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lhallee

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A0A009IHW8

ABTIR_ACIB9

MSLEQKKGADIISKILQIQNSIGKTTSPSTLKTKLSEISRKEQENARIQSKLSDLQKKKIDIDNKLLKEKQNLIKEEILERKKLEVLTKKQQKDEIEHQKKLKREIDAIKASTQYITDVSISSYNNTIPETEPEYDLFISHASEDKEDFVRPLAETLQQLGVNVWYDEFTLKVGDSLRQKIDSGLRNSKYGTVVLSTDFIKKDWTNYELDGLVAREMNGHKMILPIWHKITKNDVLDYSPNLADKVALNTSVNSIEEIAHQLADVILNR

3.2.2.-; 3.2.2.6

NAD catabolic process [GO:0019677]; signal transduction [GO:0007165]

NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NADP+ nucleosidase activity [GO:0050135]

PF13676;

3.40.50.10140;

CATALYTIC ACTIVITY: Reaction=NAD(+) = 2'cADPR + H(+) + nicotinamide; Xref=Rhea:RHEA:75299, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:194248; Evidence={ECO:0000269|PubMed:36048923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75300; Evidence={ECO:0000269|PubMed:36048923}; CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000269|PubMed:29395922, ECO:0000269|PubMed:36048923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000269|PubMed:29395922, ECO:0000269|PubMed:36048923}; CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) + nicotinamide; Xref=Rhea:RHEA:19849, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:58349, ChEBI:CHEBI:58673; Evidence={ECO:0000269|PubMed:36048923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19850; Evidence={ECO:0000269|PubMed:36048923};

FUNCTION: NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide (PubMed:29395922). In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed 2'cADPR (v-cADPR) (PubMed:29395922, PubMed:36048923). Cleaves NADP(+), but does not cyclize the product (PubMed:36048923). {ECO:0000269|PubMed:29395922, ECO:0000269|PubMed:36048923}.

Acinetobacter baumannii (strain 1295743)

A0A023I7E1

ENG1_RHIMI

MRFQVIVAAATITMITSYIPGVASQSTSDGDDLFVPVSNFDPKSIFPEIKHPFEPMYANTENGKIVPTNSWISNLFYPSADNLAPTTPDPYTLRLLDGYGGNPGLTIRQPSAKVLGSYPPTNDVPYTDAGYMINSVVVDLRLTSSEWSDVVPDRQVTDWDHLSANLRLSTPQDSNSYIDFPIVRGMAYITANYNNLTPQFLSQHAIISVEADEKKSDDNTSTFSGRKFKITMNDDPTSTFIIYSLGDKPLELRKQDNSNLVASKPYTGVIRVAKLPAPEFETLLDASRAVWPTGGDISARSDDNNGASYTIKWKTNSNEAPLLTYAYAHHLTSIDDSNVKRTDMTLQSATKGPMTALVGNEWTLRETELSPVEWLPLQAAPNPTTINEIMTEINKDIASNYTQETAKEDNYFSGKGLQKFAMLALILNKSDQTQLRNPELAQIALDKLKAAFLPYLQNEQADPFRYDTLYKGIVAKAGLPTSMGGTDDLSAEFGHSYYSDHHYHQGYFVVTAAIIHHLDPTWNADRLKAWTEALIRDVNNANDGDEYFAAFRNWDWFAGHSWAGGIKPDGALDGRDQESVPESVNFYWGAKLWGLATGNTPLTKLASLQLAVTKRTTYEYFWMLDGNKNRPENIVRNKVIGIYFEQKTDYTTYFGRFLEYIHGIQQLPMTPELMEYIRTPEFVSQEWDEKLGAIAPTVQSPWAGVLYLNYAIINPAEAYPALRKVQMDDGQTRSYSLYLTATRPHFFRRSLLAALARHGSTRRPSLPSSGDDDKHEDGFLLRFRRLNPFNLKHRIY

3.2.1.39

cell wall organization [GO:0071555]; polysaccharide catabolic process [GO:0000272]

cell surface [GO:0009986]; extracellular region [GO:0005576]

glucan endo-1,3-beta-D-glucosidase activity [GO:0042973]; glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group [GO:0052861]; glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group [GO:0052862]

PF17652;PF03639;

1.10.287.1170;1.20.5.420;

Glycosyl hydrolase 81 family

SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250|UniProtKB:P53753}.

CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000269|PubMed:34801773};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:34801773};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:34801773};

FUNCTION: Cleaves internal linkages in 1,3-beta-glucan. {ECO:0000269|PubMed:34801773}.

Rhizomucor miehei

A0A024B7W1

POLG_ZIKVF

MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAVKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPMLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGDEEKYMDYLSTQVRYLGEEGSTPGVL

2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13

clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; negative regulation of innate immune response [GO:0045824]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity [GO:0039574]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]

centrosome [GO:0005813]; extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036]

4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198]

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

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

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

PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site. {ECO:0000250|UniProtKB:P17763}.; PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.; PTM: [Envelope protein E]: N-glycosylation plays a role in virulence in mammalian and mosquito hosts, but may have no effect on neurovirulence. {ECO:0000269|PubMed:29091758}.; PTM: [Envelope protein E]: Ubiquitination by host TRIM7 promotes virus attachment and fusion of the virus and the host endosome membrane. {ECO:0000250|UniProtKB:A0A142I5B9}.; PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is glycosylated, which is required for efficient secretion of the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.; PTM: [Non-structural protein 1]: Ubiquitination by host TRIM22 leads to proteasomal degradation. {ECO:0000269|PubMed:36042495}.; PTM: [Serine protease NS3]: Ubiquitination by host TRIM22 leads to proteasomal degradation. {ECO:0000269|PubMed:36042495}.; PTM: [Serine protease NS3]: Acetylated by host KAT5. Acetylation modulates NS3 RNA-binding and unwinding activities and plays an important positive role for viral replication. {ECO:0000250|UniProtKB:Q32ZE1}.; PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. {ECO:0000250|UniProtKB:P17763}.; PTM: [RNA-directed RNA polymerase NS5]: Sumoylated, required for regulating IFN induced interferon stimulated genes/ISGs. {ECO:0000269|PubMed:32699085}.

SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000269|PubMed:36594413}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q32ZE1}. Host nucleus {ECO:0000269|PubMed:32699085}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.

CATALYTIC ACTIVITY: [RNA-directed RNA polymerase NS5]: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase NS5]: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539, ECO:0000269|PubMed:30951555}; CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; Evidence={ECO:0000250|UniProtKB:Q32ZE1}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:Q32ZE1}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q9Q6P4};

FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of the mature virus particle (By similarity). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins (By similarity). Can migrate to the cell nucleus where it modulates host functions (By similarity). Inhibits the integrated stress response (ISR) in the infected cell (PubMed:28592527). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:28592527}.; FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}.; FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH 6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Plays a role in host immune defense modulation and protection of envelope protein E during virion synthesis. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion. Contributes to fetal microcephaly in humans. Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Envelope protein E]: Binds to host cell surface receptors and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HAVCR1 in a cell-type specific manner (By similarity). In addition, host NCAM1 can also be used as entry receptor (By similarity). Interaction with host HSPA5 plays an important role in the early stages of infection as well (By similarity). Envelope protein is synthesized in the endoplasmic reticulum and forms a heterodimer with protein prM. The heterodimer plays a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimers between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes the dissociation of PrM-E heterodimers and formation of E homodimers. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion (By similarity). {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 1]: Plays a role in the inhibition of host RLR-induced interferon-beta activation by targeting TANK-binding kinase 1/TBK1. In addition, recruits the host deubiquitinase USP8 to cleave 'Lys-11'-linked polyubiquitin chains from caspase-1/CASP1 thus inhibiting its proteasomal degradation. In turn, stabilized CASP1 promotes cleavage of cGAS, which inhibits its ability to recognize mitochondrial DNA release and initiate type I interferon signaling. {ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that recruits genomic RNA, the structural protein prM/E complex, and the NS2B/NS3 protease complex to the virion assembly site and orchestrates virus morphogenesis (By similarity). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (By similarity). May disrupt adherens junction formation and thereby impair proliferation of radial cells in the host cortex (By similarity). {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. {ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). Inhibits the integrated stress response (ISR) in the infected cell by blocking stress granules assembly (PubMed:28592527). Disrupts host centrosome organization in a CEP63-dependent manner to degrade host TBK1 and inhibits innate immune response (PubMed:35793002). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000269|PubMed:28592527, ECO:0000269|PubMed:35793002}.; FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). Cooperatively with NS4B suppresses the Akt-mTOR pathway and leads to cellular dysregulation (PubMed:27524440). By inhibiting host ANKLE2 functions, may cause defects in brain development, such as microcephaly (PubMed:30550790). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (By similarity). Inhibits the integrated stress response (ISR) in the infected cell by blocking stress granules assembly (PubMed:28592527). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440, ECO:0000269|PubMed:28592527, ECO:0000269|PubMed:30550790}.; FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place (By similarity). Also plays a role in the inhibition of host RLR-induced interferon-beta production at TANK-binding kinase 1/TBK1 level (By similarity). Cooperatively with NS4A suppresses the Akt-mTOR pathway and leads to cellular dysregulation (PubMed:27524440). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed:30951555). Methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Once sufficient NS5 is expressed, binds to the cap-proximal structure and inhibits further translation of the viral genome (By similarity). Besides its role in RNA genome replication, also prevents the establishment of a cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Mechanistically, interferes with host kinases TBK1 and IKKE upstream of interferon regulatory factor 3/IRF3 to inhibit the RIG-I pathway (By similarity). Antagonizes also type I interferon signaling by targeting STAT2 for degradation by the proteasome thereby preventing activation of JAK-STAT signaling pathway (By similarity). Within the host nucleus, disrupts host SUMO1 and STAT2 co-localization with PML, resulting in PML degradation (PubMed:32699085). May also reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (PubMed:30550790). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000269|PubMed:30550790, ECO:0000269|PubMed:30951555, ECO:0000269|PubMed:32699085}.

Zika virus (isolate ZIKV/Human/French Polynesia/10087PF/2013) (ZIKV)

A0A024SC78

CUTI1_HYPJR

MRSLAILTTLLAGHAFAYPKPAPQSVNRRDWPSINEFLSELAKVMPIGDTITAACDLISDGEDAAASLFGISETENDPCGDVTVLFARGTCDPGNVGVLVGPWFFDSLQTALGSRTLGVKGVPYPASVQDFLSGSVQNGINMANQIKSVLQSCPNTKLVLGGYSQGSMVVHNAASNLDAATMSKISAVVLFGDPYYGKPVANFDAAKTLVVCHDGDNICQGGDIILLPHLTYAEDADTAAAFVVPLVS

3.1.1.74

extracellular region [GO:0005576]

cutinase activity [GO:0050525]

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:0000255|RuleBase:RU361263}.

CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000269|PubMed:25219509};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-7. {ECO:0000269|PubMed:25219509};

FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:25219509). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:25219509). {ECO:0000269|PubMed:25219509}.

Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)

A0A024SH76

GUX2_HYPJR

MIVGILTTLATLATLAASVPLEERQACSSVWGQCGGQNWSGPTCCASGSTCVYSNDYYSQCLPGAASSSSSTRAASTTSRVSPTTSRSSSATPPPGSTTTRVPPVGSGTATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNYAGQFVVYDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPDSLANLVTNLGTPKCANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFANVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVYNEKLYIHAIGPLLANHGWSNAFFITDQGRSGKQPTGQQQWGDWCNVIGTGFGIRPSANTGDSLLDSFVWVKPGGECDGTSDSSAPRFDSHCALPDALQPAPQAGAWFQAYFVQLLTNANPSFL

3.2.1.91

cellulose catabolic process [GO:0030245]

extracellular region [GO:0005576]

cellulose 1,4-beta-cellobiosidase activity [GO:0016162]; cellulose binding [GO:0030248]

PF00734;PF01341;

3.20.20.40;

Glycosyl hydrolase 6 (cellulase B) family

PTM: Asn-334 contains mainly a high-mannose-type glycan (Hex(7-9)GlcNAc(2)) in a 3:1 ration with a single GlcNAc. Asn-313 was primarily unglycosylated with a small fraction (18%) bearing a single GlcNAc at this site. {ECO:0000269|PubMed:12499406}.

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07987}.

CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91; Evidence={ECO:0000250|UniProtKB:P07987};

FUNCTION: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units. {ECO:0000250|UniProtKB:P07987}.

Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)

A0A026W182

ORCO_OOCBI

MMKMKQQGLVADLLPNIRVMKTFGHFVFNYYNDNSSKYLHKVYCCVNLFMLLLQFGLCAVNLIVESADVDDLTANTITLLFFTHSIVKICYFAIRSKYFYRTWAIWNNPNSHPLFAESNARYHAIALKKMRLLLFLVGGTTMLAAVAWTVLTFFEHPIRKIVDPVTNETEIIELPQLLIRSFYPFDAGKGITHVLVLVYQFYWVLFMLIDANSLDVLFCSWLLFACEQLQHLKQIMKPLMELSATLDTVVPNSSELFKAGSADHLRDGDNPPPPPPPQSDNMLDLDLRNIYSNRQDFTATFRPTAGMTFNGGVGPNGLTKKQEALVRSAIKYWVERHKHIVRLVTAVGDAYGFALLLHMLTTTITLTLLAYQATKVNGINVYAASTIGYILYTFGQVFLFCIFGNRLIEESTSVMEAAYSCHWYDGSEEAKTFVQIVCQQCQKAMSISGAKFFTVSLDLFASVLGAVVTYFMVLVQLK

antennal development [GO:0007469]; detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; detection of pheromone [GO:0043695]; olfactory behavior [GO:0042048]; response to pheromone [GO:0019236]; signal transduction [GO:0007165]; social behavior [GO:0035176]

plasma membrane [GO:0005886]

odorant binding [GO:0005549]; olfactory receptor activity [GO:0004984]

PF02949;

Insect chemoreceptor superfamily, Heteromeric odorant receptor channel (TC 1.A.69) family, Orco subfamily

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

FUNCTION: Odorant coreceptor which complexes with conventional odorant receptors (ORs) to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity). Obligate coreceptor of all odorant receptors (By similarity). Orco is a universal and integral part of the functional odorant receptor, involved in the dendritic localization of other olfactory receptors. Can form functional ion channels in the absence of an odor-binding odorant receptor (By similarity). Plays a central role in the perception of olfactory stimuli in ants and is essential for ant social organization (PubMed:28802042). Required for pheromone sensing (PubMed:28802042). Also required for the development and maintenance of odorant receptor neurons (ORNs) and of antennal lobe glomeruli (PubMed:28802042). {ECO:0000250|UniProtKB:Q7QCC7, ECO:0000269|PubMed:28802042}.

Ooceraea biroi (Clonal raider ant) (Cerapachys biroi)

A0A044RE18

BLI_ONCVO

MYWQLVRILVLFDCLQKILAIEHDSICIADVDDACPEPSHTVMRLRERNDKKAHLIAKQHGLEIRGQPFLDGKSYFVTHISKQRSRRRKREIISRLQEHPDILSIEEQRPRVRRKRDFLYPDIAHELAGSSTNIRHTGLISNTEPRIDFIQHDAPVLPFPDPLYKEQWYLNNGAQGGFDMNVQAAWLLGYAGRNISVSILDDGIQRDHPDLAANYDPLASTDINGHDDDPTPQDDGDNKHGTRCAGEVASIAGNVYCGVGVAFHAKIGGVRMLDGPVSDSVEAASLSLNRHHIDIYSASWGPEDDGRTFDGPGPLAREAFYRGVKAGRGGKGSIFVWASGNGGSRQDSCSADGYTTSVYTLSVSSATIDNRSPWYLEECPSTIATTYSSANMNQPAIITVDVPHGCTRSHTGTSASAPLAAGIIALALEANPNLTWRDMQHIVLRTANPVPLLNNPGWSVNGVGRRINNKFGYGLMDAGALVKLALIWKTVPEQHICTYDYKLEKPNPRPITGNFQMNFSLEVNGCESGTPVLYLEHVQVLATFRFGKRGDLKLTLFSPRGTSSVLLPPRPQDFNSNGIHKWPFLSVQTWGEDPRGKWTLMVESVSTNRNVGGTFHDWSLLLYGTAEPAQPNDPRHSSVVPSSVSAESPFDRITQHIASQEKKKKQRDSRDWQPKKVENKKSLLVSAQPELRV

3.4.21.75

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12855702}; Note=Binds 3 calcium ions per subunit. {ECO:0000250|UniProtKB:P09958};

dibasic protein processing [GO:0090472]; zymogen activation [GO:0031638]

extracellular region [GO:0005576]; membrane [GO:0016020]; trans-Golgi network [GO:0005802]

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

PF01483;PF00082;PF16470;

2.60.120.260;3.30.70.850;3.40.50.200;

Peptidase S8 family, Furin subfamily

PTM: N-glycosylated. {ECO:0000269|PubMed:12855702}.; PTM: The inhibition peptide, which plays the role of an intramolecular chaperone, is probably autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound as a potent autoinhibitor. Probably following transport to the trans Golgi, a second cleavage within the inhibition propeptide results in propeptide dissociation and bli activation. {ECO:0000269|PubMed:12855702}.

SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12855702}.

CATALYTIC ACTIVITY: Reaction=Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.; EC=3.4.21.75; Evidence={ECO:0000269|PubMed:12855702};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Active from pH 7.0 to 8.5. {ECO:0000269|PubMed:12855702};

FUNCTION: Serine endoprotease which cleaves substrates at the RX(K/R)R consensus motif. {ECO:0000269|PubMed:12855702}.

Onchocerca volvulus

A0A059TC02

CCR1_PETHY

MRSVSGQVVCVTGAGGFIASWLVKILLEKGYTVRGTVRNPDDPKNGHLRELEGAKERLTLCKADLLDYQSLREAINGCDGVFHTASPVTDDPEQMVEPAVIGTKNVINAAAEANVRRVVFTSSIGAVYMDPNRDPETVVDETCWSDPDFCKNTKNWYCYGKMVAEQAAWEEAKEKGVDLVVINPVLVQGPLLQTTVNASVLHILKYLTGSAKTYANSVQAYVDVKDVALAHILLYETPEASGRYLCAESVLHRGDVVEILSKFFPEYPIPTKCSDVTKPRVKPYKFSNQKLKDLGLEFTPVKQCLYETVKSLQEKGHLPIPTQKDEPIIRIQP

1.2.1.44

circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; lignin biosynthetic process [GO:0009809]; phenylpropanoid biosynthetic process [GO:0009699]

cytoplasm [GO:0005737]

cinnamoyl-CoA reductase activity [GO:0016621]; nucleotide binding [GO:0000166]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]

PF01370;

3.40.50.720;

NAD(P)-dependent epimerase/dehydratase family, Dihydroflavonol-4-reductase subfamily

PTM: The formation of a reversible disulfide bond reduces activity by perturbing the positioning of nearby catalytic residues. {ECO:0000269|PubMed:25217505}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24985707}.

CATALYTIC ACTIVITY: Reaction=(E)-coniferaldehyde + CoA + NADP(+) = (E)-feruloyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87305; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64650; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumaraldehyde + CoA + NADP(+) = (E)-4-coumaroyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64652, ChEBI:CHEBI:15378, ChEBI:CHEBI:28353, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85008; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64654; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; CATALYTIC ACTIVITY: Reaction=(E)-sinapaldehyde + CoA + NADP(+) = (E)-sinapoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64656, ChEBI:CHEBI:15378, ChEBI:CHEBI:27949, ChEBI:CHEBI:57287, ChEBI:CHEBI:57393, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64658; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamaldehyde + CoA + NADP(+) = (E)-cinnamoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:10620, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731, ChEBI:CHEBI:57252, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.44; Evidence={ECO:0000250|UniProtKB:Q9S9N9}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10622; Evidence={ECO:0000250|UniProtKB:Q9S9N9};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=208.6 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:25217505}; KM=307.6 uM for feruloyl-CoA {ECO:0000269|PubMed:25217505}; KM=270.3 uM for sinapoyl-CoA {ECO:0000269|PubMed:25217505}; Vmax=1235.7 nmol/sec/mg enzyme with p-coumaroyl-CoA as substrate {ECO:0000269|PubMed:25217505}; Vmax=5713 nmol/sec/mg enzyme with feruloyl-CoA as substrate {ECO:0000269|PubMed:25217505}; Vmax=3384.7 nmol/sec/mg enzyme with sinapoyl-CoA as substrate {ECO:0000269|PubMed:25217505}; Note=kcat is 1.2 sec(-1) with p-coumaroyl-CoA as substrate (PubMed:25217505). kcat is 5.8 sec(-1) with feruloyl-CoA as substrate (PubMed:25217505). kcat is 3.4 sec(-1) with sinapoyl-CoA as substrate (PubMed:25217505). {ECO:0000269|PubMed:25217505};

PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:25217505};

FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:24985707). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:24985707, PubMed:25217505). Mediates the conversion of feruloyl CoA to coniferylaldehyde (PubMed:24985707, PubMed:25217505). Also active toward p-coumaroyl-CoA and sinapoyl-CoA (PubMed:24985707, PubMed:25217505). Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (PubMed:24985707). {ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}.

Petunia hybrida (Petunia)

A0A060A682

HAP2_TETTH

MKFLAFGLIYFHFCILNRCEYITSSTIQKCYNSSNEPNNCSQKAVIVLSLENGQIANTEQVVATLNQLSDSGVNKQLQNSFIFEVTKSPVTALFPLIYLQDFNSQPLEQVIATTLFSCKDGFYDSSPTCKFQYDSKGQKILDSQGYCCYCSLSDILGMGNDLSRGKVCYALNLGAGSATAHCLKFSPLWYSAFKIQQYQLYFEVNINIYTVDSQNQKNLKQTLKLSTSNPTMKSSDNSTISKIIGTFTPTQPPADLSSYYLVKPSFPATDPRVLQGISSWMFVDKTMFTLDGTQCNKIGVSYSGFRQQSSSCSQPVGSCLQNQLENLYQSDLILLSQNKQPKYLLESQGNFNQVQFQGQTILQQGLSGSASTLITIEIDAAQIKFVTNLGIGCISQCSINNFESHSGNGKLVALVQNQGNYSAEFVLGFNCSSNVQPIQGQKLFLTANQLYNFNCSVSVNSDISAINNNCTINLYDAIGNQLDSKNILFNTTSTNHTSNQGNNTGQQQSSQEYKSSQSCSDKCSSFWSFWCYFSAGCIKEAFKSIASIAGVASALALVIFLAKNGYLVPIIRFLCCCCCKSKKKENEKNKDKTDKKSIQESCSYDRSCCSHSISQSYQVENKNKYKRSKIQRSFSSESCQDKSKKIINELSNLEETFEANKLYANIDKNSSIFEYFGFKKSFTFILYERNDILFLPQNSTILDMIGALQPQKGSYLAQKFLEIVNKNALKVVSTSPLYLLIE

fertilization [GO:0009566]; plasma membrane fusion [GO:0045026]; single fertilization [GO:0007338]

cell-cell junction [GO:0005911]; plasma membrane [GO:0005886]

fusogenic activity [GO:0140522]; lipid binding [GO:0008289]

PF10699;

HAP2/GCS1 family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25155508, ECO:0000305|PubMed:28238660}; Single-pass type I membrane protein {ECO:0000255}. Cell junction {ECO:0000269|PubMed:25155508, ECO:0000269|PubMed:28238660}. Note=Detected at the mating junction. {ECO:0000269|PubMed:25155508, ECO:0000269|PubMed:28238660}.

