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A0A1D8PT03

YCP4_CANAL

MKIAIIQYSTYGHITQLAKAVQKGVADAGYKADIFQVPETLPQEVLDKMHAPAKPTDIPIATNDTLTEYDAFLFGVPTRYGTAPAQFFEFWGATGGLWANGSLAGKPAGVFVSTSGQGGGQETTVRNFLNFLAHHGMPYIPLGYANAFALQSSMEEVHGGSPYGAGTFANVDGSRQPSTLELEIAEKQGEAFVKSATKLVKGSKKTNTTTTSKSAATSDAAGTTSGTAAGTSAATGAATGTSAPKESTKEASSSAKKEATNGTATRTQQSTKAPETAEKSSCSKCIIM

1.6.5.2

COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|PROSITE-ProRule:PRU00088};

cellular response to oxidative stress [GO:0034599]

eisosome [GO:0032126]; fungal biofilm matrix [GO:0062040]; membrane [GO:0016020]; plasma membrane [GO:0005886]

FMN binding [GO:0010181]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955]

PF03358;

3.40.50.360;

WrbA family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26325183}; Peripheral membrane protein {ECO:0000269|PubMed:26325183}.

CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2; Evidence={ECO:0000305|PubMed:26325183}; CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+); Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2; Evidence={ECO:0000305|PubMed:26325183};

FUNCTION: Flavodoxin-like protein (FLP) that plays a role in cell wall integrity, oxidative stress protection and virulence (PubMed:26087349, PubMed:26325183). FLPs act as NAD(P)H quinone oxidoreductases (PubMed:26325183). Reduces ubiquinone (coenzyme Q), enabling it to serve as an antioxidant in the membrane (PubMed:26325183). {ECO:0000269|PubMed:26087349, ECO:0000269|PubMed:26325183}.

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

A0A1D8PTL7

TRK1_CANAL

MLYRVSGFYKRHTRNFTNIDYGYYIRNFIHHIASKIYPYAKVVLPNFRAAHYFYILTLVILGSILVYPVKTCAYIDVLFFTAGASTQAGLNTVNVNDLSLYQQIVLYLLATLATPIFIHGSLLFVRLYYFERHFDNIKERSLMDYRMRKSATLARLGSAPTMSSTRLNTFNNQVLGFQEREAEKGSSSSPQSSSSQTSQPVSTAYNDQGGNDIEHHSEPSDSDDDESGNGPVTFQEKIHFEEPQRPRSQRRHSRTDSGIKFSALPHPRRRKSIDPEDMYRSINMLQEHKKNQEAKSKGIQFLNIGSPVRRKSRSSNIEAFPEEDTNPSRGDEITPATNSVGTGNNDEDEDDILIIKPPIEIENSDEANPIFTKKKKLASQIQFKETPGKAKKWITTKTRKHYNPWTSKLKKTLSNSSKKGSLSVVPTDTEDDSEDEEYASIDSETSDISDNEHAADNAEGSDVDSVGSYEEDEDEDEHNSDDDDDGEGERRLGNGASLTKAQSHLVLPSKDETGGKKYTKRSNTLDTPQQNTSDGRKIRKKAPKRKTPRTQRNASFNQHSNVSIGDGSIENVDTNDSYQRLSRTMSGNYLSWTPTVGRNSTFIKLTDEQKEELGGIEYRAVKLLIKIIVVYYVGFNIIPGVMLSIWIYCMPHYKNLMISSSISPAWWAFFTSQSSFNDLGLTLTSNSMMSFNQNAFVQILCSFLIVIGNTGFPILLRFIIWVMFKTARPLSLYKESLGFLLDHPRRCFTLLFPSVPTWWLFFILVVLNGFDLVIFCILDLHDDTFKGVDMGYRVLNGLFQAFCTRTVGFSVMDLSQLHAATQVSYLIMMYISVLPIAISVRRTNVYEEQSLGVYAKENAEGVDESAPSNYVGSHLRNQLSYDLWYICLGLFIICIAEGKRLKEQDLRFSIFAVLFEIVSAYGTVGMSMGYPGVDCSLSGEFNVISKLVIIAMMIRGRHRGLPYTIDRAIMLPNAAMKRHDRLQEEHAINRHNTMERTTTLGRVATFGNGPIDGGNNLLTRAITNIEHRLRNRRDGRSESSTVSEDPRYVVRTVSEV

chloride transport [GO:0006821]; intracellular potassium ion homeostasis [GO:0030007]; potassium ion import across plasma membrane [GO:1990573]; response to toxic substance [GO:0009636]

chloride channel complex [GO:0034707]; membrane [GO:0016020]; plasma membrane [GO:0005886]

chloride channel activity [GO:0005254]; chloride transmembrane transporter activity [GO:0015108]; high-affinity potassium ion transmembrane transporter activity [GO:0140107]; potassium ion transmembrane transporter activity [GO:0015079]

PF02386;

TrkH potassium transport family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19175416}; Multi-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:15485849, ECO:0000269|PubMed:19175416, ECO:0000269|PubMed:33069635}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29465; Evidence={ECO:0000269|PubMed:15485849, ECO:0000269|PubMed:19175416, ECO:0000269|PubMed:33069635}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:15485849, ECO:0000269|PubMed:19175416}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29824; Evidence={ECO:0000269|PubMed:15485849, ECO:0000269|PubMed:19175416};

FUNCTION: Potassium transporter that mediates K(+) influx, as well as Cl(-) efflux as a secondary function (PubMed:15485849, PubMed:19175416, PubMed:33069635). TRK1 is the major K(+) uptake transporter that regulates membrane potential and intracellular pH (PubMed:33069635). The TRK1-mediated Cl(-) efflux should serve as a Cl(-) detoxification route and may play a role in sustaining C.albicans on mammalian epithelial surfaces, or in physiological saline solutions such as saliva (PubMed:19175416). {ECO:0000269|PubMed:15485849, ECO:0000269|PubMed:19175416, ECO:0000269|PubMed:33069635}.; FUNCTION: Mediates candidacidal activities of cysteine-free peptides, but not of defensins (PubMed:16377704). The hallmark of salivary gland-secreted histatin-5 (Hst 5) killing of C.albicans is the rapid efflux of cellular ATP and other small nucleotides and ions from the cell as well as concurrent intracellular uptake of propidium iodide (PI) (PubMed:16377704). TRK1 is the channel for Hst 5-induced killing and histatin-5 may directly or indirectly alter TRK1 function, allowing the efflux of larger anions, including ATP, and the influx of small cationic dyes, such as PI (PubMed:15485849, PubMed:16377704). {ECO:0000269|PubMed:15485849, ECO:0000269|PubMed:16377704}.

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

A0A1D9BZF0

GCNA_MOUSE

MDSGSSSSSSSSGSSSGSCSTSGSGSTSGSSTTSSSSSSSSSSSSSSSSSSKEYMPELPKQRKASCVVIDSESDSDNTSDEKNTTVCEISSGDETSDIDRPGGQKLPLIVIDDDDDGSPDLKNTKQKSDEPQMSVLEKEGVECIGSDSTSPHDVCEIWDVCGSSNQTSSELEPEGEPESEAKGEPESEAKGEPESEAKGEPESEAKGESESEAKGEMETEAKGESESEAKGEMETEAKGESESEAKGEMETEAKGEPESEAKGEMETEAKGEPESEAKGEMETEAKGESESEAKGEMETEAKGESESEAKGEMETEAKGEPESEAKGEMETEAKGEPESEAKGEPEPEAAKGEMETEAAMGEVETEAAMGEPEQEITAEEAKKKRAAYLLAQQRKRKRKNRFICMSSSKPRRKRRRADPQDGADPQDGADPQDRADPQDLADPQDRGDSQDMPSLPGTSDEPIPSGQPVCPRKGMASSRGRGRGRGRGRGRGRGRGRGRGRGAKAGK

DNA damage response [GO:0006974]; DNA integrity checkpoint signaling [GO:0031570]; homologous chromosome pairing at meiosis [GO:0007129]; homologous recombination [GO:0035825]; meiotic chromosome condensation [GO:0010032]; protein-DNA covalent cross-linking repair [GO:0106300]

condensed chromosome [GO:0000793]; PML body [GO:0016605]

Serine-aspartate repeat-containing protein (SDr) family

SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:31839538}. Nucleus, PML body {ECO:0000269|PubMed:31839538}. Nucleus {ECO:0000269|PubMed:27718356}. Note=Co-localizes with SUMO2 at PML bodies in all interphase cells (By similarity). Localizes on condensed chromosomes in spermatocytes in G2 and M during meiotic prophase (PubMed:31839538). {ECO:0000250|UniProtKB:Q96QF7, ECO:0000269|PubMed:31839538}.

FUNCTION: May play a role in DNA-protein cross-links (DPCs) clearance through a SUMO-dependent recruitment to sites of DPCs, ensuring the genomic stability by protecting germ cells and early embryos from various sources of damage (PubMed:31839538). Can resolve the topoisomerase II (TOP2A) DPCs (PubMed:31839538). {ECO:0000269|PubMed:31839538}.

Mus musculus (Mouse)

A0A1E1FFL0

PRHA_PENBI

MAPMIPPRLQRFPATASADEIFAAFQEDGCVVIEGFISPEQVARFSQEVDPAMEKIPVEVTNNGNSNDRTKRFSKCVIASPTFRNEIIESDLMHELCDRVFSKPGEGMGYHFNDNMVIEVQPGAPAQRLHRDQELYPWWNSMGPAGPECVINFFCAVTPFTEENGATRLVPGSHLWPEFTQINERDCPQFGKIETVPAIMQPGDCYLMSGKVIHGAGHNATTTDRRRALALAIIRRELRPMQAFSLSVPMKLAREMSERSQTMFGFRSSVQHCDVDMVHFWGNDGKDIAHHLGLEAPSVHV

1.14.11.-

COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:Q4WAW9};

paraherquonin biosynthetic process [GO:0140874]

dioxygenase activity [GO:0051213]; metal ion binding [GO:0046872]

PF05721;

2.60.120.620;

PhyH family

CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + preaustinoid A1 = berkeleyone B + CO2 + H2O + succinate; Xref=Rhea:RHEA:65184, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:69025, ChEBI:CHEBI:69026; Evidence={ECO:0000269|PubMed:27602587, ECO:0000269|PubMed:29317628}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65185; Evidence={ECO:0000269|PubMed:27602587, ECO:0000269|PubMed:29317628}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + berkeleyone B + O2 = berkeleydione + CO2 + H2O + succinate; Xref=Rhea:RHEA:65188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:69021, ChEBI:CHEBI:69025; Evidence={ECO:0000269|PubMed:27602587}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65189; Evidence={ECO:0000269|PubMed:27602587}; CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + 2 O2 + preaustinoid A = berkeleytrione + 2 CO2 + H2O + 2 succinate; Xref=Rhea:RHEA:65192, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:69022, ChEBI:CHEBI:69023; Evidence={ECO:0000269|PubMed:27602587}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65193; Evidence={ECO:0000269|PubMed:27602587};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48.3 uM for preaustinoid A1 {ECO:0000269|PubMed:29317628};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:27602587, ECO:0000269|PubMed:29317628}.

FUNCTION: Multifunctional dioxygenase; part of the gene cluster that mediates the biosynthesis of paraherquonin, a meroterpenoid with a unique, highly congested hexacyclic molecular architecture (PubMed:27602587). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase prhL (By similarity). Synthesis of DMOA is followed by farnesylation by the prenyltransferase prhE, methylesterification by the methyl-transferase prhM, epoxidation of the prenyl chain by the flavin-dependent monooxygenase prhF, and cyclization of the farnesyl moiety by the terpene cyclase prhH, to yield the tetracyclic intermediate, protoaustinoid A (By similarity). The short chain dehydrogenase prhI then oxidizes the C-3 alcohol group of the terpene cyclase product to transform protoaustinoid A into protoaustinoid B (PubMed:27602587). The FAD-binding monooxygenase prhJ catalyzes the oxidation of protoaustinoid B into preaustinoid A which is further oxidized into preaustinoid A1 by FAD-binding monooxygenase phrK (PubMed:27602587). Finally, prhA leads to berkeleydione via the berkeleyone B intermediate (PubMed:27602587, PubMed:29317628). PrhA is a multifunctional dioxygenase that first desaturates at C5-C6 to form berkeleyone B, followed by rearrangement of the A/B-ring to form the cycloheptadiene moiety in berkeleydione (PubMed:27602587, PubMed:29317628). Berkeleydione serves as the key intermediate for the biosynthesis of paraherquonin as well as many other meroterpenoids (Probable). The cytochrome P450 monooxygenases prhB, prhD, and prhN, as well as the isomerase prhC, are probably involved in the late stage of paraherquonin biosynthesis, after the production of berkeleydione (Probable). Especially prhC might be a multifunctional enzyme that catalyzes the D-ring expansion via intramolecular methoxy rearrangement, as well as the hydrolysis of the expanded D-ring (Probable). {ECO:0000250|UniProtKB:Q5ATJ7, ECO:0000269|PubMed:27602587, ECO:0000269|PubMed:29317628, ECO:0000305|PubMed:27602587, ECO:0000305|PubMed:28759016, ECO:0000305|PubMed:29317628}.

Penicillium brasilianum

A0A1E3P8S6

EAT1_WICAA

MFFTKVLNNQVANGLKQLPVHKRVQMAYDLHIPNKTVNPNLNIRSHEPIVFVHGIFGSKKNYRHDCQKIANVTHTPVYTIDLRNHGQSMHALPFDYETLAQDVTDFCEDHGLKKVNLIGYSLGAKICMLTMLQNPDLVRSGVIIDNSPIEQPHIEIFLTQFIKSMLHVLNSTKIRADDKDWKSKANQAMRRYIPNGGIRDYLLANLINKVPKGYKSPVINYDDGYIHFQNPVRHMTEVAVKNVSAWPTEHVKGLKFEGQVRFLKGTKSAFIDEKGLEAIKEYFPNYSLSELNATHFILNERPQEYVKLICDFIKVNRYKSLQEHIRHVENFSSAELEARHNAEHERQMEELRQLTQTTPTAEQVKTIDNLASKVDLSATERQQQQNKEITV

2.3.1.268; 3.1.1.-; 3.1.2.1

cellular lipid metabolic process [GO:0044255]

mitochondrion [GO:0005739]

acetyl-CoA hydrolase activity [GO:0003986]; carboxylic ester hydrolase activity [GO:0052689]; transferase activity [GO:0016740]

PF00561;

3.40.50.1820;

AB hydrolase superfamily

SUBCELLULAR LOCATION: Mitochondrion.

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ethanol = CoA + ethyl acetate; Xref=Rhea:RHEA:55972, ChEBI:CHEBI:16236, ChEBI:CHEBI:27750, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.268; Evidence={ECO:0000269|PubMed:28356220}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1; Evidence={ECO:0000269|PubMed:28356220}; CATALYTIC ACTIVITY: Reaction=ethyl acetate + H2O = acetate + ethanol + H(+); Xref=Rhea:RHEA:58148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:27750, ChEBI:CHEBI:30089; Evidence={ECO:0000269|PubMed:28356220};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.12 mM for acetyl-CoA (for acetyl-CoA hydrolase reaction) {ECO:0000269|PubMed:28356220}; KM=2.43 mM for ethanol (for alcohol acetyltransferase reaction) {ECO:0000269|PubMed:28356220};

FUNCTION: Alcohol acetyltransferase that catalyzes the synthesis of ethyl acetate from ethanol and acetyl-CoA. Can also function as a thioesterase by hydrolyzing acetyl-CoA in the absence of ethanol, as well as esterase hydrolyzing ethyl acetate. {ECO:0000269|PubMed:28356220}.

Wickerhamomyces anomalus (strain ATCC 58044 / CBS 1984 / NCYC 433 / NRRL Y-366-8) (Yeast) (Hansenula anomala)

A0A1F4

EYS_DROME

MSNVHQFDTQTMAESPQIRRDMGRLCATWPSKDSEDGAGTALRAATPLTANGATTTGLSVTLAPKDMQRNHLLKMPTATIEKPTITATIASSSSTSTSTTRKSVTATRSLKLNPNILLPTLRILARGLLLPALILAILVGSSQAGFACLSNPCVFGVCIDGLNSSYSCYCIDGYTGIQCQTNWDECWSSPCQNGGTCVDGVAYYNCTCPEGFSGSNCEENVDECMSNPCQNGGLCRDRTNGYICTCQPGYLGSHCELDVAVCETGTGARCQHGGECIEGPGLEFTCDCPAGWHGRICQEEINECASSPCQNGGVCVDKLAAYACACPMGYTGINCEEEILICADNPCQNNALCLMEEGVPTCYCVPDYHGEKCEFQYDECQLGPRCMNGGVCIDGVDTFSCSCPPLLTGMLCECLMVGEESLDCNYTAPATQSPPRRTTTTSTMAPPTVRPVTPPETTVSPSRASEEVEIIVVTTSAPAEVVTSVLSPSSSSSSSEEGVSVEIKTPTVAPPESGSHSISVEQTTAVPAQPEPESEQEPESKPHPESESASESETETEEEIIPGTTARPPTSRSSSSSEESPSIFTTLPPLPGKPQTSASSESSGEVVTSEEYTTVPHFEVSGSKSESGSEEVTTVRPTAAPSITISVDITSSGSSSSSSESVEVFTTPAPVFVQRVTTIETSISIDYVTPTPLPETTTPRVVPVPRPTFAPEPPLDVVETTASTHHLWTEVPTTAAPFFTEYPAEVLITTHRTSAGRFTTVQPPAGVTTTSPTEDSSVELPTPHTPQIVVTILDSNEVIPSLITTTGSPTTHHHHHHHPHHEAEGTTLQPLEEDEHHHHHHHDEFTTPQPVEITTGHPLQTEDLIGVQEPAVVTTESPFAPAETTVVPVVVPATIAPLGTAAPPATPAPVPPATTTPPPSPPSLATETPTLPPTLPPVTLPPVTQPPPTIPPTPPSTQSAQTLPPPTSAINVYTTPDGPPTASQTKPSVTESSEEVEGTNTVSTGGRGSGGVPEEKAGDVDCIKLGCYNGGTCVTTSEGSRCVCRFDRQGPLCELPIIIRNAAFSGDSYVSHRIYKDIGGHESLDAVLPMHIQLKVRTRATNGLIMLAAAQGTKGGHYMALFLQKGLMQFQFSCGLQTMLLSELETPVNTGHEITIRAELDFSRNYTHCNASLLVNDTLAMSGDQPTWLKLLPPRLHTPEAILNTWLHLGGAPQAPIGLIIELPPAQSGSGFTGCLHTLRINGQAREIFGDALDGFGITECGSLACLSSPCRNGAACIKIETNDLDENGEKAEKWKCKCPTGYMGPTCEISVCEDNPCQYGGTCVQFPGSGYLCLCPLGKHGHYCEHNLEVALPSFSGSVNGLSSFVAYTVPIPLEYSLELSFKILPQTMSQISLLAFFGQSGYHDEKSDHLAVSFIQGYIMLTWNLGAGPRRIFTQKPIDFRLDAPRVPYEIKVGRIGRQAWLSVDGKFNITGRSPGSGSRMDVLPILYLGGHEIANFNTLPHDLPLHSGFQGCIYDVQLKAGQVTVPLQETRGVRGRGVGQCGTRECHRHACQHDGACLQHGATFTCICQEGWYGPLCAQPTNPCDSFNNKCYEDATCVPLVNGYECDCPVGRTGKNCEEVIRSLSDVSLTGRRSYLAVRWPYLYDGGDKLGAKRSQMVSYRNFTKKLMPPKPITTPSSHFVMKLLNEVEKQRSFSPVPLMGSKSFEEHHRVQFFFIEFQLRPLSERGLLLYFGTLNNNQDKKIGFVSLSLQGGVVEFRISGPSNHVTVVRSVRMLAIGEWHKIKMAQRGRWLTLWVEGSASSALAPSAEVLVEPDSLLYIGGLKDVSKLPHNAISGFPIPFRGCVRGLVVSGTRIVLNETNIVESRNIRDCDGTACGGDSCESGGHCWLDEKLQPHCICPEYAKGDRCEYSETCKLIPCKNNGRCLRSGRCSCPNGWGGFYCEIAMSKPTTPSFRGNSYLILPPPRIPMKDKRRGPSLYVRPREAIQVSLNFSTIEPDGLLLWSEHERSKFLGLGLEAGHLKLASNLLGSTNDTVRAPASGFIADGAWHWTSVLLDRSRLELQLDGEVIFTERLPEGGRSLGSTTPRSTLAGRRKNSSKEPTISYEDVFYLGGFPNSDSVSRRTKGRFFDPFKGCLQDIQFGAEPTAIISDFSTYQGENIGSCDLHGDEPLTV

cell morphogenesis [GO:0000902]; rhabdomere development [GO:0042052]; temperature compensation of the circadian clock [GO:0010378]

cell surface [GO:0009986]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; non-motile cilium [GO:0097730]

calcium ion binding [GO:0005509]; extracellular matrix structural constituent [GO:0005201]

PF00008;PF12661;PF02210;

2.60.120.200;2.10.25.10;

EYS family

SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:17011488, ECO:0000269|PubMed:17036004}. Note=Secreted by photoreceptor cells, through the stalk membrane into the interrhabdomeral space (IRS). Although secreted, lacks a canonical signal sequence and contains a predicted transmembrane domain. The discrepancy may be explained by protein cleavage after the transmembrane region.

FUNCTION: Essential for the formation of matrix-filled interrhabdomeral space: critical for the formation of epithelial lumina in the retina. Acts together with prominin (prom) and the cell adhesion molecule chaoptin (chp) to choreograph the partitioning of rhabdomeres into an open system. {ECO:0000269|PubMed:17011488, ECO:0000269|PubMed:17036004}.

Drosophila melanogaster (Fruit fly)

A0A1I9LM04

CNDD2_ARATH

MAPPFVFPQILRALEEDPEDNHRLFAQNPVDVTSLRPSDLEEFVKGVSFDLSDRELFCVEDQDVFDRVYSLVRSFFSLPPSCKCNLVESLRSNLSVLLPNVDSISRSVQDQEDDVPIIDRITSHRNALKIYTFFLLTVVMNEESHISSVETTKVAARGRKKQIIQSWNWEPQRGRMLNLIANSLEINLSLLFGSSDLDENYLSFIVKNSFTLFENATILKDAETKDALCRIIGASATKYHYIVQSCASIMHLIHKYDFAVVHIADAVARAESKYSDGTLAVTIIRDIGRTDPKAYVKDTAGADNVGRFLVELADRLPKLMSTNVGVLVPHFGGESYKIRNALVGVLGKLVAKAFNDVEGDMSSKSLRLRTKQAMLEILLERCRDVSAYTRSRVLQVWAELCEEHSVSIGLWNEVASLSAGRLEDKSAIVRKSALNLLIMMLQHNPFGPQLRIASFEATLEQYKRKLNELEPTEHASKESTSDGESCNGDGEIDDLHLETTTKIHQDSLSDSCQPENGEEISEKDVSVPDIGNVEQTKALIASLEAGLRFSKCMSASMPILVQLMASSSATDVENAILLLMRCKQFQIDGAEACLRKILPLAFSQDKSIYEAVENAFISIYIRKNPVDTAKQLLNLAIDSNIGDQAALEFIVNALVSKGEISSSTTSALWDFFCFNINGTTAEQSRGALSILCMAAKSSPRILGSHIQDIIDIGFGRWAKVEPLLARTACTVIQRFSEEDRKKLLLSSGSRLFGILESLITGNWLPENIYYATADKAISAIYMIHPTPETLASTIIKKSLSTVFDVVEQEEAQTDTENNKVDILTPVQVAKLSRFLFAVSHIAMNQLVYIESCIQKIRRQKTKKDKPAAESQNTEENLEATQENNGINAELGLAASDDALLDTLAERAEREIVSGGSVEKNLIGECATFLSKLCRNFSLLQKHPELQASAMLALCRFMIIDASFCESNLQLLFTVVENAPSEVVRSNCTLSLGDLAVRFPNLLEPWTENMYARLRDASVSVRKNAVLVLSHLILNDMMKVKGYIYEMAICIEDDVERISSLAKLFFHELSKKGSNPIYNLLPDILGQLSNRNLERESFCNVMQFLIGSIKKDKQMEALVEKLCNRFSGVTDGKQWEYISYSLSLLTFTEKGIKKLIESFKSYEHALAEDLVTENFRSIINKGKKFAKPELKACIEEFEEKINKFHMEKKEQEETARNAEVHREKTKTMESLAVLSKVKEEPVEEYDEGEGVSDSEIVDPSMEESGDNLVETESEEEPSDSEEEPDSAQCGTAIPRYLNQKTSGDNLIETEPEEEQSDSEPDSAQCGTTNPRSLNRKTSGDNLIETESEEEQSDSEEEPSDSEEEPDSAQCGTTNPRSLNQKTSGGEEGESESKSTESSSSIRRNLRSGSRS

cell division [GO:0051301]; chromatin organization [GO:0006325]; meiotic chromosome condensation [GO:0010032]; mitotic cell cycle [GO:0000278]; mitotic chromosome condensation [GO:0007076]

condensed chromosome, centromeric region [GO:0000779]; nucleus [GO:0005634]

histone binding [GO:0042393]

PF12717;PF12922;

1.25.10.10;

CND1 (condensin subunit 1) family

SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:25065716}. Nucleus {ECO:0000250|UniProtKB:Q15021}. Note=Associates with the chromosomes throughout meiosis. {ECO:0000269|PubMed:25065716}.

FUNCTION: Essential protein (PubMed:23929493). Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes (By similarity). The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (By similarity). Required for fertility, growth and euchromatin organization, but not for sister chromatid cohesion (PubMed:23929493). Necessary to maintain normal structural integrity of the meiotic chromosomes during the two nuclear divisions of gametogenesis, especially to maintain compaction of the centromeric repeats and 45S rDNA (PubMed:25065716). Seems also involved in crossover formation during meiotic prophase I (PubMed:25065716). Prevents centromeric and pericentromeric heterochromatin repeats association (PubMed:23929493). Contributes to the induction of stress-responsive genes in response to stress treatment (PubMed:16856987). {ECO:0000250|UniProtKB:Q15021, ECO:0000269|PubMed:16856987, ECO:0000269|PubMed:23929493, ECO:0000269|PubMed:25065716}.

Arabidopsis thaliana (Mouse-ear cress)

A0A1I9LMX5

PCEP9_ARATH

MKLLSITLTSIVISMVFYQTPITTEARSLRKTNDQDHFKAGFTDDFVPTSPGNSPGVGHKKGNVNVEGFQDDFKPTEGRKLLKTNVQDHFKTGSTDDFAPTSPGHSPGVGHKKGNVNVESSEDDFKHKEGRKLQQTNGQNHFKTGSTDDFAPTSPGNSPGIGHKKGHANVKGFKDDFAPTEEIRLQKMNGQDHFKTGSTDDFAPTTPGNSPGMGHKKGDDFKPTTPGHSPGVGHAVKNDEPKA

cellular response to nitrogen starvation [GO:0006995]; nitrate import [GO:1902025]; regulation of lateral root development [GO:2000023]; regulation of leaf morphogenesis [GO:1901371]; regulation of root development [GO:2000280]; response to ammonium ion [GO:0060359]; response to auxin [GO:0009733]; response to nitrogen compound [GO:1901698]; response to osmotic stress [GO:0006970]; response to potassium ion [GO:0035864]; root development [GO:0048364]

apoplast [GO:0048046]

hormone activity [GO:0005179]

C-terminally encoded plant signaling peptide (CEP) family

PTM: Hydroxylated peptide is more active than non-hydroxylated peptide. {ECO:0000269|PubMed:24179096}.; PTM: The mature small signaling peptide is generated by proteolytic processing of the longer precursor. {ECO:0000269|PubMed:25324386}.

SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.2]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.3]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.4]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.5]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.1]: Secreted, extracellular space, apoplast {ECO:0000305|PubMed:25324386}. Note=Accumulates in xylem sap. {ECO:0000305|PubMed:25324386}.

FUNCTION: Extracellular signaling peptide that represses primary root growth rate and significantly inhibits lateral root formation. Modulates leaf morphology (PubMed:24179096). Regulates systemic nitrogen (N)-demand signaling. Mediates up-regulation of genes involved in N uptake and assimilation pathways (PubMed:25324386). {ECO:0000269|PubMed:24179096, ECO:0000269|PubMed:25324386}.

Arabidopsis thaliana (Mouse-ear cress)

A0A1I9LN01

LAF3_ARATH

MTGWYEFPVMIGFVSAAVFLLISVAYLPLLNDLYWSTLKSLTPPAGIVADLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWGGELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGTTDELSWKDFQDVYLYADSSKKMMIRTCLFFPITTWSRLLDLKLQKGSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVASVQPDHLLDDADSVAKKLGSERAVKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSWDEFSKDVSASVLATYVGGKQLYP

3.5.-.-

de-etiolation [GO:0009704]; response to far red light [GO:0010218]; seed germination [GO:0009845]

membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]

hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]

PF07969;

3.10.310.70;3.20.20.140;2.30.40.10;

Metallo-dependent hydrolases superfamily

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14645728}.

FUNCTION: Required for phyA-controlled responses to continuous far-red light (FRc) conditions, including the inhibition of hypocotyl elongation and the regulation of XTH15/XTR7 expression. {ECO:0000269|PubMed:14645728}.

Arabidopsis thaliana (Mouse-ear cress)

A0A1J1DL12

RIDA_DERFA

MSPKRIISTPLAPQPIGPYSQAVQVGNTVYLSGQIGMNVRTNEMVTGPIRDEAQQAFTNMKAVVEASGAKMSDVVKVNIFIRNFNDFPAINDVMKEFFQSPFPARSTVGVAELPKNARVEIESIVVIE

3.5.99.10

organonitrogen compound catabolic process [GO:1901565]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]

2-iminobutanoate deaminase activity [GO:0120242]; 2-iminopropanoate deaminase activity [GO:0120243]; deaminase activity [GO:0019239]

PF01042;

3.30.1330.40;

RutC family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52758}.

CATALYTIC ACTIVITY: Reaction=2-iminobutanoate + H2O = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:39975, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:76545; EC=3.5.99.10; Evidence={ECO:0000305|PubMed:27539850}; CATALYTIC ACTIVITY: Reaction=2-iminopropanoate + H2O = NH4(+) + pyruvate; Xref=Rhea:RHEA:40671, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:44400; EC=3.5.99.10; Evidence={ECO:0000305|PubMed:27539850};

FUNCTION: Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism (PubMed:27539850). May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase (By similarity). Preferentially digests Leu and Met in cooperation with L-amino acid oxidase, but digests Phe poorly (PubMed:27539850). {ECO:0000250|UniProtKB:P52758, ECO:0000269|PubMed:27539850}.

Dermatophagoides farinae (American house dust mite)

A0A1L3THR9

CDA_PESTX

MLAPLFAALLAGAATASPIQERQSSVPVGTIITACTVPNTFALTFDDGPFAYTSELLDLLSSNGVKATFFLNGQNWGSIYDYTSVVTRMDAEGHQIGSHTWSHADLATLDAAGITSQMTQLETALTSILGKVPTYMRPPYFSTNALALSTLGGLGYHVINANIDTLDYEHDDDTIGVAFTNFQNGLASGGTVSLMHDVHAQTVHVLVQEAINAIKAKGLTPVTVGTCLGDASANWYKSGGGSGTTPPPATGGPSPDDTCGGSNGYVCQNSQCCSQWGWCGTTSEYCAAGCQAAYGPCT

3.5.1.41

COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:Q6DWK3};

cell wall organization [GO:0071555]; chitin catabolic process [GO:0006032]; evasion of host immune response [GO:0042783]; polysaccharide catabolic process [GO:0000272]

extracellular region [GO:0005576]

chitin binding [GO:0008061]; chitin deacetylase activity [GO:0004099]; metal ion binding [GO:0046872]

PF00187;PF01522;

3.30.60.10;3.20.20.370;

Polysaccharide deacetylase family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27901067}.

CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089, ChEBI:CHEBI:57704; EC=3.5.1.41; Evidence={ECO:0000269|PubMed:27901067}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465; Evidence={ECO:0000305|PubMed:27901067};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:27901067};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:27901067};

FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine polymers in chitin to form chitosan and acetate (PubMed:27901067). May play a role in evasion of the host immune response; plant chitinases liberate chitin molecules from the fungal cell wall which act as elicitors of the plant immune response, deacetylation of the liberated chitin neutralizes elicitor activity (PubMed:27901067). {ECO:0000269|PubMed:27901067}.

Pestalotiopsis sp

A0A1L4BJ46

HEMI1_HEMLE

MTFLILTILATVTPSLYSHVVQRELRVNFEPLAGQRDSWPVARAAMVTFDARSEKAREFSECRMINSMHELSRELMDSPEHTVKRASKEEMDDLVQRCSGSAEGRSWFIWPDTKWCGPGTDAKNESDLGPLEADKCCRTHDHCDYIGAGETKYGLTNKSFFTKLNCKCEAAFDQCLKESIDRAEGSAKSSMEGLHSFYFNTYSPECYEVKCSRKRDAECTNGIAIWKDSYKS

3.1.1.4

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:26335363}; Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:26335363};

arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]

extracellular region [GO:0005576]

calcium-dependent phospholipase A2 activity [GO:0047498]; metal ion binding [GO:0046872]

PF05826;

1.20.90.10;

Phospholipase A2 family, Group III subfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26335363}.

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:26335363};

FUNCTION: Scorpion venom phospholipase A2 (PLA2) that shows high hydrolytic activities towards lecithin and acts as an effective blocker of all angiogenesis key steps in vivo and in vitro (PubMed:26335363). It has no effect on apoptosis and does not display hemolytic, inflammatory or neurotoxic effects (PubMed:26335363). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:26335363}.

Hemiscorpius lepturus (Scorpion)

A0A1L4BJ98

DTPLD_HEMLE

MAHCYYNSKRGCNRVMKTVALVVLISTVMVEESRGDSQEDKKRPIWNIGHMVNAVKQIEEFLDLGANALEADVTFDDNGNPKWTYHGTPCDCFRDCLRWEYVDEYLKRIRELTSPGSSKFRKGFILLMLDLKISKLSDNAKSKAGKEIADMIIKRLWSGSGEKAQLYIVLSFPYVNDIEFVRAFRERVKSKGFASEAEKRIGWDISGNEDLGKIRDAYQKLGITDNVWQSDGITNCLTRSHDRLAEAVCKRDSDKEWPSLKKVYYWTVDKQSSMKEALKVGVDGMITNDPDDLVAVLNEFSGTHRLANINDSPWQKIPRPKSNC

4.6.1.-

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:28335389}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914};

killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042]

extracellular region [GO:0005576]

lyase activity [GO:0016829]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; toxin activity [GO:0090729]

PF13653;

3.20.20.190;

Arthropod phospholipase D family, Class II subfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28335389}.

CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652, ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892; Evidence={ECO:0000305|PubMed:28335389}; CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60648, ChEBI:CHEBI:57603, ChEBI:CHEBI:143891, ChEBI:CHEBI:143892; Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60700, ChEBI:CHEBI:15354, ChEBI:CHEBI:58168, ChEBI:CHEBI:143947; Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60704, ChEBI:CHEBI:57603, ChEBI:CHEBI:64381, ChEBI:CHEBI:143947; Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};

FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) with a high activity (PubMed:28335389). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). In vivo, shows dermonecrotic activity when intradermally injected into rabbit skin and is lethal to mice (PubMed:28335389). Induces increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). Does not show hemolytic activity (at up to 50 ug) (PubMed:28335389). {ECO:0000250|UniProtKB:A0A0D4WTV1, ECO:0000269|PubMed:28335389}.

Hemiscorpius lepturus (Scorpion)

A0A1L4BKS3

TERL_BPG20

MKRLRPSDKFFELLGYKPHHVQLAIHRSTAKRRVACLGRQSGKSEAASVEAVFELFARPGSQGWIIAPTYDQAEIIFGRVVEKVERLSEVFPTTEVQLQRRRLRLLVHHYDRPVNAPGAKRVATSEFRGKSADRPDNLRGATLDFVILDEAAMIPFSVWSEAIEPTLSVRDGWALIISTPKGLNWFYEFFLMGWRGGLKEGIPNSGINQTHPDFESFHAASWDVWPERREWYMERRLYIPDLEFRQEYGAEFVSHSNSVFSGLDMLILLPYERRGTRLVVEDYRPDHIYCIGADFGKNQDYSVFSVLDLDTGAIACLERMNGATWSDQVARLKALSEDYGHAYVVADTWGVGDAIAEELDAQGINYTPLPVKSSSVKEQLISNLALLMEKGQVAVPNDKTILDELRNFRYYRTASGNQVMRAYGRGHDDIVMSLALAYSQYEGKDGYKFELAEERPSKLKHEESVMSLVEDDFTDLELANRAFSA

3.1.21.-; 3.6.4.-

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:28100693}; Note=Nuclease activity requires 2 Mg(2+) ions per subunit (PubMed:28100693). Also active in the presence of Mn(2+) or Co(2+) but inactive with Ni(2+), Zn(2+) or Ca(2+) (PubMed:28100693). Cu(2+), Cd(2+) and Cs(2+) do not support catalysis (PubMed:28100693). {ECO:0000269|PubMed:28100693};

chromosome organization [GO:0051276]; viral DNA genome packaging [GO:0019073]

viral terminase, large subunit [GO:0098009]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]

PF17289;PF03237;

3.30.420.240;3.40.50.300;

Tequatrovirus large terminase family

FUNCTION: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer. Once the capsid is packaged with the DNA, the terminase complex is substituted by the tail. {ECO:0000255|HAMAP-Rule:MF_04146, ECO:0000305|PubMed:28100693}.

Thermus phage G20c (Thermus thermophilus phage G20c)

A0A1L5YRA2

TPIS_SCYPA

MANQRKFFVGGNWKMNGDKAAIDGIISFMKGPLNADTEVVVGCPQCYLMYTREHMPANIGVAAQNCYKTAKGAFTGEISPAMIKDCGCEWVILGHSERRNVFGEPDQLISEKVGHALEAGLKVIPCIGEKLEERESNRTEEVVFAQMKALVPNISDWSRVVIAYEPVWAIGTGKTATPEQAQDVHAKLRQWLRDNVSPQVAESTRIIYGGSVSAGNCKELAKTGDIDGFLVGGASLKPDFVTIINARA

4.2.3.3; 5.3.1.1

gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol catabolic process [GO:0019563]; glycolytic process [GO:0006096]; methylglyoxal biosynthetic process [GO:0019242]

cytoplasm [GO:0005737]; cytosol [GO:0005829]

IgE binding [GO:0019863]; methylglyoxal synthase activity [GO:0008929]; protein homodimerization activity [GO:0042803]; triose-phosphate isomerase activity [GO:0004807]

PF00121;

3.20.20.70;

Triosephosphate isomerase family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.

CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}; CATALYTIC ACTIVITY: Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate; Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474, ChEBI:CHEBI:57642; EC=4.2.3.3; Evidence={ECO:0000250|UniProtKB:P00939};

PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}.

FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis. {ECO:0000250|UniProtKB:P00939}.; FUNCTION: It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids. {ECO:0000250|UniProtKB:P00939}.

Scylla paramamosain (Mud crab)

A0A1L6K371

JUGN4_JUGNI

MAKPILLSISLCLVALVNGCLAQSGGRQQPRFGECKLKRLVALEPSNRIEAEAGVIESWDPNNQQFQCAGVAVVRRTIEPNGLLLPQYSNAPQLLYIVKGRGITGVLFPGCPETFEESQQGQSRIRPSLRSASFQRDRHQKIRHFREGDVIAFPAGVAHWCYNDGDTPVVAVALMDTTNNANQLDQNPRNFYLAGNPDDEFRPQGQQEYEQHRRQQQHQQRHGEPGQQQRGSGNNVFSGFDADFLADAFNVDTETARRLQSENDHRRSIVRVEGRQLQVIRPRWSREEQEREERKERERERESESERRQSRRGGRDDNGLEETICTLRLRENIGDPSRADIYTEEAGRISTANSHTLPVLRWLQLSAERGALYSDALYVPHWNLNAHSVVYALRGRAEVQVVDNFGQTVFDDELREGQLLTIPQNFAVVKRARNEGFEWVSFKTNENAMVSPLAGRTSAIRALPEEVLANALQIPREDARRLKFNRQESTLVRSRPSSSRSSRSERRAEV

seed maturation [GO:0010431]

extraorganismal space [GO:0043245]

IgE binding [GO:0019863]; nutrient reservoir activity [GO:0045735]

PF00190;

2.60.120.10;

11S seed storage protein (globulins) family

PTM: Proteolytically processed from a single precursor to produce an acidic and a basic chain that are linked by a disulfide bond. {ECO:0000269|PubMed:27936684}.

FUNCTION: Seed storage protein. {ECO:0000255|RuleBase:RU003681, ECO:0000305|PubMed:27936684}.

