269|PubMed:30424580}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0R4IY06

PLAT1_DANRE

MDNQQRRTDNMASGETDHLQCVEEPQPGDLIEIFRPAYQHWALYLGDGYIINLTPVDEGQATAVSSVKSVFSRKAVVRMQLLKEVVGADSYRINNKYDDDHTPLPVSEIIQRAQMLIGQEVSYDLLGSNCEHFVTLLRYGEGVSEQASRAIGAISLVTAAASAFSVLGLINTRSRNRPF

2.3.1.-; 3.1.1.32; 3.1.1.4

lens fiber cell differentiation [GO:0070306]; lipid catabolic process [GO:0016042]; N-acylphosphatidylethanolamine metabolic process [GO:0070292]; organelle disassembly [GO:1903008]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]

N-acyltransferase activity [GO:0016410]; phospholipase A1 activity [GO:0008970]; phospholipase A2 activity [GO:0004623]

PF04970;

3.90.1720.10;

H-rev107 family

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:33854238}. Mitochondrion membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Note=During eye lens differentiation, recruited from the cytosol to various organelles, including mitochondria, endoplasmic reticulum and lysosomes, immediately before organelle degradation. This translocation is triggered by organelle membrane damage and requires the C-terminal transmembrane domain. {ECO:0000269|PubMed:33854238}.

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40487, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40488; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41348, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73009, ChEBI:CHEBI:76091; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41349; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = H(+) + hexadecanoyl-sn-glycero-3-phosphocholine + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:41360, ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999, ChEBI:CHEBI:74986, ChEBI:CHEBI:78097; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41361; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + a 2-acyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + 2-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41364, ChEBI:CHEBI:57875, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078, ChEBI:CHEBI:77369; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41365; Evidence={ECO:0000250|UniProtKB:Q9HDD0};

FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase activities. Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids. Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid. Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE) which serves as precursor for N-acylethanolamines (NAEs) (By similarity). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light (PubMed:33854238). Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity) (PubMed:33854238). {ECO:0000250|UniProtKB:Q9HDD0, ECO:0000269|PubMed:33854238}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0R4IZ84

EST1A_DANRE

MADELERVRISAAELRAQASSFNIHGDDVKDLREEGKKQRQRDSKRPDLQLYKPGVGHPNRRMDSVEGAGSDTLIQPDGFGNDPKMSDESPTSPGCSYMPGTGNEDYLNDHSKPETNHKTDGHIGGDKHKLVDENAVKIIERAGTPKSPKQSRKMRKPDRQIYQPGGRRSQGNKEVGASKELDRDRSREEEVDGKSIETPLKCEKEEKRKNRRGKNDRKKQASVETPSANKTENAVENISNKVSNLHLETVESKDRDRQDDTNQIKHSEEGRKIQTGGANRGMGEDKKKERGNGKSRPGKEKGNNQVFDKKEEGEAGGKASEAPHLEGRKQRNFGAKEASRDQNLNHEKQQGNRPKEKGKPSERTDSKRVNAASKRYSQSDIRRPRNRTYSTSSASSGTSMDGLAEAERLKAEGQQFSARTLERATGQREFVRGGQTRSRRRTARTLSSTDSLEENEVWEREGRRSRAAEEAKSSTRKEGGILRVSLDKREEQASRKSTRGRGRGILVLPAHTDLTQTPDPAPPLGGMRGGMGLGRGRGGRGGGTRRLWDPNNPDKKPALVSSQQSQHASQHQALYLQQGGCGPLHFLDTDDETVGSPPVRQGEFFQNQQAAAMAYYKFQNSDNPYCYPVSANSPNTPPRYPYPYQIPYQIPGSNGMYPASAMTSFYGPYGQGGPGYPSPTVSALTPEEAEVQTRGELGKFLRLADSQELQLSNLLSRERLSQEGLERMAQLRAELLTIYERVILTDIEFSDSQNVDQTLWKNVFYQVIERFRQLLKDQNSDTAPQIKTMLMTILEEGAVFFDSLLQKLQSVFQFKLQDYMDCMAIRARPLRKTVKYALISAQRCMICQGDIARYREQASESANYGKARSWYLKAQQIAPKNGRPYNQLALLAVYTKRKLDAVYYYMRSLAASNPILTAKESLMSLFEEAKRKADQVERRLKQDSDGSAHGPKGHTGGRRGEDAARVEIWIRPSEVSGTSRPTGSESGKDSEQDGELGALSASDLNKRFILSFLHAHGKLFTKVGMESFPAVANRVLLEFRALLQHSPSPLGSTRMLQIITINMFTIYNAQIRAKGQGETRSALEEQAISLGLAMFGLLVQRCTELLKETPTEPIPAEELGEFDEMDDEEGMVRVSVFPHDLRELLPSMKVWSDWMLGHPEKWNPPPCSMQGSPDVWQCLADLCNSFSRVYHGEVLLYKADADGEGDEELRVLQLEEDKMLSGFVPLLAAPQDACYTDQGTDAAIAADCKRVTVLKYFLEALCGQEEPLLAFKGGKYISMAAPLTPSINTENKAQEQEDDVIVEESSLSASEGEIDGEMEGDGSEDDIRELRARRHALAHKLAQQQKRRDKIQAVLQTGGQLEIEVRPFYLVPDTNGFIDHLEGLRKLLACGTYILVVPLIVITELDGLAKGQDSREGVGNGAHARQVQDRARAAVMFLEKAFESRDPSIRALTSRGNTLESIAFRSEDTSGQKGNNDDVILSCCLHYCQDKAKDFMPAERNGPVRLRREVVLLTDDRNLRVKALTRNVPVRDIPAFLIWAKVG

3.1.-.-

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q86US8};

chordate embryonic development [GO:0043009]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]

chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; nucleolus [GO:0005730]; telomerase holoenzyme complex [GO:0005697]

endonuclease activity [GO:0004519]; telomerase RNA binding [GO:0070034]; telomeric DNA binding [GO:0042162]

PF10374;PF10373;PF13638;

3.40.50.1010;1.25.40.10;

SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q86US8}. Chromosome, telomere {ECO:0000250|UniProtKB:Q86US8}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q86US8}.

FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini (By similarity). Required for normal embryonic development (PubMed:19414594). {ECO:0000250|UniProtKB:Q86US8, ECO:0000269|PubMed:19414594}.; FUNCTION: Plays a role in nonsense-mediated mRNA decay. {ECO:0000250|UniProtKB:Q86US8}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A0R6Y3I5

G5K_LEIDO

MADILKSVKRIVVKVGSSILVDNQEIAAHRIEALCQFIADLQTKYEVILVTSGAVAAGYTKKEMDKSYVPNKQALASMGQPLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALEELVFGDNDRLSALVAHHFKANLLVILSDIDGYYTENPRTSTNATIRSVVHELSPDDLVAEATPNNRFATGGIVTKLQAAQFLLERGGKMYLSSGFHLEKARQFLLGGSHEIGTLFYSRVSS

2.7.2.11

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:29777624};

L-proline biosynthetic process [GO:0055129]; phosphorylation [GO:0016310]

cytosol [GO:0005829]

ATP binding [GO:0005524]; glutamate 5-kinase activity [GO:0004349]; identical protein binding [GO:0042802]

PF00696;

3.40.1160.10;

Glutamate 5-kinase family

CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11; Evidence={ECO:0000269|PubMed:29777624}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14878; Evidence={ECO:0000269|PubMed:29777624};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 mM for L-glutamate {ECO:0000269|PubMed:29777624}; KM=0.6 mM for ATP {ECO:0000269|PubMed:29777624};

PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. {ECO:0000269|PubMed:29777624}.

FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate (PubMed:29777624). May be important for growth and survival (PubMed:29777624). {ECO:0000269|PubMed:29777624}.

Leishmania donovani

A0A0S2GKZ1

LP9A_PANSI

MKYSILGLTALSFVASAAAHTLVWGVWVNGVDQGDGRNIYIRSPPNNNPVKNLTSPDMTCNVDNRVVPKSVPVNAGDTLTFEWYHNTRDDDIIASSHHGPIAVYIAPAASNGQGNVWVKLFEDAYNVTNSTWAVDRLITAHGQHSVVVPHVAPGDYLFRAEIIALHEADSLYSQNPIRGAQFYISCAQITINSSDDSTPLPAGVPFPGAYTDSTPGIQFNIYTTPATSYVAPPPSVWSGALGGSIAQVGDASLE

3.2.1.4

COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:26928935, ECO:0000269|PubMed:28364950, ECO:0000269|PubMed:29057953, ECO:0000269|PubMed:32818374, ECO:0000269|PubMed:34389999, ECO:0000269|PubMed:35204695, ECO:0000269|PubMed:36071795}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:26928935, ECO:0000269|PubMed:28364950, ECO:0000269|PubMed:29057953, ECO:0000269|PubMed:32818374, ECO:0000269|PubMed:34389999, ECO:0000269|PubMed:35204695, ECO:0000269|PubMed:36071795};

cellulose catabolic process [GO:0030245]

extracellular region [GO:0005576]

cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; metal ion binding [GO:0046872]

PF03443;

2.70.50.70;

Polysaccharide monooxygenase AA9 family

PTM: The catalytically essential N-terminal histidine His-20 is post-translationally modified by methylation to prevent protonation of the histidine side chain, and protect the critical active site of the enzyme from oxidative damage. {ECO:0000269|PubMed:37452022}.

SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26928935}.

CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:26928935, ECO:0000269|PubMed:29057953, ECO:0000269|PubMed:32818374, ECO:0000269|PubMed:34389999};

FUNCTION: Lytic polysaccharide monooxygenase that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation product (PubMed:26928935, PubMed:29057953, PubMed:32818374). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (PubMed:26928935, PubMed:29057953). Is able to cleave phosphoric acid swollen cellulose (PASC) in the presence of a reducing agent, yielding a range of cellooligosaccharides dominated by cellobiose and cellotriose (PubMed:26928935). Activity is less sensitive to the reducing agent potential when cleaving xylan, suggesting that distinct catalytic mechanisms exist for xylan and glucan cleavage (PubMed:29057953). {ECO:0000269|PubMed:26928935, ECO:0000269|PubMed:29057953, ECO:0000269|PubMed:32818374}.

Panus similis (Lentinoid fungus) (Lentinus similis)

A0A0S2UWC9

CAMT1_PETHY

MAENGAAVQENQNVIRHQEVGHKSLLQSDALYQYILETSVYPREPESMKELRELTAKHPWNLMTTSADEGQFLNMLLKLINAKNTMEIGVYTGYSLLATALAIPHDGKILAMDINRENYEIGLPVIEKAGVAHKIDFREGPALPVLDQLVEDKNNHGTYDFIFVDADKDNYINYHKRIIDLVKVGGLIGYDNTLWNGSLVAPADTPMRKYVRYYRDFILELNKALAADPRIEICMLPVGDGITLGRRIS

2.1.1.-; 2.1.1.104

COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:Q40313}; Note=Binds 1 divalent metal cation per subunit. {ECO:0000250|UniProtKB:Q40313};

circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; lignin biosynthetic process [GO:0009809]; methylation [GO:0032259]; phenylpropanoid metabolic process [GO:0009698]

cytosol [GO:0005829]

caffeoyl CoA:S-adenosyl-L-methionine O-methyltransferase activity [GO:0080076]; caffeoyl-CoA O-methyltransferase activity [GO:0042409]; metal ion binding [GO:0046872]

PF01596;

3.40.50.150;

Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family, CCoAMT subfamily

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26620524}.

CATALYTIC ACTIVITY: Reaction=(E)-caffeoyl-CoA + S-adenosyl-L-methionine = (E)-feruloyl-CoA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16925, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87136, ChEBI:CHEBI:87305; EC=2.1.1.104; Evidence={ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:26620524}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16926; Evidence={ECO:0000269|PubMed:26620524}; CATALYTIC ACTIVITY: Reaction=(E)-5-hydroxyferuloyl-CoA + S-adenosyl-L-methionine = (E)-sinapoyl-CoA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:64860, ChEBI:CHEBI:15378, ChEBI:CHEBI:57393, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156249; Evidence={ECO:0000269|PubMed:26620524}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64861; Evidence={ECO:0000269|PubMed:26620524};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=5.8 pmol/sec/mg enzyme with (E)-caffeoyl-CoA as substrate {ECO:0000269|PubMed:26620524};

PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26620524}.

FUNCTION: Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (PubMed:26620524). Methylates caffeoyl-CoA to feruloyl-CoA, also able to methylate 5-hydroxyferuloyl-CoA (PubMed:26620524). {ECO:0000269|PubMed:26620524}.

Petunia hybrida (Petunia)

A0A0S4FKT4

VSP1_CRODO

VIGGDECNINEHNFLVALYEYWSQSFLCGGTLINGEWVLTAAHCDRKHILIYVGVHDRSVQFDKEQRRFPKEKYFFNCRNNFTKWDKDIMLIRLNKPVSYSEHIAPLSLPSSPPIVGSVCRVMGWGTIKSPQETLPDVPHCANINLLDYEVCRTAHPQFRLPATIRILCAGVLEGGIDTCHRDSGGPLICNGEFQGIVSWGDGSCAQPDKPALYSKVFDHLDWIQNIIAGSETVNCPS

3.4.21.-

proteolysis [GO:0006508]

extracellular space [GO:0005615]

potassium channel regulator activity [GO:0015459]; serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729]

PF00089;

2.40.10.10;

Peptidase S1 family, Snake venom subfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26227411}.

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.43 mM for TAME {ECO:0000269|PubMed:26227411}; KM=0.92 mM for S-2302 {ECO:0000269|PubMed:34506860}; Vmax=0.06 mmol/min/ug enzyme towards TAME {ECO:0000269|PubMed:26227411};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Activity is stable from pH 3.5 and 10.5. {ECO:0000269|PubMed:26227411};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. Activity is stable after incubation at 100 degrees Celsius for 30 minutes. {ECO:0000269|PubMed:26227411};

FUNCTION: Thrombin-like snake venom serine protease (PubMed:26227411, PubMed:31131001, PubMed:34506860). Releases fibrinopeptide A and B in the conversion of fibrinogen to fibrin, with preferential activity on the alpha chain of fibrinogen (PubMed:26227411, PubMed:34506860). Also hydrolyzes N-p-toluensulfonyl arginine ester (TAME) and chromogenic artificial substrates of the blood coagulation cascade: S-2222 for factor Xa, S-2302 for kallikrein and S-2238 for thrombin (PubMed:26227411). When tested in vitro, the recombinant protein does not degrade blood clots, suggesting that this toxin lacks fibrinolytic activity (PubMed:31131001). In addition, it moderately inhibits human Kv10.1/KCNH1/EAG1 currents, with a mechanism independent of its enzymatic activity. It selectively blocks Kv10.1/KCNH1/EAG1 in a time and dose-dependent manner (IC(50)=4.2 uM for native protein and IC(50)=2.5 uM for recombinant protein). It may have a preference in interacting with Kv10.1/KCNH1/EAG1 in its closed state, since the inhibitory effect of the toxin is decreased at more depolarized potentials. Corroboratively, it may have possible antitumor applications, since it reduces the viability of human breast cancer cell line MCF-7, which strongly expresses Kv10.1/KCNH1/EAG1, but does not affect the liver carcinoma and the non-tumorigenic epithelial breast cell lines, which weakly express Kv10.1/KCNH1/EAG1 (PubMed:32161292). When tested on peripheral blood mononuclear cells (PBMC), the native protein shows mild cytotoxicity, whereas the recombinant protein does not show any cytotoxicity (PubMed:34506860). Native form is not immununogenic, since it does not induce statistically significant antibody production in mice, whereas recombinant form shows an antibody titer slightly higher than the native form (PubMed:34506860). In vivo, subplantar injection in mice paw induces a discreet paw edema (PubMed:31131001). In addition, intraperitoneal injection of the recombinant protein into mice led to fibrinogen depletion, resulting in the blood incoagulability (PubMed:31131001). {ECO:0000269|PubMed:26227411, ECO:0000269|PubMed:31131001, ECO:0000269|PubMed:32161292, ECO:0000269|PubMed:34506860}.

Crotalus durissus collilineatus (Brazilian rattlesnake)

A0A0U1QT59

TMC_DROME

MQNDEEPAAAAGTSGLSNGESLRSPPAPAPRRPKPGILRLDIGKPRRSSGGSVDFRCVGSSSSNGNTSNVATGANSENNSGVTSPHQLSVTWAPPCDLDRGGWQMQSSADAKREFYKGQRGRRAASQEDHRSYELNDFPLQNQSSDAESCHQEPHFAHQRSPGIGFDEDGGGGDIDDEESYTISVSAIMQRRASVRGYRGKRGSRSSRRASSPMDHVLDSVERRRSSVYTTSSEEGTNQESTQEQIFENIRLHKEVIQSVKLQPWPIRKKLKLVRQAKTYVARHEGALQERFAMSRSTRDLWARFKILMAARWRHWKRETASFLTVLIPWELRIKEIESHFGSGVASYFTFLRWLMWVNIMIAIPLVAFVIGPEYFATKHGETDPRKRMSDPEARVAGNLFTFWEFEGYLKYSPMFYGYYSSTSGISTSGYKLPLAYFLTAVLVYIYSFVATLRKMAENSRNSKLSSKDDECVFSWKLFTGWDFMIGHAETAHNRIASVVVGFKEALLEEAEKKKDNRNWRVILQRILVNILVMGLLGLSGATVVLLVNHSEDLAKHDNWLSRNAVNVTMTLLSFFLPMIFEALGLFENWHPRQQLRLQLARIMILNMLNLYSLMFSFIYKINSKEKPLQMLKLENETNTMELKNLLSSIEALRAMTPTTSLYGESTSDGLFDDSTSTATWGEDGGGLFSTTAAAALISTTVQRLKCYNMTVKCSKLRRNIISGKHLATTLMVLNLTTPAMVPPTLPTTLPTTFPTTLPTTLPTTLPTALPTTLPTTLPTTLPSTLATTTATTSSIWSTTEETSPTTTTTSPWTTLPPSTTTTEATTTTERATTTTEATSTTTLKITTAEINSTLSDTTKPLGKSIDTEIPNSTTNSATLSTIPATLNTTNLPLNSTTKLTTTTSTEKPQGEDNFIYTTGEDEGSYDYGSDSTSDAPDNNSYSDITDYSSEPSEIEDFDEQESTDQADDPLAKVLEQLDENETKGRRKRALAESPFFTSKYSRRHRNESAVSAGQPRETTESVNATPSRWPFNWASFRQTTPRTTTTRRVPSGILTKEEWERLRRLRGRITTTTSTSTTSTTTRRPRWRYRTTTTELTSTTEEESSTTESSTDSSSPGSTTNAFDSSSSTTEEDEYTTTEGSENRPYYVGYVDISEMGSTIYYDGDSEFLEECVITICPKGDDFFGSTTESPDSTTQSSDSKQLTTVKLTPLERKQKRLKEVQLAIKQIQTNLTTMCWETSLGQELSKVIVFDGLMSIVAPLCIDFLRALFVRYVNQNWCWDMEKTFPQYGDFKIAENILTLINNQGQVWMGIFFSPGLVLINLVKLMIMMYFRSWIVLTCNVPHEVVFKASKSNNFYLSLLLTMLFLCVLPVGYAIVWLRPSWHCGPFSEYNRIAEFITNTTRNALPKQLHEPLDYLTSSSTVIPLLLLLILIIYYLVSLTGALREANQDLRTQLQKEREEERKKIFKVPEVKQAEPTATTLTNRWRKVLEASSPVTPTQPPDFDTEEYKNQARKELISRIMKKALRKGSATSDEDSFVRRDDDDTDTEHQDSLPHDEEAKDKRFGLSRLQQIRRTRKPSLVDIVQIAKQERARAGSIVAGTSSSGTGNFPIKETHPKSRFKVEKHERKDRGSMKDKKDTRHRQSPQQQQQPPPYESPKDNEHDPDTNSRIVSASLLRRHKEQAEGEEPPTTPDAPQTPNSPVEPVEQALEESTPETPTLAKSKFHIVDEKKPPPHEVEDKPLPTPKESGSGGGSLGKFKFRKHKFKSNNVAAVKPEPEVFKFDERSVERSSDVPATHAAEYLNNEPSGTEEQDRSLPSPTPSQGQGHHQRQLSVLSRQGRKKIGNLLALVREAVNLKKDDVEQAGSDESPGPTTPTYLAYTPPPPPSVLSSVSSSTALEMPPTPEPESPTPSAPLHFGSSTSSRAPSKPPKPPMVPASATAPTATMDDLEELDTAGPITFPRRSDSHRRRTMRQDSQSSIWSDNIPTITISTTGSDECIVDAAAPQNGLPDPRSASPEPTVNIIRIDIENEHEK

chemosensory behavior [GO:0007635]; detection of chemical stimulus involved in sensory perception of sweet taste [GO:0001582]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; larval locomotory behavior [GO:0008345]; perception of rate of movement [GO:0019232]; positive regulation of mechanosensory behavior [GO:1905792]; proprioception [GO:0019230]; regulation of egg-laying behavior [GO:0046662]; regulation of mechanosensory behavior [GO:1905790]

dendrite [GO:0030425]; plasma membrane [GO:0005886]

mechanosensitive monoatomic ion channel activity [GO:0008381]

PF07810;

TMC family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000269|PubMed:27478019}.

FUNCTION: Probable ion channel (PubMed:27478019, PubMed:30853433, PubMed:31184585, PubMed:32649914). Component of mechanosensitive neurons that participates in proprioception, sensing food texture, and directing egg-laying site selection (oviposition) (PubMed:27298354, PubMed:27478019, PubMed:30853433, PubMed:31184585, PubMed:32649914). Component of multi-dendritic neurons of the labellum (md-L) where it is required for sensing the hardness and viscosity of their food, enabling them to behaviorally discriminate their preferred softness and smoothness from harder and stickier food options (PubMed:27478019). Required as part of oviposition site selection process to relay mechanosensory and chemosensory information on the hardness and sweetness of potential egg-laying substrates, thus ensuring females select the most optimal site for their eggs survival (PubMed:31184585, PubMed:32649914). Females determine the softest substrate for their eggs first by making a coarse evaluation of substrate hardness using mechanosensitive channels nan and Piezo in the leg tarsal bristles, followed by a much finer assessment using nan, iav and Tmc mechanosensitive channels on the labellum (PubMed:31184585, PubMed:32649914). This protein is required to sense subtle differences in substrate stiffness (between 0.25% and 0.3% agarose), likely acting in the md-L neurons (PubMed:32649914). Also required in neurons on the labellum, including the md-Ls, and possibly in the brain, to inhibit discrimination of egg-laying substrates of different hardness if the substrate contains sucrose (PubMed:32649914). During oviposition evaluation, activation of sweet neurons by sucrose enhances the activity of the Tmc neurons resulting in females losing their softness preference in favor of egg-laying sites that contain sucrose (PubMed:32649914). Acts in the larvae peripheral sensory neurons, to contribute to proprioception and sensory feedback for normal forward crawling behavior (PubMed:27298354, PubMed:30853433). Required for the normal activity of the proprioceptive sensory dendrites, ddaE which show preferential responses to forward locomotion, and ddaD which show preferential responses to backward locomotion (PubMed:30853433). {ECO:0000269|PubMed:27298354, ECO:0000269|PubMed:27478019, ECO:0000269|PubMed:30853433, ECO:0000269|PubMed:31184585, ECO:0000269|PubMed:32649914}.

Drosophila melanogaster (Fruit fly)

A0A0U1RPR8

GUC2D_MOUSE

MAGLQQGCHFEGQNWTAPHWKTCLPCQGPWRLTVSHLKTVSSISVLSVVFWSVLLWADSLSLLAWARETFTLGVLGPWDCDPIFAQALPSIATQLAVDQVNQDASLLPGSQLDFKVLPTGCDTPHALATFVAHKNIVAAFVGPVNPGFCSAAALLAQGWGKSLFSWACEAPEGGGDLVPTLPSAADVLLSVMRHFGWARWAIVSSHQDIWVTTAQQLATAFRTHGLPIGLVTSLGPGEKGATEVCKQLHSVHGLKIVVLCMHSALLGGLEQTTLLHCAWEEGLTDGRLVFLPYDTLLFALPYGNRSYLVLDDHGPLQEAYDAVLTVSLESSPESHAFTATEMSGGATANLEPEQVSPLFGTIYDAVILLAHALNRSETHGAGLSGAHLGDHVRALDVAGFSQRIRTDGKGRRLAQYVILDTDGEGSQLVPTHILDTSTWQVQPLGKPIHFPGGSPPAHDASCWFDPNTLCIRGVQPLGSLLTLTIACVLALVGGFLAYFIRLGLQQLRLLRGPHRILLTSQELTFLQRTPSRRRPHVDSGSESRSVVDGGSPRSVTQGSARSLPAFLEHTNVALYQGEWVWLKKFEAGVAPDLRPSSLSFLRKLREMRHENVTAFLGLFVGPGVSAMVLEHCARGSLEDLLQNENLRLDWTFKASLLLDLIRGLRYLHHRRFPHGRLKSRNCVVDTRFVLKITDHGYAEFLESHCSSRPQPAPEELLWTAPELLRGPGKATFKGDVFSLAIILQEVLTRDPPYCSWGLSAEEIIRKVASPPPLCRPLVSPDQGPLECIQLMQLCWEEAPDDRPSLDQIYTQFKSINQGKKTSVVDSMLRMLEKYSESLEDLVQERTEELELERRKTERLLSQMLPPSVAHALKMGTTVEPEYFDQVTIYFSDIVGFTTISALSEPIEVVGFLNDLYTLFDAVLDSHDVYKVETIGDAYMVASGLPRRNGNRHAAEIANLALDILSYAGNFRMRHAPDVPIRVRAGLHSGPCVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHVSQSTVQALLSLDEGYKIDVRGQTELKGKGLEETYWLTGKVGFCRPLPTPLSIKPGDPWQDRINQEIRTGFAKARQGLAEPRKSGEAGPGP

4.6.1.2

cGMP biosynthetic process [GO:0006182]; detection of carbon dioxide [GO:0003031]; detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; intracellular signal transduction [GO:0035556]; olfactory behavior [GO:0042048]; olfactory learning [GO:0008355]; positive regulation of cGMP-mediated signaling [GO:0010753]; receptor guanylyl cyclase signaling pathway [GO:0007168]; sensory perception of smell [GO:0007608]

ciliary membrane [GO:0060170]; non-motile cilium [GO:0097730]; plasma membrane [GO:0005886]

adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; guanylate cyclase activity [GO:0004383]; natriuretic peptide receptor activity [GO:0016941]; odorant binding [GO:0005549]; olfactory receptor activity [GO:0004984]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672]

PF01094;PF00211;PF07714;

3.40.50.2300;6.10.250.780;3.30.70.1230;1.10.510.10;

Adenylyl cyclase class-4/guanylyl cyclase family

SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:9096404}; Single-pass type I membrane protein.

CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:P51839};

FUNCTION: Functions as an olfactory receptor activated by urine odorants, uroguanylin and guanylin and as well by the volatile semiochemicals carbon disulfide (CS2) and carbon dioxide (CO2) (PubMed:17702944, PubMed:17724338, PubMed:20637621). Has guanylate cyclase activity upon binding of the ligand (By similarity). Activation of GUCY2D neurons leads to the cGMP-dependent activation of the CNGA3 channels, membrane depolarization and an increase in action potential frequency (PubMed:17724338, PubMed:20637621). Signaling pathways activated by GUCY2D may trigger social behaviors such as acquisition of food preference (PubMed:20637621). {ECO:0000250|UniProtKB:P51839, ECO:0000269|PubMed:17702944, ECO:0000269|PubMed:17724338, ECO:0000269|PubMed:20637621}.

Mus musculus (Mouse)

A0A0U1RRE5

NBDY_HUMAN

MGDQPCASGRSTLPPGNAREAKPPKKRCLLAPRWDYPEGTPNGGSTTLPSAPPPASAGLKSHPPPPEK

mRNA processing [GO:0006397]; negative regulation of cytoplasmic mRNA processing body assembly [GO:0010607]; nuclear-transcribed mRNA catabolic process [GO:0000956]

P-body [GO:0000932]

SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:27918561}. Note=Localizes to P-bodies at low concentrations without dissociating them. {ECO:0000269|PubMed:27918561}.

FUNCTION: Promotes dispersal of P-body components and is likely to play a role in the mRNA decapping process. {ECO:0000269|PubMed:27918561}.

Homo sapiens (Human)

A0A0U3BRC5

GFDPS_LEUCN

MSHCTIFLYKYFPGKPRYQHCSFLHPLNHKLKSLFLPITGSRFLSNSTFSVSDSAHSHQAKPHVRNAQFDFKAYMLEKITAVNQALDAALPVREPVKIHEAMRYSLLLGGKRICPIVCLAACHLVGGDESTAMPSAAALEMIHAMSLMHDDLPCMDNDDLRRGRPSNHVVFGEGATVLAGYALIARAFEHIATATQGVGPGKILRVIGELAQLIGAEGVVGGQVVDLRCGGEGQMAIGLEQLEYIHLHKTAASVEASAVAGAVLGGASEEEIERLRKYSRSAGLLFQVVDDILDVTKSSEELGKTAGKDLAAGKTTYPKLLGMEKSREMAEKLKREAQEQLLGFDPIKAAPLIALVDFIAYRDK

2.5.1.81

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P14324}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324};

response to herbivore [GO:0080027]; response to insect [GO:0009625]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; terpenoid biosynthetic process [GO:0016114]

chloroplast [GO:0009507]

farnesyltranstransferase activity [GO:0004311]; geranylfarnesyl diphosphate synthase activity [GO:0044687]; metal ion binding [GO:0046872]; transferase activity [GO:0016740]

PF00348;

1.10.600.10;

FPP/GGPP synthase family

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:26941091}.

CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019, ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769; EC=2.5.1.81; Evidence={ECO:0000269|PubMed:26941091}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25695; Evidence={ECO:0000269|PubMed:26941091}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + 2 isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + 2 diphosphate; Xref=Rhea:RHEA:66852, ChEBI:CHEBI:33019, ChEBI:CHEBI:57907, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:26941091}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66853; Evidence={ECO:0000269|PubMed:26941091}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + 3 isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + 3 diphosphate; Xref=Rhea:RHEA:66856, ChEBI:CHEBI:33019, ChEBI:CHEBI:57907, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; Evidence={ECO:0000269|PubMed:26941091}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66857; Evidence={ECO:0000269|PubMed:26941091}; CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + 4 isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + 4 diphosphate; Xref=Rhea:RHEA:66860, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57907, ChEBI:CHEBI:128769; Evidence={ECO:0000269|PubMed:26941091}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66861; Evidence={ECO:0000269|PubMed:26941091};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=34.89 uM for dimethylallyl diphosphate (in the presence of isopentenyl diphosphate) {ECO:0000269|PubMed:26941091}; KM=3.04 uM for isopentenyl diphosphate (in the presence of geranylgeranyl diphosphate) {ECO:0000269|PubMed:26941091}; KM=6.28 uM for geranyl diphosphate (in the presence of isopentenyl diphosphate) {ECO:0000269|PubMed:26941091}; KM=4.1 uM for farnesyl diphosphate (in the presence of isopentenyl diphosphate) {ECO:0000269|PubMed:26941091}; KM=1.65 uM for geranylgeranyl diphosphate (in the presence of isopentenyl diphosphate) {ECO:0000269|PubMed:26941091}; Note=kcat is 16.9x10(-6) sec(-1) with dimethylallyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). kcat is 8.2x10(-6) sec(-1) with isopentenyl diphosphate as substrate (in the presence of geranylgeranyl diphosphate) (PubMed:26941091). kcat is 6.16x10(-6) sec(-1) with geranyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). kcat is 7.19x10(-6) sec(-1) with farnesyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). kcat is 5.17x10(-6) sec(-1) with geranylgeranyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). {ECO:0000269|PubMed:26941091};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30468448}.; PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:26941091}.