FUNCTION: During fertilization, required for the formation of intercellular membrane pores and subsequent exchange of gametic pronuclei between cells. Probably initiates the formation of intercellular membrane pores by inserting part of its extracellular domain into the cell membrane of the adjoining cell in the mating pair. Mating requires the presence of HAP2 on at least one of the two cells. Mating efficiency is high when HAP2 is present on both cells, and is strongly reduced when HAP2 is present on only one of the two cells. {ECO:0000269|PubMed:25155508, ECO:0000269|PubMed:28238660}.

Tetrahymena thermophila

A0A061ACU2

PIEZ1_CAEEL

MTVPPLLKSCVVKLLLPAALLAAAIIRPSFLSIGYVLLALVSAVLPPIRKSLALPKLVGTFVIITFLFCLAVALGVGSYQISEQVVHKNDRTYICNRSDTTLFRSIGLVRFHPTGTFESTRAFLPEIIATSAALLTIIIVMFLSHRDEQLDVVGDVVTVRSESGREQRRQRKLAAIMWSAIGNSLRRLTNFVLFLFTAYVGIVKPSLSNSIYFLAFLFISTWWSTYTPLRHGVYNQIKKFLIFYSALHFLVLYTYQIPIVHHSWLPTGSFLPRLFGLTVLMDSSCPEWWKFPFVAPDFNDDDLIMKWPLYANPIVVLVFFYLTVAQYKFTRNGSREYIDDNEYGSSVHEERFVSAGTVETNVDDVGQLISISESTASAPSGRGRGNTLLLSNASSSANDDEQGRARSRSPLRNGEEQGSIPLRKVTSQVVDRNKLSNIFNTTAPGDKESAASKGMIAVMTFVIFHSYSIALTAMMTWALLYHSIFGLILLILTCILWIFRDTRKSSFAMAPIILMYIEFLLILQYFLSMDIHAEIGDPAWMNFVGIEWTTLPVHAVIILCVQTLLTLPVFLLLRLARREKFYESLSDYERQRRINSYGTFGASKTGAGGVAVAKFQDPKSRKFAAFVEYLSNKVSVYFIFVVSVVLLVVSTCFAPNFYNILFFALWALNLIYLKFSFRLYRGLAYAFWLTLTFYTSIVIIALYIYQFPGVSQWIIRNTSLSQEWLNAIGLVDFRAIGESGALFLQLLAPIALFVVTMLQLKFFHGPWSRATSPRRAENDPPTSTTEAAAVASTSGTQGRAHAAGDTLVKKLHKLANQTIELLWRFFEVHISKIVFVIIAIFIANNINALYIPLVILLSLAICLPSAADGIFSLFMCAYLFLVALSKMIYQLDIVPELSQIDRGVGADNCSHGNISMPEWFGLKKEVEGTEPIYMLFGVIVSIIALAFQSIVIYRQRHYRASLGLPESMRAKVFPDFHHSHFDRSLKNAIQFLIDYGFYKFGLEITMIAIGIDIFNRMDALAAIQCFWLVLFALNKRVFVRRIWVFYVIYMAILYPLQFFSYVGLPPDSCIEYPWSYWIPSYSDDARFNLSYLLNLSIYGVNWPSAYLIGDFFVLLLASCQLAVFRREGEDNDSIYNDGNFVIKPENPQYDFIDTKKSYVDYFKSFVFHYGHWITLMSTLAAGIAGTSLFALGYIIFTLTMLWSGNNLYVMNSTLRSFEHTLKRWNALLGYTLFTITMKVCLQIFGCVFLSWFDQSGGWGKTLCIVRQLFSITCVNNECHVLKELEDFSKACAVETKEGNIGFDVIALSFLVFQIRIFHSWYFQHCMVEYRSEVILANRGAVLKNQLIEKEMKEQNEQQKAKFNDIRRRTEAIRERYQKQIERGAAERDFEPVTYGHAKRAGDYYMFKYDPENDDLVEPVDSFVPEVDPKATAYDRLDPGQIMYAATAHDLDLAKTVQQVKKGDTIKDPDSRALIAVSEPEARKPGGTEETDGDEDEDNKDSKVESTAKFIQKMIASALDLCSVTLNKLCREHRYVGFVLSKEKQKLKSGHSESLSNTSRKLTDIRSAVDLPSLQLVQSANDVEKMETAVSVDWQQKSSATRLLNAVVNCIGAHTDILCYFFAIMTQVMTGGLITLPLPLMSLFWGNLSNPRPSKFFWVTMITYTECVIVIKFVCQFAFMPYNSITWRTEHQMDPMSLDKLFGVSQRDSFALWDIVLLFSLFFHRYMLRKLGLWKDANLTDTFTLKEEPRSASGSDTGSPKKIAQEPKVVVTQSDTLEGTSGGEIVIPSDPNAVSNMEELDCEPPIPEKQSGPIGRFIHQLFHPKFRYIRDLYPIMFGIDVICFLIMTFGYSAFGEGGSGNVLDDVKASRIPVTLVVMLVGMTLAIIIDRALYLRKSVVGKLIYQVLMIAFLHIWVFLVLPNMTRRSAISNHVAQALYVIKSCYFLVSAWQIRNGYPELCIGNLLTHSYGMTNMIAFKVFMNIPFLFELRTAIDWTWTDTSMPLFDFFNMENFYAHIFNIKCARQFEAAYPAPRGIPKGKLVKYMMGFPIIIGVVIFIFSPLLLWSLLNQIGTISMPEKVTLRISIEGYPPLYEMEAQGSNHDNAELGMIKPDQLASLNQALTDSYTTRDTNSILRSRMSVSYLKGYTYEDILIVRFRPESEIYWPISQDSRNAMIDKLSRNTSVNFEVSLEFTRPYDPNENAALKHSKSWLVPISLDMTIRAKIQSALRGDPGHPILIPQSIPAFIQVPNQGELTLPTSIGNTIINDGNPRINTTGMEKSDEARAWFDSLTLNLEQGKSQNEKMWIATSEHPGDQNAKLWIKTANTTYSGRPYLQVVGFIDRAFPSFLAKVFKGGVIAVYLSVILVVGRGLVRGIFTTSPSTVMFTELPNADHLLKICLDIYLVREAKDFMLEQDLFAKLIFLFRSPATLIEWTRMSKKKQE

cellular response to mechanical stimulus [GO:0071260]; detection of mechanical stimulus [GO:0050982]; flagellated sperm motility [GO:0030317]; monoatomic cation transmembrane transport [GO:0098655]; positive regulation of brood size [GO:0090727]; positive regulation of ovulation [GO:0060279]; regulation of membrane potential [GO:0042391]; response to mechanical stimulus [GO:0009612]

plasma membrane [GO:0005886]

mechanosensitive monoatomic ion channel activity [GO:0008381]; monoatomic cation channel activity [GO:0005261]

PF15917;PF12166;

PIEZO (TC 1.A.75) family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32490809}; Multi-pass membrane protein {ECO:0000255}.

FUNCTION: Pore-forming subunit of a mechanosensitive non-specific cation channel (By similarity). Generates currents characterized by a linear current-voltage relationship (By similarity). Plays a role in reproduction by positively regulating inter-tissue signaling to promote oocyte maturation, ovulation and fertilization, and sperm navigation from and to the spermatheca (PubMed:32490809). May play a role in regulating cytosolic and endoplasmic reticulum calcium ion release (PubMed:32490809). {ECO:0000250|UniProtKB:Q92508, ECO:0000269|PubMed:32490809}.

Caenorhabditis elegans

A0A061AE05

PAPSH_CAEEL

MLTPRDENNEGDAMPMLKKPRYSSLSGQSTNITYQEHTISREERAAAVGRHEGFRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESENVKFIEVHVSTTLEVCEQRDPKPSELYKKARAGQILGFTGIDSAYEPPENAEIILDAGKDGVQQCVQKVLDHLESKGLLPEQIPDVPAVRELFVSDDLTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDLKHKVAFVGEKSDDKEDSWPMMDDINQSIPIVLPISDDVKKGLEGVTRIALKYNGQVYAILSDPEIFEHRKDERVCRQFGTNDPRHPAVAQVLESGNWLLGGDVAVVQKIQFNDGLDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMRDTREKLLAEHKNPILLLHPLGGWTKDDDVPLDIRIKQHEAVIAERVLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGIQKPGSPDALYETTHGAKVLSMAPGLSALHILPFRVAAYDKTAKKMSFFDTSRKEDFENISGTKMRGLARNGDTPPEGFMAPTAWEVLAGYYKSLQNSN

2.7.1.25; 2.7.7.4

3'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; phosphorylation [GO:0016310]; sulfate assimilation [GO:0000103]

nucleus [GO:0005634]

adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]; sulfate adenylyltransferase (ATP) activity [GO:0004781]

PF01583;PF01747;PF14306;

3.40.50.620;3.40.50.300;3.10.400.10;

APS kinase family; Sulfate adenylyltransferase family

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16497669}.

CATALYTIC ACTIVITY: Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000269|PubMed:16497669}; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339, ChEBI:CHEBI:456216; EC=2.7.1.25; Evidence={ECO:0000269|PubMed:16497669};

PATHWAY: Sulfur metabolism; sulfate assimilation. {ECO:0000303|PubMed:16497669}.

FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway (PubMed:16497669). The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase) (PubMed:16497669). Required for normal growth and development (PubMed:16497669). Involved in several aspects of both embryonic and postembryonic development, including molting, changes in cell shape, and patterning of epithelial and muscle cells (PubMed:16497669). {ECO:0000269|PubMed:16497669}.

Caenorhabditis elegans

A0A061I403

FICD_CRIGR

MPMASVIAVAEPKWISVWGRFLWLTLLSMALGSLLALLLPLGAVEEQCLAVLRSFHLLRSKLDRTQHVVTKCTSPSTELSVTSGDVGLLTVKTKTSPAGKLEAKAALNQALEMKRQGKREKAHKLFLHALKMDPGFVDALNEFGIFSEEEKDIIQADYLYTRALTISPFHEKALVNRDRTLPLVEEIDQRYFSIIDSKVKKVMSIPKGSSALRRVMEETYYHHIYHTVAIEGNTLTLSEIRHILETRYAVPGKSLEEQNEVIGMHAAMKYINTTLVSRIGSVTIDDMLEIHRRVLGYVDPVEAGRFRRTQVLVGHHIPPHPRDVEKQMQEFTQWLNSEDAMNLHPVEFAALAHYKLVYIHPFIDGNGRTSRLLMNLILMQAGYPPITILKEQRSEYYHVLEVANEGDVRPFIRFIAKCTEVTLDTLLLATTEYSVALPEAQPNHSGLKETLPVRP

2.7.7.108; 3.1.4.-

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Note=Divalent metal cation. Prefers Mn(2+) over Mg(2+). {ECO:0000250|UniProtKB:Q9BVA6};

protein adenylylation [GO:0018117]; protein deadenylylation [GO:0044602]; regulation of IRE1-mediated unfolded protein response [GO:1903894]; response to endoplasmic reticulum stress [GO:0034976]; response to unfolded protein [GO:0006986]

endoplasmic reticulum membrane [GO:0005789]

AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]

PF02661;

1.10.3290.10;1.25.40.10;

Fic family

PTM: Auto-AMPylated in vitro. {ECO:0000250|UniProtKB:Q9BVA6}.

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVA6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9BVA6}.

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIVITY: Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:27918543}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000269|PubMed:26673894, ECO:0000269|PubMed:27918543, ECO:0000269|PubMed:29064368};

FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (PubMed:27918543). The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (PubMed:27918543). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (PubMed:27918543). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (PubMed:26673894, PubMed:27918543, PubMed:29064368). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (PubMed:27918543). Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates (By similarity). {ECO:0000250|UniProtKB:Q9BVA6, ECO:0000269|PubMed:26673894, ECO:0000269|PubMed:27918543, ECO:0000269|PubMed:29064368}.

Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

A0A067CMC7

HTP3_SAPPC

MLEVPVWIPILAFAVGLGLGLLIPHLQKPFQRFSTVNDIPKEFFEHERTLRGKVVSVTDGDTIRVRHVPWLANGDGDFKGKLTETTLQLRVAGVDCPETAKFGRTGQPFGEEAKAWLKGELQDQVVSFKLLMKDQYSRAVCLVYYGSWAAPMNVSEELLRHGYANIYRQSGAVYGGLLETFEALEAEAREKRVNIWSLDKRETPAQYKARK

3.1.31.-

extracellular space [GO:0005615]; host cell cytosol [GO:0044164]

endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]

PF00565;

2.40.50.90;

RxLR effector family; LCL3 family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29904064}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:29904064}. Note=Uptake into host cells is more efficient at a lower pH of 5.5. S.parasitica acidifies the pH of its environment, which likely leads to the exposure of a gp96 protein to the host cell surface. The gp96 protein is working as a receptor and mediates the translocation of Htp3 via lipid rafts into the cell. Finally, Htp3 is released from vesicles with the help of other effector proteins, such as Htp1, into the cytosol where it is functionally active as a nuclease. {ECO:0000269|PubMed:29904064}.

FUNCTION: Effector involved in the disease saprolegniosis in salmonids and other freshwater fish, resulting in considerable economic losses in aquaculture (PubMed:29904064). Within the host fish cells, Htp3 is released from vesicles into host cytosol where it degrades nucleic acids (PubMed:29904064). {ECO:0000269|PubMed:29904064}.

Saprolegnia parasitica (strain CBS 223.65)

A0A067XGX8

AROG2_PETHY

MALTATATTRGGSALPNSCLQTPKFQSLQKPTFISSFPTNKKTKPRTKHISAVQSPPSTTKWNLESWKTKPAFQLPDYPDKVELESVLKTLSTYPPIVFAGEARNLEEKLGEAALGNAFLLQGGDCAESFKEFSANNIRDTFRVMLQMGVVLMFGGQMPVIKVGRMAGQFAKPRSDPFEEKDGVKLPSYRGDNVNGDAFDEKSRIPDPHRMVRAYTQSVATLNLLRAFASGGYAAMQRVNQWNLDFTDQSEQGDRYRELAHRVDEAMGFMTAAGLTVDHTIMTTTDFWTSHECLLLPYEQALTREDSTSGLYYDCSAHMIWVGERTRQLDGAHVEFLRGIANPLGIKVSHKMDPDELVKLIDILNPQNKPGRITVITRMGADNMRVKLPHLIRAVRGAGQIVTWVSDPMHGNTTKAPCGLKTRSFDSIRAELRAFFDVHEQEGSYPGGVHLEMTGQNVTECVGGSRTITYNDLSSRYHTHCDPRLNASQALELAFAIAERLRRRRLGPKFSL

2.5.1.54

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O53512}; Note=Binds 1 divalent metal cation per subunit that could be manganese. {ECO:0000250|UniProtKB:O53512};

amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]

chloroplast [GO:0009507]

3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849]; metal ion binding [GO:0046872]

PF01474;

3.20.20.70;

Class-II DAHP synthase family

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24815009}.

CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; Evidence={ECO:0000250|UniProtKB:O53512};

PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}.

FUNCTION: Involved in the production of volatile organic compounds (VOCs) (PubMed:24815009). Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate (By similarity). {ECO:0000250|UniProtKB:O53512, ECO:0000269|PubMed:24815009}.

Petunia hybrida (Petunia)

A0A067XH53

AROG1_PETHY

MALSTNSTTSSLLPKTPLVQQPLLKNASLPTTTKAIRFIQPISAIHSSDSSKNTPIVSAKPSSPPAATSTAAATAVTKQEWSIDSWKTKKALQLPEYPNQEELKNVLKTIEDFPPIVFAGEARHLEEKLGEAAMGRAFLLQGGDCAESFKEFNANNIRDTFRILLQMGAVLMFGGQMPVIKVGRMAGQFAKPRSDNFEEKNGVKLPSYRGDNVNGDAFDLKSRTPDPQRLIRAYCQSAATLNLLRAFATGGYAAMQRVTQWNLDFTEHSEQGDRYRELANRVDEALGFMNAAGLTTDHPIMTTTEFWTSHECLLLPYEQSLTRLDSTSGLYYDCSAHFLWVGERTRQLDGAHVEFLRGIANPLGIKVSDKMDPSALVKLIEILNPQNKAGRITIITRMGAENMRVKLPHLIRAVRGAGQIVTWVSDPMHGNTIKAPCGLKTRPFDSIRAEVRAFFDVHEQEGSHPGGVHLEMTGQNVTECIGGSRTVTFDDLSSRYHTHCDPRLNASQSLELAFIIAERLRKRRLGSQSVLGQ

2.5.1.54

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O53512}; Note=Binds 1 divalent metal cation per subunit that could be manganese. {ECO:0000250|UniProtKB:O53512};

amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; green leaf volatile biosynthetic process [GO:0010597]

chloroplast [GO:0009507]

3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849]; metal ion binding [GO:0046872]

PF01474;

3.20.20.70;

Class-II DAHP synthase family

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24815009}.

CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; Evidence={ECO:0000250|UniProtKB:O53512};

PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}.

FUNCTION: Involved in the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26), scent attracting pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta) (PubMed:24815009). Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate (By similarity). {ECO:0000250|UniProtKB:O53512, ECO:0000269|PubMed:24815009}.

Petunia hybrida (Petunia)

A0A067XR63

XTH7_DIOKA

MNAEGGNLHREFEITWGDGRARIHNNGGLLTLSLDRASGSGFRSKNEYLFGRIEIQIKLVAGNSAGTVATYYLSSEGPTHDEIDFEFLGNSSGEPYTLHTNVFSQGKGNREQQFFLWFDPTMDFHTYTILWNPQRIIFYVDETPIREFKNLERHGIPFPRSQAMRVYSSMWNADDWATRGGLVKTDWTKAPFTASYRSYKADACVWSGEASSCGSQDSNPSDKWWMTEELNATRMKRLRWVQKKYMVYNYCVDKMRFPEGLAPECNIS

2.4.1.207

cell wall assembly [GO:0070726]; fruit ripening [GO:0009835]; xyloglucan metabolic process [GO:0010411]

apoplast [GO:0048046]; cytoplasm [GO:0005737]

hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; xyloglucan:xyloglucosyl transferase activity [GO:0016762]

PF00722;PF06955;

2.60.120.200;

Glycosyl hydrolase 16 family, XTH group 2 subfamily

PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000255|RuleBase:RU361120}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27242828}. Note=Dispersed throughout the cell. {ECO:0000269|PubMed:27242828}.

CATALYTIC ACTIVITY: Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.; EC=2.4.1.207; Evidence={ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27242828};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 5-6. Activity decreases sharply when the pH is lowered from 5 to 4. {ECO:0000269|PubMed:27242828};

FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Probably involved in cell wall assembly and synthesis in fast growing tissues and in the maintenance of firmness in mature fruits. {ECO:0000269|PubMed:27242828}.

Diospyros kaki (Kaki persimmon) (Diospyros chinensis)

A0A067XRK9

XTH6_DIOKA

MASSLTLPMAMAFTLLALSFASAMGGSMNSSRFDELFQPSWAFDHFVYEGEVLKMKLDNYSGAGFSSKGKYLFGKVTVQIKLVEGDSAGTVTAFYMSSDGTNHNEFDFEFLGNTTGEPYLVQTNVYVNGVGNREQRLNLWFDPTKDFHSYSLLWNQRQVVFMVDETPIRVHSNLEHRGIPFPKDQPMGVYSSIWNADDWATQGGRIKTDWSHAPFVASYQGFAIDACECPAAVAATDNARRCSSSAEKQFWWDMPTLSELSLHQSHQLIWVRANHLVYDYCTDTARFPVTPAECEHHRH

2.4.1.207

cell wall biogenesis [GO:0042546]; cell wall organization [GO:0071555]; fruit ripening [GO:0009835]; xyloglucan metabolic process [GO:0010411]

apoplast [GO:0048046]

hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; xyloglucan:xyloglucosyl transferase activity [GO:0016762]

PF00722;PF06955;

2.60.120.200;

Glycosyl hydrolase 16 family, XTH group 1 subfamily

PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000255|RuleBase:RU361120}.

SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27242828}. Secreted, extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}.

CATALYTIC ACTIVITY: Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.; EC=2.4.1.207; Evidence={ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27242828};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 6. Highly active between pH range 4.5-6.5. {ECO:0000269|PubMed:27242828};

FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Probably involved in cell wall restructuring during postharvest fruit softening. {ECO:0000269|PubMed:27242828}.

Diospyros kaki (Kaki persimmon) (Diospyros chinensis)

A0A067YMX8

XTH8_DIOKA

MAASPYSIFAVQLLLLASWMLSSSSSNFNQDFNIAWGGGRARILNNGELVTLSLDKASGSGFRSKNLYLFGKIDMQLKLVPGNSAGTVTTYYLSSEGSVRDEIDFEFLGNLTGEPYTLHTNVYSHGKGEREQQFRLWFDPAADFHTYSILWNSKTIVFYVDQTPVREFKNMESIGVPYLRQPMRLFSSIWNADEWATRGGLIKTDWTQAPFTTSYRNFRADNACVWAAKASSCGLAAGGNAWLSVELDAKSRGRLRWVRRNQMIYDYCVDGKRFPRGVPPECKLNLHI

2.4.1.207

cell wall biogenesis [GO:0042546]; cell wall organization [GO:0071555]; cellular response to gibberellin stimulus [GO:0071370]; fruit ripening [GO:0009835]; response to abscisic acid [GO:0009737]; xyloglucan catabolic process [GO:2000899]

apoplast [GO:0048046]

hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; polysaccharide binding [GO:0030247]; xyloglucan:xyloglucosyl transferase activity [GO:0016762]

PF00722;PF06955;

2.60.120.200;

Glycosyl hydrolase 16 family, XTH group 2 subfamily

PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000255|RuleBase:RU361120}.

SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27966647}. Secreted, extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}.

CATALYTIC ACTIVITY: Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.; EC=2.4.1.207; Evidence={ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27966647};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 6. Activity decreases sharply when the pH is lowered from 5 to 4. {ECO:0000269|PubMed:27966647};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 30-40 degrees Celsius. {ECO:0000269|PubMed:27966647};

FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Overexpression in Arabidopsis transgenic plants causes accelerated dark-induced leaf senescence and higher lipid peroxidation of the leaf cells. Overexpression in transgenic tomato plants promotes fruit ripening and softening. Probably involved in cell wall restructuring during postharvest fruit softening. {ECO:0000269|PubMed:27966647}.

Diospyros kaki (Kaki persimmon) (Diospyros chinensis)

A0A068B6Q6

CA18_CONBE

PDGRNAAAKAFDLITPTVRKGCCSNPACILNNPNQCG

extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792]

acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729]

PF07365;

Conotoxin A superfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000305}.

FUNCTION: Alpha-conotoxins bind to the nicotinic acetylcholine receptors (nAChR) and inhibit them. This toxin inhibits mammalian alpha-3-beta-2/CHRNA3-CHRNB2 nAChR (IC(50)=9.4 nM (rat), IC(50)=8.8 nM (human)), as well as the subunit chimera alpha-6/alpha-3-beta-2-beta-3 nAChR (CHRNA6/CHRNA3-CHRNB2-CHRNB3)(IC(50)=2.1 nM (rat), IC(50)=1.7 nM (human)). Binds to rat alpha-6/alpha-3-beta-2-beta-3 more rapidly than to alpha-3-beta-2, and dissociates more rapidly from alpha-3-beta-2 than from alpha-6/alpha-3-beta-2-beta-3. {ECO:0000269|PubMed:34008858}.