Juglans nigra (Black walnut) (Wallia nigra)

A0A1L6Z3A0

TPS8_PSEAD

MSRFTSATHGLNLSIKMPISVSQVPSIRSNTSKYELQKLRSTGRSVLQTRRQLAIINMTKRSEADDNDGVERRKGVFHPNLWDDGFIQSLSTVYHEQASYRERAERLIGEVKAVFDSISMGDGDQFISPSAYDTAWVARVPAIDGSSRPQFPQAIDWILLNQQQDGSWGSQSHLSLTHRLTDTLACVIALASWKIESVQIDEGLDFITRGVEKLQSESVPAEFEIIFAELLNQAKSLQLSLPYEHSCLQSLWRKQEPILANGLMDSVAKRSLSSLEEMQDHRMNTDSDGTMHVESFLSSPAVAARVLMRTGNPICLAYLNNVLNKFGDYVPGMYPVDLFQRLWMVDNVERLGIDRHFKKEIQVTLDYVYSYWNGKGIGCGRDSLSPDLNSTSLGFRTLRLHGYNVSADVLEHFKDRDGKFVCSSNPTVGEIRSVLNLYRASLLAFPGEKVMEEAETFARRYLEEIVQKIPPSKFSREIEYVLEFGWQSTVPRWEARSYIDFHGLDTYSPWTIYEMASEKFLELAKLEFNIFNSLQHTELQYLSRWWNDSGMSQMRFTRHRNVEYYTMASCIAMEPSQSAFRIGFTKLCGIATCIDDIYDTYGTIDELKLFREAVKRWDPSAIESLPEYMKSVYMVLYELVNEMAQDTERTQGRDTLDYARNAWEAIIDAHLVEAEWIASGHIPTFEEYLENSKVTSGLHIAILPILTLDVPLPDQLPLQEIDTLSRFHHLASTIGRLSGDMNAYKIDLAHGEESSCISCYMKDNPGTTEGDAHNYANVTISYLMKELNLELMGQHNRVSFLRTSKKPAFDIYRASNYMYKYRDGYTIADKETKNLVMRTLVQAVSL

4.2.3.180

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:28096378};

gibberellin biosynthetic process [GO:0009686]

chloroplast [GO:0009507]

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

PF01397;PF03936;

1.50.10.160;1.10.600.10;1.50.10.130;

Terpene synthase family

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

CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = diphosphate + pseudolaratriene; Xref=Rhea:RHEA:54116, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:138050; EC=4.2.3.180; Evidence={ECO:0000269|PubMed:28096378}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54117; Evidence={ECO:0000269|PubMed:28096378};

PATHWAY: Terpene metabolism. {ECO:0000305}.

FUNCTION: Converts geranylgeranyl diphosphate to an new 5,7-fused bicyclic diterpene, named pseudolaratriene (PubMed:28096378). Catalyzes the first committed step in pseudolaric acid B (PAB) biosynthesis (PubMed:28096378). PAB exhibits antiproliferative activity by inhibiting microtubule polymerization, and has demonstrated antitumor properties against several cancer types (Probable). {ECO:0000269|PubMed:28096378, ECO:0000305|PubMed:28096378}.

Pseudolarix amabilis (Golden larch) (Pseudolarix kaempferi)

A0A1L7NQ96

KET3E_ARTGO

MKIGCHGLVWTGHFDAEGIRYSVQKTREAGFDLVEFPLMDPFSFDVQTAKSALAEHGLAASASLGLSDATDVSSEDPAVVKAGEELLNRAVDVLAELGATDFCGVIYSAMKKYMEPATAAGLANSKAAVGRVADRASDLGINVSLEVVNRYETNVLNTGRQALAYLEELNRPNLGIHLDTYHMNIEESDMFSPILDTAEALRYVHIGESHRGYLGTGSVDFDTFFKALGRIGYDGPVVFESFSSSVVAPDLSRMLGIWRNLWADNEELGAHANAFIRDKLTAIKTIELH

5.1.3.-

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27713017}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:27713017, ECO:0000269|PubMed:30279320}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:27713017}; Note=Binds 1 divalent metal cation per subunit. Seems able to use Mg(2+), Mn(2+) or Co(2+). {ECO:0000269|PubMed:27713017, ECO:0000269|PubMed:30279320};

carbohydrate metabolic process [GO:0005975]

manganese ion binding [GO:0030145]; racemase and epimerase activity, acting on carbohydrates and derivatives [GO:0016857]

PF01261;

3.20.20.150;

Hyi family

CATALYTIC ACTIVITY: Reaction=L-ribulose = L-xylulose; Xref=Rhea:RHEA:53268, ChEBI:CHEBI:16880, ChEBI:CHEBI:17399; Evidence={ECO:0000269|PubMed:30279320}; CATALYTIC ACTIVITY: Reaction=D-allulose = keto-D-fructose; Xref=Rhea:RHEA:42360, ChEBI:CHEBI:27605, ChEBI:CHEBI:48095; Evidence={ECO:0000269|PubMed:27713017, ECO:0000269|PubMed:30279320}; CATALYTIC ACTIVITY: Reaction=keto-L-tagatose = keto-L-sorbose; Xref=Rhea:RHEA:61780, ChEBI:CHEBI:13172, ChEBI:CHEBI:134275; Evidence={ECO:0000269|PubMed:27713017}; CATALYTIC ACTIVITY: Reaction=D-ribulose = D-xylulose; Xref=Rhea:RHEA:51544, ChEBI:CHEBI:17140, ChEBI:CHEBI:17173; Evidence={ECO:0000269|PubMed:30279320}; CATALYTIC ACTIVITY: Reaction=L-allulose = keto-L-fructose; Xref=Rhea:RHEA:61784, ChEBI:CHEBI:37724, ChEBI:CHEBI:145026; Evidence={ECO:0000269|PubMed:27713017}; CATALYTIC ACTIVITY: Reaction=keto-D-tagatose = keto-D-sorbose; Xref=Rhea:RHEA:43048, ChEBI:CHEBI:13022, ChEBI:CHEBI:47693; Evidence={ECO:0000269|PubMed:27713017};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=31 mM for D-allulose {ECO:0000269|PubMed:27713017}; KM=37.5 mM for D-fructose {ECO:0000269|PubMed:27713017}; Vmax=177 umol/min/mg enzyme for the epimerization of D-allulose {ECO:0000269|PubMed:27713017}; Vmax=78.4 umol/min/mg enzyme for the epimerization of D-fructose {ECO:0000269|PubMed:27713017}; Note=kcat is 5664 min(-1) for the epimerization of D-allulose. kcat is 2509 min(-1) for the epimerization of D-fructose. {ECO:0000269|PubMed:27713017};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. Is stable from pH 6.0-11.0. {ECO:0000269|PubMed:27713017};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. Is highly stable at 55 degrees Celsius. {ECO:0000269|PubMed:27713017};

FUNCTION: Catalyzes the reversible C-3 epimerization of several ketoses. Shows the highest enzymatic activity for the epimerization of L-ribulose to L-xylulose. Is also able to convert D-allulose (also known as D-psicose) to D-fructose and, to a lesser extent, L-tagatose to L-sorbose, D-ribulose to D-xylulose, L-allulose to L-fructose and D-tagatose to D-sorbose. {ECO:0000269|PubMed:27713017, ECO:0000269|PubMed:30279320}.

Arthrobacter globiformis

A0A1L8F5J9

NMDZ1_XENLA

MGTMRLFLLAVLFLFSFARAGCDPKIVNIGAVLSTKKHEQIFREAVNQANKRHFTRKIQLNATSVTHRPNAIQMALSVCEDLISSQVYAILVSHPPAPTDHLTPTPISYTAGFYRIPVIGLTTRMSIYSDKSIHLSFLRTVPPYSHQALVWFEMMRLFNWNHVILIVSDDHEGRAAQKKLETLLEEKESKADKVLQFEPGTKNLTALLLEAKELEARVIILSASEDDATAVYKSAAMLDMTGAGYVWLVGEREISGSALRYAPDGIIGLQLINGKNESAHISDAVAVVAQAIHELFEMENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYPDGVTGRIEFNEDGDRKFANYSIMNLQNRKLVQVGIFNGSYIIQNDRKIIWPGGETERPQGYQMSTRLKIVTIHQEPFVYVRPTTSDGTCREEYTINGDPIKKVICNGPNETIPGRPTVPQCCYGFCVDLLIKLAREMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLNILKSHENGFMEELDKTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKASFRSITSTLASSFKRRRSSKDTVNVVV

chemical synaptic transmission [GO:0007268]; regulation of membrane potential [GO:0042391]; response to zinc ion [GO:0010043]

neuron projection [GO:0043005]; NMDA selective glutamate receptor complex [GO:0017146]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]

metal ion binding [GO:0046872]; NMDA glutamate receptor activity [GO:0004972]

PF01094;PF00060;PF10613;PF00497;

3.40.50.2300;3.40.190.10;

Glutamate-gated ion channel (TC 1.A.10.1) family, NR1/GRIN1 subfamily

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19524674, ECO:0000269|PubMed:21677647, ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:26912815, ECO:0000269|PubMed:27135925, ECO:0000269|PubMed:28232581, ECO:0000269|Ref.11}; Multi-pass membrane protein {ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:27062927, ECO:0000269|PubMed:28232581}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00959}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 8]: Cell membrane {ECO:0000305|PubMed:8955083, ECO:0000305|PubMed:8975675}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 7]: Cell membrane {ECO:0000269|PubMed:16214956}; Multi-pass membrane protein {ECO:0000305}.

FUNCTION: Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:16214956, PubMed:19524674, PubMed:21677647, PubMed:25008524, PubMed:26912815, PubMed:27135925, PubMed:28232581, Ref.11). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable). {ECO:0000269|PubMed:16214956, ECO:0000269|PubMed:19524674, ECO:0000269|PubMed:21677647, ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:26912815, ECO:0000269|PubMed:27135925, ECO:0000269|PubMed:28232581, ECO:0000269|Ref.11, ECO:0000305}.

Xenopus laevis (African clawed frog)

A0A1L8FDW4

PEX5_XENLA

MAMRGLIEAECGGSNPLMKLTNHFTQDKALREEGLQHVSWPPGATVVSKPLGEATEDELVSEFLHTRAPSLQSRAPHTFKMDGLLAEMQEIEQSSFRPEPLRAPGVADLALSEQWSAEFLGVEVDPVEEEDWSREFTEQADPHASPSRWAEEYLQQSEEKLWLGESEGAMAEKWTEEYQPEDDLQREAKSLVSQVTDPKLANTQFLQFVKRIGDGELSFSHAPSTPSQTVSQAEQWSEQFVHEQAEQWVDQFAPLEKDFEKAKAAVESDVDFWDKLQEEWEEMAKRDAEAHPWLSDFQDLSSKSIDKGYMFEDNNPFSEVSLPFEEGLKHLREGDLPSAVRLFEVAVKRDPQHMEAWQYLGTTQAENEQELAAISALRRCIDLKPDNLSALMALAVSYTNECLQQQACHTLREWLRHNPKYSHLVKEESSSNASRARSFGTLLSDSVFSDVRELFLSAVNSDPSQVDPDVQCGLGVLFNLSGEYQKAVDCFTAALGQRPDDYLLWNKLGATLANGNDSEAAVEAYRRALQLQPGFIRSRYNLGIACINLGAHREAIEHFLEALSMQQQSGGCESAMSDNIWSTLRMALSMIGQSDLYSSADARDLATLQAAFPPHSAAQ

pexophagy [GO:0000425]; protein import into peroxisome matrix, docking [GO:0016560]; protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein import into peroxisome matrix, substrate release [GO:0044721]; protein import into peroxisome matrix, translocation [GO:0016561]

cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]

peroxisome matrix targeting signal-1 binding [GO:0005052]; protein carrier chaperone [GO:0140597]

PF13432;PF13181;

1.25.40.10;

Peroxisomal targeting signal receptor family

PTM: Monoubiquitinated at Cys-11 by pex2 during pex5 passage through the retrotranslocation channel (By similarity). Cys-11 monoubiquitination acts as a recognition signal for the pex1-pex6 complex and is required for pex5 extraction and export from peroxisomes (PubMed:35931083). When pex5 recycling is compromised, polyubiquitinated by pex10 during its passage through the retrotranslocation channel, leading to its degradation (PubMed:35931083). {ECO:0000250|UniProtKB:P35056, ECO:0000269|PubMed:35931083}.

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:35931083}. Peroxisome matrix {ECO:0000269|PubMed:35931083}. Note=Cycles between the cytosol and the peroxisome matrix (PubMed:35931083). Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of pex13 and pex14, leading to translocation into the peroxisome matrix along with cargo proteins (PubMed:35931083). Export and recycling to the cytosol is initiated by binding to the pex2-pex10-pex12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol (PubMed:35931083). Cys-11 of pex5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the pex1-pex6 AAA ATPase complex (PubMed:35931083). Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix (PubMed:35931083). The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzymes, resetting pex5 for a subsequent import cycle (PubMed:35931083). {ECO:0000269|PubMed:35931083}.

FUNCTION: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) (PubMed:35931083). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the pex13-pex14 docking complex along with cargo proteins (PubMed:35931083). Pex5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle (PubMed:35931083). {ECO:0000269|PubMed:35931083}.; FUNCTION: In addition to promoting peroxisomal translocation of proteins containing a PTS1 peroxisomal targeting signal, mediates peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal via its interaction with pex7. Interaction with pex7 only takes place when pex7 is associated with cargo proteins containing a PTS2 peroxisomal targeting signal. Pex7 along with PTS2-containing cargo proteins are then translocated through the pex13-pex14 docking complex together with pex5. {ECO:0000250|UniProtKB:P50542}.

Xenopus laevis (African clawed frog)

A0A1L8G2K9

SPRTN_XENLA

MGDMQMSVVDPTWELLDPNPDIRALFLEFNDTFFWGQLSGVEVKWSARMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVETLLHEMIHALLFVTHNNKDHDSHGPEFCKHMERINGRTGANISVYHNFHDEVDEYRKHWWLCNGPCQKRKPYFGYVKRAMNRAPSSLDPWWADHQRTCGGSFVKVKEPENYPQKRKRKNDPTISEVNSSSHVKGKSNGVDIRTVIPFSGTGYKLFEPNKSDAPLKILNINPTKDKAAVPLLNHTPPSTNINGTFLTNKIGSAKSTPAQSILTKVSVANTKVFINLNGSPIKLPSGSKNKSHQISSKQKSVLPFFKMQKDNSFDLTLPSPSIQSTSQKPQKDISFGFTLPSQSFPSTSPGSNSENKEPLYKKLQMNDRESFIIHSGNKTNVNDNKSCTGPAATTASGLNHTIKVSCPVCGTEVLECKINDHLDTCTSSGPQKDILLDVSLPLQSFPSTSQGSNSAIKEPLYKKLQINDKDSFIIHSGNKTNVNDNKSCTRPAATTASGFNHTIKVCCPVCGTDVLQDKINDHLDTCLQNCNT

3.4.24.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040};

DNA damage response [GO:0006974]; protein autoprocessing [GO:0016540]; protein-DNA covalent cross-linking repair [GO:0106300]; proteolysis [GO:0006508]

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

double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; polyubiquitin modification-dependent protein binding [GO:0031593]; single-stranded DNA binding [GO:0003697]

PF10263;

3.30.160.60;

Spartan family

PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation. {ECO:0000250|UniProtKB:Q9H040}.

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000269|PubMed:30595436}. Note=Localizes to sites of UV damage via the PIP-box (By similarity). Recruited to stalled replication forks at sites of replication stress (By similarity). {ECO:0000250|UniProtKB:Q9H040}.

FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (PubMed:30595436, PubMed:35534579, PubMed:36608669). DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde (By similarity). Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis (By similarity). Catalyzes proteolytic cleavage of the hmces DNA-protein cross-link following unfolding by the brip1/fancj helicase (PubMed:35534579, PubMed:36608669). Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as top1, top2a, histones H3 and H4 (By similarity). Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs (PubMed:30595436). SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs (PubMed:30595436). May also act as a 'reader' of ubiquitinated pcna: facilitates chromatin association of rad18 and is required for efficient pcna monoubiquitination, promoting a feed-forward loop to enhance pcna ubiquitination and translesion DNA synthesis (By similarity). Acts as a regulator of translesion DNA synthesis by recruiting vcp/p97 to sites of DNA damage (By similarity). {ECO:0000250|UniProtKB:Q9H040, ECO:0000269|PubMed:30595436, ECO:0000269|PubMed:35534579, ECO:0000269|PubMed:36608669}.

Xenopus laevis (African clawed frog)

A0A1L8GSA2

TET3A_XENLA

MMETQPTSLPHVLPQDVYEFCDDRKSLGRLRVSEMPAESNGDGGGSKGDGAAVVAKEVPEQSNKKRKRCGVCVPCLRKEPCGACYNCVNRSTSHQICKMRKCEQLKKKRVVPLKGVEAVNKDDSKNQAKEQVPNVKNCSESILVDGPKTDQMEAGPVNHVQEGRLKKECDSTLPSKACEDLANQLLMEANSWLSNTAAPQDPCNKLNWDKPTIPNHTAATNNSNLEDAKNLVAFSAVAEAMSNYGMPASGTPSSVSMQLYEKFNYETNRDSSGHPEGNAPSCPEDLNTLKTALALAKHGVKPPNCNCDGPECPDYLEWLENKIKSSQKDSQESSFPGLGQVSKELVQKSYPKEEVLNLENKNLCPSGNLPFSQNALSLAKEKNISLQTAIAIEALTQLSSALPQTNNECPNSSSQPLINTCDQLTHFPTAKGNQLPIFPMACNELFQNQQSQLYTGKNALPVPQSPRQTSWEQNKKPSYQEGQYIPENLSQSSSVLPSDASTPQKTEFLQQWIQNADLLKSPSDPMTGLKQLLGNTDEYIKSVFKGPEALPNKIKHVKTKRTIKSIKKKSSDFLKMSPDQQLSQLLQENDFHHNAQAALQQHLHHKRNLFVDPNTMEACAQEQQNWWVPKSQKLPVSKTTENPVKERKKRRQRSPSQKQVEPKPKPPRKQVQIKKPRMKEGNAVFMPVSQISLDAFRGAEKEENQLKEMNLEKSLSNNIQPDLLESQSILVTGSQANIENRKTVNTQETCNENQASNGKASNFALCVNQANSLGAKDSCPTPSTDDASSSSGQGDSANQHTNVGDVPGQNDLSCLDDKFEDLLRQFEAEFGEDFSLPGSEAPSQNGVGPPKQQISGDPQFKMPFPSQLLPSENSTRPDAHSNPALSNNPISHNVSHNLDSLFSSKSPKKIKIESSGAITVVSTTCFYSEENQHLDGTPTKSDLPFNPTLSGFLESPLKYLTSPTKSLIDTPAKMAQAEFPTCDCVEQINEKDEGPYYTHLGSGPTVASIRELMEDRFGEKGEAIRIEKVIYTGKEGKSSRGCPIAKWVIRRQSEDEKLMCLVRQRAGHHCENAVIIILIMAWEGIPRALGDSLYSDITETITKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWSMYFNGCKYARSKTPRKFRLIGDNPKEEEFLNDNFQDLATKVAPVYQMLAPQSYENQVNNEEVAIDCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTIGRIPEDEQLHVLPLYKVSSTDEFGSEDGQAEKIRKGGIQVLASFPREVRKLSEPAKSCRQRQLDAKKAAAEKKKLQKEKLVSPDKTKQEPADTKMCQQNPGVPQQQTKPCVKVEPSNHYNTYKYNGNGVVESYSVLGSCRPSDPYSMNSVYSYHSFYAQPNLPSVNGFHSKFALPPFGFYGFPNNPVVPNQFMNYGTSDARNSGWMNNSFEKKPDVQSLADGMNQSYGSELPEQSYRRSSEVPHHYSLQNPNSQKSFNISHRTTPSPMETTPYSNLPCYNKVIKKEPVCDPLVDPFQRANSVHSQSPGVNHSLQTSDLPFKANGALPSSGRSNAEGPCSMSLPNDKSGLEKRDYFGVHSNVPALKDKQWTPYGTDVPVGQRDSLDAQSPGKVWSSCKLSDSPAVLPSFASTQTKNWNGRQASLNQGLKEPMPFQEKLWNSVAASDRCSVTPSDRSSVTPCAELQDKNWASFPNPVGNSLKTESSQNHWDPYSLDDNMDDGQSKSVKEEEDEEEIWSDSEHNFLDKNIGGVAVAPGHGSILIECARRELHATTPLKKPNRCHPARISLVFYQHKNLNQPNHGLALWEAKMKLLAERARVKEEEAARLGIKQEVKSLGKKRKWGGAATTETPPVEKKDFIPTRQATTILTDSATTAFSYAYTKVTGPYSRFI

1.14.11.80

COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6N021}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=The zinc ions have a structural role. {ECO:0000250|UniProtKB:Q6N021};

5-methylcytosine catabolic process [GO:0006211]; DNA demethylation [GO:0080111]; eye development [GO:0001654]; nervous system development [GO:0007399]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; positive regulation of transcription by RNA polymerase II [GO:0045944]

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

5-methylcytosine dioxygenase activity [GO:0070579]; methyl-CpG binding [GO:0008327]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]

PF12851;PF02008;

TET family

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0JP82}. Chromosome {ECO:0000250|UniProtKB:A0JP82}. Note=Detected on chromatin, where it binds to target gene promoters. {ECO:0000250|UniProtKB:A0JP82}.

CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-methyl-2'-deoxycytidine in DNA + O2 = a 5-hydroxymethyl-2'-deoxycytidine in DNA + CO2 + succinate; Xref=Rhea:RHEA:52636, Rhea:RHEA-COMP:11370, Rhea:RHEA-COMP:13315, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85454, ChEBI:CHEBI:136731; EC=1.14.11.80; Evidence={ECO:0000269|PubMed:23217707}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-hydroxymethyl-2'-deoxycytidine in DNA + O2 = a 5-formyl-2'-deoxycytidine in DNA + CO2 + H2O + succinate; Xref=Rhea:RHEA:53828, Rhea:RHEA-COMP:13315, Rhea:RHEA-COMP:13656, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:136731, ChEBI:CHEBI:137731; EC=1.14.11.80; Evidence={ECO:0000250|UniProtKB:Q6N021}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-formyl-2'-deoxycytidine in DNA + O2 = a 5-carboxyl-2'-deoxycytidine in DNA + CO2 + H(+) + succinate; Xref=Rhea:RHEA:53832, Rhea:RHEA-COMP:13656, Rhea:RHEA-COMP:13657, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:137731, ChEBI:CHEBI:137732; EC=1.14.11.80; Evidence={ECO:0000250|UniProtKB:Q6N021};

FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming during embryonic development. Conversion of 5mC into 5hmC probably constitutes the first step in cytosine demethylation. Selectively binds to the promoter region of target genes and contributes to regulate the expression of numerous developmental genes, including pax6, rax, sox9 and six3. May also contribute to the regulation of target genes in ways that do not require its enzyme activity. {ECO:0000269|PubMed:23217707}.

Xenopus laevis (African clawed frog)

A0A1L8GVF0

RA50S_XENLA

MSKIEKMSIQGVRSFGINDKNKQVIQFFTPLTILVGPNGAGKTTIIECLKYMTTGDFPSGSKGNTFVYHPKLAHETDVRAQICLQLKDVNGEPVAVQRSIICRQKGKSTECKTVDCVITRIKHGGPVSLRPKCEEMNKEMISALGVSSAVLNNVIFCHQEDSNWPLSEGKRLKGKFDEIFSITRYSKALETLRDVRMKEDQNVSNYQEEIKYLKENKEKAREIQDNLQSKEKQLTVSKENVKSIESQLEPLKDRLADIQRNLFKVIRLENEIKALESRKRTMEQDNQDLMEKMEKVFQGTDEELNEMYQNQCFVREKERKLNDHQREMDRACKESQRLNREKGELLVQQGHLQLEADNHQRYIKTRDSLIKSLAVQLELDGFELTPFNQRQTSNFQMLVKERQEEVEAHANQILREFSEREAMQQRQIDEIRDKKTGLERTIELKSSTESKKHTDLKKVKYDLQQLEGTSDRLHELDEELQKTAHALENVEKSCNLEALKGEVVQLQTQKSELDRNVRELDQEMEQLNKHTMTRTQMDMLKNDKADKDEQIRKMKSRHNDELISLYEYFPNKKQLEDWLYSKREDINQTRDKLARLTKELVAAEQNSNHLSNELCQKEKQSASFEEKVFDVCGSQDFNSDLSQLLEDIEKTSKQRAMLAGATAVYTQFITTLTEENQPCCPVCQRTFPSEAEVQDVINDMQSKLCLVPDKLKAAEDELKRKEKRKDEMMELKPMRQMLSDLKEKEIPEIRNKLEAINREIKRLQNDVEEQESLIVTFVSEEARAEACLQDISLMEQYQMELRDVDQKIAHYATKLLGVDLNRTVQQVNQEKLEKHHSLDNVSRRIELLQNHLQNQQEQVQQLKSRVNELTAEKLHISSNLQQRQQLEEQNVELTTELHCLSIEIKESREQVFPLESTLQKLQQEKQALLQRKESSYREAQEKVNDIKEKVKKINLHTKDIEKYIQDGKEEFKEQKESELQELTVRLNECEELKEKINREMVTIRQDIDTQKIQERCLQDNLTLRKRIEELKQVEEERDQLLKEMGQMKVTQMEKEYQELENKRETLKTNHSLTLGRQKGFEDEILRFKNELNEPKYKDAEEEYREKMIVMRTTELAIKDLDIYFKTMDQAIMKFHSIKMEEINKIIRDLWCSTYRGQDIEYIEIQSEPDEGISAADNRRTYNYRVVMIKGDTELDMRGHCSAGQKVLASLIIRLALAEIFCSNCGVLALDEPTTNLDHENIDSLAHALVEIIKSRSRQRNFQLIVITHNEDFVELLGRSEYVEHFYRIKKNIDQCSEIIRCSVSSLASYLH

3.6.-.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q92878}; Note=Binds 1 zinc ion per homodimer. {ECO:0000250|UniProtKB:Q92878};

chromosome organization involved in meiotic cell cycle [GO:0070192]; DNA double-strand break processing [GO:0000729]; DNA duplex unwinding [GO:0032508]; DNA strand resection involved in replication fork processing [GO:0110025]; metaphase chromosome alignment [GO:0051310]; R-loop processing [GO:0062176]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via telomerase [GO:0007004]

chromosome, telomeric region [GO:0000781]; condensed nuclear chromosome [GO:0000794]; Mre11 complex [GO:0030870]; site of double-strand break [GO:0035861]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded telomeric DNA binding [GO:0003691]; G-quadruplex DNA binding [GO:0051880]; metal ion binding [GO:0046872]; protein serine/threonine kinase activator activity [GO:0043539]; single-stranded telomeric DNA binding [GO:0043047]

PF13476;PF04423;PF13558;

3.40.50.300;

SMC family, RAD50 subfamily

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92878}. Chromosome, telomere {ECO:0000250|UniProtKB:Q92878}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}.

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:Q92878};

FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:19892829, PubMed:23434370). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:19892829). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (By similarity). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by mre11, to initiate end resection, which is required for single-strand invasion and recombination (By similarity). Within the complex, rad50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11 (By similarity). Rad50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the mre11 active site: ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form (By similarity). The MRN complex is also required for DNA damage signaling via activation of the atm and atr kinases: the nuclease activity of mre11 is not required to activate ATM and ATR (By similarity). The MRN complex promotes recruitment of topbp1 to DNA damage sites (PubMed:23582259). The MRN complex and rbbp8/CtIP are also required for chromosome alignment during metaphase (PubMed:23434370). {ECO:0000250|UniProtKB:Q92878, ECO:0000250|UniProtKB:Q9X1X1, ECO:0000269|PubMed:19892829, ECO:0000269|PubMed:23434370, ECO:0000269|PubMed:23582259}.

Xenopus laevis (African clawed frog)

A0A1L8GXM0

RA50L_XENLA

MSKIEKMSIQGVRSFGIEDKNKQVIQFFTPLTVLVGPNGAGKTTIIECLKYITTGDFPPGSKGKTFVHDPKVAHETDVRAQIRLQLKDVNGELVAVQRSMICTQKGKSTEFKTLEGVITRIKHGEKVSLSTKCAEMDKEMISALGVSAAVLNNVIFCHQEDSNWPLSEGRQLKVKFDEIFSATRYIKALETLKKVRTQQAHNVREYQVEIKYLKQNKEKAREIQDNLQSKEKQLAVSKENVKSIESQLEPLKDRLADIQRNLSKVMRLDNEIKALESRKRTMEQDNQDLEEKMEKVFQGTDEELNGMYQNHQRSVREKERKLNDQQREMDRACKESQRLNREKGELLVQQGRLQLEADHHQQYIKTRDSLIKSLAAQLELDGFERTPFNQRQTSNFQMLVKERQEKDEAHANQILREFSEREAMKQRQLDEMRDKKTGLERTIELKSSTQSKKHTDLKNVKYELQQLEGSSDRLQELDEELQKTERELENVEKSCNLEALRGEVLQLQNQKSELDRNVRKLDQEMEQMNTHTMTRTQMDMLKKDKADKDEQIRKIKSRHNDELSLLLGYFPNKKQLEDWLYSKRKDINQTRDKLARLTKELVAAEQNKNHLSNELRRKEEQSASFEEKVFDVCGSQDFDSDLSRLQDDIEKTSKQRAMLAGATAVYTQFITTLTEENQPCCPVCQRIFPSEAELQDVINDMQSKLRLVPDKLKSAEGELKRKEKRKDDMMELKPMRQMLADLKEKEIPEIRNKLVTINREIQRLKNDVDEQETLIATFASEEESAKACLQDISLMERYQMELRDVERKIAQYATKLQGVDLNRTVQQVSQEKQEKQHNLDNVSGKIELLRKRIQDQQEQVQQLKSAVNELTAEKLHISSNLQRRQQLEDQNVELTTELQCLAREIKEAREQLFPLESTLQKLQQEKQELLQRKESSYREAQEKVNDIKEKVKKINLLTKDIEKYSQDGKEEFKEQKESELQELIGRLNECEKLKEKVNREMVTIRQDIDTQKIQERCLQDNLTLRKRIEELKRVEEERHQLLKEMGQMKVVQMKNEYQELENKSESLKTNHSLALGRQKGFEDEILRFKKELRESQYKEAEEKYREKMIVMRTTELAIKDLDIYYKTLDQAIMKYHSIKMEEINKIVRDLWRSTYRSQDIEYIEIQSDADESVTAADKRRTYNYRVVMIKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSRQRNFQLIVITHDEDFVELLGRSEYVEHFYRIKKNIDQCSEIIRCSVNSLASYVH

3.6.-.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q92878}; Note=Binds 1 zinc ion per homodimer. {ECO:0000250|UniProtKB:Q92878};

chromosome organization involved in meiotic cell cycle [GO:0070192]; DNA double-strand break processing [GO:0000729]; DNA duplex unwinding [GO:0032508]; DNA strand resection involved in replication fork processing [GO:0110025]; metaphase chromosome alignment [GO:0051310]; R-loop processing [GO:0062176]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via telomerase [GO:0007004]

chromosome, telomeric region [GO:0000781]; condensed nuclear chromosome [GO:0000794]; Mre11 complex [GO:0030870]; site of double-strand break [GO:0035861]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded telomeric DNA binding [GO:0003691]; G-quadruplex DNA binding [GO:0051880]; metal ion binding [GO:0046872]; protein serine/threonine kinase activator activity [GO:0043539]; single-stranded telomeric DNA binding [GO:0043047]

PF13476;PF04423;PF13558;

1.10.287.1490;3.40.50.300;

SMC family, RAD50 subfamily

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92878}. Chromosome, telomere {ECO:0000250|UniProtKB:Q92878}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}.

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:Q92878};

FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:19892829, PubMed:23434370). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:19892829). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (By similarity). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by mre11, to initiate end resection, which is required for single-strand invasion and recombination (By similarity). Within the complex, rad50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11 (By similarity). Rad50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the mre11 active site: ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form (By similarity). The MRN complex is also required for DNA damage signaling via activation of the atm and atr kinases: the nuclease activity of mre11 is not required to activate ATM and ATR (By similarity). The MRN complex promotes recruitment of topbp1 to DNA damage sites (PubMed:19279141, PubMed:23582259). The MRN complex and rbbp8/CtIP are also required for chromosome alignment during metaphase (PubMed:23434370). {ECO:0000250|UniProtKB:Q92878, ECO:0000250|UniProtKB:Q9X1X1, ECO:0000269|PubMed:19279141, ECO:0000269|PubMed:19892829, ECO:0000269|PubMed:23434370, ECO:0000269|PubMed:23582259}.

Xenopus laevis (African clawed frog)

A0A1L8HU22

NEIL3_XENLA

MEALPPQVLKPLDCMSIYSRHREPENRHNELSTGRCGRGHVIFSSMKALQPQVLKPTGSHANLQQVLYAPAATIITAPASSHNDLSSLTGCSYAGVETLGKELFIYFGLKAMRVHFGMNGSMRINQPMKKGQENGRPIPIAVLEVQLTKDLICFYESTVDVRNASECQEKIRFFEELDVCSSKFSFPRAECEIKKQRTRMLCDILLDQMILPGVGNIIKNEALFDSGLHPGVQAGLLTDEQVSHLVKMTRDFTLLFYKCRKSGSALYKHYKVYKRPNCGQCGTKITVCRLGEHNRMTYFCPKCQKDKPQHVDVSKLPTRNSLIGWVQRTASNANEHVATSKEEHWACAVCTLINKPSDKQCDACLTLRPEVSSLAVSDEAAELNTDLVKYPCNNFAKVLPELKLNRRTAFGNTTLVLTDFGAKEGLADKNSQQNILNRSTFDVPLNNKYYHTKTPSNKRSNENEHWTNTLNAVNGHSAASNNVFNHPQKKLKTGHTTSNTIHLSSTISSPQSKMTGDAAAKTGNPQCSAHNVPCALQVVRKEGENKGRSFYTCSLPRERRCQYFEWADLHFPFCNHGKRCIVRTVLKIGPNNGKNFYVCPMGKDKQCNFFEWAKTE

3.2.2.-; 4.2.99.18

base-excision repair [GO:0006284]; interstrand cross-link repair [GO:0036297]

chromosome [GO:0005694]; nucleoplasm [GO:0005654]

class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA N-glycosylase activity [GO:0019104]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; MCM complex binding [GO:1904931]; zinc ion binding [GO:0008270]

PF06831;PF06839;

1.10.8.50;3.20.190.10;2.30.30.380;

FPG family

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TAT5}. Chromosome {ECO:0000269|PubMed:30842657}. Note=Recruited to replication stress sites via interaction with ubiquitinated CMG helicase. {ECO:0000269|PubMed:30842657}.

CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|PROSITE-ProRule:PRU00392, ECO:0000269|PubMed:30842657};

FUNCTION: DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA) (PubMed:30842657). Mediates interstrand cross-link repair in response to replication stress: recruited to replication stress sites via interaction with ubiquitinated CMG helicase and acts by mediating DNA glycosylase activity (PubMed:30842657). Cleaves one of the two N-glycosyl bonds comprising the interstrand cross-link, which avoids the formation of a double-strand break but generates an abasic site that is bypassed by translesion synthesis polymerases (PubMed:30842657). {ECO:0000269|PubMed:30842657}.

Xenopus laevis (African clawed frog)

A0A1L8HV70

DCK1_XENLA

MATPPKRICIDVPASPSGNKCKVKRISIEGNIAAGKSTFVNILKKANEEWDVVPEPIARWCNIQSCKDEFEELTTSQKSGGNLLQMMYEKPERWSFTFQSYACLSRIRAQLKALGGKLKEAENPVLFFERSVYSDRYIFASNLYEAECMNETEWTVYQDWHDWMNSQFGADLELDGIIYLRAIPEKCLNRVYTRGREEEQGIPMEYLEKLHYKHETWLHHRTLRTDFEYLQEIPILTLDVNEDFRDNKQKQESLIEKVKEFLSTL

2.7.1.113; 2.7.1.74; 2.7.1.76

deoxyribonucleoside monophosphate biosynthetic process [GO:0009157]; phosphorylation [GO:0016310]

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

ATP binding [GO:0005524]; deoxyadenosine kinase activity [GO:0004136]; deoxycytidine kinase activity [GO:0004137]; deoxyguanosine kinase activity [GO:0004138]

PF01712;

3.40.50.300;

DCK/DGK family

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27707}.

CATALYTIC ACTIVITY: Reaction=2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a ribonucleoside 5'-diphosphate + dCMP + H(+); Xref=Rhea:RHEA:20061, ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:57566, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=2.7.1.74; Evidence={ECO:0000269|PubMed:27906638}; CATALYTIC ACTIVITY: Reaction=2'-deoxyguanosine + ATP = ADP + dGMP + H(+); Xref=Rhea:RHEA:19201, ChEBI:CHEBI:15378, ChEBI:CHEBI:17172, ChEBI:CHEBI:30616, ChEBI:CHEBI:57673, ChEBI:CHEBI:456216; EC=2.7.1.113; Evidence={ECO:0000269|PubMed:27906638}; CATALYTIC ACTIVITY: Reaction=2'-deoxyadenosine + ATP = ADP + dAMP + H(+); Xref=Rhea:RHEA:23452, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256, ChEBI:CHEBI:30616, ChEBI:CHEBI:58245, ChEBI:CHEBI:456216; EC=2.7.1.76; Evidence={ECO:0000269|PubMed:27906638};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.34 uM for deoxycytidine {ECO:0000269|PubMed:27906638}; KM=527 uM for deoxyguanosine {ECO:0000269|PubMed:27906638}; KM=533 uM for deoxyadenosine {ECO:0000269|PubMed:27906638}; KM=12457 uM for deoxythymidine {ECO:0000269|PubMed:27906638}; KM=15081 uM for deoxyuridine {ECO:0000269|PubMed:27906638}; Vmax=0.1 umol/min/mg enzyme toward deoxycytidine {ECO:0000269|PubMed:27906638}; Vmax=6.6 umol/min/mg enzyme toward deoxyguanosine {ECO:0000269|PubMed:27906638}; Vmax=5.2 umol/min/mg enzyme toward deoxyadenosine {ECO:0000269|PubMed:27906638}; Vmax=0.6 umol/min/mg enzyme toward deoxythymidine {ECO:0000269|PubMed:27906638}; Vmax=2.5 umol/min/mg enzyme toward deoxyuridine {ECO:0000269|PubMed:27906638}; Note=kcat is 0.09 sec(-1) with deoxycytodine as substrate. kcat is 3.40 sec(-1) with deoxyguanosine as substrate. kcat is 2.73 sec(-1) with deoxyadenosine as substrate. kcat is 0.29 sec(-1) with deoxythymidine as substrate. kcat is 1.27 sec(-1) with deoxyuridine as substrate. {ECO:0000269|PubMed:27906638};

FUNCTION: Phosphorylates the deoxyribonucleosides deoxyadenosine, deoxycytidine and deoxyguanosine with highest activity against deoxycytidine followed by deadenosine and deoxyguanosine (PubMed:27906638). Shows only very minor activity against deoxyuridine and deoxythymidine (PubMed:27906638). {ECO:0000269|PubMed:27906638}.

Xenopus laevis (African clawed frog)

A0A1P8AQ95

STMP4_ARATH

MTKNMTKKKMGLMSPNIAAFVLPMLLVLFTISSQVEVVESTGRKLSWAFNGAPIVFTPPSSSCGGSPAAVMASEWMPRRPCRRTRPPGTNIPVSQSP

response to ethylene [GO:0009723]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414]

apoplast [GO:0048046]; plasma membrane [GO:0005886]

LRR domain binding [GO:0030275]; receptor serine/threonine kinase binding [GO:0033612]

Serine rich endogenous peptide (SCOOP) phytocytokine family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31001913}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:31001913}. Note=The precursor of STMP4 accumulates at the plasma membrane and is proteolytically cleaved to release the STMP4 in the apoplasm. {ECO:0000269|PubMed:31001913}.

FUNCTION: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation (By similarity). Prevents general growth and development (PubMed:31001913). {ECO:0000250|UniProtKB:B3H7I1, ECO:0000269|PubMed:31001913}.

Arabidopsis thaliana (Mouse-ear cress)

A0A1P8ASY1

JHS1_ARATH

MPPRKKPKSSALKSNKQSSANHSSQPSTFGIQQLFLRHIQNSQSTSNSHTSTADPVDQQNVNGLASDTAVLTPQNPLGTSNEKPDESKDMDQQLTEASPKISKNLKRFSPGMLIKQSQDDCGGEITWKISPVNERLRAAAKNIPKMMDLTENSLGVKSSTIRPCSLNKLVQKQCPTSGITSKVEQWLSSPSKKASKRPAFATNRVMERVNPSPDAEFEIVNTSSSGNSPFQTPPSLSCPHNKLPCTVTCSGACGSMGAGQHKKALLELLDQVEDVIAVDDKTTDDVGIVMPQARVKDDIISSVVDCAVDEGPVSLPKMQNSINPDSYFLVLEVSEKRGSGSSSKGQCPYKVLRLLDEHTGVECALYLWDEWFYSTVSPGDSINVIGEFDGDGKCDVDRQNNFLIVHPDTLVAGTRVAASFGCPRRTVLDERLRSNEHATVALLGTLQHQVFQAGLSQESPSVDGLQEYASTVIEKSIESLYACGVHEGDVRSTLFKAIPKMLNWIEHFRYSKDSEVSKVDFGSTIGKKAVKVSEVIDIEEMSWAPKYGLKGMIDASVRVIVESDMNTVNEKIMPLEFKSGKAPSGQSSIEHSAQVILYTLLMSERYLKHIDNGLLYYLQSDQTQGISVQRSDLVGLIIRRNELANDILVASTTQQLPPMLRNPNICRNCRHLDVCTIYHKADGGNTESSGLGDVFDTHVSHLSTLHFNFLRHWDRLIDLEGREMQLLRKDIAHPHGSKGSHSASYLSSMVLDVTNGFQHHNSHKETRFIYRFVRQKSSESRERVTSEDMIRTGNLATDDLDCKLRTGDRVILRTEVSHLTVANGIIADISRTHISVSLSKRLRLPWSEPSSEVSNLSHELWRIYKDEFMTSFSVMRFNLMQLFVQNGHNIRKMIVDLEPPRFDNGSILSQDPAISYIWSEKSLNNDQRQAILKILTAKDYALILGMPGTGKTSTMVHAVKALLIRGSSILLASYTNSAVDNLLIKLKAQGIEFLRIGRDEAVHEEVRESCFSAMNMCSVEDIKKKLDQVKVVASTCLGINSPLLVNRRFDVCIIDEAGQIALPVSIGPLLFASTFVLVGDHYQLPPLVQSTEARENGMGISLFRRLSEAHPQAISVLQNQYRMCRGIMELSNALIYGDRLCCGSAEVADATLVLSTSSSTSPWLKKVLEPTRTVVFVNTDMLRAFEARDQNAINNPVEASIIAEIVEELVNNGVDSKDIGIITPYNSQASLIQHAIPTTPVEIHTIDKYQGRDKDCILVSFVRSREKPRSSASSLLGDWHRINVALTRAKKKLIMVGSQRTLSRVPLLMLLLNKVKEQSGILNLLPGDLKP

3.1.-.-; 3.6.4.12

COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P38859}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P38859};

DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; meristem maintenance [GO:0010073]; replication fork reversal [GO:0071932]

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

4 iron, 4 sulfur cluster binding [GO:0051539]; 5'-flap endonuclease activity [GO:0017108]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; single-stranded DNA helicase activity [GO:0017116]

PF13086;PF13087;PF08696;

3.90.320.10;3.40.50.300;

DNA2/NAM7 helicase family

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26951435}. Chromosome {ECO:0000250|UniProtKB:P51530}. Note=Localized to nuclear foci in response to DNA damage. {ECO:0000269|PubMed:26951435}.