FUNCTION: Involved in the biosynthesis of leucosceptrane sesterterpenoids natural products, which are playing defensive roles toward herbivorus insects (e.g. Spodoptera exigua) (PubMed:26941091). Catalyzes the condensation of isopentenyl pyrophosphate (IDP) with the allylic pyrophosphates to yield geranylfarnesyl diphosphate (GFDP), the C(25) prenyl diphosphate precursor to all sesterterpenoids (PubMed:26941091). Geranylgeranyl diphosphate (GGPP) is the preferred substrate, however dimethylallyl diphosphate (DMADP), farnesyl diphosphate (FDP) and geranyl diphosphate (GDP) can also be used as allylic substrate (PubMed:26941091). {ECO:0000269|PubMed:26941091}.

Leucosceptrum canum (Hairy white-wand) (Clerodendron leucosceptrum)

A0A0X1KHF9

RPH_LISMF

MKPYVLKFQEIRPHSEALVGGKGMNLGACSNIEGVHVPAGFCLTTEAYKRTLAENNEFTQLLQRLSSLKTSDMDAIREISETIRTLIQHTQIPSEIASYMDATLLDVGGYEMPFAVRSSATAEDLPHASFAGQHDTYLNIIGKDALLQHISMCWASLFTERAIIYRIQNQFDHRKVQLAVVIQQMISPEASGILFTADPITSNRKSLSIDASFGLGEALVSGLVSADSYTVRENTITNKIIATKKLAIYSLKEGGTETRILEKSQQTKQTLTDQQIIQLAKLGRKIEAYFGKPQDIEWCLAEGAFYIVQSRPITTLYPIPEVNEPGNRVYISVAHQQMMTDAMKPLGLSFYLMTTPATMYTAGGRLFVDITQSLSAKVSRDMMVNSLGQSDPLIKDALLTVINKKGFLPPLPTEENPSHATVSGKPPVRSIPDSSSVFELVRNSENSIKHLKQSIETKSGSDLFDFIVEDLEELKRVLFNPTSIDAIMAGMDASAWLNEHIYQWLGEKNVADKLSESAPNNITSQMGLELLDVADVIRPYPAVRAYLEQTKNPDFMNELATLEGGAETKKALEDYLQKYGMRCAGEIDLTKTRWIENPLTLIPLILSNIKNFDSGASMHKFAQGEKEAFHKEQEILRRLQELPDGEQKAMETKEKIDILRHFIGYREYPKYGMINRYFIYKLALLRAGEQLVKDGILQEQEDIYFLYFEELREVVRTGQVDYELINVRKRDFATFEKLTPPRILTSDGEMINGEYKRENLPKDAILGLPVSSGTVEGRARVILDMEKADLEDGDILVTAYTDPSWTPAFVSIKGLVTEVGGLMTHGAVIAREYGLPAVVGVENATTIIKDGQQIRINGTEGYIEILD

2.7.9.6

phosphorylation [GO:0016310]; response to antibiotic [GO:0046677]

ATP binding [GO:0005524]; kinase activity [GO:0016301]

PF00391;PF01326;

3.30.1490.20;3.30.470.20;3.50.30.10;

Rifampicin phosphotransferase family

CATALYTIC ACTIVITY: Reaction=ATP + H2O + rifampicin = 21-phosphorifampicin + AMP + 2 H(+) + phosphate; Xref=Rhea:RHEA:56304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:71365, ChEBI:CHEBI:140195, ChEBI:CHEBI:456215; EC=2.7.9.6; Evidence={ECO:0000269|PubMed:24778229, ECO:0000269|PubMed:27001859, ECO:0000269|PubMed:27103605}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56305; Evidence={ECO:0000269|PubMed:24778229, ECO:0000269|PubMed:27001859, ECO:0000269|PubMed:27103605};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.27 uM for RIF {ECO:0000269|PubMed:24778229}; KM=0.57 uM for RIF {ECO:0000269|PubMed:27103605}; KM=27.21 uM for ATP {ECO:0000269|PubMed:24778229}; KM=8.38 uM for ATP {ECO:0000269|PubMed:27103605}; Note=kcat is 1.03 sec(-1) (PubMed:24778229). kcat is 2.87 sec(-1) with ATP as substrate. kcat is 2.25 sec(-1) with RIF as substrate (PubMed:27103605). {ECO:0000269|PubMed:24778229, ECO:0000269|PubMed:27103605};

FUNCTION: Catalyzes the phosphorylation of rifampicin, also known as rifampin (RIF), leading to its inactivation (PubMed:24778229, PubMed:27001859, PubMed:27103605). Confers high level resistance to a variety of clinically used rifamycin antibiotics (PubMed:24778229). Does not show phosphoenolpyruvate (PEP) synthase activity (PubMed:24778229). {ECO:0000269|PubMed:24778229, ECO:0000269|PubMed:27001859, ECO:0000269|PubMed:27103605}.

Listeria monocytogenes serotype 4b (strain F2365)

A0A125QXJ1

ABCB6_MESAU

MVTVGNYCEAEGPLGPAWAQNGLSPCFFFTLVPSTLMALGALALVLVLPCRRRDVPSGTEELFWAADSRVAPYALQLFLATLQVALPLAGLAGRVGTARGVRLPGYLLLASMLGSLASACGLWLLVAERRQARQSLAMGVWMKFRHSSGLLLLWTVAFAAENLALVSWNSPQWWWARADLGQQVQFGLWVLRYVISGGLFILGLWAPGLRPQSYTLRVHEADQDVERNQAQSTDRTSTWRDLGRKLRLLSSYLWPRGSPALQFIVLICLGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVLRVVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLFLTIVVTEWRAKFRRAMNTQENITRARAVDSLLNFETVKYYNAEGYEVERYREAIIKYQGLEWKSSASLVVLNQTQNLVIGLGLLAGSLLCAYFVSEQKLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKDVPGAGPLRFHKGQIEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRIAAGDSEVEAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVSADQILVIKDGCIIERGRHEALLSQGGVYAEMWQLQQKGQETVSEDSKPQDIA

7.6.2.5

cellular detoxification of cadmium ion [GO:0098849]; heme metabolic process [GO:0042168]; heme transmembrane transport [GO:0035351]; porphyrin-containing compound metabolic process [GO:0006778]

early endosome membrane [GO:0031901]; endolysosome membrane [GO:0036020]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; melanosome membrane [GO:0033162]; mitochondrial outer membrane [GO:0005741]; multivesicular body membrane [GO:0032585]; plasma membrane [GO:0005886]

ABC-type heme transporter activity [GO:0015439]; ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; heme binding [GO:0020037]

PF00664;PF00005;PF16185;

1.20.1560.10;3.40.50.300;

ABC transporter superfamily, ABCB family, Heavy Metal importer (TC 3.A.1.210) subfamily

PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NP58}.

SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q9NP58}. Late endosome membrane {ECO:0000250|UniProtKB:O70595}. Early endosome membrane {ECO:0000250|UniProtKB:O70595}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:Q9NP58}. Mitochondrion {ECO:0000250|UniProtKB:Q9NP58}. Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:Q9NP58}. Melanosome membrane {ECO:0000250|UniProtKB:Q9NP58}. Note=Present in the membrane of mature erythrocytes and in exosomes released from reticulocytes during the final steps of erythroid maturation. Traffics from endoplasmic reticulum to Golgi during its glycans's maturation, therefrom is first targeted to the plasma membrane, and is rapidly internalized through endocytosis to be distributed to the limiting membrane of multivesicular bodies and lysosomes. Localized on the limiting membrane of early melanosomes of pigment cells (By similarity). Targeted to the endolysosomal compartment (By similarity). {ECO:0000250|UniProtKB:O70595, ECO:0000250|UniProtKB:Q9NP58}.

CATALYTIC ACTIVITY: Reaction=ATP + H2O + heme b(in) = ADP + H(+) + heme b(out) + phosphate; Xref=Rhea:RHEA:19261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60344, ChEBI:CHEBI:456216; EC=7.6.2.5; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19262; Evidence={ECO:0000250|UniProtKB:Q9NP58}; CATALYTIC ACTIVITY: Reaction=ATP + coproporphyrin III(in) + H2O = ADP + coproporphyrin III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66664, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:131725, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66665; Evidence={ECO:0000250|UniProtKB:Q9NP58}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide a(out) + phosphate; Xref=Rhea:RHEA:61360, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58687, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361; Evidence={ECO:0000250|UniProtKB:Q9NP58}; CATALYTIC ACTIVITY: Reaction=ATP + coproporphyrinogen III(in) + H2O = ADP + coproporphyrinogen III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57309, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9DC29}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66681; Evidence={ECO:0000250|UniProtKB:Q9DC29}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + protoporphyrin IX(in) = ADP + H(+) + phosphate + protoporphyrin IX(out); Xref=Rhea:RHEA:61336, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57306, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61337; Evidence={ECO:0000250|UniProtKB:Q9NP58}; CATALYTIC ACTIVITY: Reaction=ATP + coproporphyrin I(in) + H2O = ADP + coproporphyrin I(out) + H(+) + phosphate; Xref=Rhea:RHEA:66768, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167478, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9DC29}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66769; Evidence={ECO:0000250|UniProtKB:Q9DC29}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + uroporphyrin I(in) = ADP + H(+) + phosphate + uroporphyrin I(out); Xref=Rhea:RHEA:66772, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167480, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9DC29}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66773; Evidence={ECO:0000250|UniProtKB:Q9DC29}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + uroporphyrin III(in) = ADP + H(+) + phosphate + uroporphyrin III(out); Xref=Rhea:RHEA:66776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167479, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9DC29}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66777; Evidence={ECO:0000250|UniProtKB:Q9DC29};

FUNCTION: ATP-dependent transporter that catalyzes the transport of a broad-spectrum of porphyrins from the cytoplasm to the extracellular space through the plasma membrane or into the vesicle lumen. May also function as an ATP-dependent importer of porphyrins from the cytoplasm into the mitochondria, in turn may participate in the de novo heme biosynthesis regulation and in the coordination of heme and iron homeostasis during phenylhydrazine stress. May also play a key role in the early steps of melanogenesis producing PMEL amyloid fibrils. In vitro, it confers to cells a resistance to toxic metal such as arsenic and cadmium and against chemotherapeutics agent such as 5-fluorouracil, SN-38 and vincristin (By similarity). In addition may play a role in the transition metal homeostasis (By similarity). {ECO:0000250|UniProtKB:O70595, ECO:0000250|UniProtKB:Q9NP58}.

Mesocricetus auratus (Golden hamster)

A0A126GUP6

MP1_DROME

MEPHFFFTVLWMLLMGTSSTYAQEIFGYCRTPDENSGTCINLRECGYLFELLQSEEVTEQDRRFLQASQCGYRNGQVLEKHFCFTNVQICCANSRMRNQQPQWGNHPQPTQTTKPTKRSGTKLLPMAPNCGENFGDRVVGGNETTKREFPWMALIEYTKPGNVKGHHCGGSLINHRYVLTAAHCVSAIPSDWELTGVRLGEWDASTNPDCTVGKNGRRDCNEPYVDYPVEERIPHPQYPGNSRDQLNDIALLRLRDEVQYSDFILPVCLPTLASQHNNIFLGRKVVVAGWGRTETNFTSNIKLKAELDTVPTSECNQRYATQRRTVTTKQMCAGGVEGVDSCRGDSGGPLLLEDYSNGNSNYYIAGVVSYGPTPCGLKGWPGVYTRVEAYLNWIENNVRA

3.4.21.-

melanization defense response [GO:0035006]; proteolysis [GO:0006508]; response to fungus [GO:0009620]; Toll receptor ligand protein activation cascade [GO:0160032]

endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; serine hydrolase activity [GO:0017171]; serine-type endopeptidase activity [GO:0004252]

PF12032;PF00089;

3.30.1640.30;2.40.10.10;

Peptidase S1 family, CLIP subfamily

FUNCTION: Serine protease which plays an essential role in the melanization immune response by acting downstream of sp7 to activate prophenoloxidase (PPO1) (PubMed:16861233). May function in diverse Hayan-dependent PPO1-activating cascades that are negatively controlled by different serpin proteins; Spn27A in the hemolymph and Spn77BA in the trachea (PubMed:16861233, PubMed:18854145). Regulation of melanization and PPO1 activation appears to be largely independent of the Toll signaling pathway (PubMed:16861233). {ECO:0000269|PubMed:16861233, ECO:0000269|PubMed:18854145}.

Drosophila melanogaster (Fruit fly)

A0A131MCZ8

CNNM3_CAEEL

MSKTPWALGLLIFLLTFTSPLSSSPVRSTDNSTSSKGLLNVNSSVILEPSILPSSASKPESLHLSKVRVSGLRLEAHASSTENIVLGHNKKHNVVVVPNKNVRVVLFGQNFQDIGALTFTADGSCKDLAHFFEADFSSMTPIRVVVEMSFPKTTESKDSFKLCVSEKFYANPQFVIVEDPFTMVTTEIPPVDEYMPKWLSWICLLILLCFSGLFSGLNLGLMTLSPYELQLYIASGTEQEKRDAGRILPIRKKGNQLLCTLLIGNVVVNVGVSLLMDQLVGSGFAVLVAATSCIVVFGEIIPQALCVKLGLPIGARTIPITQVLLFLMYPLTWPISKVLDIFLKEELTRSLERNKLVEMLKLSEKSIIGGQSDEFKMVLGALELYDKTVAHAMTRYEDIFMLPHTLTLGAGMVTQILDMGYTRIPIYENDRKNIVALLFVKDLALLDPDDNHNVMKIASIYNHEVRRVLVDMPLRNMLEEFKRGEYHMALVERLVEQEDKDPIYELCGLITLEDIIEEIIQCEIIDETDAVCDNVHRKKRQRKRNHDMSQIVNTAHAKCAINIQMLAVTIQVMSTCHKIFSSNYILPTILEKLIRKNCKKVETTQFSCLKEVGVVQPKPAVLFTKGEFSNKFIMILSGRAVVTIGKEEMRLEAGAWHSFGTEVLDAMAEAIERSLNQSTSRSTVSLNTEITNNSIGFIPDFDTVILYECVFCEITAADLLLAYNSSQIMQNNTKMQVVRSNSRISLIEEIPKDAVSTPIRNGSVKLRTVSEGETVHLLPKNMECHFNKQEKYEEEEE

determination of adult lifespan [GO:0008340]; innate immune response [GO:0045087]; intracellular manganese ion homeostasis [GO:0030026]; magnesium ion homeostasis [GO:0010960]; magnesium ion transport [GO:0015693]; positive regulation of gonad development [GO:1905941]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of vulval development [GO:0040026]; response to magnesium ion [GO:0032026]

basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]

transmembrane transporter activity [GO:0022857]

PF01595;

3.10.580.10;

ACDP family

SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:27564576}; Multi-pass membrane protein {ECO:0000255}.

FUNCTION: Probable metal transporter. Probably acts redundantly with the other metal transport proteins cnnm-1, cnnm-2, cnnm-4 and cnnm-5 to regulate Mg(2+) homeostasis. Promotes postembryonic gonad development by regulating Mg(2+) levels, probably via AMPK signaling. {ECO:0000269|PubMed:27564576}.

Caenorhabditis elegans

A0A139GI49

KAWA_MICA8

MKNPTLLPKLTAPVERPAVTSSDLKQASSVDAAWLNGDNNWSTPFAGVNAAWLNGDNNWSTPFAGVNAAWLNGDNNWSTPFAADGAE

defense response to bacterium [GO:0042742]

PTM: Kawaguchipeptin A contains a D-Leu and 2 prenylated Trp, whereas kawaguchipeptin B only contains unmodified amino acids. {ECO:0000269|PubMed:9249979, ECO:0000269|Ref.3}.; PTM: Kawaguchipeptin A is prenylated in vivo (Ref.3). Upon expression in E.coli of the whole operon, Trp residues are prenylated by C-prenyltransferase KgpF (PubMed:26846478). Prenylation by KgpF is likely the last enzymatic step in the biosynthetic maturation of kawaguchipeptin A (PubMed:26846478). {ECO:0000269|PubMed:26846478, ECO:0000269|Ref.3}.

FUNCTION: Both kawaguchipeptin A and B, which only differ by post-translational modifications, have antibacterial activities, since they inhibit the growth of the Gram-positive bacterium S.aureus at a concentration of 1 ug/mL. {ECO:0000269|PubMed:9249979}.

Microcystis aeruginosa (strain NIES-88 / KW-MA1-3)

A0A140H546

MAFB1_TOXGO

MWRIWRCRLSFLFATGCLLGALTAGLGSQMSDSVGRNVQAPAGVADASQEAGDVVEERTERTEEQAFALGPPRRHSSESLFPRNASVTARRRRNRRIALIATAVGVAVILAAVYVLRRRRAQRPQDPEPPAPRSVEDPEVLPEEDEASSSLPPPPPPSPPPPPPVEDPLSPESQTVDLSCLSGTTVRFFGPSHHFGGFTPLYDPAPDKRVATVDAGANALFIGGGGLNGQFAKTLLEEAEKHGIRLTPEELSQHSQRIQQSLLRRAVKSPGKLVELDTGVASPVFARSFGFVPVVPGLMWEESEVGPNVGVTFVHILKPEVTPYGNLNNNVMMYTVAPSGAAPDKTYSLAYKTTIAGVIGAAAAYNDTPAGQQYPVQGLRLPLLGGGIFRRNRSLESIGRANAEGTSLAITRYGPNFELQYMYDPSNAALHGLQEAESTYLASMLD

cytoplasmic vesicle membrane [GO:0030659]; symbiont-containing vacuole membrane [GO:0020005]

PTM: Phosphorylated. {ECO:0000269|PubMed:24781109}.

SUBCELLULAR LOCATION: Parasitophorous vacuole membrane {ECO:0000269|PubMed:24781109, ECO:0000269|PubMed:26920761, ECO:0000269|PubMed:28567444}; Single-pass type I membrane protein {ECO:0000305|PubMed:24781109}. Cytoplasmic granule membrane {ECO:0000269|PubMed:24781109}; Single-pass type I membrane protein {ECO:0000305|PubMed:24781109}. Note=Localizes to dense granules (PubMed:24781109). Localizes at the interface between the parasitophorous vacuole and the host outer mitochondrial membrane (PubMed:24781109, PubMed:26920761). {ECO:0000269|PubMed:24781109, ECO:0000269|PubMed:26920761}.

FUNCTION: During host cell infection by tachyzoites, required for tethering the parasitophorous vacuole to the host mitochondria (PubMed:24781109, PubMed:26920761, PubMed:28567444, PubMed:29505111, PubMed:33723040, PubMed:35025629). This process, known as host mitochondrial association (HMA), induces the formation of SPOTs (structures positive for outer mitochondrial membrane (OMM)), a cellular response to OMM stress, which leads to the constitutive shedding of OMM vesicles containing proteins such as mitofusins MFN1 and MFN2, which normally restrict parasite growth (PubMed:35025629). Specifically, binds to the host OMM import receptor TOMM70 to interact with SAMM50, a component of host mitochondrial intermembrane space bridging (MIB) complex (PubMed:28567444, PubMed:33723040, PubMed:35025629). By targeting SAMM50, induces the disassembly of the MIB complex, thereby promoting the formation of SPOTs (PubMed:35025629). Inhibits host TOMM70 import activity (PubMed:35025629). Plays a role in the modulation of the host innate immune response to parasite infection (PubMed:24781109, PubMed:30333181). {ECO:0000269|PubMed:24781109, ECO:0000269|PubMed:26920761, ECO:0000269|PubMed:28567444, ECO:0000269|PubMed:29505111, ECO:0000269|PubMed:30333181, ECO:0000269|PubMed:33723040, ECO:0000269|PubMed:35025629}.

Toxoplasma gondii

A0A140JWS2

PTMG_PENSI

MLFLAPGYIFPHVATPVTVAIDFAQAVKEGAYSFLDLKASPVPNPELFQPPSRVSIGMTGGREERNEEIIRGPLNYLLSLPGKDIRGKLIDALNEWFRVPEDKLSTIKEIIVILHTASLLIDDIQDSSQLRRGNPVAHRIFGVAQTINSANYAYFLAQAKLADLNDSRAFDIFTKGLLKLHRGQGMELYWRDNLICPTEEEYVEMVSCKTGGLFYLAVQLMQLNSEVTVNFSSFINLLGIIFQIRDDYMNLQSGTMTKTKGFSEDLTEGKFGYPIIHSIHAAPNDQQLIQILKLKTNDEVIKQYAVRYIESTGSFIYCREKLDLYLQEANETFQGLELLLGPSKGIRAILNFLRTR

2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};

alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386]

dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872]

PF00348;

1.10.600.10;

FPP/GGPP synthase family

CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000250|UniProtKB:Q12051};

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:25831977}.

FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems (PubMed:25831977). The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (PubMed:25831977). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (PubMed:25831977). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (PubMed:25831977). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ (PubMed:25831977). Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase ptmH which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase ptmD (PubMed:25831977). A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase ptmV and ptmI leads to the production of the prenylated form of penijanthine (PubMed:25831977). The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase ptmE (PubMed:25831977). Five sequential oxidative transformations performed by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various penitrem compounds. PtmK, ptmU and ptmM are involved in the formation of the key bicyclic ring of penitrem C via the formation of the intermediates secopenitrem D and penitrem D. PtmL catalyzes the epoxidation of penitrem D and C to yield penitrem B and F, respectively. PtmJ catalyzes the last benzylic hydroxylation to convert penitrem B to prenitrem E and penitrem F to penitrem A (PubMed:25831977). {ECO:0000269|PubMed:25831977}.

Penicillium simplicissimum

A0A140LI88

ANR31_MOUSE

MENGAEASDCDSDETVIEGSVTENEPEDEELPWRRLLLNQDTTCRSEFCFHSGVDGMQKGIHSPEIQLGLKLRKDSQEQNNKNKLLLALSEDLVLQDPQDKTAQNQVLLQTTKEFPVFTVSFPHPEVSWSHQNTGGHEAENCENLPHSKKELRENSDSPEVSLLSGTSPVAPDLVALKERLTEPVKTLAVPNTLSEPGEEVTQTMTSKETKDEESSLETFVSTLEKLLESSECTQEERLLEVMDDFNPQELFSTLSNSLGSVSVPLNAWAAQGRDELENKADAALPAKLLAAVNTGADVGPSCQGQEKSSSVSGGNGCLAVQPIMSQVDEDCTQIAQNIEDPKPFRLQTLTHENAISYEQINKKKNSDPIKNTSTQETPRVLRRSSRLEKLKASRDVVHTEAVLKKPERILSNTLSFKDQINSIFTTDSFSKRKNMHSSGFKNEQIRKSEQLRKKNGTGEMKKMCLCTINRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHDAVMNRHYKVAELLLMSGADPLFRSDHGTCALDEAKDSSMETLLMKYIPQQKKCHLSAQRNSTDPAHVEDMFQNKKPKLSSNNYTEFICDENFDRQEPGHLEINKGSNNLLMSKEYVCEHCQKDSNTTKFGKSNLNSVKNSRTNVSKRKGQKNRQQKKTQVDDRDCNLSQKIGTSSFRRTNKLLTQQQHAVQTLSDLPEESFELSTTTLSSLENGIGYNEACLVSKKSDTHVLDSSDGQELESVDQTEAASVSELSSYKEIKLLPVTTHQQPHTNQEQYSSPYKSLGNNSSNEKGKATNKWEDSFFSFIKGRSADSDSDCHTLDKSIASPKEGMSHDHHEEIMTGQEVDSQQRLSSENYFSQENDLKVHPLTTHPQEEAVNFCDSNLISVQHTPDYKNCLHEISFGNSYAKTEQSSTSCTRPPSTQKVSPLTVEVELLKGLQDSLAHRDSSPLVNQAGIHSLERKQDTDKNYTKKGPNTSSSSRPLPTVVHSQVIEITKAEKRREDLPGNEPINNTDFYSTDINKELANSSQLNQRKEKENVRKSDAELTHNDSEAERTLKSCEEKKKNMDSETHSPCDIQEHRKDQNFRKRKCSLKAPCSQGVNTTGIGKRNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHGASAGNHLKAAEILLEHGANPNQKDQKQRTALDEADDEKMKELLKSYGAIESTNGEKRNSTDLVKIPTVQPKRYKQFICDNDKAIGSPVPSHKAKKSESLPVHQTISAILQDIEEKQENLLKLEIRNSEDEEQYIGKMLEIKEVMDNILAQQKTERDDLAKKYRVSMESFKHGALREQLANLATRQKSLLVVAKKQKKIRLKIQNYKNATAVSGVGLRKLPCNSDISSDKKSQEPPTMGDSAHAQPGLLAPVSLAYGSMQEIPLSPEIESESQKINICLNAEAIRREEFSGNDINSKQNVQDCTLGGLLRSKPTDDAEKIASSSQPAALTPHAENSQAEATVKGCGFDSSALTGTINISEDKSIFSPNGACLAADPHSQKLSRCNPKRRNKKTASQQPSAGAAEPLPQAPAVLDTYTVHQTLPCLRDSAAAASHTDSTQSSLSSASAHQHPTKTVPHRNTTPRKKAVQLKDLILRGRINPGNNILEFKTQETTHRASVLPSGKLKGENGQIYQNPVTWLKELLGGGSYVTWNYAWNTVTYLGRELVKCVSEEAPMSAELNPPQLHQPHLSAGTSRESMQTIPHYLQIKEILQISKQELLPCHVMEQHWKFYVGRSHSEALLSW

homologous chromosome pairing at meiosis [GO:0007129]; meiotic DNA double-strand break formation involved in reciprocal meiotic recombination [GO:0010780]; positive regulation of meiotic DNA double-strand break formation [GO:1903343]

chromatin [GO:0000785]; nucleus [GO:0005634]

PF12796;PF18755;

1.25.40.20;

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31000436}. Chromosome {ECO:0000269|PubMed:31000436, ECO:0000269|PubMed:31003867}. Note=Localizes on chromatin between preleptotene and early pachytene (PubMed:31000436). Associates with the chromosome axes, but disappears from axes upon synaptonemal complex formation (PubMed:31000436). {ECO:0000269|PubMed:31000436}.

FUNCTION: Required for DNA double-strand breaks (DSBs) formation during meiotic recombination (PubMed:31000436, PubMed:31003867). Regulates the spatial and temporal patterns of pre-DSB recombinosome assembly and recombination activity by acting as a scaffold that anchors REC114 and other factors to specific genomic locations, thereby regulating DSB formation (PubMed:31000436, PubMed:31003867). Plays a key role in recombination in the pseudoautosomal regions of sex chromosomes (PubMed:31000436). {ECO:0000269|PubMed:31000436, ECO:0000269|PubMed:31003867}.

Mus musculus (Mouse)

A0A140LIF8

IRGM2_MOUSE

MEEAVESPEVKEFEYFSDAVFIPKDGNTLSVGVIKRIETAVKEGEVVKVVSIVKEIIQNVSRNKIKIAVTGDSGNGMSSFINALRLIGHEEKDSAPTGVVRTTQKPTCYFSSHFPYVELWDLPGLGATAQSVESYLEEMQISIYDLIIIVASEQFSLNHVKLAITMQRMRKRFYVVWTKLDRDLSTSTFPEPQLLQSIQRNIRDSLQKEKVKEHPMFLVSVFKPESHDFPKLRETLQKDLPVIKYHGLVETLYQVCEKTVNERVESIKKSIDEDNLHTEFGISDPGNAIEIRKAFQKTFGLDDISLHLVALEMKNKHFNTSMESQETQRYQQDDWVLARLYRTGTRVGSIGFDYMKCCFTSHHSRCKQQKDILDETAAKAKEVLLKILRLSIPHP

3.6.5.-

cellular response to interferon-beta [GO:0035458]; defense response [GO:0006952]; defense response to protozoan [GO:0042832]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640]; negative regulation of non-canonical inflammasome complex assembly [GO:0160076]; protein targeting to vacuolar membrane [GO:0044395]; response to bacterium [GO:0009617]

cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; vacuolar membrane [GO:0005774]

GTP binding [GO:0005525]; GTPase activity [GO:0003924]

PF05049;

3.40.50.300;

TRAFAC class dynamin-like GTPase superfamily, IRG family

PTM: Ubiquitinated; polyubiquitinated in the cytosol, promoting Gbp1 recruitment to the T.gondii parasitophorous vacuole membranes. {ECO:0000269|PubMed:34078740}.

SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:34078740}. Golgi apparatus membrane {ECO:0000269|PubMed:34078740}. Cytoplasm, cytosol {ECO:0000269|PubMed:34078740}. Note=Localizes to parasitophorous vacuole membranes. {ECO:0000269|PubMed:34078740}.

CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:34078740}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:34078740};

FUNCTION: Immunity-related GTPase that plays important roles in innate immunity and inflammatory response (PubMed:17641048, PubMed:33124745, PubMed:33124769, PubMed:34078740, PubMed:34338548). Acts as a dynamin-like protein that binds to intracellular membranes and promotes remodeling and trafficking of those membranes (By similarity). Required for clearance of acute protozoan and bacterial infections (PubMed:17641048, PubMed:34078740, PubMed:34338548). Acts by participating to Tgtp1/Irgb6 and Gbp1-mediated parasite killing by promoting their accumulation on the T.gondii parasitophorous vacuole membranes (PubMed:34078740). Also required for prolonged loading of ubiquitin and p62/Sqstm1 to parasitophorous vacuole membranes (PubMed:34078740). Also acts as a key negative regulator of the inflammatory response by inhibiting the non-canonical inflammasome, thereby protecting against Casp11-driven septic shock during endotoxemia (PubMed:33124745, PubMed:33124769). {ECO:0000250|UniProtKB:Q60766, ECO:0000269|PubMed:17641048, ECO:0000269|PubMed:33124745, ECO:0000269|PubMed:33124769, ECO:0000269|PubMed:34078740, ECO:0000269|PubMed:34338548}.

Mus musculus (Mouse)

A0A140N5J7

KDSC_ECOBD

MSKAGASLATCYGPVSADVMAKAENIRLLILDVDGVLSDGLIYMGNNGEELKAFNVRDGYGIRCALTSDIEVAIITGRKAKLVEDRCATLGITHLYQGQSNKLIAFSDLLEKLAIAPENVAYVGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCDLLLLAQGKLDEAKGQSI

3.1.3.45

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12639950}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:12639950}; Note=Mg(2+). The phosphatase activity is also stimulated by cobalt ions, whereas baryum, zinc, and manganese ions are less effective stimulators. {ECO:0000269|PubMed:12639950};

lipopolysaccharide biosynthetic process [GO:0009103]

3-deoxy-manno-octulosonate-8-phosphatase activity [GO:0019143]; metal ion binding [GO:0046872]

PF08282;

3.40.50.1000;

KdsC family

CATALYTIC ACTIVITY: Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate; Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45; Evidence={ECO:0000269|PubMed:12639950};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=75 uM for KDO 8-P {ECO:0000269|PubMed:12639950}; Vmax=500 umol/min/mg enzyme {ECO:0000269|PubMed:12639950}; Note=kcat is 175 sec(-1). {ECO:0000269|PubMed:12639950};

PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 3/3. {ECO:0000305|PubMed:12639950}.; PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. {ECO:0000305|PubMed:12639950}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. High catalytic activity is observed between pH 5.5 and 7.0. {ECO:0000269|PubMed:12639950};

FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. {ECO:0000269|PubMed:12639950}.