Conus betulinus (Beech cone)

A0A068J840

UGT1_PANGI

MKSELIFLPAPAIGHLVGMVEMAKLFISRHENLSVTVLIAKFYMDTGVDNYNKSLLTNPTPRLTIVNLPETDPQNYMLKPRHAIFPSVIETQKTHVRDIISGMTQSESTQVVGLLADLLFINIMDIANEFNVPTYVYSPAGAGHLGLAFHLQTLNDKKQDVTEFRNSDTELLVPSFANPVPAEVLPSMYVDKEGGYDYLFSLFRRCRESKAIIINTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGDGQNSDEAAVILGWLDDQPPSSVVFLCFGSYGSFQENQVKEIAMGLERSGHRFLWSLRPSIPKGETKLQLKYSNLKEILPVGFLDRTSCVGKVIGWAPQVAVLGHESVGGFLSHCGWNSTLESVWCGVPVATWPMYGEQQLNAFEMVKELGIAVEIEVDYKKDYFNMKNDFIVRAEEIETKIKKLMMDENNSEIRKKVKEMKEKSRAAMSENGSSYNSLAKLFEEIM

2.4.1.363

terpenoid biosynthetic process [GO:0016114]

UDP-glycosyltransferase activity [GO:0008194]

PF00201;

3.40.50.2000;

UDP-glycosyltransferase family

CATALYTIC ACTIVITY: Reaction=(20S)-protopanaxadiol + UDP-alpha-D-glucose = (20S)-ginsenoside C-K + H(+) + UDP; Xref=Rhea:RHEA:57976, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:75950, ChEBI:CHEBI:77146; EC=2.4.1.363; Evidence={ECO:0000269|PubMed:24603359, ECO:0000269|PubMed:26032089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57977; Evidence={ECO:0000269|PubMed:24603359, ECO:0000269|PubMed:26032089}; CATALYTIC ACTIVITY: Reaction=(20S)-ginsenoside Rg3 + UDP-alpha-D-glucose = (20S)-ginsenoside Rd + H(+) + UDP; Xref=Rhea:RHEA:57984, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:67988, ChEBI:CHEBI:67991; EC=2.4.1.363; Evidence={ECO:0000269|PubMed:26032089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57985; Evidence={ECO:0000269|PubMed:26032089}; CATALYTIC ACTIVITY: Reaction=(20S)-ginsenoside Rh2 + UDP-alpha-D-glucose = (20S)-ginsenoside F2 + H(+) + UDP; Xref=Rhea:RHEA:57988, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:77145, ChEBI:CHEBI:77147; EC=2.4.1.363; Evidence={ECO:0000269|PubMed:26032089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57989; Evidence={ECO:0000269|PubMed:26032089}; CATALYTIC ACTIVITY: Reaction=(20S)-protopanaxatriol + UDP-alpha-D-glucose = (20S)-ginsenoside F1 + H(+) + UDP; Xref=Rhea:RHEA:57980, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:75951, ChEBI:CHEBI:77150; EC=2.4.1.363; Evidence={ECO:0000269|PubMed:26032089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57981; Evidence={ECO:0000269|PubMed:26032089}; CATALYTIC ACTIVITY: Reaction=dammarenediol-II + UDP-alpha-D-glucose = (20S)-20-O-(beta-D-glucosyl)-3-hydroxydammarene + H(+) + UDP; Xref=Rhea:RHEA:59044, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:62416, ChEBI:CHEBI:142484; EC=2.4.1.363; Evidence={ECO:0000269|PubMed:24603359, ECO:0000269|PubMed:26032089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59045; Evidence={ECO:0000269|PubMed:24603359, ECO:0000269|PubMed:26032089};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=359 uM for protopanaxadiol {ECO:0000269|PubMed:24603359}; KM=178 uM for dammarenediol II {ECO:0000269|PubMed:24603359}; Vmax=254 nmol/min/mg enzyme with protopanaxadiol as substrate {ECO:0000269|PubMed:24603359}; Vmax=423 nmol/min/mg enzyme with dammarenediol II as substrate {ECO:0000269|PubMed:24603359}; Note=kcat is 9.4 sec(-1) with protopanaxadiol as substrate (PubMed:24603359). kcat is 12.7 sec(-1) with dammarenediol II as substrate (PubMed:24603359). {ECO:0000269|PubMed:24603359};

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

FUNCTION: Component of the dammarane-type triterpene saponins (e.g. ginsenosides or panaxosides) biosynthetic pathway (PubMed:26032089, PubMed:29378087). Glycosyltransferase that catalyzes the biosynthesis of ginsenoside F1 from protopanaxatriol (PPT) (PubMed:26032089). Triggers C20-OH glycosylation of ginsenoside Rg3 to produce ginsenoside Rd (PubMed:26032089). Mediates the conversion of protopanaxadiol (PPD) to the ginsenoside compound K (PubMed:24603359, PubMed:26032089). catalyzes the production of 20S-O-beta-(D-glucosyl)-dammarenediol II form dammarenediol II (DM) (PubMed:24603359). {ECO:0000269|PubMed:24603359, ECO:0000269|PubMed:26032089, ECO:0000303|PubMed:29378087}.

Panax ginseng (Korean ginseng)

A0A068Q5Q5

DEPOL_BPKNT

MALIRLVAPERVFSDLASMVAYPNFQVQDKITLLGSAGGDFTFTTTASVVDNGTVFAVPGGYLLRKFVGPAYSSWFSNWTGIVTFMSAPNRHLVVDTVLQATSVLNIKSNSTLEFTDTGRILPDAAVARQVLNITGSAPSVFVPLAADAAAGSKVITVAAGALSAVKGTYLYLRSNKLCDGGPNTYGVKISQIRKVVGVSTSGGVTSIRLDKALHYNYYLSDAAEVGIPTMVENVTLVSPYINEFGYDDLNRFFTSGISANFAADLHIQDGVIIGNKRPGASDIEGRSAIKFNNCVDSTVKGTCFYNIGWYGVEVLGCSEDTEVHDIHAMDVRHAISLNWQSTADGDKWGEPIEFLGVNCEAYSTTQAGFDTHDIGKRVKFVRCVSYDSADDGFQARTNGVEYLNCRAYRAAMDGFASNTGVAFPIYRECLAYDNVRSGFNCSYGGGYVYDCEAHGSQNGVRINGGRVKGGRYTRNSSSHIFVTKDVAETAQTSLEIDGVSMRYDGTGRAVYFHGTVGIDPTLVSMSNNDMTGHGLFWALLSGYTVQPTPPRMSRNLLDDTGIRGVATLVAGEATVNARVRGNFGSVANSFKWVSEVKLTRLTFPSSAGALTVTSVAQNQDVPTPNPDLNSFVIRSSNAADVSQVAWEVYL

4.-.-.-

adhesion receptor-mediated virion attachment to host cell [GO:0098671]; symbiont entry into host cell via disruption of host cell envelope [GO:0098994]; symbiont entry into host cell via disruption of host cell glycocalyx [GO:0098996]

virus tail [GO:0098015]

lyase activity [GO:0016829]

2.160.20.10;

K1-specific depolymerase family

SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Tail appendage. {ECO:0000305}.

FUNCTION: Functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides (PubMed:35130876). Displays a lyase activity that specifically degrades the K1-type polysaccharides of Klebsiella pneumoniae capsule (PubMed:25001459, PubMed:35130876). {ECO:0000269|PubMed:25001459, ECO:0000269|PubMed:35130876}.

Klebsiella phage NTUH-K2044-K1-1 (Bacteriophage NTUH-K2044-K1-1)

A0A072ULZ1

GLB12_MEDTR

MEENKKTVDGSVDFTEEQEALVVKSWNAMKNNSCDLSLKFFTKILEIAPPAKQMFSFLKDSNVPLEQNPKLKPHAMSVFLMTCESAVQLRKAGKVRVRESNLKKLGATHFKTGVQDEHFEVTKQALLETIEEAIPEMWSLAMKNAWAEAHDQLANAIKVEMKEAHDQMDNANLIINMEENTGSCFTEEQEALVVKSWNAIKYNSGDLSLKFFKKILEIAPPAKQLFSFLKDSNVPLEHNPKLKPHAMSVFLMTCESAVQLRKAGKVTVRESNLKKLGATHFKTGVKDEHFEVTKQALLETIKEALPEMWSPAMENAWGEAHDQLANAIKAEMKKTDHDHQTNVEDKSKPSS

1.7.2.-

COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:33329665}; Note=Binds 2 heme groups per subunit. {ECO:0000269|PubMed:33329665};

response to ammonium ion [GO:0060359]; response to hypoxia [GO:0001666]; response to nitrate [GO:0010167]; response to nitric oxide [GO:0071731]; response to symbiotic bacterium [GO:0009609]

heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825]

PF00042;

1.10.490.10;

Plant globin family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2XE98}. Nucleus {ECO:0000250|UniProtKB:A2XE98}.

CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:33329665}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77712; Evidence={ECO:0000269|PubMed:33329665}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000269|PubMed:33329665};

FUNCTION: Phytoglobin that regulates the fine tuning of nitric oxide (NO) concentration in the cytosol in response to sudden changes in O(2) availability, and performs both symbiotic and nonsymbiotic functions (PubMed:33329665). Exhibits NO dioxygenase activity in the presence of O(2) but nitrite reductase (NiR) activity in the absence of O(2) (e.g. during flooding or in waterlogged soil) (PubMed:33329665). May not function as an oxygen storage or transport protein (By similarity). Extremely reactive toward the physiological ligands O(2), nitric oxide (NO), and nitrite with a very high affinity for O(2) through an hexacoordinate heme iron because of a very low dissociation constant (PubMed:33329665). {ECO:0000250|UniProtKB:O04986, ECO:0000269|PubMed:33329665}.; FUNCTION: [Isoform 2]: Very high affinity for O(2) through two hexacoordinate heme irons (PubMed:33329665). Extremely reactive toward the physiological ligands O(2), nitric oxide (NO), and nitrite (PubMed:33329665). {ECO:0000269|PubMed:33329665}.; FUNCTION: [Isoform 4]: Very high affinity for O(2) through a single hexacoordinate heme iron (PubMed:33329665). Extremely reactive toward the physiological ligands O(2), nitric oxide (NO), and nitrite (PubMed:33329665). {ECO:0000269|PubMed:33329665}.

Medicago truncatula (Barrel medic) (Medicago tribuloides)

A0A072UR65

CHT5B_MEDTR

MANILNLKHLLTLALILLALATKSSTSSSSSITRVKGIYWLENPFFPPTTVDTSLFTHIFYSFLTPNNITYKLEISSSQILSLNTFTKTFKTKSPPAATLFSIGGAGSNSSLLAFIASDPPACAAFINSTIDVARTFGFDGIDLDWEFPKNTKEMNDLGEMLFQWRKAISDEGATTGRPPLLLTAAVYFAVNFSIYGEPRMYPVNSINENLDWVNVMSYELRGPRSNKTGAPSGTFDPKSNVSVVSGLLSWIHSGVVPEKLVMGMPLYGKSWKLRDPNVHGIGAPSVGSGPGVNGLMAYFQVLDFNRQKSAKVEYDVDTASVYSYSGSTWIGYDNPFTVSIKVGFAQALKLRGYFFWVAGLDTLDWKIATQASKAWKLV

3.2.1.14

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

extracellular region [GO:0005576]

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

PF00704;

3.10.50.10;3.20.20.80;

Glycosyl hydrolase 18 family, Chitinase class V subfamily

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

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.5 mM for (GlcNAc)6 {ECO:0000269|PubMed:27383628}; KM=8.6 mM for (GlcNAc)5 {ECO:0000269|PubMed:27383628};

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

FUNCTION: Possesses chitinase activity in vitro toward glycol chitin, carboxymethyl-chitin, colloidal chitin, and the chitin oligosaccharides (N-acetylglucosamine) (GlcNAc)6 and (GlcNAc)5 (PubMed:27383628). Hydrolyzes (GlcNAc)6 into (GlcNAc)4 and (GlcNAc)2, or two (GlcNAc)3 molecules (PubMed:27383628). Has the capacity to reduce hyphal growth of the fungus Trichoderma viride in an agar-plate bioassay (PubMed:27383628). {ECO:0000269|PubMed:27383628}.

Medicago truncatula (Barrel medic) (Medicago tribuloides)

A0A072VDF2

CCR1_MEDTR

MPAATAAAAAESSSVSGETICVTGAGGFIASWMVKLLLEKGYTVRGTLRNPDDPKNGHLKKLEGAKERLTLVKVDLLDLNSVKEAVNGCHGVFHTASPVTDNPEEMVEPAVNGAKNVIIAGAEAKVRRVVFTSSIGAVYMDPNRSVDVEVDESCWSDLEFCKKTKNWYCYGKAVAEAAAWDVAKEKGVDLVVVNPVLVLGPLLQPTINASTIHILKYLTGSAKTYANATQAYVHVRDVALAHILVYEKPSASGRYLCAETSLHRGELVEILAKYFPEYPIPTKCSDEKNPRVKPHIFSNKKLKDLGLEFTPVSECLYETVKSLQDQGHLSIPNKEDSLAVKS

1.2.1.-; 1.2.1.44

lignin biosynthetic process [GO:0009809]; phenylpropanoid biosynthetic process [GO:0009699]

cytoplasm [GO:0005737]

cinnamoyl-CoA reductase activity [GO:0016621]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]

PF01370;

3.40.50.720;

NAD(P)-dependent epimerase/dehydratase family, Dihydroflavonol-4-reductase subfamily

PTM: The formation of a reversible disulfide bond reduces activity by perturbing the positioning of nearby catalytic residues. {ECO:0000250|UniProtKB:A0A059TC02}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A059TC02}.

CATALYTIC ACTIVITY: Reaction=(E)-coniferaldehyde + CoA + NADP(+) = (E)-feruloyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87305; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64650; Evidence={ECO:0000269|PubMed:20876124}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumaraldehyde + CoA + NADP(+) = (E)-4-coumaroyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64652, ChEBI:CHEBI:15378, ChEBI:CHEBI:28353, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85008; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64654; Evidence={ECO:0000269|PubMed:20876124}; CATALYTIC ACTIVITY: Reaction=(E)-sinapaldehyde + CoA + NADP(+) = (E)-sinapoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64656, ChEBI:CHEBI:15378, ChEBI:CHEBI:27949, ChEBI:CHEBI:57287, ChEBI:CHEBI:57393, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64658; Evidence={ECO:0000269|PubMed:20876124}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamaldehyde + CoA + NADP(+) = (E)-cinnamoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:10620, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731, ChEBI:CHEBI:57252, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.44; Evidence={ECO:0000250|UniProtKB:Q9S9N9}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10622; Evidence={ECO:0000250|UniProtKB:Q9S9N9}; CATALYTIC ACTIVITY: Reaction=(E)-caffeyl aldehyde + CoA + NADP(+) = (E)-caffeoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:74867, ChEBI:CHEBI:15378, ChEBI:CHEBI:28323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87136; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:74869; Evidence={ECO:0000269|PubMed:20876124};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=54.5 uM for feruloyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=7.2 uM for sinapoyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=161 uM for caffeoyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=56.8 uM for coumaroyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Vmax=1.64 umol/min/mg enzyme with feruloyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Vmax=0.15 umol/min/mg enzyme with sinapoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Vmax=0.085 umol/min/mg enzyme with caffeoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Vmax=0.25 umol/min/mg enzyme with coumaroyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Note=kcat is 60.1 min(-1) with feruloyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 5.5 min(-1) with sinapoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 3.1 min(-1) with caffeoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 9.0 min(-1) with coumaroyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). {ECO:0000269|PubMed:20876124};

PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000250|UniProtKB:A0A059TC02}.

FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:20876124). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:20876124). Mediates the conversion of feruloyl-CoA to coniferylaldehyde (PubMed:20876124). Also active, with a lower efficiency, toward coumaroyl-CoA, caffeoyl CoA and sinapoyl-CoA (PubMed:20876124). Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (By similarity). {ECO:0000250|UniProtKB:A0A059TC02, ECO:0000269|PubMed:20876124}.

Medicago truncatula (Barrel medic) (Medicago tribuloides)

A0A075BSX9

HLNO_SHIS7

MTEKIYDAIVVGAGFSGLVAARELSAQGRSVLIIEARHRLGGRTHVVNFLGRPVEIGGAGVHWCQPHVFAEMQRYGFGFKEAPLADLDKAYMVFADGQKIDVPPATFDEEYTTAFEKFCSRSRELFPRPYSPLDNHEVSNLDGVSARDHLESLGLNELQLASMNAELTLYGGAPTTELSYPSFVKFHALASWDTITFTDSEKRYHVQGGTNALCQAIFDDCRADSEFGVPVEAVAQTDNGVTVTLADKRVFRALTCVLTLPTKVYADVRFEPPLPPEKRAFIEHAEMADGAELYVHVRQNLGNTFTFCDDPNPFNAVQTYAYDDELGTILKITIGRQSLINLENFDAIAAEIRKIHGDVEVLEALPYNWAMDEYARTSYPAMRKGWFSRYKDMAKPENRLFFAGSATADGWHEYIDGAIESGIRVGREIRHFMKATA

1.5.3.5

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:25002425}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:25002425};

alkaloid metabolic process [GO:0009820]; nicotine catabolic process [GO:0019608]

(S)-6-hydroxynicotine oxidase activity [GO:0018531]; nucleotide binding [GO:0000166]

PF01593;

3.50.50.60;

Flavin monoamine oxidase family

CATALYTIC ACTIVITY: Reaction=(S)-6-hydroxynicotine + H2O + O2 = 6-hydroxypseudooxynicotine + H2O2; Xref=Rhea:RHEA:11880, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58182, ChEBI:CHEBI:58682; EC=1.5.3.5; Evidence={ECO:0000269|PubMed:25002425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11881; Evidence={ECO:0000269|PubMed:25002425}; CATALYTIC ACTIVITY: Reaction=(S)-6-hydroxynicotine + O2 = 6-hydroxy-N-methylmyosmine + H2O2; Xref=Rhea:RHEA:46976, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58182, ChEBI:CHEBI:87164; Evidence={ECO:0000269|PubMed:25002425}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46977; Evidence={ECO:0000269|PubMed:25002425};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.019 mM for (S)-6-hydroxynicotine {ECO:0000269|PubMed:25002425}; KM=0.033 mM for 6-hydroxynornicotine {ECO:0000269|PubMed:27568381}; KM=2.03 mM for nicotine {ECO:0000269|PubMed:25002425}; Note=kcat is 7.3 sec(-1) with (S)-6-hydroxynicotine as substrate. kcat is 0.396 sec(-1) with nicotine as substrate (PubMed:25002425). kcat is 5.9 sec(-1) with 6-hydroxynornicotine as substrate (PubMed:27568381). {ECO:0000269|PubMed:25002425, ECO:0000269|PubMed:27568381};

PATHWAY: Alkaloid degradation; nicotine degradation; 6-hydroxypseudooxynicotine from nicotine (S-isomer route): step 2/2. {ECO:0000305}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Stable between pH 6.0 and 9.8. {ECO:0000269|PubMed:25002425};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. Stable at temperatures lower than 50 degrees Celsius. {ECO:0000269|PubMed:25002425};

FUNCTION: Involved in the degradation of L-nicotine (PubMed:25002425). Catalyzes the oxidation of (S)-6-hydroxynicotine (6-hydroxy-L-nicotine) to 6-hydroxypseudooxynicotine (PubMed:25002425). Oxidation of the pyrrolidine ring of (S)-6-hydroxynicotine leads to the formation of the optically inactive 6-hydroxy-N-methylmyosmine, which hydrolyzes spontaneously to 6-hydroxypseudooxynicotine (PubMed:25002425). Acts with absolute stereospecificity on the L-form of 6-hydroxynicotine (PubMed:25002425). Also involved in the degradation of nornicotine, and catalyzes the oxidation of 6-hydroxynornicotine to 6-hydroxymyosmine, which hydrolyzes to 6-hydroxypseudooxynornicotine (PubMed:27568381). In vitro, converts (S)-nicotine into N-methylmyosmine, which spontaneously hydrolyzes spontaneously into pseudooxynicotine, but catalytic efficiency is about 1900-fold higher with (S)-6-hydroxynicotine (PubMed:25002425). {ECO:0000269|PubMed:25002425, ECO:0000269|PubMed:27568381}.

Shinella sp. (strain HZN7)

A0A075D5I4

PINMT_RAUSE

MAEKQQAVAEFYDNSTGAWEVFFGDHLHDGFYDPGTTATIAGSRAAVVRMIDEALRFANISDDPAKKPKTMLDVGCGIGGTCLHVAKKYGIQCKGITISSEQVKCAQGFAEEQGLEKKVSFDVGDALDMPYKDGTFDLVFTIQCIEHIQDKEKFIREMVRVAAPGAPIVIVSYAHRNLSPSEGSLKPEEKKVLKKICDNIVLSWVCSSADYVRWLTPLPVEDIKAADWTQNITPFYPLLMKEAFTWKGFTSLLMKGGWSAIKVVLAVRMMAKAADDGVLKFVAVTCRKSK

2.1.1.-

alkaloid biosynthetic process [GO:0009821]; methylation [GO:0032259]; vindoline biosynthetic process [GO:1900985]

plant-type vacuole membrane [GO:0009705]

N-methyltransferase activity [GO:0008170]

PF13847;

3.40.50.150;

Class I-like SAM-binding methyltransferase superfamily, gTMT family

SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:35166361}.

CATALYTIC ACTIVITY: Reaction=picrinine + S-adenosyl-L-methionine = ervincine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:76143, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:70505, ChEBI:CHEBI:194555; Evidence={ECO:0000269|PubMed:26848097}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76144; Evidence={ECO:0000269|PubMed:26848097};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for picrinine {ECO:0000269|PubMed:26848097}; KM=9.3 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:26848097}; Vmax=126.1 pmol/sec/mg enzyme with picrinine as substrate {ECO:0000269|PubMed:26848097}; Vmax=97.2 pmol/sec/mg enzyme with S-adenosyl-L-methionine as substrate {ECO:0000269|PubMed:26848097}; Note=kcat is 5.8 sec(-1) with picrinine as substrate (PubMed:26848097). kcat is 4.5 sec(-1) with S-adenosyl-L-methionine as substrate (PubMed:26848097). {ECO:0000269|PubMed:26848097};

PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. {ECO:0000269|PubMed:26848097}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:26848097};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22 degrees Celsius. {ECO:0000269|PubMed:26848097};

FUNCTION: S-adenosyl-L-methionine-dependent N-methyltransferase involved in the biosynthesis of biologically active monoterpenoid indole alkaloids (MIAs) natural products including vindoline (PubMed:26848097). Catalyzes the conversion of picrinine to N-methylpicrinine (ervincine) (PubMed:26848097). Accepts also, with low efficiency, 21-hydroxycyclolochnericine and norajmaline as substrates (PubMed:26848097). {ECO:0000269|PubMed:26848097}.

Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)

A0A075D657

PINMT_VINMI

MYTCSIIIYILTFWQLSKIKKQVAAAEKQVMTVTEKQEAVAEFYDKSTDAWEVFFGEHLHDGFYEPGTTATIPGSKVAVVRMIDELLRFAGISDDPEKKPKTMLDVGCGLGGTCLHVAKKYDIKCTGITISPEQVKCAQDLAATQGLESKVSFDVGDALDMPYKDGTFDLVFTIQCIEHIQDKEKFIREMVRVAAPGAPVVIAGYAARNLSPSEESLKPEEKMVLEKICDHIVLSWLCSTGDYVKWLTPLPVQDIKVWDLTQNITPFYPLCIKEAFTWKSFTSLLKMGGWSAIKVVFAVKMMAMAAEEGLLKFAAVTCRKSK

2.1.1.-

alkaloid biosynthetic process [GO:0009821]; methylation [GO:0032259]; vindoline biosynthetic process [GO:1900985]

cytosol [GO:0005829]

N-methyltransferase activity [GO:0008170]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

PF08241;

3.40.50.150;

Class I-like SAM-binding methyltransferase superfamily, gTMT family

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:35166361}.