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=3.6.4.12; Evidence={ECO:0000250|UniProtKB:P51530};

FUNCTION: Essential protein required during embryogenesis (PubMed:15266054). Key enzyme involved in DNA replication and damage repair, shoot apical meristem (SAM) maintenance, and development (PubMed:26951435). Involved in Okazaki fragments processing. Possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5'-3' helicase and endonuclease activities. While the ATPase and endonuclease activities are well-defined and play a key role in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase activity is atypical: it cannot load onto its tracking strand internally and has an absolute free 5'-end requirement (By similarity). {ECO:0000250|UniProtKB:Q9URU2, ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:26951435}.

Arabidopsis thaliana (Mouse-ear cress)

A0A1P8AUY4

MDN1_ARATH

MAIDGSFNLKLALETFSVRCPKVAAFPCFTSILSKGGEVVDNEEVIHALGDAFLHPEFTVPLVHCFLPIIRNVVDRVVGLLRLVDDLKSSIDYSDDVSSVLDNAMTEGISVIDFYVRRGQRLELHECACLAFSRALHFNTSLLGSILNYFEKAPPPYERILVKDIVSESRMEATDAYLLCLRVSYRFLVIRPEVFSKLWDWSCYLDSMKRLSECPRQQRHFLEKYRDAVWCGIQILSVVLRCSDRLAGCFGFEEEEALSCLLRWEEFCQDIEIEKAGLYIQLPTYTALKSLQQFNTLVPGINKRQSAGLEADEPQMKIRRLDTWDVNSFSEPFEIHSRVKKSFEMVSLAVSQKRPVLLYGPSGSGKSALIRKLADESGNHVVFIHMDDQLDGKTLVGTYVCTDQPGEFRWQPGSLTQAIMNGFWVVLEDIDKAPSDVPLVLSSLLGGSCSFLTSQGEEIRIAETFQLFSTISTPECSVSHIRDAGNSLSPLWRRIVVYPPDRESLQSILGARYPNLGPVAEKLIETFETINSALRPQFSSSTTENSATFSSPSRFSLRDLLKWCERVHGLPSYDGHAVYQEAADIFSASNMSVKNRVAVSEIVASIWNVAVPESQDKPPIQEFSGILKIGRVSLPLGETASHDRSRFVETRTSTRLLEKIARSVEYNEPVLLVGETGTGKTTLVQNLAHWIGQKLTVLNLSQQSDIVDLLGGFKPIDPKLMCTMVYNEFNELARDLKIKDDSKIMKWLQDNFRAKKWHTFLTGLLDIIKGIEGRITERMEGKIGEARSRSGRKRKKPEEELKNCACLRTKVNKIRQQIHSGGMVFTFVEGAFVTALREGHWVLLDEVNLAPPEILGRLIGVLEGVRGSLCLAERGDVMGIPRHLNFRLFACMNPATDAGKRDLPFSFRSRFTEYAVDDDICDDDLEIFVRRFLGGRGSDSKLVANIVWFYKEAKRLSEESLQDGANQKPQYSLRSLYRALEYAIKAEAIGGFQKALYDGFSMFFLSLLDASSAKIVEPIIKRISGENIRSQPLQRYLGELKGSSDKFVGSYVKTKSVIDHLNHLAHAIFIKRYPVLLQGPTSSGKTSLVKYLAAISGNKFVRINNHEQTDIQEYLGSYMTDSSGKLVFHEGALVKAVRGGHWIVLDELNLAPSDVLEALNRLLDDNRELFVPELSETISAHPNFMLFATQNPPTLYGGRKILSRAFRNRFVEIHVDEIPEDELSEILTTKCSIANSHASKMVEVMKDLQRNRQSSKAFAGKHGYITPRDLFRWAYRFRTYDGTSHEELAREGYYILAERLRDDTEKVVVQEVLERHFRVSLAKDDLYNMELPRLDSIQNRKFTWTQSMRRLFFLIDRSYKLREPVLLVGDTGGGKTTICQILSDVKKKRLHILNCHQYTETSDFLGGFFPVRDRSKLITEYENQVKQLELSQALTPFGQDIVICGDISRAEVSIKSVEVALEKYKNGSVIGVAATPQDVDFLEKIRNNMVMLYQKWRAIFVWQDGPLVEAMRAGNIVLVDEISLADDSVLERMNSVLETDRKLSLAEKGGPVLEEVVAHEDFFVLATMNPGGDYGKKELSPALRNRFTEIWVPPITDTEELRSIAFSGLSSLKESNVVDPIINFWEWFNRLHTGRTLTVRDLLSWVAFVNMATESLGPAYAILHGAFLVLLDGLSLGTGFSGRDGQDLREKCFAFLLQQLELFASDTLPLELSRMELYGWGDSKAICEKSKSVRHEGMFGIDPFFISKGDENPEIGGFEFLAPTTHRNVLRVLRAMQLSKPILLEGSPGVGKTSLILALGKYSGHKVVRINLSEQTDMMDLLGSDLPVESDEDMKFAWSDGILLQALKEGSWVLLDELNLAPQSVLEGLNAILDHRAQVFIPELGCTFECPPTFRVFACQNPSTQGGGRKGLPKSFLNRFTKVYVDELVEDDYLFICRSLYPSVPSPLLSKLIALNRQLHDGTMLYRKFGHDGSPWEFNLRDVIRSCQFMQEAIHDLEVESFLNVLYIQRMRTATDRKEVLRIYKAIFDKTPSINPYPRVQLNPAYLVVGTAAIKRNLNQSNIASEQLKLLPEIRQNLEAVAHCVQNKWLCILVGPSSSGKTSVIRILAQLTGYPLNELNLSSATDSSDLLGCFEQYNAFRNFRLVMTRVEHLVDEYNSLLLQSSQEALFSNRSGLVSRWLSYLNKIDSSLVENPLFFLNDSETLSTLEEVVEDLEQVLKEGVLPVSWSKKYLEQISKTILQLQTHEKKQSTKFEWVTGMLIKAIEKGEWVVLKNANLCNPTVLDRINSLVEPCGSITINECGIVNGEPVTVVPHPNFRLFLSVNPKFGEVSRAMRNRGVEVFMMGPHWQLNEDGSNCEELVLRGVERFLALSGIPGYKLVTSMAKAHVHAWLNGQSFGVRITYLELEQWVHLFQLLLMNGNQLLWSLQLSWEHIYLSSLGVTDGKEVVDFVRETYLSDVELSELDSFMGGDLYLPGGWPKPFNLRDLTWYSRETTVRQNCMYLEFLGAQYASHQPKISDNVKSRDRELAAGEPRIIYSIDSWTLKKVLFPKALIGSSCAPDAANFENDLASKMLLFAANWTIEQATEEDIQLYLAWFSWFGSRLQQHCPFLLCFLNTLKVEFEHPIWNHISRCRKNLKFLCRLDPDAVPIPMLSSKLIDVAASNDQSKPYSKSLFESLNSVGVLRRSYQQWLVESNDNHTDVSTFTRFLDSLRVLEKKILCEIVGAPSFSVLIQLYTEVIDNHSFFWSGLVSSSDEYLLFSFWSLIKSIKKMHSFFPGEVQVVLEESKNINNIVLHGHPEKSMLWAYGGHPSLPVSAELFHKQQEFLQLCSTVWPLKSESDEHGNDHLTKAIPFSGPELCLLALEGLCISSYIADEDDVDYVAAVQLDEIYQTFLERLKLEKKRLEDKMGFSEIDNTENITASCCVFCPEIVTTGSGFSSWVKTCFIASSESCSLDVELLAALQHLLVARPTEHQDLVDIRKLLKPALEYSLSSTRPPQTLVAHQKLLWAIDAHASELGVDTKIAGFALEIWYWWHSVLWKNSQIGLMNISDTGNCQILSPSMLIQPVKTATVAQILENVFSVKDYSVQSMKLLSASRYLWKSSQPYQEMPGSLLSIARSLFQQIIYTHQKSFESETFVAIKSVFHAIEKKQNKMDGIQNLISLIGSSSHNKLKSVTHSFVGPLAKRLYSDSSSNALCPTFVEFYCNLGLAWLYLGGLRFHLLNSLDVIDPAMKITCKLLKLEEKISSLELNIKVRGECGYLSGLLYSGNNDESSEHTLSKLKTEHKRLQRKVIFRSDPKKYQDLRRALDEFAGFLTRPISLVNDIEVLDWNQVVEQVFNWQETAISFIDRMSSDYSEYVDITQPIQVSVYEMKLGLSLFVSGALLGKLLNRFDIDMVDSVMETIYALMRFPRDSSIASTTYTECLPPLHLSHGANSRAKSLGLDVGLLHKLISVSSAEDSRKASELQLKVALYKNLHARVLQFVANTGLLDEASFELLDKIYVELARIWMEMKFQAKTKADNLPGLYKFRSRDFKIDSVMEVDISALGKYFPNESFSEWQEYLADDDTKNVKDMTHIDQDEENLEDDWDLIQEHLDSIYSTHNELFGFCDLSEKSGRFCITDSRRLDSFTDSYELGVSMIKGLRGLFTSSLDAKLVPEHLLRLCLENKKNFTSNYQSASKYNFYKDLDGPELGKMVKFLTPLQQRINSLLQEREDHPGLQKLSGVLQMLLAIPSSTPLAKALSGLQFLLCKVHKLQEEGCKLPISDLLEPIISLASSWQKVEFERWPTLLDEVQDQYELNARKLWLPLFSVLFQKDAVEISEHENESISQSLVEFIETSNVGEFRRRLQLLFCFLLQLSMGSSLGIYSSDSHKRRVEMCYNIFGFYIQFLPVVMEQLDLNRKNVETELKEVLKLCRWERPDNYLYNETTKRTRQKVKKLIQKFTDMLRLPVMLVKPDLTKERAQFLPLLDPDLMDGASDMRIEVLVSALDAEQLRDRSSWYVVWWNKLKESVGRFHQEMHYKTLLMGAEHQYSSPVYQGDWKNLWSTVARIGETIAGCSDLWRNSDRDVAKKRALFELLKLLESSGLQKHKFENIEMSNHFKGLLYQPAYDPKHLLLLTHTKSNIHPSMGVEDQNKENSLVEWRVANEFYFKSLASVQLMLNIDRKHSDVTAEQVKRAISFLNHLVEIQRQQRKSAYAFAELFNRFRQCVLSLARLLGDSVGADRKDDSVFSFPQNQHAVFNCLWLQKQLFDNITAMLLEESALLRTVGSTHLDSCQAVKTSSRSLLSFIEILIPIAQNSKASLDRLLLDCNGFIITPSSSLKQFVTQHMVQVLRQNFDQLTDLENQISSFCENNEKSYCRDVLLSQFSPVFKEGKLLAENLNCLLNVRDQSTGMEPKERLFLEENLASIFANVKDVIGKLCSYKDGSLSQEEEMNITTWDGLFKKAENDLNLDNLCKLLSESFGSIEQLLNSSGVLSAGVGDQLKQLQAFLDLLLSFGDCYLKEFLAISKTVSLITHVLASVLADLFTKGFGISKNEEDDDSKVDKSEAAEGTGMGDGVGAKDVSDQIEDEDQLHGTDKKEEEEKEQDDVLGKNKGIEMSDEFDGKEYSVSEDEEEDKEDEGSEDEPLDNGIGDVGSDAEKADEKPWNKDEEDEEENMNEKNESGPSIVDKDTRSRELRAKDDGVETADEPEESNTSDKPEEGNDENVEQDDFDDTDNLEEKIQTKEEALGGLTPDVDNEQIDDDMEMDKTEEVEKEDANQQEEPCSEDQKHPEEGENDQEETQEPSEENMEAEAEDRCGSPQKEEPGNDLEQEPETEPIEGKEVMSEDMMKPNFRNDNISGVESGSQNPHGSNVLGAGSTAPQENLSATDVTDELTDSMDLPSSSNTEMNLMMTNMANGETLTDNLPKMEFPQNQSSTAQQTKVNPYRNVGDALKEWKERVRISSDLGEKQEAENEMEDPDASEYGFASQFDAGTSQALGPALPEQVNTDMREGESEEEKLAGNQDDVSPMDIDDLNPENKPAVQSKPSISNSIAEQVQEPDTDRTHQENSPIHNFGDGNSRMDSMVSVDNTFLGEEACNLDRMQVTDNDSESNQDNQEDPDARSNAVVLWRRCELLTAKPSQELAEQLRLILEPTLASKLSGDYRTGKRINMKKVIPYIASHYRKDKIWLRRTKPNKRDYQVVIAVDDSRSMSESGCGDFAIRALATVCRAMSQLELGSLAVASFGKQGSIKMLHDFGQSFTTESGIKMISNLTFKQENLIEDQPVVNLLRNMNEMLENLASTRRQSYGSNPLQQLVLIIGDGKFHEREKLKRTVRSFLQQKRMVVYLLLDDAEQSVFDLADYVYDGERRPYKKMNYLDSFPFPYYIVLRDIEALPRTLGDVLRQWFELMQSSRD

abscisic acid-activated signaling pathway [GO:0009738]; embryo sac development [GO:0009553]; regulation of developmental growth [GO:0048638]; ribosomal large subunit export from nucleus [GO:0000055]

chloroplast envelope [GO:0009941]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasmodesma [GO:0009506]; preribosome, large subunit precursor [GO:0030687]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]

PF07728;PF17865;PF17867;PF21108;

3.40.50.300;

Midasin family

SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q12019}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q12019}.

FUNCTION: Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits. Functions at successive maturation steps to remove ribosomal factors at critical transition points, first driving the exit of early pre-60S particles from the nucleolus and then driving late pre-60S particles from the nucleus (By similarity). Required for female gametophyte development (PubMed:23572950). Involved in the expression regulation of genes related to plant growth and development (PubMed:27824150). {ECO:0000250|UniProtKB:Q12019, ECO:0000269|PubMed:23572950, ECO:0000269|PubMed:27824150}.

Arabidopsis thaliana (Mouse-ear cress)

A0A1P8AW69

KTN81_ARATH

MAKRGYKLQEFVAHSGNVNCLSIGKKTSRLLLTGGDDYKVNLWSIGKTTSPMSLCGHTSPVDSVAFNSEEVLVLAGASSGVIKLWDLEESKMVRAFTGHRSNCSAVEFHPFGEFLASGSSDTNLRVWDTRKKGCIQTYKGHTRGISTIEFSPDGRWVVSGGLDNVVKVWDLTAGKLLHEFKCHEGPIRSLDFHPLEFLLATGSADRTVKFWDLETFELIGTTRPEATGVRAIAFHPDGQTLFCGLDDGLKVYSWEPVICRDGVDMGWSTLGDFCINEGKFIGCSYYRNSVGIWVSDISELEPYGAVSEDKNECMVKRFSVLNDQSERMGSGPRGSVSPDYETREIKNIYVDCGNLNVAQNPGSLKATLPLESGKVATMVSEKQNAAYFGPAGDKYSSTSRDSDSGEESSYSERESIPFSRTKSGMLLRPAHVRKTLAKFEESKQSAVVQSATRKKSGLAVEEEPQTQNAFLSEQNASKPFDAEDSIIKGITNKFEKALSSEPPTDEANRMFLKPPRIHRSSNSKYNDTRRAMSADPATFGKGGMENSGDVEDIPSKTERVLSREKPGDEQKNTEYPSGSRELNPVKIVEGVNVVSGRTRSLVEKFERGEKTTHTEGASTTIEQNNNAVQEDPRKTSRQTGETPVISTRRARSTPARVMPIVLNRDSNVTSDEPPLTQPARTSSFPVMPVILNQASNVTYDEPSVALTQESRTSHARILPVTFNQATNITSEEASVTLRRQRRNSAARVRPVLLSQATSHECPVTSVRPLRTSPARVMPTKLNQSVNMTSDTSHIASMHRVSPTQMLATPTVIDQVADMTLDETHATQIQPACDNMPQKEEPNISDREDDSDITENLMLTHNEFLSTLQSRLTKLQIVRHFWERSDVKGAIGALRKLTDQSVQADVISILTEKIEILTLDMFSQLVPVLTSLLGSRTERPVNVSLDMLLKLVAVFGTVIRSTVSAPRIVGVDLHANERLEICQICSAGLHKIQRILPVLARRGGLITRKAQELNLVLQEP

microtubule depolymerization [GO:0007019]; microtubule severing [GO:0051013]; regulation of unidimensional cell growth [GO:0051510]

cytoplasm [GO:0005737]; katanin complex [GO:0008352]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]

microtubule binding [GO:0008017]

PF13925;PF00400;

2.130.10.10;

WD repeat KATNB1 family

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:28978669}. Note=Present in dynamic discrete particles specifically localized to microtubule (MT) crossovers and branching nucleation sites. {ECO:0000269|PubMed:28978669}.

FUNCTION: May participate in a complex which severs microtubules in an ATP-dependent manner (By similarity). Microtubule severing may promote rapid reorganization of cellular microtubule arrays (By similarity). Confers precision to microtubule (MT) severing by specific targeting of KTN1 to MT cleavage sites such as crossover or branching nucleation sites (PubMed:28978669). Together with other KTN80s, regulates cell elongation by modulating MT organization (PubMed:28978669). {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:28978669}.

Arabidopsis thaliana (Mouse-ear cress)

A0A1R3RGK0

OTAA_ASPC5

MTFTSHPQSEPLAIIGLACKYANDINSPLDLYQQVMAARSMHGPMPPSRMDAAFYYHPSSEATGTTYAKGGYFLQSDLNAFDSPFFQLSEIDVLAMDPQQKMLLENVYHALENAGIPLKDAVSSSTSVFVGCSNNDHLALANADLLLALKGKGTGTSPSILANRISWFYDFQGTSQTIDTACSSSLVAFHQGCMDVRAGKSTMSIISGVNLMEHPAPTMYLSSLGVLSPDGRSMSFDARANGYGRGEGLGTVIIKPLTAALRDGNRIRAIVRSTGSNQDGRTPGITVPSPTAQERLIREVYKAADLDPSRTGYVEAHGTGTPVGDPLEVQAISAALGMSRDSPLYVGSVKSVVGHLEGGAGMAGLISATMAVESKTIPPVAGLQTLNPRIPQRPDLKFAKEATPWPREDVRRASINSFGFGGTNAHVVLEDVEGFFSDLFGQQLPGALQLSEVTSKALVPSAMKSAVNGIPADQPPKESSVNRLFVISAFDEAGIQRNAASLASHLESMRAITGSDGEERLLNDLCHTLNEKRTRFDWRSYHVADSIDSLRNSLQNPRPIRQSPAEKVVRFIFTGQGANWAGMAYDLLVYPLFRRRIQEAAIFLKELGSDWDLYERIASQSGELDEPTFAQSSCVAVQVALVDLLASWNVTPQTVVGHSSGEIAAAYCAGQISRQAAWKVAFCRGQVCARRTDGQGRMLAAAMPVTQLEQLVARVNKGQSTAVKVGCYNSPKNLTLTGRAEDILRAKLELDDVGALNRLLPVKVAYHSDYMRDAAPEYLDLLGDLDFGDSIHADAGIKMVSSVTGRAVSAGEAQQPSYWVDNLVSPVRFSTALLASMDDPSATGAREDALIEIGPHSTLRTAIKETFADVREFQSIQYGSLLKRYETDGSTILRTFGMLVCSGHKISLAAINDRRVGAKKTPRLLTGLPSYAFDHSRSMRGTSRRIEQAKFPAYKRHELLGVPVEDTNPVEQRWRNILRPDDLPWLRMNRMNGQIHFPGVAYLLMATEAAIQRVGNTVAISGVRLGNVSMLAPLPIPDSAAGVEIQFSIYPMKIHANSGTDWSTFRIVSYDSAEKTWTEHCVGSVRVETGPHESHEPHPGNATREECTESVDIAQMYSRFTTAGMDFGEYLRNIQEMKLSPDHQACTATITAPDIPCQAHDHYSLHPCTFESILHALLHLCKSSQGPMVTTYIEEVLVLSPQDTGVCGFEACAQTQRASATTWRSDVTITANTGRQQIRVTGLDLVQLPPSEDASDAESFYVVKWKPDVKLLTSVDALRDSASMYVAQHLPTLDEHEGFQLASGIFLLDTMDYVTRTGLPALPQHHQAFMQWMEKECRSIADGTVPLLDTALFEGIRASPDRRRELLARVAQLSARGELLVRVGTQMVPILEQKIDCLEVMFGPDNLMDRTYEEGLPGQIAPSVAGYLHCLAHAQTGIKVLEVGAGTGSATKVILDSLKPTERQDGGGLVSSVSTYHFTDISAAFFEKARARFPDWADILRPKVLNIELDPADQGFEMGSYDLVIATHVLHATADLSVSLKNIRGLLKEGGDLIVIENIQPDLMCSPLAFGLLPGWWRSVEPYRKTNPLITKDQWDQELRNAGLQSRLLIDDTDEGVNEMTAFVASRVREPPATQHVCSIIYSSRYGGQYELASQVARDLPPSCTASLVDLADISPEHTSTIGIVLVGYQGLDLSELSAHEYDRVNFLLTAFHRLLWVTCDEDEVPKSAMASGLVRTARWERDHDGVNFILLGISHRVPSASAAVSQMIRVCDHAFFSHELVPRNAEFRLEGSVLLTNRLFPATGINECIASSSRPRSKQVALEAVQHPVKLTSIGPHQPNGFHFVEDPQVDEPLLPDEVKIQIRAVGLDESDVEEMNRLIPGESAGSQGTGVVVEVGPAVHDIHVGDRVMALRTGHSGSLQTVLRTHSSAVTQVPEGLSLADAAAVPLPFTTAYHGLVNVARLEPQDTILIHNAGGATGQAAVQFACMLGATVYATVESDAQRQALLDYGVDRSRLLDGPSFAQQLARRGAKGSVDVLFNLSRESLEDRDLACLSQFGRLVGVHGQGSLPAGPTNRSYATVSIRELVQVRPKALHGTLRTISDLLTSRAIRPITPVRAGYSELQTVLSQIRQGNAGPWVLEPRANDTIPVAMKPLGDYQFDPCASYLLIGGFGGIGRSVVRWMLTRGAKNFIFLSRSGASSVPAKQLCADLLDAGCGVSDTVCDVTDATAVENALQQCGKSMPPIRGCLQCSMVLEDSMLSNMSHAQFLNAITPKVQGTIHVASALSSVKSNLDFFVLLSSSAGIIGNRGQANYSAANAFLDAFAAHLVSRGYPATSISLGSVLSVGWVAENQDRLPIALSYGAISEDLLLAILEYHMDPSWGAAQSPGTCHTVAGVRSARDFQRQSIPLPGFMAYPLFSPLRAIAGASQTAEEVAEAPIAQGLRGATSMEDAVELVTRAIVYKLARIMALSAKEIDAQRSLASYGVDSLVTVDLKAWFQREVGATVASGDLLGDSTIVQLAQQAAGGSRLVSVAMKGTE

2.3.1.-

COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|PROSITE-ProRule:PRU00258};

fatty acid biosynthetic process [GO:0006633]; methylation [GO:0032259]; ochratoxin A biosynthetic process [GO:1900818]

3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]; polyketide synthase activity [GO:0016218]

PF00698;PF08240;PF16197;PF00109;PF02801;PF08659;PF08242;PF21089;PF00550;PF14765;

3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;3.40.50.150;

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 9 H(+) + 4 malonyl-CoA + 5 NADPH = 7-methylmellein + 3 CO2 + 5 CoA + 4 H2O + 5 NADP(+); Xref=Rhea:RHEA:72767, 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:192524; Evidence={ECO:0000305|PubMed:24699234}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72768; Evidence={ECO:0000305|PubMed:24699234};

PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:24699234, ECO:0000269|PubMed:30054361}.

FUNCTION: Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of ochratoxin A (OTA), a mycotoxin composed of a chlorinated type I polyketide dihydroisocoumarin moiety linked to L-phenylalanine, and demonstrated to have nephrotoxic, immunotoxic, genotoxic, neurotoxic, and teratogenic properties (PubMed:24699234, PubMed:30054361). OtaA catalyzes the condensation of one acetate and 4 malonate units to form the isocoumarin group (PubMed:24699234). The pathway begins with the highly reducing polyketide synthase otaA that catalyzes the formation of the isocoumarin group during the initial stages of biosynthesis, starting from one acetate and 4 malonate units, to originate the characteristic pentaketide skeleton 7-methylmellein (7-MM) of the OTA molecule. The newly identified cyclase otaY might be involved in the polyketide cyclization reaction during the initial steps of the OTA biosynthesis. 7-MM is then oxidized into 7-carboxymellein (also called ochratoxin beta) by the cytochrome P450 monooxygenase otaC. The NRPS encoded by the otaB gene is involved in the linking of phenylalanine to the dihydroisocoumarin ring. The reaction catalyzed by NRPS results in the production of ochratoxin B (OTB), which is the non-chlorinated analog of OTA and which subsequently serves as the substrate of the halogenase otaD for chlorination activity to form the final molecular structure of OTA, containing a chlorine atom in the C-5 position of the molecule (Probable) (PubMed:33391201). {ECO:0000269|PubMed:24699234, ECO:0000269|PubMed:30054361, ECO:0000305|PubMed:33391201}.

Aspergillus carbonarius (strain ITEM 5010)

A0A1S3PBB7

KNG_SALSA

MKLGVRLCVLVVFSLQLWGPGQGQELEPEQVLAFCDDKDVEAAVDLALVKYNQKLPYGNQLALYQILESSKAQNDSCTQYFVEFNSRVTDCPAGGDKVWRDCDYLPTGNKVPRPCKATVHMSETDKKVLAVFCDPVEAPVVAERTTCLGCPREIDVESEDLKDPLTYSITRFNADSDSSHHFILNSVGFATRQVVAGFRYRLMFDMRKSNCSKADHKELNDECHPDPDVELAHCNSTVDVAPWRHETAEANVECAPGPLDNFDVFRRRPPGWSPLRNFNNFAEVKTTQASTASAKEESSEESQERSPSAVTMANPEPALPSVAPTTAAESPFHCPSKPWKQFVPPTTLRPAQEKSPTPLPVVEEGLSDLDLLGKK

negative regulation of blood coagulation [GO:0030195]; positive regulation of cytosolic calcium ion concentration [GO:0007204]

blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; vacuole [GO:0005773]

cysteine-type endopeptidase inhibitor activity [GO:0004869]

PF00031;

3.10.450.10;

PTM: N-glycosylated, with sialylated biantennary complex-type glycans. {ECO:0000269|PubMed:11447131}.; PTM: O-glycosylated, sialylated oligosaccharides. {ECO:0000269|PubMed:11447131}.; PTM: Bradykinin is released from kininogen by kallikrein. {ECO:0000250|UniProtKB:P01042}.; PTM: The N-terminus is blocked. {ECO:0000269|PubMed:10583403}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12397376}. Vacuole {ECO:0000269|PubMed:12397376}.

FUNCTION: Inhibits papain and ficin (cysteine proteinases) but not trypsin (a serine proteinase). {ECO:0000269|PubMed:10583403}.

Salmo salar (Atlantic salmon)

A0A1S3X835

MBP2C_TOBAC

MYKPQQQQQLFDLQDNNGAAFDNGGTDPSCWLSHENEISRTDSSLSSSNVDPLLFNDLVQIVPLVQSLIDRKEKSSFTRRGSMTYTKMPSRESLYKKTSEVKGRNAGQSTATKKHRDQNKNVSSSQDGYAENFSTPSSTSSLTEKDREELMTLREKVEDLQKKLLEKDELLKEAEILKNEITATNAELDEMKKDISEKDFLVKTTQVQLSDALVKLADKKAAVEKLEWEAMTSSKKVERLQEDLDLLQGEISSFIQFVHALTGNDSRDSAEECNVIPYPWDQNVEIDKLNERDLQKMEAAREAYIAAVAAAKENPDEASLSAASTARSYLQSLVLRT

defense response [GO:0006952]; negative regulation of protein transport [GO:0051224]; plasmodesmata-mediated intercellular transport [GO:0010497]; positive regulation of defense response to virus by host [GO:0002230]; regulation of cytoskeleton organization [GO:0051493]; transport of virus in host, cell to cell [GO:0046740]

cytoplasm [GO:0005737]; microtubule cytoskeleton [GO:0015630]

microtubule binding [GO:0008017]; RNA binding [GO:0003723]

Microtubule binding protein 2C family

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12913144}. Note=Microtubule-associated (PubMed:12913144). Localized in cytosolic punctae when associated with KN-1 (PubMed:17965274). {ECO:0000269|PubMed:12913144, ECO:0000269|PubMed:17965274}.

FUNCTION: Prevents homeodomain proteins (e.g. STM) association to plasmodesmata and, consequently, cell-to-cell transport. Binds to RNA. Alters KN1 RNA-binding capacity (PubMed:17965274). Regulates cytoskeleton (e.g. actin) organization that determinates cell shape (By similarity). Interferes with cell-to-cell transport of tobacco mosaic virus movement protein (TMV-MP) by mediating its accumulation at microtubules, thus interfering with cell-to-cell virus movement. {ECO:0000250|UniProtKB:Q9LEZ4, ECO:0000269|PubMed:12913144, ECO:0000269|PubMed:17965274}.

Nicotiana tabacum (Common tobacco)

A0A1S3XSG2

DAO1_TOBAC

MATTKQKVTAPSSSTAPCCPSTSILRREATAAVAGVGDGLQNWNNVPSVDDKQKKTASSALASLASTEPLSSNTSTKGIQIMTRAQTCHPLDPLSAAEISVAVATVRAAGETPEVRDGMRFIEVVLLEPDKSVVALADAYFFPPFQSSLMPRTKGGSLIPTKLPPRRARLIVYNKKTNETSIWIVELNEVHAAARGGHHRGKVISSNVVPDVQPPIDAQEYAECEAVVKSYPPFRDAMRRRGIDDLDLVMVDPWCVGYHSEADAPSRRLAKPLVFCRTESDCPMENGYARPVEGIYVLVDVQNMQIIEFEDRKLVPLPPADPLRNYTAGETRGGVDRSDVKPLHIIQPEGPSFRISGNYIEWQKWNFRIGFTPREGLVIHSVAYLDGSRGRRPIAHRLSFVEMVVPYGDPNDPHYRKNAFDAGEDGLGKNAHSLKRGCDCLGYIKYFDAHFTNFTGGVETTENCVCLHEEDHGMLWKHQDWRTGLAEVRRSRRLTVSFVCTVANYEYAFYWHFYQDGKIEAEVKLTGILSLGALQPGEYRKYGTTILPGLYAPVHQHFFVARMNMAVDCKPGEAHNQVVEVNVKVEEPGKENVHNNAFYAEETLLRSELQAMRDCDPFSARHWIVRNTRTVNRTGQLTGYKLVPGPNCLPLAGPEAKFLRRAAFLKHNLWVTQYAPGEEFPGGEFPNQNPRVGEGLASWVKQDRPLEESDIVLWYIFGITHVPRLEDWPVMPVEHIGFVLQPHGFFNCSPAVDVPPPSACDSESRDSDVTETSVAKSTATSLLAKL

1.4.3.-; 1.4.3.21

COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P46883}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P12807}; Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807, ECO:0000250|UniProtKB:P46883}; COFACTOR: Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; Evidence={ECO:0000250|UniProtKB:P46883}; Note=Contains 1 topaquinone per subunit. {ECO:0000250|UniProtKB:P46883};

alkaloid metabolic process [GO:0009820]; amine metabolic process [GO:0009308]; nicotine biosynthetic process [GO:0042179]; putrescine catabolic process [GO:0009447]

peroxisome [GO:0005777]

aliphatic amine oxidase activity [GO:0052595]; copper ion binding [GO:0005507]; primary amine oxidase activity [GO:0008131]; putrescine oxidase activity [GO:0050232]; quinone binding [GO:0048038]

PF01179;PF02727;PF02728;

3.10.450.40;2.70.98.20;

Copper/topaquinone oxidase family

PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.

SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24287136}.

CATALYTIC ACTIVITY: Reaction=a primary methyl amine + H2O + O2 = an aldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938, ChEBI:CHEBI:228804; EC=1.4.3.21; Evidence={ECO:0000269|PubMed:24287136}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154; Evidence={ECO:0000269|PubMed:24287136}; CATALYTIC ACTIVITY: Reaction=H2O + N-methylputrescine + O2 = 4-methylaminobutanal + H2O2 + NH4(+); Xref=Rhea:RHEA:71015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58039, ChEBI:CHEBI:190141; Evidence={ECO:0000250|UniProtKB:A0A1S4BDC4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71016; Evidence={ECO:0000250|UniProtKB:A0A1S4BDC4};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=163 uM for putrescine {ECO:0000269|PubMed:24287136}; KM=478 uM for N-methylputrescine {ECO:0000269|PubMed:24287136}; KM=492 uM for cadaverine {ECO:0000269|PubMed:24287136}; Vmax=561 pmol/sec/mg enzyme with putrescine as substrate {ECO:0000269|PubMed:24287136}; Vmax=928 pmol/sec/mg enzyme with N-methylputrescine as substrate {ECO:0000269|PubMed:24287136}; Vmax=840 pmol/sec/mg enzyme with cadaverine as substrate {ECO:0000269|PubMed:24287136};

PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:16656744}.; PATHWAY: Amine and polyamine degradation; putrescine degradation. {ECO:0000269|PubMed:24287136}.

FUNCTION: Involved in putrescine catabolism in peroxisomes (PubMed:24287136). May also be involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:16656744). Oxidizes preferentially non-N-methylated amines (PubMed:24287136). {ECO:0000269|PubMed:16656744, ECO:0000269|PubMed:24287136}.

Nicotiana tabacum (Common tobacco)

A0A1S3YCW2

ADC1A_TOBAC

MPALGCCVDAAVSPPPGYSFLWDSSLPAPEIFPSGVPPSTNTAVATTTTTHWSPAHSSALYSIDGWGAPYFTVNSSGDISVKPHGTDTLPHQEIDLLKVVKKASDPKNLGGLGLQFPLVVRFPDILKNRLESLQSVFDYAVQSQGYEAHYQGVYPVKCNQDRFVVEDIVKFGSGFRFGLEAGSKPELLLAMSCLCKGSHEGLLVCNGFKDAEYISLALVARKLMLNTVIVLEQEEELDLVIDISKKMAVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQIVRVVKKLEESGMLDCLQLLHFHIGSQIPSTALLADGVGEAAQIYCELVRLGAGMKYIDCGGGLGIDYDGTKSCDSDCSVGYGLQEYASTVVQAVRFVCDRKNVKHPVICSESGRAIVSHHSVLIFEAVSSTTTRSQELSSVDLQSFVEKLNDDARADYRNLSAAAIRGEYDTCVLYADQLKQRCVEQFKDGDLDIEQLAAVDGICDFVSKAIGASDPVRTYHVNLSIFTSVPDFWAIDQLFPIVPIHKLDERPVVRGILSDLTCDSDGKIDKFIGGESSLPLHELGSNGGGGGDGGKYYLGMFLGGAYEEALGGLHNLFGGPSVLRVSQSDSPHSFAVTCAVPGPSCADVLRAMQHEPELMFETLKHRAEEFVHNDDEQEEDKGLAFASLASSLAQSFNNMPYLVTNSSCCLTAAANNGGYYYCNDENIVGVGAESAAAEEELWPYCVA

4.1.1.19

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P21170}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P11926};

alkaloid metabolic process [GO:0009820]; arginine catabolic process [GO:0006527]; nicotine biosynthetic process [GO:0042179]; spermidine biosynthetic process [GO:0008295]

chloroplast [GO:0009507]

arginine decarboxylase activity [GO:0008792]

PF02784;

1.20.58.930;3.20.20.10;

Orn/Lys/Arg decarboxylase class-II family, SpeA subfamily

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

CATALYTIC ACTIVITY: Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682, ChEBI:CHEBI:58145; EC=4.1.1.19; Evidence={ECO:0000250|UniProtKB:Q9SI64};

PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:32242247}.; PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. {ECO:0000250|UniProtKB:Q9SI64}.

FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:32242247). Required for the biosynthesis of putrescine (By similarity). Catalyzes the first step of polyamine (PA) biosynthesis to produce putrescine from arginine (By similarity). {ECO:0000250|UniProtKB:Q9SI64, ECO:0000269|PubMed:32242247}.

Nicotiana tabacum (Common tobacco)

A0A1S3Z5Y0

SIPK_TOBAC

MDGSGQQTDTMMSDAGAEQPPPAPQPVAGMDNIPATLSYGGRFIQYNIFGNIFEVTAKYKPPILPIGKGAYGIVCSALNSETIENVAIKKIANAFDNKIDAKRTLREIKLLRHMDHENIVAIRDIIPPPQREAFNDVYIAYELMDTDLHQIIRSNQGLSEEHCQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARVTSETDFMTEYVVTRWYRPPELLLNSSDYTAAIDIWSVGCIFTELMDRKPLFPGRDHVHQLRLIMELIGTPSEAEMEFLNENAKRYIRQLPLYRRQSFTEKFPHVHPAAIDLVEKMLTFDPRRRITVEGALAHPYLNSLHDISDEPICMTPFSFDFEQHALTEEQMKELIYRESLAFNPEYQHM

2.7.12.2

defense response [GO:0006952]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]

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

ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]

PF00069;

1.10.510.10;

Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2; Evidence={ECO:0000305|PubMed:9618567}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10597; Evidence={ECO:0000305|PubMed:9618567}; 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=2.7.12.2; Evidence={ECO:0000305|PubMed:9618567}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000305|PubMed:9618567}; 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=2.7.12.2; Evidence={ECO:0000305|PubMed:9618567}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000305|PubMed:9618567};

FUNCTION: Phosphorylates myelin basic protein (MBP) in vitro (PubMed:9618567). May be involved in disease resistance (Probable). {ECO:0000269|PubMed:9618567, ECO:0000305|PubMed:9618567}.

Nicotiana tabacum (Common tobacco)

A0A1S4AUX8

ODC1A_TOBAC

MAGQTIIVSGLNPAAILQSTIGGGASPTAAAAENGTRKVIPLSRDALQDFMLSIITQKLQDEKQPFYVLDLGEVVSLIDQWKSALPNIRPFYAVKCNPEPSFLSILSAMGSNFDCASRAEIEYVLSLGISPDRIVFANPCKPESDIIFAAKVGVNLTTYDSEDEVYKIRKHHPKSELLLRIKPMFDGNARCPMGPKYGALPEEVEPLLRAAQAARLTVSGVSFHIGSGDADSNAYLGAIAAAKEVFETAAKLGMSKMTVLDVGGGFTSGHQFTTAAVAVRSALKQHFDDQPELTIIAEPGRFFAETAFTLATTIIGKRVRGELREYWINDGLYGSMNCVLYDHATVNATPLAVLSNRTNVTCGGSKTFPTTVFGPTCDALDTVLRDYQLPELQVNDWLVFPNMGAYTKAAGSNFNGFNTSAIVTHLAYAYPS

4.1.1.17

COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P11926};

alkaloid metabolic process [GO:0009820]; nicotine biosynthetic process [GO:0042179]; polyamine biosynthetic process [GO:0006596]; putrescine biosynthetic process from ornithine [GO:0033387]; response to wounding [GO:0009611]; tyramine biosynthetic process [GO:1901695]

chloroplast [GO:0009507]; cytoplasm [GO:0005737]

ornithine decarboxylase activity [GO:0004586]

PF02784;PF00278;

3.20.20.10;

Orn/Lys/Arg decarboxylase class-II family

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

CATALYTIC ACTIVITY: Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911, ChEBI:CHEBI:326268; EC=4.1.1.17; Evidence={ECO:0000250|UniProtKB:P11926};

PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:32242247}.; PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1. {ECO:0000250|UniProtKB:O22616}.

FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:27126795, PubMed:32242247). Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine (By similarity). Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis (By similarity). {ECO:0000250|UniProtKB:P11926, ECO:0000269|PubMed:27126795, ECO:0000269|PubMed:32242247}.

Nicotiana tabacum (Common tobacco)

A0A1S4BDC4

MPO1_TOBAC

MATTKQKVTAPSPSPSSSTASCCPSTSILRREATAAIAVVGDGLQNWTNIPSVDEKQKKTASSALASLPTTEPLSTNTSTKGIQIMTRAQTCHPLDPLSAAEISVAVATVRAAGETPEVRDGMRFIEVVLVEPDKSVVALADAYFFPPFQSSLMPRTKGGSQIPTKLPPRRARLIVYNKKTNETSIWIVELNEVHAAARGGHHRGKVIASNVVPDVQPPIDAQEYAECEAVVKSYPPFRDAMRRRGIDDLDLVMVDPWCVGYHSEADAPSRRLAKPLVFCRTESDCPMENGYARPVEGIYVLVDVQNMQIIEFEDRKLVPLPPVDPLRNYTAGETRGGVDRSDVKPLHIIQPEGPSFRISGNYVEWQKWNFRIGFTPREGLVIHSVAYLDGSRGRRPIAHRLSFVEMVVPYGDPNDPHYRKNAFDAGEDGLGKNAHSLKRGCDCLGYIKYFDAHFTNFTGGVETTENCVCLHEEDHGMLWKHQDWRTGLAEVRRSRRLTVSFVCTVANYEYAFYWHFYQDGKIEAEVKLTGILSLGALQPGEYRKYGTTILPGLYAPVHQHFFVARMNMAVDCKPGEAHNQVVEVNVKVEEPGKENVHNNAFYAEETLLRSELQAMRDCDPFSARHWIVRNTRTVNRTGQLTGYKLVPGPNCLPLAGPEAKFLRRAAFLKHNLWVTQYAPGEDFPGGEFPNQNPRVGEGLASWVKQDRPLEESDIVLWYIFGITHVPRLEDWPVMPVEHIGFVLQPHGYFNCSPAVDVPPPFACDSESRDSDVTETSVAKSTATSLLAKL

1.4.3.-; 1.4.3.21

COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P46883}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P12807}; Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807, ECO:0000250|UniProtKB:P46883}; COFACTOR: Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; Evidence={ECO:0000250|UniProtKB:P46883}; Note=Contains 1 topaquinone per subunit. {ECO:0000250|UniProtKB:P46883};

alkaloid metabolic process [GO:0009820]; amine metabolic process [GO:0009308]; nicotine biosynthetic process [GO:0042179]; response to auxin [GO:0009733]; response to jasmonic acid [GO:0009753]

peroxisome [GO:0005777]

aliphatic amine oxidase activity [GO:0052595]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; methylputrescine oxidase activity [GO:0052599]; primary amine oxidase activity [GO:0008131]; protein homodimerization activity [GO:0042803]; quinone binding [GO:0048038]

PF01179;PF02727;PF02728;

3.10.450.40;2.70.98.20;

Copper/topaquinone oxidase family

PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.

SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24287136}.

CATALYTIC ACTIVITY: Reaction=a primary methyl amine + H2O + O2 = an aldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938, ChEBI:CHEBI:228804; EC=1.4.3.21; Evidence={ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012, ECO:0000269|PubMed:24287136}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154; Evidence={ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012, ECO:0000269|PubMed:24287136}; CATALYTIC ACTIVITY: Reaction=H2O + N-methylputrescine + O2 = 4-methylaminobutanal + H2O2 + NH4(+); Xref=Rhea:RHEA:71015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58039, ChEBI:CHEBI:190141; Evidence={ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012, ECO:0000269|PubMed:24287136}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71016; Evidence={ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012, ECO:0000269|PubMed:24287136};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=309 uM for putrescine {ECO:0000269|PubMed:24287136}; KM=57 uM for N-methylputrescine {ECO:0000269|PubMed:24287136}; KM=215 uM for cadaverine {ECO:0000269|PubMed:24287136}; KM=0.19 mM for N-methylputrescine {ECO:0000269|PubMed:17174363}; KM=0.76 mM for putrescine {ECO:0000269|PubMed:17174363}; KM=1.79 mM for cadaverine {ECO:0000269|PubMed:17174363}; KM=0.35 mM for 1,3-diaminopropane {ECO:0000269|PubMed:17174363}; KM=36 uM for N-methylputrescine {ECO:0000269|PubMed:17283012}; KM=247 uM for putrescine {ECO:0000269|PubMed:17283012}; KM=362 uM for cadaverine {ECO:0000269|PubMed:17283012}; KM=158 uM for 1,3-diaminopropane {ECO:0000269|PubMed:17283012}; KM=96 uM for N-methyl-1,3-diaminopropane {ECO:0000269|PubMed:17283012}; KM=249 uM for n-butylamine {ECO:0000269|PubMed:17283012}; Vmax=28.8 nmol/sec/mg enzyme with N-methylputrescine as substrate {ECO:0000269|PubMed:17174363}; Vmax=11.1 nmol/sec/mg enzyme with putrescine as substrate {ECO:0000269|PubMed:17174363}; Vmax=5.2 nmol/sec/mg enzyme with cadaverine as substrate {ECO:0000269|PubMed:17174363}; Vmax=11.3 nmol/sec/mg enzyme with 1,3-diaminopropane as substrate {ECO:0000269|PubMed:17174363}; Vmax=926 pmol/sec/mg enzyme with N-methylputrescine as substrate {ECO:0000269|PubMed:17283012}; Vmax=902 pmol/sec/mg enzyme with putrescine as substrate {ECO:0000269|PubMed:17283012}; Vmax=715 pmol/sec/mg enzyme with cadaverine as substrate {ECO:0000269|PubMed:17283012}; Vmax=666 pmol/sec/mg enzyme with 1,3-diaminopropane as substrate {ECO:0000269|PubMed:17283012}; Vmax=1270 pmol/sec/mg enzyme with N-methyl-1,3-diaminopropane as substrate {ECO:0000269|PubMed:17283012}; Vmax=862 pmol/sec/mg enzyme with n-butylamine as substrate {ECO:0000269|PubMed:17283012}; Vmax=750 pmol/sec/mg enzyme with putrescine as substrate {ECO:0000269|PubMed:24287136}; Vmax=512 pmol/sec/mg enzyme with N-methylputrescine as substrate {ECO:0000269|PubMed:24287136}; Vmax=920 pmol/sec/mg enzyme with cadaverine as substrate {ECO:0000269|PubMed:24287136};

PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:16656744, ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012}.

FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:16656744, PubMed:17174363, PubMed:17283012). Amine oxidase which mediates the deamination of N-methylputrescine to produce 4-methylaminobutanal (PubMed:17174363, PubMed:17283012). Oxidizes preferentially N-methylated amines (PubMed:24287136). {ECO:0000269|PubMed:16656744, ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012, ECO:0000269|PubMed:24287136}.

Nicotiana tabacum (Common tobacco)

A0A1S4EWW7

VA1_AEDAE

MASHVIVKFITAAILIGSCYANYCDQSLCRRGPHVACNAPTQFGSACGQEPKFVKMDARMKNLLLKKHNELRAEIACGKHGFPQAARMPTLVWDDELAHIASFNARKCIFAHDKCRNTREFKFAGQNLAITAFAGYNFQAADRAENFTQEWFNEHKDCPKSYVDSYPMSHSGPQIGHFTQMVNDRAWKMGCSMVHYKNGRVIKYYLVCNYSMTNMIEEPIYTRGSAGSKCQTGQNPQYRGLCSPREKVRSESYRG

multicellular organism reproduction [GO:0032504]

extracellular space [GO:0005615]

PF00188;

3.40.33.10;

CRISP family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31937766}. Host endosome {ECO:0000269|PubMed:31937766}. Host mitochondrion {ECO:0000269|PubMed:31937766}. Note=Delivered into the human immune cells by endocytosis in a RhoA-dependent manner; escapes from host endosomes to mitochondria. {ECO:0000269|PubMed:31937766}.

FUNCTION: Activates autophagy in human monocytic cells, dendritic cells and macrophages (PubMed:31937766). Does not affect cytokine expression in human monocytic cells (PubMed:31937766). {ECO:0000269|PubMed:31937766}.; FUNCTION: (Microbial infection) Promotes dengue virus type 2 replication in human monocytic cells, dendritic cells and macrophages (PubMed:31937766). Pro-viral properties are linked to BECN1-mediated autophagy activation in the host (PubMed:31937766). Does not directly interact with the purified envelope protein of dengue virus type 2 (PubMed:31937766). {ECO:0000269|PubMed:31937766}.; FUNCTION: (Microbial infection) Promotes Zika virus replication in human monocytic cells, dendritic cells and macrophages (PubMed:31937766). Facilitates Zika virus transmission from infected mosquitoes to the host in mouse model (PubMed:31937766). Pro-viral properties are linked to BECN1-mediated autophagy activation in the host (PubMed:31937766). Does not affect Zika virus replication in human endothelial cells and keratinocytes (PubMed:35215815). {ECO:0000269|PubMed:31937766, ECO:0000269|PubMed:35215815}.; FUNCTION: (Microbial infection) Promotes Semliki Forest virus replication in human monocytic cells. {ECO:0000269|PubMed:31937766}.; FUNCTION: (Microbial infection) Does not influence Batai virus replication in human monocytic cells. {ECO:0000269|PubMed:31937766}.

Aedes aegypti (Yellowfever mosquito) (Culex aegypti)

A0A1S4F020

CBPB1_AEDAE

MIPRIVVVLLSVLAVVTARRSYEGYKVYGIVPESPDEAEILYQIRQSNPDLDFWHLTKQPGDEARVLVAPKDQRSFLIKLIRHGLHYQEVISDVEGTLAPYNEPRTRGMSLDRDVSTSYLRHNEINEYLQTLSQKYPSLVSVEEAGTSYEGRSIKTITINKKPGNAVVFLDAGIHAREWIAPATALYAIEQLVEHSSENQEVLSNLTWVIMPVVNPDGYEFSHETDRFWRKTRKPTGKTCKGTDGNRNFDYHWGEVGASTQACADTFRGETAFSEPETRAVRDAVMKLKGSCKFYLSLHSYGNYILYPWGWTSKLPETWEAIDEVAQAGAEAIKQSTGSRYTVGSSTNVLYAAAGGSDDWAFAVAEVPISITMELPGGGNGGFNPPPSSIEKIVNESWVGIKAMALKVAQMF

3.4.17.2

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P15086}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:34658092, ECO:0000269|PubMed:34750241};

proteolysis [GO:0006508]

endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]

metallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270]

PF00246;PF02244;

3.30.70.340;3.40.630.10;

Peptidase M14 family

SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:25521592}.

CATALYTIC ACTIVITY: Reaction=Preferential release of a C-terminal lysine or arginine amino acid.; EC=3.4.17.2; Evidence={ECO:0000269|PubMed:34658092, ECO:0000269|PubMed:34750241};

FUNCTION: Carboxypeptidase that preferentially hydrolyzes arginine and lysine residues at the C-terminus (PubMed:34750241). During infection by dengue virus, may play a role in preventing viral packaging, maturation, and release from the midgut (PubMed:25521592). {ECO:0000269|PubMed:25521592, ECO:0000269|PubMed:34750241}.

Aedes aegypti (Yellowfever mosquito) (Culex aegypti)

A0A1S4GMJ4

CLC9_ANOGA

MCILTLVERKHLKNMVHVRLLVMMHILIIYSTFGAVRRPINIRVLEGNSCDTPQVIGGKCMNISLCDPAFVHSIAYQEHTPVCQQNAFYRVICCQPFLDFCENSKQFQIMHGIEAEPGMFPHLARLGLKSEEDGIAWTCSANIISERFLLTAAHCNPVNIAGLGCAESMQCDQQNTVKSFISNPKYKTSFKYHDIALVELEQNIRFNKRVLPICPYISKTDLHESEDLVIAGWGATESHFQSPRLMFATVRTVLQNDCKDHYASLLKASPNKKLHQGITDEMYCAQGALVDNVTEYIDACSGDSGGPLQTKQNNNLYLIGVISTGFGCGSSSPGLYTRVASYFGWIKETVSATRDN

3.4.21.-

defense response to bacterium [GO:0042742]; defense response to symbiont [GO:0140546]; innate immune response [GO:0045087]; positive regulation of melanization defense response [GO:0035008]; proteolysis [GO:0006508]

extracellular space [GO:0005615]

serine-type endopeptidase activity [GO:0004252]

PF00089;

2.40.10.10;

Peptidase S1 family, CLIP subfamily

PTM: Secreted as a full-length protein (PubMed:12364791). Following bacterium E.coli infection, proteolytically cleaved into two chains, p12 and p30, which remain covalently linked (PubMed:12364791). {ECO:0000269|PubMed:12364791}.

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph (PubMed:33045027). Recruited by CLIPA8 to microbial surfaces where it is cleaved into the two chain active form (PubMed:33045027). {ECO:0000269|PubMed:33045027}.

FUNCTION: Probable serine protease which plays an essential role in the innate immune response against bacteria and protozoa infection by activating the melanization cascade (PubMed:33045027). In the susceptible strain G3, appears to be dispensable for ookinete elimination which occurs by lysis (PubMed:33045027). {ECO:0000269|PubMed:33045027}.

Anopheles gambiae (African malaria mosquito)

A0A1S4H5M5

CLA28_ANOGA

MKVLLFCIVISLTTLIASGQDIEEELRCPGGYCVSKYLCPNGTFIDDIKHAQTTQLIGLRAGLDIDDFDDCNDYLLVCCQSAPAPTATSTEKPATSDELIEPPPSTNLACGQANEGGLIYDLRNNETLSQYAEYPWVVYILALKKQEANSGDFVCGGTLIHSRLVVTTAHNTDGKTDLVARFGEWDISTTKEPFPQQDIDVAEVIKHPQYVFNPIQNDIALLVLAENVQYAAHIRPICLPQPTDEFVGQRCVSNGWGKERGVYANVMKKLTLPVIGRANCTRMLRYAGLGPFYTLREGFLCAGGEVAVDMCKGDGGSPLACQTESGTYVLAGIVSWGIGCGGFNTPGVYVAVNRYVQWLNEHIVDQALNESFDIKL

defense response to bacterium [GO:0042742]; innate immune response [GO:0045087]; positive regulation of melanization defense response [GO:0035008]; positive regulation of protein processing [GO:0010954]; proteolysis [GO:0006508]

extracellular space [GO:0005615]

serine-type endopeptidase activity [GO:0004252]

PF00089;

2.40.10.10;

Peptidase S1 family, CLIP subfamily

PTM: Secreted as a full-length protein (PubMed:31765430, PubMed:33045027). Proteolytically cleaved into two chains which probably remain covalently linked (PubMed:31765430). Cleavage is induced by fungus B.bassiana and Gram-positive or Gram-negative bacteria infection (PubMed:31765430, PubMed:33045027). {ECO:0000269|PubMed:31765430, ECO:0000269|PubMed:33045027}.

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31765430, ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph. {ECO:0000269|PubMed:31765430, ECO:0000269|PubMed:33045027}.

FUNCTION: Inactive serine protease which plays an essential role in the innate immune response against bacteria, fungi and protozoa infection by activating the melanization cascade (PubMed:31765430, PubMed:33045027). In the melanization cascade, acts downstream of TEP1, SPCLIP1 and CLIPA8 to promote CLIPC9 proteolytic cleavage (PubMed:31765430, PubMed:33045027). In the susceptible strain G3, appears to be dispensable for parasite P.berghei ookinete elimination which occurs by lysis (PubMed:31765430). Required for the melanization of Gram-positive and Gram-negative bacteria (PubMed:31765430, PubMed:33045027). Required for the melanization of fungus B.bassiana (PubMed:31765430). {ECO:0000269|PubMed:31765430, ECO:0000269|PubMed:33045027}.

Anopheles gambiae (African malaria mosquito)

A0A1S4H5S2

CLA8_ANOGA

MPSWWCCCCLVVLLYAQRMIVPSSAQNDGSDELQECPGGFCSPKYLCPNGTYNEANAQNQEIIMLRFGEEDVCQDYMQVCCSNATSMRYELVTNNEPVEYGCGISNPGGLIYQVEGNRTYAQYGEFPWVVAILEAFYSSNEQQFTYVGGGTLIHPRFVVTAAHIFNKTENLVASFGEWDMNRDENVYPKQNIDIDRTIIVHPEYNSVGLLNDIALAQLKQNVVYDKHIRPICLPNPTDRFDDQLCISTGWGIEALTSAYANVLKRVDLPVIARASCKKLFAETRLGPFFRLHKSVLCAGGEEGADMCDGDGGSGLACPNESGAYVLAGIVSWGLSCHQQNVPGAYVNVARFVTWINATIEGIL

defense response to bacterium [GO:0042742]; defense response to symbiont [GO:0140546]; innate immune response [GO:0045087]; positive regulation of melanization defense response [GO:0035008]; positive regulation of protein processing [GO:0010954]; proteolysis [GO:0006508]

extracellular space [GO:0005615]

serine-type endopeptidase activity [GO:0004252]

PF18322;PF00089;

2.40.10.10;

Peptidase S1 family, CLIP subfamily

PTM: Secreted as a full-length protein (PubMed:17537726). Proteolytically cleaved into two chains which remain covalently linked (PubMed:17537726). Cleavage is induced by Gram-positive or Gram-negative bacteria infection (PubMed:17537726). {ECO:0000269|PubMed:17537726}.

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17537726, ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph. {ECO:0000269|PubMed:17537726, ECO:0000269|PubMed:33045027}.

FUNCTION: Inactive serine protease which plays an essential role in the innate immune response against bacteria, fungi and protozoa infection by activating the melanization cascade (PubMed:16922859, PubMed:17537726, PubMed:23166497, PubMed:33045027). In the melanization cascade, acts downstream of TEP1 and SPCLIP1 to promote CLIPA28 and CLIPC9 proteolytic cleavage and CLIPC9 recruitment to microbial surfaces (PubMed:33045027). In the resistant strain L3-5, required for the melanization of killed parasite P.berghei ookinetes which results in their clearance (PubMed:16922859). In the susceptible strain G3, appears to be dispensable for ookinete elimination which occurs by lysis (PubMed:16922859, PubMed:33045027). Required for the melanization of Gram-positive and Gram-negative bacteria (PubMed:17537726). During the late stage of fungus B.bassiana-mediated infection, required for the initiation of hyphae melanization by promoting prophenoloxidase PPO activation (PubMed:23166497). {ECO:0000269|PubMed:16922859, ECO:0000269|PubMed:17537726, ECO:0000269|PubMed:23166497, ECO:0000269|PubMed:33045027}.

Anopheles gambiae (African malaria mosquito)

A0A1S4HE51

CLA30_ANOGA

MAFSLRIGIRTTDSKRCLVLLVLVVLLTVLACLPPSVEGNFPVGKFRRCNNNKGICVSREQCLNGQINTVGHTQIEPRLLNDDDIDECDVYGMQCCNLPSTNVPADSDEEEQEEEEKEKKGGTVTTTTTEEPDDPDWSRQCGQRTDVTERADQDGETNRFEFPWSVALFSKAQFFGKVRKEFLCGGTLIDDYLVLTAARCVNQKDRNTLVVQLGRWNLDAGKESRMQEIAVEELIIHRGYVLSSHLHNVALLVLANGAQLGRAANRVCLPDHSVQFGPDTLCYVVGWSNSPSPNTSNRQLKLRSMVAPVQECTATIRRSTGAWDFRLLSENICTTYLDDTVPCERAPGSGFVCESPTLPGQYFLVGIASYAVRQCHKYRAHDVFVHVPDYIEWVDGHVVNQSRQTSFYRPDPISFD

antibacterial innate immune response [GO:0140367]; defense response to bacterium [GO:0042742]; defense response to symbiont [GO:0140546]; positive regulation of melanin biosynthetic process [GO:0048023]; positive regulation of melanization defense response [GO:0035008]; positive regulation of protein processing [GO:0010954]; proteolysis [GO:0006508]

extracellular region [GO:0005576]; extracellular space [GO:0005615]

serine-type endopeptidase activity [GO:0004252]

PF18322;PF00089;

2.40.10.10;

Peptidase S1 family, CLIP subfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph. {ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:33045027}.

FUNCTION: Probable inactive serine protease which plays an essential role in the innate immune response against bacteria and protozoa infection by activating the melanization cascade (PubMed:24039584, PubMed:33045027). Binds to the surface of parasite P.berghei ookinetes and bacterium E.coli where it promotes the accumulation of mature TEP1 which leads to the melanization of the microbe (PubMed:24039584, PubMed:33045027). {ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:33045027}.

Anopheles gambiae (African malaria mosquito)

A0A1S4NYE3

CDIA_ECOST

MHQPPVRFPYRLLSYLISTIIAGQPLLPAVGAVITPQNGAGMDKAANGVPVVNIATPNGAGISHNRFTDYNVGKEGLILNNATGKLNPTQLGGLIQNNPNLKAGGEAKGIINEVTGGNRSLLQGYTEVAGKAANVMVANPYGITCDGCGFINTPRATLTTGRPVMNADGSLQALEVTEGSITINGAGLDGTRSDAVSIIARATEVNAALHAKDLTVTAGANRVTADGRVSALKGEGDVPKVAVDTGALGGMYARRIHLTSTESGVGVNLGNLYAREGDIILSSSGKLVLKNSLAGGNTTVTGTDVSLSGDNKAGGNLSVTGTTGLTLNQSRLVTDKNLVLSSSGQIVQNGGELTAGQNAMLSAQHLNQTSGAVNAAENVTLTTTGGITLKGRSVAGKTLTVSSGSLNNGGTLGAGRDATVKTGTFSNTGAVQGNGLKVTATDLTSTGSIKSGSTLDISARNATLSGDAGAKDSARVTVSGTLENRGRLVSDDVLTLSATQINNSGTLSGAKELVASADTLTTTEKSVTNSDGNLMLNSASSTLAGETSAGGTVSVKGNSLKTTTTAQTQGNSVSVDVQNAQLDGTQAARDILTLNASEKLTHSGKSSAPSLSLSAPELTSSGVLVASALNTQSQTLTNSGLLQGEASLTVNTQRLDNQQNGTLYSAADLTLDIPDIRNSGLITGDNGLTLNTASLSNPGKITADTLNVRATTLDGDGLLQGAAALALAGDTLSQGSHGRWLTAGDLSLRGKTLNTAGTTQGQNLTVQADRWANSGSVLATGNLTASATGQLTSTGDIMSQGDTTLNAATTDNRGSLLSAGTLSLDGNSLDNSGTVQGNHVTLHHRSTDNSGTVTGLSGLTLHSADGLTNSGALLSQNSLVLSAGDVTNSGRIQGQNITLDASSLTSSGAVQSALDLALTLSGDVIAATGSKITALGDARLTGKVLGNQGLISAKTLEVNGDSLSNSGEISGVNSLNVTLSGNLQQHGKMLTGGALNVNARDISNSGQLQGADNRITASSLANSGRVQGESGLTLTLLNALTNQTSGVLLSQNVSALSAPVLTNDGTIQGNGKTTLSAATQAHNSGKILSGGELTFTTPDYSGSGWLQATDLLLNVAKLAGNGTVMAANQATLTGNSLTNRGLFQAAQLNVNTQTITNSGTLLGNQGLTIKGNNLNNAGGKVFSGGDMLAEMVSLSGAGQLVALGNLTLKLTRGLTAQGVIAANKQLSVSSQGDITNGATLQGNGITLNAAGRLTNNGQLTAGNGTTALSGSGIAMNASGSLQAGGDVSLTSRGDITLDAFTGTTGSLMLTAAGAVINTALLYAGNNLSLFASTIRNHHGDMLAGDSLVMQKDVSGAANAEVINTSGNIETTRGDITIRTGHLLNQREGINETKSYIPVENVAVPDGANSVSVRVGDLGEDGWGYYVKSWSGTAGGGFDAWAVPTEKGATRKFLTGTTRVDVGATGGDARISAGNNLLIDADKLDNTGSHLLASGFVSLSGSQLNNQSFFGYTQDEYNVYRYYGKLAMIPNDGHLQYGDASADDRVTFTLSGAPEYVTRDTGQALRAVIQAGKNVTAVFSSDISNTSTTSNAGRITNTLAAPEINTPAEKNISPRMAQLAPDGTEMLTVTAPDWTDTITRLTIGSGTDLASGIVEGNYPLPSGNNGYFVPSADPDSPYLITVNPKLDGLGKVDSSLFAGLYDLLRMHPGQAPRETDPAYTDEKQFPGSSYFLDRLGLKPEKDYRFLGDAAFDTRYVSNYMLNQIGGRYINGVGSDTDQMRYLMDNAARAQKALGLKFGVALTADQVAALDQSILWYKAVTIKGQTVMVPEVYLSPKDVTLQNGSIISGQNVHLAGGNVTNSGSTLMAQNNLTIDSADSLGNLESGLINAGGALGLKAMGDINNISATITGKTVRLESLAGNVNNLTRYSHWQLDAPEDSLALKHTYTGSIASVSAMDSLDIRADKNISVTGAEISAGDRAALIAGNDLSLNAIDRVSSRRHANSESHQRSAGLTTITAGDSVMLSAGRDVSSQGAGIAAEDNITVRAGRDVNLLAEESVTGSSSYSKKKTVIDETVRQQGAEIASGGDTTITAGRDITAVASSVTATGNISVNAGRDVALTTATESDYHYLETKKKSGGFLSKKTTHTISENSATREAGALLSGNRVTVNAGDNLTVQGSDVVADRDVSLAAGNHVDVLAATSTDTSWRFKETKKSGLMGTGGIGFTIGSSKTTHDRREAGTTQSQSASTIGSTAGNVSITAGKQAHISGSDVIANRDISITGDSVVVDPGHDRRTVDEKFEQKKSGLTVALSGTVGSAINNAVTSAQETKESSDSRLKALQATKTALSGVQAGQAAAMATATGDPNATGVSLSLTTQKSKSQQHSESDTVSGSTLNAGNNLSVVATGKNRGDNRGDIVIAGSQLKAGGNTSLDAANDILLSGAANTQKTTGRNSSSGGGVGVSIGAGKGAGISVFASVNAAKGSEKGNGTEWTETTTDSGKTVTINSGRDTVLNGAQVNGNRIIADVGHDLLISSQQDTSKYDSKQTSVAAGGSFTFGSMTGSGYIAASRDKMKSRFDSVAEQTGMFAGDGGFDITVGRHTQLDGAVIASTATPDKNHLDTGTLGFSDLHNEADYKVSHSGISLSGGGSFGDKFQGNMPGGMISAGGHSGHAEGTTQAAVAEGTITIRDRDNQKQNPADLSRDPAHANDSISPIFDKEKEQRRLQTVGLISDIGSQVADIARTQGELNALKAAKEATGETLPANATEKQRQEYLAKLRDTPEYKKEQEKYGTGSEIQLGIQAATAALQGLAGGNLAGALAGASAPELAHLLKSTEKDPAVNAIAHAILGGAVAAMQGNNVAAGAAGAATGELAARAIAGMLYPGVKQSDLSEEQKQTISTLATVSAGLAGGLTGNSSASAAVGAQSGKNAVDNNYLSVSEKTELEIAKQTLKNSKNPAEREKAQQKYDALLEKDIASDKEVIAACGNGNAGSSACASARLKVIASKEGYEDGPYNSKYSQQYADAYGQIVNLLDITSVDVQNQQQVKDAMVSYFMATLGVDQKTAQGYVETTQGLEIAAASMTPLFGQAVANKITALVDKANKYPSGIGFKINQPEHLAQLDGYSQKKGISGAHNADVFNKAVVDNGVKIISETPTGVRGITQVQYEIPTKDAAGNTTGNYKGNGAKPFEKTIYDPKIFTDEKMLQLGQEAAAIGYSNAIKNGLQAYDAKAGGVTFRVYIDQKTGIVSNFHPK

3.1.-.-

COFACTOR: Note=tRNase activity is metal-independent. {ECO:0000269|PubMed:29923643};

extracellular region [GO:0005576]

endonuclease activity [GO:0004519]; toxin activity [GO:0090729]

PF21726;PF13332;PF04829;PF05860;

2.160.20.10;

CdiA toxin family; Bacterial EndoU family

PTM: The CT domain is cleaved upon binding to receptor Tsx on target cells. {ECO:0000269|PubMed:30388452}.

SUBCELLULAR LOCATION: Secreted {ECO:0000255}. Target cell, target cell cytoplasm {ECO:0000305|PubMed:30388452}. Note=Secreted to the cell surface by CdiB, its two partner secretion pathway (TPS) partner (Probable). Toxin translocation into the target cell depends on the proton motive force of the target cell, but not on tolA or tonB (By similarity). Forms filaments that extend about 33 nm away from the host cell surface; multiple filaments can be found on a single cell (PubMed:30388452). {ECO:0000250|UniProtKB:Q3YL96, ECO:0000269|PubMed:30388452}.

FUNCTION: Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring target bacteria in a contact-dependent fashion (target cell counts decrease 1000- to 10000-fold with this CDI) (PubMed:28351921, PubMed:29923643). Uses outer membrane nucleoside transporter Tsx on target cells as a receptor (PubMed:28351921). Gains access to the cytoplasm of target cells by using integral inner membrane protein PTS system glucose-specific EIICB component (ptsG) (Probable). Targeting of the C-terminal domain (CT) domain (residues 2931-3253) in the absence of immunity protein inhibits cell growth and causes tRNA(UUC-Glu) cleavage; expression of cognate immunity protein CdiI-STECO31 neutralizes growth inhibition leaving tRNA(UUC-Glu) is intact, whereas non-cognate immunity proteins do not confer protection (PubMed:29923643). The CT domain cleaves tRNA; it is most active against tRNA(UUC-Glu), but also has modest activity against tRNA(GUC-Asp), tRNA(UUG-Gln), tRNA(CCC-Gly), tRNA(UCC-Gly), tRNA(GCC-Gly), tRNA(UUU-Lys), tRNA(GGU-Thr) and tRNA(CCA-Trp); tRNA cleavage is inhibited by cognate immunity protein CdiI. Cleavage of tRNA(UUC-Glu) occurs in the anticodon loop between cytosine(37) and 2-methyladenosine(38) (C37-m2A38) and probably also occurs in the anticodon loop of other tRNAs as well (PubMed:29923643). {ECO:0000269|PubMed:28351921, ECO:0000269|PubMed:29923643, ECO:0000305|PubMed:28351921}.; FUNCTION: The CdiA protein is thought to be exported from the cell through the central lumen of CdiB, the other half of its two-partner system (TPS). The TPS domain probably remains associated with CdiB while the FHA-1 domain forms an extended filament (33 nm long) with the receptor-binding domain (RBD) at its extremity; in the secretion arrested state the C-terminus of the RBD and YP domains form a hairpin-like structure as the FHA-2, PT and CT domains are periplasmic. The YP domain is probably responsible for this arrest at the point where it re-enters the host cell periplasm. Upon binding to a target cell outer membrane receptor (Tsx for this CDI) a signal is transmitted to activate secretion. The filament becomes about 5 nm longer, the rest of CdiA is secreted and the FHA-2 domain becomes stably associated with the target cell's outer membrane where it facilitates entry of the toxic CT domain into the target cell periplasm. From there the toxic CT domain is cleaved and gains access to the target cell cytoplasm via an inner membrane protein (PTS system glucose-specific EIICB component, ptsG for this CDI). {ECO:0000305|PubMed:30388452}.

Escherichia coli (strain STEC_O31)

A0A1S5RW73

KPS_SALDI

MSFATSLPRPTTTGAAGFGLPLATCISLSVSHSFSPKFGICNNTSLRLKSKAGSGCYEGIHRSQLAASTILEGHTPINPEVESEKIRLIERIRLMFRSMDDGEISVSPYDTAWVALVEDIGGSGGPQFPTSLEWISNNQLDDGSWGDRKFVLYDRILNTLACVVALTTWKMHPNKCEKGLRFISDNIEKLADEDEELMPVGFEIALPSLIDLAKRLCIEIPDNSASIKNIYAKRDSKLKRIPMDLMHKKPTSLLFSLEGMEGLNWDKLLDFQSEGSFLSSPSSTAYALHHTKDELCLEYLLKAVKKFNGGVPNAYPVDMFEHLWSVDRLRRLGISRYFQVEIDECLDYVYRYWTNKGICWARNMCVQDSDDSSMGFRLLRLYGYDVSIDVFKQFEEGGQFCSIPGQMTHAITGMYNLYRASQLMFPQEHILADARNFTANLLHQKRVTNSIVDKWIITKDLPGEVAYALDVPFYASLPRLEARFFLEQYGGDDDVWIGKTLYRMLYVNCNTYLELAKLDYKHCQTVHQLEWNSMQTWYRECNLGEFGLSERSLLLAYYIAASTAFEPEKSSERLAWAITTILVETIMSQELSDEQKREFVDEFVNISIINNQNGGRYKPGNRLVEVLINTVTLMAEGRGTDQQLSNAWKNWLKTWEEGGDLGEAEARLLLHTIHLSSGLDESSFSHPKYQQLLEATSKVCHQLRLFQNLKANDAQGSTSRLVTVTTFQIEAGMQELVKLIFTKTLEDLTSATKQSFFNIARSFYYTAYCPADTIDSHINKVLFEKIV

5.5.1.28

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:28204567};

diterpenoid biosynthetic process [GO:0016102]; gibberellin biosynthetic process [GO:0009686]

chloroplast [GO:0009507]

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 = (-)-kolavenyl diphosphate; Xref=Rhea:RHEA:54684, ChEBI:CHEBI:58756, ChEBI:CHEBI:138310; EC=5.5.1.28; Evidence={ECO:0000269|PubMed:27865008, ECO:0000269|PubMed:28204567}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54685; Evidence={ECO:0000269|PubMed:27865008, ECO:0000269|PubMed:28204567};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 uM for geranylgeranyl diphosphate {ECO:0000269|PubMed:28204567}; Note=kcat is 0.88 sec(-1) with geranylgeranyl diphosphate as substrate. {ECO:0000269|PubMed:28204567};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:28204567};

FUNCTION: Involved in the biosynthesis of clerodane diterpenoids natural products, including salvinorin A with potent agonistic activity on brain kappa-opioid receptors, thus conferring hallucinogenic properties (PubMed:30468448). Diterpene synthase that catalyzes the formation of (-)-kolavenyl diphosphate from geranylgeranyl diphosphate (GGPP) as the first reaction in salvinorin A biosynthesis (PubMed:27865008, PubMed:28204567). {ECO:0000269|PubMed:27865008, ECO:0000269|PubMed:28204567, ECO:0000303|PubMed:30468448}.

Salvia divinorum (Maria pastora) (Diviner's sage)

A0A1S6M251

B4GT5_PIG

MRVRRGLLRLPRRSLLAALFFFSLSSSLLYFVYVAPGIVNTYLFMMQAQGILIRDNMRTIGAQVYEQVVRSAYAKRNSSVNDSDYPLDLNHSETFLQTTTFLPEDFTYFANHTCPERLPSMKGPIDINMSEIGMDTIHELFSKDPAIKLGGHWKPSDCVPRWKVAILIPFRNRHEHLPVLLRHLIPMLQRQRLQFAFYVVEQVGTQPFNRAMLFNVGFQEAMKDLDWDCLVFHDVDHIPENDRNYYGCGQMPRHFATKLDKYMYLLPYNEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGDTGKYKSIPYHHRGEVQFLGRYALLRKSKERQGLDGLNNLNYFANITYDALYKNITVNLTPELAQVTEY

2.4.1.-; 2.4.1.274

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UBX8};

carbohydrate metabolic process [GO:0005975]; central nervous system myelination [GO:0022010]; central nervous system neuron axonogenesis [GO:0021955]; ganglioside biosynthetic process via lactosylceramide [GO:0010706]; glycoprotein biosynthetic process [GO:0009101]; glycosylation [GO:0070085]; neuron maturation [GO:0042551]; positive regulation of embryonic development [GO:0040019]; protein glycosylation [GO:0006486]; regulation of protein stability [GO:0031647]

Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]

metal ion binding [GO:0046872]; UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity [GO:0008489]

PF02709;PF13733;

Glycosyltransferase 7 family

SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein. Golgi apparatus {ECO:0000269|PubMed:29546034}. Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}.

CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + UDP-alpha-D-galactose = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31495, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950, ChEBI:CHEBI:22801, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.274; Evidence={ECO:0000250|UniProtKB:Q9JMK0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31496; Evidence={ECO:0000250|UniProtKB:Q9JMK0};

PATHWAY: Protein modification; protein glycosylation.; PATHWAY: Sphingolipid metabolism.

FUNCTION: Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer) (By similarity). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation (By similarity). Plays a role in the glycosylation of BMPR1A and regulation of its protein stability (By similarity). Essential for extraembryonic development during early embryogenesis (By similarity). {ECO:0000250|UniProtKB:Q9JMK0}.; FUNCTION: (Microbial infection) May play a role in the glycosylation of porcine reproductive and respiratory syndrome virus GP5 protein and may be involved in the regulation of viral proliferation. {ECO:0000269|PubMed:29546034}.

Sus scrofa (Pig)

A0A1S7LCW6

MAMP_MAGMO

MKLKGTTIVALGMLVVAIMVLASMIDLPGSDMSATPAPPDTPRGAPIVGGQGQAMGLPVAMQRRRGEQRAPVPALSDANGGFVAPNVQFSEAHWQGMEALPLSIELKRKLKLPLDLEGLLIDETSLNAAVSGLLAGDVLVAINGRKVKTLKKMQKETRRVQMDRRASLTVYRKGRLLTLTLSEEKNLGLAQVETAPMILPGDIMPHPYRGPCTQCHAIGTTGHITPDPDGIVLPPGPIRAGAKMPHRDRGPCAACHAIIQ

1.-.-.-

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:24097349}; Note=Binds 2 heme groups via the magnetochrome (MCR) motifs. {ECO:0000269|PubMed:24097349};

plasma membrane [GO:0005886]

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

PF18509;PF13180;

2.30.42.60;

Magnetosome MamP family

PTM: Subject to proteolytic cleavage which requires both MamE and MamO. {ECO:0000250|UniProtKB:Q2W8Q1}.

SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:Q2W8Q1}; Single-pass membrane protein {ECO:0000305|PubMed:24097349}. Note=Not seen in magnetosome membranes. {ECO:0000250|UniProtKB:Q2W8Q1}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 for oxidation of Fe(2+). {ECO:0000269|PubMed:24097349};

FUNCTION: Oxidizes Fe(2+) at alkaline pH; successively forms ferrihydrite (Fe(3+)(2)O(3) 0.5 H(2)O) then magnetite (Fe(3)O(4)) from an Fe(2+) solution. {ECO:0000269|PubMed:24097349}.

Magnetococcus massalia (strain MO-1)

A0A1U8F5V2

IFI4E_CAPAN

MATEAPPPVDTTEVPPFTAAETAVKQPHKLERKWTFWFDNQSKPKQGAAWGSSLKKAYTFDTVEEFWSLYDQIFKPSKLTVNADFHLFKAGIEPKWEDPECANGGKWTVTSSRKANLETMWLETLMALVGEQFDDSEDICGVVASVRRSQDKLSLWTKTATNEAAQMGIGRKWKEIIDTEKISYSFHDDSKRERSAKSRYTV

negative regulation of defense response to virus [GO:0050687]; response to virus [GO:0009615]

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

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

PF01652;

3.30.760.10;

Eukaryotic initiation factor 4E family

PTM: According to the redox status, the Cys-101-Cys-140 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A445AGS0}. Nucleus {ECO:0000250|UniProtKB:A0A445AGS0}.

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:16760413, PubMed:21073716). {ECO:0000250|UniProtKB:O04663, ECO:0000250|UniProtKB:P29557, ECO:0000269|PubMed:16760413, ECO:0000269|PubMed:21073716}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000269|PubMed:16760413, ECO:0000269|PubMed:21073716}.

Capsicum annuum (Capsicum pepper)

A0A1U8GR65

IF4E1_CAPAN

MATAEMEKTTTFDEAEKVKLNANEADDEVEEGEIVEETDDTTSYLSKEIATKHPLEHSWTFWFDNPVAKSKQAAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLVVGADLHCFKHKIEPKWEDPVCANGGTWKMSFSKGKSDTSWLYTLLAMIGHQFDHEDEICGAVVSVRGKGEKISLWTKNAANETAQVSIGKQWKQFLDYSDSVGFIFHDDAKRLDRNAKNRYTV

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-126-Cys-164 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}.

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 (PubMed:18182024). 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 (PubMed:18182024). Key component of recessive resistance to potyviruses (PubMed:12492847, PubMed:15842624, PubMed:15971038, PubMed:16760413, PubMed:18182024, PubMed:21073716). {ECO:0000269|PubMed:12492847, ECO:0000269|PubMed:15842624, ECO:0000269|PubMed:15971038, ECO:0000269|PubMed:16760413, ECO:0000269|PubMed:18182024, ECO:0000269|PubMed:21073716}.; 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:12492847, ECO:0000269|PubMed:15842624, ECO:0000269|PubMed:15971038, ECO:0000269|PubMed:16760413, ECO:0000269|PubMed:18182024, ECO:0000269|PubMed:21073716}.