Escherichia coli (strain B / BL21-DE3)

A0A142I5B9

POLG_ZIKVK

MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGTDTSVGIVGLLLTTAMAVEVTRRGNAYYMYLDRSDAGEAISFPTTMGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLVWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAAKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVPINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMAICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRYGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPMLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMMRRIIGDEEKYVDYLSTQVRYLGEEGSTPGVL

2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13

fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]

extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell surface [GO:0044228]; membrane [GO:0016020]; viral capsid [GO:0019028]; virion membrane [GO:0055036]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198]

PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949;

1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10;

Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family

PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site. {ECO:0000250|UniProtKB:P17763}.; PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.; PTM: [Envelope protein E]: N-glycosylation plays a role in virulence in mammalian and mosquito hosts, but may have no effect on neurovirulence. {ECO:0000250|UniProtKB:A0A024B7W1}.; PTM: [Envelope protein E]: Ubiquitination by host TRIM7 promotes virus attachment and fusion of the virus and the host endosome membrane. {ECO:0000269|PubMed:32641828}.; PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is glycosylated, which is required for efficient secretion of the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.; PTM: [Non-structural protein 1]: Ubiquitination by host TRIM22 leads to proteasomal degradation. {ECO:0000250|UniProtKB:A0A024B7W1}.; PTM: [Serine protease NS3]: Ubiquitination by host TRIM22 leads to proteasomal degradation. {ECO:0000250|UniProtKB:A0A024B7W1}.; PTM: [Serine protease NS3]: Acetylated by host KAT5. Acetylation modulates NS3 RNA-binding and unwinding activities and plays an important positive role for viral replication. {ECO:0000250|UniProtKB:Q32ZE1}.; PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. {ECO:0000250|UniProtKB:P17763}.; PTM: [RNA-directed RNA polymerase NS5]: Sumoylated, required for regulating IFN induced interferon stimulated genes/ISGs. {ECO:0000250|UniProtKB:A0A024B7W1}.

SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host cell surface {ECO:0000269|PubMed:33432092}.; SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q32ZE1}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.

CATALYTIC ACTIVITY: [RNA-directed RNA polymerase NS5]: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase NS5]: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; Evidence={ECO:0000250|UniProtKB:Q32ZE1}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:Q32ZE1}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q9Q6P4};

FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of the mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Inhibits the integrated stress response (ISR) in the infected cell (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}.; FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH 6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Plays a role in host immune defense modulation and protection of envelope protein E during virion synthesis. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion. Contributes to fetal microcephaly in humans. Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Envelope protein E]: Binds to host cell surface receptors and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HAVCR1 in a cell-type specific manner (PubMed:32641828). In addition, host NCAM1 can also be used as entry receptor (PubMed:32753727). Interaction with host HSPA5 plays an important role in the early stages of infection as well (PubMed:33432092). Envelope protein is synthesized in the endoplasmic reticulum and forms a heterodimer with protein prM. The heterodimer plays a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimers between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes the dissociation of PrM-E heterodimers and formation of E homodimers. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:32641828, ECO:0000269|PubMed:32753727, ECO:0000269|PubMed:33432092}.; FUNCTION: [Non-structural protein 1]: Plays a role in the inhibition of host RLR-induced interferon-beta activation by targeting TANK-binding kinase 1/TBK1. In addition, recruits the host deubiquitinase USP8 to cleave 'Lys-11'-linked polyubiquitin chains from caspase-1/CASP1 thus inhibiting its proteasomal degradation. In turn, stabilized CASP1 promotes cleavage of cGAS, which inhibits its ability to recognize mitochondrial DNA release and initiate type I interferon signaling. {ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that recruits genomic RNA, the structural protein prM/E complex, and the NS2B/NS3 protease complex to the virion assembly site and orchestrates virus morphogenesis (PubMed:31662457). Antagonizes also the host alpha/beta interferon antiviral response (By similarity). May disrupt adherens junction formation and thereby impair proliferation of radial cells in the host cortex (By similarity). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000269|PubMed:31662457}.; FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. {ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). Leads to translation arrest when expressed ex vivo (By similarity). Disrupts host centrosome organization in a CEP63-dependent manner to degrade host TBK1 and inhibits innate immune response (By similarity). Inhibits the integrated stress response (ISR) in the infected cell (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). Cooperatively with NS4B suppresses the Akt-mTOR pathway and leads to cellular dysregulation (By similarity). By inhibiting host ANKLE2 functions, may cause defects in brain development, such as microcephaly (By similarity). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (By similarity). Leads to translation arrest when expressed ex vivo (By similarity). Inhibits the integrated stress response (ISR) in the infected cell (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place (By similarity). Also plays a role in the inhibition of host RLR-induced interferon-beta production at TANK-binding kinase 1/TBK1 level (By similarity). Cooperatively with NS4A suppresses the Akt-mTOR pathway and leads to cellular dysregulation (By similarity). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (By similarity). Methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Once sufficient NS5 is expressed, binds to the cap-proximal structure and inhibits further translation of the viral genome (By similarity). Besides its role in RNA genome replication, also prevents the establishment of a cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Mechanistically, interferes with host kinases TBK1 and IKKE upstream of interferon regulatory factor 3/IRF3 to inhibit the RIG-I pathway (By similarity). Antagonizes also type I interferon signaling by targeting STAT2 for degradation by the proteasome thereby preventing activation of JAK-STAT signaling pathway (By similarity). Within the host nucleus, disrupts host SUMO1 and STAT2 co-localization with PML, resulting in PML degradation (By similarity). May also reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:Q32ZE1}.

Zika virus (isolate ZIKV/Human/Cambodia/FSS13025/2010) (ZIKV)

A0A142ZC57

LOS_BOTBR

MKYTDFLAHPDEIIPTIRMMYADYRLKNMEIKDPSVRFCYNMLNRVSRSFAMVIQQLPVELRDATCVFYLILRALDTVEDDMAIPKEVKIPMLRTFHEHLSDRSWKIKCGYGPYVDLMDNYPLVTDVYLRFDEGTKAVIKDITRRMGNGMADFIDLDEVLTIPQYDLYCHYVAGLCGIGMCKLFVDSGLEKEDLVAEEDLANQMGLFLQKNNIVRDYLEDINELPAPRMFWPKEIWGNYAKQLDEFKDPKNLDKAMLCLNHMVTDALRHCEVGLRSLSLLHNPNILRAVLIPQVMGVRTLTLVYNNPEVFRGVVKMRRGETAKIFVTTTSKLSFFRTYLQFANEMEQKCLTEAKNDPMVALTLKRVQGVQAACRAAIVKAEIAEGAKGPSTAMVLAGALLIAALAYFAYVYSAGGTSLKALPLFGVVIILAIGLFGRNLALKTV

2.5.1.148; 2.5.1.21

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P37268};

cholesterol biosynthetic process [GO:0006695]; ergosterol biosynthetic process [GO:0006696]; farnesyl diphosphate metabolic process [GO:0045338]; sterol biosynthetic process [GO:0016126]

endoplasmic reticulum membrane [GO:0005789]

farnesyl-diphosphate farnesyltransferase activity [GO:0004310]; farnesyltranstransferase activity [GO:0004311]; metal ion binding [GO:0046872]; squalene synthase activity [GO:0051996]

PF00494;

1.10.600.10;

Phytoene/squalene synthase family

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21; Evidence={ECO:0000269|PubMed:27050299}; CATALYTIC ACTIVITY: Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate + NADP(+) + squalene; Xref=Rhea:RHEA:32295, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:175763; EC=2.5.1.21; Evidence={ECO:0000269|PubMed:27050299}; CATALYTIC ACTIVITY: Reaction=2 (2E,6E,10E)-geranylgeranyl diphosphate + H(+) + NADPH = all-trans-lycopaoctaene + 2 diphosphate + NADP(+); Xref=Rhea:RHEA:58176, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58756, ChEBI:CHEBI:142538; EC=2.5.1.148; Evidence={ECO:0000269|PubMed:27050299};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.07 mM for geranylgeranyl diphosphate {ECO:0000269|PubMed:27050299}; KM=0.13 mM for farnesyl diphosphate {ECO:0000269|PubMed:27050299}; KM=0.11 mM for phytil diphosphate {ECO:0000269|PubMed:27050299};

FUNCTION: Converts the C20 geranylgeranyl diphosphate (GGPP) to the C40 lycopaoctaene, the first committed intermediate in the production of lycopadiene (PubMed:27050299, PubMed:28813599). Converts farnesyl diphosphate (FPP) into squalene, a precursor for sterol biosynthesis in eukaryotes (PubMed:27050299, PubMed:28813599). Converts with low efficiency the C20 phytyl diphosphate (PPP) to the C40 lycopadiene in vitro. This reaction may not have biological significance in vivo (PubMed:27050299). {ECO:0000269|PubMed:27050299, ECO:0000269|PubMed:28813599}.

Botryococcus braunii (Green alga)

A0A143ZZK9

ATP4_PLAF7

MSSQNNNKQGGQDINNKKDSDDIKPSVSKEDLINSLKNDELNKNTTMDQNDMKKNENMNIKKNEVLNNSNNVEDGDNENSKFMNKSKEGLNNINGEKNDDNNSIVKVEESPKSIGYNYYASESIENLCKEFGLESINTGLNSEQVKINRDKYGENFIEKDEVVPVWLIFLSQYCSPVVLLLLVAAVASLALNEVVEGVAIISIVTLNACLATYMEKSSGDAIGKLAEMASPQCTVLRNGQKVVIPSREVVVGDVVLINTGDSISADLRLFDVIELKTNESLLTGESEDIKKTIVADNLSTPFATNLCFATTSVTSGSGKGIVISTGLDTQVGKIASQLKKSSKGSKLTPLQVALNKLGGLIGLIAIIVLVVIISLAVIIKYRDPAHADKDPTFVIIIIGVGFAVSSIPEGLPMVVTITLSAGAKDMVKKNANVRKLPAVETLGCCSVICSDKTGTLTEGKMTAINAVTICKNSSLSDENNKLTKTFDFYPTKGFEPCGGLFDSNELTSEKKKEIVIAKNQNTSYDKVLYNYGNPSNKSVIVDKTRSLMFAAYLNSYDTTLSRDPKTLKWGIHGNMSEGPIVVAAAKVGYSFINNPNHKSYLDNFQRLDDLEVTFNSSRKMKITFYKLKTVNVFENVYLDKPGKVYTHVALIKGAPDRLLDRSTHLLEETSMKKVQVSWNSTITQEERNVLIKKNLELSQKALRVLSICIKPLTDQNIEELKKLEDADERLKYVNYDENGGFIPMGYVASFDPPRPGVKEAIQTCREAQVKVIMITGDQKPTAVAIGKLIGLIEEKSEQVEDINSLAIECSELHINKNPNEPILPNDQLDEFTDKILIYSRAQPEDKITIVQSLKRKGYLVAMTGDGVNDAPALKAADIGVAMGINGTEVAKGASEMILIDDNFCTVVSAIDVGRTIFSNIQKFVCFLLGTNIGEIIYLSVAIVAQMPFPLEALQILFLNLMTDGCPAVALSREPPNDDNMKTPPRPKKQPIMTKRWWFYGILPHTIFEALCVLLSLAFSLYICTGFYNLNGIHNLCKTVNLVDVNDANVYHEYKYFCSSYEYRISTDYVGWVTNVSFWDPQNNEAVNFWGAAKGKVENINPLSDIVHPELRLRMQDGCSGDLTLDENGWCRPKDNKTSDGYNDELEGILKKGFEDVTAKGSKRGRTMAFISAVWCEMLRAYTVRSWEPFYKVFNRNMWMHLACSISATLTFLSTCIPGITSILNTTCLLWWQYLLAIFWALLNLFLDEIVPKVIYRRKYMTIKN

7.2.2.3

calcium ion transmembrane transport [GO:0070588]; intracellular calcium ion homeostasis [GO:0006874]; manganese ion transport [GO:0006828]

endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]

ABC-type sodium transporter activity [GO:0140679]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; P-type calcium transporter activity [GO:0005388]; P-type sodium transporter activity [GO:0008554]

PF13246;PF00689;PF00690;PF00122;PF00702;

3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;

Cation transport ATPase (P-type) (TC 3.A.3) family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20813948, ECO:0000269|PubMed:23414762, ECO:0000269|PubMed:29986883, ECO:0000269|PubMed:8813672}; Multi-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.3; Evidence={ECO:0000269|PubMed:23414762, ECO:0000269|PubMed:29986883, ECO:0000269|PubMed:31311978, ECO:0000269|PubMed:36180431}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14634; Evidence={ECO:0000305};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 mM for ATP (in the presence of 150-153 mM of Na(+)) {ECO:0000269|PubMed:29986883}; KM=16.1 mM for Na(+) {ECO:0000269|PubMed:29986883};

FUNCTION: Sodium-exporting ATPase (PubMed:23414762, PubMed:29986883, PubMed:31311978, PubMed:36180431). Required for the extrusion of Na(+) from the intraerythrocytic parasites to maintain a low cytosolic concentration of Na(+) (PubMed:23414762, PubMed:25322084, PubMed:25453091, PubMed:29555632, PubMed:36180431). {ECO:0000269|PubMed:23414762, ECO:0000269|PubMed:25322084, ECO:0000269|PubMed:25453091, ECO:0000269|PubMed:29555632, ECO:0000269|PubMed:29986883, ECO:0000269|PubMed:31311978, ECO:0000269|PubMed:36180431}.

Plasmodium falciparum (isolate 3D7)

A0A144A134

ISN1_PLAF7

MKNLDINTFDNIEDIPLGSSEQDPYDFFTLSDRNVMNSDMKKNIVQWNSRYSYNQLKNKDSLIMFLVEIFRSLFVSNCIDKNIDNVLLSIEEMFIDHYYNPQHSRLKYLIDDVGIFFTKLPITKAFHTYNKKYRITKRLYAPPTFNEVRHILNLAQILSLEEGLDLLTFDADETLYPDGHDFNDEVLASYISCLLKKMNIAIVTAASYNNDAEKYQKRLENLLKYFSKHNIKDGSYKNFYVMGGESNYLFKCNEEATLYSVPENEWRHYKKFVDYDTVQEILNISEKCLEKVIKDFGLCAQIQRKEKSIGLVPNKIPSLNIKNEQKNYMIKYEVLEEAVIRIKKEIIKNKITAPYCAFNGGQDLWVDVGNKAEGLLILQKLLKIQKKKCCHIGDQFLHSGNDFPTRFCSLTLWVSNPQETKACLKSIMHLNIKSFIPEVLYENQ

3.1.3.99

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32591529};

IMP catabolic process [GO:0006204]; inosine salvage [GO:0006190]; nicotinamide riboside biosynthetic process [GO:0071590]; nicotinic acid riboside biosynthetic process [GO:0071592]

cytoplasm [GO:0005737]

ATP binding [GO:0005524]; IMP 5'-nucleotidase activity [GO:0050483]; magnesium ion binding [GO:0000287]

PF06437;

3.40.50.1000;

ISN1 family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32591529}.

CATALYTIC ACTIVITY: Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718, ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053; EC=3.1.3.99; Evidence={ECO:0000269|PubMed:32591529};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.34 mM for IMP (at pH 5, 25 degrees Celsius and in the absence of ATP) {ECO:0000269|PubMed:32591529}; KM=66 mM for IMP (at pH 8, 25 degrees Celsius and in the absence of ATP) {ECO:0000269|PubMed:32591529}; KM=6.8 mM for IMP (at pH 8, 25 degrees Celsius and in the presence of ATP) {ECO:0000269|PubMed:32591529}; KM=105.5 mM for AMP (at pH 5, 25 degrees Celsius and in the absence of ATP) {ECO:0000269|PubMed:32591529}; KM=72.2 mM for AMP (at pH 8, 25 degrees Celsius and in the absence of ATP) {ECO:0000269|PubMed:32591529}; KM=71.7 mM for AMP (at pH 8, 25 degrees Celsius and in presence of ATP) {ECO:0000269|PubMed:32591529}; Note=kcat is 10.3 sec(-1) with IMP as substrate (at pH 5, 25 degrees Celsius and in the absence of ATP) (PubMed:32591529). kcat is 13.5 sec(-1) with IMP as substrate (at pH 8, 25 degrees Celsius and in the absence of ATP) (PubMed:32591529). kcat is 21 sec(-1) with IMP as substrate (at pH 8, 25 degrees Celsius and in the presence of ATP) (PubMed:32591529). kcat is 23.2 sec(-1) with AMP as substrate (at pH 5, 25 degrees Celsius and in the absence of ATP) (PubMed:32591529). kcat is 12.5 sec(-1) with AMP as substrate (at pH 8, 25 degrees Celsius and in the absence of ATP) (PubMed:32591529). kcat is 19.4 sec(-1) with AMP as substrate (at pH 8, 25 degrees Celsius and in the presence of ATP) (PubMed:32591529). {ECO:0000269|PubMed:32591529};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-5. {ECO:0000269|PubMed:32591529};

FUNCTION: Specifically, catalyzes the dephosphorylation of inosine monophosphate (IMP) into inosine (PubMed:32591529). By dephosphorylating IMP, plays a role in the purine salvage pathway (PubMed:32591529). Does not have phosphotransferase activity with IMP as phosphate donor and adenosine as phosphate acceptor (PubMed:32591529). {ECO:0000269|PubMed:32591529}.

Plasmodium falciparum (isolate 3D7)

A0A144A2H0

AMPP_PLAF7

MQLNFLLFVFIFLMVFHLNIFNKGKRQNLVSAYLNHFKKSYFSGVTSGSDCVNKSEVSSDNNNNNNNNNNKIAHNFFSKKYQRNFENNNLSENQENNKNIIYSGSNIFKNIYNTEMMSNNNTVDVNMMDNNPAARLEELRTIMKKNKIDVYILINSDEHNSEIINEKDKKIVKITNYSGADGILIVTKDKPILYVNALYELQAMNELDQNLFTLRISRIDNRDEIFETISSLEFNTIAFDGKNTSVVFYEKLRKALLNAYPKKKIVEKIIYNNNFDDVNKKDDENVLNFLVLEKSLVEIKDYPVNNKTLYIHDRKYNGACAGEKIDKLKQSLMYDIKNVDNLLLSELDEIAYLLNLRGYDYQYSPLFYSYLLFQFDREEQDFSKIVFFTTVKNLPADVKNLLEINKVIVKEYEEIVPYLRDVVIPSIPKHNDDNPDFKKYDISLSPYINLMIYKLFDRKNVLLQNSPVVKMKAVKNDVEIDNMKQAHILDGLALLQFFHWCEQKRKTKELFNETEMSLRHKVDYFRSTKKNFIFPSFSTISASGPNAAVIHYECTDKTNATIKPAIYLLDSGGQYLHGTTDVTRTTHFGEPTAEEKRIYTLVLKGHLRLRKVIFASYTNSSALDFIARENLFNNFMDYNHGTGHGVGLTLNVHEGGCSIGPVGGAPLKKNMVLSNEPGYYMKDKFGVRIENMQYVISKEITDTTEYLSFDDLTMYPYEKKLLDFSLLTNQEIKELNEYHTTIRNTLLPLVKQSPQEYGESVEKYLIEITEPIAIHNN

3.4.11.9

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19574214}; Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000269|PubMed:27462122};

hemoglobin catabolic process [GO:0042540]; proteolysis [GO:0006508]

cytoplasm [GO:0005737]; food vacuole [GO:0020020]; vacuolar lumen [GO:0005775]

manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]

PF01321;PF16189;PF00557;PF16188;

3.90.230.10;3.40.350.10;

Peptidase M24B family

PTM: The N-terminus may be proteolytically cleaved to generate a 73-kDa mature form. {ECO:0000269|PubMed:19574214}.

SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214}. Cytoplasm {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214}. Note=Localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested. {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214}.

CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; Evidence={ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214, ECO:0000269|PubMed:27462122};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.51 mM for human hemoglobin peptide HbPep1 (FPHFD) (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; KM=0.86 mM for human hemoglobin peptide HbPep1 (FPHFD) (at pH 5.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; KM=1.4 mM for human hemoglobin peptide HbPep2 (YPWTQ) (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; KM=1.8 mM for human hemoglobin peptide HbPep2 (YPWTQ) (at pH 5.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; Note=kcat is 8.6 sec(-1) with for human hemoglobin peptide HbPep1 (FPHFD) as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:19574214). kcat is 5.4 sec(-1) with for human hemoglobin peptide HbPep1 (FPHFD) as substrate (at pH 5.5 and 37 degrees Celsius) (PubMed:19574214). kcat is 1500 sec(-1) with for human hemoglobin peptide HbPep2 (YPWTQ) as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:19574214). kcat is 12 sec(-1) with for human hemoglobin peptide HbPep2 (YPWTQ) as substrate (at pH 5.5 and 37 degrees Celsius) (PubMed:19574214). {ECO:0000269|PubMed:19574214};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 (PubMed:19574214). Active at pH 5.5-7.5 (PubMed:19574214). {ECO:0000269|PubMed:19574214};

FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides (PubMed:17895246, PubMed:19574214, PubMed:27462122). In the food vacuole, involved in the final step of host hemoglobin catabolism, by cleaving hemoglobin-derived oligopeptides (PubMed:17895246, PubMed:19574214). In the cytoplasm, may be involved in the last steps of the turnover of ubiquitinated proteins (Probable). {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214, ECO:0000269|PubMed:27462122, ECO:0000305|PubMed:19574214}.

Plasmodium falciparum (isolate 3D7)

A0A144LUY5

CTCN1_ECHES

MMIKIAVVLCAVMATTMVRAKYVEEQELADLLDLLISEEVSSPDDAVALQGWWRRTVDKVRNAGRKVAGFASKACGALGHSPQEARAKVLEAFPEMKEADLDEEDIGKYCGYAHALNGR

defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]

FUNCTION: [Centrocin 1, heavy chain]: Has antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and against fungi with minimum inhibitory concentration (MIC) between 0.78 uM and 50 uM. Shows little hemolytic activity even at a concentration of 100 uM. {ECO:0000269|PubMed:27007817}.; FUNCTION: [Centrocin 1, light chain]: Has no antimicrobial activity. Shows no hemolytic activity. {ECO:0000269|PubMed:27007817}.

Echinus esculentus (Sea urchin)

A0A145P7T2

RAM1_LOTJA

MINSMCGSSVSLKSENSRNKPQPTSPNESVLQSKKNATQSSADLEQTSLNLTPPSLNLPALKFDLDGDVEVQSPDSSMWESFFSDHLLDGDFMISSPVRNNVPSPQASTFNSNYNYAHQGIQSQSLSGCSPPRFSSPLGAFNSNKGKGLSPLHRVFNSPNNQYMQHVENLALPAIEEFLEEYQGDHGLGGGGGYSNSSNKVSSDIGSSSECFDMQNHIPSMLDSLTMQNSSRYCGSVSEDSSVHGGSSQLSQDSDFYHQMGSMASASLSQALQQERYQEKQQKQHQTQQQQQPQQQQQNLTVPIPIGMDQEQDSGLQLVHLLLACAEAVAKEEYMLARRYLHHLNRVVTPLGDSMQRVAACFTESLSARLAATLTTKPQSISNGTSMPRSSSSSCLSPFPSNSIEVLKIYQIVYQACPYVKFAHFTANQAIFEAFEAEERVHVIDLDILQGYQWPTFMQALAARPGGAPFLRITGVGPCIDSVRETGRCLTELAHSLRIPFEFHPVGEQLEDLKPHMFNRRVGEALAVNTVNRLHRVPGSHLGNLLSMIRDQAPNIVTLVEQEASHNGPYFLGRFLEALHYYSAIFDSLDATFPPESAQRAKVEQYIFAPEIRNIVACEGAERIERHERLEKWRKIMEGKGFRGVALSPNAVTQSRILLGLYSCDGYRLTEDKGCLLLGWQDRAIIAASAWRC

arbuscular mycorrhizal association [GO:0036377]; regulation of DNA-templated transcription [GO:0006355]; response to symbiotic fungus [GO:0009610]

cytoplasm [GO:0005737]; nucleus [GO:0005634]

DNA-binding transcription factor activity [GO:0003700]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565]

PF03514;

GRAS family

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25560877}. Cytoplasm {ECO:0000269|PubMed:25560877}.

FUNCTION: Transcription factor acting as a central regulator of arbuscular mycorrhiza (AM)-related genes (e.g. PT4) required for the morphogenesis of arbuscules upon symbiosis with AM fungi (e.g. Rhizophagus irregularis) (PubMed:25560877, PubMed:27020747). Also involved in restricting mycorrhizal colonization of the root meristem (By similarity). {ECO:0000250|UniProtKB:A0A0M4FMK2, ECO:0000269|PubMed:25560877, ECO:0000269|PubMed:27020747}.

Lotus japonicus (Lotus corniculatus var. japonicus)

A0A151V4J3

AA13_PYRO7

MKWSVIQALALASGVQAHGYLTFPMSRTGLNAQAGPDTCPECTILEPVTAWPDLDSAQVGRSGPCGYNARVSVDYNQPGPRWGSAPVVTYKGGDVADVQWCVDNNGDHGGMFTYRICQDQALVDKLLTPGYLPSEAEKQAAENCFRAGTLPCTDVNGQSCGYSPDCSPGQACWRNDWFTCKGFQDTKCRGVDNAPLNSCYTSIAGGYTVSSRIKIPNYVSNHTLLSFKWNSFQTPQIYLTCADIKITAPDSQSPPTTTTTSTPASPPPTSCATPAASVAVTFRSKTTTSVGQTVKIAGSIAQLGGWDASKAPALSASQYTSSNPLWTTTISLPAGATFEYKFIRVESSGAVTYESGANRVYTVPRDCAGTATVDTAWK

1.14.99.55

COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q7SCE9}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q7SCE9};

polysaccharide catabolic process [GO:0000272]

extracellular region [GO:0005576]

metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; starch binding [GO:2001070]

PF00686;

2.60.40.10;

Polysaccharide monooxygenase AA13 family

PTM: O-mannosylated. {ECO:0000269|PubMed:27397613}.

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27397613}.

CATALYTIC ACTIVITY: Reaction=starch + reduced acceptor + O2 = D-glucono-1,5-lactone-terminated malto-oligosaccharides + short-chain malto-oligosaccharides + acceptor + H2O.; EC=1.14.99.55; Evidence={ECO:0000269|PubMed:27397613};

FUNCTION: Starch-active lytic polysaccharide monooxygenase that oxidizes the C1 position of starch substrates (PubMed:27397613). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable). {ECO:0000269|PubMed:27397613, ECO:0000305}.

Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)

A0A163UT06

SET17_CAEEL

MNIKHNYISYFQMNGIQIPGISNPEAIIPITGEKKSYKLVLDFNDGAISIIEARYLDSKLHREIQDLSDNDVTILGTEISDGAYDENLDIHCDKCNKFYRPYCRLHPLFKIPDRVLKRDESSNLSFSQQTLPILFRIEESKLPNAGLGVIAEVFIPVGMVFGPYKGRRCQKKTDFYKDGYAWLIKSGDKRFYIDGSDAERSNWLRYINSPRFEDEQNMLAFQTNGKIFYRVIKPIRINQELLVWYGSSYGNEFVESENGNKYKKPAKNPFICVGAQR

2.1.1.-; 2.1.1.364

methylation [GO:0032259]; oligodendrocyte development [GO:0014003]; regulation of DNA-templated transcription [GO:0006355]

nucleus [GO:0005634]

histone H3K4 methyltransferase activity [GO:0042800]; histone H3K4 monomethyltransferase activity [GO:0140945]

PF21549;

2.170.270.10;

Class V-like SAM-binding methyltransferase superfamily

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29702639}. Note=In males and hermaphrodites, localizes to foci in the nucleus of spermatocytes, which express the mono- and di-methyl states of 'Lys-4' of histone H3 (PubMed:29702639). These foci are stable nuclear structures with slow diffusion and liquid-like properties (PubMed:29702639). In turn, these foci co-localize with the transcription start sites for major sperm proteins (PubMed:29702639). {ECO:0000269|PubMed:29702639}.

CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:24685137}; CATALYTIC ACTIVITY: Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364; Evidence={ECO:0000269|PubMed:24685137};

FUNCTION: Histone methyltransferase that specifically mono- and di-methylates 'Lys-4' of histone H3 in vitro (PubMed:24685137). Does not tri-methylate 'Lys-4' of histone H3 in vitro (PubMed:24685137). Promotes spermatid development and fertility by positively regulating the transcription of spermatocyte-specific genes in primary spermatocytes (PubMed:29702639). Together with spr-5, required for transgenerational fertility (PubMed:24685137). {ECO:0000269|PubMed:24685137, ECO:0000269|PubMed:29702639}.

Caenorhabditis elegans

A0A166U5H3

BMT_KITPR

MAGMKTSPSQDEEACVLAIQLATSTVLPMILKSAIELDILNTISKAGPGNYLSPSDLASKLLMSNPHAPIMLERILRVLATYKVLGCKPSELSDGEVEWLYCWTPVCKFLSNNEDGASIAPLLLVHQDQVPMKSWYHLTDAILDGGTAFNKAYGMNIFDYASQDPQFNKVFNRSMAGHSTITMKKILETYNGFEGLKSIVDVGGGSGATLNMIISKYPTIKGINFDLPHVVGDSPIHPGVEHVGGDMFASVPKGDAIFLKWIFHSWSDEDCLRILKNCYEALADNKKVIVAEFIIPEVPGGSDDATKSVVHLDAVMLAYVPGGKERTEKEFEALATSAGFKSFRKVCCAFNTWIMEFSK

2.1.1.69

aromatic compound biosynthetic process [GO:0019438]; coumarin biosynthetic process [GO:0009805]; methylation [GO:0032259]; response to jasmonic acid [GO:0009753]

cytoplasm [GO:0005737]

5-hydroxyfuranocoumarin 5-O-methyltransferase activity [GO:0030752]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

PF08100;PF00891;

3.40.50.150;1.10.10.10;

Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family, COMT subfamily

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27252733}.

CATALYTIC ACTIVITY: Reaction=bergaptol + S-adenosyl-L-methionine = bergapten + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11808, ChEBI:CHEBI:18293, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77728; EC=2.1.1.69; Evidence={ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11809; Evidence={ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994};

PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}.; PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}.

FUNCTION: O-methyltransferase involved in the biosynthesis of furocoumarins natural products such as bergapten, a photosensitizer used for medical purpose such as treating psoriasis and vitiligo or facilitating resistance to microbial infection and other stresses (PubMed:27252733, PubMed:30934718, PubMed:31666994). Catalyzes specifically the methylation of bergaptol (PubMed:27252733, PubMed:30934718, PubMed:31666994). Not active on xanthotol, isoscopoletin, scopoletin and esculetin (PubMed:27252733, PubMed:30934718). {ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}.