CATALYTIC ACTIVITY: Reaction=picrinine + S-adenosyl-L-methionine = ervincine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:76143, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:70505, ChEBI:CHEBI:194555; Evidence={ECO:0000269|PubMed:26848097}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76144; Evidence={ECO:0000269|PubMed:26848097};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20.1 uM for picrinine {ECO:0000269|PubMed:26848097}; KM=15.8 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:26848097}; Vmax=100.8 pmol/sec/mg enzyme with picrinine as substrate {ECO:0000269|PubMed:26848097}; Vmax=135 pmol/sec/mg enzyme with S-adenosyl-L-methionine as substrate {ECO:0000269|PubMed:26848097}; Note=kcat is 5.1 sec(-1) with picrinine as substrate (PubMed:26848097). kcat is 6.9 sec(-1) with S-adenosyl-L-methionine as substrate (PubMed:26848097). {ECO:0000269|PubMed:26848097};

PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. {ECO:0000269|PubMed:26848097}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:26848097};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22 degrees Celsius. {ECO:0000269|PubMed:26848097};

FUNCTION: S-adenosyl-L-methionine-dependent N-methyltransferase involved in the biosynthesis of biologically active monoterpenoid indole alkaloids (MIAs) natural products including vindoline (PubMed:26848097). Catalyzes the conversion of picrinine to N-methylpicrinine (ervincine) (PubMed:26848097). Accepts also, with low efficiency, 21-hydroxycyclolochnericine and norajmaline as substrates (PubMed:26848097). {ECO:0000269|PubMed:26848097}.

Vinca minor (Common periwinkle)

A0A075F7E9

LERK1_ORYSI

MVALLLFPMLLQLLSPTCAQTQKNITLGSTLAPQGPASSWLSPSGDFAFGFRPVEGNTSFYLIAVWFNKISDKTVVWYAKNTDQDPSIVEVPSDSFLQLTNDGALSLKDRSGQEGWNPQVTGVAYASMRDTGNFVLLGADGTTKWQTFDMPSDTILPTQVIPCNKTRNKSLRARLDIDDYSSGRFLLDVQTDGNLALYLVAVPSGSKYQQYWSTDTTGNGSELVFSETGKVYFALTDGTQINISSDAGIGSMADYFHRATLDPDGVFRQYVYPKKANAGILGGETWTALSMQPQNICHAIVSDVGSGVCGFNSYCTFDGTRNQIASCQCPPWYKFFDEQKKYKGCKQDFQPHSCDLEEATALAQFELRPIYGVDWPLSDYEKYEPIGQDDCGRLCVIECFCAMAVYNQSTSTCWKKKLPLSNGNMADYVQRTVLLKVPSSNSSQFMISTSSNKWKRNRKHWVLGSSLILGTSILVNFALISIFLFGTYCRITTKKNIPLSQASSKSQLPLKTFTYKELEKATAGFHEILGAGASGVVYKGQLEDELKTNIAVKTIHKLQPETEKEFMVEVETIGQTFHKNLVRLLGFCNERAERLLVYEFMTNGPLNRLLFDNSRPHWNTRVHIALGVARGFLYLHDECSKQIIHCDIKPQNILLDDNLVAKISDFGLAKLLLTNQTRTKTGIRGTRGYVAPEWFKNIGISTKVDVYSFGVILLELVCCRRNVELEVVDEEQTIVTYWANDCYRSGRIDLLVEGDDEAIYDIKKVERFVTVALWCLQEDPSMRPNMLKVTQMLDGAVAIPSPPDPCSFISSLP

2.7.11.1

defense response [GO:0006952]; phosphorylation [GO:0016310]; response to other organism [GO:0051707]

membrane [GO:0016020]

ATP binding [GO:0005524]; carbohydrate binding [GO:0030246]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]

PF01453;PF00069;

2.90.10.10;1.10.510.10;

Protein kinase superfamily, Ser/Thr protein kinase family

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

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305}; 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:0000305};

FUNCTION: Involved in innate immunity. Required for the expression of defense-related genes PR1A, LOX2 and CHS1 upon biotic stresses. Required for basal resistance to the fungal blast (M.grisea), bacterial blight (O.oryzae pv. oryzae, Xoo) and the herbivorous insect brown planthopper (N.lugens, BPH). May be involved in several defense signaling pathways. Involved in the promotion of seed germination. Required for the expression of alpha-amylase genes during seed germination (PubMed:15685292). Involved in resistance against the brown planthopper (BPH). Member of the BPH3 (BPH resistance locus 3) cluster which contains LECRK1, LECRK2 and LECRK3 (PubMed:25485617). {ECO:0000269|PubMed:15685292, ECO:0000269|PubMed:25485617}.

Oryza sativa subsp. indica (Rice)

A0A075F932

SYT1_ANSCY

MVSESHHEALAAPPATTVAAAPPSNVTEPASPGGGGGKEDAFSKLKEKFMNELNKIPLPPWALIAIAIVAVLLILTCCFCLCKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQDDDAETGLTDGEEKEEPKEVEKLGKIQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKYETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEYKVAMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQIVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQPEEEVDAMLAVKK

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains. {ECO:0000250|UniProtKB:P21707};

calcium ion-regulated exocytosis of neurotransmitter [GO:0048791]; cell differentiation [GO:0030154]; cellular response to calcium ion [GO:0071277]; multicellular organismal reproductive process [GO:0048609]; positive regulation of dendrite extension [GO:1903861]; regulation of calcium ion-dependent exocytosis [GO:0017158]; regulation of dopamine secretion [GO:0014059]; regulation of hormone secretion [GO:0046883]; regulation of regulated secretory pathway [GO:1903305]; response to calcium ion [GO:0051592]; synaptic vesicle endocytosis [GO:0048488]

axon [GO:0030424]; chromaffin granule membrane [GO:0042584]; cytoplasm [GO:0005737]; dense core granule [GO:0031045]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]

calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; clathrin binding [GO:0030276]; phosphatidylserine binding [GO:0001786]; phospholipid binding [GO:0005543]; syntaxin binding [GO:0019905]

PF00168;

2.60.40.150;

Synaptotagmin family

SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein {ECO:0000250|UniProtKB:P21707}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein {ECO:0000250|UniProtKB:P21707}. Cytoplasm {ECO:0000250|UniProtKB:P21707}. Note=Synaptic vesicles and chromaffin granules. {ECO:0000250|UniProtKB:P21707}.

FUNCTION: Calcium sensor that participates in triggering neurotransmitter release at the synapse (By similarity). May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. May play a role in dendrite formation by melanocytes (By similarity). May play a role in regulating the secretion of hormones relevant to the reproduction and egg-laying of female geese (PubMed:25146222). {ECO:0000250|UniProtKB:P21579, ECO:0000250|UniProtKB:P46096, ECO:0000269|PubMed:25146222}.

Anser cygnoides (Swan goose)

A0A075FBG7

ELS_MARVU

MSITFNLKIAPFSGPGIQRSKETFPATEIQITASTKSTMTTKCSFNASTDFMGKLREKVGGKADKPPVVIHPVDISSNLCMIDTLQSLGVDRYFQSEINTLLEHTYRLWKEKKKNIIFKDVSCCAIAFRLLREKGYQVSSDKLAPFADYRIRDVATILELYRASQARLYEDEHTLEKLHDWSSNLLKQHLLNGSIPDHKLHKQVEYFLKNYHGILDRVAVRRSLDLYNINHHHRIPDVADGFPKEDFLEYSMQDFNICQAQQQEELHQLQRWYADCRLDTLNYGRDVVRIANFLTSAIFGEPEFSDARLAFAKHIILVTRIDDFFDHGGSREESYKILDLVQEWKEKPAEEYGSKEVEILFTAVYNTVNDLAEKAHIEQGRCVKPLLIKLWVEILTSFKKELDSWTEETALTLDEYLSSSWVSIGCRICILNSLQYLGIKLSEEMLSSQECTDLCRHVSSVDRLLNDVQTFKKERLENTINSVGLQLAAHKGERAMTEEDAMSKIKEMADYHRRKLMQIVYKEGTVFPRECKDVFLRVCRIGYYLYSSGDEFTSPQQMKEDMKSLVYQPVKIHPLEAINV

4.2.3.131; 4.2.3.189; 4.2.3.190

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]

chloroplast [GO:0009507]

9,13-epoxylabda-14-ene synthase activity [GO:0106239]; magnesium ion binding [GO:0000287]; manoyl oxide synthase activity [GO:0062206]; 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=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:24990389}; 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:24990389}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33984; Evidence={ECO:0000269|PubMed:24990389}; CATALYTIC ACTIVITY: Reaction=8-hydroxycopalyl diphosphate = (13R)-manoyl oxide + diphosphate; Xref=Rhea:RHEA:54516, ChEBI:CHEBI:33019, ChEBI:CHEBI:64283, ChEBI:CHEBI:138234; EC=4.2.3.190; Evidence={ECO:0000269|PubMed:24990389};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:24990389}.

FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid including marrubiin and other labdane-related furanoid diterpenoids with potential applications as anti-diabetics, analgesics or vasorelaxants (Probable). Terpene synthase the catalyzes the conversion of peregrinol diphosphate to 9,13(R)-epoxy-labd-14-ene, from (+)-copalyl diphosphate ((+)-CPP) to miltiradiene and from 8-hydroxycopalyl diphosphate (LPP, labda-13-en-8-ol diphosphate) to manoyl oxide (PubMed:24990389). {ECO:0000269|PubMed:24990389, ECO:0000305|PubMed:24990389}.

Marrubium vulgare (White horehound)

A0A075QQ08

IF4E1_TOBAC

MVDEVEKPASLEESKTNTREVEEGAEEVIESDDTMSSLGNPCKAMKHPLEHSWTFWFDNPSGKSKQAAWGSSIRPIYTFSTVEDFWSVYNNIHHPSKLAVGADFHCFKNKIEPKWEDPVCASGGKWTMSFSRGKSDTCWLYTLLAMIGEQFDCGDEICGAVINVRVRQEKIALWTRNAANETAQVSIGKQWKEFLDYNDSIGFIFHDDAKKLDRAAKNRYSV

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-120-Cys-158 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:K0P2S0}. Cytoplasm {ECO:0000250|UniProtKB:K0P2S0}.

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:15988567). 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:15988567). Key component of recessive resistance to potyviruses (Ref.2). {ECO:0000269|PubMed:15988567, ECO:0000269|Ref.2}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection (e.g. potato virus Y (PVY) and pepper mottle virus (PepMoV)) by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000269|Ref.2}.

Nicotiana tabacum (Common tobacco)

A0A075TJ05

OTASE_ASPNG

MVRRIASATPMVQSPMSPLGTTYCVRPNPVSLNLQRRPLVIASTDEAKVTIIYAGLLIPGDGEPLRNAALVISDKIIAFVGSEADIPKKYLRSTQSTHRVPVLMPGLWDCHMHFGGDDDYYNDYTSGLATHPASSGARLARGCWEALQNGYTSYRDLAGYGCEVAKAINDGTIVGPNVYSSGAALSQTAGHGDIFALPAGEVLGSYGVMNPRPGYWGAGPLCIADGVEEVRRAVRLQIRRGAKVIKVMASGGVMSRDDNPNFAQFSPEELKVIVEEAARQNRIVSAHVHGKAGIMAAIKAGCKSLEHVSYADEEVWELMKEKGILYVATRSVIEIFLASNGEGLVKESWAKLQALADSHLKAYQGAIKAGVTIALGTDTAPGGPTALELQFAVERGGMTPLEAIKAATANAPLSVGPQAPLTGQLREGYEADVIALEENPLEDIKVFQEPKAVTHVWKGGKLFKGPGIGPWGEDARNPFL

3.4.17.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24947135};

proteolysis [GO:0006508]

extracellular region [GO:0005576]

carboxypeptidase activity [GO:0004180]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]

PF01979;

3.20.20.140;

Metallo-dependent hydrolases superfamily, Ochratoxinase amidase 2 family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24947135}.

CATALYTIC ACTIVITY: Reaction=H2O + ochratoxin A = L-phenylalanine + ochratoxin alpha; Xref=Rhea:RHEA:72751, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:166829, ChEBI:CHEBI:192527; Evidence={ECO:0000269|PubMed:24947135}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72752; Evidence={ECO:0000269|PubMed:24947135};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:24947135};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 66 degrees Celsius. {ECO:0000269|PubMed:24947135};

FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine (PubMed:24947135, PubMed:33647354). Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products (PubMed:24947135). {ECO:0000269|PubMed:24947135, ECO:0000269|PubMed:33647354}.

Aspergillus niger

A0A075TMP0

PATD_PENEN

MASTTPSTYKQAVFKEQGAGLTLEEVALTLPKRDEILVKVEACGVCHSDHFAQTNLMGGGFPLVPGHEIIGRVAAVGEGETVWKEGDRIGGAWHGGHDGTCGACKKGFFQMCDNEQVNGISRNGGYAEYCIIRREAAVHIPDHVNAAKYAPMLCAGVTVFNAMRHMKIPPGELVAIQGLGGLGHLALQYANKFGYRVVALSRDSTKEEFARKLGAHEYIDTSREDPVAALQKLGGASLIVSTAPVPEIINPLIQGLGVMGKLLILSIVGGIEVHTGLLVGKGKSIWSWPSGHATDSEDAIAFADLHGIDCLIEEFPLDKCNEAFAAMMEGSVRFRAVITM

1.1.1.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q96533}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q96533};

patulin biosynthetic process [GO:0140723]

cytosol [GO:0005829]

alcohol dehydrogenase (NAD+) activity [GO:0004022]; alcohol dehydrogenase (NADP+) activity [GO:0008106]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; polyketide synthase activity [GO:0016218]

PF08240;PF00107;

3.90.180.10;3.40.50.720;

Zinc-containing alcohol dehydrogenase family

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.

CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + neopatulin = (E)-ascladiol + NADP(+); Xref=Rhea:RHEA:62224, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145111, ChEBI:CHEBI:145112; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62225; Evidence={ECO:0000269|PubMed:30680886};

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

FUNCTION: Alcohol dehydrogenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatD catalyzes the conversion of neopatulin into E-ascladiol (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

Penicillium expansum (Blue mold rot fungus)

A0A075TMP8

PATI_PENEN

MDILQLAPTHLLAILLSSTSALFLITYLLRAGHRPSDLPNGPPTVPLFGNELQVPKSDAHFQFSRWAKEYGGFFTLKRYNNTTIVISDQKLIKTLLDKKSNIYSHRPASLVSHLITQSDHLLVMQYGERWRMLRKTIHQYFMEPRCERDHWKVQEAEAKQMLHDYLTMPEDHMLHPKRYSNSITNSLVFGIRTKTVHDEYMKKLFYLMDKWSLVQELGATPPVDSFALLRYVPQWMLGNWRNRAVEVGDLMQSLYQTVLDQVKERRQRGIQRDSFMDRVLDTLKQTPLSENELRFLGGVLMEGGSDTSSSLILTIIQAMTKYPEVQAKAHAQIDSIIGHNRSPAWSDWSKLPYINMIIKESHRWRPVSPLGVPHAVAEDDHIDGKLIPQGSSIVLNVWGMHHDSDRWQEPEHFQPERFADFPALASGYAGSERRDHLGYGAGRRICPGIHLAERNLIIGIAKLLWAFEFLEPLGSDSDISAHSGASKGFLHCPKDYGCVIRLRSPEKRETIMREFAEAQEVFARFD

1.-.-.-

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

patulin biosynthetic process [GO:0140723]

endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; polyketide synthase activity [GO:0016218]

PF00067;

1.10.630.10;

Cytochrome P450 family

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30680886}; Single-pass membrane protein {ECO:0000269|PubMed:30680886}.

CATALYTIC ACTIVITY: Reaction=3-hydroxybenzyl alcohol + O2 + reduced [NADPH--hemoprotein reductase] = gentisyl alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:62212, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:5325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17069, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62213; Evidence={ECO:0000269|PubMed:30680886};

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatI catalyzes the conversion of m-hydroxybenzyl alcohol into gentisyl alcohol (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

Penicillium expansum (Blue mold rot fungus)

A0A075TR33

PATO_PENEN

MRLHQSPPRLLVCILSVLQVSAGLSSNCRCMPGDSCWPSLNDWARFNTSIGGRLVDTQPLGQPCHDPFYTASECNELKQQWTHPELHDASSSSIMSAAVANETCDAFTPRSKPCTLGAMVRYAVNASSPDDFVQTIRFSQERNIRLVIRNTGHDYAGKSTGAGALSIWTHSLKEIDFLNYTSAHYTGPAVRMTAGIQGTDINPAAHKKGLVIVGGECATVGPVGGFTQGGGHSALSSRFGLAADQVLEWEVVDGMGRLLTASPTQNPDLYWALSGGGGGTFGVVYAVTVKTFPDFAVTGVVLQFENIDPSSNRFFEAVGHYHRHLPTYTSAGGMAIAQITNSSFLLTPLTLPAYTAAATKKLLGPFLQDLHQLNISYTLNVTESASYFQHYMKLIEPNPTQLVQNAQYGGRLLPLDLIERNNSQLTDAVQKLTADGVTFVGIGLNVSSSVTGDIWNSVLPGWRTAAMTVILTTSWPLGANLTKMKILADKMTTKWVPILTALSPESGCYMSEADPQQPDWKQTFYGRNYDSLYAIKTKYDPLQTFYATTAVGSEDWQVEAGGRLCQATRKN

1.-.-.-

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};

patulin biosynthetic process [GO:0140723]

fungal-type vacuole lumen [GO:0000328]; vacuole [GO:0005773]

FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491]; polyketide synthase activity [GO:0016218]

PF08031;PF01565;

3.30.465.10;

Oxygen-dependent FAD-linked oxidoreductase family

SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:30680886}.

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatO acts with patJ in the vacuole to convert gentisyl alcohol to isoepoxydon (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

Penicillium expansum (Blue mold rot fungus)

A0A075TR41

PATJ_PENEN

MAPFVPYHYSAGQSTIVKFGGLLTTEFLEPPPGRCFLFRQTYRHTIEGSIPENLRKLINSPDRPKGPPPHFHQFQTEYFRVENGVLGISVDGVVRRITPEDGEISVKAGSVHNFFIHPDSPENMTVYLSASDSGNDYQLDRVFFENWYGYWHDALLHDGGIDWIQFLAIQDGGDAYTPAPAWVPFRRQVGYWTCVIVGRWIGGLLGYKPFFREYTTDWDFAVAKMKGSFFQRHLVHAAFEEEKSWTKQAELEPKGKPENAEFEPWTEDMSPAPLSLGPVAYEQGLFHGVQPGSVNGSNGHSTGVESKLEQLGSRAQRRVVIDDAGK

1.-.-.-

patulin biosynthetic process [GO:0140723]

cytoplasmic vesicle lumen [GO:0060205]; fungal-type vacuole lumen [GO:0000328]; vacuole [GO:0005773]

oxidoreductase activity [GO:0016491]; polyketide synthase activity [GO:0016218]

2.60.120.10;

Oxidoreductase OpS7 family

SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:30680886}. Cytoplasmic vesicle lumen {ECO:0000269|PubMed:30680886}.

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

FUNCTION: Probable oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatJ acts with patO in the vacuole to convert gentisyl alcohol to isoepoxydon (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

Penicillium expansum (Blue mold rot fungus)

A0A075TRC0

PATK_PENEN

MHSVSPSTYPSGGTSPAPADTPGTEYSEYEFSNDVAVVGMACRVAGGNHNPELLWQSLLSQKSAVGEIPEMRWEPYYRRDPRNAKELKKTTSRGYFLDRLEDFDCQFFGISPKEAEQMDPQQRVSLEVASEALEDAGIPAKSLSGSDTAVFWGVNSDDYSKLVLEDLPNVEAWMGIGTAYCGVPNRISYHLNLMGPSTAVDAACASSLVAVHHGVQAIRLGESQVAIVGGVNALCGPGLTRVLDKAGAISSDGSCKSFDDDAHGYARGEGAGALVLKSLHRALLDHDNVLAVIKGSAVAQDGKTNGIMAPNAKAQQLAARTALNVAGVDPSTVRYVEAHATSTPLGDPTEISAIAGVYGTNRPADDPCYIGSIKPNIGHLEAGAGVMGFIKAILTIQKGVLPPQANLTNLNSRIDWKTAGVKVVQEATPWPSSDPIRRAGVCSYGYGGTVSHAVIEEFNPILRPDPLDDGAATGPGLLLLSGPQEKRLALQAKTLREWMTADGKDNNLSEILTTLATRRDHHDYRAALVVDDHLDATQVLQALANGTDHSFTTQSRVLGADVSKDVVWVFSGHGAQWPDMGKQLIHNPVFFAAIQPLDELIQAEIGLSPIELLRTGDFESSDRVQILTYLMQIGLSAILQSNGITPQAVIGHSVGEIAASVVAGALTSAEGALIVTRRALLYRQVMGKGGMILVNLPSAETEEILGRRQDLVVAIDSSPSSCVVAGDKDIVAETAEAFKARGVKTFTVKSDIAFHSPTLNVLMDPLRDALGQALAPTVHIKLYSTALVDPRGQDVRDLEYWTGNMVNRVRLTSAIQAAVEDGYRLFLEVSTHPVVSHSINETLMDAGLEDFAVIPTLLRKKPTEKHILHSIAQLHCRGAEVNWAAQMPGRWATGLPTTTWMHKPIWRKIETAPLHTGLTHDVEKHTLLGQRIPVPGTDTFVYTSRLDNETKPFPGSHPLHGTEIVPAAGLINTFLKGTGGQMLQNVVLRVPVAINAPRSVQVVVQQDQVKVVSRLISSDPSLSDDDASWVTHTTAYWDRKVLGSADRIDLAAVKARLTTKLADNFSIDYLDKVGVSAMGFPWAVTEHYRDTKQMLARVDVNPAVLGDDPLPWDSSSWAPVLDAATSVGSTVFQTAALRMPAQIERVEIFTSEDPPKISYLFVEEASDSVPTSHVSVLSETGEVLAKFTAMRFSEIEGTPGVSGSMESLVHQIAWPPATPAEEPLLITKVILVSPDATARAQYAATLPTQVQSFQFSTTEDFFSNASSLPLEKGTVVAYIPGEVASLAEVPAASESFTWNLLELIKFIVNGSLPIKVFTLTSSVGDGQTPTALAQSPLIGLARIIASEHPDLGSLIDIEEPKIPLSTMRYIQGADVIRISDGIARVSRFRSLPRTKLRPASEGPRLLPRPDGTYLITGGLGILGLEVADFLVEKGARRLLLISRRALPPRRTWDQVSEDLQPTIAKIRLLESRGASVHVLPLDITKPDAVEQLSTALDRLSLPAVQGVVHAAGVLDNEMVLQTTRDAFNRVLAPKIAGALALHEVFPPKSVDFFVMFSSCGNLVGFTGQASYGSGNAFLDTLATHRARLGDSGAVAFQWTAWRGLGMGSSTDFINAELEAKGITDVTRDEAFAAWQHLAKYDIDHGVVLRSLAIDDGEPVPVPILNDIVVRRVSELSGSAQAAAGSSGNDAVPSSGPELKAYLDEKIRGCVAKVLQMTAEDVDSKAALADLGVDSVMTVTLRRQLQQTLKIPVPPTLTWSHPTVSHLVVWFAEKIGK

2.3.1.165

fatty acid biosynthetic process [GO:0006633]; patulin biosynthetic process [GO:0140723]

cytosol [GO:0005829]

3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; 6-methylsalicylic acid synthase activity [GO:0050641]; fatty acid synthase activity [GO:0004312]; phosphopantetheine binding [GO:0031177]; polyketide synthase activity [GO:0016218]

PF00698;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;

3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.366.10;3.40.50.720;3.10.129.110;

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 3 H(+) + 3 malonyl-CoA + NADPH = 6-methylsalicylate + 3 CO2 + 4 CoA + H2O + NADP(+); Xref=Rhea:RHEA:12240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:36658, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=2.3.1.165; Evidence={ECO:0000269|PubMed:30680886};

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

FUNCTION: 6-methylsalicylic acid synthase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886, PubMed:35339702). PatK catalyzes the first step of the pathway which is the synthesis of 6-methylsalicylic acid via condensation of 1 acetate and 3 malonate units (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000269|PubMed:35339702, ECO:0000305|PubMed:30680886}.