Capsicum annuum (Capsicum pepper)

A0A1U8QK63

PKIC_EMENI

MALEEVPSVSRDLDHSALRALSSASPSSLPSSCSRSTTSLLFQSKGIEFRLSIPDTFLSLVEPHRNAFLASYSTQGNTQSPLELALSFLYFLLDQKVSPLVLSSVLRAFNLEFLGNRSEIHSLIADLTPIPKQRQRWLGIYYRFLEASDDKRAEIPLSSIFQHARTNEFQLMAVFGGQGECSRTCLNEFAELYSSYEPMLRRLVGVIGPCLYNLSTSDEYSSYYRNQPLDLKAWITDENHVPDLGFVASAPVSVPVIGALSLARYCVTCHITGCNPGLMRSMLRTATGHSQGLLAAIVVAVSHSWDSFYQATEEVIELLFRLGWECHHAAPCSMVPAANYADVDGANGPSYMLSLRGLKRQETEATIDHVNASLPEDKRLYLALINAYDQFVVAGPVASLLRLESHLVEITSKDIDQSRIPFRDRKPYIQHSFLPVSTPFHTPYLTRAAARVKKQFAARPIPTRRLAIPVYHTHTGLDLRKQGGCALSIAIDAIASEPCNWPCAVASYHASHILTFDRGGLAPLIKRVREGCGVRVVQVADLDTRDSEMATMRDLFATKLLPTSTKLQSWGQQFRPGLASGPKIQLETRLNRVLGAPPIMVAGMTPTTVHPDFVAAIMNAGYHAELAGGGYHNASAMEAAIYDLVSSIPKERGITCNLIYANPRSISWQIELLRRLSNGNVRIDGLTIGAGVPSLTVASEYIETLGLRHISFKPGSVAAIRKVVEIAREHPDFPVILQWTGGRGGGHHSFEDFHAPIIATYGIIRQEPNVYLVAGSGFGDSDSVYPYLTGSWSVAMGHPAMPFDGILLGSRMMVAKEAHTSPAVRRIIAATPGVSDSEWEKTYSGPAGGVITVTSEMGEPIHKIATRGVCLWADLDKTVFSLSRRDRLTYLAQHRRSIIQRLNADFAKPWFGCNSDGEAVDLEDMTYLEVLKRLTALMFVPNKQWIDASYIEFTMTIAQRWLQRLQFDSEAAASLTISLLRKAPDRFLAIFADVCPTAEGDLLNPEDISFFLMQCKTPGRKPVNFIPALDDDFEFYFKKDSLWQAEDVDAVLDQDAERVCILHGPIAARYSKSDSEPAGYILDSILNGVVARLRETSTAEMLLPKLERGHTTPASWSTLSLTERDTSEETSDTSITSLSELIENHSFSSGGVDSVPRPSHPLWMRALLEDDVVLQGTLRQKNPFRDLIQSSPNTVVNYNQDSSELMVTAQEPYHISSFMRAVCHDGVMDKRNERIKSFYSLLWFGHDCDTSQSLNGVFYGPDITLTEDLLDEYNATIGPAYSDHRQMVPSTDVLPISMGIIIAWDVISRPLILRQIGGDLLRLVHRSNTFEYYSDTRLRLGDSVSSRSEVQAVYDDDGGRVVIVEAQILRSRVPVMTVTSTFLFRGSKGTTVPAFRRAREQKWTYDVTSEFEESILLSRNWFRPCDPSLTLVGKSMIFDLNSLVKYHDDGNMELHVQGTAMSQTNGQQQKLAIVDFRNTCTGNPVLDFLQRRGKLAEPRTEFKIPGWAGKSTMDIQMPPSNEPYAQLSKDFNPIHTSPIFSSLAGVPGTLCHGMCTSAIAERVLEHLGLGGDRERLRRFEARFTDMVMPLEKLVVEIKHTGMVDGRMCFSILAKRKETDERVLEGDAEVEQPRTAYLFTGQGSQSKGMGMDLYKTSTGQFLLTNKGGLFWTSCKTTQSPLPIRQKYLDITTEVVLPNGKRVQKPVFPGLTPTSTSYTFRHPRGLLYSTQFAQPAILLFEAAAFAELRAKGYVSHGAVYAGHSLGEFGALSALSRSVPTGALVELAFYRGSVMQASVASDNDGGTTYGMVAMNPKRVGTFFTQTTLDRLVSQIAAQSQELLEIVNFNIEGEQYVCSGTIDRPISGGTWPSLSG

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]; fatty-acyl-CoA synthase activity [GO:0004321]

PF00698;PF08354;PF13452;PF01575;PF16073;

1.20.1050.120;1.20.930.70;3.30.1120.100;3.30.70.3320;6.10.60.10;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:P07149}; 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:P07149}; 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:P07149}; 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:P07149}; 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:P07149}; 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:P07149};

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:22510154}.

FUNCTION: Fatty acid synthase beta subunit; part of the pki gene cluster that mediates the biosynthesis of 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde (PubMed:22510154). The first step in the pathway is the generation of the decanoyl starter unit by the FAS composed of subunits pkiB and pkiC, which is then transferred directly from the FAS to the SAT domain of the non-reducing polyketide synthase pkiA (PubMed:22510154). PkiA condenses the decanoyyl starter unit with 4 malonyl-CoA units and performs one methylation step to yield 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde (PubMed:22510154). {ECO:0000269|PubMed:22510154}.

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

A0A1U8QLG8

PBCB_EMENI

MSPPLDSALEPLSEYKETAFPRTEKDPSQYKEHDLVTPEKEIQTGYFSPRGSHSSHGSHDSSASSNISLDDARMSDVNNSPNVFHDDPDTIDEKLSMYWKAANETVIREPYDYIAGIPGKEIRRKLLEAFNHWYKVDEQSCQAIATTVGMAHNASLLIDDIQDSSKLRRGVPCAHEVFGIAQTINSANYVYFLAQNQLFRLRSWPQAISVFNEEMVNLHRGQGMELFWRDNLLPPSMDDYLQMIANKTGGLFRMIVRLLQTSSRQVIDVEQLVDVLGLYFQILDDYKNIREEKMAAQKGFFEDLTEGKFSFPICHAIGEGAKNRTALLHMLRLKTDDMKIKQEAVCILDNAGSLDYTREVLYGLDRKARSLLREFKTPNPFMEALLDAMLSSLQACH

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]; mycotoxin biosynthetic process [GO:0043386]; plastoquinone biosynthetic process [GO:0010236]; terpenoid biosynthetic process [GO:0016114]; ubiquinone biosynthetic process [GO:0006744]

mitochondrion [GO:0005739]; transferase complex [GO:1990234]

dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659]

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; terpenoid biosynthesis. {ECO:0000305|PubMed:22506079}.

FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) (PubMed:22506079, PubMed:27098256). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors (PubMed:22506079, PubMed:27098256). The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes (PubMed:22506079, PubMed:27098256). Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene (PubMed:22506079, PubMed:27098256). The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable). {ECO:0000269|PubMed:22506079, ECO:0000269|PubMed:27098256, ECO:0000305|PubMed:22506079}.

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

A0A1U8QNG8

HXNS_EMENI

MDALLPRSSPQLKFYLNGTPISLTSPHPRWTLLDFIRSQDGLKGTKLGCGEGGCGALSGKHVITIEGLGTVDHPHPLQERIAQLHGSQCGFCTPGIVMSLYAMIRNAYDPVTGKFQLSADDIESKGHLDGNLCRCTGYKPILNAARTFIEDDLGSVPSIVESELVGTEEETESDMGAHSGSGDTGSRSSGSCGRPGGCCKDSPGISSCSSRETDMTTPSLPDSPVLKQYDFIPYTPTTELIYPPGLAKFVPELLCYGDAEQAWVKPRSVQEALEILSQCPSATLVTGASEVQVDVRFKDFRPSVSVFVGDITEMTGISWSEDMKTLYIGGSASLSDIEAECLRCIPLLKAVNLGSESVLSAIARTLRYFAGRQIRNAACLAGNIATASPISDMNPLLLAVGATVHARTSAEETTIPMSEMFKGYRKTALPSGSLITKIAVPMPSKDQIEIVNAYKQAKRKDDDIAIVTAAFRVRIAPGPDYTVQEASLAFGGMAPTTVLAHKTASALEGKRWGDEAVLDIVLTSLGEEFNLPYSVPGGMATYRRTLTLSLFVRFWNYVNQKLGLEYDSDLIEEIHRGISTGTRDDDNPHAQRVVGQQIPHLSGLKHATGEAEYVDDMPPLHRELHGALVLSERAHAKILSVNWTPALERGAVGYVDHTSLPEEKNHWGPVVHDEPVFAKGEVHAHGQPIGLVYADDAMTAQIAAKAVIVTYEDLPAILTIDEAIEARSFFNYGKELRRGAPPEEIRKELDDCEYTLSGTTKIGGQEHFYLETNAAIAVPHTEDGSMDVWSSTQNTMETQDFLSQVTNVPRHKINARVRRMGGAFGGKESRSVPIACIVAVAAKKARRPVRIMLNRDEDMMTSGQRHPVQCRWKVGFNREGKLLVLDADTYNNAGYSVDMSAAVMDRCLTHIENCYYIPNVWLRGWVCKTNTHSNTAFRGFGAPQAMYITESIISAVAEKVGIDVDEIRRRNLYQVGQRTPFNQVLDEDWHVPLLLEQVREEADYDARKKEIERFNSEHRWRKRGIALIPTKFGISFATALHLNQASAAVRVYTDGSVLLNHGGTEMGQGLYTKMVQVAAQELRVPVDQVYTQDTSSYQTANASPTAASSGSDLNGMAIKHACDQINERLRPYREKYGEDADLGTIAKAAYRDRVNLSAAGYYKMPTIGYEWGNYSENVKPMYFYFTQRQGVACTEVELDLLTGTHTVLRADLKMDIGRSINPAIDYGQIEGAFVQGQGLFTMEESLWTRSGQLATRGPGTYKIPGFADIPQVFNSSKGIGEPPLFMGSSVLFALRDALSHARRERGVSEPLVLDSPATVERLRLAVGDDLVHRAQVQRKDGEQGFFVAVA

1.-.-.-

COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:P80457}; Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250|UniProtKB:P80457}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P80457}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250|UniProtKB:P80457}; Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. {ECO:0000250|UniProtKB:P80457};

2 iron, 2 sulfur cluster binding [GO:0051537]; FAD binding [GO:0071949]; iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; xanthine dehydrogenase activity [GO:0004854]

PF01315;PF03450;PF00941;PF01799;PF02738;PF20256;

3.10.20.30;3.30.465.10;1.10.150.120;3.90.1170.50;3.30.365.10;3.30.390.50;3.30.43.10;

Xanthine dehydrogenase family

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=90.4 uM for hypoxanthine {ECO:0000269|PubMed:363427}; KM=36.15 uM for 2-hydroxypurine {ECO:0000269|PubMed:363427}; KM=524.5 uM for 6,8-dihydroxypurine {ECO:0000269|PubMed:363427}; KM=188.6 uM for nicotinate {ECO:0000269|PubMed:363427};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.4. {ECO:0000269|PubMed:363427};

FUNCTION: Nicotinate hydroxylase, part of the hnx cluster involved in the purine degradation (PubMed:4581274). The nicotinate hydroxylase hnxS accepts nicotinate as a substrate and catalyzes the first step of nicotinate catabolism (PubMed:4581274). HnxS accepts also hypoxanthine, but not xanthine, as a substrate (PubMed:29212709, PubMed:363427, PubMed:4581274). The major facilitator-type transporters hxnP and hxnZ are probably involved in the uptake of nicotinate-derived metabolites, and the oxidoreductases hxnT and hxnY in the further metabolism of 6-OH nicotinic acid (PubMed:4581274). {ECO:0000269|PubMed:29212709, ECO:0000269|PubMed:363427, ECO:0000269|PubMed:4581274}.

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

A0A1U8QWA2

ATR12_EMENI

MAIIDTTKDLSALFTQQVRASPNALALEDDKTSYTYAELDKEVEELSRRLRSYGVSRDSLVGVLLPRSAHFVIACLAALRAGGAFLVLELAYPPDLLADVLEDATPAVVVTHRSETGKIKGSVPVISLDEPPVDANGHTVEPGPLPVDDDLDRLAFVSYSSGTTGKPKGIANPHRAPVLSYNLRFGVQDLQPGDRVACNVFFIWEILRPLIRGATVVAVPDDHSYDPAALVDLLASRHITETLMTPTLLATILSRHSDIGARLPELRTLWLNGEVVTTDLARRAIRALPNTRLLNCYSACETHEIACGDIKEIVSDESQYCPVGPLLDPKHAYIVNEQGEKVEEGVSGELCVGGPMLARGYINRPETTAKAFIPDPFSNSPGAVMYRTGDRARMLPSGLLEITGRVGAMIKLRGYSVVPGKVENDIVKHLAVRQCAVVAHGEGLERQLVAYIVADQEHSEERPTVEINSSGHSPGARRALTKFLAHYMIPALWVQVDELPTHEVSGKIDLKRLPPPPTEVLANGNGKKEDPIGIEDIAAIWAVALKVPKATLKPEDNFFDLGGHSLSIADLSSRLSRKFGFRIPIVRLAENSTLSGHLDTVRAIRDGHTAAVQADLPAVLRTDATLDEEIRSDAKICSLTDAKTVLLTGVTGFLGAFLLKDLVDSTSAHIICLVRFNEPEDDDQPGGVARIRRNLLDLGLWNDSIMERVEILPGNLSRSRFGLTPDAFQELAQRVDVIVHAAASVNLVYPYAALRAANVGGTREILRLASQGGATVQYVSTNGVLPPSGEKGWPEDTMLDMKDVPTKLLDGYGQTKWVAEQLVLEAGRRGLPVRVHRIGTVSGHSQSGAANAWDLLTALIVESIKLGKYPDVEGWRAEMTPVDFVSKAIIHLANQTAVEQTVFHIGDPDPVNTRSVFEDLKTLGYPTEPLSWDDWVALWTSQRGHVKGGDGGFTVDILRSGMPSIEFLRGIVVLDNSATRPIRREVERPKVDRFLLETYTRHWFARGWLKRPPIRQRQLSPIPKGPLSGKVAVVTGASSGIGAAVATALAREGAHVALGARRLDALESLKEKLSASGVKVVTCKTDVTDRKQVEGLVKAATEELGPVDILVACAGVMYFTMMANTQMDEWERTVDVNCKGILNSLASTVPGMLARGKGHVVAISSDAGRKVFPGLGVYSASKFFVEATLQALRLETAGQGLRVTAVQPGNTATDLLGMSTDAEAIKKYGEPSGAQILDPEDVANSIIYALRQPEHVAMNEILIEPRDEPI

1.1.1.-; 1.2.1.-

organonitrogen compound biosynthetic process [GO:1901566]; secondary metabolite biosynthetic process [GO:0044550]

oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]

PF00106;PF00501;PF07993;PF00550;

3.30.300.30;1.10.1200.10;3.40.50.12780;3.40.50.720;

NRP synthetase family

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.1 mM for glycine betaine {ECO:0000269|PubMed:31061132}; KM=0.24 mM for glycine betaine aldehyde {ECO:0000269|PubMed:31061132}; KM=5.8 mM for N,N-dimethylglycine {ECO:0000269|PubMed:31061132}; KM=90 mM for 3,3,-dimethylbutyraldehyde (for the aldehyde reductase R2 domain alone) {ECO:0000269|PubMed:31061132};

FUNCTION: NRPS-like enzyme with an unusual domain architecture that converts back glycine betaine to choline via a 2-step reduction mechanism, and thereby can be an alternative source of choline (PubMed:31061132). Permits direct reutilization of endogenously stored glycine betaine for on-demand biosynthesis of choline and choline derivatives, including phospholipid phosphatidylcholine (PC) which has an essential role in maintaining membrane integrity and functionality, or choline-O-sulfate, a mean for intracellular sulfate storage (PubMed:31061132). Glycine betaine is activated by the adenylation (A) domain, and transferred to the thiolation (T) domain (PubMed:31061132). Movement of the phosphopantetheine arm to the thioester reductase domain R1 then allows thioester reduction by NADPH of glycine betainoyl thioester to glycine betaine aldehyde, which is in turn reduced to choline by the aldehyde reductase domain R2 (PubMed:31061132). {ECO:0000269|PubMed:31061132}.

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

A0A1V0E492

TPS1_PIPNI

MACVSDLVAFTQPLIIGAKPLEIVRRSAAFHPNVWGDYFLKLSQDEKKLESMRERAKVLKEKVLKKLSTIEGGERLELIDTLYHLGVAYNFEKEIEEALEKIYKAYDEDATQDNLCTLALRFRLLRQHGWNASSDVFNKFKETKNGNFKESVASDVLGMLSLYEASYVGTKEDKILEEAISFTTRNLSAALPNMEPLLAERVAHSLELPLHKRLQRLEARYFITMYEKNNAHDEMLLEYAKLDYNLLQALHQNEMKELTKWWTKIDLVGKMKFPRDRVTECYFWPLGAFFEPQHSRGRIFATKITQLTSIIDDLYDVYGTQEELQLFTDVIQRWDMNAKKSLPDYIKPLYEALLSTLKDFEEELSLEGNAYRASFMQQAMKNICMAYFDEAKWYNRGTTPKVEEYLNSAEISCGYPVVATACFTGAGEITTKKLLEWIQSQPKYMKDTCRLCRIVDDIKTYKFEEERGHVASVVACYMEEHKCNEDEALEKLNEDVMNTWKDINKACMRPTPFPMVVMNIIRNLSRVMEILYQFGDGYTFADTVTKERLNLLLKDPIPV

4.2.3.104; 4.2.3.57

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};

beta-caryophyllene biosynthetic process [GO:1901937]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; sesquiterpene biosynthetic process [GO:0051762]

alpha-humulene synthase activity [GO:0080017]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]

PF01397;PF03936;

1.10.600.10;1.50.10.130;

Terpene synthase family, Tpsa subfamily

CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene + diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295; Evidence={ECO:0000269|PubMed:29248443}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate; Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.104; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896; Evidence={ECO:0000269|PubMed:29248443};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21 uM for (2E,6E)-farnesyl diphosphate {ECO:0000269|PubMed:29248443}; Note=kcat is 0.455 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate. {ECO:0000269|PubMed:29248443};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:29248443}.

FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds that contribute to the characteristic flavors of black pepper (PubMed:29248443). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into beta-caryophyllene and, as a minor compound, into alpha-humulene (PubMed:29248443). {ECO:0000269|PubMed:29248443}.

Piper nigrum (Black pepper)

A0A1V0E4A6

TPS2_PIPNI

MDAVSCAINALSAQAPPKHLGGNNVGRKSVTFPKDIWGDYFLKISPNEEKLDSWRVRAKELKEKVFDILSCAKGAEQVHIIDALYHLGVSYQFEKEIEEALKNMLTTYNDDTSTEDDLYTLALRFRLLRQNGFHASTKALNKFKDAHGSFREDLASDVMGLLSLYEASYAGTVDDLILDEALAFTKIHLKAALPHLDSHLAQRVSHSLELPLHKRIQRLEAREFISLCEKDDSIVIKELLEFAKLDYNILQALHQWELKELTKWWKKLNLVGKMTFARDRMTEIYFYVSGFFFEPQYSRGRIISSKILAICSVVDDEYDVYGTLDELQVFTDAICRLDVAAMENLPEYVKPLYEAIFFSLKEFEEELAREGNAYRVNYLREEVKNLCKSYLQETKWLHQRYIPTLEEYLLVSEISSTYTVIFNGCFVGCGEIATKEVFEWFQAFPKLLSDSARIGRIADDIMSCKFEQSRGHCPSAVECCMEEHQCTKEVALGNLDGVLGRAWKDMNKACMRPTPFPMEVLRPIVNLARMAEISYQYEDGYTFSGGKTKERISMLYKDPIPV

4.2.3.-

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};

cadinene biosynthetic process [GO:1901928]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; sesquiterpene biosynthetic process [GO:0051762]

(+)-delta-cadinene synthase activity [GO:0047461]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]

PF01397;PF03936;

1.10.600.10;1.50.10.130;

Terpene synthase family, Tpsa subfamily

CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate; Xref=Rhea:RHEA:56556, ChEBI:CHEBI:33019, ChEBI:CHEBI:140564, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56557; Evidence={ECO:0000269|PubMed:29248443}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = alpha-cadinene + diphosphate; Xref=Rhea:RHEA:69444, ChEBI:CHEBI:33019, ChEBI:CHEBI:80749, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69445; Evidence={ECO:0000269|PubMed:29248443}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + H2O = (-)-delta-cadinol + diphosphate; Xref=Rhea:RHEA:69448, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:156223, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69449; Evidence={ECO:0000269|PubMed:29248443};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18.4 uM for (2E,6E)-farnesyl diphosphate {ECO:0000269|PubMed:29248443}; Note=kcat is 0.694 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate. {ECO:0000269|PubMed:29248443};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:29248443}.

FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds that contribute to the characteristic flavors of black pepper (PubMed:29248443). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into alpha-cadinene, delta-cadinene and delta-cadinol (PubMed:29248443). {ECO:0000269|PubMed:29248443}.

Piper nigrum (Black pepper)

A0A1V0QSA8

ERIE_HERER

MSAPINGTVEKSYVPGAELWCQEDETAITEPYTYVNSMPGKDVRGRFIEAANHWLHVEPEPLAVICKIVAMLHNASLVIDDIEDNSQLRRGQPVAHKIYGLAQAINSANYVYFLALKEADQLKPYQREGYNSHEIILGALTSVSDFAAQDLLYSVFSDELVNLHRGQGLELVWRDSLRCPTEEQYIDMVNKKTGGLFRLAIKLLTACSSNPSTIDYVPLFNLFGVFFQIRDDLMNLDDNEYEKNKGFAEDLTEGKFSFPVIHGITAQKDNSVLINVLQKRPTTPPLKLHAIHHLRNNTGSFKYTETILNSLETRLRGEIDALGGNPGLLKLVDLLSVRK

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};

isoprenoid biosynthetic process [GO:0008299]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744]

mitochondrion [GO:0005739]; transferase complex [GO:1990234]

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:31535864}.

FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of erinacines, cyathane-xylosides that show unique biological activities, including leishmanicidal activity, stimulating activity for nerve growth-factor synthesis, and agonistic activity toward the kappa opioid receptor (PubMed:28371074, PubMed:31535864). The geranylgeranyl diphosphate (GGPP) synthase eriE catalyzes the first step in erinacines biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (By similarity). GGPP is then substrate of the diterpene cyclase eriG for the production of cyatha-3,12-diene. The cytochrome P450 monooxygenase eriI then hydroxylates cyatha-3,12-diene at C-14 of the seven-membered ring to produce erinacol, which is further hydroxylated at C-15 by the cytochrome P450 monooxygenase eriC to yield cyathadiol. The cytochrome P450 monooxygenase eriA then catalyzes C-11 hydroxylation in the presence of the short chain dehydrogenase/reductase (SDR) eriH, which leads to the production of cyathatriol. The acetyltransferase eriL converts cyathatriol into 11-O-acetyl-cyathatriol. The SDR eriH catalyzes further oxidation of 11-O-acetyl-cyathatriol into 1-O-acetylcyathin A3. Finally, the glycosyl transferase eriJ tranfers xylose from UDP-xylose onto C-14 of 11-O-acetyl-cyathatriol to form eracine Q. EriJ is also able to convert 11-O-acetyl-cyathatriol to eracine Q2 by using UDP-D-glucose as cosubstrate, but at a lower rate. In the absence of eriL and eriJ, the SDR eriH is able to convert cyathatriol to cyathin A3; this is likely a switching mechanism in the biosynthesis of cyathins (C-14 ketogroup)and erinacines (C-14 glycosylated group). The roles of the SDR eriB, the polyprenyl transferase eriF and the dehydrogenase eriK have still to be identified (Probable). {ECO:0000250|UniProtKB:Q12051, ECO:0000269|PubMed:28371074, ECO:0000269|PubMed:31535864, ECO:0000305|PubMed:31535864}.

Hericium erinaceus (Lion's mane mushroom) (Hydnum erinaceus)

A0A1W2P872

NOVA2_MOUSE

MEPEAPDSRKRPLETPPEVVCTKRSNTGEEGEYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKSKDFYPGTTERVCLVQGTAEALNAVHSFIAEKVREIPQAMTKPEVVNILQPQTTMNPDRAKQAKLIVPNSTAGLIIGKGGATVKAVMEQSGAWVQLSQKPEGINLQERVVTVSGEPEQVHKAVSAIVQKVQEDPQSSSCLNISYANVAGPVANSNPTGSPYASPADVLPAAAAASAAAASGLLGPAGLAGVGAFPAALPAFSGTDLLAISTALNTLASYGYNTNSLSLGLNSAAASGVLAAVAAGANPAAAAAANLLASYAGDAGAGPGAGAAPPPPPPPGALGSFALAAAANGYLGAGAGGAAGAGGAPLVAAAAAAGAAGGFLTAEKLAAESAKELVEIAVPENLVGAILGKGGKTLVEYQELTGARIQISKKGEFLPGTRNRRVTITGSPAATQAAQYLISQRVTYEQGVRASNPQKVG

central nervous system neuron development [GO:0021954]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of cold-induced thermogenesis [GO:0120163]; neuron differentiation [GO:0030182]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of axon guidance [GO:1902667]; regulation of RNA metabolic process [GO:0051252]

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

mRNA binding [GO:0003729]; RNA binding [GO:0003723]; sequence-specific mRNA binding [GO:1990825]

PF00013;

3.30.1370.10;

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30638744}.

FUNCTION: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion or exclusion. It binds specifically to the sequences 5'-YCAY-3' and regulates splicing in only a subset of regulated exons (PubMed:14615540). Binding to an exonic 5'-YCAY-3' cluster changes the protein complexes assembled on pre-mRNA, blocking U1 snRNP binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhances spliceosome assembly and exon inclusion (PubMed:16041372). With NOVA1, they perform unique biological functions in different brain areas and cell types. Uniquely regulates alternative splicing events of a series of axon guidance related genes during cortical development, being essential for central nervous system development by regulating neural networks wiring (PubMed:16041372, PubMed:27223325). Regulates differentially alternative splicing on the same transcripts expressed in different neurons. This includes functional differences in transcripts expressed in cortical and cerebellar excitatory versus inhibitory neurons where is required for, respectively, development of laminar structure and motor coordination and synapse formation. Also the regulation the regulation of intron retention can sequester the trans-acting splicing factor PTBP2, acting as a variable cis-acting scaffolding platform for PTBP2 across various natural conditions (PubMed:30638744). {ECO:0000269|PubMed:14615540, ECO:0000269|PubMed:16041372, ECO:0000269|PubMed:27223325, ECO:0000269|PubMed:30638744}.

Mus musculus (Mouse)

A0A1W5T1U1

POXE_PENOX

MAPSQAPREPIAIVGSGCRFPGESSSPSKLWELLQAPRDVQTEIPPTRFNPHGFYHPDNLHHGTSNVRHSYLLTEDHRHFDAQFFGIKPAEAHCIDPQQRLLMETVYESLESAGLRLEDLRGSETAVYVGLMCGDYADIVLRDPESFPMYLSTGTARSIMSNRISYFFDWHGPSMTIDTACSSSLVAVHEAVQTLRLGRSRVAVAAGSNLCLSPEPYIAESKLQMLSPTGRSRMWDIQADGYARGDGVAAVVLKTLSAALADGDHIECLIRETSVNQDGRTRGITMPSSEAQTRLIQDTYARAGLDPLKPQERCQYFEAHGTGTPTGDPLEAAAIRQAFFPGDNNQDRGCLFVGSIKTVVGHTEGTAGLAGVLKASLALRNGIIPPNLLFNQLNPKIKPFYTNLEIATAAKPWPVLPAGVPRRASVNSFGFGGTNAHAIIEAYEPALTAPSKSTEPDIAFIPFVFSAASESALRRMLELYAQHLSKNPTINARDLGWTLQARRSRFPFSIAVPGATTDQLRSNLETRLNSTDARQPLKIVKQESRPENPRILGVFTGQGAQWATMGRALYQSPKVRQIIQELDASLQALPVGERPSWTLASELTADASVSRIKAAEISQPMCTAVQVVLVQLLQSAGVVFDAVVGHSSGEIAAAYAAGFLSGTDAIRIAYYRGLCARLAQGAHGEKGAMMAVGTGVEDALELCAEPEFRGRMSVAAVNSSASVTLSGDADAITQAKEILDEEKKFARVLVVDKAYHSHHMQACSGRYLSCLAKARIAVSAPTDTKCVWYSTVRQGPVTEADLADLTGPYWNDNMVSPVLFAQAVETALAARGPFNMAVEVGPHPALRGPAQQTVQDVLETSLPYTPTLQRGMNDVEAMAECLGLLWQGLAPGFVDLSSYDAFLSQGAVSRVIKDLPRYSWDHDRVFWYESRVSRATRQRIAASHPILGTRCPDGVEQEFRWRNFLSLKELPWLTGHRIQGQIIFPGAGYISAAVDSARAMSSNESIQLVELQELLIRQAIVFEDENASVEILVSITDVTHHSKDMVRAQFSFYSAVGKESTQMTLNASGRLVITYGPVRKDALPVQRPSLVDMVDVPSERFYNALDPLGYSYTGRFRALKSMQRKLGIATGLVTRQEAADLSSVTLDPAMLDAAIQAVLLAKSFPGDGELWCSQVPKVIHRIAVNPTLCDPSGNGVESTFPLDAVLTMMKASDTQGDVDVYSADGQYTMIRMEGIHAVPLEATNADRDRPFFSGVVWGPAAPDSQTVNFDATATPEEYELAYVLERVATFYLRKIHLAFPMDHSARHEGPYVGLLNYATYVTQQVASGYHRYTQPHWARDTVAVIKSESQRFPNNIDLAVMHIIGEHMVDVISTRATILEHLTKDNLLSRYYEQAMGIGHFSDYLASVVEQIVHRYPQMKVLEIGAGTGMATKKVIQRVGHSFGSYTFTDISSGFFENAREIFASHQDQMVYKVLDAEKDPVAQGFGEQSYDLIVASFVLHATSHLETTLHNLRRLLKPGGYVVMLEVTNLEQSRLGYIFGSLPGWWLGANDGRILSPCVPTEEWDRLLKLTGFSGVDTFTSDADALPYPASAIVSQAVDETVDFLRNPLGTPSDFVNRATPVVLIGGASSSVRVIRDVVKRHLDTRFDQVQVVDRLSDFVAISPAVSNGLLTLNLSDLEEPVFQNMTADSLAALKLLYERSNYVLWVTEDARAGNPHQNQSLGFGRSMMVEMPHVQSQFLDLDRITETSSVASRIVDAALRFVGVNMPDRGGDVASAGLLWSTEPEIAVIGGRELLPRIKLNRSQNLRYNASRRAIAEDVDMDQKSVQLVRNGNAYVLEQGSTSGFGNQTPGYTRIRVDVSSLKSLHLGRGNALYLVAGTVLATGEKVIGFADKNSSIVDIPPSWMSHRPDISMAALILSIIARLFSRAILSSISPGGVLVVAEPDELLAPVLEWQASQQKIRVVFVTTQEDAPERPNWVVLHSQVHVRSLPKLAPTEPVTILDLSTGEEPSALALKLRNSLHPASAFERLTYWFSDHARRGEIHIPAEAMLTMYRPPMSPPASDSVIASHSFPVTDVSQIPAARCPLAVVDWQSTSHVPALIRPVDHYPMLKSNKTYWLVGLTGSLGLSLCAWMIHQGAQNVVLTSRNPKIDQIILQELRSLGARVEVYAGDVTNQESLRGVYDRICQTLPPVAGVGQGAMVLIDTMIKDMEIDAMQSVLQPKVKGSINLDELFSAERPLDFFIFFSSATCVTGNIGQSNYAAANMFMTGLAANRNRRGLAGSVMNIGAIMGVGYVTRETSEALQRNLLKSGHVWMSEQDFHTIFAEAILAGTPGSDANVEITCGLRITNASEEQRPLWSFNPRFQHLVVMEEQVEETYEQDKKGMSLKLQLREARTTDEIYEVIKECFIVKLQIMLGLDDAATNSITSKAADDLGIDSLNTVEIRSWFLKEMKVDIPVLRILGGATIGEIIKFVLEKLPSDMTPSLGLSPPTGAASKATSQPNPKPKVVVERRNVPRLEKKIVHSAGSRTSSSVTGTSKSVSPARSMDTASSQTSEAASPSIHTEEITKPLKPLAPLLKADVVSSNLGKVITPVEQTAALSVRKEPLSFGQSRFWFLKLYLEDQTTFNITCLLRMTGPLSVDSLSRAVTAVGQRHEALRTCFTVEDGQSPVQTILPESTLKLERQEYRTMADVNTATKKLTQHVYEMESGRLMRVILLSSAPNSSVHYVLVGYHHINMDGVSLEVFLHDLEKAYRGQPLSSDLLQYPDYAAKQRQERNQGAWQDDLTFWKNEMVGSNLEIPLLPLASVAIRKPLTQYRHHRVEQRLDARLGAQIRQLCQSIKATPSHFYLATFTTLLARLTRTREIWVGMADANRIQAETADSIGNYLNLLALRMQYDPDQPFVASVQAARKKSYGALAHSRIPFDVLLSELQVPRSSTHSPLFQVFMDYRHDVREKRMFGDCQLEGVEYEMGRTAYDIALDVVDTADDGPLIIMGLQESLYSPDTAQMLLNSFLEMVRAFAQDSKQPGGHVSLFSASDLEKALALGNGSVVASQWPATLSHRIDDMAKQYPQKLALNDGDNLRLTFQQMSQRADSIASALLSANVSRQQRVAVFQHPSSDCICSILAILRIGATYVPLDLRLELARLRSIVQDCEPTVFLVDSHTQSQAPDLMLTRPAMTINIADLPRIAPFPVMNRAAAEDEAVILYTSGSTGNPKGVPLTHENLRVNIEGNQAEFQFGPDDCLLQQIAFSFDFSVWQIFMALANGASLFIAPSTHRGDPVALMDLVVREDITITGATPSEYRSWFQHGDLARLKTSQWKTAVSAGEAMTTNMIRDFQALNKSDLRLVNGYGPTEASMSSNKLVVPYLTNKDHPEEWMEKGAVVAGYTAPNYSIYIVDEAMNLLPIGLPGQILIGGPGIASGYLNNKELSCIRFINDKYASPEQRACGWRWAHLTGDRGRIGADGRLRIEGRIEGDTQVKLRGYRIDLQDVEAAMLKASPGAFKDLVVSLHQATQALVAHVVFSQHYPAHKHSQALEIKSLELPRYMWPARTVSIDQMPVTVHGKLDRKALQTMDLPAIEPMKQTSTAHLNEAQAQMVQLWEEVISKDILAAHHIVAESDFFAVGGTSMLLVDLQRQIKSWFKMEIALAELFSANTLEKMALLIKPQEDIATPAAVDAAPPSSPSPLALTASLPPAPTTINWSEEVQLPRVLREQTSSGTTVSVPEKTSGLRLVLTGATGFIGQALLQQLTANPAISTVHCIAVRDPSAIPAHEKILVHAGDLTHAALGLAPVEAQAIFREVDAVIHNGADVSFMKSYHSLRRTNVESTIALIQNSLSRQIPFHYISSSGIANLAGTTTFAEVSAASFIPPTDGSQGYLATKWVSERLLEEAHREFGLPVYIHRPSSVTGSNAPPLDLMDNLMTYARRLKAVPMPERSSWKGYLDFVPVEQVVRDVTGDVLSAAGTVPSARASKVHYIHHLGRQVSLTGLHRYLERETGAVYRVLKMGEWLEEATQVGMDALLRTYLESMDKEDVKVVFPRLVAGKRHASTVGVAKGVKIGESWLEKGKTLLFSW

2.3.1.-; 6.3.2.-

amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; lactone biosynthetic process [GO:1901336]; methylation [GO:0032259]; organonitrogen compound biosynthetic process [GO:1901566]; polyketide biosynthetic process [GO:0030639]; toxin biosynthetic process [GO:0009403]

3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]

PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765;

3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150;

NRP synthetase family

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:28365998}.

FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety (PubMed:28365998). The first step of the pathway is provided by the HR-PKS poxF that serves in a new mode of collaborative biosynthesis with the PKS-NRPS poxE, by providing the olefin containing amino acid substrate via the synthesis of an ACP-bound dec-4-enoate (PubMed:28365998). The cytochrome P450 monooxygenase poxM-catalyzed oxidation at the alpha-position creates the enzyme-bound 2-hydroxydec-4-enoyl-ACP thioester, which may be prone to spontaneous hydrolysis to yield 2-hydroxydec-4-enoic acid due to increased electrophilicity of the carbonyl (PubMed:28365998). 2-hydroxydec-4-enoic acid can then be further oxidized by poxM to yield the alpha-ketoacid 2-oxodec-4-enoicacid, which is reductively aminated by the aminotransferase poxL to yield (S,E)-2-aminodec-4-enoic acid (PubMed:28365998). The Hybrid PKS-NRPS synthetase poxE then performs condensation between the octaketide product of its PKS modules and the amino group of (S,E)-2-aminodec-4-enoic acid which is activated and incorporated by the adenylation domain (PubMed:28365998). The resulting aminoacyl product can be cyclized by the Diels-Alderase PoxQ and reductively released by the reductive (R) domain of poxE to yield an aldehyde intermediate (Probable) (PubMed:28365998). The released aldehyde is then substrate for a Knoevenagel condensation by the hydrolyase poxO followed by an oxidation at the 5-position of the pyrrolidone ring (PubMed:28365998). The presence of the olefin from the amino acid building block allows for migration of the substituted allyl group to occur (PubMed:28365998). This allylic transposition reaction takes place in a conjugate addition, semipinacol-like fashion to yield a succinimide intermediate (PubMed:28365998). Iterative two-electron oxidations of the C7 methyl of the succinimide intermediate to the carboxylic acid can be catalyzed by one of two remaining cytochrome P450 monooxygenasess poxC or poxD to yield oxaleimide A (PubMed:28365998). Subsequent oxidation yields the maleimide scaffold oxaleimide I (PubMed:28365998). Both oxaleimide A and oxaleimide I can undergo oxidative modifications in the decalin ring to yield the series of products oxaleimides B to H (PubMed:28365998). {ECO:0000269|PubMed:28365998, ECO:0000305|PubMed:32039410}.

Penicillium oxalicum

A0A1W6QDI7

KSL1_ISORU

MSLAFNLRVIPFSGHTIQSRRGLFPVHESPMITTKPFAAVKCSLTTSTDLMGKIKEKFNGKVHTSLPAITTHSADTPSNLCIIDTLQRLGVDRYFQSEIDSILDDTYRLWQLKKEDIFSDITTHAMAFRLLRVKGYQVSSEELAPYADQEHVNLQEIDVPTVIELYRAAQERVTEEDSTLKKLYVWTSTFLKQQLLTDAIPDKKLHEQVDYYLKNYHGILDRMGVRRSLDLYDVGHYKTLKAADGFSNLCNEDFLAFARQDFNISQAQHQKELQQLQRWYSDCRLDTLKFGRDVVRVSNFLTSAMSGDPELSDVRLAFAKHIVLVTRIDDFFDHGGSKEESYKILELVKEWKEKPAGEYGSEEVEILFTAVYNTVNELAEMAHIEQGRSVKDLLIKLWVEILSMFKIELDTWSDDTALTLDEYLSSSWVSIGCRICILISMQFLGVKLTDEMLLSEECTDLCRHVSMVDRLLNDVQTFEKERKENTGNSVSLLLAAHKDERAINEEEAITKAKDLAEYNRRKLMQIVYKTGTIFPRKCKDMFLKVCRIGCYLYSSGDEFTTPQQMMEDMKSLVYEPLTIHPPEANNVVGKKTELCQQLVKPYVCHTFCKKYTVSRPSNVMMTCYID

4.2.3.131

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q40577}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};

gibberellin biosynthetic process [GO:0009686]; miltiradiene biosynthetic process [GO:1901946]; terpenoid biosynthetic process [GO:0016114]

chloroplast [GO:0009507]

magnesium ion binding [GO:0000287]; miltiradiene synthase activity [GO:0062205]; terpene synthase activity [GO:0010333]

PF01397;PF03936;

1.10.600.10;1.50.10.130;

Terpene synthase family

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

CATALYTIC ACTIVITY: Reaction=(+)-copalyl diphosphate = diphosphate + miltiradiene; Xref=Rhea:RHEA:33983, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635, ChEBI:CHEBI:65037; EC=4.2.3.131; Evidence={ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33984; Evidence={ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526}.

FUNCTION: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities (PubMed:28381502, PubMed:28445526). Catalyzes the conversion of (+)-copalyl diphosphate ((+)-CPP) to miltiradiene (PubMed:28381502, PubMed:28445526). {ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526}.

Isodon rubescens (Rabdosia rubescens)

A0A1W7HCY1

IUTB_VIBVL

MSGHSFFEHLFEHSQHVTPYLHGAIKPRPERCAEHGFIHIEHASSDHIRALYESLKLAHPEAGAAYWLTRTWTLLCWQPLYVAFIAIYSCQGLPKLSSMGQHVQPRFVSGYQFDDDEYRQGSEQELIAHAGKELCALFDYFRQEMSLWTRIRPGFTQHLFADGVFGCLVKLSQFYPTLSGDYFLEQARLWLAACQLPEKLIQSLRYDETSRQLSLVRTSCCLVYKCQGRELCRDCPRHPDNKRE

1.16.1.10

COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:P39405}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P39405};

cellular response to iron ion starvation [GO:0010106]

cytoplasm [GO:0005737]

2 iron, 2 sulfur cluster binding [GO:0051537]; ferric-chelate reductase (NADH) activity [GO:0140618]; ferric-chelate reductase (NADPH) activity [GO:0052851]; metal ion binding [GO:0046872]

PF11575;

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28150143}.