Kitagawia praeruptora (Peucedanum praeruptorum)

A0A172J1V3

PHZM_LYSAN

MTENNRAGAVPLSSILLQMITGYWVTQSLYVAAKLGIADLVADAPKPIEELAAKTGAKAPLLKRVLRTIASIGVFTETEPGIFGITPLAALLRSGTPDSMRPQAIMHGEEQYRAWADVLHNVQTGETAFEKEFGTSYFGYLAKHPEADRVFNEAQAGYTKQVAHAVVDAYDFSPFKTVIDIGAGYGPLLSAILRSQPEARGILFDQPHVAQAAGKRLAEAGVGDRCGTVGGDFFVEVPADGDVYILSLLLHDWDDQRSIEILRNCRRAMPAHGKLLIVELVLPEGEEPFFGKWLDLHMLVLLGAQERTADEFKTLFAASGFALERVLPTASGLSIVEARPI

2.1.1.-

methylation [GO:0032259]; phenazine biosynthetic process [GO:0002047]

identical protein binding [GO:0042802]; O-methyltransferase activity [GO:0008171]; protein homodimerization activity [GO:0042803]; S-adenosyl-L-methionine binding [GO:1904047]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

PF16864;PF00891;

3.40.50.150;1.10.10.10;

Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family

CATALYTIC ACTIVITY: Reaction=1,6-dihydroxyphenazine + S-adenosyl-L-methionine = 1-hydroxy-6-methoxyphenazine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:72523, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192365, ChEBI:CHEBI:192366; Evidence={ECO:0000269|PubMed:29510028}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72524; Evidence={ECO:0000269|PubMed:29510028}; CATALYTIC ACTIVITY: Reaction=1-hydroxy-6-methoxyphenazine + S-adenosyl-L-methionine = 1,6-dimethoxyphenazine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:72527, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192366, ChEBI:CHEBI:192367; Evidence={ECO:0000269|PubMed:29510028}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72528; Evidence={ECO:0000269|PubMed:29510028}; CATALYTIC ACTIVITY: Reaction=1-hydroxy-6-methoxyphenazine N(10)-oxide + S-adenosyl-L-methionine = 1,6-dimethoxyphenazine N(5)-oxide + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:72635, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192368, ChEBI:CHEBI:192369; Evidence={ECO:0000269|PubMed:29510028}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72636; Evidence={ECO:0000269|PubMed:29510028}; CATALYTIC ACTIVITY: Reaction=1,6-dihydroxyphenazine N(5),N(10)-dioxide + S-adenosyl-L-methionine = 1-hydroxy-6-methoxyphenazine N(5),N(10)-dioxide + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:72639, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192372, ChEBI:CHEBI:192373; Evidence={ECO:0000269|PubMed:29510028}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72640; Evidence={ECO:0000269|PubMed:29510028}; CATALYTIC ACTIVITY: Reaction=1-hydroxy-6-methoxyphenazine N(5),N(10)-dioxide + S-adenosyl-L-methionine = 1,6-dimethoxyphenazine N(5),N(10)-dioxide + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:72643, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192373, ChEBI:CHEBI:192374; Evidence={ECO:0000269|PubMed:29510028}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72644; Evidence={ECO:0000269|PubMed:29510028};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33.6 uM for 6-hydroxy-1-methoxyphenazine N(5)-oxide (at pH 7.8 and at room temperature) {ECO:0000269|PubMed:29510028}; Vmax=2.9 umol/min/mg enzyme with 6-hydroxy-1-methoxyphenazine N(5)-oxide as substrate (at pH 7.8 and at room temperature) {ECO:0000269|PubMed:29510028}; Note=kcat is 0.6 min(-1) with 6-hydroxy-1-methoxyphenazine N(5)-oxide as substrate. {ECO:0000269|PubMed:29510028};

FUNCTION: Involved in the biosynthesis of phenazine natural products including myxin, an N(5),N(10)-dioxide phenazine antiobiotic, which has antimicrobial activity. O-methyltransferase, which converts iodinin (1,6-dihydroxyphenazine N(5),N(10)-dioxide) to myxin (1-hydroxy-6-methoxyphenazine N(5),N(10)-dioxide). Catalyzes both monomethoxy and dimethoxy formation of phenazine natural compounds. Acts on a wide variety of substrates, catalyzing O-methylation of phenazines with non-, mono- or di-N-oxide. Highest activity with 1,6-dihydroxyphenazine (DHP) as substrate. Less active with monohydroxy-containing and monohydroxy-monomethoxy-containing phenazines. Least active with non-phenazine substrates, such as 8-hydroxyquinoline and 6-hydroxyquinoline. Is not able to convert 1-hydroxyphenazine to 1-hydroxy-N5-methylphenazine (pyocyanine), hence does not function as an N-methyltransferase. {ECO:0000269|PubMed:29510028}.

Lysobacter antibioticus

A0A172U6X0

LR3E_METSD

MAFPKRLEYGGHALVWSGDWSAAGARKAIAGAARAGYDYIEIALLDPWQIDVALTKDLLQEYNLRAHASLGLSAATDVTSTDPAIVAKGDELLRKATDVLYALGGSELCGVIYCALGKYPGPASRENRANSVAAMQRLADYAADKGINIDLEVVNRYETNIMNTGLEGLAFLDEVNRPNAFLHLDTYHMNIEENGMAKSVLAAGDRLGYVHIGESHRGYLGTGNVDFASFFAALKQIDYRGPITFESFSSEIVDPKLSNTLCVWRNLWHDSDDLAGKALEFIKQRY

5.1.3.31

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:33838083};

isomerase activity [GO:0016853]; metal ion binding [GO:0046872]

PF01261;

3.20.20.150;

Hyi family

CATALYTIC ACTIVITY: Reaction=L-ribulose = L-xylulose; Xref=Rhea:RHEA:53268, ChEBI:CHEBI:16880, ChEBI:CHEBI:17399; EC=5.1.3.31; Evidence={ECO:0000269|PubMed:33838083}; CATALYTIC ACTIVITY: Reaction=D-ribulose = D-xylulose; Xref=Rhea:RHEA:51544, ChEBI:CHEBI:17140, ChEBI:CHEBI:17173; EC=5.1.3.31; Evidence={ECO:0000269|PubMed:33838083}; CATALYTIC ACTIVITY: Reaction=D-allulose = keto-D-fructose; Xref=Rhea:RHEA:42360, ChEBI:CHEBI:27605, ChEBI:CHEBI:48095; EC=5.1.3.31; Evidence={ECO:0000269|PubMed:33838083}; CATALYTIC ACTIVITY: Reaction=keto-L-tagatose = keto-L-sorbose; Xref=Rhea:RHEA:61780, ChEBI:CHEBI:13172, ChEBI:CHEBI:134275; Evidence={ECO:0000269|PubMed:33838083}; CATALYTIC ACTIVITY: Reaction=keto-D-tagatose = keto-D-sorbose; Xref=Rhea:RHEA:43048, ChEBI:CHEBI:13022, ChEBI:CHEBI:47693; EC=5.1.3.31; Evidence={ECO:0000269|PubMed:33838083};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=22.4 mM for L-ribulose {ECO:0000269|PubMed:33838083}; KM=27.8 mM for L-allulose {ECO:0000269|PubMed:33838083}; Note=kcat is 4923 min(-1) with L-ribulose as substrate. kcat is 4103 min(-1) with D-allulose as substrate. {ECO:0000269|PubMed:33838083};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius with D-allulose as substrate. {ECO:0000269|PubMed:33838083};

FUNCTION: Catalyzes the epimerization of various ketoses at the C(3) position (PubMed:33838083). Exhibits the highest enzymatic activity toward L-ribulose, followed by D-ribulose, D-allulose and D-fructose (PubMed:33838083). Shows lower activity with L-xylulose, L-tagatose, D-xylulose, D-tagatose, L-sorbose, D-sorbose, and weak activity with L-allulose and L-fructose (PubMed:33838083). {ECO:0000269|PubMed:33838083}.

Methylomonas sp. (strain DH-1)

A0A178VEK7

DUO1_ARATH

MRKMEAKKEEIKKGPWKAEEDEVLINHVKRYGPRDWSSIRSKGLLQRTGKSCRLRWVNKLRPNLKNGCKFSADEERTVIELQSEFGNKWARIATYLPGRTDNDVKNFWSSRQKRLARILHNSSDASSSSFNPKSSSSHRLKGKNVKPIRQSSQGFGLVEEEVTVSSSCSQMVPYSSDQVGDEVLRLPDLGVKLEHQPFAFGTDLVLAEYSDSQNDANQQAISPFSPESRELLARLDDPFYYDILGPADSSEPLFALPQPFFEPSPVPRRCRHVSKDEEADVFLDDFPADMFDQVDPIPSP

cell cycle G2/M phase transition [GO:0044839]; generative cell mitosis [GO:0055047]; pollen sperm cell differentiation [GO:0048235]; positive regulation of DNA-templated transcription [GO:0045893]

generative cell nucleus [GO:0048555]; nucleus [GO:0005634]

DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]

PF00249;

1.10.10.60;

SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:15694308}. Note=Accumulates in sperm-cell nuclei. {ECO:0000269|PubMed:15694308}.

FUNCTION: Transcription activator that acts as a positive regulator of male germline development by promoting both gametic cell specification and cell cycle progression (PubMed:15618418, PubMed:15694308, PubMed:19300502, PubMed:21285328). Binds to canonical MYB sites 5'-AACCGTC-3', 5'-AAACCGC-3' and 5'-AACCGT-3' in promoters to trigger the expression of male germline-specific or enriched genes (e.g. MGH3, GEX2 and GCS1), including those required for fertilization (PubMed:19300502, PubMed:21285328). Required for sperm cell specification leading to pollen maturation by activating a germline-specific regulon (PubMed:15618418, PubMed:15694308, PubMed:19300502, PubMed:21285328). Involved in pollen mitosis entry at G2-M transition via the regulation of CYCB1-1, DAZ1 and DAZ2 expression (PubMed:15618418, PubMed:19300502, PubMed:24876252). {ECO:0000269|PubMed:15618418, ECO:0000269|PubMed:15694308, ECO:0000269|PubMed:19300502, ECO:0000269|PubMed:21285328, ECO:0000269|PubMed:24876252}.

Arabidopsis thaliana (Mouse-ear cress)

A0A178WF56

CSTM3_ARATH

MAQYHQQHEMKQTMAETQYVTAPPPMGYPVMMKDSPQTVQPPHEGQSKGSGGFLRGCLAAMCCCCVLDCVF

negative regulation of response to salt stress [GO:1901001]; regulation of reactive oxygen species biosynthetic process [GO:1903426]; response to salt stress [GO:0009651]; sodium ion homeostasis [GO:0055078]

cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]

PF12734;

CYSTM1 family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29272523}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:29272523}. Mitochondrion {ECO:0000269|PubMed:30701352}.

FUNCTION: Negatively regulates salt stress responses and Na(+) homeostasis (PubMed:29272523, PubMed:30701352). Prevents Na(+) efflux, disturbs reactive oxygen species (ROS) homeostasis, and represses the expression of nuclear salt stress-responsive genes (PubMed:30701352). Involved in resistance to abiotic stress (PubMed:29272523). {ECO:0000269|PubMed:29272523, ECO:0000269|PubMed:30701352, ECO:0000303|PubMed:29272523}.

Arabidopsis thaliana (Mouse-ear cress)

A0A193AU77

GGT24_PUNGR

MGSESLVHVFLVSFPGQGHVNPLLRLGKRLASKGLLVTFTTPESIGKQMRKASNIGEEPSPIGDGFIRFEFFEDGWDEDEPRRQDLDQYLPQLEKVGKEVIPRMIKKNEEQNRPVSCLINNPFIPWVSDVAESLGLPSAMLWVQSCACFAAYYHYYHGLVPFPSESAMEIDVQLPCMPLLKHDEVPSFLYPTTPYPFLRRAIMGQYKNLDKPFCVLMDTFQELEHEIIEYMSKICPIKTVGPLFKNPKAPNANVRGDFMKADDCISWLDSKPPASVVYVSFGSVVYLKQDQWDEIAFGLLNSGLNFLWVMKPPHKDSGYQLLTLPEGFLEKAGDKGKVVQWSPQEQVLAHPSVACFVTHCGWNSSMEALSSGMPVVAFPQWGDQVTDAKYLVDVFKVGVRMCRGEAENKLIMRDVVEKCLLEATVGPKAAEVKENALKWKAAAEAAVAEGGSSDRNIQAFVDEVKRRSIAIQSNKSEPKPVVQNAAVADHFGAKATTNGVAADLAGSNADGKVELVA

2.4.1.120; 2.4.1.136; 2.4.1.170; 2.4.1.177; 2.4.1.194; 2.4.1.81

3,4-dihydroxybenzoate metabolic process [GO:0046278]; cinnamic acid ester metabolic process [GO:0009801]; ferulate metabolic process [GO:0033494]

cytoplasm [GO:0005737]

4-hydroxybenzoate 4-O-beta-D-glucosyltransferase activity [GO:0047250]; cinnamate beta-D-glucosyltransferase activity [GO:0050412]; flavone 7-O-beta-glucosyltransferase activity [GO:0047891]; gallate 1-beta-glucosyltransferase activity [GO:0047913]; isoflavone 7-O-glucosyltransferase activity [GO:0050004]; quercetin 3-O-glucosyltransferase activity [GO:0080043]; quercetin 7-O-glucosyltransferase activity [GO:0080044]; sinapate 1-glucosyltransferase activity [GO:0050284]; UDP-glucosyltransferase activity [GO:0035251]

PF00201;

3.40.50.2000;

UDP-glycosyltransferase family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27227328}.

CATALYTIC ACTIVITY: Reaction=3,4,5-trihydroxybenzoate + UDP-alpha-D-glucose = 1-O-galloyl-beta-D-glucose + UDP; Xref=Rhea:RHEA:15249, ChEBI:CHEBI:15834, ChEBI:CHEBI:16918, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.136; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=3,4-dihydroxybenzoate + UDP-alpha-D-glucose = 1-O-(3,4-dihydroxy-benzoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:52844, ChEBI:CHEBI:36241, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:136876; EC=2.4.1.136; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=4-hydroxybenzoate + UDP-alpha-D-glucose = 4-(beta-D-glucosyloxy)benzoate + H(+) + UDP; Xref=Rhea:RHEA:15153, ChEBI:CHEBI:11935, ChEBI:CHEBI:15378, ChEBI:CHEBI:17879, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.194; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamate + UDP-alpha-D-glucose = 1-O-(trans-cinnamoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:13437, ChEBI:CHEBI:15669, ChEBI:CHEBI:16279, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.177; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-sinapate + UDP-alpha-D-glucose = 1-O-(trans-sinapoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:13305, ChEBI:CHEBI:16546, ChEBI:CHEBI:30023, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.120; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumarate + UDP-alpha-D-glucose = 1-O-(trans-4-coumaroyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:57472, ChEBI:CHEBI:12876, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:71498; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-caffeate + UDP-alpha-D-glucose = 1-O-[(E)-caffeoyl]-beta-D-glucose + UDP; Xref=Rhea:RHEA:57464, ChEBI:CHEBI:614, ChEBI:CHEBI:57770, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-ferulate + UDP-alpha-D-glucose = 1-O-[(E)-feruloyl]-beta-D-glucose + UDP; Xref=Rhea:RHEA:57468, ChEBI:CHEBI:29749, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:81321; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=genistein + UDP-alpha-D-glucose = genistein 7-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:56056, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:74224, ChEBI:CHEBI:140305; EC=2.4.1.170; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=apigenin + UDP-alpha-D-glucose = apigenin 7-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:59760, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58470, ChEBI:CHEBI:58885, ChEBI:CHEBI:77722; EC=2.4.1.81; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=luteolin + UDP-alpha-D-glucose = H(+) + luteolin 7-O-beta-D-glucoside + UDP; Xref=Rhea:RHEA:19577, ChEBI:CHEBI:15378, ChEBI:CHEBI:57545, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:77791; EC=2.4.1.81; Evidence={ECO:0000269|PubMed:27227328};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.98 mM for gallic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.17 mM for 4-hydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=4.44 mM for 3,4-dihydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.77 mM for caffeic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=0.86 mM for cinnamic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.06 mM for coumaric acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.32 mM for ferulic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=0.78 mM for sinapic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; Vmax=0.39 uM/sec/mg enzyme with gallic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.43 uM/sec/mg enzyme with 4-hydroxybenzoic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.96 uM/sec/mg enzyme with 3,4-dihydroxybenzoic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.63 uM/sec/mg enzyme with caffeic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.32 uM/sec/mg enzyme with cinnamic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.31 uM/sec/mg enzyme with coumaric acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.47 uM/sec/mg enzyme with ferulic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.31 uM/sec/mg enzyme with sinapic acid as substrate (at pH 5.0 and 30 degrees Celsius); Note=kcat is 0.55 sec(-1) with gallic acid as substrate. kcat is 0.6 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 1.35 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.89 sec(-1) with caffeic acid as substrate. kcat is 0.45 sec(-1) with cinnamic acid as substrate. kcat is 0.44 sec(-1) with coumaric acid as substrate. kcat is 0.66 sec(-1) with ferulic acid as substrate. kcat is 0.44 sec(-1) with sinapic acid as substrate. {ECO:0000269|PubMed:27227328};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. {ECO:0000269|PubMed:27227328};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity remains fairly constant between 20-55 degrees Celsius. Active even at 0 degrees Celsius. {ECO:0000269|PubMed:27227328};

FUNCTION: Glucosyltransferase that catalyzes the formation of 1-O-beta-D-glucose esters with hydroxybenzoic acids and cinnamic acid including its derivatives as preferred glucosyl acceptors. Has significant activity with gallic acid (3,4,5-trihydroxybenzoic acid), 3,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, cinnamic acid, sinapic acid, coumaric acid, caffeic acid and ferulic acid in vitro. Gallic acid is the predicted native substrate of the enzyme, which thus catalyzes the formation of 1-O-galloyl-beta-D-glucose, the first committed step of hydrolyzable tannins (HTs) biosynthesis, with punicalagin isomers being the major HTs of pomegranate. Catalyzes the formation of flavonoid glucosides with genistein, apigenin and luteolin in vitro. Has low activity with benzoic acid, 2-hydroxybenzoic acid, 3-hydroxybenzoic acid, 2,4-dihydroxybenzoic acid, naringenin and quercetin. No activity with catechol, resveratrol, chlorogenic acid, catechin and epicatechin (building blocks of proanthocyanidins) or cyanidin, delphinidin and pelargonidin (the three anthocyanidins). {ECO:0000269|PubMed:27227328}.

Punica granatum (Pomegranate)

A0A193AUF6

GGT23_PUNGR

MGSESSLVHVFLVSFPGQGHVNPLLRLGKRLASKGLLVTFTTPESIGKQMRKASNISDQPAPVGDGFIRFEFFEDGWDEDEPRRQDLDQYLPQLEKVGKVLIPQMIQKNAEQGRPVSCLINNPFIPWVSDVAETLGLPSAMLWVQSCACFLAYYHYYHGLVPFPSENAMEIDVQLPSMPLLKHDEVPSFLYPTTPYPFLRRAILGQYKNLEKPFCILMDTFQELEHEIIEYTSKICPIKTVGPLFKNPKAPNTTVKGDFMKADDCIGWLDSKPASSVVYVSFGSVVYLKQDQWDEIAYGLLNSGVNFLWVMKPPHKDSGYTVLTLPEGFLEKAGDRGKVVQWSPQEQVLAHPATACFVTHCGWNSSMEALTSGMPVVAFPQWGDQVTDAKYLVDEFKVGVRMCRGEAEDKLITRDVVEQCLREATQGPKAAEMKKNALKWKAAAEASFVEGGSSDRNLQAFVDEVKRRSIEITASKPAVKAAPNGVVAAAESVVETKANGKVELAA

2.4.1.120; 2.4.1.136; 2.4.1.170; 2.4.1.177; 2.4.1.194; 2.4.1.81

3,4-dihydroxybenzoate metabolic process [GO:0046278]; cinnamic acid ester metabolic process [GO:0009801]; ferulate metabolic process [GO:0033494]

cytoplasm [GO:0005737]

4-hydroxybenzoate 4-O-beta-D-glucosyltransferase activity [GO:0047250]; cinnamate beta-D-glucosyltransferase activity [GO:0050412]; flavone 7-O-beta-glucosyltransferase activity [GO:0047891]; gallate 1-beta-glucosyltransferase activity [GO:0047913]; isoflavone 7-O-glucosyltransferase activity [GO:0050004]; quercetin 3-O-glucosyltransferase activity [GO:0080043]; quercetin 7-O-glucosyltransferase activity [GO:0080044]; sinapate 1-glucosyltransferase activity [GO:0050284]; UDP-glucosyltransferase activity [GO:0035251]

PF00201;

3.40.50.2000;

UDP-glycosyltransferase family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27227328}.

CATALYTIC ACTIVITY: Reaction=3,4,5-trihydroxybenzoate + UDP-alpha-D-glucose = 1-O-galloyl-beta-D-glucose + UDP; Xref=Rhea:RHEA:15249, ChEBI:CHEBI:15834, ChEBI:CHEBI:16918, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.136; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=3,4-dihydroxybenzoate + UDP-alpha-D-glucose = 1-O-(3,4-dihydroxy-benzoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:52844, ChEBI:CHEBI:36241, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:136876; EC=2.4.1.136; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=4-hydroxybenzoate + UDP-alpha-D-glucose = 4-(beta-D-glucosyloxy)benzoate + H(+) + UDP; Xref=Rhea:RHEA:15153, ChEBI:CHEBI:11935, ChEBI:CHEBI:15378, ChEBI:CHEBI:17879, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.194; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamate + UDP-alpha-D-glucose = 1-O-(trans-cinnamoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:13437, ChEBI:CHEBI:15669, ChEBI:CHEBI:16279, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.177; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-sinapate + UDP-alpha-D-glucose = 1-O-(trans-sinapoyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:13305, ChEBI:CHEBI:16546, ChEBI:CHEBI:30023, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.120; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumarate + UDP-alpha-D-glucose = 1-O-(trans-4-coumaroyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:57472, ChEBI:CHEBI:12876, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:71498; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-caffeate + UDP-alpha-D-glucose = 1-O-[(E)-caffeoyl]-beta-D-glucose + UDP; Xref=Rhea:RHEA:57464, ChEBI:CHEBI:614, ChEBI:CHEBI:57770, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=(E)-ferulate + UDP-alpha-D-glucose = 1-O-[(E)-feruloyl]-beta-D-glucose + UDP; Xref=Rhea:RHEA:57468, ChEBI:CHEBI:29749, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:81321; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=genistein + UDP-alpha-D-glucose = genistein 7-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:56056, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:74224, ChEBI:CHEBI:140305; EC=2.4.1.170; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=apigenin + UDP-alpha-D-glucose = apigenin 7-O-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:59760, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58470, ChEBI:CHEBI:58885, ChEBI:CHEBI:77722; EC=2.4.1.81; Evidence={ECO:0000269|PubMed:27227328}; CATALYTIC ACTIVITY: Reaction=luteolin + UDP-alpha-D-glucose = H(+) + luteolin 7-O-beta-D-glucoside + UDP; Xref=Rhea:RHEA:19577, ChEBI:CHEBI:15378, ChEBI:CHEBI:57545, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:77791; EC=2.4.1.81; Evidence={ECO:0000269|PubMed:27227328};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.89 mM for gallic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.19 mM for 4-hydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=2.46 mM for 3,4-dihydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.06 mM for caffeic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.12 mM for cinnamic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=0.94 mM for coumaric acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=1.58 mM for ferulic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; KM=0.86 mM for sinapic acid (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:27227328}; Vmax=0.37 uM/sec/mg enzyme with gallic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.43 uM/sec/mg enzyme with 4-hydroxybenzoic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.54 uM/sec/mg enzyme with 3,4-dihydroxybenzoic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.45 uM/sec/mg enzyme with caffeic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.4 uM/sec/mg enzyme with cinnamic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.37 uM/sec/mg enzyme with coumaric acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.52 uM/sec/mg enzyme with ferulic acid as substrate (at pH 5.0 and 30 degrees Celsius); Vmax=0.35 uM/sec/mg enzyme with sinapic acid as substrate (at pH 5.0 and 30 degrees Celsius); Note=kcat is 0.52 sec(-1) with gallic acid as substrate. kcat is 0.61 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 0.76 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.64 sec(-1) with caffeic acid as substrate. kcat is 0.56 sec(-1) with cinnamic acid as substrate. kcat is 0.52 sec(-1) with coumaric acid as substrate. kcat is 0.72 sec(-1) with ferulic acid as substrate. kcat is 0.5 sec(-1) with sinapic acid as substrate. {ECO:0000269|PubMed:27227328};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:27227328};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity remains fairly constant between 20-55 degrees Celsius. Active even at 0 degrees Celsius. {ECO:0000269|PubMed:27227328};

FUNCTION: Glucosyltransferase that catalyzes the formation of 1-O-beta-D-glucose esters with hydroxybenzoic acids and cinnamic acid including its derivatives as preferred glucosyl acceptors. Has significant activity with gallic acid (3,4,5-trihydroxybenzoic acid), 3,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, cinnamic acid, sinapic acid, coumaric acid, caffeic acid and ferulic acid in vitro. Gallic acid is the predicted native substrate of the enzyme, which thus catalyzes the formation of 1-O-galloyl-beta-D-glucose, the first committed step of hydrolyzable tannins (HTs) biosynthesis, with punicalagin isomers being the major HTs of pomegranate. Catalyzes the formation of flavonoid glucosides with genistein, apigenin and luteolin in vitro. Has low activity with benzoic acid, 2-hydroxybenzoic acid, 3-hydroxybenzoic acid, 2,4-dihydroxybenzoic acid, naringenin and quercetin. No activity with catechol, resveratrol, chlorogenic acid, catechin and epicatechin (building blocks of proanthocyanidins) or cyanidin, delphinidin and pelargonidin (the three anthocyanidins). {ECO:0000269|PubMed:27227328}.

Punica granatum (Pomegranate)

A0A193CHJ5

PA2BC_CROTA

MRALWIVAVLLVGVEGHLLQFNKMIKFETRKNAIPFYAFYGCYCGWGGRGRPKDATDRCCFVHDCCYGKLAKCNTKWDIYPYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC

3.1.1.4

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PIRSR:PIRSR601211-2}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000255|PIRSR:PIRSR601211-2};

arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644]

extracellular region [GO:0005576]

calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; ion channel regulator activity [GO:0099106]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]

PF00068;

1.20.90.10;

Phospholipase A2 family, Group II subfamily, D49 sub-subfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU361236, ECO:0000305|PubMed:35737043}.

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:35737043};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=9.8 umol/min/mg enzyme (monomer CBc) {ECO:0000269|PubMed:35737043};

FUNCTION: Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission (By similarity). It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non-enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4) (By similarity). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit (By similarity). At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor (By similarity). {ECO:0000250|UniProtKB:C0HM14}.; FUNCTION: Monomer CBc: The basic subunit of crotoxin is a snake venom phospholipase A2 (PLA2) that exhibits weak neurotoxicity (10-fold less than the heterodimer) and very strong anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (By similarity). In addition, it shows the same effects described for the heterodimer and binds the nucleotide-binding domain (NBD1) of CFTR chloride channels and increases the channel current (By similarity). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:35737043). {ECO:0000250|UniProtKB:P62022, ECO:0000269|PubMed:35737043}.

Crotalus tzabcan (Yucatan neotropical rattlesnake) (Crotalus simus tzabcan)

A0A193KX02

TOMT_DANRE

MVSPAIALAFLPLLLTLIIRYRYYFVLLYRAVLTRWVRDCLSGISREERAFQYILTHATPGDSQSILDTFDTWCSKVEFISNIGPKKGKILDRLLQENCPITVLELGTHCGYSTVRMARSLPIGARIYSVEMDQRNAQVAEKIIRLAGFDDDMVELIQRPSDEVIPRLREDLGVERLDLVLMDHWKRCYLPDLHLLEDSGLIGQGSIILADNVIFPGAPNFLRYARRCGLYEVRVHRATLEYMRGIPDGMAELTYIGIK

2.1.1.6

auditory behavior [GO:0031223]; catecholamine catabolic process [GO:0042424]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; developmental process [GO:0032502]; dopamine metabolic process [GO:0042417]; endocytosis [GO:0006897]; hair cell differentiation [GO:0035315]; inner ear receptor cell stereocilium organization [GO:0060122]; methylation [GO:0032259]; neuromast development [GO:0048884]; sensory perception of sound [GO:0007605]

basolateral plasma membrane [GO:0016323]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]

catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; orcinol O-methyltransferase activity [GO:0102938]

PF01596;

3.40.50.150;

Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family

SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:28534737}. Golgi apparatus {ECO:0000269|PubMed:28534737}. Basolateral cell membrane {ECO:0000269|PubMed:28534737}. Note=Enriched in an apical membrane compartment above the nucleus in the hair cells. Not detectable in the hair bundle. May be present at lower levels in the endoplasmic reticulum and the basolateral membrane. {ECO:0000269|PubMed:28534737}.

CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000250|UniProtKB:P21964};

FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones (By similarity). Required for auditory function. Component of the hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the asymmetric tip-link MET complex. Required for transportation of TMC1 and TMC2 proteins into the mechanically sensitive stereocilia of the hair cells. The function in MET is independent of the enzymatic activity (PubMed:28534737). {ECO:0000250|UniProtKB:P21964, ECO:0000269|PubMed:28534737}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A1B0GTW7

CIROP_HUMAN

MLLLLLLLLLLPPLVLRVAASRCLHDETQKSVSLLRPPFSQLPSKSRSSSLTLPSSRDPQPLRIQSCYLGDHISDGAWDPEGEGMRGGSRALAAVREATQRIQAVLAVQGPLLLSRDPAQYCHAVWGDPDSPNYHRCSLLNPGYKGESCLGAKIPDTHLRGYALWPEQGPPQLVQPDGPGVQNTDFLLYVRVAHTSKCHQETVSLCCPGWSTAAQSQLTAALTSWAQRRGFVMLPRLCLKLLGSSNLPTLASQSIRITGPSVIAYAACCQLDSEDRPLAGTIVYCAQHLTSPSLSHSDIVMATLHELLHALGFSGQLFKKWRDCPSGFSVRENCSTRQLVTRQDEWGQLLLTTPAVSLSLAKHLGVSGASLGVPLEEEEGLLSSHWEARLLQGSLMTATFDGAQRTRLDPITLAAFKDSGWYQVNHSAAEELLWGQGSGPEFGLVTTCGTGSSDFFCTGSGLGCHYLHLDKGSCSSDPMLEGCRMYKPLANGSECWKKENGFPAGVDNPHGEIYHPQSRCFFANLTSQLLPGDKPRHPSLTPHLKEAELMGRCYLHQCTGRGAYKVQVEGSPWVPCLPGKVIQIPGYYGLLFCPRGRLCQTNEDINAVTSPPVSLSTPDPLFQLSLELAGPPGHSLGKEQQEGLAEAVLEALASKGGTGRCYFHGPSITTSLVFTVHMWKSPGCQGPSVATLHKALTLTLQKKPLEVYHGGANFTTQPSKLLVTSDHNPSMTHLRLSMGLCLMLLILVGVMGTTAYQKRATLPVRPSASYHSPELHSTRVPVRGIREV

3.4.24.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P08148}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08148};

cell adhesion [GO:0007155]; establishment of left/right asymmetry [GO:0061966]; proteolysis [GO:0006508]

cytoplasm [GO:0005737]; membrane [GO:0016020]

metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]

PF01457;

3.10.170.20;3.90.132.10;

Peptidase M8 family

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.

FUNCTION: Putative metalloproteinase that plays a role in left-right patterning process. {ECO:0000250|UniProtKB:A0A1D5NSK0}.

Homo sapiens (Human)

A0A1B1FHP3

DPAS_CATRO

MAGKSAEEEHPIKAYGWAVKDRTTGILSPFKFSRRATGDDDVRIKILYCGICHTDLASIKNEYEFLSYPLVPGMEIVGIATEVGKDVTKVKVGEKVALSAYLGCCGKCYSCVNELENYCPEVIIGYGTPYHDGTICYGGLSNETVANQSFVLRFPERLSPAGGAPLLSAGITSFSAMRNSGIDKPGLHVGVVGLGGLGHLAVKFAKAFGLKVTVISTTPSKKDDAINGLGADGFLLSRDDEQMKAAIGTLDAIIDTLAVVHPIAPLLDLLRSQGKFLLLGAPSQSLELPPIPLLSGGKSIIGSAAGNVKQTQEMLDFAAEHDITANVEIIPIEYINTAMERLDKGDVRYRFVVDIENTLTPPSEL

1.1.1.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00327}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P00327};

alcohol metabolic process [GO:0006066]; alkaloid biosynthetic process [GO:0009821]; lignin biosynthetic process [GO:0009809]

cytosol [GO:0005829]

alcohol dehydrogenase (NADP+) activity [GO:0008106]; cinnamyl-alcohol dehydrogenase activity [GO:0045551]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]

PF08240;PF00107;

3.90.180.10;3.40.50.720;

Zinc-containing alcohol dehydrogenase family

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29724909}.

CATALYTIC ACTIVITY: Reaction=dihydroprecondylocarpine acetate + NADP(+) = H(+) + NADPH + precondylocarpine acetate; Xref=Rhea:RHEA:58576, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142769, ChEBI:CHEBI:142770; Evidence={ECO:0000269|PubMed:29724909}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58578; Evidence={ECO:0000269|PubMed:29724909};

PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:29724909}.

FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine, catharanthine, tabersonine, vincadifformine, vindoline, vincristine, quinine and strychnine) biosynthesis pathway. Converts precondylocarpine acetate to dihydroprecondylocarpine acetate. {ECO:0000269|PubMed:29724909}.

Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)

A0A1B1J8Z2

CHIT5_LOTJA

MIIKLLVALIHYLHETMAVQSIITTPLLVILMSLRSYAFTEPSLHRQQPPSKGGVRAAYWPAWSDFSTSSIDTNYFTHIYYAFVQPAPESFNLEITESYKKWAPKYDGIHNIRPRVTTLLSIGGGGNNATLFSEMASSKQNRASFINSTIHVARKHEFNGLDLDWEWPGDEKDMSNLALLLKEWYKALVVEANTSRKSRLLLTSAVYFNSTISLIGNGPRSYPVRAIRKYLDWASPMCFDYNGAWANETGFNAALYDPNSNISTKYGIGSWIGSGVPAEKLVMGLPLYGRAWELKDPNDHGVGAKAVGPAVDTDGSMDYDEILVFNKDTGAKVVYDEVAVSFYSYSGTTWIGYDDGPSITKKVQFARSMGLKGYFFWAIGKDKDWTISKQASNAWGY

3.2.1.14

chitin catabolic process [GO:0006032]; defense response to fungus [GO:0050832]; nodulation [GO:0009877]; polysaccharide catabolic process [GO:0000272]

extracellular region [GO:0005576]

chitin binding [GO:0008061]; chitinase activity [GO:0004568]

PF00704;

3.10.50.10;3.20.20.80;

Glycosyl hydrolase 18 family, Chitinase class V subfamily

CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000255|PROSITE-ProRule:PRU10053, ECO:0000269|PubMed:27383628};

PATHWAY: Glycan degradation; chitin degradation. {ECO:0000305}.

FUNCTION: Possesses chitinase activity in vitro toward glycol chitin, carboxymethyl-chitin, colloidal chitin, and the chitin oligosaccharides (N-acetylglucosamine) (GlcNAc)6 and (GlcNAc)5 (PubMed:27383628). Hydrolyzes (GlcNAc)6 into (GlcNAc)4 and (GlcNAc)2, or two (GlcNAc)3 molecules (PubMed:27383628). Has the capacity to inhibit hyphal growth of the fungus Trichoderma viride in an agar-plate bioassay (PubMed:27383628). Involved in symbiotic signaling (PubMed:30284535). Required for root hair infection threads (ITs) elongation and nodule development (PubMed:30284535). Possesses Nod factor (NF) hydrolase activity (PubMed:30284535). NFs are lipo-chitooligosaccharide signaling molecules produced by nitrogen-fixing rhizobia to initiate nodulation (symbiosis) on the roots of legumes (PubMed:30284535). Modulates NF levels and signaling to complete transition of infected nodules to functional nitrogen-fixing organs (PubMed:30284535). {ECO:0000269|PubMed:27383628, ECO:0000269|PubMed:30284535}.

Lotus japonicus (Lotus corniculatus var. japonicus)

A0A1B1WAJ0

RAD1_LOTJA

MSPPLYSVLLEDENSVFLLDLDLSSPMGFHAYPHLPILDSSIANWSLPFSISDETFRESKKLKRTMIPISSADFSISSSSSLSVSVNSIPRLNFRDHIRTYKRYLAAEELPEDTNSSESVVGAEEDGCADGMRLVQLLIACAEAVACRDKAHASMLLSELKSNALVFGSSFQRVASCFVQGLAERLTLIQPIGSGAGVSQSMMNIMDAASEEMEEAYRLVYETCPHIQFGHFVANSTILEAFEGESFVHVVDLGMSLGLPHGHQWRGLIHSLANRASGHGRVRRLRITAIGLCIARLQAIGDELSDYANNLGINLEFSVVQKNLENLQPEDIKVNDDEALVVNSILQLHCVVKESRGALNSVLQMIHGLSPKVLVMVEQDSSHNGPFFLGRFMESLHYYSAIFDSLDAMLPKYDTKRAKMEQFYFAEEIKNIVSCEGPLRMERHERVDQWRRRMSRAGFQAAPIKMVAQAKQWLLKNKICDGYTVVEEKGCLVLGWKSKPIVAASCWKC

arbuscular mycorrhizal association [GO:0036377]; cellular response to phosphate starvation [GO:0016036]; detection of phosphate ion [GO:0010247]; regulation of DNA-templated transcription [GO:0006355]; response to symbiotic fungus [GO:0009610]

nucleus [GO:0005634]

DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]

PF03514;

GRAS family

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25560877}.

FUNCTION: Transcription factor acting as a regulator of arbuscular mycorrhiza (AM)-related genes (e.g. PT4, STR and RAM2) (PubMed:25560877). Required for the morphogenesis of arbuscules upon symbiosis with AM fungi (e.g. Rhizophagus irregularis) (PubMed:25560877). Also involved in restricting mycorrhizal colonization of the root meristem (PubMed:25560877). {ECO:0000269|PubMed:25560877}.

Lotus japonicus (Lotus corniculatus var. japonicus)

A0A1B2CTC5

PENN_PENTH

MYHQLESHGVFPTLGDDAAKLVRTTHVQEIAFTPISEIQRFCEAQNISCDSFYLNVWSLVLRAFAETNSVCVGFGDFRPSGARLDQALFKILQTTLSPKSSILSILQGFKQDERAFSVNHREPAHNTGVVFISEASGPLDLASLGKLKYDLLMVVSFDSKSIPISLFLVYRPSTLSQSHAENLSSNITQAMQQVLARPNSFVNDVELFSTFNKSLVLCWNGLERKAASLLEVIQGHVRSRPDHPAICAWDGTISYSQLDMLTTQWASYLQSRGVQPGCLVPIMMEHSKWAIIGEIAILKAGAAFVPIDPAHPVSRLKGIVQRTKANIAVSSGHLIDKLSSLVDTVVEISDQTTSGLPEAVRHGAANPVPFDRTAYVLFTSGSTGQPKGCVVSYRALSDVVHQTTALNIDSESRVLQFASYTYGMSLIEVHCTLAAGATICIPSDYHRLNALSSAIQSTQVTWAILTASTTLTIAETARYLRTLVVAGEPMGIDHVRSLADKVELLQAFGLTEWGGICCVSQRIRSEGDVRLIGRSPTANLWLIDPTDGSKLAPVGAAAELFVEGPALADGYLEDPHQTAAVFIKRPPWIPAPTGVRLYRTGDLVRYTGDGNLLYIARKDSQVKIRGMRVELGEVEYQIRQAFPALGEAIAVATTTKESSGMPILAAFLHMENQLDLSGQSFSHMIDTIKTSLRKTLPDYMWPSIYIPLDSVPLTISRKIDRKDLQLRVQKSTRMELEENQVSSACIVAPLTDTERHVHRFVAELLHLDPLSFGMNQNFINLGGDSVSAMRLVNKCKYQGYRVTVGEILEVRTLSDIVSLVRTATTSSSVPSAGAEISRSDAPTESPATGSFEGSGYTTIPRLSQSGPIEQSFSQARMWFLEELHPGSSWYILPYATRLQGPLQLDHLEAALSALSERHETLRTTFESRDGTGLQIVAPFRPKPLEVIEVTSDSSIAALRTALQEQMKPFDLTKDTWRSAVLRLSPTDHVFSVVFHHIISDGWSVDVFMKTLETFYSAVIRGQPPLHITKPLQIQYRDFSIWQRQEQSRIHQKQIAYWIQQLHGSKPAEFLCDKPRPTKPSIAAGSMDVKIDGELYQALQGFCRSRQVTPFTTLLAAFRTTHYRLTGASDATIGIPSASRTRPELEELIGYFGNVQCIRTVIDSRGQSFQQLVQQVQSATTAASQNQDVPFDQVVSRLLKDRDMSRHPLVQVTFVLHPQANFGQLHLEGLRAEHLHLPQVTRLDLEFHLYPGDGCLQGDILYSADLFNPETIRTLRSVFYDVLSEGLCHPDIEIGSLLLTDAYPVLDQRGLIYTAHEAPFQGCSIIDMFHQQVAAHGDQMAIKDTHTQLTYCELDRRSDMLATWLKNSFLFVEETPVGVFGNRSCESIVTILGILKAGLAYVPLDADAPPQRTEMILSCLPSCQLVLLLSGLMAPPTLPSNIKFAYVSNSSDVKVEEVDAFLTHTPTPRATNLAYIVFTSGTTGTPKGVMVEHRGVVRLAKDPEIVAHTRDFKVASHVLNPAFDASGFEVYATLLNGGTLVCIDKNIVWDYAALGATLVKHGVQRAFFTTAVLKQCLLSAPYIMSDLEILYVGGDKLDPHDMAVARRFGKVRIFNVYGPTENSVVSTRYAIPDGEAAVNGMPIGRSIAGSGAYVMDPNLRLVPIGAMGELVVTGLGLARGYTNPEQNIGRFVTVSIGGQVVHAYRTGDMVRYRPSDAQLEFFGRMDQQVKIRGYRVELAEIDNALALNSLVSSAVTVLQTQEDQEQELVSFVTIQDTAANVENLEEHISNAHVNSWKDHAEGGDHYGKLGAVDPATLGRDFLGWVSMYDGEAIDTEVMTEWLEDTIAAIHLCDAASALEIGTGTGMILFNLIDSLKEYYGLEPSRQAVEFVQRAVRCVPKAASKVRIQQGTASALVGLKATGPIDLAVVNSVAQYFPSAKYMTRVIKQLIQLHDLNCIFFGDIRSYGLYEEFQASKVLHLYGHTLSAREFSQKMAEIVQLEKELLIDPAFFTALATEFPELIEHVEIMPKRMKTTNELSCYRYTAILHIRRPSQSLLVHEVEQSSWLDFEASGLDYRSLTQMLKTSNDVSVLAFSNIPFKKTIMERHVVNFLRHLPTGAGSAGWSMDVCQQALVCPAIDATELIDVAQLTGWQVEISWARQHSQFGGLDAIFHRLKPEDNGSRVFFQFPTDHGRRGLSCAFSNDPLALQRNQRIENELLENLRARLPSYMVPKRIRVLDRMPINNIGKVDRQALAKRVDIPPPAGVLTARSSPRNDMSFTDDIERAMWEEFAGVLGVEVGIADSFFDCGGHSLMAIKLVSRINKRLQSTVPVSDLFQYPSVSRLAGRVRGFRAPSNSTVSYQPFSLLPGSLSRLPYIDSPYGSEPHLPPSTEIIDMLPVTESQAWFLADWSLVSHSFRIEGALDVDGLRAACQAVVRHHATLRTVFTKLLGRLVQVVCGSVDAPFAHVYTDGDLESECRSLCAADGGAPSGLTTGFTLLSRSTIEHIFILRFSHAQYDGISLSSILSDLAAAYAGTAPLPTTAPFSGYVHVAALSRSVALDFWKKYLEGSVLTTLRPSNTAINARVVDLTREAVGKLHQLADITFPTIVNAAIAITLASLVKRNDVTFACVMSSRGVLSQGADSVQGPCVNRTLIRVQLSPDSTALGFCRGLRKNQARVSAENHLELGDVLENCTSWSSSDRLAPWITHLPADKATSTLALPGACITYRSTDVRINPRNQILVRSVITDQQQACIQVQVSSTVMDGSYAFSLASKILNTAQALSMSAERTLSSIDVHE

6.3.2.-; 6.3.2.40

amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; antibiotic biosynthetic process [GO:0017000]; heterocycle biosynthetic process [GO:0018130]; monocarboxylic acid biosynthetic process [GO:0072330]; toxin biosynthetic process [GO:0009403]

cytosol [GO:0005829]

ligase activity [GO:0016874]; phosphopantetheine binding [GO:0031177]

PF00501;PF00668;PF08242;PF00550;

3.30.300.30;1.10.1200.10;3.40.50.1820;3.30.559.10;3.40.50.12780;3.30.559.30;3.40.50.150;

NRP synthetase family

CATALYTIC ACTIVITY: Reaction=anthranilate + 2 ATP + O-methyl-L-tyrosine + S-adenosyl-L-methionine = (-)-4'-methoxycyclopeptine + 2 AMP + 2 diphosphate + 2 H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74487, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:193537, ChEBI:CHEBI:193554, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q5AR54}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74488; Evidence={ECO:0000250|UniProtKB:Q5AR54}; CATALYTIC ACTIVITY: Reaction=anthranilate + 2 ATP + L-phenylalanine + S-adenosyl-L-methionine = 2 AMP + cyclopeptine + 2 diphosphate + 2 H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:35091, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57856, ChEBI:CHEBI:58095, ChEBI:CHEBI:59789, ChEBI:CHEBI:71320, ChEBI:CHEBI:456215; EC=6.3.2.40; Evidence={ECO:0000250|UniProtKB:Q5AR54}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35092; Evidence={ECO:0000250|UniProtKB:Q5AR54};

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:25859931}.; PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:25859931}.; PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25859931}.

FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group (PubMed:25859931). The first stage is catalyzed by the nonribosomal peptide synthetase penN that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (By similarity). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase penM through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (By similarity). PenM also converts its first product methoxydehydrocyclopeptin to 4'-methoxycyclopenin (By similarity). The following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase penL (By similarity). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase penI then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase penH to yield conjugated aryl diene (PubMed:25859931). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase penG to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain, or undergo cyclization to yield yaequinolones J1 and J2 (PubMed:25859931). The conversion of the styrenyl quinolone into the tetrahydrofuran-containing yaequinolone C is performed by the FAD-dependent monooxygenase penE and involves epoxidation of the terminal C7'-C8' olefin, followed by epoxide ring opening initiated by the C3' hydroxyl group (PubMed:25859931). The predicted cysteine hydrolase penJ acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet cyclization step, increasing the yield of yaequinolone C (PubMed:25859931, PubMed:28114276). PenF catalyzes the cationic rearrangement of the epoxide formed by penE (before ring opening to produce yaequinolone C) into yaequinolone D (PubMed:28114276). Finally, the short-chain dehydrogenase/reductase (SDR)-like reductase penD, catalyzes both the dehydration of yaequinolone D and the reduction of the resulting oxonium to yield penigequinolone (PubMed:28114276). {ECO:0000250|UniProtKB:C8VJQ3, ECO:0000250|UniProtKB:Q5AR53, ECO:0000250|UniProtKB:Q5AR54, ECO:0000269|PubMed:25859931, ECO:0000269|PubMed:28114276, ECO:0000305|PubMed:25859931}.

Penicillium thymicola

A0A1B4XBK0

SDNC_SORAA

MSFDQFAPFMTLGRPDAVCDECSRPVAPNSISDDDAAVNTTETDTQHANIPEEQDVINIKLDSTFNAESSAETIDLKVEGVKLAIVSQQPTYEAITAETTSSVATSEEASSDTATSLTNLTSREPSPSSSSASSVAEECPSEEPASDDTVPAASEKNHPDGTLNPNYHDARADEVHPQHEVVQVQAPHLPPPQGVQPAATENPDHDSLFSVFTQDHNPLLSGTIVGAPADYVASTPGKKIRDKAASALNIWLQVSPDDLNQIRTVIDMLHNASLILDDVEDGSVSRRGRPATHMIFGMPQAINSAGYQINRAMMEVLKLGSQDCLEIFIEELDRLYIGQGYDLFWTFNIKRPSVEKYISMVDYKTGSLFNMLVRFMAAKTGAKGGVETDNNKAPIAPPDLTRLVVLLGRYFQIRDDYMNLTSDEYTLQKGFCDDLDEGKFSLTLVHALENSPEAEKSILRHLLTQRLSSNGQGMSLAQKHLVIDIVKGAGSLEYTVTALRKIGMEIVNELDQIEGVTGIENKELRRLVEVLRV

2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};

alcohol biosynthetic process [GO:0046165]; antibiotic biosynthetic process [GO:0017000]; isoprenoid biosynthetic process [GO:0008299]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386]

dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872]

PF00348;

1.10.600.10;

FPP/GGPP synthase family

CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000250|UniProtKB:Q12051};

PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:27072286}.

FUNCTION: Geranylgeranyl diphosphate synthase; part of the gene cluster that mediates the biosynthesis of sordarin and hypoxysordarin, glycoside antibiotics with a unique tetracyclic diterpene aglycone structure (PubMed:27072286). First, the geranylgeranyl diphosphate synthase sdnC constructs GGDP from farnesyl diphosphate and isopentenyl diphosphate (PubMed:27072286). The diterpene cyclase sdnA then catalyzes the cyclization of GGDP to afford cycloaraneosene (PubMed:27072286). Cycloaraneosene is then hydroxylated four times by the putative cytochrome P450 monooxygenases sdnB, sdnE, sdnF and sdnH to give a hydroxylated cycloaraneosene derivative such as cycloaraneosene-8,9,13,19-tetraol (PubMed:27072286). Although the order of the hydroxylations is unclear, at least C8, C9 and C13 of the cycloaraneosene skeleton are hydroxylated before the sordaricin formation (PubMed:27072286). Dehydration of the 13-hydroxy group of the hydroxylated cycloaraneosene derivative might be catalyzed by an unassigned hypothetical protein such as sdnG and sdnP to construct the cyclopentadiene moiety (PubMed:27072286). The FAD-dependent oxidoreductase sdnN is proposed to catalyze the oxidation at C9 of the hydroxylated cycloaraneosene derivative and also catalyze the Baeyer-Villiger oxidation to give the lactone intermediate (PubMed:27072286). The presumed lactone intermediate would be hydrolyzed to give an acrolein moiety and a carboxylate moiety (PubMed:27072286). Then, [4+2]cycloaddition would occur between the acrolein moiety and the cyclopentadiene moiety to give sordaricin (PubMed:27072286). SdnN might also be involved in the [4+2]cycloaddition after the hypothesized oxidation to accommodate the oxidized product and prompt the [4+2]cycloaddition (PubMed:27072286). GDP-6-deoxy-D-altrose may be biosynthesized from GDP-D-mannose by the putative GDP-mannose-4,6-dehydratase sdnI and the short-chain dehydrogenase sdnK (PubMed:27072286). The glycosyltransferase sdnJ catalyzes the attachment of 6-deoxy-D-altrose onto the 19-hydroxy group of sordaricin to give 4'-O-demethylsordarin (PubMed:27072286). The methyltransferase sdnD would complete the biosynthesis of sordarin (PubMed:27072286). Sordarin can be further modified into hypoxysordarin (PubMed:27072286). The unique acyl chain at the 3'-hydroxy group of hypoxysordarin would be constructed by an iterative type I PKS sdnO and the trans-acting polyketide methyltransferase sdnL. SdnL would be responsible for the introduction of an alpha-methyl group of the polyketide chain (PubMed:27072286). Alternatively, the beta-lactamase-like protein sdnR might be responsible for the cleavage and transfer of the polyketide chain from the PKS sdnO to sordarin (PubMed:27072286). Two putative cytochrome P450 monooxygenases, sdnQ and sdnT, might catalyze the epoxidations of the polyketide chain to complete the biosynthesis of hypoxysordarin (PubMed:27072286). Transcriptional regulators sdnM and sdnS are presumably encoded for the transcriptional regulation of the expression of the sdn gene cluster (PubMed:27072286). {ECO:0000269|PubMed:27072286}.

Sordaria araneosa (Pleurage araneosa)

A0A1C3NSL9

AJM1_CAEEL

MSTTTPEKPEEIIDATGTSDTAEKIEVVISKEEPAEQKNEVEEPDYAQVPAESEDDAAQELAPTDSAIQVVHVLEAPQKAELVTIPLAHSEAEDHKLADADRDQEEELVFNEERRKTVTMDDNASLRSASITFDANRDEQDLLNESFASNPTDETVLMQKTKDEMDATSERPRSPLDLPPPPASVVLHPSAPPPPPPPLSSTEVVGNTTTTTTTHYAPKTWNDPSITTAPKIPVSLLSGAQPLPSVLTQRTTTSSYSAPNYSASSMSGVPSDVAPPPPLPIPNQSSSSAASYQHHHASSISKSISSSREDLLSEHATSRSTVREIPVHRAPSTAPSHSSVFEYHMMPTTTSTYHHVETPSDEYYRREVMTRTIITRSTEALSQTPLGRPASPLDRYLPYPTTTTTTSGDGRTREEKTVDYKVTYHRDIEEQERRIREDQARRQQEEQDRRDREDNARRILAQREHQEMERLREQQNLSERALAERERADKERLQQERLLRQQREKKRREEWDRLESIRLAEEEAELARRRALEKERIDREKAEEERKTMERLERERARLERERLEEERRQKEKAETERIERERREHERIEIERIERIKRERIERERREREEKKAEEDRLLRERLELERIERERRELEARERQELELQRREAEDRERQRLEDEAREMRRREEERREAELVADVHRQAEERERLRKRQEREEAERLERIRLEQQKIDMERIDAERRERERKEEERREFELIEAARRKKEARDRDRLDEMERERVREEEERREKERREQERRIAAEKERKRRQEEEEEIARLNELQRAAAARQAQRNAELDRQRQRDELDRKAQELSEREMREKERRDRERANEEAQLADLLERERHNQLIRENERREAVERANNRRLEDRRSRDKLDHIVRERSEKEQFELEKRRLLAEKEAMNRKKNHLLSSETLAKLTQPMYYTTREPEVTTKVERQVIERIDRNVWVEDVPYAPSQSAMGYLDNDENNRDRLYNPNDLNRNGSSRSRYQRAKNEKARRDFYHSSQDSADPVTERFRKSTDDLTTRSRPEYRGPLLQKFHDSEFRTTALNETDGLPYRRMGPSPYEQPFAKLLEETERRYAHYNSRASNPSIYQSSRYYYPERHGQPQHTDNTRAESVVAYERESRRESPADQAHIRSRSADYLMDRRIREETEVPENQLQKTRVEPHDQSPRESRISEYEMRFRKSTEKLTVPDWYRENRPQGQTAQTSTYRYGNGVEPMSTTTTTTTVINGTSSHQQAPPPVPPQPIGNIGLPRGMFDRYKDDIEELRRSRSSLHQTGQQETSNRQGSTLSVGGIVDQGHALPGYTVSEVPNAWNLHTSRTSRVVEVADTFVGTSSHEYGNFTNRYGGRVTIEEVLDSIFQKVTPTNQRLNFDRSYPQADELFQGNVDGPGIYTNNYSVMRQVLKSPERAEHILQNEELFVRCTECHRTRELSAARLFFVSCKHCYTYYCSRECRHNNWPNHSGRCSFARINTLCKDVIMKVREDEQAQAFMSKVARDGFSVSGRGSVNIRLSSPQLAQAYVSNGWRALSAYPNDQLLYYYTVKALIAERKEPSLIALCNRYEPREKFILSVSIIADIEHCPETPPPETRELSAVQFSSPRSRYEAIQNQNAPYFSEFAHNV

cell-cell junction organization [GO:0045216]; embryo development ending in birth or egg hatching [GO:0009792]

adherens junction [GO:0005912]; apical junction complex [GO:0043296]; apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; cell-cell junction [GO:0005911]; ciliary basal body [GO:0036064]; dendrite terminus [GO:0044292]; plasma membrane [GO:0005886]

cytoskeletal protein binding [GO:0008092]; metal ion binding [GO:0046872]

6.10.140.2220;

SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:27623382}. Cell projection, cilium {ECO:0000269|PubMed:27623382}. Cell junction, adherens junction {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:27623382}. Note=grdn-1-dependent localization at sensory neuron dendritic tips (PubMed:27623382). The coiled-coil domain is sufficient to localize to apical junctions (PubMed:11715019). {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:27623382}.

FUNCTION: Controls adherens junction integrity (PubMed:11715019). Required for the correct rate and completion of elongation of the embryos (PubMed:11715019). {ECO:0000269|PubMed:11715019}.

Caenorhabditis elegans

A0A1C7D1B7

ELP3_DEHMC

MKKLSRTISGVTPVAVMTKPLPCPGKCIYCPTFAATPQSYTPESPAVLRAKSCEYQAYKQVALRLRIIQDMGHPTDKVELIIMGGTFLSADITYQYGFIKDCYDALNGVVAGSLEEAKTINETAQHRCVGLCIETRPDICGKAEIQRMIDFGTTRVELGVQMLDDDIYKLVERGHRVSDVAEATCLLREYGLKVHYHWMPGLPGSSPEKDLALSRMVFEDPRFCPDGLKLYPTMVVEGTILEQWWKEGRYTPYPNGTMTGLIADIKALVPPYVRISRVLRDIPAVFISAGLKDSLRDGVRQILESRHQKCRCIRCREYGHRQRKGQTSGEPTLRRLDYPASGGKEIFLSFEDASDTLYGLLRLRIPCASLPVLGQKYGAKTGLVRELHVYGTELSLGEQGDQSAQHRGLGRKLLAEAECLARDEFGLDSLAILSGVGAREYYRSLGYELVAGYMCKHLD

2.3.1.311

COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:27455459}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250|UniProtKB:Q02908};

tRNA acetylation [GO:0051391]; tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation [GO:0002926]; tRNA wobble uridine modification [GO:0002098]

cytoplasm [GO:0005737]; elongator holoenzyme complex [GO:0033588]

4 iron, 4 sulfur cluster binding [GO:0051539]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; S-adenosyl-L-methionine binding [GO:1904047]; tRNA binding [GO:0000049]; tRNA uridine(34) acetyltransferase activity [GO:0106261]

PF04055;PF16199;

3.40.630.30;

ELP3 family

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407, Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74882; EC=2.3.1.311; Evidence={ECO:0000269|PubMed:27455459}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021; Evidence={ECO:0000269|PubMed:27455459};

PATHWAY: tRNA modification. {ECO:0000269|PubMed:27455459}.

FUNCTION: tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:27455459). The proposed mechanism is the following: (i) recruits S-adenosyl-L-methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not show protein lysine acetyltransferase activity (By similarity). {ECO:0000250|UniProtKB:D5VRB9, ECO:0000269|PubMed:27455459}.

Dehalococcoides mccartyi (strain CBDB1)

A0A1C8AX29

PIGK_MONRU

MEASDQSQAKLTLSFGGIQHAFSVPIEDLSALQDQKDAFLRSRSQASLSETREPCSPAELMLDYLEFLSCRNLPPPLTKPVLLAFSRNFLHNTEIHSLLAKPEYTPQTRRRLVRTYYMAALSAAESHVKESALLDAARQGNFQLAAVFGGQSTANPACVRELAELFAAYTPFLGDLISTAAPTLSALCRLPETKEHFCGRHIDIETWLHDPASIPDGDFIATAPVSCPVVGLLNLAHYAVTCHVLGKTPGELRSHLQGVTGHSQGIVAAVAISLSDSWESFYEAARMTVETLFWIGFECHQRSPRTSVSLDQVQDSLQNGHGRPSCMLSIVGLSRAHIQDILLKLNRSLPEDEQVYLALDNARDSFVVAGPSCSLVHLHTYLRSLKADASIDQTRIPHSLRKPTVQHQFLPISVPFHTPYLQEAARAIKERLFPWRVVSGKLTIPVYDNRTGNDLRKSDNVNLIHTMVDSICWEPCSWPAALGIENISHIVAFGSGGVGELAMRLKDGQGVRVIIGSEFQSRDEEIGTKADLFSPTLLASSTIVGSWGERFRPRLSKSPTGEVKIETKLSRLLDTPPLMVAGMTPTTAAWDFVSAITNAGYHVELAGGGYYDMDAMAVAVKKLVASIPPGRGITCNVIYASPQTLSGQVTLLRRLSSQGLPIDGLTIGAGIPSLEVVSEYIQALGLRHISLKPGSITAIREVIEIAKAHPDFPIILQWTGGRGGGHHSFEDFHAPILRTYGALRRCSNIILVAGSGFGGSEDTYPYLSGTWSAQYGLPAMPFDGILLGSRIMVAKEAHTSPAAKRLITEASGVSDSDWEKTYQEATGGVITVVSEMGQPIHKIATRGVLFWAEMDKTIFSLPRTKRVPELLKRRDYIIKRLNADFAKPWFGQNSKGEPVDLSEMTYIEVLRRLVALMYVSHQSRWIDPSYMTLLMDVSVRILERFSIVDELDDALVLREPHRFVENIVRLCPPAAHDILSPEDVAWFLLRCKARGQKPVNFIPALDDDFETFFKKDSLWQSEDVDALIDQDAGRCCILHGPVAAQYSQDRDEPAKEILDGITQSWIDMIRHDFYPGGVTPSSDSGSLSSESWSVLTPDLTSRDESALLDIIPEMQAYCPSISSLGRSGSPWIHALLSDEFILQGRDRRPNPCRRVFHFGPGGSLQFDRAKSEITVSMENHAGNRSVMRIVCENGADISVDLQQPSAYTDEMVSLPLKFQYDPGMVPVGISEVMEGRNERIKSFYSKVWFGEDICRGMNARSVFHGSEMALTEAMHRDLLSTVSLAYPHSETALSGVDVFPISVGMFPVWDAMARPLVVNDIDGDLLRLVHESNTFEYCEASTPLRVGDVVSSTAAVRAVYIEDAGKHVVVEASIERSGKPVMKVVSTFLFKGVFNDWNSTFKTNKEPELVLDVQSDLDELVLRDREWLLLHDPSQSLVGCSLLFRLETQVTWKNRNTYRSLDVSGLVFLQQASDDLKEIGAVAFHAGECVGNPVLSFLQRKGSPATSPTPLTSPGWPGVSSLEVQLPTSNEMYTRTSRDYNPIHVSPLFSQWADLPGTITQGMYTSAISAAVLEHLALNGDRRRFRRFSARFTDMVLPGDRLLVNVKHVGSIQGRMLFNVSAFKQATNNMVLEAEAELEQPPTAFFFTGQGSQKPNMGMDLYNSSPVAKAIWDEADKYIFETYGWSILDIVKNNPKTLTIHFRGKHGRKIRANYLSMENKTVTPDGQIVKKPILPGLTDQTQSYTFTEPSGLLFFSTFAQPSIVVMEKATFEDMRSKGLIPQSAVFAGHSLGEYGALLAFSGFMSVRNLVDLVFYRGLSMQFAMERDERGETNFGMVAASPQRVGKSDAVFTESHLRSLVQMISIASHELLEMVNLNIENEQYVCAGTDTETQLLLEEMSTTEDRTTTKLYKLILKSIPATKKLPMPIRLQRGRCTIPIPGIDVPFHSSYLRSTVSSYRKILQQYISEEDVHLERLVGRWIPNVTAKPFMADEGYVREVFNITQSPILKEMLEL

1.3.1.9; 2.3.1.38; 2.3.1.39; 2.3.1.86; 3.1.2.14; 4.2.1.59

long-chain fatty acid biosynthetic process [GO:0042759]

fatty acid synthase complex [GO:0005835]

(3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity [GO:0004317]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; [acyl-carrier-protein] S-malonyltransferase activity [GO:0004314]; enoyl-[acyl-carrier-protein] reductase (NADH) activity [GO:0004318]; fatty acid synthase activity [GO:0004312]; fatty acyl-[ACP] hydrolase activity [GO:0016297]

PF00698;PF08354;PF17951;PF17828;PF13452;PF01575;PF16073;

1.20.1050.120;1.20.930.70;3.30.1120.100;6.10.140.1400;6.10.60.10;6.20.240.10;3.20.20.70;3.10.129.10;3.40.366.10;

Fungal fatty acid synthetase subunit beta family

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83139; EC=2.3.1.86; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA; Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446; EC=2.3.1.38; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP]; Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449; EC=2.3.1.39; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14; Evidence={ECO:0000250|UniProtKB:Q8TGA1};

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:26946170, ECO:0000269|PubMed:28959415}.