Penicillium expansum (Blue mold rot fungus)

A0A075TRK9

PATE_PENEN

MRLTSGIFHAAIAVAAVGAVLPEGPSSSKTHRNEYARRMLGSSFGIPKNQTFDYLVIGGGTAGLTIATRLAEQGVGSVAVIEAGGFYELNNGNLSQIPAQDAFYVGTDLDDWQPGIDWGFHTTPQAGAYDRVSHYARGKCLGGSSARNYMAYQRGTKAAHQRWADTVGDSSYTWEQFLPFFEKSLHFTPANDALRGANASVVSDPSVLGNGDGPLSVTYPHYAQAFATWAKHAFIEIGLQIRSGFQSGALLGQSYGLYTINATTMHRESSETSFLRKGLADPNLTVFQSALAKRIRFQDKRAVGVDVETMGRAYTLSARKEIVLSAGAFQSPQLLMVSGVGPAATLKAHNIPLVADRPGVGQNMQDHIIYAPSYRVNVITQSALLNEEFEAQANRDYNERAAGIYANPTSDILAWEKIPEPKRSAWFSNHTRQVLAEYPDDWPEVEFLTMGGYFGYQRNYIRDNPSDGYNYASLAVSLCTPRSRGNVTITSPDAGVPPVINPNWLTDPVDVELAVAAFKRTRDFFNTTAIKPILIGPEYFPGSQVATDAEILDHVRKSFDTIFHASCTCAMGLANDTQAVVDSKARVIGVEALRVVDASALPFLPPGHPQSTLYALAEKIACEISGNC

1.1.-.-

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:E4QP00};

patulin biosynthetic process [GO:0140723]

cell cortex [GO:0005938]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; vacuole [GO:0005773]

flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on CH-OH group of donors [GO:0016614]; polyketide synthase activity [GO:0016218]

PF05199;PF00732;

3.50.50.60;3.30.560.10;

GMC oxidoreductase family

SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:30680886}. Vacuole {ECO:0000269|PubMed:30680886}. Secreted {ECO:0000269|PubMed:30680886}. Secreted, cell wall {ECO:0000269|PubMed:30680886}.

CATALYTIC ACTIVITY: Reaction=(E)-ascladiol + A = AH2 + patulin; Xref=Rhea:RHEA:62228, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:74926, ChEBI:CHEBI:145112; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62229; Evidence={ECO:0000269|PubMed:30680886};

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

FUNCTION: Patulin synthase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatE catalyzes the last step of the pathway which is the conversion of E-ascladiol to patulin (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

Penicillium expansum (Blue mold rot fungus)

A0A075TRL5

PATH_PENEN

MEPFLLLLLVLLPAIVLVRYAFTYGHRTSTMPIGPPTLPFIGNIHQITKKYTHIKFTEWAAQYGGLYMLKIGNGNMAVITDRRLVKEVLDRKSGIYSHRPHSFVSHDLITKGNHLLVMHYGDQWRTFRRLVHQHLMETMVENHHTKIVNAEAIQLVRDYMIDPEHHMAHPKRYSNSITNSIVFGIRTANREGANMRRLYKLMEEWSEVMETGATPPVDLFPWLKLLPQWLFNNYIDRAKAIGVQMETLYVDILNKVIKRREDGHNNGTFMDKVLDSQEKHNLPWHQLAFIGGVLMEGGSDTSSSLTLAIVQALIQNPDVQRKAHAEIDAVVGHNRSPVWEDFEKLPYINMIIKEGHRWRPILPLCFPHALGEDDWVDGKFLPKGTIVVVNTWGMHMDPSQPDDPAAFIPERFAKHPQLAPDYVPGTWERRDHYGYGVGRRICPGIHLAERNMFLGIAKLLWAFDFQPGEGPIDSDPVTGYHNGFLYCAKDYSCRPVIRNEVIRDTIEREYATATADVFSRFTEG

1.-.-.-

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

patulin biosynthetic process [GO:0140723]

endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; polyketide synthase activity [GO:0016218]

PF00067;

1.10.630.10;

Cytochrome P450 family

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30680886}; Single-pass membrane protein {ECO:0000269|PubMed:30680886}.

CATALYTIC ACTIVITY: Reaction=3-methylphenol + O2 + reduced [NADPH--hemoprotein reductase] = 3-hydroxybenzyl alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:62208, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17069, ChEBI:CHEBI:17231, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62209; Evidence={ECO:0000269|PubMed:30680886};

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatH catalyzes the conversion of m-cresol into m-hydroxybenzyl alcohol (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

Penicillium expansum (Blue mold rot fungus)

A0A075TXZ1

PATG_PENEN

MAKIDVHHHFYPPAMRQALDRAGGDPSGWYIPPWTLELDQDITRQMKVTTTILSVTAPGPGIEPDVTKAAALARSCNESAAAIRDAKPQQYGFFASVPSLFDTAAVLKEIEYACTTLRADGVTLFTRYGKGSNYLGHAAFRPIWADLSRRGAVVFIHPTHPVDTQLINTWLPQPMFDYPHETGRAAMDLLTSGILQDYPGCKIILSHAGGTLPYLIHRAATMLPLMPRTLGLSTEELVEAARTFYFDTAISSNPVTLKALFEFAAPGHVLFGSDFPNAPHDAILRFTNFLEAYELPEETKRQVDSGAALELFPRLKGILDKAKL

4.1.1.52

patulin biosynthetic process [GO:0140723]

cytosol [GO:0005829]

6-methylsalicylate decarboxylase activity [GO:0047596]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; polyketide synthase activity [GO:0016218]

PF04909;

3.20.20.140;

Metallo-dependent hydrolases superfamily, ACMSD family

SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.

CATALYTIC ACTIVITY: Reaction=6-methylsalicylate + H(+) = 3-methylphenol + CO2; Xref=Rhea:RHEA:23112, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17231, ChEBI:CHEBI:36658; EC=4.1.1.52; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23113; Evidence={ECO:0000269|PubMed:30680886};

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

FUNCTION: 6-methylsalicylic acid decarboxylase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatG catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

Penicillium expansum (Blue mold rot fungus)

A0A076FFM5

F8H1_OCIBA

MPFPMEVLQASSLSFPLLRRHSRNNLINKFRNPTLPRIDIPRQNIDLKTFAATTPTVACPPSDPEIIPEKKEDKFDWYENWYPVATVCDLDKRRPHGRKVIGIDVVVWWDRKENAWKVFDDTCPHRLAPLSEGRIDQWGRLQCVYHGWCFDGVGACKFIPQAPHDGPPVETSKKACVKGVYPSCVRNGIVWFWPNSDPKYKDIYLTNKPHYIPELDDPSFTCTTITREVPYGYEILAENLMDPSHVPYAHYGILELEKVKESSKRDREGGHEMEISVGTIDVNGFSAKHVSADYYFVPPYVYYGRITPNAATKTKDATLPVVPEEKTAMIVFYCIPVTPGYSRLIYAGARNFAVQIDRFVPRWITHMSHNLIFDSDLFLLHVEEQKLKDLDWHKSCYIPTKADGQVVAFRRWLNKYGGTQVDWRNNFTPALPPTPSREQLFDRYWSHTAECSSCSVACKRLNALEIGLQAMSLVFVAMAAAVSAPATRYSMVAMAVLSFLASKWLSHFIHKTFYNHGYDHAFV

1.14.15.-

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

flavonoid metabolic process [GO:0009812]

chloroplast [GO:0009507]; chloroplast membrane [GO:0031969]; cytoplasm [GO:0005737]

2 iron, 2 sulfur cluster binding [GO:0051537]; chlorophyllide a oxygenase [overall] activity [GO:0010277]; metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497]

PF08417;PF00355;

2.102.10.10;

SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000269|PubMed:25139498}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:25139498}.

CATALYTIC ACTIVITY: Reaction=2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] + salvigenin = 8-hydroxysalvigenin + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:73455, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:192703, ChEBI:CHEBI:192704; Evidence={ECO:0000269|PubMed:25139498}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73456; Evidence={ECO:0000269|PubMed:25139498};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for salvigenin {ECO:0000269|PubMed:25139498}; Vmax=60.3 pmol/sec/mg enzyme with salvigenin as substrate {ECO:0000269|PubMed:25139498};

PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}.

FUNCTION: Rieske-type, PAO-family oxygenase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects (PubMed:25139498). Catalyzes the 8-hydroxylation of salvigenin (SALV) to produce 8-hydroxysalvigenin (8-OH-SALV) (PubMed:25139498). Can also use cirsimaritin (CIRM) as substrate with low efficiency (PubMed:25139498). {ECO:0000269|PubMed:25139498}.

Ocimum basilicum (Sweet basil)

A0A078CGE6

M3KE1_BRANA

MARQMTSSQFHKSKTLDNKYMLGDEIGKGAYGRVYIGLDLENGDFVAIKQVSLENIVQEDLNTIMQEIDLLKNLNHKNIVKYLGSLKTKTHLHIILEYVENGSLANIIKPNKFGPFPESLVTVYIAQVLEGLVYLHEQGVIHRDIKGANILTTKEGLVKLADFGVATKLNEADVNTHSVVGTPYWMAPEVIEMSGVCAASDIWSVGCTVIELLTCVPPYYDLQPMPALFRIVQDDSPPIPDSLSPDITDFLRQCFKKDSRQRPDAKTLLSHPWIRNSRRALQSSLRHSGTIRYMKGADSSSEKDGEGSQDIAESVSAEKVGMSKTNSKSKLGVGSFRSEKDQSSASDIGEERADSEDDIMSDQGPTLSIHDNKSSLQSSTCSISSDAKGTSQDGKSEPDGNLEMEASEGRRKASATKQVGKESSIQMQQRSHSFGPKGEDRGLRKAVKTPSSYGGNELTRFSDPPGDACLHDLFHPLNKVPEGKLNEASASTPASNANQGDSPVADGGKNDLATKLRARIAQKQMEGETGHSNDGGDLFRLMMGVLKDDVIDIDGLVFDEKASPDNLLPLQAVEFSRLVSSLRPSETEDAIVTSCQKLVAMFRHRPEQKVVFVTQHGFLPVMDLLDSPKSRVTCAVLQLINEIIKDNIDFQENACLVGLIPLVMSFAGPERDRSREIRKEAAYFLQQLCQSSSLTLQMFIACRGIPVLVGFLEADYAKYRSMVHLAIDGMWQVFKLKRSTPRNDFCRIAAKNGILLRLINTLYSLNEATLLASEGRSGQLDQHEALLSVIDHPDVLKTRPGGGEEPSNSQRSDLYQPDGDRPRSSSAALDATEDVKQHHRISISSNRTSTDKIQKLAESASNGYAVTQPEQVRPLLSLLEKEPPSRHVSGQLDYVKHIAGLEKHESILPLLRASIDTMPRYFSKTMSKKVMAIEGAASASGVLSGSGVLNARLGSDTSSGLLSHMVTTLSAEVASQYLEKVADLLLEFARADTTVKSYMCSQSLLSRLFHMFNRVEPPILLKILKCTNHLSTDPNCLESLQRADAIKHLIPNLEVKEGNLVDQIHHEVLSALFNLCKINKRRQEQAAENGIIPHLMLFVMSDSPLKQYALPLLCDMAHASRNSREQLRSHGGLDVYLSLLDDEYWSVIALDSIAVCLAQDNDNRKVEQALLKDDAIYTLVNFFQSCPERHFVHILEPFLKIITKSSRINTTLAVNGLTPLLIARLDHQDAIARLNLLKLIKAVYEHHPRPKQLIVENDLPQRLQNLIEERREGQHLGGQVLVKQMATSLLKALHINTVL

2.7.11.1

cell cycle [GO:0007049]; cell division [GO:0051301]; MAPK cascade [GO:0000165]; protein autophosphorylation [GO:0046777]; regulation of cell division [GO:0051302]

cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]

PF00069;

1.25.10.10;1.10.510.10;

Protein kinase superfamily, Ser/Thr protein kinase family

PTM: Autophosphorylated. {ECO:0000269|PubMed:11489177}.

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q8T2I8}. Nucleus, nucleolus {ECO:0000269|PubMed:15292395}. Cell membrane {ECO:0000250|UniProtKB:Q9LJD8}. Note=Accumulates in the nucleolus during interphase (PubMed:15292395). Localized to the plasma membrane in developing pollen grains (By similarity). {ECO:0000250|UniProtKB:Q9LJD8, ECO:0000269|PubMed:15292395}.

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:11489177}; 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:11489177};

FUNCTION: Serine/threonine-protein kinase involved in the spatial and temporal control system organizing cortical activities in mitotic and postmitotic cells (PubMed:11489177). Required for the normal functioning of the plasma membrane in developing pollen. Involved in the regulation of cell expansion and embryo development (By similarity). {ECO:0000250|UniProtKB:Q9LJD8, ECO:0000269|PubMed:11489177}.

Brassica napus (Rape)

A0A087WPF7

AUTS2_MOUSE

MDGPTRGHGLRKKRRSRSQRDRERRSRAGLGTGAAGGIGAGRTRAPSLASSSGSDKEDNGKPPSSAPSRPRPPRRKRRESTSAEEDIIDGFAMTSFVTFEALEKDVAVKPQERAEKRQTPLTKKKREALTNGLSFHSKKSRLSHSHHYSSDRENDRNLCQHLGKRKKMPKGLRQLKPGQNSCRDSDSESASGESKGFQRSSSRERLSDSSAPSSLGTGYFCDSDSDQEEKASDASSEKLFNTVLVNKDPELGVGALPEHNQDAGPIVPKISGLERSQEKSQDCCKEPVFEPVVLKDPHPQLPQLPSQAQAEPQLQIPSPGPDLVPRTEAPPQFPPPSTQPAQGPPEAQLQPAPLPQVQQRPPRPQSPSHLLQQTLPPVQSHPSSQSLSQPLSAYNSSSLSLNSLSSRSSTPAKTQPAPPHISHHPSASPFPLSLPNHSPLHSFTPTLQPPAHSHHPNMFAPPTALPPPPPLTSGSLQVPGHPAGSTYSEQDILRQELNTRFLASQSADRGASLGPPPYLRTEFHQHQHQHQHTHQHTHQHTFTPFPHAIPPTAIMPTPAPPMFDKYPTKVDPFYRHSLFHSYPPAVSGIPPMIPPTGPFGSLQGAFQPKTSNPIDVAARPGTVPHTLLQKDPRLTDPFRPMLRKPGKWCAMHVHIAWQIYHHQQKVKKQMQSDPHKLDFGLKPEFLSRPPGPSLFGAIHHPHDLARPSTLFSAAGAAHPTGTPFGPPPHHSNFLNPAAHLEPFNRPSTFTGLAAVGGNAFGGLGNPSVTPNSVFGHKDSPSVQNFSNPHEPWNRLHRTPPSFPTPPPWLKPGELERSASAAAHDRDRDVDKRDSSVSKDDKERESVEKRHPSHPSPAPPVPVSALGHNRSSTDPTTRGHLNTEAREKDKPKEKERDHSGSRKDLTTEEHKAKESHLPERDGHSHEGRAAGEEPKQLSRVPSPYVRTPGVDSTRPNSTSSREAEPRKGEPAYENPKKNAEVKVKEERKEDHDLPTEAPQAHRTSEAPPPSSSASASVHPGPLASMPMTVGVTGIHAMNSIGSLDRTRMVTPFMGLSPIPGGERFPYPSFHWDPMRDPLRDPYRDLDMHRRDPLGRDFLLRNDPLHRLSTPRLYEADRSFRDREPHDYSHHHHHHHHPLAVDPRREHERGGHLDERERLHVLREDYEHPRLHPVHPASLDGHLPHPSLLTPGLPSMHYPRISPTAGHQNGLLNKTPPTAALSAPPPLISTLGGRPGSPRRTTPLSAEIRERPPSHTLKDIEAR

actin cytoskeleton organization [GO:0030036]; axon extension [GO:0048675]; dendrite extension [GO:0097484]; innate vocalization behavior [GO:0098582]; neuron migration [GO:0001764]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of Rac protein signal transduction [GO:0035022]; positive regulation of transcription by RNA polymerase II [GO:0045944]; righting reflex [GO:0060013]

cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; growth cone [GO:0030426]; nucleus [GO:0005634]

chromatin binding [GO:0003682]

PF15336;

AUTS2 family

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19948250, ECO:0000269|PubMed:25519132, ECO:0000269|PubMed:25533347}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25533347}. Cell projection, growth cone {ECO:0000269|PubMed:25533347}. Note=Detected both in cytoplasm and nucleus (PubMed:25533347). Colocalizes with RAC1 at actin-rich growth cones (PubMed:25533347). Detected on the promoter region of actively transcribed genes (PubMed:25519132). {ECO:0000269|PubMed:25519132, ECO:0000269|PubMed:25533347}.

FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. The PRC1-like complex that contains PCGF5, RNF2, CSNK2B, RYBP and AUTS2 has decreased histone H2A ubiquitination activity, due to the phosphorylation of RNF2 by CSNK2B. As a consequence, the complex mediates transcriptional activation (By similarity). In the cytoplasm, plays a role in axon and dendrite elongation and in neuronal migration during embryonic brain development. Promotes reorganization of the actin cytoskeleton, lamellipodia formation and neurite elongation via its interaction with RAC guanine nucleotide exchange factors, which then leads to the activation of RAC1 (PubMed:25533347). {ECO:0000250|UniProtKB:Q8WXX7, ECO:0000269|PubMed:25533347}.

Mus musculus (Mouse)

A0A087X1C5

CP2D7_HUMAN

MGLEALVPLAMIVAIFLLLVDLMHRHQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREAMVTRGEDTADRPPAPIYQVLGFGPRSQGVILSRYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFADQAGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLPHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAKKEKAKGSPESSFNDENLRIVVGNLFLAGMVTTSTTLAWGLLLMILHLDVQRGRRVSPGCPIVGTHVCPVRVQQEIDDVIGQVRRPEMGDQAHMPCTTAVIHEVQHFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWKKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQPRPSHSRVVSFLVTPSPYELCAVPR

1.14.14.1

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413;

arachidonic acid metabolic process [GO:0019369]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805]

cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]

aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]

PF00067;

1.10.630.10;

Cytochrome P450 family

SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000305|PubMed:15051713}. Mitochondrion {ECO:0000269|PubMed:18838503}.

CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000269|PubMed:15051713};

FUNCTION: May be responsible for the metabolism of many drugs and environmental chemicals that it oxidizes. It may be involved in the metabolism of codeine to morphine (PubMed:15051713). However, another study could not confirm it (PubMed:18838503). {ECO:0000269|PubMed:15051713, ECO:0000269|PubMed:18838503}.

Homo sapiens (Human)

A0A088MIT0

BRKP2_PHYNA

MAFLKKSLFLVLFLGVVSLSFCEEEKREEHEEEKRDEEDAESLGKRYGGLSPLRISKRVPPGFTPFRSPARSISGLTPIRLSKRVPPGFTPFRSPARRISEADPGFTPSFVVIKGLSPLRGKRRPPGFSPFRVD

defense response [GO:0006952]

extracellular region [GO:0005576]

toxin activity [GO:0090729]

PF03032;

Frog skin active peptide (FSAP) family, Bradykinin-related peptide subfamily

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26443407}.

FUNCTION: [[Val1,Thr6]-bradykinyl-Ser,Pro,Ala]: May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. May target bradykinin receptors (BDKRB). {ECO:0000250|UniProtKB:P84899}.; FUNCTION: [Bradykinin]: May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. May target bradykinin receptors (BDKRB). {ECO:0000250|UniProtKB:L0PIN3}.; FUNCTION: [Des-Arg9-bradykinin]: May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. May target bradykinin receptors (BDKRB). {ECO:0000250|UniProtKB:L0PIN3}.; FUNCTION: [[Hyp3]-bradykinyl-Val,Asp]: May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. May target bradykinin receptors (BDKRB). {ECO:0000250|UniProtKB:L0PIN3}.

Physalaemus nattereri (Cuyaba dwarf frog) (Eupemphix nattereri)

A0A088MLT8

IQIP1_MOUSE

MRLEELKRLQNPLEQVDDGKYLLENHQLAMDVENNIENYPLSLQPLESKVKIIQRAWREYLQRQDPLEKRSPSPPSVSSDKLSSSVSMNTFSDSSTPDYREDGMDLGSDAGSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDDRGYRDDGCPAREPGDVSARIGSSGSGSRSAATTMPSPMPNGNLHPHDPQDLRHNGNVVVAGRPNASRVPRRPIQKTQPPGSRRGGRNRASGGLCLQPPDGGTRVPEEPPAPPMDWEALEKHLAGLQFREQEVRNQGQARTNSTSAQKNERESIRQKLALGSFFDDGPGIYTSCSKSGKPSLSARLQSGMNLQICFVNDSGSDKDSDADDSKTETSLDTPLSPMSKQSSSYSDRDTTEEESESLDDMDFLTRQKKLQAEAKMALAMAKPMAKMQVEVEKQNRKKSPVADLLPHMPHISECLMKRSLKPTDLRDMTIGQLQVIVNDLHSQIESLNEELVQLLLIRDELHTEQDAMLVDIEDLTRHAESQQKHMAEKMPAK

axon ensheathment [GO:0008366]; negative regulation of cytoskeleton organization [GO:0051494]; positive regulation of hippo signaling [GO:0035332]

axon initial segment [GO:0043194]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; node of Ranvier [GO:0033268]; plasma membrane [GO:0005886]

ankyrin binding [GO:0030506]; calmodulin binding [GO:0005516]; transmembrane transporter binding [GO:0044325]

PF15157;PF10148;

SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:18550753}. Cytoplasm {ECO:0000250|UniProtKB:B3KU38}. Note=Localizes to the axon initial segments (AIS) and nodes of Ranvier of neurons and is absent from dendrites. {ECO:0000269|PubMed:18550753}.

FUNCTION: May play a role in action potential conduction in myelinated cells through the organization of molecular complexes at nodes of Ranvier and axon initial segments (PubMed:25950943, PubMed:25953347, PubMed:27979964). May also play a role in axon outgrowth and guidance (PubMed:25953347). {ECO:0000269|PubMed:25950943, ECO:0000269|PubMed:25953347, ECO:0000269|PubMed:27979964}.