CATALYTIC ACTIVITY: Reaction=2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH; Xref=Rhea:RHEA:15061, Rhea:RHEA-COMP:11342, Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.16.1.10; Evidence={ECO:0000269|PubMed:32681432}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15063; Evidence={ECO:0000269|PubMed:32681432}; CATALYTIC ACTIVITY: Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342, Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.10; Evidence={ECO:0000269|PubMed:32681432}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28797; Evidence={ECO:0000269|PubMed:32681432};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=6.83 nmol/min/mg enzyme with Fe(3+)-aerobactin as substrate and glutathione (GSH) as electron donor (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:32681432}; Vmax=2.32 nmol/min/mg enzyme with Fe(3+)-vulnibactin as substrate and glutathione (GSH) as electron donor (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:32681432}; Vmax=1.44 nmol/min/mg enzyme with ferrioxamine B as substrate and glutathione (GSH) as electron donor (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:32681432}; Vmax=1.1 nmol/min/mg enzyme with Fe(3+)-vibriobactin as substrate and glutathione (GSH) as electron donor (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:32681432}; Vmax=10.98 nmol/min/mg enzyme with Fe(3+)-nitrilotriacetic acid (NTA) as electron acceptor and glutathione (GSH) as electron donor (at pH 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:32681432}; Vmax=14.24 nmol/min/mg enzyme with Fe(3+)-nitrilotriacetic acid (NTA) as electron acceptor and simultaneous presence of glutathione (GSH) and NADPH as electron donors (at pH 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:32681432};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 with Fe(3+)-nitrilotriacetic acid (NTA) as electron acceptor. {ECO:0000269|PubMed:32681432};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius with Fe(3+)-nitrilotriacetic acid (NTA) as electron acceptor. {ECO:0000269|PubMed:32681432};

FUNCTION: Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-aerobactin reductase catalyzing the reduction of Fe(3+)-aerobactin, a citrate-hydroxamate siderophore produced by other bacteria. Catalyzes reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus, in the absence of VuuB (PubMed:28150143, PubMed:32681432). Catalyzes reduction of ferrioxamine B and Fe(3+)-vibriobactin in vitro. No activity with Fe(3+)-enterobactin. Catalyzes reduction of ferric chelating compound Fe(3+)-nitrilotriacetic acid (NTA) in the presence of NADH, NADPH or reduced glutathione (GSH) as its electron donor in vitro. Catalyzes also reduction of ferric chelating compounds Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of GSH as its electron donor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor and GSH as donor (PubMed:32681432). {ECO:0000269|PubMed:28150143, ECO:0000269|PubMed:32681432, ECO:0000305}.

Vibrio vulnificus

A0A1Y2IY60

LP9_TRAC3

MFTKLIIAASLAASVAAHATFQELWINGVDQGSSCVRLPQSNSPVTSVSTPDLACNASPHPSDGICQVMPGDEVTVEMHQQPNDRSCATEAIGGDHYGPVLVYMAKVDDATTAVGSSAQWFKVAEIGLPSSNPDYWGTEVLNDNCGHYTFKVPSDIAPGNYLIRAEVIALHVASSIGGAQFYMSCYQVNVGGSGSANPPTVSIPGAYSATDPGILINIYEPLSTYTIPGPTPYATTSPAVANTPYPTTATWNTALQPSTVPTAVPTPGTPGIGKA

3.2.1.4

COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q4WP32}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q4WP32};

cellulose catabolic process [GO:0030245]

extracellular region [GO:0005576]

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: Secreted {ECO:0000305|PubMed:37463979}.

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:37463979};

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 oxidation products (PubMed:37463979). 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:37463979). Shows only weak binding properties to cellulose, and low cellulolytic oxidative activity which questions the involvement of X282 extension-containing AA9 proteins in the degradation of plant cell wall and opens new avenues as to the divergence of function of some AA9 members (PubMed:37463979). {ECO:0000269|PubMed:37463979}.

Trametes coccinea (strain BRFM310) (Pycnoporus coccineus)

A0A1Y3DYH2

ADA_PLAKN

MNILQEPIDFLKKDELKNIDLSQMDKKERYKIWKRIPKCELHCHLDLCFSADFFLSCVRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIRVADIFQDYEMIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKHNLDIELIHQAIVKGIKEVVELLDHKIDVTLLCIGDTGHRAADIKASADFCLKHKADFVGFDHGGHEVDLKPYKEIFDYVKEGGMHLTVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVSESQELIDMVKENNILLEVCPISNVLLKNAKSFDTHPIRKLYDAGVKVSVSSDDPGMFLTNINDDYEKLYTHLHFTLEDFMKMNEWALEKSFIGCDIKEKIKKLYF

3.5.4.31; 3.5.4.4

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:A5KE01}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:A5KE01};

adenosine catabolic process [GO:0006154]; hypoxanthine salvage [GO:0043103]; inosine biosynthetic process [GO:0046103]; negative regulation of adenosine receptor signaling pathway [GO:0060169]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; purine ribonucleoside salvage [GO:0006166]

cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]

2'-deoxyadenosine deaminase activity [GO:0046936]; 5'-methylthioadenosine deaminase activity [GO:0090614]; adenosine deaminase activity [GO:0004000]; metal ion binding [GO:0046872]

PF00962;

3.20.20.140;

Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family

CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:19728741}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine; Xref=Rhea:RHEA:25025, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:28938, ChEBI:CHEBI:48595; EC=3.5.4.31; Evidence={ECO:0000269|PubMed:19728741};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=120 uM for adenosine (at pH 8) {ECO:0000269|PubMed:19728741}; KM=22 uM for 5'-methylthioadenosine (MTA) (at pH 8) {ECO:0000269|PubMed:19728741}; Note=kcat is 6.8 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.51 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741). {ECO:0000269|PubMed:19728741};

PATHWAY: Purine metabolism; purine nucleoside salvage. {ECO:0000305|PubMed:19728741}.

FUNCTION: Catalyzes the hydrolytic deamination of adenosine to produce inosine (PubMed:19728741). Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI) (PubMed:19728741). Plays an essential role in the purine salvage pathway which allows the parasite to use host cell purines for the synthesis of nucleic acids (Probable). {ECO:0000269|PubMed:19728741, ECO:0000305|PubMed:19728741}.

Plasmodium knowlesi

A0A1Z0YU59

MAMB1_DENAN

RPSFCNLPVKPGPCNGFFSAFYYSQKTNKCHSFTYGGCKGNANRFSTIEKCRRTCVG

extracellular region [GO:0005576]

serine-type endopeptidase inhibitor activity [GO:0004867]; toxin activity [GO:0090729]

PF00014;

4.10.410.10;

Venom Kunitz-type family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28630289}.

FUNCTION: Selectively interacts with vasopressin V2 receptor (V2R/AVPR2) and fully inhibits three major signaling pathways of this receptor that are GalphaS protein, the interaction with beta-arrestin and activation of MAP kinase (PubMed:28630289, PubMed:35122240). Inhibits vasopressin binding human V2R in the nanomolar range (Ki=5.02 nM), and also potently inhibits vasopressin-induced cAMP production (IC(50)=94 nM) (PubMed:35122240). In vivo, this protein shows an aquaretic effect (PubMed:28630289, PubMed:35122240). Urine output increases and urine osmolality decreases dramatically under treatment with this protein, without differences observed between healthy mice and the pcy mice model of the autosomal-dominant polycystic kidney disease (ADPKD) (PubMed:28630289). This protein does not modify electrolyte, protein and urea excretions in the urine samples, but produces a 3-fold decrease of creatinine levels (PubMed:28630289). Intraperitoneal injection of this protein into the pcy mice significantly reduces the number of renal cysts and the total area of cysts (PubMed:28630289). This protein also shows high efficacy in preventing hyponatremia in rat models (induced by DAVP) (PubMed:33052234). Is highly visible in mice liver and kidney after intravenous injection (PubMed:33052234). Is rapidly eliminated in the liver, whereas it exhibits slow elimination in the kidney due to the high expression of V2R which acts as a reservoir (PubMed:33052234). In addition, its elimination from blood is rapid (PubMed:33052234). Fluorescent MQ1 probes could also be used for imaging V2R-overexpressing cancer cells; note that these probes label the three renal cancer cell lines CAKI-2, ACHN and A498 that highly express V2R (PubMed:33052234). In vivo, does not show any toxicity on animals, even at highest doses tested, such as prostration, spidy coat, appetite or weight loss (PubMed:33052234). {ECO:0000269|PubMed:28630289, ECO:0000269|PubMed:33052234, ECO:0000269|PubMed:35122240}.

Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps)

A0A1Z2R986

EGLN_DANRE

MKSICCVLVLCLLLCRRSTASESICELKDVSGNSNDWIVLREKPLGCWTDFQTENGTEVHIINLEDNPSVFTVNLLKANKSVVIFTSSSAQSSHAMLFDNPAVSIYVTNKTSLTFIHPTQKPLQILTAPPAGNVSAVLRWAAETFGGVTSVTNARNPKTITFTGVKGSQNSSRCELMPETPTEKPFIHLELNEPIEALKSCYMKHEGEKLHIINIPDGVTIRHVSVHLLSDCNVVLRGPAGTHWIIKNSLRIGILSNNQIHLQSFPLRPRMAISDNPTDIRQKALSYFSSGFISSYSEIRLNVTNVELWITDYSISSAPTEVEKTTPSPTSPPFPVQMQLFSSPDFTTPIDNNSRVLSDKRVYAEISSQTFREASIRVSSCWVRSTPVTREMPFREEPCFIKDCPKRLSFSFQILQDLPAGSWDLECAVKLCGVKRINNEESCTSETPVKRNVQVKPFTPTTNSCFEFGLSAVLGIAFGGFLIGVLLTGALWFIKIRTGHPVALGMRSTAAELSVLSISGCPCGLTKRQPVPTHPSPSENSSANASIGSTQSTPTSSMA

angiogenesis [GO:0001525]; blood vessel morphogenesis [GO:0048514]; cell migration [GO:0016477]; cellular response to mechanical stimulus [GO:0071260]; endothelial cell morphogenesis [GO:0001886]; epithelial to mesenchymal transition [GO:0001837]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; transforming growth factor beta receptor signaling pathway [GO:0007179]

cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]

glycosaminoglycan binding [GO:0005539]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity [GO:0005024]; type II transforming growth factor beta receptor binding [GO:0005114]

PF00100;

2.60.40.4100;

SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17813}; Single-pass type I membrane protein {ECO:0000255}.

FUNCTION: Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis. Required for normal structure and integrity of adult vasculature. Important for endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis. {ECO:0000269|PubMed:28530658}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A218N034

WTF4_SCHKA

MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDESTLPPYSEIWKYIKTVSEDSSTGPTETTNPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFFVTIGITCPILLITIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAVGLYNSREKWVVIIWLLWVVICYTLFLRSKFGNLNLNKALICSTCSISAALLLFLLYVRLPFWTLKHMFSGLFQVLGVQSCVVIVTKGLTYLFDKHIDATGYEIEASSLFVIGNFLFFYEMECPGALKRMPKFIRNGIASFLEGIGNIGRAFRGANDNNDIPLGEMEVESEV

meiotic drive [GO:0110134]; protein localization to vacuole [GO:0072665]

ascus epiplasm [GO:0072324]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; perinuclear endoplasmic reticulum [GO:0097038]; vacuolar membrane [GO:0005774]; vacuole [GO:0005773]

PF03303;

WTF family

SUBCELLULAR LOCATION: [Isoform 1]: Spore membrane {ECO:0000255, ECO:0000269|PubMed:28631612, ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:32032353, ECO:0000269|PubMed:33108274}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000255, ECO:0000269|PubMed:33108274}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000269|PubMed:28631612, ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:33108274}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000269|PubMed:28631612, ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:33108274}. Cytoplasm {ECO:0000269|PubMed:28631612}. Spore membrane {ECO:0000269|PubMed:28631612, ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:32032353, ECO:0000269|PubMed:33108274}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000255, ECO:0000269|PubMed:33108274}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000255, ECO:0000269|PubMed:33108274}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000269|PubMed:28631612, ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:33108274}.

FUNCTION: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus; the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-specific, leading to poisoning of all progeny that do not inherit the allele. {ECO:0000269|PubMed:28631612, ECO:0000269|PubMed:32790622, ECO:0000269|PubMed:33108274}.; FUNCTION: [Isoform 1]: Localizes isoform 2 to the vacuole thereby facilitating its degradation. {ECO:0000269|PubMed:28631612, ECO:0000269|PubMed:32790622, ECO:0000269|PubMed:33108274}.; FUNCTION: [Isoform 2]: Forms toxic aggregates that disrupt spore maturation. {ECO:0000269|PubMed:28631612, ECO:0000269|PubMed:32790622, ECO:0000269|PubMed:33108274}.

Schizosaccharomyces kambucha (Fission yeast)

A0A248QE08

FAP_CHLVA

MASITSRASARASCSQANTRAGRVALSGGALLRPARPARSFVPARKQQQGAVRRGGALSARASAVEDIRKVLSDSSSPVAGQKYDYILVGGGTAACVLANRLSADGSKRVLVLEAGPDNTSRDVKIPAAITRLFRSPLDWNLFSELQEQLAERQIYMARGRLLGGSSATNATLYHRGAAGDYDAWGVEGWSSEDVLSWFVQAETNADFGPGAYHGSGGPMRVENPRYTNKQLHTAFFKAAEEVGLTPNSDFNDWSHDHAGYGTFQVMQDKGTRADMYRQYLKPVLGRRNLQVLTGAAVTKVNIDQAAGKAQALGVEFSTDGPTGERLSAELAPGGEVIMCAGAVHTPFLLKHSGVGPSAELKEFGIPVVSNLAGVGQNLQDQPACLTAAPVKEKYDGIAISDHIYNEKGQIRKRAIASYLLGGRGGLTSTGCDRGAFVRTAGQALPDLQVRFVPGMALDPDGVSTYVRFAKFQSQGLKWPSGITMQLIACRPQSTGSVGLKSADPFAPPKLSPGYLTDKDGADLATLRKGIHWARDVARSSALSEYLDGELFPGSGVVSDDQIDEYIRRSIHSSNAITGTCKMGNAGDSSSVVDNQLRVHGVEGLRVVDASVVPKIPGGQTGAPVVMIAERAAALLTGKATIGASAAAPATVAA

4.1.1.106

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:28860382}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:28860382};

glycine betaine biosynthetic process from choline [GO:0019285]

chloroplast [GO:0009507]; mitochondrial inner membrane [GO:0005743]

choline dehydrogenase activity [GO:0008812]; flavin adenine dinucleotide binding [GO:0050660]; lyase activity [GO:0016829]

PF05199;PF00732;

3.50.50.60;3.30.560.10;

GMC oxidoreductase family

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

CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + H(+) + hnu = a long-chain alkane + CO2; Xref=Rhea:RHEA:18969, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30212, ChEBI:CHEBI:57560, ChEBI:CHEBI:83563; EC=4.1.1.106; Evidence={ECO:0000269|PubMed:28860382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18970; Evidence={ECO:0000269|PubMed:28860382}; CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoate + hnu = CO2 + pentadecane; Xref=Rhea:RHEA:56060, ChEBI:CHEBI:7896, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:28897, ChEBI:CHEBI:30212; EC=4.1.1.106; Evidence={ECO:0000269|PubMed:28860382, ECO:0000269|PubMed:37000872}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56061; Evidence={ECO:0000269|PubMed:28860382, ECO:0000269|PubMed:37000872}; CATALYTIC ACTIVITY: Reaction=H(+) + hnu + octadecanoate = CO2 + heptadecane; Xref=Rhea:RHEA:77243, ChEBI:CHEBI:15378, ChEBI:CHEBI:16148, ChEBI:CHEBI:16526, ChEBI:CHEBI:25629, ChEBI:CHEBI:30212; Evidence={ECO:0000269|PubMed:28860382, ECO:0000269|PubMed:37000872}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77244; Evidence={ECO:0000269|PubMed:28860382, ECO:0000269|PubMed:37000872}; CATALYTIC ACTIVITY: Reaction=H(+) + heptadecanoate + hnu = CO2 + hexadecane; Xref=Rhea:RHEA:77375, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30212, ChEBI:CHEBI:32366, ChEBI:CHEBI:45296; Evidence={ECO:0000269|PubMed:28860382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77376; Evidence={ECO:0000269|PubMed:28860382}; CATALYTIC ACTIVITY: Reaction=H(+) + hnu + tetradecanoate = CO2 + tridecane; Xref=Rhea:RHEA:77379, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30212, ChEBI:CHEBI:30807, ChEBI:CHEBI:35998; Evidence={ECO:0000269|PubMed:28860382, ECO:0000269|PubMed:37000872}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77380; Evidence={ECO:0000269|PubMed:28860382, ECO:0000269|PubMed:37000872}; CATALYTIC ACTIVITY: Reaction=H(+) + hnu + octanoate = CO2 + heptane; Xref=Rhea:RHEA:77383, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:25646, ChEBI:CHEBI:30212, ChEBI:CHEBI:43098; Evidence={ECO:0000269|PubMed:37000872}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77384; Evidence={ECO:0000269|PubMed:37000872};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 (with palmitate as substrate) (PubMed:28860382, PubMed:37000872). Optimum pH is 6.0 (with octanoate as substrate) (PubMed:37000872). {ECO:0000269|PubMed:28860382, ECO:0000269|PubMed:37000872};

FUNCTION: Catalyzes the decarboxylation of free fatty acids to n-alkanes or n-alkenes in response to blue light (PubMed:28860382, PubMed:30106504, PubMed:30673222). Substrate preference is toward fatty acids with C16 or C17 chains (PubMed:28860382, PubMed:30106504, PubMed:30673222). Converts n-octanoic acid (C8 chain) more efficiently than palmitate (n-hexadecanoic acid, C16 chain) into n-heptane (C7 chain) and n-pentadecane (C15 chain), respectively, partly due to an autocatalytic effect of its n-heptane product (PubMed:37000872). Saturated fatty acids are converted to alkanes, not alkenes (PubMed:28860382). The decarboxylation is initiated through electron abstraction from the fatty acid by the photo-excited FAD (PubMed:28860382). {ECO:0000269|PubMed:28860382, ECO:0000269|PubMed:30106504, ECO:0000269|PubMed:30673222, ECO:0000269|PubMed:37000872}.

Chlorella variabilis (Green alga)

A0A250YGJ5

SIR6_CASCN

MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVRQSSNVVFHTGAGISTASGIPDFRGPHGVWTMEERGLAPKFDTTFENARPTQTHMALVQLERVGLLHFVVSQNVDGLHVRSGFPRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKTTGRLCTVAKARGLRACRGELRDTILDWEDALPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGKLVIVNLQPTKHDRHADLRIHGYVDDVMTQLMKHLGLEIPAWDGPRVLEKALPPLPRPPTPKLEPTDKSLAQLNGSVPADSKPEPCTWHNGSQPASPKREQPDSPAPRRPPKRVKAEVTPS

2.3.1.-; 2.3.1.286; 2.4.2.-

cardiac muscle cell differentiation [GO:0055007]; circadian regulation of gene expression [GO:0032922]; determination of adult lifespan [GO:0008340]; double-strand break repair [GO:0006302]; ketone biosynthetic process [GO:0042181]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of glycolytic process [GO:0045820]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; pericentric heterochromatin formation [GO:0031508]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of insulin secretion [GO:0032024]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of protein localization to chromatin [GO:0120187]; positive regulation of stem cell differentiation [GO:2000738]; protein delipidation [GO:0051697]; protein destabilization [GO:0031648]; regulation of circadian rhythm [GO:0042752]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of lipid catabolic process [GO:0050994]; regulation of lipid metabolic process [GO:0019216]; retrotransposon silencing [GO:0010526]

chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]

chromatin DNA binding [GO:0031490]; damaged DNA binding [GO:0003684]; DNA damage sensor activity [GO:0140612]; metal ion binding [GO:0046872]; NAD+ binding [GO:0070403]; NAD+-protein-arginine ADP-ribosyltransferase activity [GO:0106274]; NAD-dependent histone H3K18 deacetylase activity [GO:0097372]; NAD-dependent histone H3K56 deacetylase activity [GO:0140765]; NAD-dependent histone H3K9 deacetylase activity [GO:0046969]; NAD-dependent protein deacetylase activity [GO:0034979]; NAD-dependent protein demyristoylase activity [GO:0140773]; NAD-dependent protein depalmitoylase activity [GO:0140774]; nucleosome binding [GO:0031491]; nucleotidyltransferase activity [GO:0016779]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; TORC2 complex binding [GO:1904841]; transcription corepressor activity [GO:0003714]

PF02146;

2.20.28.200;3.40.50.1220;

Sirtuin family, Class IV subfamily

PTM: Acetylated at Lys-33. Deacetylation at Lys-33 by SIRT1 promotes homomultimerization and binding to double-strand breaks (DSBs) sites. {ECO:0000250|UniProtKB:Q8N6T7}.; PTM: Phosphorylation at Ser-10 by MAPK8/JNK1 in response to oxidative stress stimulates the mono-ADP-ribosyltransferase activity on PARP1, leading to PARP1 recruitment to double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q8N6T7}.; PTM: Monoubiquitinated at Lys-170 by STUB1/CHIP, preventing its degradation by the proteasome. {ECO:0000250|UniProtKB:Q8N6T7}.; PTM: Sumoylated, leading to specifically decrease ability to deacetylate histone H3 at 'Lys-56' (H3K56ac). {ECO:0000250|UniProtKB:Q8N6T7}.

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P59941}. Chromosome {ECO:0000250|UniProtKB:Q8N6T7}. Chromosome, telomere {ECO:0000250|UniProtKB:Q8N6T7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P59941}. Note=Predominantly nuclear. Associated with pericentric heterochromatin and telomeric heterochromatin regions. Localizes to DNA damage sites: directly recognizes and binds double-strand breaks (DSBs) sites via a tunnel-like structure that has high affinity for DSBs (By similarity). A fraction localizes to the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P59941, ECO:0000250|UniProtKB:Q8N6T7}.

CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:31002797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43637; Evidence={ECO:0000269|PubMed:31002797}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-tetradecanoyl-L-lysyl-[protein] + NAD(+) = 2''-O-tetradecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:70567, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15437, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:141129, ChEBI:CHEBI:189674; Evidence={ECO:0000250|UniProtKB:Q8N6T7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70568; Evidence={ECO:0000250|UniProtKB:Q8N6T7}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-hexadecanoyl-L-lysyl-[protein] + NAD(+) = 2''-O-hexadecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:70563, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14175, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:138936, ChEBI:CHEBI:189673; Evidence={ECO:0000250|UniProtKB:Q8N6T7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70564; Evidence={ECO:0000250|UniProtKB:Q8N6T7}; CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + NAD(+) = H(+) + N(6)-(ADP-D-ribosyl)-L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58220, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15088, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:142515; Evidence={ECO:0000250|UniProtKB:P59941}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58221; Evidence={ECO:0000250|UniProtKB:P59941}; CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, ChEBI:CHEBI:142554; Evidence={ECO:0000250|UniProtKB:P59941}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19150; Evidence={ECO:0000250|UniProtKB:P59941};

FUNCTION: NAD-dependent protein deacetylase, deacylase and mono-ADP-ribosyltransferase that plays an essential role in DNA damage repair, telomere maintenance, metabolic homeostasis, inflammation, tumorigenesis and aging (By similarity). Displays protein-lysine deacetylase or defatty-acylase (demyristoylase and depalmitoylase) activity, depending on the context (By similarity). Acts as a key histone deacetylase by catalyzing deacetylation of histone H3 at 'Lys-9', 'Lys-18' and 'Lys-56' (H3K9ac, H3K18ac and H3K56ac, respectively), suppressing target gene expression of several transcription factors, including NF-kappa-B (PubMed:31002797). Acts as an inhibitor of transcription elongation by mediating deacetylation of H3K9ac and H3K56ac, preventing release of NELFE from chromatin and causing transcriptional pausing (By similarity). Involved in DNA repair by promoting double-strand break (DSB) repair: acts as a DSB sensor by recognizing and binding DSB sites, leading to (1) recruitment of DNA repair proteins, such as SMARCA5/SNF2H, and (2) deacetylation of histone H3K9ac and H3K56ac (By similarity). SIRT6 participation to DSB repair is probably involved in extension of life span (PubMed:31002797). Also promotes DNA repair by deacetylating non-histone proteins, such as DDB2 and p53/TP53 (By similarity). Specifically deacetylates H3K18ac at pericentric heterochromatin, thereby maintaining pericentric heterochromatin silencing at centromeres and protecting against genomic instability and cellular senescence (By similarity). Involved in telomere maintenance by catalyzing deacetylation of histone H3 in telomeric chromatin, regulating telomere position effect and telomere movement in response to DNA damage (By similarity). Required for embryonic stem cell differentiation by mediating histone deacetylation of H3K9ac (By similarity). Plays a major role in metabolism by regulating processes such as glycolysis, gluconeogenesis, insulin secretion and lipid metabolism (By similarity). Inhibits glycolysis via histone deacetylase activity and by acting as a corepressor of the transcription factor HIF1A, thereby controlling the expression of multiple glycolytic genes (By similarity). Has tumor suppressor activity by repressing glycolysis, thereby inhibiting the Warburg effect (By similarity). Also regulates glycolysis and tumorigenesis by mediating deacetylation and nuclear export of non-histone proteins, such as isoform M2 of PKM (PKM2) (By similarity). Acts as a negative regulator of gluconeogenesis by mediating deacetylation of non-histone proteins, such as FOXO1 and KAT2A/GCN5 (By similarity). Promotes beta-oxidation of fatty acids during fasting by catalyzing deacetylation of NCOA2, inducing coactivation of PPARA (By similarity). Acts as a regulator of lipid catabolism in brown adipocytes, both by catalyzing deacetylation of histones and non-histone proteins, such as FOXO1 (By similarity). Also acts as a regulator of circadian rhythms, both by regulating expression of clock-controlled genes involved in lipid and carbohydrate metabolism, and by catalyzing deacetylation of PER2 (By similarity). The defatty-acylase activity is specifically involved in regulation of protein secretion (By similarity). Has high activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins, such as RRAS2 and TNF, thereby regulating their secretion (By similarity). Also acts as a mono-ADP-ribosyltransferase by mediating mono-ADP-ribosylation of PARP1, TRIM28/KAP1 or SMARCC2/BAF170 (By similarity). Mono-ADP-ribosyltransferase activity is involved in DNA repair, cellular senescence, repression of LINE-1 retrotransposon elements and regulation of transcription (By similarity). {ECO:0000250|UniProtKB:P59941, ECO:0000250|UniProtKB:Q8N6T7, ECO:0000269|PubMed:31002797}.

Castor canadensis (American beaver)

A0A286QZ36

RAC1_STIJA

MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGRPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRTKWYPEVSHHCPSTPIILVGTKLDLRDDKETMNKLSERSLRPIAYPQGLQMQKEIHAVKYLECSALTQKGLKTVFDEAIRAVLCPPAKNKSKRSCQLL

cortical cytoskeleton organization [GO:0030865]; defense response to Gram-negative bacterium [GO:0050829]; engulfment of apoptotic cell [GO:0043652]; establishment or maintenance of cell polarity [GO:0007163]; innate immune response [GO:0045087]; mitotic cytokinesis [GO:0000281]; motor neuron axon guidance [GO:0008045]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell shape [GO:0008360]; small GTPase-mediated signal transduction [GO:0007264]

cell projection [GO:0042995]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886]

GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901]

PF00071;

3.40.50.300;

Small GTPase superfamily, Rho family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63000}; Lipid-anchor {ECO:0000250|UniProtKB:P63000}; Cytoplasmic side {ECO:0000250|UniProtKB:P63000}.

FUNCTION: Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. {ECO:0000250|UniProtKB:P63000}.

Stichopus japonicus (Sea cucumber)

A0A286R227

NIA_ULVPR

MGVRHSASKDYIAGRPLVPGEAPLDKKNSNFSSWKPVTEIDDRDAKCADNWVPRHPDLIRLTGKHPFNSEPPHADVMKEGWLTPVSMHFVRNHGAVPRLEWGSHRITITGLVERPMEITMDDIAKLPAVTVPCLLTCCGNRRKEVNMVKNSQGFSWGPGAVSVNNWTGARLSDVLKLVGVKSQAQGAKYVHFCGPKGELPKGVDGSYGTALTLGHALDPSMDVLIAYKQNGQFLHPDHGFPCRMLIPGWIGGRSVKWLSHLHVSDKDSQNWYHFHDNKVLPPHVDAESAAKQGWWKDPSFILKELNINSTISSPGHDERILMDQNRRYTMKGYAYSGGGRKIVRVEVSFNGGETWSHPAKIIVTETPNQAGKHWTWVHWELPVDTSQFFTATEVVCRAWDESQNTQPAVLTWTLLGQGNNSMFRLRLHKEVDPQGRLCIRFQQPAPILPGPLGNVGWREQEAGSAVPSAPAAVAAAAPGLDSTKKYVTKAMLEQHVEEASVWFAYKGKVYDGTKFLDDHPGGADSILMAGGEDATEDFDAVHSDSAKKQLEQFYIAELAPEGVPVPANLLYGGVDAAVVVMPGTAAAPLPAIDVDAPFLNPKKQKAAELKEKIKISHDVTLFRFGLEHDEQLLGLPTGKHMLIRKKVTNAEGDEEVVMRAYTPTTANETRGHFDLVVKIYKANVHPKFPEGGKFSQILEALEVGDTVEVKGPIGHFHYDRPGHYKNHKLESEVKRINMIAGGTGLTPMYQVMKAILSNPSDLTEIRLLYANQTEADILLRPELEALAKSHPDRVKIHYTVDRPTPGWKYSSGFIDLDMCERALFRYEPGTISVLCGPPPMLKFACHPNLEKMGFEKGVTSIEF

1.7.1.1

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:29371148}; Note=Binds 1 FAD (per monomer/chain). {ECO:0000269|PubMed:29371148}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250|UniProtKB:P49050}; Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. {ECO:0000250|UniProtKB:P49050}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000305|PubMed:29371148}; Note=Binds 1 heme group. The heme group is called cytochrome b-557. {ECO:0000305};

cellular response to nitrite [GO:0071250]; nitrate assimilation [GO:0042128]; nitrate metabolic process [GO:0042126]; sulfur compound metabolic process [GO:0006790]

mitochondrion [GO:0005739]

FAD binding [GO:0071949]; heme binding [GO:0020037]; molybdenum ion binding [GO:0030151]; molybdopterin cofactor binding [GO:0043546]; nitrate reductase (NADH) activity [GO:0009703]; nitrate reductase activity [GO:0008940]; sulfite oxidase activity [GO:0008482]

PF00173;PF00970;PF03404;PF00175;PF00174;

2.60.40.650;3.10.120.10;3.40.50.80;3.90.420.10;2.40.30.10;

Nitrate reductase family

CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + nitrite = H(+) + NADH + nitrate; Xref=Rhea:RHEA:17913, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.7.1.1; Evidence={ECO:0000269|PubMed:29371148};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for NADH in the ferricyanide reduction by the FAD-binding domain (at ph 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:29371148}; Vmax=9055 umol/min/mg enzyme in the ferricyanide reduction by the FAD-binding domain (at ph 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:29371148}; Note=kcat is 4900 sec(-1) for NADH in the ferricyanide reduction by the FAD-binding domain (at ph 7.0 and 25 degrees Celsius). {ECO:0000269|PubMed:29371148};

FUNCTION: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. {ECO:0000305}.

Ulva prolifera (Green seaweed) (Enteromorpha prolifera)

A0A286Y9D1

PHF14_DANRE

MDRGSKRRQVKPLADSLLDALDYDSSDDSDFKVGESSGSEGTGNGSDEEGSKESAAGSESDSDAAAASADEEGIDDLETKDLNQEDDEEEKVKESFSEETSSKETGGSSRSRKKGEKSSDMEPNGSATTEENSAEPKKWNLRRNRPMLDFTTMEELNEMDDYDSEDDNDWRPTQGKKKGKASSGKEKEGSGEEDDDDDDGGSDEEDNEDDNDDDDDDDDEGNDDESSSSDSEEEGKKPKKKAGKNTGAFDEEETNDSHSTSHGKGNEDSLLERPQTWSSQRMEHILICCVCLGDNSEDADEIIQCDNCGVTVHEGCYGVDGESDSIMSSASENSTEPWFCDACKNGVSPSCELCPSQDGIFKETDAGRWVHVVCALYVPGVAFGDIDKLRPVTLTEMNYSKYGAKECSLCEDTRFARTGVCISCDAGMCRSFFHVTCAQREGLLSEAAAEEDIADPFFAYCKQHADRFDRKWKRKNYLALQSYCKVSLQEREKQLTPEAQARITTRLQQYRAKAELSRNTRPQAWVPREKLPRPLTSSASAIRKLMRKAELMGISTDIFPVDTSDISASVDGRRKHKQPALTADFVNYYLERNMRMIQIQDNIVEQKNLKDKLESEQEKLHMEYDKLCESLEDLQNVNGQLRTEGQSIWSMMGGIVGQKLNVPAVLKAPKERKPSKKEGGSPGKSSSLPAMLYSCGICKKNQDQHLLLLCDTCKLHYHLGCLDPPLTRMPKKTKNSYWQCSECDQASSDEADIAMETLPDGTKRSRRQIKGPIKFIPQEMSPEPKKPQVRGTRTRGQKRKRMSICEEEKMEEPLPRERRQRQSTLQKKPKADDTRTECTTCKGPGDNENLVRCDECRLCYHFGCLDPPLKKSPKQTGYGWICQECDTSSSKEEEAQEVEEESVNEETAEQEIPD

lung alveolus development [GO:0048286]; mesenchymal cell proliferation [GO:0010463]; mesenchymal cell proliferation involved in lung development [GO:0060916]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of mesenchymal cell proliferation [GO:0072201]; negative regulation of mesenchymal cell proliferation involved in lung development [GO:2000791]; negative regulation of platelet-derived growth factor receptor-alpha signaling pathway [GO:2000584]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]

nucleus [GO:0005634]

histone binding [GO:0042393]; histone reader activity [GO:0140566]; zinc ion binding [GO:0008270]

PF00628;PF13831;PF13832;

2.30.30.1150;3.30.40.10;

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9D4H9}.

FUNCTION: Histone-binding protein (PubMed:34365506). Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) (PubMed:34365506). Represses PDGFRA expression, thus playing a role in regulation of mesenchymal cell proliferation (By similarity). {ECO:0000250|UniProtKB:Q9D4H9, ECO:0000269|PubMed:34365506}.

Danio rerio (Zebrafish) (Brachydanio rerio)

A0A287B8J2

DCTN1_PIG

MAQSKRHVYSRTPSGSRMSAEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLRREGTDSNAKTSKLRGPKPKKAPTARKTTTRRPKPTRPASTGVAGASSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEASDIALLLRDLETSCSDIRQFCKKIRRRMPGTDAPGIPAALAFGAQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGTPSSSPYECLRQSCNILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGIRGPPPSGIATLVSGIAGEEQQRGGAPGQAPGIVPGPGLVKDSPLLLQQISAMRLHISQLQHENSVLKGAQMKASLAALPPLHVAKLSLPPHEGPGSELAAGALYRKTNQLLETLNQLSTHTHVVDITRSSPAAKSPSAQLLEQVTQLKSLSDTIEKLKDEVLKETVSQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHDRLIS

cell division [GO:0051301]; cytoplasmic microtubule organization [GO:0031122]; establishment of mitotic spindle orientation [GO:0000132]; nuclear migration [GO:0007097]

axon [GO:0030424]; cell cortex [GO:0005938]; cell tip [GO:0051286]; centriole [GO:0005814]; centrosome [GO:0005813]; dynein complex [GO:0030286]; kinetochore [GO:0000776]; microtubule associated complex [GO:0005875]; microtubule plus-end [GO:0035371]; nuclear envelope [GO:0005635]; spindle pole [GO:0000922]

microtubule plus-end binding [GO:0051010]

PF01302;PF12455;

1.10.287.2610;2.30.30.190;

Dynactin 150 kDa subunit family

PTM: Ubiquitinated by a SCF complex containing FBXL5, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q14203}.; PTM: Phosphorylation by SLK at Thr-145, Thr-146 and Thr-147 targets DCTN1 to the centrosome. It is uncertain if SLK phosphorylates all three threonines or one or two of them. PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope, promotes its dissociation from microtubules during early mitosis and positively regulates nuclear envelope breakdown during prophase. {ECO:0000250|UniProtKB:Q14203}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14203}. Nucleus envelope {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14203}. Note=Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules. Localization at centrosome is regulated by SLK-dependent phosphorylation. Localizes to centrosome in a PARKDA-dependent manner. Localizes to the subdistal appendage region of the centriole in a KIF3A-dependent manner. PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope. {ECO:0000250|UniProtKB:Q14203}.

FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (PubMed:33734450). Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation (By similarity). {ECO:0000250|UniProtKB:Q14203, ECO:0000269|PubMed:33734450}.

Sus scrofa (Pig)

A0A291NUG3

STING_PTEPA

MLHSSLHPSIPQPRGRRAKKAAFVLLSVCLVVLWDLGERPEHILQWLMLHLASLQLGLLFKGVCSLVEELRHVHSRYQGSYWKAVRACLGCPIRCGTLLLLSCYFYTPFPNTTHLPFTWTLALLGLSQALSILLDLQDLAPAEVSAVCERRNLNVAQGMAWSFYIGYLRLILPGLPARIHSYNQHHNNLLRGAGSHRLYILFPLDCGVPDDLSMVDPNIRFLHELPLQKADRAGIKSRVYTNSVYELLENGRPVGACVLEYATPLQTLFAMSQDSRAGFSREDRLEQAKLFCKTLEDILADAPECQNNCRLVVYQEPAEGGNFSLSQEILRHLKQEEKEEVTVDSARTSVMPDPSMLPQGPELLISSMDQPLPLRTDVF

autophagosome assembly [GO:0000045]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of macroautophagy [GO:0016239]; positive regulation of type I interferon production [GO:0032481]; reticulophagy [GO:0061709]

autophagosome membrane [GO:0000421]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]

2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; proton channel activity [GO:0015252]; signaling adaptor activity [GO:0035591]

PF15009;

1.20.5.5200;3.40.50.12100;

STING family

PTM: Phosphorylation by TBK1 leads to activation and production of IFN-beta (By similarity). Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by TBK1 at Ser-366 in the pLxIS motif (By similarity). The phosphorylated pLxIS motif constitutes an IRF3-binding motif, leading to recruitment of the transcription factor IRF3 to induce type-I interferons and other cytokines (By similarity). In contrast, lacks phosphorylation site at position 358, leading to reduced production of type-I interferons and other cytokines (PubMed:29478775). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:29478775}.

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase TBK1 is recruited (By similarity). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (By similarity). Localizes in the lysosome membrane in a TMEM203-dependent manner. {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6}.

CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q86WV6};

FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes low production of type I interferon (IFN-alpha and IFN-beta) (PubMed:29478775). Compared to other mammals, STING1-dependent type I interferon induction is strongly reduced in bats, suggesting that the cGAS-STING pathway promotes a limited inflammatory response (PubMed:29478775). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, cyclic UMP-AMP (2',3'-cUAMP), and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding to c-di-GMP, cUAMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (By similarity). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). Promotes autophagy by acting as a proton channel that directs proton efflux from the Golgi to facilitate MAP1LC3B/LC3B lipidation (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:29478775}.

Pteronotus parnellii (Parnell's mustached bat)

A0A291NUI4

STING_RHIFE

MPHSSLHPSIPRPRGHRAKKAAFVLLSTCLAALWELGEPADHILRWLVLHLASEQLGLLFKGLCSLAEEIRHVHSRYQGSYWRAFRACLGCPIRCGVLLLLSCYCYTFLPNTAGLPFAWIVALLGLSQALNILLDLQGLAPAVVSTVCEQGNFNVAHGLAWSYYIGYLRLILPGLQARIHTYNQRHNNTVRGTGVHKLYILLPLDCGVPDDLSVADPNIRFLHELPKQSADRAGIKGRVYTNSIYEILENGKPVGTCVLEYATPLQTLFAMSQDSRAGFSREERLEQAKLFCQTLGDILADVPESQYCRLIVYLDAAEGSSFSLSQEILKHLKQEEKEEVTVGTMGSSGVLESSTLDKEPQLLISGMDQPLPLRTDVF

autophagosome assembly [GO:0000045]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of macroautophagy [GO:0016239]; positive regulation of type I interferon production [GO:0032481]; reticulophagy [GO:0061709]

autophagosome membrane [GO:0000421]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]

2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; proton channel activity [GO:0015252]; signaling adaptor activity [GO:0035591]

PF15009;

1.20.5.5200;3.40.50.12100;

STING family

PTM: Phosphorylation by TBK1 leads to activation and production of IFN-beta (By similarity). Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by TBK1 at Ser-365 in the pLxIS motif (By similarity). The phosphorylated pLxIS motif constitutes an IRF3-binding motif, leading to recruitment of the transcription factor IRF3 to induce type-I interferons and other cytokines (By similarity). In contrast, lacks phosphorylation site at position 357, leading to reduced production of type-I interferons and other cytokines (PubMed:29478775). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:29478775}.

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase TBK1 is recruited (By similarity). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (By similarity). {ECO:0000250|UniProtKB:Q86WV6}.

CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q86WV6};

FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes low production of type I interferon (IFN-alpha and IFN-beta) (PubMed:29478775). Compared to other mammals, STING1-dependent type I interferon induction is strongly reduced in bats, suggesting that the cGAS-STING pathway promotes a limited inflammatory response (PubMed:29478775). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, cyclic UMP-AMP (2',3'-cUAMP), and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding to c-di-GMP, cUAMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (By similarity). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). Promotes autophagy by acting as a proton channel that directs proton efflux from the Golgi to facilitate MAP1LC3B/LC3B lipidation (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:29478775}.

Rhinolophus ferrumequinum (Greater horseshoe bat)

A0A291NUI5

STING_EIDHE

MSHSSLHPSIPWPRGHKAKVAAFVLLIVCLAALWKLGEPSDHLLQWLVLHLASLHLRLLFKRVCCLAEELCHIHPRYQGNYSRAVRACLGCPIRYGAVLLLSCYFYVSLPNTVDLPLTWMLAHLGLSEALNILLGLQSLTPAEISTICEQRNFNVAHGLAWSYYIGYLQLILPGLRARIHTYNQLHSNTLQGVGSHRLYILFPLDCGVLDDLSAADPNIRFLHELPRQSADRAGIKGRVYTNSVYELLEKGKPVGTCVLEYATPLQTLFAMSQDGRAGFSQEDRLEQAKLFCRTLEDILADAPESQKNCRLIVYQEPTEESDFSLSQEILKHLRQEEREEVTMGTAGTFVAPGSSTLHQEPELLISGMDQPLPLRTDIF

autophagosome assembly [GO:0000045]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of macroautophagy [GO:0016239]; positive regulation of type I interferon production [GO:0032481]; reticulophagy [GO:0061709]

autophagosome membrane [GO:0000421]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]

2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; proton channel activity [GO:0015252]; signaling adaptor activity [GO:0035591]

PF15009;

1.20.5.5200;3.40.50.12100;

STING family

PTM: Phosphorylation by TBK1 leads to activation and production of IFN-beta (By similarity). Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by TBK1 at Ser-366 in the pLxIS motif (By similarity). The phosphorylated pLxIS motif constitutes an IRF3-binding motif, leading to recruitment of the transcription factor IRF3 to induce type-I interferons and other cytokines (By similarity). In contrast, lacks phosphorylation site at position 358, leading to reduced production of type-I interferons and other cytokines (PubMed:29478775). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:29478775}.

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase TBK1 is recruited (By similarity). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. Localizes in the lysosome membrane in a TMEM203-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6}.

CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q86WV6};

FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes low production of type I interferon (IFN-alpha and IFN-beta) (PubMed:29478775). Compared to other mammals, STING1-dependent type I interferon induction is strongly reduced in bats, suggesting that the cGAS-STING pathway promotes a limited inflammatory response (PubMed:29478775). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, cyclic UMP-AMP (2',3'-cUAMP), and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding to c-di-GMP, cUAMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (By similarity). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). Promotes autophagy by acting as a proton channel that directs proton efflux from the Golgi to facilitate MAP1LC3B/LC3B lipidation (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:29478775}.

Eidolon helvum (Straw-colored fruit bat)

A0A2D0TC04

PDE_NAJAT

LKQSKQPLESCRNRCNETFSEELSYCSCDNKCTERKACCWDYQDICVLPTQSWSCNKLRCGEKRMANVLCSCSEDCLTKKDCCTDYKSICKRETSWLKDQCASSSASQCPEGFDQSPLILFSMDGFRAEYLETWDTLMPNINKLKTCGTHAKYMRAVYPTKTFVNHYTIVTGLYAETHGIIDNNMYDVKLNQNFSLSGSNMRNAAWWGGQPIWHTASYQGLKAATYFWPGSEVKINGSYPTIYKVYNKSTPFEARVMEVLKWLDLPKAKRPDFSTLYIEEPDTTGHKFGPVSGQVIKSLQMADRTLGMLMEGLKQRNLHNCVNLILLADHGMEAISCNRLEYMTDYFNTVDFFMYEGAAPRIRSKNVPKDFYTFDSEAIVKKLTCRKPKQHFKAYLAKDLPKRLHFANNIRIDKVNLMVDRQWLAVRNKKYKYCSGGTHGYDNEFKSMEAIFLAHGPGFKEKTEVTSFENIEVYNLMCDLLKLKPAPNNGTHGSLNHLLKNPFYNPSPAKEQSPPLYCLFGPVPSPDVSGCKCSSITDLEAVNQRLNLIDQAKMQSEADNLPYGRPHVLQHSKYCLLHQTKYISAYSQDILMPLWNSYTISKSLVKPTSAPPSASDCLRLDVRIPTVQSQTCSNYQPDLAITPGFLYPPDFSSSGPEQYDALITSNIVPMYKEFARLWNYFHSTLLPKYATERNGLNVISGPIFDYNYDGHFDPYDTIDQYVNNTKIPIPTHYFVVLTSCENSTKTPLNCPPGSLKVLSFILPHRPDNSESCADKSPDNLWVEERMQTHTARVRDVELLTGLDFYSALKQPLSETLRLKTFLPIFINSVN

3.6.1.-

COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:W8E7D1}; Note=Binds 2 divalent metal cations per subunit. {ECO:0000269|Ref.1, ECO:0007744|PDB:5GZ4, ECO:0007744|PDB:5GZ5};

nucleoside triphosphate catabolic process [GO:0009143]

extracellular region [GO:0005576]

ADP phosphatase activity [GO:0043262]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; nucleoside triphosphate diphosphatase activity [GO:0047429]; toxin activity [GO:0090729]

PF01223;PF01663;PF01033;

4.10.410.20;3.40.720.10;3.40.570.10;

Nucleotide pyrophosphatase/phosphodiesterase family

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:W8E7D1}.

CATALYTIC ACTIVITY: Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:W8E7D1};

FUNCTION: Hydrolyzes ADP with high activity. Shows weak or no activity on 5'-AMP, 5'-GMP, 3'-AMP, ATP, cAMP, and cGMP. Is devoid of monophosphatase and proteinase activities. Dose-dependently inhibits platelet aggregation induced by ADP and collagen. {ECO:0000250|UniProtKB:W8E7D1}.

Naja atra (Chinese cobra)

A0A2H1A768

CDR1_CANAR

MSEKPFVDAPPPEDGVAHQVSPHDNGSLSEEANSINEYTGFGAHQEGEIRELARTFTNMSHDSGHDLSKTNTSQDLLKYLSHMSEVPGVEPFDPEQISEQLNPDSPNFNAKFWVKNMRKLFDSNPDYYKPSKLGLAYRNLRAYGVAADSDYQPTVSNGLWKMAVDYWHDMRKIDESRCFDILKTMDGYFKPGEVTVVLGRPGSGCSTLLKTIACNTYGFHIGEESQISYDGMTPDEIHKHHRGDVVYSAETDVHFPHLSVGDTLEFAAKLRTPQNRGEVSRLEHAKHMASVTMATYGLSHTRNTPVGNDFVRGVSGGERKRVSIAEVSLSGANIQCWDNATRGLDAATALEFIRALKTSAAILDATPLIAIYQCSQDAYDLFDNVIVLYEGYQIFFGKASEAKQFFLDMGYECPQRQTTADFLTSLTNPEERVVKPGFENKVPRTAKEFSDYWRNSSNYKVLTAGIDKYLAEVADGSQREAYRASHVAKQSDHTRPSSPYTVSFFMQTRYIIGRNFLRMKGDPSIVIFSIFGQGVMGLILSSVFYNLQPTTGSFYYRGAAMFFAVLFNAFASLLEIMSLFEARPIVEKHKKYALYRPSADALASIISELPVKLCMSTCFNFSFYFMVHFRRDPGRFFFYWLFCGLCTLCMSHMFRSLGAVSTSLAAAMTPATSVLLAMVIFTGFVIPIPSMLGWCRWIQYINPVSYVFESLMVNEFHGRKFECAQFVPSGGPYDQVAAVNRVCSTAGARPGEDFVDGTAYLQTSFEYVNAHKWRNLGIVVAYIVVFLGVYIALTEFNKGAMQKGEIALFLRGSLKKVRKQREQNEAKVNDVENNLPNEKISYSDAMEKDSGESSTSDDKLPNQRQIFHWKDLTYQVKIKAENRVILNHVDGWVKPGQITALMGASGAGKTTLLNCLSERLTTGTVTDGVRMVNGHGLDSSFQRSIGYVQQQDIHLATSTVREALTFSAYLRQPSHVSKKEKDEYVDYVIDLLEMGAYSDALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLANHGQAILCTIHQPSAILLQEFDRLLFLQKGGKTVYFGDLGKNCQGLIDYFEKHGAHPCPPDANPAEWMLEVVGAAPGSKAAQDYFEVWRNSEEYQEVQRELAYMENELGKLPVDEDPESRKKYATSLIKQYFIVTWRTFQQYWRSPGYIYSKFFLVITASLFNGFAFFHSGTSQQGLQNQMFSMFMFYMPLQTLIQQMLPYYVMQREIYEVREAPSRTFSWFAFIASQITTEIPFQVVLGTVAFFCWYYPVGLYQNATPTDTVHERGALMWLLVTAFYVYTISLGQMVVAFMEIADNAANMVNLMFIMCLNFCGVLATPEALPGFWIFMYRCNPFTYLIQAMLSTGLANTKIVCSSREILHFQPPSGQTCGQYMQQFISAAGGYLLDESATDQCDFCAMSQTNTFLDSVHAVYSERWRNFGIFIAFIAINMIGTIFFYWLARVPKSSKSKNH

xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961]

membrane [GO:0016020]; plasma membrane [GO:0005886]

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

PF01061;PF00005;PF14510;PF06422;

3.40.50.300;

ABC transporter superfamily

SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:30718246}; Multi-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=ATP + fluconazole(in) + H2O = ADP + fluconazole(out) + H(+) + phosphate; Xref=Rhea:RHEA:61916, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:46081, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:33353950, ECO:0000269|PubMed:36836283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61917; Evidence={ECO:0000269|PubMed:33353950, ECO:0000269|PubMed:36836283}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + itraconazole(in) = ADP + H(+) + itraconazole(out) + phosphate; Xref=Rhea:RHEA:33503, ChEBI:CHEBI:6076, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:37367600}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33504; Evidence={ECO:0000305|PubMed:37367600}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + voriconazole(in) = ADP + H(+) + phosphate + voriconazole(out); Xref=Rhea:RHEA:61912, ChEBI:CHEBI:10023, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:36836283, ECO:0000269|PubMed:37367600}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61913; Evidence={ECO:0000269|PubMed:36836283, ECO:0000269|PubMed:37367600};

FUNCTION: Pleiotropic ABC efflux transporter that confers resistance to numerous chemicals including itraconazole, fluconazole, voriconazole and posaconazole. {ECO:0000269|PubMed:30696744, ECO:0000269|PubMed:30718246, ECO:0000269|PubMed:33353950, ECO:0000269|PubMed:35893151, ECO:0000269|PubMed:36836283, ECO:0000269|PubMed:37367600, ECO:0000269|PubMed:37493629}.

Candida auris (Yeast)

A0A2H4DGV8

C7BL6_INUHU

MEPFTTFSLVASSLILLICWALVKANKPAKNLPPGPPKLPIIGNMHQLESQSPHRVLRKLSRKYGPIMHLQLGQVPTVVISTPRLVEEVVKHHDINFADRPTNTTSQIFYYNNQNVAWSSYGNYWRQIKKIVTLELLSVKKVRSFSSIRAEELTRAVKSVEPSVGSTINFRDLTSQTVNNMVSRATLGDVCKERHILLDTMNDILKTFNSFNVVNFFPSLQFLNVITGKKAKWLKIHKQLDHILENILEEHKSKPKGNQDDEDLIDVLLRVKDAGGQELPITNDNVKAITLEMLTAGTSSSSMTIEWAFCELMRHPEVMKKVQSDVRSAVKGNKVTEDDIQNMHYLKLVVKETLRLHGVPILVPRQNREDCNVLGYHIPAKTKILINAWACGTDPDTWEDPESFIPERFEKSSVSYFGTDFQLIPFGTGRRICPGVNFGIGTVEAVLSNFLYHFDWKLPDGVKPQDIDMTEVTGISTLPKYPLHIVPVSTVSQQK

1.14.14.168; 1.14.14.170

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798};

response to jasmonic acid [GO:0009753]; sesquiterpene biosynthetic process [GO:0051762]; terpenoid biosynthetic process [GO:0016114]

membrane [GO:0016020]

germacrene A acid 8beta-hydroxylase activity [GO:0102614]; heme binding [GO:0020037]; iron ion binding [GO:0005506]

PF00067;

1.10.630.10;

Cytochrome P450 family

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

CATALYTIC ACTIVITY: Reaction=germacra-1(10),4,11(13)-trien-12-oate + O2 + reduced [NADPH--hemoprotein reductase] = 8beta-hydroxygermacra-1(10),4,11(13)-trien-12-oate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:57964, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:61301, ChEBI:CHEBI:142464; EC=1.14.14.168; Evidence={ECO:0000269|PubMed:29086444}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57965; Evidence={ECO:0000269|PubMed:29086444}; CATALYTIC ACTIVITY: Reaction=germacra-1(10),4,11(13)-trien-12-oate + O2 + reduced [NADPH--hemoprotein reductase] = 8-epi-inunolide + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:57968, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:61301, ChEBI:CHEBI:142470; EC=1.14.14.170; Evidence={ECO:0000269|PubMed:29086444}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57969; Evidence={ECO:0000269|PubMed:29086444}; CATALYTIC ACTIVITY: Reaction=germacra-1(10),4,11(13)-trien-12-oate + O2 + reduced [NADPH--hemoprotein reductase] = 8alpha-hydroxygermacra-1(10),4,11(13)-trien-12-oate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:58032, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:61301, ChEBI:CHEBI:142490; Evidence={ECO:0000269|PubMed:29086444}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58033; Evidence={ECO:0000269|PubMed:29086444};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:29086444}.

FUNCTION: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones (PubMed:29086444). Hydroxylates germacrene A acid to 8-beta-hydroxy-germacrene A and 8-alpha-hydroxy-germacrene A acids (PubMed:29086444). Unlike 8-alpha-hydroxy-germacrene A acid with is spontaneously converted into inunolide (12, 8-alpha), 8-beta-hydroxy-germacrene A cannot undergo spontaneous lactonization (PubMed:29086444). {ECO:0000269|PubMed:29086444}.

Inula hupehensis (Inula helianthus-aquatilis subsp. hupehensis)

A0A2I0BVG8

CDPK1_PLAFO

MGCSQSSNVKDFKTRRSKFTNGNNYGKSGNNKNSEDLAINPGMYVRKKEGKIGESYFKVRKLGSGAYGEVLLCREKHGHGEKAIKVIKKSQFDKMKYSITNKIECDDKIHEEIYNEISLLKSLDHPNIIKLFDVFEDKKYFYLVTEFYEGGELFEQIINRHKFDECDAANIMKQILSGICYLHKHNIVHRDIKPENILLENKHSLLNIKIVDFGLSSFFSKDNKLRDRLGTAYYIAPEVLRKKYNEKCDVWSCGVILYILLCGYPPFGGQNDQDIIKKVEKGKYYFDFNDWKNISEEAKELIKLMLTYDYNKRITAKEALNSKWIKKYANNINKSDQKTLCGALSNMRKFEGSQKLAQAAILFIGSKLTTLEERKELTDIFKKLDKNGDGQLDKKELIEGYNILRSFKNELGELKNVEEEVDNILKEVDFDKNGYIEYSEFISVCMDKQILFSEERLRDAFNLFDTDKSGKITKEELANLFGLTSISEQMWNEVLGEADKNKDNMIDFDEFVNMMHKICDNKSS

2.7.11.1

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27923926};

female gamete generation [GO:0007292]; intracellular signal transduction [GO:0035556]; male gamete generation [GO:0048232]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]

cytoplasm [GO:0005737]; host cell plasma membrane [GO:0020002]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; sperm flagellum [GO:0036126]; symbiont-containing vacuole membrane [GO:0020005]

ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]

PF13499;PF00069;

1.10.238.10;1.10.510.10;

Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily

PTM: Myristoylated. Myristoylation, palmitoylation and the basic cluster motif are required for the localization to the parasitophorous vacuole membrane. {ECO:0000250|UniProtKB:P62344}.; PTM: Palmitoylated. Palmitoylation increases in merozoites in response to low level of extracellular K(+) in the host blood. Myristoylation, palmitoylation and the basic cluster motif are required for the localization to the parasitophorous vacuole membrane. {ECO:0000250|UniProtKB:P62344}.; PTM: Phosphorylation at Ser-64 occurs at late schizont stage and regulates CDPK1 protein-protein interaction. Phosphorylated at Ser-28, Ser-34 and Ser-64 in merozoites in response to low extracellular level of K(+). Phosphorylation at Thr-231 may regulate CDPK1 kinase activity. Phosphorylation increases in response to an increase in intracellular Ca(2+) levels (By similarity). Autophosphorylated in vitro (PubMed:27923926). Autophosphorylation does not affect membrane localization in vitro (By similarity). {ECO:0000250|UniProtKB:P62344, ECO:0000269|PubMed:27923926}.

SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Cell membrane {ECO:0000269|PubMed:29311293}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}; Cytoplasmic side {ECO:0000250|UniProtKB:P62344}. Parasitophorous vacuole membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Cytoplasm {ECO:0000269|PubMed:29311293}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:29311293}. Host cell membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Note=Localizes to the host erythrocytic membrane at low level (By similarity). Localizes to the cell membrane in the nascent merozoites contained within the late-stage schizonts and in free merozoites. Colocalizes with MTIP around developing merozoites in segmented schizonts, also localizes in membranes around the mature food vacuole/residual body of the schizonts. Ser-64 phosphorylated form localizes at the apical pole in punctate structures in merozoites within late schizonts in free merozoites. In trophozoites and schizonts, localizes to the parasitophorous vacuole (PV) and in membranous systems derived from the PV including intraparasitic vacuoles and the tubovesicular system, an extension of the parasitophorous vacuole membrane into the host cell cytoplasm. Localization to the cytoplasm in trophozoite or schizonts is minimal (By similarity). In female stage V gametocytes and gametes, localizes to the cell membrane. In stage V male gametocytes, localizes to the cell membrane and in the cytoplasm. In male gametes, localizes to the residual body, cell membrane and in the flagella (PubMed:29311293). Calcium and/or autophosphorylation does not affect membrane localization (By similarity). {ECO:0000250|UniProtKB:P62343, ECO:0000250|UniProtKB:P62344, ECO:0000269|PubMed:29311293}.

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:27923926}; 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:27923926};

FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (PubMed:27923926). By phosphorylating various proteins, required for microneme secretion and thus merozoite egress from and invasion of host erythrocytes (By similarity). During gametogenesis, essential for the development of both male and female gametes (PubMed:29311293). Phosphorylates SERA5 p50 which enhances SERA5 p50 protease activity; however, SERA5 p50 protease activity has been shown in other studies to be controversial. Probably by phosphorylating SERA5 p50, plays a role in merozoite egress from host erythrocytes. Probably prior or during merozoite invasion of host erythrocytes, phosphorylates rhoptry protein RhopH3 which is required for RhopH3 localization to rhoptries and for its secretion. Probably in late schizonts, phosphorylates myosin A tail domain-interacting protein MTIP and glideosome-associated protein 45 GAP45, both of which are components of the motor complex that generates the force required by the parasite to invade host cells. In late schizonts, phosphorylates inner membrane complex protein IMC1g. In late schizonts, phosphorylates PKA regulatory subunit PKAr in a calcium-dependent manner, which may contribute to the dissociation of regulatory PKAr and catalytic PKAc subunits and promote the activation of PKAc. May phosphorylate raf kinase inhibitory protein RKIP which in turn may regulate CDPK1 catalytic activity (By similarity). May phosphorylate proteins of the host erythrocyte membranes (By similarity). {ECO:0000250|UniProtKB:P62343, ECO:0000250|UniProtKB:P62344, ECO:0000269|PubMed:27923926, ECO:0000269|PubMed:29311293}.

Plasmodium falciparum (isolate NF54)

A0A2I0C265

PLM9_PLAFO

MFFINFKKIKKKQFPIYLTQHRIITVFLIFIYFINLKDCFHINNSRILSDVDKHRGLYYNIPKCNVCHKCSICTHENGEAQNVIPMVAIPSKRKHIQDINKEREENKYPLHIFEEKDIYNNKDNVVKKEDIYKLRKKKKQKKNCLNFLEKDTMFLSPSHDKETFHINHMNKIKDEKYKQEYEEEKEIYDNTNTSQEKNETNNEQNLNINLINNDKVTLPLQQLEDSQYVGYIQIGTPPQTIRPIFDTGSTNIWIVSTKCKDETCLKVHRYNHKLSSSFKYYEPHTNLDIMFGTGIIQGVIGVETFKIGPFEIKNQSFGLVKREKASDNKSNVFERINFEGIVGLAFPEMLSTGKSTLYENLMSSYKLQHNEFSIYIGKDSKYSALIFGGVDKNFFEGDIYMFPVVKEYYWEIHFDGLYIDHQKFCCGVNSIVYDLKKKDQENNKLFFTRKYFRKNKFKTHLRKYLLKKIKHQKKQKHSNHKKKKLNKKKNYLIFDSGTSFNSVPKDEIEYFFRVVPSKKCDDSNIDQVVSSYPNLTYVINKMPFTLTPSQYLVRKNDMCKPAFMEIEVSSEYGHAYILGNATFMRYYYTVYRRGNNNNSSYVGIAKAVHTEENEKYLSSLHNKINNL

3.4.23.-

entry into host cell by a symbiont-containing vacuole [GO:0085017]; protein processing [GO:0016485]

cytoplasmic vesicle [GO:0031410]; membrane [GO:0016020]; rhoptry [GO:0020008]

aspartic-type endopeptidase activity [GO:0004190]

PF00026;

2.40.70.10;

Peptidase A1 family

PTM: Autocleaved into a p55 mature form. {ECO:0000250|UniProtKB:Q8ILG2}.

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, rhoptry {ECO:0000269|PubMed:29074774}. Note=In schizonts, localizes to the bulb of rhoptries. {ECO:0000269|PubMed:29074774}.

FUNCTION: During the asexual blood stage, initiates the proteolytic maturation of several rhoptry proteins and thus, is required for merozoite invasion of host erythrocytes and probably the subsequent development of the ring-stage (PubMed:29074774). Cleaves rhoptry associated protein 1 RAP1 and apical sushi protein ASP during schizont maturation (PubMed:29074774). Also cleaves rhoptry protein RON3 (By similarity). {ECO:0000250|UniProtKB:Q8ILG2, ECO:0000269|PubMed:29074774}.

Plasmodium falciparum (isolate NF54)

A0A2I2F2I5

CFOL_ASPCN

MLRSRQATNALRAVGQTRPLRSQTAVAFTQSLNKVPSNRRSEATVATASSTASGAFNSQVRPTPSPTFNQYDSKVQPLTGMSRNVTDESFIGKTGGEIFHDMMLRQGVKHIFGYPGGAILPVFDAIYNSTHFDFILPRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNIVTPMQDALLDGTPMVVFCGQVPTTSIGSDAFQEADIVGISRPCTKWNVMVKNIAELPRRINEAFQIATTGRPGPVLVDLPKDVTAGILRRAIPTDAAIPSLPSASIQDAMDLNHKQLEASIARVAKLVNMAKQPVIYAGQGVIQSESGPELLKKLSDLASIPVTTTLQGLGGFDELDYKSLHMLGMHGSAYANMAMQEADLIIALGGRFDDRVTLNVSKFAPGARAAAAENRGGIVQFEIMPKNINKVVEATEAIVGDVGANLRLLLPHVESRSTDDRSAWYTKIDAWKKKWPLSDYQKTERHGLIKPQTLIEELSNLCADRKEKTYITTGVGQHQMWTAQHFRWRHPRTMITSGGLGTMGYGLPAAIGAKVAQPDALVVDIDGDASFNMTLTELSTAAQFNIGVKVIVLNNEEQGMVTQWQNLFYEDRYAHTHQANPDFIKIADAMGIQGQRVADPTKIKESLQWLIDTDGPALLEVITDKKVPVLPMVPGGCGLHEFIVFNPEDEKTRRGLMRERTCGLHG

2.2.1.6

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P07342}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P07342}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250|UniProtKB:P07342}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250|UniProtKB:P07342};

amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099]

acetolactate synthase complex [GO:0005948]; mitochondrion [GO:0005739]

acetolactate synthase activity [GO:0003984]; flavin adenine dinucleotide binding [GO:0050660]; magnesium ion binding [GO:0000287]; pyruvate decarboxylase activity [GO:0004737]; thiamine pyrophosphate binding [GO:0030976]

PF02775;PF00205;PF02776;

3.40.50.970;3.40.50.1220;

TPP enzyme family

SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2; Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6; Evidence={ECO:0000250|UniProtKB:P07342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25250; Evidence={ECO:0000250|UniProtKB:P07342}; CATALYTIC ACTIVITY: Reaction=2-oxobutanoate + H(+) + pyruvate = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + CO2; Xref=Rhea:RHEA:27654, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16763, ChEBI:CHEBI:49256; EC=2.2.1.6; Evidence={ECO:0000250|UniProtKB:P07342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27655; Evidence={ECO:0000250|UniProtKB:P07342};

PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4. {ECO:0000250|UniProtKB:P07342}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4. {ECO:0000250|UniProtKB:P07342}.

FUNCTION: Acetolactate synthase catalytic subunit, mitochondrial; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity (PubMed:36704842). Is not direcly involved in chlorflavonin biosynthesis but acts as a self-resistant protein that effectively confers chlorflavonin resistance to the native host (PubMed:36704842). As a catalytic subunit of mitochondrial acetolactate synthase, catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate (AHB). The first product is the precursor for valine and leucine biosynthesis, while the second leads to isoleucine (By similarity). {ECO:0000250|UniProtKB:P07342, ECO:0000269|PubMed:36704842}.

Aspergillus candidus

A0A2I2F2N6

CFOA_ASPCN

MSRPELIPDILIRHAGESCEKVAFAGPGWTITYGDLEKRTRRLAAHLVHAGIGRGDFVAIVLGRCLQTVESVLAITRAGAVGVPLDSRSPSSELAKVLEHSGARVIITDGRYLTTVRTAAAEGSLIILSTEEIPKMDAIEGKHQIARYQDWIEDAEYSTLDIQIDNLREDEQAFLHYTSGTTSLPKGVLSNQRSWLLNVNSLVSAFELTPEDRFFWPLPLFHCIGHLLCIMGTVVVGASAYLPDADQTLFDSLRDTNAQETTLIVGAPTTFHDLMDAAKRSDPTSPLFLPRLRACMYAGSSASGSLGAQIKEYLGVPLLNNYGCTEGCGSIAVSRTGHTYRHNSSISLLPHWEIKLVDPDGHPVQDGEQGEVCIGGPGLMLEYYRETRTPFTPDGWYPTGDIAIRSSSAAGAELTLVGRRKEIIIRGGENIHPHELEHVLLRHPGVADVVVAGMPHRLLGETPAAFIVKSVANMDFDLSALLAACREVLPDYKIPTAFYEIDTVPRTVIGKPKRLTMTAYTNKPLTARSMLQSRDLIEALVMAETVSACTIDAGPESESNTDWLRRHFDQPFSFLGLSSMAGVVLRDRLAGLTGLDDLPNTLVFDYSTPAAVSTYLHGRLLGPKTAPLPSSTPTTKADSEVEPIAIVSMACRYPGGISSPEDLWQLVSDEIDATTDFPDDRGWDVESLYSTDPDTPNTSTTKRGGFLPDFARFDAGLFGMAPREALATDPQQRLLLETTWELAERGGIAPLSLQGSQTGVFVGTLYEDYEENGFGNDELEAHLGLGSSSSVVSGRVSYCFGLHGPSLVVSTGCSSSLVAIHLAAQSLRNRECSLTIAGGITTMATPRPFTMFSRRRGLSSDGRCRAYSSDASGTGWSEGVGLLLLERLSDAKRNGHQILGLIRGSAVNSDGKSNGLTAPNGPAQQMCIQSALAQAGMSPENVDVLEGHGTATPLGDPIEVQAVISAYGNGDRKNIDSARRSESLLLGSIKSNIGHTQAAAAVAGIIKMVQAMRHGVAPASLHIREPSPQIDWEGSGVELLSKARQWPSVNRPRRAAVSSFGIGGTNSHIILEQPEPVQMQDSTSKRISAAFPWLISGASEVALRAQAHSLLTAWREADSNTFSPLRNQEPADIAFSLATARSALKYRATVTYALGANMHNQIETTLERLAQGEPHPDVMTAHTNTTGNKPRLACLFSGQGSWMPTIDTLEELRATFPVFSAAFQAACDEVDMHLECPLVHAITDGSMLDRTDFAQATLFVFEVAMFRLLESFGIRPDFVAGHSLGEIAAAHAAGALSLRDAATIVTTRAKLMASLPPNGGMVSIAATEAEVAIELSQFDGIASIAAVNSQTSVVVSGTQEAIQAVADRFTSLGRRATVLRNVKHGFHSQLMDHILPGLENALPSSMESENPTTIPLVSTVTGKRAAAAQLRSSNHWIRHVSEPVRFADAVNELRSKEHVSVFVEIGPSAVLSPHVPDAAATHGTVDKLLGMLGQLWARGVPVDWQAVFDGSGARFVDLPVYAFQRQRYWLPYTPLLPVTSMGAVTEQAQERTSGVFGGSRLGHEMIFNATSIPGTGTIICSGYLSTARQLWLRDHIIGGQSLVPASAFTELALRAAQECAERSEISSLILDEMIVIASLDLSSAEDEEQGEPGEVEIQVLIGESQPEDAATQNQRTVDVYSRPRGVATQHEWTQHATGTFQLISQPNPSQESFINGTDPTKAESDVNISEAYAVLSGAGLTYGPSFQGVRAIWRLHDNDLLVQIDPPQDQSQMSTSILHPAVLDAALHASTLASAEKVASGDIRLPFSFRGIQVFEAVGASSPILARIHHIGENSFSMTMTDHSSGVVLAKISEVQLRTWQPTVAGGDLYRLEWIDFASKPTTSTTTDKIVRFESSHDVDATAVSKAVHEGLAEALHAVHEWRADKSPAADEVRLVFVTERATSTGGNSDIDLVAAAVWGFVRSAQAEFGGARVALIDLDGSSESEEALTAALVSREEIVAVHGGKTMIPRLGKQPSVTEPPQAMSLDVSGTVLITGGTGGLGAMLSRDIVHAHGAKSLLLVSRSGIEATGARELYDELRSANAAVRVEACDVSDRAQLAALLDNHNHHQYPPITTVIHCAGVVSDAFLGSQTPERVSSVLRPKVDAAWNLHDLVPDTVRSFVLFSSYVSVLGNEGQAAYSAGNAFLDALARFRVARGLPALSLAWGPWANDAGMAAGSKLDAIPPRIANARPFTDQQGLSLLYRALHMQATNPSEPVLLPLLLRGPFPLVPSAGPAYKTKTNAKRESGSSAVWRRNIAAVPSENRHDTLLGLVRDEIAAVLGYQGQDMLPDQRLDDLGFDSFTSVMLTNRLRVLTGLSYLPVTLALDYDTTTALVEYLLPRIEAEPQPEVDTDSDASTTAGDTSVSRDSGKEDELSPSSSVTTLALEEQDDLNPEIFRGLATIHRRLSQLEQYTAAADLLASAALAMPTFPKTGTVLSSYAAEPQRLATGPSASSNSELPLPLVFIAPFFPRIKIEGVGLSVYSNLASAMNGKRDVFELPHPEAQAVPSDLGTLADLHVHTIRKHFSDRPGIILAGYSAGGTVAYAVASKLANAESEQPRLAGFVLVDTYLTMTGRGDPDWLNALPAEALVSRLQVPPSLGHPKGMGSDSLVGDLDVALAKVGGYFRALRDWDIGLHPLPDALSTLFVRAVDPSDKMPKDTDVWRPRWPRADLTVDVPGSHLALLDKRYAPGAAGEIERWAREDLNA

2.3.1.-; 6.3.2.-

COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|PROSITE-ProRule:PRU00258};

fatty acid biosynthetic process [GO:0006633]; flavonoid biosynthetic process [GO:0009813]; heterocycle biosynthetic process [GO:0018130]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403]

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

3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]

PF00698;PF00501;PF13193;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF14765;PF00975;

3.30.300.30;3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.40.366.10;3.40.50.12780;3.40.50.720;3.10.129.110;

NRP synthetase family

PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis. {ECO:0000269|PubMed:36704842}.

FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity (PubMed:36704842). Within the pathway, the PKS-NRPS cfoA, is responsible for the generation of the key precursor chalcone (PubMed:36704842). The adenylation (A) domain activates benzoic acid or p-hydroxybenzoic acid which are transferred to the thiol group of the pantetheinyl residue of the T domain, and further transferred to the adjacent PKS portion of cfoA. Within the PKS portion of cfoA, benzoic acid or p-hydroxybenzoic acid act as starter units for respectively four malonyl-CoA molecules for elongation by the AT and KS domains. Afterwards, chalcone is cyclized through Claisen condensation and thereby released either spontaneously or catalyzed by the TE domain (PubMed:36704842). Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3' (PubMed:36704842). {ECO:0000269|PubMed:36704842}.

Aspergillus candidus

A0A2I4E5L6

VCL6_JUGRE

MAFKPKIPIALLLLTSLLAICAGLALAMQDPELKQCKHQCRHQRQFDEQEKEHCQRSCDEYHIEKKARERAERRRSEEGSSREEGYEEEELGGEREEENPYVFEDEDFETRVRTDEGRIQVLEKFTKRSKLLRGIENFRVAILEANPQTFISPAHFDAELVVFVAKGRATITTVREEKRENFNVEQGDIMRIPAGTPVYLINRDENEKLYIVKILRPVSVPGHFEAFHGSGGEDPESFYRAFSWEVLEAALKTRRDQLEKLFGKQTQGVIIKASKEQIRSMSKHEETTPRIWPFGGDSTHPFNLFHKRPSQSNQFGRLFETDPKECKQLQDLDLMVSFANITKGSMAGPYYNSRATKISVVIEGEGYFEMACPHLSSSGSRGQREGSGSSRRRSRSGPSYQQIRGRLRPGMVFVAPAGHPVAVIASRNKNLQVLCFDVNAQGNIRFPLAGKNNIVNEFEKEAKELAFNFPAREVEKIFRNQDQEFFFPGPSRQPEEGGRAFE

protein homotrimerization [GO:0070207]; seed maturation [GO:0010431]

extraorganismal space [GO:0043245]

nutrient reservoir activity [GO:0045735]

PF00190;

2.60.120.10;

7S seed storage protein family

PTM: N-glycosylated; paucimannose-type structures containing xylose. {ECO:0000269|PubMed:30054513}.

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Denaturation starts at 45 degrees Celsius. At temperatures above 75 degrees Celsius, begins to precipitate, and eventually becomes irreversibly denatured. Cannot be resolubilized in aqueous solution after being heated up to 95 degrees Celsius and then cooled down to 25 degrees Celsius. {ECO:0000269|PubMed:30054513};

FUNCTION: Seed storage protein. {ECO:0000305|PubMed:30054513}.

Juglans regia (English walnut)

A0A2I6PJ05

GGS1_HYPPI

MVPNANSNTVSLQSPNAIPPRTSSTGYITPFPPAKSVLRPVPESDWLGQNNTRNRSSSTTAIPLTGMHATGPQDPARYETEDLNYTSRKTWSEQKEKVLVGPFEYLFAHPGKDFRTLMVNSFNAWLEVPQESLDVITKVVGMLHTASLLVDDVEDNSLLRRGLPVAHSIFGTAQTINSANYVYFCALQELQKLKNPEAINVYTEELLNLHRGQGMDLFWRDTLTCPTEEEYLEMVGNKTGGLFRLAIKLMQAESGTPIDCVPLVNILGIIFQIQDDYRNLSSPEYGQNKGLCEDLTEGKFSFLIIHSIRSNPSNLQLLNILKQKTTDDEVKRYAVKYMEGTGSFEYTQKVISILVDRARKMTDELDNGRGKSVGIHKILDKLVV

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]; mycotoxin biosynthetic process [GO:0043386]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744]

mitochondrion [GO:0005739]; transferase complex [GO:1990234]

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:29283570}.

FUNCTION: Catalyzes the trans-addition of the 3 molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranylgeranyl pyrophosphate (GGPP). GGPP is a precursor for the biosynthesis of many secondary metabolites, including the indole diterpenes nodulisporic acids (NA). {ECO:0000305|PubMed:29283570}.

Hypoxylon pulicicidum

A0A2I7G3B0

ALDH1_TANCI

MSSGANGNSKSLAYDIKFTKLFINGEFVDSISGSTFETIDPATEEVLATVAEGREEDVDLAVKAAREAFDNGPWPRLSGEARRKILLKFADLIEENADEIATLEVIDTGKPFQIARYVENSWTSETFRYFAGAADKIRGATLKMSSDFQAYTLREPIGVVGHIIPWNAPAYLFAMKVAPALAAGCTVVIKPAENTPLVGLFMAYLSKLAGVPDGVINVVNGFGSTAGAAVSSHMDIDAVTFTGSTKVGRTIMQAAAASNLKPVSLELGGKSPFIVFDDADIEKAAEIAVLGVLSNKGELCVAGSRVFVHEGIYDAFVKKLEATVKNWATGDRFDAATRHGPQNNKQQYEKVLSYIELGKKEGATLVTGGKPFGNKGYYIEPTLFTNVTDEMTIAKEEIFGPVIMVLKFKTIEEVIRRANATTYGLAAGIMTKNIDIANTVTRSIRAGSVWVNCYLALDRDTPFGGYKMSGFGREQGLEALEHYLQVKTVTTPIYNSPWL

1.2.1.-; 1.2.1.5

isoprenoid biosynthetic process [GO:0008299]

aldehyde dehydrogenase (NAD+) activity [GO:0004029]; aldehyde dehydrogenase (NADP+) activity [GO:0033721]

PF00171;

Aldehyde dehydrogenase family

CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.5; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NADP(+) = a carboxylate + 2 H(+) + NADPH; Xref=Rhea:RHEA:11888, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.5; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11889; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) + octanal = 2 H(+) + NADPH + octanoate; Xref=Rhea:RHEA:59904, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59905; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=(1R,3R)-chrysanthemal + H2O + NAD(+) = (1R,3R)-chrysanthemate + 2 H(+) + NADH; Xref=Rhea:RHEA:60708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:143899, ChEBI:CHEBI:143900; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60709; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=(1R,3R)-chrysanthemal + H2O + NADP(+) = (1R,3R)-chrysanthemate + 2 H(+) + NADPH; Xref=Rhea:RHEA:60716, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:143899, ChEBI:CHEBI:143900; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60717; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=(E)-hept-2-enal + H2O + NADP(+) = (E)-hept-2-enoate + 2 H(+) + NADPH; Xref=Rhea:RHEA:60720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:143912, ChEBI:CHEBI:143913; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60721; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=dodecanal + H2O + NADP(+) = dodecanoate + 2 H(+) + NADPH; Xref=Rhea:RHEA:60724, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:27836, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60725; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=citral + H2O + NADP(+) = 3,7-dimethylocta-2,6-dienoate + 2 H(+) + NADPH; Xref=Rhea:RHEA:60728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:23316, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142930; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60729; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) + perillyl aldehyde = 2 H(+) + NADPH + perillate; Xref=Rhea:RHEA:60732, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15421, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62641; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60733; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesal + H2O + NADP(+) = (2E,6E)-farnesoate + 2 H(+) + NADPH; Xref=Rhea:RHEA:60736, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15894, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83276; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60737; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=(S)-(-)-citronellal + H2O + NADP(+) = (S)-(-)-citronellate + 2 H(+) + NADPH; Xref=Rhea:RHEA:60740, ChEBI:CHEBI:368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:143914; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60741; Evidence={ECO:0000269|PubMed:29122986};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.6 uM for trans-chrysanthemal (in the presence of NAD(+)) {ECO:0000269|PubMed:29122986}; KM=4.4 uM for trans-chrysanthemal (in the presence of NADP(+)) {ECO:0000269|PubMed:29122986}; KM=20.4 uM for NAD(+) {ECO:0000269|PubMed:29122986}; KM=68.6 uM for NADP(+) {ECO:0000269|PubMed:29122986}; Note=kcat is 0.11 sec(-1) with trans-chrysanthemal as substrate (in the presence of NAD(+)) (PubMed:29122986). kcat is 0.096 sec(-1) with trans-chrysanthemal as substrate (in the presence of NADP(+)) (PubMed:29122986). kcat is 0.09 sec(-1) with NAD(+) as substrate (in the presence of trans-chrysanthemal) (PubMed:29122986). kcat is 0.086 sec(-1) with NADP(+) as substrate (in the presence of trans-chrysanthemal) (PubMed:29122986). {ECO:0000269|PubMed:29122986};

PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:29122986}.

FUNCTION: Component of the monoterpenoid pyrethrins biosynthesis; pyrethrins are widely used plant-derived pesticide (PubMed:30468448). Mediates the conversion of trans-chrysanthemal into trans-chrysanthemic acid (PubMed:29122986). Can also use octanal, hept-2-enal, dodecanal, citral, farnesal, citronellal and perillyl aldehyde as substrates (PubMed:29122986). {ECO:0000269|PubMed:29122986, ECO:0000303|PubMed:30468448}.

Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum cinerariifolium)

A0A2I7G3B3

ADH2_TANCI

MSLNTPDVIICKAAVVRELGRSVMVEEIKVDPPKATEVRIKMLFASICHTDMLCFDGFPTPLFPRIPGHEGVGMVESVGEDIKTKLKPGDIVMPLFMGECGQCLNCKSKRTNLCHAYPLTLSGLLLDGTSRMSIAKTEETIYHHLSCSTWSEYMVIDINYVLKIDPKMHLPYASFLSCGFTTGFGAPWKETQITKGSIVAVFGLGAVGLGAIKGAQMQGASIIIGVDINENKAAKGKAFGMTHFINPKDHPNQLVSDMVRDITDGLGVDYCFECTGIASLLKEIIEASKIGFGTTILIGAAPDNVPISSLSLINGRTLKGTTFGGVRTRSDLPIILQKCMNEEIELDELMSHEIRLENIHEIFEILKKPDCVKILINFD

1.1.1.-; 1.1.1.144; 1.1.1.347

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P40394}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P40394};

formaldehyde catabolic process [GO:0046294]; isoprenoid biosynthetic process [GO:0008299]

cytosol [GO:0005829]

alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; perillyl-alcohol dehydrogenase activity [GO:0018457]; S-(hydroxymethyl)glutathione dehydrogenase activity [GO:0051903]; zinc ion binding [GO:0008270]

PF08240;PF00107;

3.90.180.10;3.40.50.720;

Zinc-containing alcohol dehydrogenase family, Class-IV subfamily

CATALYTIC ACTIVITY: Reaction=(R,R)-chrysanthemol + NAD(+) = (1R,3R)-chrysanthemal + H(+) + NADH; Xref=Rhea:RHEA:60668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:143898, ChEBI:CHEBI:143899; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60669; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=NAD(+) + nerol = H(+) + NADH + neral; Xref=Rhea:RHEA:60672, ChEBI:CHEBI:15378, ChEBI:CHEBI:29020, ChEBI:CHEBI:29452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60673; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=(S)-(-)-citronellol + NAD(+) = (S)-(-)-citronellal + H(+) + NADH; Xref=Rhea:RHEA:60676, ChEBI:CHEBI:88, ChEBI:CHEBI:368, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60677; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=NAD(+) + perillyl alcohol = H(+) + NADH + perillyl aldehyde; Xref=Rhea:RHEA:10664, ChEBI:CHEBI:15378, ChEBI:CHEBI:15420, ChEBI:CHEBI:15421, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.144; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10665; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=(6E)-8-hydroxygeraniol + NAD(+) = (6E)-8-hydroxygeranial + H(+) + NADH; Xref=Rhea:RHEA:58848, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64235, ChEBI:CHEBI:64238; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58849; Evidence={ECO:0000269|PubMed:29122986}; CATALYTIC ACTIVITY: Reaction=(2E)-geraniol + NAD(+) = (2E)-geranial + H(+) + NADH; Xref=Rhea:RHEA:34347, ChEBI:CHEBI:15378, ChEBI:CHEBI:16980, ChEBI:CHEBI:17447, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.347; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34348; Evidence={ECO:0000269|PubMed:29122986};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=236 uM for trans-chrysanthemol {ECO:0000269|PubMed:29122986}; KM=193 uM for NAD(+) {ECO:0000269|PubMed:29122986}; Note=kcat is 0.75 sec(-1) with trans-chrysanthemol as substrate (in the presence of NAD(+)) (PubMed:29122986). kcat is 0.64 sec(-1) with NAD(+) as substrate (in the presence of trans-chrysanthemol) (PubMed:29122986). {ECO:0000269|PubMed:29122986};

PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:29122986}.

FUNCTION: Component of the monoterpenoid pyrethrins biosynthesis; pyrethrins are widely used plant-derived pesticide (PubMed:30468448). Mediates the conversion of trans-chrysanthemol into trans-chrysanthemal (PubMed:29122986). {ECO:0000269|PubMed:29122986, ECO:0000303|PubMed:30468448}.

Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum cinerariifolium)

A0A2J6L8Y7

IF4E1_LACSA

MVEEIMKSEEQKLIDVNKHRGVRSDGEEDEQLEEGEIVGGDADTLSSSSSSRPGTAIAQHPLEHSWTFWFDTPSAKSKQVAWGSSMRPIYTFSSVEEFWSLYNNIHRPSKLAQGADFYCFKNKIEPKWEDPVCANGGKWTMTFTKAKSDTCWLYTLLAMIGEQFDHGDDICGAVVNVRARQEKIALWTKNAANESAQLSIGKQWKEFIDYNDTIGFIFHEDAKTLDRSAKNKYTV

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-133-Cys-171 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}.

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:12857809). {ECO:0000250|UniProtKB:P29557, ECO:0000269|PubMed:12857809}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000269|PubMed:12857809}.

Lactuca sativa (Garden lettuce)

A0A2J8C362

CUTI1_VERDA

MQTSALLLAAQALVASAGLIERQSCPSIHVFGARETTVGPGYGSAGTVVNLILNAYPGSTAEAIVYPACGGQSSCGGISYGNSAMQGTNAVASAVNSFNQRCPNTQIVLVGYSQGGQIMDNALCGGGDPGSGITNTAVPLTASAVTAVKAAILMGSPRYRAGFPYNVGTCTAQGFAARPAGFVCPSGSKIQNYCDSPDPYCCTGNNQAVHQGYGGVYGQAALTFVRSKLNSGGSPPTTPPTTPPTTPPTTPPTTPPPSGSCAALYGQCGGQGWNGATCCSQGTCRASNQWYSQCL

3.1.1.74

carbohydrate metabolic process [GO:0005975]; symbiont entry into host [GO:0044409]

extracellular region [GO:0005576]

carboxylic ester hydrolase activity [GO:0052689]; cellulose binding [GO:0030248]

PF00734;PF01083;

3.40.50.1820;

Cutinase family

PTM: The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. {ECO:0000250|UniProtKB:P11373}.

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29068240}.

CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000305|PubMed:29068240};

FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:29068240). May degrade cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:29068240). May also degrade suberin, a specialized macromolecule found in the cell wall of various plant tissues (PubMed:29068240). Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (By similarity). Involved in pathogenesis (PubMed:29068240). {ECO:0000250|UniProtKB:P00590, ECO:0000269|PubMed:29068240}.

Verticillium dahliae (Verticillium wilt)

A0A2K1ZPK4

NRP32_POPTR

MPVEENYQPLLQEEEERAYDSDEKVLIIGVDSDTESGGSTVLPPFSWKKLWLFTGPGFLMSIAFLDPGNLEGDLQAGAIAGYSLLWLLLWATAMGLLVQLLSARLGVATGRHLAELCREEYPTWASMVLWIMAELALIGADIQEVIGSAIAIKILSNGFVPLWAGVTITACDCFIFLFLENYGVRKLEAVFAVLIGIMAVTFGWMFADAKPSASELFLGILIPKLSSRTIQQAVGVVGCIIMPHNVFLHSALVQSREIDHNKKDRVQEALRYYSIESTTALVISFVINLFVTTVFAKGFYGTELANSIGLVNAGQYLQDKYGGGFFPILYIWGIGLLAAGQSSTITGTYAGQFIMGGFLNLRLKKWLRALITRSCAIIPTMIVALVFDTSEDSLDVLNEWLNVLQSIQIPFALIPLLCLVSKEQIMGTFKIGPILKMVAWLVAALVMVINGYLLLDFFFNEVTGVAFTTVVCGFTGAYVAFIIYLISRGFTCFSRCCPSKQIEVE

defense response to bacterium [GO:0042742]; intracellular iron ion homeostasis [GO:0006879]; iron ion transmembrane transport [GO:0034755]; iron ion transport [GO:0006826]; manganese ion transmembrane transport [GO:0071421]; manganese ion transport [GO:0006828]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; regulation of vacuolar transport [GO:1903335]

plant-type vacuole membrane [GO:0009705]; vacuolar membrane [GO:0005774]

cadmium ion transmembrane transporter activity [GO:0015086]; manganese ion transmembrane transporter activity [GO:0005384]; metal ion transmembrane transporter activity [GO:0046873]

PF01566;

NRAMP (TC 2.A.55) family

SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:35700212}; Multi-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=Mn(2+)(in) = Mn(2+)(out); Xref=Rhea:RHEA:28699, ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:35700212}; CATALYTIC ACTIVITY: Reaction=Fe(2+)(in) = Fe(2+)(out); Xref=Rhea:RHEA:28486, ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:35700212};

FUNCTION: Divalent metal transporter (PubMed:35700212). Can transport manganese (Mn) and iron (Fe) (PubMed:35700212). Involved in the release of metals stored in the vacuole (PubMed:35700212). {ECO:0000269|PubMed:35700212}.

Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)

A0A2K3D5Z7

CMD1_CHLRE

MSVALASEYQLVQNAQLPQRWSQSARKSLAILEATARKEATAQMEAAGGSFCGQFPVDPAFKVLSLEYSAPNPDIARAIRRVDSVPNPPLPSHVVAIQSTAVDADLSLAMGVSLTPGRHTSYLVDARALQQSNSAAVAARKADGDKWGPACDEMFRGCRCVTGQEVVFYTAVKEPAGEVEGGEGSLFKPSFDGPAFRPSWGELSGKATGVVACVLQVPIGKETDIICAEYDNLVSKGQFATVDRFGGDHTVNMTGNALIQNDGKAISKGYAVAHRARVTSNVYGKANDVSLQRLAETVWSVVEKRLSFMPAYRDLVITEQGKPFMLGATATNIISLTENQGVMLHLDTDDGVWTIILWFHRHSGIIAGGEFVLPSLGISFQPLDFTIVVFAANTIVHGTRPLQTTGKIIRWGSSHFLRFKDVNALAQLGAAYGVDELDAKQRDQLEEVDAANSKDGVGAARRVASCMAAERKAAIEAQKAACVRGVVMNPCTGRMPSLLFWQVWRKPPALAVRANAVAGKKRAAADVDFCGA

1.14.99.-

COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:31043749, ECO:0000269|PubMed:33531488}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:33531488};

5-methylcytosine catabolic process [GO:0006211]; regulation of photosynthesis [GO:0010109]

nucleus [GO:0005634]

dioxygenase activity [GO:0051213]; iron ion binding [GO:0005506]; methylcytosine to 5-glyceryl-methylcytosine dioxygenase activity [GO:0120204]

TET family

SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.

CATALYTIC ACTIVITY: Reaction=a 5-methyl-2'-deoxycytidine in DNA + L-ascorbate + O2 = a (8S,9S)-5-glyceryl-2'-deoxycytidine in DNA + CO2 + glyoxylate; Xref=Rhea:RHEA:60132, Rhea:RHEA-COMP:11370, Rhea:RHEA-COMP:15515, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:36655, ChEBI:CHEBI:38290, ChEBI:CHEBI:85454, ChEBI:CHEBI:143613; Evidence={ECO:0000269|PubMed:31043749, ECO:0000269|PubMed:33531488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60133; Evidence={ECO:0000269|PubMed:31043749, ECO:0000269|PubMed:33531488}; CATALYTIC ACTIVITY: Reaction=a 5-methyl-2'-deoxycytidine in DNA + L-ascorbate + O2 = a (8S,9R)-5-glyceryl-2'-deoxycytidine in DNA + CO2 + glyoxylate; Xref=Rhea:RHEA:60136, Rhea:RHEA-COMP:11370, Rhea:RHEA-COMP:15516, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:36655, ChEBI:CHEBI:38290, ChEBI:CHEBI:85454, ChEBI:CHEBI:143614; Evidence={ECO:0000269|PubMed:31043749, ECO:0000269|PubMed:33531488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60137; Evidence={ECO:0000269|PubMed:31043749, ECO:0000269|PubMed:33531488};

FUNCTION: Dioxygenase that catalyzes DNA modification by mediating the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-glyceryl-methylcytosine (5gmC) (PubMed:31043749, PubMed:33531488). Catalyzes the conjugation of a glyceryl moiety from L-ascorbate (vitamin C) to the methyl group of 5mC through a carbon-carbon bond (PubMed:31043749, PubMed:33531488). 5gmC DNA modification may be required during photosynthesis as an epigenetic mark that couteracts DNA methylation (PubMed:31043749). {ECO:0000269|PubMed:31043749, ECO:0000269|PubMed:33531488}.

Chlamydomonas reinhardtii (Chlamydomonas smithii)

A0A2K3DU55

PGPP1_CHLRE

MRSVPGPSPPCTRSLAHSCRAAARGPCGSARPRARSVSARAHSSEASDMARVQQNFNSAGVGLFFSLFGGNQSLALPHLAAPDIRHVDWRALKAAGFKGLVFDKDNTLSLPFALEVEPRLQPALAGCLEAFGGRAVLYSNSAGLQQYDPEGKEAAALEAALGIPVLRHADKKPGGGCAELEAHFGCPAPQLIMVGDRYLTDIAFGNRHGMLTVHVQPLTTSGEPFGVVMARRIEEFWVARWTSFGVHPPAHSLAPHDTLAAYVKDQPIA

3.1.3.27

cardiolipin biosynthetic process [GO:0032049]; chloroplast organization [GO:0009658]; glycerolipid metabolic process [GO:0046486]; phospholipid dephosphorylation [GO:0046839]; photosynthesis [GO:0015979]; thylakoid membrane organization [GO:0010027]

chloroplast [GO:0009507]; mitochondrion [GO:0005739]

phosphatase activity [GO:0016791]; phosphatidylglycerophosphatase activity [GO:0008962]

PF09419;

3.40.50.1000;

HAD-like hydrolase superfamily

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

CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate; Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27; Evidence={ECO:0000269|PubMed:25910650}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33752; Evidence={ECO:0000269|PubMed:25910650};

PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2. {ECO:0000269|PubMed:25910650}.

FUNCTION: Phosphatidylglycerophosphate phosphatase involved in the biosynthesis of phosphatidylglycerol (PG), a phosphoglycerolipid predominantly present in chloroplastic thylakoid membranes and which has important photosynthetic function (PubMed:25910650). Required for thylakoid membranes development and chloroplast function (By similarity). {ECO:0000250|UniProtKB:Q9LXR9, ECO:0000269|PubMed:25910650}.

Chlamydomonas reinhardtii (Chlamydomonas smithii)

A0A2K3DZC4

BSD2_CHLRE

MNSAALNARTASVAPQPQACHACKCRQLLSRRVPPAQRQVECSAIAPETLQDIIVGGAVVGAVSVALYAGLKKDPVPCSLCQGTGGIRCFACGGDGRNATVSRDDLYDSKALGGGVAPPKRDPLGRTINPRDCKVCRGAGLVLCSQCKGTGFQSAF

chaperone-mediated protein folding [GO:0061077]; ribulose bisphosphate carboxylase complex assembly [GO:0110102]

chloroplast stroma [GO:0009570]; protein folding chaperone complex [GO:0101031]

metal ion binding [GO:0046872]; protein folding chaperone [GO:0044183]

BSD2 chaperone family

SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:25124725}. Note=Associates with chloroplastic polysomes. {ECO:0000269|PubMed:25124725}.

FUNCTION: Chloroplast chaperone required for RuBisCo biogenesis and translational regulation of the RuBisCo large subunit (RbcL) (PubMed:25124725). Stabilizes an end-state assembly intermediate of eight RbcL subunits until the small subunits (RBCSs) become available to produce a complete stable RuBisCo complex containing eight small and eight large subunits (By similarity). {ECO:0000250|UniProtKB:Q9SN73, ECO:0000269|PubMed:25124725}.

Chlamydomonas reinhardtii (Chlamydomonas smithii)

A0A2K5QCI5

APOA1_CEBIM

MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDSVKDSGRDYVSQFESSALGKQLNLKLLDNWDSLTSTVNKLREDLGPVTQEFWDNLEKETGWLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEVKLYSQKLEPLRTEFQEGALQKLQDLQEKLSPLAEQVRDRARAHVDTLRTQLAPYSDELRQRLATRLEVLKESGGASLAEYHAKASEHLSALGEKAKPALEDLRQGLLPVLESFKVSFLSALEEYAKKLSSQ

adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor signaling pathway [GO:0007186]; glucocorticoid metabolic process [GO:0008211]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle remodeling [GO:0034375]; integrin-mediated signaling pathway [GO:0007229]; lipid storage [GO:0019915]; lipoprotein biosynthetic process [GO:0042158]; negative regulation of cell adhesion molecule production [GO:0060354]; negative regulation of cytokine production involved in immune response [GO:0002719]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; negative regulation of very-low-density lipoprotein particle remodeling [GO:0010903]; phosphatidylcholine biosynthetic process [GO:0006656]; phospholipid efflux [GO:0033700]; phospholipid homeostasis [GO:0055091]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of cholesterol metabolic process [GO:0090205]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phospholipid efflux [GO:1902995]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; protein stabilization [GO:0050821]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of intestinal cholesterol absorption [GO:0030300]; regulation of protein phosphorylation [GO:0001932]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; vitamin transport [GO:0051180]

endocytic vesicle [GO:0030139]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361]

amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803]

PF01442;

1.20.5.20;6.10.140.380;1.20.120.20;

Apolipoprotein A1/A4/E family

PTM: Glycosylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}.

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02647}.

FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. {ECO:0000250|UniProtKB:P02647}.

Cebus imitator (Panamanian white-faced capuchin) (Cebus capucinus imitator)

A0A2K5TU92

SIR6_MACFA

MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVWQSSHVVFHTGAGISTASGIPDFRGPHGVWTMEERGLAPKFDTTFESARPTQTHMALVQLERVGLLRFLVSQNVDGLHVRSGFPRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKATGRLCTVAKARGLRACRGELRDTILDWEDSLPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGRLVIVNLQPTKHDRHADLRIHGYVDEVMTRLMKHLGLEIPAWDGPHVLERALPPLPRPPTPKLEPKEESPTRINGSIPAGSCLEPCAQHNGSEPASPKRERPTSPAPNRPPKRVKAEAVPS

2.3.1.-; 2.3.1.286; 2.4.2.-

cardiac muscle cell differentiation [GO:0055007]; circadian regulation of gene expression [GO:0032922]; double-strand break repair [GO:0006302]; ketone biosynthetic process [GO:0042181]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of glycolytic process [GO:0045820]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; neuron differentiation [GO:0030182]; pericentric heterochromatin formation [GO:0031508]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of insulin secretion [GO:0032024]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of protein localization to chromatin [GO:0120187]; positive regulation of stem cell differentiation [GO:2000738]; protein delipidation [GO:0051697]; protein destabilization [GO:0031648]; regulation of circadian rhythm [GO:0042752]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of lipid catabolic process [GO:0050994]; regulation of lipid metabolic process [GO:0019216]; retrotransposon silencing [GO:0010526]

chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]

chromatin DNA binding [GO:0031490]; damaged DNA binding [GO:0003684]; DNA damage sensor activity [GO:0140612]; metal ion binding [GO:0046872]; NAD+ binding [GO:0070403]; NAD+-protein-arginine ADP-ribosyltransferase activity [GO:0106274]; NAD-dependent histone H3K18 deacetylase activity [GO:0097372]; NAD-dependent histone H3K56 deacetylase activity [GO:0140765]; NAD-dependent histone H3K9 deacetylase activity [GO:0046969]; NAD-dependent protein deacetylase activity [GO:0034979]; NAD-dependent protein demyristoylase activity [GO:0140773]; NAD-dependent protein depalmitoylase activity [GO:0140774]; nucleosome binding [GO:0031491]; nucleotidyltransferase activity [GO:0016779]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; TORC2 complex binding [GO:1904841]; transcription corepressor activity [GO:0003714]

PF02146;

2.20.28.200;3.40.50.1220;

Sirtuin family, Class IV subfamily

PTM: Acetylated at Lys-33. Deacetylation at Lys-33 by SIRT1 promotes homomultimerization and binding to double-strand breaks (DSBs) sites. {ECO:0000250|UniProtKB:Q8N6T7}.; PTM: Phosphorylation at Ser-10 by MAPK8/JNK1 in response to oxidative stress stimulates the mono-ADP-ribosyltransferase activity on PARP1, leading to PARP1 recruitment to double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q8N6T7}.; PTM: Monoubiquitinated at Lys-170 by STUB1/CHIP, preventing its degradation by the proteasome. {ECO:0000250|UniProtKB:Q8N6T7}.; PTM: Sumoylated, leading to specifically decrease ability to deacetylate histone H3 at 'Lys-56' (H3K56ac). {ECO:0000250|UniProtKB:Q8N6T7}.

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P59941}. Chromosome {ECO:0000250|UniProtKB:Q8N6T7}. Chromosome, telomere {ECO:0000250|UniProtKB:Q8N6T7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P59941}. Note=Predominantly nuclear. Associated with pericentric heterochromatin and telomeric heterochromatin regions. Localizes to DNA damage sites: directly recognizes and binds double-strand breaks (DSBs) sites via a tunnel-like structure that has high affinity for DSBs (By similarity). A fraction localizes to the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P59941, ECO:0000250|UniProtKB:Q8N6T7}.

CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:30135584}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43637; Evidence={ECO:0000269|PubMed:30135584}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-tetradecanoyl-L-lysyl-[protein] + NAD(+) = 2''-O-tetradecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:70567, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15437, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:141129, ChEBI:CHEBI:189674; Evidence={ECO:0000250|UniProtKB:Q8N6T7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70568; Evidence={ECO:0000250|UniProtKB:Q8N6T7}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-hexadecanoyl-L-lysyl-[protein] + NAD(+) = 2''-O-hexadecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:70563, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14175, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:138936, ChEBI:CHEBI:189673; Evidence={ECO:0000250|UniProtKB:Q8N6T7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70564; Evidence={ECO:0000250|UniProtKB:Q8N6T7}; CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + NAD(+) = H(+) + N(6)-(ADP-D-ribosyl)-L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58220, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15088, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:142515; Evidence={ECO:0000250|UniProtKB:P59941}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58221; Evidence={ECO:0000250|UniProtKB:P59941}; CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, ChEBI:CHEBI:142554; Evidence={ECO:0000250|UniProtKB:P59941}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19150; Evidence={ECO:0000250|UniProtKB:P59941};

FUNCTION: NAD-dependent protein deacetylase, deacylase and mono-ADP-ribosyltransferase that plays an essential role in DNA damage repair, telomere maintenance, metabolic homeostasis, inflammation, tumorigenesis and aging (PubMed:30135584). Displays protein-lysine deacetylase or defatty-acylase (demyristoylase and depalmitoylase) activity, depending on the context (By similarity). Acts as a key histone deacetylase by catalyzing deacetylation of histone H3 at 'Lys-9', 'Lys-18' and 'Lys-56' (H3K9ac, H3K18ac and H3K56ac, respectively), suppressing target gene expression of several transcription factors, including NF-kappa-B (PubMed:30135584). Acts as an inhibitor of transcription elongation by mediating deacetylation of H3K9ac and H3K56ac, preventing release of NELFE from chromatin and causing transcriptional pausing (By similarity). Involved in DNA repair by promoting double-strand break (DSB) repair: acts as a DSB sensor by recognizing and binding DSB sites, leading to (1) recruitment of DNA repair proteins, such as SMARCA5/SNF2H, and (2) deacetylation of histone H3K9ac and H3K56ac (By similarity). SIRT6 participation to DSB repair is probably involved in extension of life span (By similarity). Also promotes DNA repair by deacetylating non-histone proteins, such as DDB2 and p53/TP53 (By similarity). Specifically deacetylates H3K18ac at pericentric heterochromatin, thereby maintaining pericentric heterochromatin silencing at centromeres and protecting against genomic instability and cellular senescence (By similarity). Involved in telomere maintenance by catalyzing deacetylation of histone H3 in telomeric chromatin, regulating telomere position effect and telomere movement in response to DNA damage (By similarity). Required for embryonic stem cell differentiation by mediating histone deacetylation of H3K9ac (By similarity). Plays a major role in metabolism by regulating processes such as glycolysis, gluconeogenesis, insulin secretion and lipid metabolism (By similarity). Inhibits glycolysis via histone deacetylase activity and by acting as a corepressor of the transcription factor HIF1A, thereby controlling the expression of multiple glycolytic genes (By similarity). Has tumor suppressor activity by repressing glycolysis, thereby inhibiting the Warburg effect (By similarity). Also regulates glycolysis and tumorigenesis by mediating deacetylation and nuclear export of non-histone proteins, such as isoform M2 of PKM (PKM2) (By similarity). Acts as a negative regulator of gluconeogenesis by mediating deacetylation of non-histone proteins, such as FOXO1 and KAT2A/GCN5 (By similarity). Promotes beta-oxidation of fatty acids during fasting by catalyzing deacetylation of NCOA2, inducing coactivation of PPARA (By similarity). Acts as a regulator of lipid catabolism in brown adipocytes, both by catalyzing deacetylation of histones and non-histone proteins, such as FOXO1 (By similarity). Also acts as a regulator of circadian rhythms, both by regulating expression of clock-controlled genes involved in lipid and carbohydrate metabolism, and by catalyzing deacetylation of PER2 (By similarity). The defatty-acylase activity is specifically involved in regulation of protein secretion (By similarity). Has high activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins, such as RRAS2 and TNF, thereby regulating their secretion (By similarity). Also acts as a mono-ADP-ribosyltransferase by mediating mono-ADP-ribosylation of PARP1, TRIM28/KAP1 or SMARCC2/BAF170 (By similarity). Mono-ADP-ribosyltransferase activity is involved in DNA repair, cellular senescence, repression of LINE-1 retrotransposon elements and regulation of transcription (By similarity). {ECO:0000250|UniProtKB:P59941, ECO:0000250|UniProtKB:Q8N6T7, ECO:0000269|PubMed:30135584}.

Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)

A0A2K8FQU5

TAT_CATRO

MASKMVEIVSKMFIKPSSPTPQSLRRYNLSSIDQTIDSEVTSLAFFYTYNPSHESSKIGDLLKNSLSKTLVSYYQFAGRLIENDYIDCNDEGVEFVEVRIHGRMNDILKRGKSFATDLVLPTRIIALHEDSLLIVQLSHFDCGGIAIGFGASHKVSDGVSNVMFMKDWASSTSLSTFHKPTPLLTADSIFPPEDNKLLSNKSIVSFQQCLGKRFVFSTEAIEKLKSKAIEYGIQKPSRVEVVTAFLCQCAANCDLPRKKPYAIISAVNLRPYLALPQNSIGNIFSFYFCINDEGMDNQFSALISKLRNGKQKLLENIISKEKLTYESQMQELTKCLDQLNISSLDTYFCSSWCRFPVYDIDFGWGKPILVSPFQPHVKDLILLMDSPEGDGIEALITMEEKKMAAFEKNEELRSFAYLDSPEPEALIIPEEDKSFE

2.3.1.-

indole alkaloid biosynthetic process [GO:0035835]; response to jasmonic acid [GO:0009753]

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

acetyltransferase activity [GO:0016407]

PF02458;

3.30.559.10;

Plant acyltransferase family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29438577}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:29438577}.

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + horhammericine = 19-O-acetylhorhammericine + CoA; Xref=Rhea:RHEA:61068, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:144375, ChEBI:CHEBI:144376; Evidence={ECO:0000269|PubMed:29438577, ECO:0000269|PubMed:31009114}; CATALYTIC ACTIVITY: Reaction=(-)-(R)-19-hydroxytabersonine + acetyl-CoA = (-)-(R)-19-O-acetyltabersonine + CoA; Xref=Rhea:RHEA:61072, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:144372, ChEBI:CHEBI:144377; Evidence={ECO:0000269|PubMed:29438577, ECO:0000269|PubMed:31009114}; CATALYTIC ACTIVITY: Reaction=(-)-minovincinine + acetyl-CoA = (-)-echitovenine + CoA; Xref=Rhea:RHEA:61076, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:144373, ChEBI:CHEBI:144384; Evidence={ECO:0000269|PubMed:29438577, ECO:0000269|PubMed:31009114};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for acetyl-CoA (at pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:29438577}; KM=9 uM for (-)-minovincinine (at pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:29438577}; KM=58 uM for horhammericine (at pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:29438577}; KM=78 uM for 19-hydroxytabersonine (at pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:29438577}; Vmax=0.14 umol/sec/ug enzyme toward acetyl-CoA (at pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:29438577}; Vmax=0.13 umol/sec/ug enzyme with (-)-minovincinine as substrate (at pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:29438577}; Vmax=0.02 umol/sec/ug enzyme with horhammericine as substrate (at pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:29438577}; Vmax=1.32 umol/sec/ug enzyme with 19-hydroxytabersonine as substrate (at pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:29438577};

PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:31009114}.

FUNCTION: Component of the monoterpenoid indole alkaloids (MIAs, e.g. echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and horhammericine) biosynthetic pathway; MIAs are used in cancer treatment and other medical applications (PubMed:31009114). Acyltransferase catalyzing the conversion of horhammericine to 19-O-acetylhorhammericine, of 19-hydroxytabersonine to 19-O-acetyltabersonine and of minovincinine to echitovenine (PubMed:29438577, PubMed:31009114). {ECO:0000269|PubMed:29438577, ECO:0000269|PubMed:31009114}.

Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)

A0A2K9RFZ2

TPS2_VITAC

MSLRFNLIVTPFSNHRIRNRRETFPAQEFPVATSKSAVKVKCNLITSTDLVGKVREKINGKVDNSLEVPAIHPVDIPSNLCMIDTLERLGVDRYFQSEIDGVLEETYRLWQQKEKDIFADVTCRAMAFRLLRVKGYEVSSDELAPYADQAHVNLQISDVTAVIELYRASQERIYEEESTLEKLHAWTSTYLKQQLVSGTISDKKLHKQVEYYLKNYHGILDLVGIRRSLDLYDIDHYQILKAADRFRTICKDLLAFSRQDFNNCQAQYQRELQLLQRWYEDCRLDKLNYGRDVLRISYFVSSAIIGDPELSDARLAFAKYCVLTTCIDDFFDHAGSREESYRILELVKEWKEKPAEDYGSKEVEFLFTAVYNTVNELAEMAYVEQGRCVKSLLIKLWVELLTSFKKELDSWTDDTALSLDEYLSSSWVSITSRINILTSIQFLGLKLSEEMLSSQECTDLCRHGSLVVRLLNDMQTFEKERRENTKNSVSILLEAPKHEGAITEEEVISKIKEIVEQNRRKLMQMVYQRGTIFPRKCKDVFLKSCRGGYYLYSNGDEFTSPVQIMEDMKLCYEPLTFHPLEANNGGNKN

4.2.3.-; 4.2.3.189

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q40577}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};

gibberellin biosynthetic process [GO:0009686]

chloroplast [GO:0009507]

(13S)-vitexifolin A synthase activity [GO:0062204]; 9,13-epoxylabda-14-ene synthase activity [GO:0106239]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]; Viteagnusin D synthase activity [GO:0062203]

PF01397;PF03936;

1.10.600.10;1.50.10.130;

Terpene synthase family

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

CATALYTIC ACTIVITY: Reaction=9alpha-copalyl diphosphate + H2O = (13S)-vitexifolin A + diphosphate; Xref=Rhea:RHEA:40027, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58622, ChEBI:CHEBI:76954; Evidence={ECO:0000269|PubMed:29315936}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40028; Evidence={ECO:0000269|PubMed:29315936}; CATALYTIC ACTIVITY: Reaction=peregrinol diphosphate = (13R)-9,13-epoxylabd-14-ene + diphosphate; Xref=Rhea:RHEA:54512, ChEBI:CHEBI:33019, ChEBI:CHEBI:138232, ChEBI:CHEBI:138233; EC=4.2.3.189; Evidence={ECO:0000269|PubMed:29315936}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54513; Evidence={ECO:0000269|PubMed:29315936}; CATALYTIC ACTIVITY: Reaction=H2O + peregrinol diphosphate = diphosphate + viteagnusin D; Xref=Rhea:RHEA:62180, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:138232, ChEBI:CHEBI:145543; Evidence={ECO:0000269|PubMed:29315936}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62181; Evidence={ECO:0000269|PubMed:29315936};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:29315936, ECO:0000305|PubMed:30468448}.

FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid including cleroda-dienols, and peregrinol lactones and furan derivatives, dopaminergic diterpenoids that can bind to dopamine receptors in the human pituitary gland, have probably ability to lower prolactin levels, and are used to treat menstrual cycle disorders (e.g. premenstrual syndrome and mastodynia) (Probable). Terpene synthase the catalyzes the conversion of peregrinol diphosphate to viteagnusin D and 9,13(R)-epoxy-labd-14-ene, and of syn-copalyl diphosophate to vitexifolin A (PubMed:29315936). {ECO:0000269|PubMed:29315936, ECO:0000305|PubMed:12809367, ECO:0000305|PubMed:29315936, ECO:0000305|PubMed:30468448}.

Vitex agnus-castus (Chaste tree)

A0A2L0ART2

TXF1A_SCOMU

MEKKIIFLVFLVALLALPGFISTEVIKKDTPYKKRKFPYKSECLKACATSFTGGDESRIQEGKPGFFKCTCYFTTG

envenomation resulting in positive regulation of blood pressure in another organism [GO:0044499]; negative regulation of voltage-gated potassium channel activity [GO:1903817]; positive regulation of vasoconstriction [GO:0045907]

extracellular region [GO:0005576]

potassium channel regulator activity [GO:0015459]; toxin activity [GO:0090729]

Scoloptoxin-15 family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29358396}.

FUNCTION: Blocks voltage-gated potassium channels Kv7.4/KCNQ4 (IC(50)=2.5 uM), Kv7.1/KCNQ1 (IC(50)=2.8 uM), Kv7.2/KCNQ2 (IC(50)=2.7 uM) and Kv7.5/KCNQ5 (IC(50)=2.7 uM). Targets the pore domain, in particular negatively charged residues 'Asp-266' and 'Asp-288', of KCNQ4 and probably other KCNQ channel family members where these residues are conserved. In vivo, shows vasoconstrictive activity resulting in acute hypertension when injected intravenously in mice. Also induces coronary vasospasms ultimately leading to heart failure. Induces seizures when injected into the hippocampus of mice. Decreases respiratory rate while increasing respiratory amplitude, probably by triggering a contraction of the bronchial ring. {ECO:0000269|PubMed:29358396}.

Scolopendra mutilans (Chinese red-headed centipede) (Scolopendra subspinipes mutilans)

A0A2L0VXR5

PLE4_CLIPA

MRIPNVFLSYLRQVAVDGTLSSCSGVKSRKPVIAYGFDDSQDSLVDENDEKILEPFGYYRHLLKGKSARTVLMHCFNAFLGLPEDWVIGVTKAIEDLHNASLLIDDIEDESALRRGSPAAHMKYGIALTMNAGNLVYFTVLQDVYDLGMKTGGTQVANAMARIYTEEMIELHRGQGIEIWWRDQRSPPSVDQYIHMLEQKTGGLLRLGVRLLQCHPGVNNRADLSDIALRIGVYYQLRDDYINLMSTSYHDERGFAEDMTEGKYTFPMLHSLKRSPDSGLREILDLKPADIALKKKAIAIMQDTGSLVATRNLLGAVKNDLSGLVAEQRGDDYAMSAGLERFLEKLYIAE

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 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};

antibiotic biosynthetic process [GO:0017000]; plastoquinone biosynthetic process [GO:0010236]; terpenoid biosynthetic process [GO:0016114]; ubiquinone biosynthetic process [GO:0006744]

mitochondrion [GO:0005739]; transferase complex [GO:1990234]

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; terpenoid biosynthesis. {ECO:0000269|PubMed:27143514, ECO:0000269|PubMed:29388775}.

FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of pleuromutilin, a tricyclic diterpene showing antibacterial properties (PubMed:27143514, PubMed:29388775). The geranylgeranyl diphosphate (GGPP) synthase catalyzes the first step in pleuromutilin biosynthesis (PubMed:27143514, PubMed:29388775). GGPP is then substrate of the premutilin synthase (PS) to yield premutilin (PubMed:29388775). Premutilin synthase is a bifunctional enzyme composed of the fusion of a class II diterpene cyclase (DTC) and a class I diterpene synthase (DTS), with the corresponding domains and active sites containing characteristic aspartate-rich motifs. GGPP is first converted to mutildienyl-diphosphate (MPP) at the class II DTC site (PubMed:29388775). MPP is subsequently further cyclized at the class I DTS site, followed by a 1,5-hydride shift and addition of water prior to terminating deprotonation, to yield premutilin (PubMed:29388775). In addition to the aforementioned GGPP synthase and bifunctional diterpene synthase, the cluster contains also three cytochrome P450 monooxygenases, a short-chain alcohol dehydrogenase, and an acyltransferase, involved in the conversion of premutilin to pleuromutilin (PubMed:27143514, PubMed:29388775). The cytochrome P450 monooxygenases P450-1 and P450-2 hydroxylate premutilin at C-11 and C-3, respectively, producing 11-hydroxypremutilin and 3-hydroxypremutilin (By similarity). The combination of the actions of both ple5 and ple6 leads to the production of 3,11-dihydroxypremutilin (By similarity). The short chain dehydrogenase SDR further converts 3,11-dihydroxypremutilin into mutilin (By similarity). The acetyltransferase ATF then acetylates mutilin to produce 14-O-acetylmutilin (By similarity). Finally, the cytochrome P450 monooxygenase P450-3 catalyzes hydroxylation on the alpha position of the acetyl side chain of 14-O-acetylmutilin to yield pleuromutilin (By similarity). {ECO:0000250|UniProtKB:A0A6S6QJ62, ECO:0000269|PubMed:27143514, ECO:0000269|PubMed:29388775}.

Clitopilus passeckerianus (Pleurotus passeckerianus)

A0A2L2DDD0

FIG02_BOARA

MAFLKKSLFLVLFLGIVSLSVCEEEKREGEEKEEKREEEEGKEENEDGNEEHKEKRFLGAILKIGHALAKTVLPMVTNAFKPKQ

defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; defense response to protozoan [GO:0042832]; defense response to virus [GO:0051607]; hemolysis in another organism [GO:0044179]; innate immune response [GO:0045087]; regulation of defense response to virus [GO:0050688]

extracellular region [GO:0005576]

PF03032;

Frog skin active peptide (FSAP) family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32443921}.

FUNCTION: Antimicrobial peptide that displays antibacterial, antiprotozoal, and antiviral activity (PubMed:32443921). Exhibits antibacterial activity against the Gram-positive bacteria S.epidermidis ATCC 12228 (MIC=4 uM), E.casseliflavus ATCC 700327 (MIC=4 uM), S.aureus ATCC 25923 (MIC=8 uM) and E.faecalis ATCC 29212 (MIC=8 uM), and the Gram-negative bacteria E.coli ATCC 25922 (MIC=8 uM), K.pneumoniae ATCC 13883 (MIC=8 uM), the multi-resistant clinical isolate strain K.pneumoniae carbapanemase (KPC) MR (MIC=16 uM), and P.aeruginosa ATCC 27853 (MIC=32 uM) (PubMed:32443921). Displays antiprotozoal activity against the epimastigote form of T.cruzi (IC(50)=6.32 uM) (PubMed:32443921). Does not show antimicrobial against the fungi C.albicans ATCC 90028 and C.parapsilosis ATCC 22019 (PubMed:32443921). Displays antiviral activity against the human viruses chikungunya (EC(50)=17.9 uM), Dengue serotype 4 (EC(50)=20.8 uM) and Yellow Fever (EC(50)=21.8 uM) (PubMed:32443921). Shows moderate cytolytic activity against human erythrocytes (HC(50)=48.9 uM), and activates the oxidative burst in human neutrophils (PubMed:32443921). Also displays anti-proliferative effects against MCF-7 breast cancer cells (IC(50)=15.3 uM) and B16F10 murine melanoma cells (IC(50)=12.8 uM) (PubMed:32443921). {ECO:0000269|PubMed:32443921}.

Boana raniceps (Chaco tree frog) (Hyla roeschmanni)

A0A2L2DDE6

FIG01_BOARA

MAFLKKSLFLVLFLGLVSLSIGEEEKREEEEKNEEGANQEENAENKEKRFIGTLIPLALGALTKLFKG

defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; defense response to protozoan [GO:0042832]; hemolysis in another organism [GO:0044179]; innate immune response [GO:0045087]

extracellular region [GO:0005576]

PF03032;

Frog skin active peptide (FSAP) family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32967114}.

FUNCTION: Antimicrobial peptide that displays antibacterial and antiprotozoal activity (PubMed:32967114). Exhibits antibacterial activity against the Gram-positive bacteria S.epidermidis ATCC 12228 (MIC=2 uM), E.casseliflavus ATCC 700327 (MIC=16 uM), S.aureus ATCC 25923 (MIC=4 uM) and E.faecalis ATCC 29212 (MIC=8 uM), and the Gram-negative bacteria E.coli ATCC 25922 (MIC=16 uM) and K.pneumoniae ATCC 13883 (MIC=4 uM) (PubMed:32967114). Displays antiprotozoal activity against the epimastigote form of T.cruzi (IC(50)=15.9 uM) (PubMed:32967114). Does not show antimicrobial activity against the Gram-negative bacterium P.aeruginosa ATCC 27853, or the fungi C.albicans ATCC 90028 and C.parapsilosis ATCC 22019 (PubMed:32967114). Shows high cytolytic activity against human erythrocytes (HC(50)=10 uM), and displays anti-proliferative effects against various cancer cell lines including MCF-7 breast cancer cells (IC(50)=13.7 uM), HeLa cervical adenocarcinoma cells (IC(50)=11.1 uM) and B16F10 murine melanoma cells (IC(50)=10.5 uM) (PubMed:32967114). {ECO:0000269|PubMed:32967114}.

Boana raniceps (Chaco tree frog) (Hyla roeschmanni)