FUNCTION: Fatty acid synthase subunit beta; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants (PubMed:26946170, PubMed:28959415, PubMed:34220766). PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring (PubMed:28959415). The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2-oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially invoved in the biosynthesis of orange and red pigments via desaturation of C6(7) (PubMed:28959415). {ECO:0000269|PubMed:26946170, ECO:0000269|PubMed:28959415, ECO:0000269|PubMed:34220766}.

Monascus ruber (Mold)

A0A1C9ZP88

LP9A_GLOTR

HGYVDQVTIGGQVYTGYQPYQDPYESPVPQRIERAIPGNGPVEDLTLLDIQCNGSGGSGTKPAALIASAAAGDEIAFHWTTWPSSHVGPVITYMGKVPSNTDITSYSPTGSDVIWFKIDEAGYENGKWAATDIMSAQNSTWTVTIPKALAPGQYIVRHEIIALHQAETYPGAQFYPDCFQVQVTGPGTETPTSQALVSFPGGYTPTTPGITFNVYSGSITSYPIPGPPVWTSNEAFSGGSSSSAAASSTAVASSTADSSSSAAATQSSSAAASGSAAPSSSAIGTSTASSAAASGTAIVDANTCMNNYNKCIDAGQPDPDWSGCTATKDACLAGATYQRLARSGTLGRLSF

3.2.1.4

COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q1K8B6}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q1K8B6};

cellulose catabolic process [GO:0030245]

extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]

cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497]

PF03443;

2.70.50.70;

Polysaccharide monooxygenase AA9 family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:27590806};

FUNCTION: Lytic polysaccharide monooxygenase (LMPO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (PubMed:27590806). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (PubMed:27590806). {ECO:0000269|PubMed:27590806}.; FUNCTION: [Isoform LPMO9A-2]: Has broad specificity, cleaving at any position along the beta-glucan backbone of xyloglucan, regardless of substitutions (PubMed:27590806). Shows minor activity on glucomannan (PubMed:27590806). {ECO:0000269|PubMed:27590806}.

Gloeophyllum trabeum (Brown rot fungus) (Agaricus trabeus)

A0A1D5AG16

PIGJ_MONRU

MAVRKLVPETAPVVDDAPASTSVDHKRSLAHKLLIELLSYQLALPVRWIETQNELLQWPETIQRYVEVGPRTTLVTMAKKTAARRASSQIVSASKLSTLKFLCTSDNTAEIYYEYPQESGAPVEEEGSKSDAAAPALAVSGSSRTATTAKATVTTPSSSSPETAPPAASTPSQGTPAGGSTTPDIPLSAKHVVLAMIAQKFRRAFDNIPTQKTVQELSGGKSTLQNEIMGDLAVEFGQLPDGGEYIPLDALGDALQGNFPGKPGKQMSSLITKLISRKMPGGFNQAAMQNHLEREWGFSKAHGQVVICLAITVEPESRLESADSAREFLDGLVSRYASYAGITMTPRGKGNVSADHSSAVMVDESVLNGIKREQRDYQIKELELLSKHLQLDTAADDAVLNELRASQKSLEEKLDRWASEFDDKFFSGIEAIFDARKVRQYDSWWNWAREDTMRLLSRMRPGQLPLQHLQEQGLVAQLLRRWEPSCAEIVQNFLDTGECKEPFLATAAEILRLGSDALKKSPVYRFTTPSMKPRTVISATGCVEYSEVPRENSSYIALLKQGLVAASGERVPYVHLKKKAPDQAWRYDAQSTEILLEALGTGSGAGLTFSGKTVLVTGAGPNSIGAAVVRGLLNGGAKVIVTTSRSVSSAASFFQRMYRECAARGATMAVVPFNQASKRDCESLVEYIYGAHSPVDGDLDYLVPFGAIPEKVELSKLDGASELAHRAMLVNILRILGLVYKEKEQRGLRTRPTTVIVPLSFNLGGFGGDGLYPESKIGLEALFNRYFSGNWSDYLSICGAAIGWVRGTTLSQSIRLLGEAIEHANGLDVITFSQEEMAFNILALMTPSIAETCEEGPVYADLTGGAKAIANIKDVMAAARAKFLKESSIQKALLAERAYEQRVLYGSESPRNDTSSPRPRLSTKRARLSLEFPEVPSKSDLKAHLVDLQGMVDLSRTVVVVGFSELGPWGNARTRWQMEHLTDLTPEGYIEMAWIMGLVEHFQGHLDGKPFVGWVDAQTKQPVADAEFKEKYQAHILAHAGLRFVEPDLLGGYDPSKKEFLQEIVVEEALPSFSTSKANADAFRLRLGDKVAVRRMPESDEYLVQVKRGAHFFVPKAVPFNRGVAGLLPAGWDPLRYGIPEDIVQQVDPVTLYALCCVSEALLSAGIRDPYELYRYIHVSELANCLGTGAGAQSAAQRLYKKRYLDHAVQSDILSESFLNTTAAWVNMLVFSSTGPIKTPVGACATAIESLDIGCDAIRSGRSQVALVGGYDDFREEASYEFAMMNATASSVGELAQGRLPREMSRPSTTTRGGFVESAGCGVQLIMNAELAIEMGLPIHAIIAYTQMAGDKIGRSIPAPGQGILTAARETSAGHDSALLDLAHRRKRLTDEVDAVHQWVTQQLAATRGPAGWPDRAIDEIEATALRKIKHAQHAWGNDIRCQDPSISPLKASLATWGLTIDDVQVVSMHGTSTKANDTNEADVISQQMDHLGRRPGNPLLAVCQKALTGHPKGAAGAWQLHGCMQMLQTGIVPGNRNADNIDSKLRQHRHIVYPMESMPMPQLKAAMLTSFGFGQKGGIAVVVAARHLFSAMAEDELEAYRRRVAKRQREADSAYVSGIMSKSLFKAKEVSVWGKSDASMSRMLLDPKARVGGHPENNNNNNNNSSSKRNTSIERLTRLLLPSQKPETEASPEGQQSTSLTASIQALLASQSTTRPTSTSIGVDVEAISSIPMGNAVFLERNFTRSERDHCFSSPTPQASFAGRWSAKEAVFKSLQTPSVGAGAAMAEIEIVSDGGVPKVQLHGRAKEVALAKGIRNIQASITHSGETVTAVALAESSPMC

1.1.1.100; 2.3.1.41; 2.3.1.86

heterocycle biosynthetic process [GO:0018130]; long-chain fatty acid biosynthetic process [GO:0042759]; organic cyclic compound biosynthetic process [GO:1901362]

fatty acid synthase complex [GO:0005835]

3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; holo-[acyl-carrier-protein] synthase activity [GO:0008897]; magnesium ion binding [GO:0000287]

PF01648;PF18325;PF18314;PF00109;PF02801;

3.30.70.2490;3.40.47.10;3.90.25.70;6.10.140.1410;3.90.470.20;3.40.50.720;

Thiolase-like superfamily, Fungal fatty acid synthetase subunit alpha family

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83139; EC=2.3.1.86; Evidence={ECO:0000250|UniProtKB:P19097}; CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41; Evidence={ECO:0000250|UniProtKB:P19097}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100; Evidence={ECO:0000250|UniProtKB:P19097};

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:26946170, ECO:0000269|PubMed:28959415}.

FUNCTION: Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants (PubMed:26946170, PubMed:28959415, PubMed:34220766). PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring (PubMed:28959415). The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2-oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially invoved in the biosynthesis of orange and red pigments via desaturation of C6(7) (PubMed:28959415). {ECO:0000269|PubMed:26946170, ECO:0000269|PubMed:28959415, ECO:0000269|PubMed:34220766}.

Monascus ruber (Mold)

A0A1D5NS60

ZN16L_DANRE

MSRKRNHCYMETGASSESQGAFVDSAGPFSRDEEDFSELEPDEQLVCSVTEITEHLGRNITVVLESALSEIRKLVGVRIRVLKMELREKSDEIELLKAKLESAEKDGRVSNFSSLDFRKSEHQKYGAEPKKAKTGTPVVKKENINAICDYLMKDKNQRGAAEVESDHSNQAFGSERDVRTEAQPHGSLSLWPDSGPADTDAETDIFSMLPSASKRMYDYEWMTGVELNSAEFKGDSETKCEDVPPMDEEDENEDSEEGRGSLRSVSDHFPLDTQGSPGEDRSSPAEDSMDRMEPGQQFTSHTFICPFCGTLCPDSSFLEEHIKLMHHGESLLQSTSAGSSSQAEGDSGEAGPASRGAREKKVEGGYECGDCGRHFNYLGNLRQHQRIHTGEKPFVCPECGERFRHTARLKSHRLSHSGAQSPFPCPQCGKGFPVLSGLKRHQRVHTGESPYACPQCGRRFKELGNLYTHMRIHSGATPYTCYQCGRSFRHLGTYKSHRCMPATQMPSEHSPPWAQEDKVQTGRLQGYV

central nervous system myelination [GO:0022010]; positive regulation of myelination [GO:0031643]; positive regulation of oligodendrocyte differentiation [GO:0048714]; regulation of transcription by RNA polymerase II [GO:0006357]

nucleus [GO:0005634]

DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]

PF00096;

3.30.160.60;

Krueppel C2H2-type zinc-finger protein family

SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.

FUNCTION: Probable transcription factor (Probable). Important for development and migration of oligodendrocyte precursor cells, and normal myelination of axons in the central nervous system (CNS) (PubMed:26459222). Functions autonomously in oligodendrocytes to promote CNS myelination (PubMed:26459222). Seems to act in parallel with notch3 during oligodendrocyte development (PubMed:26459222). {ECO:0000269|PubMed:26459222, ECO:0000305}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A1D5NSK0

CIROP_DANRE

MSFLLCIGILLLPWFPCVCGKCIFDQIQRSVNVVSPPTAQYASAYRFKTQRSKRHIMPMDNLQPIRIKIWIPSESPALSDWEREKLMSAVGEAVSEVSSLLSVKRVKDRLLLNRDVNKYCKFIWRNSSTLNHMKCGRAHENYRFESCLGVIIPDEHLDGCSVYPNPEHPVPTVLRPRGPGVPDADFLLYVFTHNTEKCRAESSVLAYTAHCQTGSDGRPLAGTMVICRETLKKERYTYQHFVKVTTVIHELFHVLGFSKELLSNWKDFGVDCWSHGQVTSTDQTGQVRLYSPTVIRAMQKHFNSTHTDLGAPLENKDAALDGLSSHWEARVLQGSIMAASLVEASLVRIDAITLAALQDTGWYSVNHSRAQSLVWGEGEGSDFGSVSACHNSSAFFCTGSGLGCHFLHLNKGECVTDQYLDGCHIFKPLANASECWIEDNARSGMNEGGGEIFGSDSRCFISNITRLNNVTAYTPVSGHCYRHRCTGINKYHIQVKDSDWMDCPAGTSIEVSGYQGFIFCPENRLCKYSDLAPPTSTQRTESLFSDTTAQSDLGMMEKDAAVQPSFTSLFLVSEAKISLAAVLSLMAVFALLSAAVLLYRKNLSVRVHAASYRTPLPHILYRN

3.4.24.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P08148}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08148};

cell adhesion [GO:0007155]; determination of heart left/right asymmetry [GO:0061371]; establishment of left/right asymmetry [GO:0061966]; proteolysis [GO:0006508]

cytoplasm [GO:0005737]; membrane [GO:0016020]

metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]

PF01457;

3.10.170.20;3.90.132.10;2.30.34.10;

Peptidase M8 family

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.

FUNCTION: Plays an essential role for patterning the left-right axis. Requires solely on the left side, downstream of the leftward flow, but upstream of dand5, a nodal inhibitor involved in left-right patterning. {ECO:0000269|PubMed:34903892}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A1D5NSM8

SVEP1_DANRE

MMVTLRLALTLRLTVLLLYWSGCTCWPSHAQQFSLQSLRQTSQARQNLSESAESKVERLGQVFRKNVRLLRERGGCLDLVFLVDESSSVGASNFKSELRFVRKMLSDFPVAPEATRVALVTFSSKSHVVTRADYVSAPKAHQHKCSLFSKEIPSITYRGGGTYTRGAFQRAAQILRQSRENATKVIFLITDGYSNGGDPRPVAAALRERGVEIFTLGIWQGNIRELHEMASQPKDQHCFFVHNFAEFEALARRALHEDLPSGNYIQEDLAQCSSLCDGGKDCCDLMASCKCGTHTGQYDCVCEKGYYGKGLQHECTACPSATYKPEAVAGGASTCLPCPDPHHTSRPGSTDISDCVCLEGYRPHNNTCQAVVCPVLSPPENGFFIQNVCNNQFNSACGVRCLPGFDLQGDGIRLCQPDGTWSGVQPSCRIRSCPDLSPPHHGMLNCSERSAPYRLECLVRCEQGYRLQGRARITCLANSQWSGPQPRCVEVRCPPIVTLKHIHLMPSTCGENEVRTGAVCQLSCPYGYSLIGDSKVKCLPTGNWSDNLHKATCTDVEPPWIQCPGDVITETDEHQRSANVSLSAPMLRDNSGDEVMVQVTPVLNPMQTFPIGTEFITYTATDRTGNKANCSFTVTVVDTEPPLIDRCRSPPTVKATGRKTAVYWEEPQFSDNSGAQLNISSTHSSGDIFPVGETSVYYTATDPSGNNRTCELIITVRGSTCEKPFVPVNGDFSCAKTKEGMNCTLICRQGYSLAQNAVHSYFCANNGIWEPPRSPDRPDCSLNRIANNGFKPFEMLFKASRCDDLNLVRSFSGEFSNVLKNTVPNICGGDDVSCKLEMTLPAQCLEYNYDYPNGFAIGPGGWGSNWGSQNGEDYAYFDSGFAPEHQLQKDASSQHGSHMRTKRHRKITGPTREQKIQIHFNITASIPLPLSRNDSAEIVNQKRLLRALEQLTNRLKRTLAKQPFSTFHVSSEMIVADPKSLESKKATLYCRPGSVLKGRVCVLCPVGTYFSLEYAECESCWRGSYQNEEGQMECKSCPDGSSTPYLHSRSQAECKAQCQPGSSSLTGLETCESCPLGEYQPGFGSQDCLSCPSTTTTVNRGALDVNECGVPCSAGHFSRTGLVPCYPCPRDYYQPEEGRSYCLSCPFYGTTTITGARAIQQCSSFGSSFLPKEESATTAPEVIVRKDYQASSQMFHECLLNPCQNQGTCEEVGVGYVCTCLPGFTGAKCESDIDECDSAPCQNGGLCRDGMGDFQCQCQPGFVGLLCEAEVNECSSSPCLNEGICVDEVNYFSCSCPDGFTGPRCEMEINECASSPCQNEGVCKDLEGGYFCTCAQGFTGDNCEVDVNECYSAPCLNGGTCVDAINDFRCECVNGYRGRLCQVDVDDCELNLCLNGATCVDGVATFTCRCPPGFNGTRCETEMPYSFDLEFEVSGIHGYVMMDGHMPSLTQITCTFWMRSSDTVNYGTPVSYAVEGSDNAFLLIDYNGWVLYVNGKERITDCPAVNDGLWHHIGVTWRSKDGDWRVYIDGSPSDGGKGLSIGTTIPGGGALVLGQDQDQRGDGFNPVESFVGTLSQLNIWNYVLTPQQIRSLASSCPHDLQKGNVFAWPDFLGGVTGRVKTTSKSIFCADCPLVETSVPHLLSSSKAVSPGSKVQFSCSPGFYLVGEPVQLCLNRGQWSHAEPICERVECGPPPDLEHGQYHGEDFYAGSSVLYQCKPGFYLLGESKMQCTNNGKWIGNPPACLDVDECSLGSECDEHASCQNTDGSHICTCIAPYSGDGRNCTEPVKCKDPGVPEFGQREGTNFIMGSEVVFSCKEGYELIGSSQLTCTEEGFWKQDVPYCKALSCPHPTLPKYGILKGANFTYGSKVTFSCEKGYVPLEPIESQCQSDLKWSREPHICQPITCGEPPVVDYAEYTLNGKIYRSTLSYTCIEGYRLQGAMELQCESSGEWTSPPPMCARVDCGKPPPLKDAVIKGDNFTLGSKIYYICKDGYTLLGAETQECLPSGNWTRNSSQCVPRSCGPPPQVDHALPDTGHQLFGDIAIYFCDDGYTAGNNTKLFCNAQGVWAPPDGFGIPHCIANFCQRPPDLPHAILDSINKPKYASNTEVSYKCEEGFVLNTTGTLKCLIGGEWTPSPSDIGCMPVRCSKPESIEKGYVSGNNYGFGAVIAYSCDKGYFIRGEKKRICKASGEWGGVLPTCQPISCPSPPRLANGFIQGQIRKNSYVYNSKVTYACNDGYRLTGKPERTCMANKQWSNSNSLVCVLLTCPTPPDIKNGLYHGSTFEVGSKVEFVCNEGYELIGDTVWTCLKFGNWDKSIIPRCSPVQCPEPPLEENHLVLRGLDSDSGTVELSCEEGYVLHGARTLRCTPSQEWNDSFPVCKQVFCGPPPEVAFGDPSDTQSYFGSVVTYSCMDGFTLRKEGSVHCQANGNWSKPYPQCIPVECPHPEDIPNGIVDVQGLMYLSTAVYSCKAGYDILGNSTVLCGQSGQWIGGIPVCHPVKCAAPKEIPNGSVRYSKLQFSQSITYFCQRGYRIQGPETLTCLENGQWDQEAPTCVPIYCSPPKPIDNGFVEGRDRKFGVTIFYSCFPGFLLVGNNHLTCEDHGWSSSEPKCVLADCGLPPHIDFGDYSKVQELSAEYDMVTSQQLPVDNSFLHGSLVKYHCHSGYEINGAIMLMCREDGTWNGTAPMCTPAQCEAPPSPENGSVMVTDSALGSLAEYSCAEGYELNGQTIRQCISGQQWSDDAPRCLPISCGNPGGIANGEVIGKSFHFKELIHYECHSGFVLEGVETRTCQVDGKWDNKAPLCKEVSCGRPVVSKDVLVRGDDHTFGKRLLFSCNLGFILLGAPTIVCLANGSWNEVPPKCLPANCGQPPSIENGRVTGTDYGYNGMVRYACDIGYVLTGNPTLICRADGLWDDPPPRCDIITCDPPEDISHGYLNGSSFNFDDIVEYICFPGYEVVGSPILRCAAEGVWLGQVPECRPCVCSPPVFKYGSILGRDHTCGASIWFRCDDGYKILGSSEAICDKGGVWSPGVPICTRGRCSIPPPAVPNAVIQGSTAYTIDTVTYRCRPGYHLKGFPHISCGRLGRWGEPNLSCEPISCGVPPLISNAETVGAVLTYGSKAQYRCKEGFELATKTDSITCQSDGTWSKHGVRCRPSPCTLPTNLTHVVITGKQLTPVGGTVIVSCRPGYYLEGPGLSECTVSGKWSPPLASCLPVICEKPLPILNGLVEGISYNYGDVVNFTCQQGFLLQGHSVRTCQGDKTWSGTQPVCAAVSCGPPPVVPNAVASSSGQTYKSIVSYTCRQGTSLVDSQNLTCQANGSWSLPTPICEVPGGCEKITDLLNGKVQEHNLSSGRALEFHCNKGYTLQGESLVMCVGNGSWSSPFPVCLPKPCPPLPHGWTVGSANATQTVFSVGQSVQVSCPKGQRVKSNQGKGIATLTCRSDQTWTPISAVCERVSCGPPLYVSNGVVRGAVFQFGDMVLYSCYAGFTMEGSSRSVCLDNGTWTQPPTCKAVCWRHCQNGGVCQRPNTCSCPEGWMGRFCEEPICILPCLNGGRCVAPYQCECPAGWTGTRCHNAVCSMPCLNGGRCIRPNRCHCSPGWGGYDCSRKRKSAYFHF

cell migration [GO:0016477]; epidermal cell differentiation [GO:0009913]; epidermis development [GO:0008544]; epithelial cell-cell adhesion [GO:0090136]; lymph vessel development [GO:0001945]; lymph vessel morphogenesis [GO:0036303]; negative regulation of complement activation, classical pathway [GO:0045959]

cytoplasm [GO:0005737]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634]

calcium ion binding [GO:0005509]

PF00008;PF12947;PF07699;PF12661;PF02494;PF00354;PF00084;PF00092;

2.60.120.200;2.10.70.10;2.10.25.10;2.10.50.10;3.40.50.410;

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A2AVA0}. Nucleus {ECO:0000250|UniProtKB:Q4LDE5}. Cytoplasm {ECO:0000250|UniProtKB:Q4LDE5}. Membrane {ECO:0000250|UniProtKB:Q4LDE5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q4LDE5}.

FUNCTION: Required for embryonic lymphatic vascular development, via promotion of parachordal lymphangioblast development, cell alignment and migration both dorsally and ventrally (PubMed:28179430, PubMed:28179432, PubMed:37097004). Required for the formation of facial lymphatic structures and formation of brain lymphatic endothelial cells (PubMed:37097004). Acts in tandem with vegfa signaling to promote tip cell specification and the stabilization of lumenized vascular connections between neighboring arterial intersegmental vessel sprouts, thereby facilitating dorsal longitudinal anastomotic vessel formation in response to low blood flow (PubMed:35312765). Plays a role in epidermal differentiation, potentially via mediating cell-cell adhesion (PubMed:27892606). {ECO:0000269|PubMed:27892606, ECO:0000269|PubMed:28179430, ECO:0000269|PubMed:28179432, ECO:0000269|PubMed:35312765, ECO:0000269|PubMed:37097004}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A1D5NY17

TM182_CHICK

MKLSVGIFFGGLFAALGVLLFLVAFGTDYWLLATEIGRCSKAPEDAGTEKATFHHEGFFWRCWFSGNVREHNTSMWKFWYTNQSPSKNCTHAYLSPFPHIRDEHNSTSYDSAVIYRGFWTVLMLLGVITIVMASFLIICAAPFASHILYKAGGGFYILAGVLFSLVVVMYVIWVQAMADLENYTNMKKMDCPDFAVYVRYGWSFMLAPIGVFFALLAGMLFLLVGRAIYLNSD

muscle organ development [GO:0007517]; myotube cell development involved in skeletal muscle regeneration [GO:0014906]; myotube differentiation involved in skeletal muscle regeneration [GO:0014908]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of myoblast fusion [GO:1901740]

plasma membrane [GO:0005886]

PF13903;

1.20.140.150;

TMEM182 family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:34427057}; Multi-pass membrane protein {ECO:0000255}.

FUNCTION: Negatively regulates myogenesis and skeletal muscle regeneration via its association with ITGB1 (PubMed:34427057). Modulates ITGB1 activation by decreasing ITGB1-LAMB1 interaction and inhibiting ITGB1-mediated intracellular signaling during myogenesis (PubMed:34427057). {ECO:0000269|PubMed:34427057}.

Gallus gallus (Chicken)

A0A1D5PPP7

CASP6_CHICK

MSGAERRPAAGRVQLDSKPTPTTTADGNQNITEVDAFDKRQTFDPAVQYKMNHQRRGVALIFNHEHFFWHLRLPDRRGTLADRNNLKRSLTDLGFEVRIFDDLKAEDVLKKVFEASRDDYSNADCFVCVFLSHGENDHVYAYDAQIKIETITNMFRGDKCQSLVGKPKIFIIQACRGDKHDDPVLVQDSVDSKDETTVNQTEVDAAGVYTLPAGADFIMCYSVAQGYFSHRETVNGSWYIQDLCEALGKHGSSLEFTELLTVVNRKVSHRKVDICRDINAIGKKQIPCFASMLTKKLYFHPKSK

3.4.22.59

activation of innate immune response [GO:0002218]; apoptotic chromosome condensation [GO:0030263]; apoptotic DNA fragmentation [GO:0006309]; apoptotic nuclear changes [GO:0030262]; apoptotic process [GO:0006915]; hepatocyte apoptotic process [GO:0097284]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; lens fiber cell differentiation [GO:0070306]; positive regulation of apoptotic process [GO:0043065]; positive regulation of necroptotic process [GO:0060545]; positive regulation of neuron apoptotic process [GO:0043525]; protein autoprocessing [GO:0016540]; proteolysis [GO:0006508]; pyroptosis [GO:0070269]

cytoplasm [GO:0005737]; nucleus [GO:0005634]

cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; cysteine-type peptidase activity [GO:0008234]

PF00656;

3.40.50.1460;

Peptidase C14A family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P55212}. Nucleus {ECO:0000250|UniProtKB:P55212}.

CATALYTIC ACTIVITY: Reaction=Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-.; EC=3.4.22.59; Evidence={ECO:0000250|UniProtKB:P55212};

FUNCTION: Cysteine protease that plays essential roles in programmed cell death, development and innate immunity (PubMed:11953316). Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear structural protein lamin-A/LMNA thereby inducing nuclear shrinkage and fragmentation (PubMed:11953316). Lamin-A/LMNA cleavage is required for chromatin condensation and nuclear disassembly during apoptotic execution (PubMed:11953316). Plays an essential role in defense against viruses by acting as a central mediator of the ZBP1-mediated pyroptosis, apoptosis, and necroptosis (PANoptosis), independently of its cysteine protease activity. PANoptosis is a unique inflammatory programmed cell death, which provides a molecular scaffold that allows the interactions and activation of machinery required for inflammasome/pyroptosis, apoptosis and necroptosis (By similarity). {ECO:0000250|UniProtKB:P55212, ECO:0000269|PubMed:11953316}.

Gallus gallus (Chicken)

A0A1D5PRR9

FANCM_CHICK

MSGGRQRTLPEAWRRAAGPALQAGRDADGNDDDDDELLAAAAAELDPDPNPNVDPNPGPGPEAAAGGFCAAAGALWIYPTNRPERPYQLRMARAALFANTLLCLPTGLGKTFVAAVVMYNFYRWFPSGKVLFLAPTKALVAQQMEACAQLMGIPGRDMAEMTGGTQALSRRELWASRRVFFLTPQIMVNDLSRGTCPAVEVKCLVVDEAHKALGNHAYCQVVKELSRYTTQFRVLALTATPGSDTKAVQQVVSNLLIAQIELCSEDSPEIQPYSHERQVEKIVVPLGEELGGIQRAYIHVLETFAGRLIKLGVLARRDVPSLTKYQIILARDQYRKNPSPQNVGMQPGIIEGDFALCISLYHGYELLQQMGVRSLFIYLCGIMDGSKGLTRTKNELGRNEDFMRLYQQLTDMFSDTCQTSANGNLHKSRTVSENKKEFIYSHPKLKKLEEIVIEHFKSRKMGCSDQTTSGGTCVDTRVMIFSSFRDSVQEIAEMLSRFSPVVRVMTFVGHSTGKSTKGFTQKEQLEVVKRFREGGYNTLVSTCVGEEGLDIGEVDLIICFDAQKSPIRLVQRMGRTGRQRQGRVVVILAEGREERTYNQSQSNRRSIQKAISGNKMLHFYQHSPRMIPEGINPELHRMFITAEKYKPNDSGRLPKGRPSSLHHKSALFSCVTDPKEMHCHENWSLSPEEFEIWDRLYRLKENDGVKEPILPHTRFETLENLDKTSKPEEEAAHKLSLSEWSIWQSRPFPTSMVDHSDRCYHFISVMELIEVMRQEQGDCSYELELQPHLRIEDIHVRRNKGHLSTTSSAFAQKTHSSKRDMARTKRPFVPDVNDNEREFFSIFKTTNTKTPRTAPGLDLEEPELPTDTNGSEPCSARRLTLVASTDQGSPKEEEIEKVTFDLNEFNDLCDDGESTVAHESAAVKDLRLLDKHCSSVGLNHTDLGYSSFTAEKSPASSDLFYLPESHVDSFVLVSSSAELAGLEGAFSCVKGLLAHSPPPVSKLEGIEELLRHEETLCPLPKVSCRSYSGQLPHGDFPSSLAVDQSLLPAESPELEVTIGLSAAVNTCVSKPASTPTAAGGAEERPPGGGSFHSLLGKEGFTANHTDNPPNKHFVQGDEEDSEMKRDVTIDGEKSIHLFEDEHTYKVNDEMPSVDVEPLLRLGSGGHTARPSAGPASQQPPSGDSPRGDTACGEGAARGEMAPGGAWGRGSAAEQALHNSELCDYSQELFSVNFDLGFSIEECEEEIFEGDTDAMNTPKLNSASRSRADVQLTANRKSLNDGCRVQTPPKWDCKGLKGRNISTPLPLQSGHVRDTAVPGGTAGGRTGRGSPGASPPSPATPTGRRVSSAEATRRIRKKVFSTVREETPEVCPTDKVNPNSQRNSFGSSASDALHTTGGRTENLEGTNLHTSRVFPAEGTSSESEEEIVFQRKNRRNNVLRSPDVGSDSDFGSPVCAVRKRRHPLTVSDVSSDDGVDFHKNPNRGTRGCSAAGSKAQLRGVKRQKVRSKVTCKNAARQFLDEEAELSQQDESCVSSDETEDTDKELSSSLAQFLNDDAEVTQVLNDSEMRGVYLKSVRSPALGSRYRMVHREFNSTEIFSQIPEQDEAYAEDSFCVAEGDEETCNKSESSEEEEVCVNFDLLNNESFGGGGGRYLTRRRKKLHGANMEQNCSAPVQKKPSRIIVLSDSSGEETNVSNEKGTAAHCSRAGRENAELLTSMPSVSSVPHKKSAGDVSAHQSAESKSGMLLGLKASVSEVLDFHPGPRSGSGKEALQAAAQHLQLESSVKNSAGNAPGATKASPALLDGDTALCVLVDSREISSGADVISSLKAVHGLKVQVCSLGSGDYVVSNRMAVERKFQSELLSSVNRTKVTQRLQRLQGMFERVCVIVEKDRTRPGETSRFSQRTQHYDATLAALLQAGIRVLFSSCQEETAVLLKELALLEQRKNAAICVPTEVEGHKQEMLNFYLSLPNISYLAALNMCHHFSSVRTMVNSSPSDIAAGARVSLQRAEETYRYLRYGFDTQMLPESLCAKGKSNTATRS

3.6.4.13

double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; interstrand cross-link repair [GO:0036297]

nucleus [GO:0005634]

3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; four-way junction DNA binding [GO:0000400]; four-way junction helicase activity [GO:0009378]; nuclease activity [GO:0004518]; RNA helicase activity [GO:0003724]

PF00270;PF02732;PF16783;PF00271;

3.40.50.10130;1.10.150.20;1.20.1320.20;3.40.50.300;

DEAD box helicase family, DEAH subfamily, FANCM sub-subfamily

PTM: Phosphorylated; hyperphosphorylated in response to genotoxic stress. {ECO:0000269|PubMed:19465393}.

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19465393}.

CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q8IYD8};

FUNCTION: DNA-dependent ATPase component of the Fanconi anemia (FA) core complex (By similarity). Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:16116434, PubMed:19465393). In complex with CENPS and CENPX, binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA) and Holliday junction substrates (By similarity). Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork (By similarity). This activity is strongly stimulated in the presence of CENPS and CENPX (By similarity). In complex with FAAP24, efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates (By similarity). In vitro, on its own, strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA (By similarity). {ECO:0000250|UniProtKB:Q8IYD8, ECO:0000269|PubMed:16116434, ECO:0000269|PubMed:19465393}.