Mus musculus (Mouse)

A0A089QRB9

MSL3_MYCTU

MRTATATSVAVIGMACRLPGGIDSPQRLWEALLRGDDLVGEIPADRWDANVYYDPEPGVPGRSVSRWGAFLDDVGGFDCDFFGLTEREATAIDPQHRLLLEVSWEAIEHAGVDPATLAESQTGVFVGLTHGDYELLSADCGAAEGPYGFTGTSNSFASGRVAYTLGLHGPAVTVDTACSSGLTAVHQACRSLDDGESDLALAGGVVVTLEPRKSVSGSLQGMLSPTGRCHAFDEAADGFVSGEGCVVLLLKRLPDAVRDGDRVLAIVRGTAANQDGRTVNIAAPSAQAQIAVYQQALAAAGVEASTVGMVEAHGTGTPVGDPVEYASLAAVYGTEGPCALTSVKTNFGHLQSASGPLGLMKTILALRHGVVPQNLHFCRLPDQLAEIDTELFVPQANTSWPDNTGQPRRAAVSSYGMSGTNVHAILEQAPVSEPAASGPELTPEAGGLALFPVSATSAEQLHVTAARLADWVDQNGNAGSRVSMRDLGYTLSCRRAHRPVRTVVTASSFDELSAALRDVAGDQIPYQPAVGHDDRGPVWVFSGQGSQWPGMGTELLVAEPVFAATVAAMEPVIARESGFSVTEAMSAPQTVSGIDRVQPTIFAVQVALAAALKSYGVRPGAIIGHSLGEAAAAVVAGALSLHDGLRVICRRSRLMSRIAGSGAMASVELPGQQVLSELAIRGISDVVLSVVASPTSTVVGGATQSIRDLVAAWEQQDVLAREVAVDVASHTPQVDPILDELLEVLAEVDPTAPEIPYYSATLWDPRERPSFTGEYWVENLRYTVRFAAAVQAALKDGYRVFGELAPHPLLTYAVEQNAASLDMPIATLAAMRRGEQLPFGLRGFVADVHNAGAKVDFSVQYPDGRLVDAPLPSWTHRTLMLSREDSHRSHTGAVQAVHPLLGAHVHLLEEPERHVWQAGVGTGAHPWLGDHRIHNVAAFPGAAYCEMALAAARTTLGELSEVRDIKFEQTLLLDEQTVVSSAATIAAPGILQFAVESHQEGEPARRASAMLHALEEMPQPPGYDTNALTAAHESSMSGEELRKMFNSLGIQYGPAFSGLVAVHTARGDVTTVLAEVALPGAIRSQQSAYASHPALLDACFQSVLVHPEVQKATVGGLMLPVGVRRLRNYHSTRSAHYCLARVTSSSRAGECEADLDVFDQAGTVLLTVEGLRLAAGISEHERANRVFDERLLTIEWERGELPEVPQIDAGSWLLLSASEADPLTAQLADALNAVGAQSTSVASASDVAQLRSLLGGRLTGVVVVTGPPTGGLTQCGRDYVSQLVGIARELAELPGEPPRLFVVTRSAASVLPSDLANLEQAGLRGLMRVIDSEHPHLGATAIDVDNDETVAALVASQLQSGSQEDETAWRNGIWYTARLRPGPLRPAERRTAVVEYRRDGMRLQIRTPGDLESLEFVTFDRVAPGPGEIEVAVTASSVNFADVLVAFGRYPTFEGYRQQLGIDFAGVVTAVGPDVTEHRIGDHVGGMSANGCWSTFVRCDARLAVTLPPELPVAAAAAVPTASATAWYALHDLARICSDDKVLIHSGTGGVGQAAIAIARAAGCEIFATAGSAQRRQLLHDMGVEHVYDSRSTEFAEQIRGDTDGYGVDVVLNSLPGAAQRAGIELLAFGGRFVEIGKRDIYGDTRLGLFPFRRNLSLYAVDLALLTHSHPHTVRRLLKTVYQHTVEGTLPVPQTTHYPIHDAAVAIRLVGGAGHTGKVVLDVPRTGEGVAVVPPEQVRTSRPDGAYLVTGGLGGLGLFLAGELAAAGCGRIVLNSRSTPSPHATRVIERLRAAGADIQVECGDIADAATAHRVVAVATASGLPVRGVLHAAAVVEDATLANVTDELIDRCWAPKVHGAWNIHRATAAQPLEWFCLFSSAAALVGSPGQGAYAAANSWLDAFAHWRRAQGLPATSIAWGAWAEIGRATALAEGTGAAIAPAEGARAFQTLLRYGRAYSGYAPIMGTPWLTAFAQRSRFAEAFHATGQNQPATGKFLAELGSLPREEWPRTVRRLVSDQISLLLRRTIDPDRPLSDYGLDSLGNLELRTRIETETGIRVSPTKITTVRGLAEHVCDELAAAQSAPV

2.3.1.252

DIM/DIP cell wall layer assembly [GO:0071770]; methyl-branched fatty acid biosynthetic process [GO:1902321]; secondary metabolite biosynthetic process [GO:0044550]

plasma membrane [GO:0005886]; polyketide synthase complex [GO:0034081]

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

PF00698;PF08240;PF00107;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF14765;

3.40.47.10;1.10.1200.10;3.30.70.250;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;

SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.

CATALYTIC ACTIVITY: Reaction=3 (S)-methylmalonyl-CoA + a long-chain fatty acyl-CoA + 9 H(+) + holo-[mycolipanoate synthase] + 6 NADPH = 3 CO2 + 4 CoA + 3 H2O + long-chain mycolipanoyl-[mycolipanoate synthase] + 6 NADP(+); Xref=Rhea:RHEA:50344, Rhea:RHEA-COMP:12617, Rhea:RHEA-COMP:12618, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57327, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64479, ChEBI:CHEBI:83139, ChEBI:CHEBI:132361; EC=2.3.1.252; Evidence={ECO:0000305|PubMed:12207710};

PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305|PubMed:12207710}.

FUNCTION: Polyketide synthase involved in the biosynthesis of methyl-branched fatty acids such as mycolipanoic, mycolipenic (phthienoic) and mycolipodienoic acids required for the synthesis of a major class of polyacylated trehaloses. Catalyzes the elongation of CoA esters of long-chain fatty acids by incorporation of three methylmalonyl (but not malonyl) residues, to form trimethyl-branched fatty-acids. {ECO:0000269|PubMed:12207710}.

Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

A0A095AMW7

MLES_LEUME

MNTTGYDILRNPFLNKGTAFSEAERQQLGLTGTLPSQIQTIEEQAEQAYKQFQAKSPLLEKRIFLMNLFNENVTLFYHLMDQHVSEFMPIVYDPVVAESIEQYNEIYTNPQNAAFLSVDRPEDVENALKNAAAGRDIKLVVVTDAEGILGMGDWGVNGVDIAVGKLMVYTAAAGIDPATVLPVSIDAGTNNKELLHNPLYLGNKHERIAGEQYLEFIDKFVTAEQNLFPESLLHWEDFGRSNAQVILDKYKESIATFNDDIQGTGMIVLAGIFGALNISKQKLVDQKFVTFGAGTAGMGIVNQIFSELKQAGLSDDEARNHFYLVDKQGLLFDDTEGLTAAQKPFTRSRKEFVNPEQLINLETIVKELHPTVLIGTSTQPGTFTETIVKSMAENTERPIIFPLSNPTKLAEATAEDLIKWTGGKALVATGIPAADVDYKGVTYKIGQGNNALIYPGLGFGLVASTAKLLTQETISAAIHALGGLVDTDEPGAAVLPPVSNLTDFSQKIAEITAQSVVNQGLNREKIVDPKQAVQDAKWSAEY

4.1.1.101

COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16345941}; COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:16345941};

malate metabolic process [GO:0006108]; malolactic fermentation [GO:0043464]; pyruvate metabolic process [GO:0006090]

cytosol [GO:0005829]

carboxy-lyase activity [GO:0016831]; malate dehydrogenase (decarboxylating) (NAD+) activity [GO:0004471]; malolactic enzyme activity [GO:0043883]; manganese ion binding [GO:0030145]; NAD binding [GO:0051287]

PF00390;PF03949;

3.40.50.10380;3.40.50.720;

Malic enzymes family

CATALYTIC ACTIVITY: Reaction=(S)-malate + H(+) = (S)-lactate + CO2; Xref=Rhea:RHEA:46276, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526, ChEBI:CHEBI:16651; EC=4.1.1.101; Evidence={ECO:0000269|PubMed:16345941};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.043 mM for NAD {ECO:0000269|PubMed:16345941}; KM=16.7 mM for (S)-malate {ECO:0000269|PubMed:16345941};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.35. {ECO:0000269|PubMed:16345941};

FUNCTION: Involved in the malolactic fermentation (MLF) of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. Catalyzes the decarboxylation of L-malate to L-lactate. {ECO:0000269|PubMed:16345941}.

Leuconostoc mesenteroides

A0A095C6S0

OXDA2_CRYD2

MSFDAVVIGSGVIGLSIARELDNRGLKVAMVARDLAEDSLSVGFASPWAGCNWYSFAEGGTPAAEWDAITFSKLAKLAEDHPDLCEKIPFCSVWDLPKSDSESEPWFKDLVFEYKKLKSTPGQHLAGGKKFGYSFKSYVLHAPNYIRHLSSEIRARGIPIHRYRLSSIDEAYNLPGIGKVSLVVNASGLGAKSLIGVEDEKVYSGRGQTVLVRAPGFKACIMHTEGFYADLDESGREITPPPPAYIIPRPGPEGHVVLGGVYQKDNWSTLPDLKEAERILKDCYNLAPELAGPNGKSWKDIEIISHNVGLRPAREGEPRLEIEEREVGTGANGGNGYEVAPKFGCEGERRKVAVVHAYGIGSAGFQASLGMAEKASDLVEKYLSGRRTSAKL

1.4.3.3

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P80324};

aspartate catabolic process [GO:0006533]; cellular detoxification [GO:1990748]; D-amino acid catabolic process [GO:0019478]; nitrogen utilization [GO:0019740]

peroxisomal matrix [GO:0005782]

D-amino-acid oxidase activity [GO:0003884]; D-aspartate oxidase activity [GO:0008445]; FAD binding [GO:0071949]

PF01266;

3.30.9.10;3.40.50.720;

DAMOX/DASOX family

SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P80324}.

CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:26132227}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21817; Evidence={ECO:0000269|PubMed:26132227}; CATALYTIC ACTIVITY: Reaction=D-methionine + H2O + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, ChEBI:CHEBI:28938, ChEBI:CHEBI:57932; Evidence={ECO:0000269|PubMed:26132227}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78208; Evidence={ECO:0000269|PubMed:26132227}; CATALYTIC ACTIVITY: Reaction=D-serine + H2O + O2 = 3-hydroxypyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17180, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; Evidence={ECO:0000269|PubMed:26132227}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70952; Evidence={ECO:0000269|PubMed:26132227}; CATALYTIC ACTIVITY: Reaction=D-histidine + H2O + O2 = 3-(imidazol-5-yl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:78227, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58133, ChEBI:CHEBI:142967; Evidence={ECO:0000269|PubMed:26132227}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78228; Evidence={ECO:0000269|PubMed:26132227}; CATALYTIC ACTIVITY: Reaction=D-proline + O2 = 1-pyrroline-2-carboxylate + H2O2; Xref=Rhea:RHEA:78259, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:39785, ChEBI:CHEBI:57726; Evidence={ECO:0000269|PubMed:26132227}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78260; Evidence={ECO:0000269|PubMed:26132227}; CATALYTIC ACTIVITY: Reaction=D-alanine + H2O + O2 = H2O2 + NH4(+) + pyruvate; Xref=Rhea:RHEA:22688, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57416; Evidence={ECO:0000269|PubMed:26132227}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22689; Evidence={ECO:0000269|PubMed:26132227}; CATALYTIC ACTIVITY: Reaction=D-leucine + H2O + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78211, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:143079; Evidence={ECO:0000269|PubMed:26132227}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78212; Evidence={ECO:0000269|PubMed:26132227}; CATALYTIC ACTIVITY: Reaction=D-valine + H2O + O2 = 3-methyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78203, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:74338; Evidence={ECO:0000269|PubMed:26132227}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78204; Evidence={ECO:0000269|PubMed:26132227};

FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:26132227). Enables the organism to utilize D-amino acids as a source of nutrients (PubMed:26132227). Enables the organism to utilize D-alanine, D-cysteine, D-histidine, D-leucine, D-methionine, D-phenylalanine, D-proline, D-serine, D-threonine, D-aspartate and D-valine as a nitrogen source and may also contribute to utlization of D-tryptophan, D-tyrosine and D-asparagine as a nitrogen source (PubMed:26132227). Protects the organism from the toxicity of D-amino acids, including from D-alanine (PubMed:26132227). May play a role in its interaction with the host (PubMed:26132227). {ECO:0000269|PubMed:26132227}.

Cryptococcus deuterogattii (strain R265) (Cryptococcus gattii VGII (strain R265))

A0A096MJN4

SEPT4_RAT

MIKHFLEDNSDDAELSKFVKDFPGSEPCHPTESKTRVARPQILEPRPQSPDLCDDDVEFRATLWSQPSDSQQYFCPPAPLSPSSRPRSPWGKLDPYDSSEDDKEYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLGAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDAVNNTECWRPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTPSEVDRKKCKIREEIEHFGIKIYQFPDCDSDEDEDFKLQDQALKESIPFAVIGSNTVVEARGRRVRGRLYPWGIVEVENPGHCDFVKLRTMLVRTHMQDLKDVTRETHYENYRAQCIQSMTRLVVKERNRNKLTRESGTDFPIPAVPPGTDPETEKLIREKDEELRRMQEMLHKIQRQMKETH

brain development [GO:0007420]; cytoskeleton-dependent cytokinesis [GO:0061640]; flagellated sperm motility [GO:0030317]; hematopoietic stem cell homeostasis [GO:0061484]; negative regulation of stem cell proliferation [GO:2000647]; neuron migration [GO:0001764]; positive regulation of apoptotic process [GO:0043065]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of protein ubiquitination [GO:0031398]; regulation of exocytosis [GO:0017157]; sperm capacitation [GO:0048240]; sperm mitochondrion organization [GO:0030382]; spermatid development [GO:0007286]; spermatid differentiation [GO:0048515]; tissue morphogenesis [GO:0048729]

axon [GO:0030424]; axon terminus [GO:0043679]; cell division site [GO:0032153]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; microtubule cytoskeleton [GO:0015630]; mitochondrion [GO:0005739]; motile cilium [GO:0031514]; perikaryon [GO:0043204]; septin complex [GO:0031105]; septin ring [GO:0005940]; sperm annulus [GO:0097227]; sperm flagellum [GO:0036126]; synaptic vesicle [GO:0008021]

GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; molecular adaptor activity [GO:0060090]

PF00735;

3.40.50.300;

TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family

PTM: Phosphorylated by DYRK1A. {ECO:0000250|UniProtKB:P28661}.

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28661}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:P28661}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:O43236}. Cell projection, axon {ECO:0000250|UniProtKB:P28661}. Cell projection, dendrite {ECO:0000250|UniProtKB:P28661}. Perikaryon {ECO:0000250|UniProtKB:P28661}. Note=Found in the sperm annulus, a fibrous ring structure connecting the midpiece and the principal piece of the sperm flagellum (By similarity). In platelets, found in areas surrounding alpha-granules (By similarity). Expressed and colocalized with SLC6A3 and SNCA in axon terminals, especially at the varicosities (By similarity). {ECO:0000250|UniProtKB:O43236, ECO:0000250|UniProtKB:P28661}.

FUNCTION: Filament-forming cytoskeletal GTPase. Pro-apoptotic protein involved in LGR5-positive intestinal stem cell and Paneth cell expansion in the intestines, via its interaction with XIAP (By similarity). May also play a role in the regulation of cell fate in the intestine (By similarity). Positive regulator of apoptosis involved in hematopoietic stem cell homeostasis; via its interaction with XIAP (By similarity). Negative regulator of repair and hair follicle regeneration in response to injury, due to inhibition of hair follicle stem cell proliferation, potentially via its interaction with XIAP (By similarity). Plays an important role in male fertility and sperm motility (By similarity). During spermiogenesis, essential for the establishment of the annulus (a fibrous ring structure connecting the midpiece and the principal piece of the sperm flagellum) which is a requisite for the structural and mechanical integrity of the sperm (By similarity). Involved in the migration of cortical neurons and the formation of neuron leading processes during embryonic development (By similarity). Required for dopaminergic metabolism in presynaptic autoreceptors; potentially via activity as a presynaptic scaffold protein (By similarity). {ECO:0000250|UniProtKB:P28661}.

Rattus norvegicus (Rat)

A0A096MJY4

MEF2C_RAT

MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLCAVPPPNFEMPVTIPVSSHNSLVYSNPVSSLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNIQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGACTSTHLSQSSNLSLPSTQSLNIKSEPVSPPRDRTTTPSRYPQHTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT

AMPA selective glutamate receptor signaling pathway [GO:0098990]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; B cell homeostasis [GO:0001782]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853]; blood vessel development [GO:0001568]; blood vessel remodeling [GO:0001974]; cardiac muscle cell differentiation [GO:0055007]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cardiac ventricle formation [GO:0003211]; cartilage morphogenesis [GO:0060536]; cell differentiation [GO:0030154]; cell fate commitment [GO:0045165]; cell morphogenesis involved in neuron differentiation [GO:0048667]; cell proliferation in bone marrow [GO:0071838]; cellular response to calcium ion [GO:0071277]; cellular response to fluid shear stress [GO:0071498]; cellular response to glucose stimulus [GO:0071333]; cellular response to growth factor stimulus [GO:0071363]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to organic cyclic compound [GO:0071407]; cellular response to parathyroid hormone stimulus [GO:0071374]; cellular response to retinoic acid [GO:0071300]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to trichostatin A [GO:0035984]; cellular response to xenobiotic stimulus [GO:0071466]; chondrocyte differentiation [GO:0002062]; dentate gyrus development [GO:0021542]; embryonic heart tube development [GO:0035050]; embryonic skeletal system morphogenesis [GO:0048704]; embryonic viscerocranium morphogenesis [GO:0048703]; endochondral ossification [GO:0001958]; epithelial cell proliferation involved in renal tubule morphogenesis [GO:2001013]; excitatory postsynaptic potential [GO:0060079]; gene expression [GO:0010467]; germinal center formation [GO:0002467]; glomerulus morphogenesis [GO:0072102]; heart development [GO:0007507]; heart looping [GO:0001947]; humoral immune response [GO:0006959]; learning or memory [GO:0007611]; MAPK cascade [GO:0000165]; melanocyte differentiation [GO:0030318]; monocyte differentiation [GO:0030224]; muscle cell fate determination [GO:0007521]; myotube differentiation [GO:0014902]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of gene expression [GO:0010629]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of ossification [GO:0030279]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vascular associated smooth muscle cell migration [GO:1904753]; negative regulation of vascular associated smooth muscle cell proliferation [GO:1904706]; negative regulation of vascular endothelial cell proliferation [GO:1905563]; nephron tubule epithelial cell differentiation [GO:0072160]; neural crest cell differentiation [GO:0014033]; neuron development [GO:0048666]; neuron differentiation [GO:0030182]; neuron migration [GO:0001764]; NMDA selective glutamate receptor signaling pathway [GO:0098989]; osteoblast differentiation [GO:0001649]; outflow tract morphogenesis [GO:0003151]; platelet formation [GO:0030220]; positive regulation of alkaline phosphatase activity [GO:0010694]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of behavioral fear response [GO:2000987]; positive regulation of bone mineralization [GO:0030501]; positive regulation of cardiac muscle cell differentiation [GO:2000727]; positive regulation of cardiac muscle cell proliferation [GO:0060045]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of cell proliferation in bone marrow [GO:0071864]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of macrophage apoptotic process [GO:2000111]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of skeletal muscle cell differentiation [GO:2001016]; positive regulation of skeletal muscle tissue development [GO:0048643]; positive regulation of transcription by RNA polymerase II [GO:0045944]; primary heart field specification [GO:0003138]; regulation of dendritic spine development [GO:0060998]; regulation of DNA-templated transcription [GO:0006355]; regulation of germinal center formation [GO:0002634]; regulation of megakaryocyte differentiation [GO:0045652]; regulation of neuron apoptotic process [GO:0043523]; regulation of neurotransmitter secretion [GO:0046928]; regulation of sarcomere organization [GO:0060297]; regulation of synapse assembly [GO:0051963]; regulation of synaptic activity [GO:0060025]; regulation of synaptic plasticity [GO:0048167]; regulation of synaptic transmission, glutamatergic [GO:0051966]; renal tubule morphogenesis [GO:0061333]; response to ischemia [GO:0002931]; response to nutrient levels [GO:0031667]; response to vitamin E [GO:0033197]; roof of mouth development [GO:0060021]; secondary heart field specification [GO:0003139]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287]; sinoatrial valve morphogenesis [GO:0003185]; skeletal muscle cell differentiation [GO:0035914]; skeletal muscle tissue development [GO:0007519]; smooth muscle cell differentiation [GO:0051145]; sympathetic neuron axon guidance [GO:0097492]; transdifferentiation [GO:0060290]; ventricular cardiac muscle cell differentiation [GO:0055012]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; postsynapse [GO:0098794]; protein-containing complex [GO:0032991]; sarcomere [GO:0030017]; sarcoplasm [GO:0016528]

chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; histone deacetylase binding [GO:0042826]; HMG box domain binding [GO:0071837]; minor groove of adenine-thymine-rich DNA binding [GO:0003680]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976]

PF12347;PF00319;

3.40.1810.10;

MEF2 family

PTM: Phosphorylated on Ser-59; which enhances DNA binding activity. Phosphorylated on Ser-396; which is required for Lys-391 sumoylation and inhibits transcriptional activity. {ECO:0000250}.; PTM: Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation. {ECO:0000250}.; PTM: Sumoylated on Lys-391 with SUMO2 but not SUMO1; which represses transcriptional activity. {ECO:0000250}.; PTM: Proteolytically cleaved in cerebellar granule neurons on several sites by caspase 3 and caspase 7 following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation. {ECO:0000250}.

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15862299}. Cytoplasm, sarcoplasm {ECO:0000269|PubMed:15862299}.

FUNCTION: Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes (PubMed:15862299). Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. May also be involved in neurogenesis and in the development of cortical architecture (By similarity). {ECO:0000250|UniProtKB:Q8CFN5, ECO:0000269|PubMed:15862299}.

Rattus norvegicus (Rat)

A0A096MK47

MLIP_RAT

MTSCVLAGSIETTPKVSPGDSEAKPLIFTFVPTLRRLPTHIQLADTSKFLVKIPEEPTDKNPETVNRFEYSDHMTFSCESKEERDQRILDYPSEVSGKNSQRKEFNTKEPQGMQKGDLFKAEYVFIVDSDGEDEATCRQGEQGPPGATGNIATRPKSLAISSSLASDVVRPKVRGVDVKVSSHPEIPHGIAPQQKHGQLTSPTTSEQLAHKPPAFSFVSPTNQKTPPVPAKVSGTTVLEEFHIRRLDVHGASEEETATYFHTTAHDSPLPAWKGASTLVFSPSAQLPGSSLCGSNVADHTRGLAPEAQKKVSTSSALNPREDVRTSPSPASGASLRSPSASYIPVRIVMHSLSPSPKPLTSSSHGSLSTVCSQTSSSGNLSKSGLKSPVPSRLSLLTAILKSNPSHQRPLSPASCPTFSLNSLASSTLTLDQKIKQTPSTPKKSLSSCSLTTGSTEQEQASAESHQPCHLSFFSKTTPLSQAQPPSPPALASSSYAATDTEKIPGSTLRSSTTPPQSQTDLFSLADVPSVTPGLSPLSSSKGRKDGDLRAPEKNRNICTRPSTLSFIPPINESTALSSSGKCFHPSPALSDLIDRSKRTCSQRHSDQRPNPSALPTPPVSRAGSASHPHLGYSILPPESSLTQALQRSPSALHPSCGSATCPSRTGMPDSTASNRSSRVSTPSLPVSLTRTKELISPCALSMSAGPENKKPKQYKTKSSYKAFAAIPTNTLLLEQKALDEPARTESNSKASVSDLPVELCFPAQLRQQTEELCATIDKVLQDSLSMHSSDSPSRPSQTMLGSETIKTPTTHPRAAGRETKYANLSSSSSTTSESQLTKPGVIRPVPIKSKLFLKKEEEVYEPNPFSKYLEDSSGLFSEQDMAIPHKPVSLHPLYQSKLYPPAKSLLRPQTLSHADCLTPGPFSHLSSFSLRDEQEKSPTLLSQDTYNKPGHPMVTIPEHDTLDSKE

negative regulation of cardiac muscle hypertrophy [GO:0010614]; negative regulation of cardiac muscle hypertrophy in response to stress [GO:1903243]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; transcription by RNA polymerase II [GO:0006366]

cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear lumen [GO:0031981]; nucleus [GO:0005634]; PML body [GO:0016605]; sarcolemma [GO:0042383]

lamin binding [GO:0005521]; transcription corepressor activity [GO:0003714]

PF15274;

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5FW52}. Nucleus envelope {ECO:0000250|UniProtKB:Q5FW52}. Nucleus, PML body {ECO:0000250|UniProtKB:Q5FW52}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5FW52}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q5FW52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5FW52}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5FW52}.