Gallus gallus (Chicken)

A0A1D5PUP4

RECK_CHICK

MAAAVAAWPWALFCLAAVPPLLSPGAAGLSCCYHAKDNLMCRDVCEQILSSKSDSRLKHLLQRAPEYCPESMGEVWGCINSSLPGVLKKSDGWVGLGCCELAIAVECRQACKQASSKNDILKVCRKEYENALFSCINRNEMGSICCSYAGHHTNCREYCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDYACQTACKRILMSMKTELEIVDGLIEGCKTMPLPQDPLWQCFLESSRSVHPGVTVHPPPSTGLDGAKLHCCSKANSSTCRELCTKLYSTSWGSSQSWQEFDRFCEYNAVEVSMLTCLADVREPCQLGCRNLSYCTNFNNRPTELFRSCNSQSDQGAMNDMKLWEKGSIKMPFINIPVLDINKCQPEMWKAIACSLQIKPCHSKSRGSIICKSDCVEILKKCGDHNKFPEGHTAESICELLSPTDDLENCIPLDTYLSPSSLGNIVEDVTHPCNPNPCAANQLCEVNRKGCQSGELCLPYLCVPGCKLGEASDFIVRQGTLIQVPSSAGDVGCYKICTCGHTGLLENCVEMHCVDLQKSCIVGGQKKSHGTSFNIDCNVCSCFAGNLICSTRQCLTEHSSEDERQKFTGLPCNCVDQFVPVCGQNGRTYPSACIARCVGLQDNQFEFGSCISKDPCNPNPCSKNQRCIPKKQVCLTSFGKFECSQHECVPRQLNCDQTQDPVCDTDSVEYSNVCTLYQKGKNLAYRGPCQPFCKSVEPVCGHNGETYSSVCAAYSDRVAVDYYGHCQAVGVLSDYGFHTECAFVKCPQLSATGCKPVIAPGACCPLCAGMLRILYDKDKLDNFARVTNKKPITVLDILEKLRLHVSVPQCDVFGYLSIESEIVILIIPVDQKPKPLQIEACNKEAEKIESLINSDSPTLASHVPLSALIASQVQVSFSISSPSVKVGPVLHCLFISFSFTLLKLMDYI

blood vessel maturation [GO:0001955]; canonical Wnt signaling pathway [GO:0060070]; extracellular matrix organization [GO:0030198]; negative regulation of metalloendopeptidase activity [GO:1904684]; regulation of angiogenesis [GO:0045765]; regulation of establishment of blood-brain barrier [GO:0090210]; sprouting angiogenesis [GO:0002040]

extracellular space [GO:0005615]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; Wnt signalosome [GO:1990909]

coreceptor activity [GO:0015026]; endopeptidase inhibitor activity [GO:0004866]; metalloendopeptidase inhibitor activity [GO:0008191]; serine-type endopeptidase inhibitor activity [GO:0004867]

PF07648;

3.30.60.30;

RECK family

PTM: Localizes to the plasma membrane via its GPI-anchor (PubMed:23329048). Released from the plasma membrane following cleavage of the GPI-anchor by GDPD5/GPE2 (PubMed:23329048). {ECO:0000269|PubMed:23329048}.

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23329048}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:23329048}.

FUNCTION: Functions together with ADGRA2 to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B) (By similarity). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). Acts as a Wnt7-specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7. ADGRA2 is then required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex. Also acts as a serine protease inhibitor (By similarity). {ECO:0000250|UniProtKB:O95980, ECO:0000250|UniProtKB:Q9Z0J1}.

Gallus gallus (Chicken)

A0A1D5PXA5

TRPV4_CHICK

MADPEDPRDAGDVLGDDSFPLSSLANLFEVEDTPSPAEPSRGPPGAVDGKQNLRMKFHGAFRKGPPKPMELLESTIYESSVVPAPKKAPMDSLFDYGTYRQHPSENKRWRRRVVEKPVAGTKGPAPNPPPILKVFNRPILFDIVSRGSPDGLEGLLSFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMREFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVHYLTENGHKQADLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGIFQHIIRREIADEDVRHLSRKFKDWAYGPVYSSLYDLSSLDTCGEEVSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYISVVSYLCAMIIFTLIAYYRPMEGPPPYPYTTTIDYLRLAGEIITLLTGILFFFSNIKDLFMKKCPGVNSFFIDGSFQLLYFIYSVLVIVTAGLYLGGVEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCPSSESCSEDHSNCTLPTYPSCRDSQTFSTFLLDLFKLTIGMGDLEMLESAKYPGVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPLFLRRVFRSGEMVTVGKGTDGTPDRRWCFRVDEVNWSHWNQNLGIISEDPGKSDTYQYYGFSHTVGRLRRDRWSTVVPRVVELNKSCPTEDVVVPLGTMGTAEARERRHGQTPSSPL

actin filament organization [GO:0007015]; calcium ion import across plasma membrane [GO:0098703]; intracellular calcium ion homeostasis [GO:0006874]; osmosensory signaling pathway [GO:0007231]

adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; cilium [GO:0005929]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; calcium channel activity [GO:0005262]; calmodulin binding [GO:0005516]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; monoatomic cation channel activity [GO:0005261]; phosphatidylinositol binding [GO:0035091]; SH3 domain binding [GO:0017124]

PF00023;PF00520;

1.10.287.70;1.25.40.20;

Transient receptor (TC 1.A.4) family, TrpV subfamily, TRPV4 sub-subfamily

SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000305|PubMed:11081638, ECO:0000305|PubMed:19864432}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9EPK8}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9EPK8}.

CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:11081638, ECO:0000269|PubMed:19864432};

FUNCTION: Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity (PubMed:11081638, PubMed:19864432). Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:11081638). Also activated by phorbol esters (PubMed:19864432). Channel activity seems to be regulated by a calmodulin-dependent mechanism (By similarity). {ECO:0000250|UniProtKB:Q9HBA0, ECO:0000269|PubMed:11081638, ECO:0000269|PubMed:19864432}.

Gallus gallus (Chicken)

A0A1D6E0S8

WAK17_MAIZE

MPSRSPACRPRGRNRRSAADAVARPLALALILVSTLPRAAHSQDLALPPVQPRGVRRTMTCDNIPEPFGTRSRGASRLPGFEVTCGPNREAMLSIGGDAYMIDFVSVSGSYVVVFAEPITQVCYDGKGKPTPDTGTGAKSSEGTTTTFTWSLEGTPFTFSKSNKLVNFGCNRTLMANFFIVPGDSSPLYTSCTTTCNTLQISGSCLGEACCEAPMDQVNGAKAFSLSFERTTANGTGEEDGTCSAAFFLDKDETVFTFSGDEVRPLKTALLPPGERRMVLDWAIGSTSCEQTQSYTFEKLCKYGTCVDAPTGAGYLCKCPSGYDGNPYVSDGCQDINECRNYNSNNCTYQNLCNNTLGGYTCSCPENNIGDGYRTGTGCNTTLATPVSPSQQPQGINVCDHPEKNPCTYIKYCIDLEGVVSCACPEGMSGDGRKNGRGCCFSCQKHFPLDTVLGVSLVLMVTTTTAASCYCWAVKKRELGRKRAELFRKNGGLLLQQRFSTITSQGEDQYSSKIFSAEELKAATDNYSESRILGRGGQGTVYKGILPDQTVVAIKKSKVFDESQVEQFVNEIAILSQIDHPNVVKLLGCCLETQVPLLVYEFISNGTLFQHIHNRNATRPLTWEDCLRIAAETADALAYLHSASSIPIIHRDIKSSNILLDGNFVAKIADFGASRSVPFDQTHITTLIQGTIGYLDPEYFQSSQLTEKSDVYSFGVVLAELLTRQKPISAARPEDSCNLAMHLVVLFNKGRLLQEIEPHILAEAGEDQCYAVAELSVRCLNVKGEERPAMVVVASVLQELRRSFTIDQAVGIKDESIQENSEQEEKHLHESRSIPSLQSSEVSTQCSMEAKMSSFC

2.7.11.1

COFACTOR: [Isoform 1]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q1MX30}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q1MX30};

cell surface receptor signaling pathway [GO:0007166]; detection of symbiotic fungus [GO:0009603]; innate immune response [GO:0045087]; phosphorylation [GO:0016310]; positive regulation of plant-type hypersensitive response [GO:0034052]

external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; protein serine/threonine kinase activity [GO:0004674]

PF00069;

2.10.25.10;1.10.510.10;

Protein kinase superfamily, Ser/Thr protein kinase family

SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:36577386}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:36577386}; Peripheral membrane protein {ECO:0000305|PubMed:36577386}. Note=Associates with the plasma membrane via interactions with WAK17 isoform 1. {ECO:0000269|PubMed:36577386}.

CATALYTIC ACTIVITY: [Isoform 1]: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q1MX30}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q1MX30};

FUNCTION: [Isoform 1]: Kinase that contributes to activation of the hypersensitive response, a form of programmed cell death, upon fungal infection. {ECO:0000269|PubMed:36577386}.; FUNCTION: [Isoform 2]: Secreted protein that contributes to activation of the hypersensitive response, a form of programmed cell death, upon fungal infection (PubMed:36577386). May sense the presence of fungal material and relay the signal to WAK17 isoform 1 (Probable). {ECO:0000269|PubMed:36577386, ECO:0000305|PubMed:36577386}.

Zea mays (Maize)

A0A1D6EFT8

EDSB_MAIZE

MAPSNIVVQSSSTPPVAGGDEEFAPSVWGDFFVTYATPVSQASEQRMSERAELLKAQVRQAFDAASMDVAGLITYVDTLERLGLDNHFRDLIGAALERIGAEELPEHGGGLHIVALRFRLLRQHGIWVSTDVFDAFREDAGGFCSSLCSDDPRGLLSLYNAAHMAVPGEVVLDDAIAFARGRLLDIISKGEVRSPVSEQITRALDIPLPRFTRRLETMHYIAEYEHEEAHDGLLLELARLNFVLVRALHLRELKDLSLWWRELYNTVKLPYARDRMVEIYFWTCGMLHEEEYSLARMFFAKTFGMVSLMDDTFDVHATLDECHKLKEAMQRWDESEVSILPEYLRLLYIKTLSNFKEFEEILEPNKKYRMAYTKEAYKLCSKNYLKEAIWSNQKYQPSFKEHEELSIMTSGLPMLTILTLMGFGDEATPEAFEWVSSVPEMVRAGSQVTRFLNDLSSYKLGKNKKDMPGSVETYMVENGLTGDEAAAAIAALLENRWRILNQTRMEIDHTLLPAAQVVLNMARANEIIYLHGRDAYTFGADLKDLVTTLFLKQVLPL

4.2.3.197

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7};

defense response to fungus [GO:0050832]; diterpenoid biosynthetic process [GO:0016102]; sesquiterpene biosynthetic process [GO:0051762]; terpene biosynthetic process [GO:0046246]

cytoplasm [GO:0005737]

magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]

PF01397;PF03936;

1.10.600.10;1.50.10.130;

Terpene synthase family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.

CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + 2 H2O = 7-epi-ent-eudesmane-5,11-diol + diphosphate; Xref=Rhea:RHEA:58164, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:142536, ChEBI:CHEBI:175763; EC=4.2.3.197; Evidence={ECO:0000269|PubMed:29570233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58165; Evidence={ECO:0000269|PubMed:29570233};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30187155}.

FUNCTION: Component of the volatile terpenes biosynthesis pathways (PubMed:30187155). Dihydroxylated sesquiterpenoid synthase that generates dually hydroxylated products directly from (E,E)-farnesyl diphosphate, primarily eudesmane-2,11-diol, along with two closely related structural isomers (PubMed:29570233). {ECO:0000269|PubMed:29570233, ECO:0000303|PubMed:30187155}.

Zea mays (Maize)

A0A1D6HSP4

C92C5_MAIZE

MELASTMSVAMALAAAIFVVLCSVVASARGRREKALKLPPGPRGWPVLGSLGALAGALPPHRALAALAARHGPLMHLRLGSYHTVVASSADAARLVLRTHDSALADRPDTAAGEITSYGYLGIVHTPRGAYWRMARRLCATELFSARRVESFQDVRAQEMRALARGLFGCAAGRRAVAVREHVAGATMRNILRMAVGEKWSGCYGSPEGEAFRRSLDEAFAATGAVSNVGEWVPWLGWLDVQGFKRKMKRLHDLHDHFYEKILVDHEERRRLAQASGGEFVATDLVDVLLQLSEESTKLESESEARLPRDGVKALIQDIIAGGTESSAVTIEWAMAELLRHPEAMAKATDELDRVVGSGRWVAERDLPELHYIDAVVKETLRLHPVGPLLVPHYARERTVVAGYDVPAGARVLVNAWAIARDPASWPDAPDAFQPERFLGAAAAVDVRGAHFELLPFGSGRRICPAYDLAMKLVAAGVANLVHGFAWRLPDGVAAEDVSMEEHVGLSTRRKVPLFAVAEPRLPVHLYSATE

1.14.14.58; 1.14.14.59

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242};

defense response [GO:0006952]; response to herbivore [GO:0080027]; terpenoid biosynthetic process [GO:0016114]

membrane [GO:0016020]

4,8,12-trimethyltrideca-1,3,7,11-tetraene synthase activity [GO:0097007]; DMNT synthase activity [GO:0102171]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; terpene synthase activity [GO:0010333]

PF00067;

1.10.630.10;

Cytochrome P450 family

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=(6E,10E)-geranyllinalool + O2 + reduced [NADPH--hemoprotein reductase] = (3E,7E)-4,8,12-trimethyltrideca 1,3,7,11-tetraene + but-3-en-2-one + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:13545, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:48058, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:74299, ChEBI:CHEBI:74322; EC=1.14.14.58; Evidence={ECO:0000269|PubMed:27662898}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13546; Evidence={ECO:0000269|PubMed:27662898}; CATALYTIC ACTIVITY: Reaction=(3S,6E)-nerolidol + O2 + reduced [NADPH--hemoprotein reductase] = (3E)-4,8-dimethylnona-1,3,7-triene + but-3-en-2-one + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55424, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:48058, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:59958, ChEBI:CHEBI:60158; EC=1.14.14.59; Evidence={ECO:0000269|PubMed:27662898}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55425; Evidence={ECO:0000269|PubMed:27662898};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14.2 uM for (E)-nerolidol {ECO:0000269|PubMed:27662898}; KM=5.6 uM for (6E,10E)-geranyllinalool {ECO:0000269|PubMed:27662898};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30187155}.

FUNCTION: Involved in the biosynthesis of homoterpenes, attractants of herbivores parasitoids and predators (e.g. predatory mites and parasitoid wasps) (By similarity). Component of the volatile terpenes biosynthesis pathways (PubMed:30187155). Converts mainly nerolidol to dimethylnonatriene (DMNT) and, to a lower extent, geranyllinalool to trimethyltridecatetraene (TMTT) (PubMed:27662898). {ECO:0000250|UniProtKB:Q9LSF8, ECO:0000269|PubMed:27662898, ECO:0000303|PubMed:30187155}.

Zea mays (Maize)

A0A1D6IEG9

CRP1_MAIZE

MPASLLPPTFLPHHLRRLAPAGCTTSSVTSSSVSIPASRYDFEPLLAYLSSPSVSASLTSPSPPASVPAPEHRLAASYSAVPSHEWHALLRDLAASDASLPLAFALLPFLHRHRLCFPLDLLLSSLLHSLSVSGRLLPHSLLLSFPPSLSDPPSPLLLNSLLAASAAASRPAVALRLLSLLREHDFLPDLASYSHLLASLLNTRDPPDAALLERLLGDLRESRLEPDAPLFSDLISAFARAALPDAALELLASAQAIGLTPRSNAVTALISALGTAGRVAEAEALFLEFFLAGEIKPRTRAYNALLKGYVRIASLKNAEQVLDEMSQCGVAPDEATYSLLVDAYTRAGRWESARILLKEMEADGVKPSSYVFSRILAGFRDRGDWQKAFAVLREMQASGVRPDRHFYNVMIDTFGKYNCLGHAMDAFNKMREEGIEPDVVTWNTLIDAHCKGGRHDRAAELFEEMRESNCPPGTTTYNIMINLLGEQEHWEGVEAMLSEMKEQGLVPNIITYTTLVDVYGRSGRYKEAIDCIEAMKADGLKPSPTMYHALVNAYAQRGLADHALNVVKAMKADGLEVSILVLNSLINAFGEDRRVVEAFSVLQFMRENGLRPDVITYTTLMKALIRVEQFDKVPVIYEEMITSGCAPDRKARAMLRSGLKYIKHMRVA

chloroplast mRNA processing [GO:0010239]; chloroplast organization [GO:0009658]; mRNA processing [GO:0006397]; positive regulation of translation [GO:0045727]

chloroplast [GO:0009507]; chloroplast nucleoid [GO:0042644]; chloroplast stroma [GO:0009570]; cytoplasm [GO:0005737]; thylakoid membrane [GO:0042651]

mRNA binding [GO:0003729]; single-stranded RNA binding [GO:0003727]

PF01535;PF13041;PF13812;PF17177;

1.25.40.10;

PPR family, P subfamily

SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:10228173}.

FUNCTION: Required for the translation of the chloroplast petA and petD mRNAs. Required for the processing of the petD mRNA from a polycistronic precursor (PubMed:8039510). Binds with high affinity to the 5'-UTR of the chloroplastic petA transcript (PubMed:18669444). Activates psaC and petA translation by binding their 5'-UTRs (PubMed:16141451, PubMed:23735295). {ECO:0000269|PubMed:16141451, ECO:0000269|PubMed:18669444, ECO:0000269|PubMed:23735295, ECO:0000269|PubMed:8039510}.

Zea mays (Maize)

A0A1D6K6U5

CPPS2_MAIZE

MVLSSSCTTVPHLSSLAVVQLGPWSSRIKKKTDAVAVPAAAGRWRARARAQDTSESAAVAKGSSLTPIVRTDAESRRTRWPTDDDDAEPLVDEIRAMLTSMSDGDISVSAYDTAWVGLVPRLDGGEGPQFPAAVRWIRNNQLPDGSWGDAALFSAYDRLINTLACVVTLTRWSLEPEMRGRGLSFLGRNMWKLATEDEESMPIGFELAFPSLIELAKSLGVHDFPYDHQALQAIYSSREIKVKRIPKEVMHTVPTSILHSLEGMPGLDWARLLKLQSSDGSFLFSPAATAYALMNTGDDRCFSYIDRTVKKFNGGVPNVYPVDLFEHIWAVDRLERLGISRYFQKEIEQCMDYVNRHWTEDGICWARNSDVKEVDDTAMAFRLLRLHGYSVSPDVFKNFEKDGEFFAFVGQSNQAVTGMYNLNRASQISFPGEDVLHRAGPFSYEFLRRKQAEGALRDKWIISKDLPGEVVYTLDFPWYGNLPRVEARDYLEQYGGGDDVWIGKTLYRMPLVNNDVYLELARMDFNHCQALHQLEWQGLKKWYTENRLMDFGVAQEDALRAYFLAAASVYEPCRAAERLAWARAAILANAVSTHLRNSPSFRERLEHSLRCRPSEETDGSWFNSSSGSDAVLVKAVLRLTDSLAREAQPIHGGDPEDIHKLLRSAWAEWVREKADAADSVCNGSSAVEQEGSRMVHDKQTCLLLARMIEISAGRAAGEAASEDGDRRIIQLTGSICDSLKQKMLVSQDPEKNEEMMSHVDDELKLRIREFVQYLLRLGEKKTGSSETRQTFLSIVKSCYYAAHCPPHVVDRHISRVIFEPVSAAK

5.5.1.13

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q38802};

defense response [GO:0006952]; diterpene phytoalexin biosynthetic process [GO:0051502]; diterpenoid biosynthetic process [GO:0016102]; gibberellin biosynthetic process [GO:0009686]

chloroplast [GO:0009507]

ent-copalyl diphosphate synthase activity [GO:0009905]; isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]

PF01397;

1.50.10.160;1.10.600.10;1.50.10.130;

Terpene synthase family, Tpsc subfamily

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = ent-copalyl diphosphate; Xref=Rhea:RHEA:14841, ChEBI:CHEBI:58553, ChEBI:CHEBI:58756; EC=5.5.1.13; Evidence={ECO:0000269|PubMed:16307364, ECO:0000269|PubMed:29475898}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14842; Evidence={ECO:0000269|PubMed:16307364, ECO:0000269|PubMed:29475898};

PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis. {ECO:0000305}.

FUNCTION: Involved in gibberellin biosynthesis (PubMed:16307364). Catalyzes the conversion of geranylgeranyl diphosphate to the gibberellin precursor ent-copalyl diphosphate (ent-CPP) (PubMed:16307364). Involved in the production of antifungal dolabralexin phytoalexins in response to biotic and abiotic stresses (PubMed:29475898). In response to fungal infection and in associtation with KSL4, is involved in the production dolabradiene, a type of antifungal phytoalexin (PubMed:29475898). {ECO:0000269|PubMed:16307364, ECO:0000269|PubMed:29475898}.

Zea mays (Maize)

A0A1D6L709

VP8_MAIZE

MPHSVLARLPPGSVRLVAAFGLLLLVSLLVLHRRPGRPHVAAAAASDRLTDPSRSRLFLSQSPGANASIAADLRALTAGPHLAGTPASAGAAAHVLARLRAAGLQTLTREYEPLLSYPGHASLALLRPDGSLLARLSLEEPADEGRRVVPPYHAYAPSGGAVAEAVFVNLGREEDYVVLERLGVGVRGRVAVARRGGGYRGGVVARAADKGAVAVLIAGNADGGVERGVVLLGGPGDPLTPGWAATSGAERLKFDDKAVKQRFPSIPSMPVSAKTAAAIIRSLGGPAIPAEWKDGLGVDTGGLGPGPTLVNFTYQEDRKFYKIRDIFGIIKGQEEPDRYVILGNHRDAWTYGAVDPNSGTAALLDIARRLGIMLQSGWKPRRSIILCSWDGEEFGMIGSTEWVEDNLEDLHSKAVAYLNVDCAVQGVGFFAGSTPQLDKLLVDITRQVRDPDVTGKMVHDTWNEMSGGIKIERLARTDSDFAPFLHHAGIPSVDLYYGEEFPGYHTALDTYNWMEKHGDPFFLRHLAITEIWGLLALRLANDPVLPFDYQAYTSQLQEHIKTLSALTSNGHAVNLMNGCVNDLSGAAMEVLKEMKKLQQMDLYDEHARMRRRLLNDRLLLAERSFLQPEGLQGRGWFKHLLYSPPEDYESKLSFFPGIADAISRSANLSDKEQEVAMQHEVWKVCRAIQRAASVLRGEFSEQKPTNFSSLVTP

3.4.17.21

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q04609}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q04609};

embryo development ending in seed dormancy [GO:0009793]; flower development [GO:0009908]; leaf vascular tissue pattern formation [GO:0010305]; maintenance of meristem identity [GO:0010074]; photomorphogenesis [GO:0009640]; proteolysis [GO:0006508]; regulation of floral meristem growth [GO:0010080]; regulation of inflorescence meristem growth [GO:0010081]; regulation of root meristem growth [GO:0010082]; regulation of seed maturation [GO:2000034]

plasma membrane [GO:0005886]

carboxypeptidase activity [GO:0004180]; metal ion binding [GO:0046872]; metallocarboxypeptidase activity [GO:0004181]

PF04389;PF04253;

3.50.30.30;1.20.930.40;3.40.630.10;

Peptidase M28 family, M28B subfamily

SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.; EC=3.4.17.21; Evidence={ECO:0000305};

FUNCTION: Involved in the regulation of meristem development and seed maturation processes. Mediates regulation of embryonic regulatory genes and genes controlling abscisic acid (ABA) biosynthesis and turnover in developing seeds. May be required for the synthesis of small signaling molecules that integrates meristem and embryo formation in seeds. {ECO:0000269|PubMed:18203869}.

Zea mays (Maize)

A0A1D6LAB7

RH3B_MAIZE

MASLTLPALALALSNPGAVRLRAAAFRCWALRRRGWAAAGALASPNSVLSEHAFKRLQLGSDDEDGEGPYGSDADEGFEAGEGDNEELAIARLGLPDELVATLEKRGITHLFPIQRAVLIPALEGRDLIARAKTGTGKTLAFGIPMIKQLIEQDDGRITRRGRTPRVLVLAPTRELAKQVEKEIKESAPKLGTVCVYGGVSYNVQQNALSRGVDVVVGTPGRIIDLINGGSLQLGEVQYLVLDEADQMLAVGFEEDVETILQQLPAGRQSMLFSATMPSWVKKLSRRYLNNPLTIDLVGDQDEKLAEGIKLYAIPLTTTSKRTVLSDLITVYAKGGKTIVFTRTKKDADEVSLALTNSIASEALHGDISQHQRERTLNGFRQGKFTVLVATDVAARGLDIPNVDLIIHYELPNDPETFVHRSGRTGRAGKAGTAILMFTSSQKRTVKSLERDVGCNFEFISPPSIEEVLESSAEHVIATLRGVHPESTKYFLGAAEKLTEELGPHALASALAHLSGFSQPPSSRSLISHEQGWVTLQLTREQGFGRGFFSPRSVTGFLSDVCSAAADEVGKIYLTADENVQGAVFDLPEEIAKDLLTMELPPGNTLTKISKLPALQDDGPATDSYGRFSNDRGSRNNRRSRGGGASRGRGGWDTDGEDRFRRGGRSLRSDNDSWSDDDWSGGGRKSNRSSSFGSRSSSYSSRGSPSFGGRSSSFGGRESNRSFSGACFNCGESGHRATDCPNK

3.6.4.13

chloroplast organization [GO:0009658]; Group II intron splicing [GO:0000373]; ribosome biogenesis [GO:0042254]

chloroplast stroma [GO:0009570]; cytoplasm [GO:0005737]; cytosol [GO:0005829]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; zinc ion binding [GO:0008270]

PF00270;PF08152;PF00271;PF00098;

3.40.50.300;4.10.60.10;

DEAD box helicase family, DDX21/DDX50 subfamily

SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:22576849}.

CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000305};

FUNCTION: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts. Binds specific group II introns in chloroplasts and facilitates their splicing. Is required for rRNA maturation in plastids and may contribute to the assembly of the large (50S) ribosomal subunit. Required for normal development of chloroplasts. {ECO:0000269|PubMed:22576849}.

Zea mays (Maize)

A0A1D6LTV0

TPS26_MAIZE

MAGITGVMNMKLAARPSSGRHSRGCRPAVVPSAGKQMLLVRRHPPGSASWPTRATGGGGGGVPAGATAADSSGQAKEEEEEDRASRNTSSFEPSIWGDFFLTYSSPLATSSAQKARMVHRAEQLKKQVAKLIAASGACSLYHRIHLVDALERLCLDYLFEDEINDMVTQIHNVDVSGCDLQTVAMWFYLLRNHGYRVSSDVVFAKFRDEQGGFAANNPRDLLNLYNAACLRTHGETILDEAASFTSKCLKSLAPYTYMEASLASEIKRALEIPLPRSVRIYGAKSRIAEYGNQTEANELVLELAKLNYNLVQLQHQEELKIITRWWNDLELQTRLSFARDRVVECYFWMVGVYFEPSYSRARVILSKVLAIVSLLDDTYDVYGTSQECELFTKCIESWDPAATGGRLPGNMKFIFAKILDTCQSFEDELAPDEKYRMHYLKTFIIDLVRAYNEEVKWREQGYVPATVEEHLQVSARSGGCHLLSCTSFVGMGDVADQEAFEWVRGVPKIVKALCIILRLSDDLKSYEREKMSSHVASTMESCMKEHQVPLEVARVKIQETIDETWKDFNEEWLNLNTNSHLPRELLERIFNLTRTMVYIYQQDDAYTNCHVIKDTINSLFVEPVSIT

4.2.3.-; 4.2.3.111; 4.2.3.113; 4.2.3.114; 4.2.3.15; 4.2.3.16

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:B2C4D0}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:B2C4D0}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q5GJ60};

diterpenoid biosynthetic process [GO:0016102]; response to wounding [GO:0009611]; terpenoid biosynthetic process [GO:0016114]

chloroplast [GO:0009507]

(4S)-limonene synthase activity [GO:0050552]; gamma-terpinene synthase activity [GO:0102903]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; terpene synthase activity [GO:0010333]

PF01397;PF03936;

1.10.600.10;1.50.10.130;

Terpene synthase family, Tpsb subfamily

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18218975}.

CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol + diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.111; Evidence={ECO:0000269|PubMed:18218975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32552; Evidence={ECO:0000269|PubMed:18218975}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (4S)-limonene + diphosphate; Xref=Rhea:RHEA:12869, ChEBI:CHEBI:15383, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.16; Evidence={ECO:0000269|PubMed:18218975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12870; Evidence={ECO:0000269|PubMed:18218975}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + gamma-terpinene; Xref=Rhea:RHEA:32559, ChEBI:CHEBI:10577, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.114; Evidence={ECO:0000269|PubMed:18218975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32560; Evidence={ECO:0000269|PubMed:18218975}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:18218975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:18218975}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene; Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.113; Evidence={ECO:0000269|PubMed:18218975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501; Evidence={ECO:0000269|PubMed:18218975}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = 4-terpineol + diphosphate; Xref=Rhea:RHEA:60028, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:78884; Evidence={ECO:0000269|PubMed:18218975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60029; Evidence={ECO:0000269|PubMed:18218975};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30187155}.

FUNCTION: Component of the volatile terpenes biosynthesis pathways (PubMed:30187155). Mediates the synthesis of a blend of monoterpenes. Converts mainly geranyl diphosphate to alpha-terpineol. Triggers also the biosynthesis of minor monoterpenes including limonene, gamma-terpinene, beta-myrcene, terpinolene and 4-terpineol (PubMed:18218975). {ECO:0000269|PubMed:18218975, ECO:0000303|PubMed:30187155}.

Zea mays (Maize)

A0A1D8EJF9

IF4E1_SOLPI

MAAAEMERTMSFDAAEKLKAADGGGGEVDDELEEGEIVEESNDTASYLGKEITVKHPLEHSWTFWFDNPTTKSRQTAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLIMGADFHCFKHKIEPKWEDPVCANGGTWKMSFSKGKSDTSWLYTLLAMIGHQFDHGDEICGAVVSVRAKGEKIALWTKNAANETAQVSIGKQWKQFLDYSDSVGFIFHDDAKRLDRNAKNRYTV

defense response to virus [GO:0051607]; translational initiation [GO:0006413]

cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634]

RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743]

PF01652;

3.30.760.10;

Eukaryotic initiation factor 4E family

PTM: According to the redox status, the Cys-129-Cys-167 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}. Note=Binds to potyvirus viral genome-linked protein (VPg) in the nucleus and with potyvirus nuclear inclusion protein A (NIa-Pro) and nuclear inclusion protein B (NIb) in the cytoplasm. {ECO:0000250|UniProtKB:C6ZJZ3}.

FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses (PubMed:27655175). {ECO:0000250|UniProtKB:P29557, ECO:0000269|PubMed:27655175}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection (e.g. potato virus Y (PVY) and tobacco etch virus (TEV)) by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000269|PubMed:27655175}.

Solanum pimpinellifolium (Currant tomato) (Lycopersicon pimpinellifolium)

A0A1D8PCL1

HGT1_CANAL

MSSKIERIFSGPALKINTYLDKLPKIYNVFFIASISTIAGMMFGFDISSMSAFIGAEHYMRYFNSPGSDIQGFITSSMALGSFFGSIASSFVSEPFGRRLSLLTCAFFWMVGAAIQSSVQNRAQLIIGRIISGIGVGFGSAVAPVYGAELAPRKIRGLIGGMFQFFVTLGIMIMFYLSFGLGHINGVASFRIAWGLQIVPGLCLFLGCFFIPESPRWLAKQGQWEAAEEIVAKIQAHGDRENPDVLIEISEIKDQLLLEESSKQIGYATLFTKKYIQRTFTAIFAQIWQQLTGMNVMMYYIVYIFQMAGYSGNSNLVASSIQYVINTCVTVPALYFIDKVGRRPLLIGGATMMMAFQFGLAGILGQYSIPWPDSGNDSVNIRIPEDNKSASKGAIACCYLFVASFAFTWGVGIWVYCAEIWGDNRVAQRGNAISTSANWILNFAIAMYTPTGFKNISWKTYIIYGVFCFAMATHVYFGFPETKGKRLEEIGQMWEERVPAWRSRSWQPTVPIASDAELARKMEVEHEEDKLMNEDSNSESRENQA

carbohydrate transport [GO:0008643]; cellular response to heat [GO:0034605]; cellular response to neutral pH [GO:0036244]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to heat [GO:0036168]; filamentous growth of a population of unicellular organisms in response to neutral pH [GO:0036178]; glucose transmembrane transport [GO:1904659]; negative regulation of complement activation [GO:0045916]

extracellular vesicle [GO:1903561]; membrane [GO:0016020]; plasma membrane [GO:0005886]

carbohydrate:proton symporter activity [GO:0005351]; glucose transmembrane transporter activity [GO:0005355]

PF00083;

1.20.1250.20;

Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.

FUNCTION: High-affinity glucose transporter (PubMed:10612724, PubMed:12187386). Acts as a multifunctional complement-evasion molecule that causes down-regulation of complement activation by acquisition of human complement factors FH and C4BP (PubMed:21844307). Functions also as a human immunodeficiency virus (HIV) receptor via binding the viral gp160 protein (PubMed:21844307). Modulates hyphae formation (PubMed:21844307). {ECO:0000269|PubMed:10612724, ECO:0000269|PubMed:21844307, ECO:0000305|PubMed:12187386}.

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

A0A1D8PDV7

VPS34_CANAL

MATLSQPQSALPKTKIATTFGLSKDLKSPISVKVCYLECTRNNVSLVPLSTKFEDPTVFKKLSQIYKNSDLFVEIRVYDGKNNNLISTPVRTSYKAFNNKGRTWNQQLKLNIDYNQISIDAYLKFSICEIIDTKPSVFGVSYLSLFSHDSSTLRSGSHKIPVFMEDDPQYSKNIQYGTLIGLTDLEKRLIDYENGKYPRLNWLDKMVLPKVDATFLKTNNKDHDYYLYIELPQFEFPIVYSDIIYQIPTIEPITETTSKIPPDDTLNSNIIINSIDIPMATSHDPSIMKVYDPDFHITANNHLNPNATTFDPVELKYRKLERNIDNNTILDKELKPTPQLRDELLRIMIKPSNAELTDNEKNLIWKFRYYFSKNNSGNDPSNKSVKSFLPKFLRSINWENDYELDHTFKEIIPFYWNVDKLQIGDALELLGDYFNPYTLGKPTYQDDSMTSKSSKMKSDEKRFIKIYNNVCFLRKLAVERLKLANSEELLLYLLQLVQALKYEALIYEKSPPFCERSDQIEDNASSTLKSPLADFLIERAVENEKLGNFFYWYVKVENEDQLNNPHIDGPIKIYMDILNRYIELLKAHCHENRLPYYKHLKHQIWFIKKLTSLVELLRASFKKNEATAKKVEYLREYLANSGNELLKFPEPFPLPLDPSVMICGCYPEESSVFKSSLAPLKITLKTIEKKKHGHATSQLFGKRSRYGKYPLMFKIGDDLRQDQLVIQIIDLMDQLLKNENLDLKLTPYKILATSPISGLIQFVPNETLDSILSKTYPTSVTYSGGGETSDVPPSVSNNGILNYLRLHSQEQQSEEPISKSILSTNTSQSNTEIPVLPRQPKPTITSDLGVSPILMDNYVKSCAGYCVITYILGVGDRHLDNLLLSPNGKFWHADFGYILGRDPKPFPPLMKLPIQVIDGMGGLHHENYNVFKSYCFITYTTLRKNSNLILNLFQLMLDANIPDIQFDPSRVIEKVQEKFCLQMTEEEAILHFQNLINDSVNAFLPVVIDRLHSLAQYWRA

2.7.1.137

ascospore-type prospore membrane formation [GO:0032120]; autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cellular response to osmotic stress [GO:0071470]; cellular response to starvation [GO:0009267]; endocytosis [GO:0006897]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; nuclear division [GO:0000280]; nuclear migration along microtubule [GO:0030473]; pexophagy [GO:0000425]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; vacuolar protein processing [GO:0006624]; vacuolar transport [GO:0007034]; vacuole organization [GO:0007033]; vesicle-mediated transport [GO:0016192]

cytoplasm [GO:0005737]; endosome [GO:0005768]; endosome membrane [GO:0010008]; fungal-type vacuole membrane [GO:0000329]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleus-vacuole junction [GO:0071561]; peroxisome [GO:0005777]; phagophore assembly site [GO:0000407]; phosphatidylinositol 3-kinase complex, class III, type I [GO:0034271]; phosphatidylinositol 3-kinase complex, class III, type II [GO:0034272]

1-phosphatidylinositol-3-kinase activity [GO:0016303]; ATP binding [GO:0005524]; protein kinase activity [GO:0004672]

PF00454;PF00792;PF00613;

2.60.40.150;1.10.1070.11;1.25.40.70;

PI3/PI4-kinase family

PTM: Autophosphorylated. {ECO:0000269|PubMed:15632428}.

SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P22543}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22543}. Endosome membrane {ECO:0000250|UniProtKB:P22543}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22543}.

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000269|PubMed:10870104, ECO:0000269|PubMed:15632428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; Evidence={ECO:0000269|PubMed:10870104, ECO:0000269|PubMed:15632428};

FUNCTION: Multifunctional phosphatidylinositol 3-kinase involved in acidification of vacuoles, pH-dependent cell growth, and autophagocytosis (PubMed:15632428, PubMed:15861817). Plays an important role in protein transport and virulence (PubMed:11223944, PubMed:15632428). Component of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure (By similarity). Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II (By similarity). This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes) (By similarity). Finally, it might also be involved in ethanol tolerance and cell wall integrity (By similarity). {ECO:0000250|UniProtKB:P22543, ECO:0000269|PubMed:11223944, ECO:0000269|PubMed:15632428, ECO:0000269|PubMed:15861817}.

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

A0A1D8PFP2

ROB1_CANAL

MTPSSTKKIKQRRSTSCTVCRTIKRKCDGNTPCSNCLKRNQECIYPDVDKRKKRYSIEYITNLENTNQQLHDQLQSLIDLKDNPYQLHLKITEILESSSSFLDNSETKSDSSLGSPELSKSEASLANSFTLGGELVVSSREQGANFHVHLNQQQQQQQPSPQSLSQSSASEVSTRSSPASPNSTISLAPQILRIPSRPFQQQTRQNLLRQSDLPLHYPISGKTSGPNASNITGSIASTISGSRKSSISVDISPPPSLPVFPTSGPTLPTLLPEPLPRNDFDFAPKFFPAPGGKSNMAFGATTVYDADESMVMNVNQIEERWGTGIKLAKLRNVPNIQNRSSSSSSTLIKVNKRTIEEVIKMITNSKAKKYFALAFKYFDRPILCYLIPRGKVIKLYEEICAHKNDLATVEDILGLYPTNQFISIELIAALIASGALYDDNIDCVREYLTLSKTEMFINNSGCLVFNESSYPKLQAMLVCALLELGLGELTTAWELSGIALRMGIDLGFDSFIYDDSDKEIDNLRNLVFWGSYIIDKYAGLIFGRITMLYVDNSVPLIFLPNRQGKLPCLAQLIIDTQPMISSIYETIPETKNDPEMSKKIFLERYNLLQGYNKSLGAWKRGLSREYFWNKSILINTITDESVDHSLKIAYYLIFLIMNKPFLKLPIGSDIDTFIEIVDEMEIIMRYIPDDKHLLNLVVYYALVLMIQSLVAQVSYTNANNYTQNSKFMNQLLFFIDRMGEVLRVDIWLICKKVHSNFQQKVEYLEKLMLDLTEKMEQRRRDEENLMMQQEEFYAQQQQQQQQQQQQPKHEYHDHQQEQEQQEQLQEEHSEKDIKIEIKDEPQPQEEHIHQDYPMKEEEENLNQLSEPQTNEEDNPAEDMLQNEQFMRMVDILFIRGIENDQEEGEEQQQQQQQQEQVQQEQVQQEQVQQDQMELEEDELPQQMPTSPEQPDEPEIPQLPEILDPTFFNSIVDNNGSTFNNIFSFDTEGFRL

DNA-templated transcription [GO:0006351]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:1900445]; regulation of single-species biofilm formation on inanimate substrate [GO:1900231]; regulation of transcription by RNA polymerase II [GO:0006357]; single-species biofilm formation on inanimate substrate [GO:0044011]

chromatin [GO:0000785]; nucleus [GO:0005634]

DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270]

PF04082;PF00172;

4.10.240.10;

SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.

FUNCTION: Transcription factor that mediates conventional biofilm formation and plays a key role in microcolony formation under both flow and static conditions and to epithelial surfaces (PubMed:22265407, PubMed:23637598, PubMed:28793308, PubMed:30252918, PubMed:36847358). Modulates infection of mammalian hosts (PubMed:25693184, PubMed:34408988, PubMed:36847358). {ECO:0000269|PubMed:22265407, ECO:0000269|PubMed:23637598, ECO:0000269|PubMed:25693184, ECO:0000269|PubMed:28793308, ECO:0000269|PubMed:30252918, ECO:0000269|PubMed:34408988, ECO:0000269|PubMed:36847358}.

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

A0A1D8PHA3

CYT1_CANAL

MFRTAYKTMNQSMVQKFIAGGVGVTGLTASYLLYQDSMTADAMTAAEHGLHPPAYNWPHNGMFETFDHASIRRGFQVYREVCAACHSLDRIAWRNLVGVSHTTSEAKAMAEELEYDDEPDDEGKPRKRPGKLADYIPGPYENEQAARAANQGAYPPDLSLIVKARHGGSDYIFSLLTGYPDEPPAGVVLPEGSNYNPYFPGGAIAMGRVLFDDLVEYEDGTPATTSQMAKDVSTFLNWASEPEHDDRKKWGLKALVVLSSLYLLSIWVKRFKWTPIKNRKFRFDPPKK

7.1.1.8

COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000250|UniProtKB:P07143}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000250|UniProtKB:P07143};

mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]

mitochondrial respiratory chain complex III [GO:0005750]; plasma membrane [GO:0005886]

electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121]

PF02167;

1.10.760.10;1.20.5.100;

Cytochrome c family

SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07143}; Multi-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000250|UniProtKB:P07143};

FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation (PubMed:34525326, PubMed:36923588). The complex plays an important role in the uptake of multiple carbon sources present in different host niches (PubMed:36923588). {ECO:0000269|PubMed:34525326, ECO:0000269|PubMed:36923588}.

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

A0A1D8PJA8

TOS1_CANAL

MKFSSTTLLAGLSSLTATVSAGCSFEGGNYYCSETKKVIYKGIGFSGTYMDVTNMDESTGKCTQQSYSFSGNLSPLDEELSVHFRGPLTLLQFGVYYPSSSGNSKRQIDDQDCNVKHVHHKHKRATEVVQVTQTVFVDGNGNTVTSQALQTSTVESSPAVSSAAADDNANSGSGSGSSAGSGSGYGSVSALDGEGKAYRSDISTKSAPTSTSAQPSSSETASVDGAWTRDSYYTPGSTDNCVFLNYHGGSGSGVWSAKFGNSLSYANADNSGGSSTPVPLEETTIKSGEEYIIFSGSKCGSSSDCGYYRKGTVAYHGFKGASKIFVFEFEMPSDTNGNGYNQDMPAVWLLNAKIPRTLQYGEATCSCWKTGCGELDLFEVLSSGSNKMISHLHDGQGSSQNSNNGGGGSQDYFERPTSGTFKGVVIFEGDEIHILQVDDETEFGSSLDEETVNAWLKEAGSVATIGY

3.2.1.39

cell wall organization [GO:0071555]; metabolic process [GO:0008152]

cell surface [GO:0009986]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; hyphal cell wall [GO:0030446]

hydrolase activity, acting on glycosyl bonds [GO:0016798]

PF10287;PF10290;

2.60.120.200;

PGA52 family

PTM: Cleaved by KEX2 in vitro. {ECO:0000269|PubMed:18625069}.

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26453650, ECO:0000303|PubMed:17905924}.

CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000250|UniProtKB:P38288};

FUNCTION: Probable circularly permuted 1,3-beta-glucanase involved in cell wall modification through beta-1,3-glucan network alterations such as increased branching or remodeling (By similarity). Plays a role in engulfment by host macrophages (PubMed:26087349). {ECO:0000250|UniProtKB:P38288, ECO:0000269|PubMed:26087349}.

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

A0A1D8PJX3

RIP1_CANAL

MSSLAFRTLRNGLGLKSSVRALSTTTTTLSNYQQPDYSSYLNNKSGQGSRNFTYFMVGSMGLLSAAGAKSTVEAFLSSFAASADVLAMAKVEVKLGAIPEGKNVIIKWQGKPVFIRHRTADEIEEANQVDIKTLRDPQNDADRVKKPEWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPEYDFTDDETLLVG

7.1.1.8

COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628};

mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]

mitochondrial respiratory chain complex III [GO:0005750]; plasma membrane [GO:0005886]

2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; ubiquinol-cytochrome-c reductase activity [GO:0008121]

PF00355;PF02921;

2.102.10.10;1.20.5.270;

Rieske iron-sulfur protein family

SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P08067}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08067}.

CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000250|UniProtKB:P08067, ECO:0000255|RuleBase:RU004494};

FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation (PubMed:34525326, PubMed:36923588). The complex plays an important role in the uptake of multiple carbon sources present in different host niches (PubMed:36923588). {ECO:0000269|PubMed:34525326, ECO:0000269|PubMed:36923588}.

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

A0A1D8PN96

TAC1_CANAL

MDTSSSSGTHPSTFNNLTKQQELTGNDPNDTNRKRIRVACDSCRRKKIKCNGSYPCGNCIQAKNTSNCHFTERPVRKKLKPTKQDNKSTANSNGVSKRKYNDTFSGNSINIKTEKQENTTFGINDNKSSDLESRLSRIENSMSRMMHTLENFSQNFMTQAIRNNHSNSSMFNNNSLSPTPSEDFNKSAFDSEEQQTSHSYKNLKDRVKDANELLKLRNWDEFVGTHSITCIFSRESLDWMEKTLGSYGEEYLTPIRNLPLVFHSELKPYIMKWIDPPVVDKLQRKKLLESPFPTDSKLISKLIDLYYEETSMINILVDESRVRSLFAAYYNNFAEPIATKRRRFKLSELLLMTSILLISLSCLTEDDFSEERITTPASSTSSNYSAASANLLGDYNKNRLIALQNSLENSAIFYYHRISVISEGLETVEALLMFIIYVESNWLTSFFNYTIITVTIRFAQEIGLHRAETYNNLDLEEATKRRKIWWFCYFFDIEFSFKSGKPPVINTNDVTTNSDEDLLRVITQLKQYGPLSPKDRMYSPVCHTISTSLLDLSGSDSICLDILKIIQSGDILDDPFYFQFCALLQSRIRSNSYHDLFIASAEKRDFSSISNTLEKLNADMFELAMYLADEAKPRFYNDPKFTSVQASTGTSIRRDTILAMKLTFFSHLMIINRYPLMIATEDSKFDDRVIKFRNLSLDSARTILMLIKGWHRESASALFYNWAIYFPVAAYLVLVAAIINHPQLPESGTNLNLLIETSLSFFKSSKQWNSSNDSQDKQQNSTICVNKIVAIELIVRLMLRVVIKVYELHNNVEILANNPALQNHLQEAEEKFPDIFQNHAEFTSKMIALVGASPFGGCGSRNTSSCNLRDNSTNHGQNNMNPSPTITNNTYNSNINTGSNSTGEPQVCYAQSPSYNASLSNIINNESTGRSPATSTSINQSMMNENYDLFNDYLIDNSAVNLPFSQFNNLPNFFFDNNLGI

cellular response to oxidative stress [GO:0034599]; cellular response to steroid hormone stimulus [GO:0071383]; DNA-templated transcription [GO:0006351]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:1900445]; regulation of transcription by RNA polymerase II [GO:0006357]

nucleus [GO:0005634]; transcription regulator complex [GO:0005667]

DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; transcription coactivator activity [GO:0003713]; zinc ion binding [GO:0008270]

PF04082;PF00172;

4.10.240.10;

PTM: Phosphorylated (PubMed:30104273). Phosphorylation leads to hyperactivation (PubMed:30104273). {ECO:0000269|PubMed:30104273}.

SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:15590837, ECO:0000269|PubMed:19561319}.

FUNCTION: Transcriptional activator of drug-responsive genes including the ABC-type transporters CDR1 and CDR2, as well as HSP12 and RTA3 (PubMed:15590837, PubMed:17905926, PubMed:19561319, PubMed:30104273). Binds the cis-acting regulatory drug-responsive elements (DREs) with the consensus sequence 5'-CGGAWATCGGATATTTTTTT-3' in the promoters of target genes (PubMed:15590837, PubMed:19561319). {ECO:0000269|PubMed:15590837, ECO:0000269|PubMed:17905926, ECO:0000269|PubMed:19561319, ECO:0000269|PubMed:30104273}.

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

A0A1D8PNR5

DUR31_CANAL

MAQLSSQGNNAIIYLSYAFMLATGLFLAWKFSSNKDFLSSNGTQRGIPLALNFVASAMGVGIITTYAQIANIAGLHGLLVYTICGAIPIVGFAVVGPVIRRKCPDGFILTEWVRHRFGMVTALYLSAFTCLTMFLFMVGELSAIRSAIETLTGLNALGAVIVECVVTTIYTFFGGFRVSFITDNFQGVCVLLLLIICAAGMGSYIEIDTSKIGPSGLLKANKLGWQLVYILFVAIVTNDCFMSGFWLRTFASKTDKDLWIGTSIAAFVTFAICTLIGTTGFLAVWSGDLIVGDENGYDAFFILLSKMPRWLVAFVLIFCIVLSTCTFDSLQSAMVSTISNDVFRNKLHINYVRIMLILIMVPIVVLAVKVADNILQIYLIADLVSAAIIPSVFLGLADTWFWYLRGFDVMAGGLGALLGVFIFGTVYYHSAREGGKLLLIWNGLYDSSDWGPFGAFVIAPVGGVIITLASAALRIAVLYAYSKVTGKEFTALDKPVTVEVENQDHTYGSIDDDESDTKKVV

cellular response to metal ion [GO:0071248]; cellular response to starvation [GO:0009267]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; intracellular pH elevation [GO:0051454]; spermidine transport [GO:0015848]; transmembrane transport [GO:0055085]

membrane [GO:0016020]

spermidine transmembrane transporter activity [GO:0015606]

PF00474;

1.20.1730.10;

Sodium:solute symporter (SSF) (TC 2.A.21) family

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=spermidine(in) = spermidine(out); Xref=Rhea:RHEA:35039, ChEBI:CHEBI:57834; Evidence={ECO:0000269|PubMed:22033918}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35041; Evidence={ECO:0000269|PubMed:22033918};

FUNCTION: Spermidine transporter that is also used by salivary gland-secreted histatin 5 (Hst 5) to enter into candidal cells (PubMed:22033918, PubMed:23613860, PubMed:24247141). A major component of host nonimmune defense systems is salivary histatins, a family of small (3-4 kDa), histidine-rich, cationic proteins secreted by major salivary glands in humans and higher primates. Hst 5 is the most potent of the 12 histatin family members and has fungicidal activity against blastoconidial and filamentous forms of Candida albicans (PubMed:22033918). DUR31 only functions under high concentrations of Hst 5 (PubMed:22033918). Hst 5 cojugates to spermidine to be uptaken by DUR31 (PubMed:24247141). {ECO:0000269|PubMed:22033918, ECO:0000269|PubMed:23613860, ECO:0000269|PubMed:24247141}.

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

A0A1D8PPK1

EBP1_CANAL

MTIESTNSFVVPSDTELIDVTPLGSTKLFQPIKVGNNVLPQRIAYVPTTRFRASKDHIPSDLQLNYYNARSQYPGTLIITEATFASERGGIDLHVPGIYNDAQAKSWKKINEAIHGNGSFSSVQLWYLGRVANAKDLKDSGLPLIAPSAVYWDENSEKLAKEAGNELRALTEEEIDHIVEVEYPNAAKHALEAGFDYVEIHGAHGYLLDQFLNLASNKRTDKYGCGSIENRARLLLRVVDKLIEVVGANRLALRLSPWASFQGMEIEGEEIHSYILQQLQQRADNGQQLAYISLVEPRVTGIYDVSLKDQQGRSNEFAYKIWKGNFIRAGNYTYDAPEFKTLINDLKNDRTIIGFSRFFTSNPDLVEKLKLGKPLNYYNREEFYKYYNYGYNSYDESEKQVIGKPLA

1.6.99.1

COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q02899};

steroid metabolic process [GO:0008202]

cell surface [GO:0009986]; cytosol [GO:0005829]; fungal-type vacuole [GO:0000324]; hyphal cell wall [GO:0030446]

estrogen binding [GO:0099130]; FMN binding [GO:0010181]; hormone binding [GO:0042562]; NADPH dehydrogenase activity [GO:0003959]; steroid binding [GO:0005496]

PF00724;

3.20.20.70;

NADH:flavin oxidoreductase/NADH oxidase family

CATALYTIC ACTIVITY: Reaction=A + H(+) + NADPH = AH2 + NADP(+); Xref=Rhea:RHEA:13149, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.99.1; Evidence={ECO:0000250|UniProtKB:P43084};

FUNCTION: Oxidoreductase that binds mammalian estrogens with high affinity. {ECO:0000250|UniProtKB:P43084}.

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

A0A1D8PQ86

ALS9_CANAL

MLPQFLLLLLYLTVSTAKTITGVFNSFDSLTWTRSVEYVYKGPETPTWTAVLGWSLNSTTADAGDTFTLIMPCVFKFITSQTSVDLTADGVSYATCDFNAGEEFTTFSSLSCTVNSVSVSYDKASGTVKLPITFNVGGTGSSVDLTDSKCFTAGKNTVTFMDGDTKISTTVDFDASPVSPSGYITSSRIIPSLNKASSLFVSPQCENGYTSGIMGFVTSQGATIDCSNINIGISKGLNDWNFPVSSESFTYTKTCSSSGIIVEYENVPAGYRPFVDAYISSENVEQYTLTYANEYTCKNGNTVVDPFTLTWWGYKNSEADSNGDIIVVTTKTVTASTTAVTTLPFNPTVDKTETIEVLQPIPTTTITTSYIGISTSYETFTATIGGTATVIVDTPYHITTTVTTFWTGSVTTTTTYSNPTGSIDTVIVQIPSPDPTTTITEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTPSVSSFESKTFYSSEAQSSLEIDSSNTFMTSISVSTASSYDESSTIVSSAFPTLHISSYSLSTSFVPPVTLPRYVNTTISSSPSFESSSMYSSVTSAVTSIDNDREVPTSTTTYLHSKLYSESISTVIQTKSSDWSLSLGNSNKPESASTVSEESLHYLSTPGPSSSEYSISFTSEKEGHVSSYVPRVSYTSSVKVSISSTMSSENGMSATHTFGISTNTIPSSTETSIKSATVTTPVSESTNTGMSIFMSTTTESKTTDITTETSVSGEVNLGSATVKVSSSEFISKGTVTRIMPTELTNSESTFTASPSFVLTSTESSVIETPATIEMSSRSSSYSVPLSKLRSEGETTRVIPTSSTATGSTVIGSPSSVSTSNESIITGSSSFVSTTAETISTRSIVTESIVAGSPSLVLTTTVLDTTETTITETSIVGESSSRSLTFKASSLSKGEITGTVTPEMSVSTSKATTGTTSEVSIKESLTTKVPTFTSTTIKPETSETQHSESRTTQIPYSETKGSQLSTANSQVSQTGSSKSSIFESAISKDESTFVSATVKSITTPAVTQYQTSLPNPAVSVSEESGKKSSIIESQTENSATQHSIYFDSIETSTLSNTLANTLVSGAMKNSETTSELTTSDKAIGFSTTTETSIPGATNSALSPSVDSGKSSMLGWSGGIVSTVSTSTRLEDSTATSSSITAANQDSLNPSTVSKYPHGSETIDNGSNGSSHSSSALASTISASHSIKFSAHQTTLSQSLISSSTKTVIASTYDGSGSVIKLHSWFYGLVTIFFLFI

cell adhesion [GO:0007155]; cell adhesion involved in multi-species biofilm formation [GO:0043710]; cell adhesion involved in single-species biofilm formation [GO:0043709]; cell-cell adhesion [GO:0098609]

extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]

cell adhesion molecule binding [GO:0050839]

PF05792;PF11766;

2.60.40.1280;2.60.40.2430;

ALS family

PTM: N-glycosylated and O-glycosylated.; PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. {ECO:0000305|PubMed:12845604}.

SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Secreted, cell wall. Note=Identified as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer. {ECO:0000305|PubMed:12845604}.

FUNCTION: Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections (PubMed:17510860, PubMed:22321066, PubMed:22429754). Allele ALS9-2 contributes to endothelial cell adhesion, whereas ALS9-1 does not (PubMed:17600078). {ECO:0000269|PubMed:17510860, ECO:0000269|PubMed:17600078, ECO:0000269|PubMed:22321066, ECO:0000269|PubMed:22429754}.

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

A0A1D8PQB9

ALS4_CANAL

MLLQFLLLSLCVSVATAKVITGIFDSFNSLTWTNAASYSYRGPANPTWTAVIGWSLDGATASAGDTFTLDMPCVFKFITDQTSIDLVADGRTYATCNLNSAEEFTTFSSVSCTVTTTMTADTKAIGTVTLPFSFSVGGSGSDVDLANSQCFTAGINTVTFNDGDTSISTTVDFEKSTVASSDRILLSRILPSLSQAVSLFLPQECANGYTSGTMGFSTAGTGATIDCSTVHVGISNGLNDWNYPISSESFSYTKTCTSTSVLVTYQNVPAGYRPFVDAYVSATRVSSYAMRYTNIYACVGAASVDDSFTHTWSGYSNSQAGSNGITIVVTTRTVTDSTTAVTTLPFNSESDKTKTIEILQPIPTTTITTSYVGVTTSYSTKTAPIGETATVIVDVPYHTTTTVTSEWTGTITTTTTRTNPTDSIDTVVVQVPSPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNPTVTTTEYWSQSYATTTTVTSPPGGTDIVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNPTVTTTEYWSQSYATTTTVTSPPGGTDIVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPSPTVTTTEYWSQSYATTTTVTAPPGGTATVIIKEPPNYTVTTTEYWSQSYATTTTITAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPSPTVTTTEYWSQSYATTTTVTAPPGGTATVIIREPPNYTVTTTEYWSQSYATTTTITAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNPTVTTTEYWSQSYATTLTITAPPGGTNSVIIRVHSSTNDESSESTFSTLSVPSFSGSISIVSTVSRPHYVNSTVTHLPSSSSKPVDIPSSDVVTSTNDNSLTSLTGSENGKTSVAISTTFCDDENGCQTSIPQGSVVRTTATTTATTTTIIGDNNGSGKSKSGELSSTGSVTTNTATPDVPSTKVPSNPGAPGTGVPPPLAPSTETQTTNNVPGSPNIPATGTTDIIRESTTVSHTVTGNGNTGVPMNPNPVLTTSTSLTGATNSATNPSHETSVNTGSGGSTNIVTPPSSATATVVIPGTDNGATTKGQDTAGGGNSNGSTATTNIQGGNNEPGNQPGTNTTGEPVGTTDTQSVESISQPTTLSQQTTSSLISTPLASTFDGSGSIVQHSGWLYVLLTAISIFF

adhesion of symbiont to host [GO:0044406]; cell adhesion involved in multi-species biofilm formation [GO:0043710]; cell adhesion involved in single-species biofilm formation [GO:0043709]; cell-cell adhesion [GO:0098609]; cellular response to temperature stimulus [GO:0071502]; hyphal growth [GO:0030448]

extracellular region [GO:0005576]; extracellular vesicle [GO:1903561]; fungal-type cell wall [GO:0009277]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; yeast-form cell wall [GO:0030445]

cell adhesion molecule binding [GO:0050839]

PF05792;PF11766;

2.60.40.1280;2.60.40.2430;

ALS family

PTM: N-glycosylated and O-glycosylated. {ECO:0000305}.; PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. {ECO:0000305|PubMed:12845604}.

SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:12845604}. Secreted, cell wall {ECO:0000269|PubMed:22106872}. Note=Identified as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer (Probable). Covers the surface of yeast-form cells (PubMed:22106872). {ECO:0000269|PubMed:22106872, ECO:0000305|PubMed:12845604}.

FUNCTION: Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections. {ECO:0000269|PubMed:22321066, ECO:0000269|PubMed:22429754}.

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

A0A1D8PS71

PHYA_CANAL

MVSVSKLINNGLLLTSQSVFQDVATPQQASVQQYNILNFLGGSAPYIQRNGYGISTDIPAGCEIAQIQLYSRHGERYPSKSNGKSLEAIYAKFKNYNGTFKGDLSFLNDYTYFVKDQSNYAKETSPKNSEGTYAGTTNALRHGAAFRAKYGSLYKENSTLPIFTSNSNRVHETSKYFARGFLGDDYEEGKTVKFNIISEDADVGANSLTPRSACSKNKESSSSTAKKYNTTYLNAIAERLVKPNPGLNLTTSDVNNLFSWCAYEINVRGSSPFCDLFTNEEFIKNSYGNDLSKYYSNGAGNNYTRIIGSVILNSSLELLKDTENSNQVWLSFAHDTDLEIFHSALGLLEPAEDLPTSYIPFPNPYVHSSIVPQGARIYTEKLQCGNDAYVRYIINDAVVPIPKCATGPGFSCKLDDFENFVKERIGDVDFIKQCGVNSTYPSELTFYWDYKNVTYNAPLEL

3.1.3.-; 3.1.3.8

hyphal growth [GO:0030448]

cell surface [GO:0009986]; cell wall-bounded periplasmic space [GO:0030287]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]

4-phytase activity [GO:0008707]; acid phosphatase activity [GO:0003993]

PF00328;

3.40.50.1240;

Histidine acid phosphatase family

SUBCELLULAR LOCATION: Secreted {ECO:0000305}.

CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:58130; EC=3.1.3.8; Evidence={ECO:0000269|PubMed:29216308}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990; Evidence={ECO:0000269|PubMed:29216308}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:195535; Evidence={ECO:0000250|UniProtKB:P34752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116; Evidence={ECO:0000250|UniProtKB:P34752}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535, ChEBI:CHEBI:195537; Evidence={ECO:0000250|UniProtKB:P34752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120; Evidence={ECO:0000250|UniProtKB:P34752}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol 1,2-bisphosphate + phosphate; Xref=Rhea:RHEA:77131, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195537, ChEBI:CHEBI:195539; Evidence={ECO:0000250|UniProtKB:P34752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132; Evidence={ECO:0000250|UniProtKB:P34752}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate; Xref=Rhea:RHEA:77135, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195539; Evidence={ECO:0000250|UniProtKB:P34752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136; Evidence={ECO:0000250|UniProtKB:P34752};

FUNCTION: Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate (PubMed:29216308). Myo-inositol 2-monophosphate is the end product (By similarity). Responsible of about 25% of the phytase activity (PubMed:29216308). The residual phytase activity might be contributed by other cytosolic or cellular enzymes such as acid phosphatase that also degraded the substrate phytate (PubMed:29216308). Is essential for human tissue damage during infection (PubMed:29216308). {ECO:0000250|UniProtKB:P34752, ECO:0000269|PubMed:29216308}.

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)