FUNCTION: Required for myoblast differentiation into myotubes, possibly acting as a transcriptional regulator of the myogenic program (By similarity). Required for cardiac adaptation to stress through integrated regulation of the AKT/mTOR pathways and FOXO1. Regulates cardiac homeostasis and plays a role in the protection against cardiac hypertrophy (PubMed:22343712, PubMed:26436652). Binds chromatin (By similarity). May act as a transcriptional cofactor for ISL1, repressing its transcriptional activity (By similarity). May also repress MYOCD transcriptional activity (By similarity). {ECO:0000250|UniProtKB:Q5FW52, ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:26436652}.

Rattus norvegicus (Rat)

A0A096P8D3

IDH_OSTTA

MTRVERGRVLARAIERAVAHRASARRWTTTTRTPAWMVTGWMGGRGVDRSTAMTRFERCGSTASSKITAAPMVYVRGEEMTAYVMDLIRSRWIEPRVDVGGWETFDLRAKNRDDTEDRVLRDVIEAGKRIKAIFKEPTVTPTADQVKRLGLRKSWGSPNGAMRRGWNGITISRDTIHIDGVELGYKKPVLFERHAVGGEYSAGYKNVGKGKLTTTFTPSEGPDAGKTVVVDEREIVDEEAAVVTYHNPYDNVHDLARFFFGRCLEAKVTPYVVTKKTVFKWQEPFWQIMRTVFDEEFKAQFVAAGVMKEGEELVHLLSDAATMKLVQWRQGGFGMAAHNYDGDVLTDELAQVHKSPGFITSNLVGVHEDGTLIKEFEASHGTVADMDEARLRGEETSLNPLGMVEGLIGAMNHAADVHNIDRDRTHAFTTKMRTVIHQLFREGKGTRDLCGPSGLTTEQFIDAVAERLDA

1.1.1.41

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25724193, ECO:0000269|Ref.4}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25724193}; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000269|Ref.4};

isocitrate metabolic process [GO:0006102]; NAD metabolic process [GO:0019674]; NADP metabolic process [GO:0006739]; tricarboxylic acid cycle [GO:0006099]

cytosol [GO:0005829]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]

isocitrate dehydrogenase (NAD+) activity [GO:0004449]; isocitrate dehydrogenase (NADP+) activity [GO:0004450]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]

PF00180;

3.40.718.10;

Isocitrate and isopropylmalate dehydrogenases family

SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH; Xref=Rhea:RHEA:23632, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.41; Evidence={ECO:0000269|PubMed:25724193}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23633; Evidence={ECO:0000269|PubMed:25724193};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=226 uM for NAD(+) with Mg(2+) as cofactor {ECO:0000269|PubMed:25724193}; KM=265 uM for NAD(+) with Mn(2+) as cofactor {ECO:0000269|PubMed:25724193};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 with Mn(2+) as cofactor and 8.5 with Mg(2+) as cofactor. {ECO:0000269|PubMed:25724193};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:25724193};

FUNCTION: Performs an essential role in the oxidative function of the tricarboxylic acid cycle and respiration (Probable). Catalyzes the decarboxylation of isocitrate to produce 2-oxoglutarate and generate NADH to provide electrons for energy production (Probable). {ECO:0000305|PubMed:25724193}.

Ostreococcus tauri

A0A097PTA8

DEFCO_COPCI

MKLSTSLLAIVAVASTFIGNALSATTVPGCFAECIDKAAVAVNCAAGDIDCLQASSQFATIVSECVATSDCTALSPGSASDADSINKTFNILSGLGFIDEADAFSAADVPEERDLTGLGRVLPVEKRQNCPTRRGLCVTSGLTACRNHCRSCHRGDVGCVRCSNAQCTGFLGTTCTCINPCPRC

defense response to bacterium [GO:0042742]

extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218]

lipid binding [GO:0008289]

PF18251;

3.30.30.140;

Invertebrate defensin family

PTM: Contains a unique connectivity of 6 cysteine bonds in contrast to most other CS-alpha-beta defensins which are linked by 3 or 4 disulfide bonds. {ECO:0000305}.; PTM: Disulfide bonds are essential for structural integrity and antibacterial activity, since activity is lost after treatment with reducing agents. Thanks to disulfide bonds and N-terminal pyroglutamate, the protein is extremely stable in a wide pH and temperature range and insensitive toward proteases. {ECO:0000269|PubMed:25342741}.

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25342741, ECO:0000305|PubMed:28825809}. Target cell membrane {ECO:0000269|PubMed:25342741, ECO:0000305|PubMed:28825809}. Note=specific localization at active cell wall synthesis sites. {ECO:0000269|PubMed:25342741}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 1-8. {ECO:0000269|PubMed:25342741};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 4-90 degrees Celsius. {ECO:0000269|PubMed:25342741};

FUNCTION: Antimicrobial peptide that acts against Gram-positive bacteria (Listeria spp., Enterococcus spp., B.subtilis, B.anthracis, P.aeruginosa) (PubMed:25342741, PubMed:28825809). Is not active against Gram-negative bacteria (PubMed:25342741). It selectively inhibits peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio), probably anchoring lipid II to the membrane, thus inhibiting cell wall synthesis (PubMed:25342741, PubMed:28825809). The interaction with lipid II involves the third position of the pentapeptide (PubMed:25342741). Shows bactericidal activity at about 2-fold minimal inhibitory concentrations (MIC), but does not form pore across the membrane (PubMed:25342741). {ECO:0000269|PubMed:25342741, ECO:0000269|PubMed:28825809}.

Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)

A0A0A0LLY1

SRBP1_CUCSA

MASSSVEFRCFVGGLAWATDSNSLEKAFSVYGEIVEAKIVSDRETGRSRGFGFVTFLEEEAMRSAIEAMNGHILDGRNITVNEAQQRGGGGGGGYNRGGGYGGRRDGGGFSRGGGGGYGGGGGGGYGGGRDRGYGGGGGYGGGRDSRGSGGGGSEGGWRN

defense response [GO:0006952]; extracellular transport [GO:0006858]; miRNA transport [GO:1990428]; regulation of defense response to virus [GO:0050688]; regulation of RNA splicing [GO:0043484]; RNA transport [GO:0050658]

cytosol [GO:0005829]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleus [GO:0005634]

miRNA binding [GO:0035198]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; single-stranded RNA binding [GO:0003727]; siRNA binding [GO:0035197]

PF00076;

3.30.70.330;

GR-RBP family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31812689}. Note=Observed in the phloem translocation stream. {ECO:0000269|PubMed:31812689}.

FUNCTION: Possibly has a role in RNA transcription or processing during stress (By similarity). Binds sequence non-specifically to RNAs and DNAs (By similarity). Mediates cell-to-cell trafficking of RNA interference (RNAi) signals (small RNAs (sRNA), e.g. small interfering RNA (siRNA) and microRNA (miRNA)) which regulate growth and development, as well as responses to environmental inputs, including pathogen attack; can compromise zucchini yellow mosaic virus (ZYMV) and tobacco rattle virus (TRV) infections at the early stage (PubMed:31812689). {ECO:0000250|UniProtKB:Q9LIS2, ECO:0000269|PubMed:31812689}.

Cucumis sativus (Cucumber)

A0A0A1C3I2

HMGR1_PANGI

MDVRRRLPPKLRRPLPITESSHHHRKTPFPADVDRSPSPTPKASDALPLPLYLTNGIFFTLFFSVAYYLLHRWRDKIRSSTPLHIVTLSELAAIVSLIASFIYLLGFFGIDFVQSFVSRADVDVDIDVEPDILEADRRPCSKLMDQPPPPPVVMSSEEDEEIVKSVVSGKTPSYSLESKLGDCYRAASIRREAVQRTTGRSLLGLPLDGFDYESILGQCCEMPIGYVQIPVGIAGPLLLNGCEYVVPMATTEGCLVASTNRGCKAIYACGGATGILLKDGMTRAPVVRFSTAKRASDLKFFLEDPLNFDTLAVVFNKSSRFARLQSIQCSMAGKNLYIRFCCSTGDAMGMNMVSKGVQNVLEFLQSDFPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIITDDVVKKVLKTTVPALVELNMLKNLAGSAVAGALGGFNAHAANIVSAVFIATGQDPAQNIESSHCITMMEAINNGKDLHISVTMPSIEVGTVGGGTQLASQSACLNLLGVKGANKESHGSNSRLLATIVAGSVLAGELSLMSAIAAGQLVRSHMKYNRSSRDMSKIGS

1.1.1.34

coenzyme A metabolic process [GO:0015936]; response to absence of light [GO:0009646]; response to jasmonic acid [GO:0009753]; saponin biosynthetic process [GO:0016135]; sterol biosynthetic process [GO:0016126]; triterpenoid biosynthetic process [GO:0016104]

chloroplast membrane [GO:0031969]; endoplasmic reticulum membrane [GO:0005789]; peroxisomal membrane [GO:0005778]

hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420]

PF00368;

1.10.3270.10;3.30.70.420;

HMG-CoA reductase family

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in intracellular vesicles. {ECO:0000269|PubMed:24569845}.

CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000255|PROSITE-ProRule:PRU10003};

PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. {ECO:0000305}.

FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:24569845, PubMed:29378087). Promotes triterpenes accumulation in roots (PubMed:24569845). {ECO:0000250|UniProtKB:P14891, ECO:0000269|PubMed:24569845, ECO:0000303|PubMed:29378087}.

Panax ginseng (Korean ginseng)

A0A0A1C930

HMR2A_PANGI

MDVRRRPVKSLSSAKTATAGEPPKSQQQHPKASDALPLPLYLTNGLFFTMFFSVMYFLLHRWREKIRNSTPLHVVTLSELAALVLLMASVIYLLGFFGIGFVRSVIRPSPDAWDILEDDNAINEEDSRREPCAEAIDCSLPPKPKIVHMVPQKALNPKSAFADMMVEQPALAIAPLTEEDEEIVKSVVTGKIPSYSLESKLGDCKKAASIRREALQRITGKSLAGLPLDGFDYKSILGQCCEMPVGYVQIPVGIAGPLLLNETEYSVPMATTEGCLVASTNRGCKAIYASGGATSVLLRDGMTRAPVVRFSTVKRAAELKFFLEEPLNYDTPAHVFNKSSRFGRLQGIKCAVAGKNLYIRFTCSTGDAMGMNMVSKGVQNVLDFLQSDFPDMDVMGISGNYCSDKKPAAVNWIEGCGKSVVCEAIIKEEVVKKVLKTNVAALVELNMLKNLAGSAVAGALGGFNAHASNIVSAVYISTGQDPAQNVESSHCITMMEAVNNGKDLHISVTMPSIEVGTVGGGTQLASQSACLNLLGVKGASKESPGSNSRLLASIVAGSVLAGELSLMSALAAGQLVKSHMKYNRSSKDITKLSS

1.1.1.34

coenzyme A metabolic process [GO:0015936]; ergosterol biosynthetic process [GO:0006696]; response to jasmonic acid [GO:0009753]; saponin biosynthetic process [GO:0016135]; triterpenoid biosynthetic process [GO:0016104]

chloroplast membrane [GO:0031969]; endoplasmic reticulum membrane [GO:0005789]; peroxisomal membrane [GO:0005778]

hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420]

PF00368;

1.10.3270.10;3.30.70.420;

HMG-CoA reductase family

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000250|UniProtKB:A0A0A1C3I2}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in intracellular vesicles. {ECO:0000269|PubMed:24569845}.

CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000255|PROSITE-ProRule:PRU10003};

PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. {ECO:0000305}.

FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:24569845, PubMed:29378087). {ECO:0000250|UniProtKB:P14891, ECO:0000269|PubMed:24569845, ECO:0000303|PubMed:29378087}.

Panax ginseng (Korean ginseng)

A0A0A1H8I4

AIS_PSESP

MFPRLPTLALGALLLASTPLLAAQPVTTLTVLSSGGIMGTIREVAPAYEKATGVKLDIAAAPSMGDTPQAIPNRLARNEPADVVLMVGSALDKLVASGQVAKDSRVDLGQSFIAMAVRQGAPKPDISNMDAFKQTLEKAQSVAYSDSASGVYLSRILFPRMQLDKSFMAKARMIPAEPVGAVVARGEAQLGFQQLSELKAVPGIDIVGLIPDQAQKMTLYSGAMVSKSQHPEAARALLQYLASKDAAKAIEDSGLKPVPAQP

5.3.3.7

cellular response to calcium ion [GO:0071277]; cellular response to iron ion [GO:0071281]; cellular response to magnesium ion [GO:0071286]; cellular response to manganese ion [GO:0071287]; cellular response to nickel ion [GO:0071289]; cellular response to silver ion [GO:0071292]; response to DDT [GO:0046680]; response to mercury ion [GO:0046689]

outer membrane-bounded periplasmic space [GO:0030288]

aconitate delta-isomerase activity [GO:0047614]

PF13531;

3.40.190.10;

CATALYTIC ACTIVITY: Reaction=trans-aconitate = cis-aconitate; Xref=Rhea:RHEA:17265, ChEBI:CHEBI:15708, ChEBI:CHEBI:16383; EC=5.3.3.7; Evidence={ECO:0000269|PubMed:26293748};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.9 mM for cis-aconitic acid {ECO:0000269|PubMed:26293748}; KM=80 mM for trans-aconitic acid {ECO:0000269|PubMed:26293748}; Note=kcat and kcat/KM are 4500 sec(-1) and 760 sec(-1) mM(-1), respectively for cis-aconitic acid. kcat and kcat/KM are 15000 sec(-1) and 190 sec(-1) mM(-1), respectively for trans-aconitic acid. {ECO:0000269|PubMed:26293748};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:26293748};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:26293748};

FUNCTION: Involved in assimilation of trans-aconitic acid. Preference for cis-aconitic acid is 14-fold higher than for trans-aconitic acid. Not active on intermediates of tricarboxylic acid (TCA) cycle including citric acid, succinic acid, fumaric acid, and 2-oxoglutaric acid or on other dicarboxilic acids including itaconic acid, formic acid, citraconic acid or maleic acid. {ECO:0000269|PubMed:26293748}.

Pseudomonas sp

A0A0A1HA03

708C1_FAGES

MMGDLTTSFPATTLTTNDQPHVVVCSGAGMGHLTPFLNLASALSSAPYNCKVTLLIVIPLITDAESHHISSFFSSHPTIHRLDFHVNLPAPKPNVDPFFLRYKSISDSAHRLPVHLSALSPPISAVFSDFLFTQGLNTTLPHLPNYTFTTTSARFFTLMSYVPHLAKSSSSSPVEIPGLEPFPTDNIPPPFFNPEHIFTSFTISNAKYFSLSKGILVNTFDSFEPETLSALNSGDTLSDLPPVIPIGPLNELEHNKQEELLPWLDQQPEKSVLYVSFGNRTAMSSDQILELGMGLERSDCRFIWVVKTSKIDKDDKSELRKLFGEELYLKLSEKGKLVKWVNQTEILGHTAVGGFLSHCGWNSVMEAARRGVPILAWPQHGDQRENAWVVEKAGLGVWEREWASGIQAAIVEKVKMIMGNNDLRKSAMKVGEEAKRACDVGGSSATALMNIIGSLKR

2.4.1.360

UDP-glucosyltransferase activity [GO:0035251]

PF00201;

3.40.50.2000;

UDP-glycosyltransferase family

CATALYTIC ACTIVITY: Reaction=a 3'-hydro-2'-hydroxy-beta-oxodihydrochalcone + UDP-alpha-D-glucose = a 3'-(beta-D-glucopyranosyl)-2'-hydroxy-beta-oxodihydrochalcone + H(+) + UDP; Xref=Rhea:RHEA:51504, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:142482, ChEBI:CHEBI:142483; EC=2.4.1.360; Evidence={ECO:0000269|PubMed:25142187, ECO:0000269|PubMed:32699169}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51505; Evidence={ECO:0000269|PubMed:25142187, ECO:0000269|PubMed:32699169};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.4 uM for 2-hydroxynaringenin {ECO:0000269|PubMed:25142187}; KM=40 uM for 2-hydroxypinocembrin {ECO:0000269|PubMed:25142187}; KM=36.5 uM for 2-phenyl-2',4',6'-trihydroxyactophenone {ECO:0000269|PubMed:25142187}; KM=3.73 uM for phloretin {ECO:0000269|PubMed:32699169}; KM=14.66 uM for 2',4',6'-trihydroxyacetophenone {ECO:0000269|PubMed:32699169}; KM=58.1 uM for UDP-glucose with 2-hydroxypinocembrin as acceptor {ECO:0000269|PubMed:25142187}; KM=56.95 uM for UDP-glucose with phloretin as acceptor {ECO:0000269|PubMed:32699169}; KM=42.55 uM for UDP-glucose with 2',4',6'-trihydroxyacetophenone as acceptor {ECO:0000269|PubMed:32699169};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:25142187};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45-50 degrees Celsius. {ECO:0000269|PubMed:25142187};

FUNCTION: UDP-glucose-dependent glucosyltransferase catalyzing the C-glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin, 2-hydroxyeriodictyol and 2-hydroxypinocembrin) and phloretin (PubMed:25142187). No activity with flavanones, flavones or flavonols (PubMed:25142187). Exhibits C-glycosylation activity toward 2',4',6'-trihydroxyacetophenone and phloretin using UDP-glucose as sugar donor (PubMed:32699169). Can use UDP-galactose as sugar donor, but catalytic efficiency is 14-fold lower toward UDP-galactose than toward UDP-glucose (PubMed:32699169). {ECO:0000269|PubMed:25142187, ECO:0000269|PubMed:32699169}.

Fagopyrum esculentum (Common buckwheat) (Polygonum fagopyrum)

A0A0A1I6E7

NDB4S_ANDCR

MEIKYLLTVFLVLLIVSDHCQAFLFSLIPHAISGLISAFKGRRKRDLDGQIDRFRNFRKRDAELEELLSKLPIY

defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; killing of cells of another organism [GO:0031640]

extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218]

Non-disulfide-bridged peptide (NDBP) superfamily, Short antimicrobial peptide (group 4) family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25332684}. Target cell membrane {ECO:0000250}. Note=Forms a helical membrane channel in the prey. {ECO:0000250}.

FUNCTION: Has antimicrobial activity against the Gram-positive bacteria S.aureus (MIC=8 uM) and the yeast C.albicans (MIC=16 uM). Causes hemolysis on horse erythrocytes (64 uM for 100% hemolysis). Minimum bactericidal concentrations have also been tested against S.aureus and is four-fold higher (MBC=32 uM). {ECO:0000269|PubMed:25332684}.

Androctonus crassicauda (Arabian fat-tailed scorpion)

A0A0A1I6N9

NDB4T_ANDCR

MEIKYLLTVFLVLLIVSDHCQAFLFSLIPNAISGLLSAFKGRRKRNLDGQIDRFRNFRKRDAELEELLSKLPIY

defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; killing of cells of another organism [GO:0031640]

extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218]

Non-disulfide-bridged peptide (NDBP) superfamily, Short antimicrobial peptide (group 4) family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25332684}. Target cell membrane {ECO:0000250}. Note=Forms a helical membrane channel in the prey. {ECO:0000250}.

FUNCTION: Has antimicrobial activity against the Gram-positive bacteria S.aureus (MIC=8 uM) and the yeast C.albicans (MIC=16 uM). Causes hemolysis on horse erythrocytes (64 uM for 100% hemolysis). Minimum bactericidal concentrations have also been tested against S.aureus and is four-fold higher (MBC=32 uM). {ECO:0000269|PubMed:25332684}.

Androctonus crassicauda (Arabian fat-tailed scorpion)

A0A0A6ZFY4

UGT29_PANGI

MDNQNGRISIALLPFLAHGHISPFFELAKQLAKRNCNVFLCSTPINLSSIKDKDSSASIKLVELHLPSSPDLPPHYHTTNGLPSHLMLPLRNAFETAGPTFSEILKTLNPDLLIYDFNPSWAPEIASSHNIPAVYFLTTAAASSSIGLHAFKNPGEKYPFPDFYDNSNITPEPPSADNMKLLHDFIACFERSCDIILIKSFRELEGKYIDLLSTLSDKTLVPVGPLVQDPMGHNEDPKTEQIINWLDKRAESTVVFVCFGSEYFLSNEELEEVAIGLEISTVNFIWAVRLIEGEKKGILPEGFVQRVGDRGLVVEGWAPQARILGHSSTGGFVSHCGWSSIAESMKFGVPVIAMARHLDQPLNGKLAAEVGVGMEVVRDENGKYKREGIAEVIRKVVVEKSGEVIRRKARELSEKMKEKGEQEIDRALEELVQICKKKKDEQ

2.4.1.365

response to molecule of fungal origin [GO:0002238]; saponin biosynthetic process [GO:0016135]; terpene biosynthetic process [GO:0046246]; terpenoid biosynthetic process [GO:0016114]

UDP-glycosyltransferase activity [GO:0008194]

PF00201;

3.40.50.2000;

UDP-glycosyltransferase family

CATALYTIC ACTIVITY: Reaction=(20S)-ginsenoside F2 + UDP-alpha-D-glucose = (20S)-ginsenoside Rd + H(+) + UDP; Xref=Rhea:RHEA:58004, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:67988, ChEBI:CHEBI:77145; EC=2.4.1.365; Evidence={ECO:0000269|PubMed:25320211}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58005; Evidence={ECO:0000269|PubMed:25320211}; CATALYTIC ACTIVITY: Reaction=(20S)-ginsenoside Rh2 + UDP-alpha-D-glucose = (20S)-ginsenoside Rg3 + H(+) + UDP; Xref=Rhea:RHEA:58000, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:67991, ChEBI:CHEBI:77147; EC=2.4.1.365; Evidence={ECO:0000269|PubMed:25320211, ECO:0000269|PubMed:25769286}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58001; Evidence={ECO:0000269|PubMed:25320211, ECO:0000269|PubMed:25769286};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=149 uM for ginsenoside Rh2 (at pH 8 and 40 degrees Celsius) {ECO:0000269|PubMed:25769286}; KM=311 uM for ginsenoside Rh2 (at pH 7 and 35 degrees Celsius) {ECO:0000269|PubMed:25320211}; KM=188 uM for ginsenoside F2 (at pH 7 and 35 degrees Celsius) {ECO:0000269|PubMed:25320211}; Vmax=25 nmol/min/mg enzyme with ginsenoside Rh2 as substrate (at pH 8 and 40 degrees Celsius) {ECO:0000269|PubMed:25769286}; Note=kcat is 8.6 sec(-1) with ginsenoside Rh2 as substrate (at pH 7 and 35 degrees Celsius). kcat is 0.41 sec(-1) with ginsenoside F2 as substrate (at pH 7 and 35 degrees Celsius) (PubMed:25320211). kcat is 1111 sec(-1) with ginsenoside Rh2 as substrate (at pH 8 and 40 degrees Celsius) (PubMed:25769286). {ECO:0000269|PubMed:25320211, ECO:0000269|PubMed:25769286};

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

FUNCTION: Component of the dammarane-type triterpene saponins (e.g. PPD-type ginsenosides or panaxosides) biosynthetic pathway (PubMed:25320211, PubMed:25769286, PubMed:27746309, PubMed:29378087). Glycosyltransferase that catalyzes the conversion of ginsenoside Rh2 to ginsenoside Rg3 (PubMed:25320211, PubMed:25769286, PubMed:27746309). Triggers the biosynthesis of ginsenoside Rd from ginsenoside F2 (PubMed:25320211). {ECO:0000269|PubMed:25320211, ECO:0000269|PubMed:25769286, ECO:0000269|PubMed:27746309, ECO:0000303|PubMed:29378087}.

Panax ginseng (Korean ginseng)

A0A0A7EPL0

PIAL1_ARATH

MVIPATSRFGFRAEFNTKEFQASCISLANEIDAAIGRNEVPGNIQELALILNNVCRRKCDDYQTRAVVMALMISVKSACQLGWFPERETQELLAIIDLMWNGFSCPENVTSCVNSPVTLISQVIERFYPCVKLGHILVSFEAKPESKMMMKDFHISKKMPHSPKQKVGLFVVRTEDISRSNCIVHPQGVSFLLNGKGIDKRVNISMESGPQLPTNVTALLNLGANLLQAIGCFGGSYLIAIAFMDVIPLPNKPLLKDYVHPEVVGSNSDCDIIEGPSRISLSCPISRTRIKLPVKGHVCKHLQCFDFWNYVNMNTRRPSWRCPHCNQSVCYTDIRVDQKLRKILEEVGRNAADVVISADGTWMVETENDEDVELVPETTHDHGDPNSFINLGPTVKNPARDENEMETSTQVEEHNPCLSEIQGPSNDTHRPASDYTMLNQSHTSTNTLPQLPRTLNAFDGQQFVNLPQVINTRDSPASQALPMTFSPTPSPQDILATNAANFGTSMPAAQSSQFQGSHVTSLGNCEGRTSDLMARWNHIYGRVQTQFPPAPLSHHHYSMQNQSPSPAQQRPVPSYIAHPQTFHVNYGENADQRWMPSSIAHPQTLPVNYGGNTNQRPIPSSIAHPQTLPVNYRGNTDHRSTPYSITHLQTLLNYGGNADQRPMPSSITNLQTLPATYGGYAHQRPMSSSITHPRTSPVNYGGTPDQRPMPSSITHPQTLPVSYGGTTDQILNPGGAMGQFSSREFMNLTPANTENWRPQSRMRGSVAPGTGYDHMIIHPTRPVHPQAQTPPAPLSTSYDGADEIQAFIGHPSYPVSNNETQAGTSSLPVAEGLGYSGSFWSMPPETW

2.3.2.-

positive regulation of sulfur metabolic process [GO:0051176]; protein sumoylation [GO:0016925]; regulation of gene silencing by regulatory ncRNA [GO:0060966]; response to abscisic acid [GO:0009737]; response to osmotic stress [GO:0006970]; response to salt stress [GO:0009651]

nucleus [GO:0005634]

ligase activity [GO:0016874]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; zinc ion binding [GO:0008270]

PF02891;

3.30.40.10;

PIAL protein ligase family

SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.

PATHWAY: Protein modification; protein sumoylation. {ECO:0000269|PubMed:25415977}.

FUNCTION: Together with MOM1 and PIAL2, regulates transcriptional gene silencing (TGS) independently of changes in DNA methylation (PubMed:27113777). E4-type SUMO ligase that promotes SUMO chain formation in a SCE1-dependent manner and thus contributes to a pathway for proteolytic removal of sumoylation substrates (PubMed:25415977). Involved in stress responses (e.g. osmotic, salt and abscisic acid ABA) and sulfur metabolism (PubMed:25415977). {ECO:0000269|PubMed:25415977, ECO:0000269|PubMed:27113777}.

Arabidopsis thaliana (Mouse-ear cress)

A0A0A7EQR3

GCE_CERUI

MFKPSFVALALVSYATAQASAPQWGQCGGIGWTGPTACPSGWACQQLNAYYSQCLQGAAPAPARTTAAPPPPPATTAAPPPPTTSAPTGSSPVAGACGAIASTVPNYNNAKLPDPFTFANGTALRTKADWSCRRAEISALIQNYEAGTLPPKPPVVTASFSKSGNTGTLAITAGLSNSQTIKFSPTISYPSGTPPANGWPLIIAYEGGSIPIPAGVATLTYSNSDMAQQNSASSRGQGLFYQLYGSTHSASAMTAWVWGVSRIIDALEMTPTAQINTQRIGVTGCSRDGKGALMAGAFEERIALTIPQESGSGGDACWRLSKYEIDNGNQVQDAVEIVGENVWFSTNFNNYVQKLPTVPEDHHLLAAMVAPRAMISFENTDYLWLSPMSSFGCMTAAHTVWQGLGIADSHGFAQVGGHAHCAWPSSLTPQLNAFINRFLLDQSATTNVFTTNNQFGKVQWNAANWITWTTPTLT

3.1.1.117

carbohydrate metabolic process [GO:0005975]; lignin catabolic process [GO:0046274]

extracellular region [GO:0005576]

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

PF00734;

3.40.50.1820;

Carbohydrate esterase 15 (CE15) family

PTM: N-glycosylated (PubMed:25425346). {ECO:0000269|PubMed:25425346}.

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25425346}.

CATALYTIC ACTIVITY: Reaction=a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-O-methyl-alpha-D-glucuronate derivative + an alcohol + H(+); Xref=Rhea:RHEA:67452, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:171667, ChEBI:CHEBI:171668; EC=3.1.1.117; Evidence={ECO:0000269|PubMed:25425346, ECO:0000269|PubMed:26712478}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453; Evidence={ECO:0000305|PubMed:25425346, ECO:0000305|PubMed:26712478};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.6 mM for benzyl (methyl 4-O-methyl-alpha-D-glucopyranoside) uronate {ECO:0000269|PubMed:25425346}; KM=80 mM for benzyl (methyl alpha-D-glucopyranoside) uronate {ECO:0000269|PubMed:25425346}; KM=55 mM for phenylpropyl (methyl alpha-D-glucopyranoside) uronate {ECO:0000269|PubMed:25425346}; KM=8.9 mM for phenyl (methyl alpha-D-glucopyranoside) uronate {ECO:0000269|PubMed:25425346}; KM=4.6 mM for threo-l-[4-(benzyloxy)-3-methoxyphenyl]-3-hydroxy-2- (2-methoxyphenoxy) propyl (methyl 4-O-methyl-alpha-D-glucopyranosid) uronate {ECO:0000269|PubMed:26712478};

FUNCTION: Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin (PubMed:25425346, PubMed:26712478). {ECO:0000269|PubMed:25425346, ECO:0000269|PubMed:26712478}.

Cerrena unicolor (Canker rot fungus) (Daedalea unicolor)

A0A0A7GEY4

GGPPS_GEOAI

MISEIIKDRAKLVNEKIEELLKEQEPEGLYRAARHYLKAGGKRLRPVITLLSAEALGEDYRKAIHAAIAIETVHNFTLVHDDIMDEDEMRRGVKTVHTLFGIPTAILAGDTLYAEAFEILSMSDAPPENIVRAVSKLARVCVEICEGQFMDMSFEERDSVGESEYLEMVRKKTGVLIGISASIPAVLFGKDESVEKALWNYGIYSGIGFQIHDDLLDISGKGKIGKDWGSDILEGKKTLIVIKAFEEGIELETFGKGRASEEELERDIKKLFDCGAVDYARERAREYIEMAKKNLEVIDESPSRNYLVELADYLIERDH

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};

farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744]

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:0000269|PubMed:30062607}; 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:0000269|PubMed:30062607}; 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:0000269|PubMed:30062607};

PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000305}.; PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000305}.; PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000305}.

FUNCTION: Catalyzes the addition of 3 molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranylgeranyl pyrophosphate (GGPP). Catalyzes the synthesis of geranylgeranyl pyrophosphate as a major product and of farnesyl pyrophosphate in smaller amounts. {ECO:0000269|PubMed:30062607}.

Geoglobus acetivorans

A0A0A7HFE1

CAS10_STRTR

MKKEKIDLFYGALLHDIGKVIQRATGERKKHALVGADWFDEIADNQVISDQIRYHMANYQSDKLGNDHLAYITYIADNIASGVDRRQSNEESDEDASAKIWDTYTNQADIFNVFGAQTDKRYFKPTVLNLKSKPNFASATYEPFSKGDYAAIATRIKNELAEFEFNQAQIDSLLNLFEAILSFVPSSTNSKEIADISLAEHSRLTAAFALAIYDYLEDKGRHNYKEDLFTKASAFYEEEAFLLASFDLSGIQDFIYNIATSGAAKQLKARSLYLDFMSEYIADSLLDKLGLNRANLLYVGGGHAYFVLANTEKTVETLVQFEKDFNQFLLANFQTRLYVAFGWGSFAAKDIMSELNSPESYRQIYQKASRMISEKKISRYDYRTLMLLNRGGKSSERECEICHSVENLVSYHDQKVCDICRGLYQFSKEIAHDHFIITENEGLPIGPNACLKGVAFEKLSQESFSRVYVKNDYKAGTIKATHVFVGDYQCDEIHKYAALSKNEDGLGIKRLAVVRLDVDDLGAAFMAGFSRQGNGQYSTLSRSATFSRSMSLFFKVYINQFASDKKLSIIYAGGDDVFAIGSWQDIIAFTVELRQNFIKWTNGKLTLSAGIGLFADKTPISLMAHQTGELEEAAKGNEKDSISLFSSDYTFKFDRFITNVYDDKLEQIRYFFNHQDERGKNFIYKLIELLRNYESEEKMNVARLAYYLTRLEELTDKDERDKFKQFKKLFFKWYTNNESDRKEAELALLLYVYEIRKD

2.7.7.-; 3.1.-.-

COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:27105119, ECO:0000269|PubMed:28663439}; Note=Degradation of ssDNA requires Mn(2+), Co(2+) or Ni(2+); Mg(2+), Ca(2+) or Zn(2+) do not activate ssDNase activity (PubMed:27105119). Formation of cOA requires Mn(2+), Co(2+) or Zn(2+), Mg(2+) is not as efficient (PubMed:28663439). {ECO:0000269|PubMed:27105119, ECO:0000269|PubMed:28663439};

defense response to virus [GO:0051607]

ATP binding [GO:0005524]; endonuclease activity [GO:0004519]; exonuclease activity [GO:0004527]; RNA binding [GO:0003723]; transferase activity [GO:0016740]

PF20824;PF18211;PF01966;

3.30.70.270;1.10.3210.10;

CRISPR-associated Cas10/Csm1 family

CATALYTIC ACTIVITY: Reaction=6 ATP = cyclic hexaadenylate + 6 diphosphate; Xref=Rhea:RHEA:58276, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:142456; Evidence={ECO:0000269|PubMed:28663439};

FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities. In a heterologous host this Csm effector complex restricts ssRNA phage MS2, suggesting it may target RNA viruses in vivo. {ECO:0000269|PubMed:25458845}.; FUNCTION: Csm functions as a non-specific ssDNase. Base-pairing between crRNA and target RNA to form a ternary Csm complex activates a ssDNase activity; target RNA cleavage suppresses the ssDNase, a temporal control that prevents uncontrolled DNA degradation. Viral RNA transcripts probably tether the Csm complex to the viral genome, recruiting Cas10 ssDNA activity which is able to degrade DNA in the transcription bubble, spatially controlling the DNase activity. {ECO:0000269|PubMed:27105119}.; FUNCTION: This subunit has a weak ssDNase activity that is dramatically activated by the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA). Target RNA and ssDNA are cleaved simultaneously, although RNase activity (of Csm3) is much faster. RNA cleavage by Csm3 is not required for ssDNase activity as Csm complex with inactive Csm3 still has ssDNase activity; however as the cleaved target RNA products dissociate away ssDNase activity decreases. Self-recognition, with subsequent repression of the ssDNase activity, occurs when the 5' handle of the crRNA bases pairs with the 3' flanking sequence of the target RNA (which would occur if the CRISPR locus were transcribed as an anti-pre-crRNA). This protein has low activity on dsDNA which is not stimulated by the Csm complex. {ECO:0000269|PubMed:27105119}.; FUNCTION: This subunit is a single-strand-specific deoxyribonuclease (ssDNase) which digests both linear and circular ssDNA; it has both exo- and endonuclease activity. {ECO:0000250|UniProtKB:B6YWB8}.; FUNCTION: When associated with the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic oligoadenylates (cOA) from ATP, producing cyclic triadenylate (cA3) up to cyclic hexaadenylate (cA6), which is the active cOA. The enzyme is also able to cyclize pppA3 up to pppA6. cOAs are second messengers that induce an antiviral state important for defense against invading nucleic acids. Synthesis of cOA can occur with AMP plus ATP, 2'dATP or 3'dATP (but no other nucleotides), and requires a free 3'-OH ribose moiety. {ECO:0000269|PubMed:28663439}.

Streptococcus thermophilus

A0A0A7HIF0

CSM3_STRTR

MTFAKIKFSAQIRLETGLHIGGSDAFAAIGAIDSPVIKDPITNIPIIPGSSLKGKMRTLLAKVYNEKVAEKPSDDSDILSRLFGNSKDKRFKMGRLIFRDAFLSNADELDSLGVRSYTEVKFENTIDRITAEANPRQIERAIRNSTFDFELIYEITDENENQVEEDFKVIRDGLKLLELDYLGGSGSRGYGKVAFEKLKATTVFGNYDVKTLNELLTAEV

3.1.-.-

COFACTOR: Name=a metal cation; Xref=ChEBI:CHEBI:25213; Evidence={ECO:0000269|PubMed:25458845}; Note=Endonucleolytic cleavage of target ssRNA by the Csm complex requires a divalent metal ion; Mg(2+) has the best activity in vitro, but Mn(2+), Ca(2+), Zn(2+), Ni(2+), and Co(2+) also support cleavage. {ECO:0000269|PubMed:25458845, ECO:0000305|PubMed:27105119};

defense response to virus [GO:0051607]

endonuclease activity [GO:0004519]; RNA binding [GO:0003723]

PF03787;

CRISPR-associated Csm3 family

FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities. In a heterologous host this Csm effector complex restricts ssRNA phage MS2, suggesting it may target RNA viruses in vivo. {ECO:0000269|PubMed:25458845}.; FUNCTION: Csm functions as a non-specific ssDNase. Base-pairing between crRNA and target RNA to form a ternary Csm complex activates a ssDNase activity; target RNA cleavage suppresses the ssDNase, a temporal control that prevents uncontrolled DNA degradation. Viral RNA transcripts probably tether the Csm complex to the viral genome, recruiting Cas10 ssDNA activity which is able to degrade DNA in the transcription bubble, spatially controlling the DNase activity. {ECO:0000269|PubMed:27105119}.; FUNCTION: This subunit has the target ssRNA endonuclease activity; it cleaves multiple sites in the target RNA at 6 nucleotide intervals. The number of cleavage sites in the target RNA correlates with the number of Csm3 subunits in the Csm effector complex (PubMed:25458845). In the Csm complex target RNA and ssDNA are cleaved simultaneously, although RNase activity (of Csm3) is much faster. RNA cleavage by Csm3 is not required for ssDNase activity as Csm complex with inactive Csm3 still has ssDNase activity; however as the cleaved target RNA products dissociate away ssDNase activity decreases (PubMed:27105119). {ECO:0000269|PubMed:25458845, ECO:0000269|PubMed:27105119}.

Streptococcus thermophilus

A0A0A7HIX6

CSM6A_STRTR

MKILISAVGTTDPISNNHDAALLHIARNYRPDKIVLVYSQEMMVKQDLINKVLLSIEGYNPIIEIDSTILNNDEVFLFDKMYEVMGQIVQKYTNDDNEIILNLSSGTPQIISALFALNRINDYNTQAIQVATPKNRANREYTALTESEIDALIMENQDNRLDFVDRSIKDKSEKFTQALVKRHLRSLIASFDYQAAEAIINRKEYNKLLSKKKIAYIREKLYDFSRVFKNQSILSDILSFPLDDSQKKALNYYLMIDVLKEREHIADVLIKAKSLAEFVIEETIKKDHEGLIVFDGNLPKLNPSFPDCEAILDDIDKKMKKSRGIEDTEERIFSVQSTLNLLSYLNILEFYEYDSQLQTAINGILSLNGERNKVAHGLSEIDTRLLSRKKLKQLSENLRLLLVDCLGIDSSYFNYYDKQNKELIKMLE

3.1.-.-

defense response to virus [GO:0051607]

endonuclease activity [GO:0004519]; nucleotide binding [GO:0000166]; RNA binding [GO:0003723]

PF09659;

3.40.50.10770;

CRISPR-associated Csm6 family

FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities. In a heterologous host this Csm effector complex restricts ssRNA phage MS2, suggesting it may target RNA viruses in vivo. This protein is not part of the Csm complex. {ECO:0000269|PubMed:25458845}.; FUNCTION: Csm functions as a non-specific ssDNase. Base-pairing between crRNA and target RNA to form a ternary Csm complex activates a ssDNase activity; target RNA cleavage suppresses the ssDNase, a temporal control that prevents uncontrolled DNA degradation. Viral RNA transcripts probably tether the Csm complex to the viral genome, recruiting Cas10 ssDNA activity which is able to degrade DNA in the transcription bubble, spatially controlling the DNase activity. {ECO:0000269|PubMed:27105119}.; FUNCTION: A single-strand-specific endoribonuclease (ssRNase) that is approximately 1000-fold stimulated by cyclic oligoadenylate (cOA); although several species of cOA are synthesized by this organism only cyclic hexaadenylate (cA6) stimulates the ssRNase activity. Cleaves preferentially within GA or AA dinucleotides, although the presence of cA6 broadens the preference. Linear oligoadenylates do not activate the RNase. {ECO:0000269|PubMed:28663439}.

Streptococcus thermophilus

A0A0B0QJR1

HEPT_APHF2

MTNIEPVIIETRLELIGRYLDHLKKFENISLDDYLSSFEQQLITERLLQLITQAAIDINDHILSKLKSGKSYTNFEAFIELGKYQILTPELAKQIAPSSGLRNRLVHEYDDIDPNQVFMAISFALQQYPLYVRQINSYLITLEEEND

3.1.27.-

toxin-antitoxin complex [GO:0110001]

endonuclease activity [GO:0004519]; nucleotide binding [GO:0000166]; RNA nuclease activity [GO:0004540]

PF01934;

1.20.120.580;

HepT RNase toxin family

PTM: Di-AMPylated by cognate antitoxin MntA on Tyr-109 when both are expressed in E.coli; GMPylation occurs much less often. Leads to an increase of mass of 659 Da. Di-AMPylation moves the catalytic His-107 away from the catalytic center, leading to loss of nuclease activity and thus toxicity. Probably one subunit of the dimer is di-AMPylated, the complex dissociates and then reassociates to di-AMPylate the other HepT subunit. {ECO:0000269|PubMed:33290744}.

CATALYTIC ACTIVITY: Reaction=(tRNA)-3'-end (ribonucleoside 5'-phosphate)-(guanosyl 5'-phosphate)-(cytosyl 5'-phosphate)-(cytosyl 5'-phosphate)-(adenosine 5'-phosphate) + H2O = GpCpCpA + H(+) + tRNA 3'-end (ribonucleotide 3'-phosphate); Xref=Rhea:RHEA:66608, Rhea:RHEA-COMP:17075, Rhea:RHEA-COMP:17076, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:167197, ChEBI:CHEBI:167198; Evidence={ECO:0000269|PubMed:33290744};

FUNCTION: Toxic component of a type VII toxin-antitoxin (TA) system. Upon cloning in E.coli inhibits cell growth for several hours; eventually cells recover and start growing. Cleaves the last 4 nucleotides from the tRNA acceptor stem (shown in vitro with E.coli tRNA-Glu(UUC)); only cleaves intact tRNA. Has no activity on mRNA. Neutralized by coexpression with cognate antitoxin MntA, which is due to di-AMPylation of the RNase. {ECO:0000269|PubMed:33290744}.

Aphanizomenon flos-aquae (strain 2012/KM1/D3)

A0A0B4J1F4

ARRD4_MOUSE

MGGEAGADGPRGRVKSLGLVFEDESKGCYSSGETVAGHVLLEAAEPVALRGLRLEAQGRATSAWGPSAGARVCIGGGSPAASSEVEYLNLRLSLLEAPAGEGVTLLQPGKHEFPFRFQLPSEPLATSFTGKYGSIQYCVRAVLERPQVPDQSVRRELQVVSHVDVNTPPLLTPMLKTQEKMVGCWLFTSGPVSLSVKIERKGYCNGEAIPIYAEIENCSSRLVVPKAAIFQTQTYLASGKTKTVRHMVANVRGNHIGSGSTDTWNGKMLKIPPVTPSILDCCIIRVDYSLAVYIHIPGAKRLMLELPLVIGTIPYSGFGRRNSSVASQFSMDMCWLALALPEQPEAPPNYADVVSEEEFSRHVPPYPQPSDCDGEACYSMFACIQEFRFQPPPLYSEVDPHPGDAQETQPVSFIL

extracellular vesicle biogenesis [GO:0140112]; positive regulation of interferon-beta production [GO:0032728]; protein K63-linked ubiquitination [GO:0070534]; protein transport [GO:0015031]; protein ubiquitination [GO:0016567]

cytoplasm [GO:0005737]; early endosome [GO:0005769]; endosome [GO:0005768]; extracellular vesicle [GO:1903561]; plasma membrane [GO:0005886]

ubiquitin ligase-substrate adaptor activity [GO:1990756]

PF02752;PF00339;

2.60.40.640;

Arrestin family

SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:19605364}. Cell membrane {ECO:0000269|PubMed:19605364, ECO:0000269|PubMed:27462458}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle {ECO:0000269|PubMed:19605364}. Note=Also found in extracellular vesicles different from exosomes. {ECO:0000269|PubMed:27462458}.

FUNCTION: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates (PubMed:27462458). Plays a role in endocytosis of activated G protein-coupled receptors (GPCRs) (By similarity). Through an ubiquitination-dependent mechanism also plays a role in the incorporation of SLC11A2 into extracellular vesicles (PubMed:27462458). May play a role in glucose uptake (By similarity). Participates in innate immune response by promoting IFIH1/MDA5 activation through interaction with TRIM65 (By similarity). {ECO:0000250|UniProtKB:Q8NCT1, ECO:0000269|PubMed:27462458}.

Mus musculus (Mouse)

A0A0B4J1G0

FCG3A_MOUSE

MWQLLLPTALVLTAFSGIQAGLQKAVVNLDPKWVRVLEEDSVTLRCQGTFSPEDNSIKWFHNESLIPHQDANYVIQSARVKDSGMYRCQTALSTISDPVQLEVHMGWLLLQTTKWLFQEGDPIHLRCHSWQNRPVRKVTYLQNGKGKKYFHENSELLIPKATHNDSGSYFCRGLIGHNNKSSASFRISLGDPGSPSMFPPWHQITFCLLIGLLFAIDTVLYFSVRRGLQSPVADYEEPKIQWSKEPQDK

antibody-dependent cellular cytotoxicity [GO:0001788]; cell surface receptor signaling pathway [GO:0007166]; cellular response to lipopolysaccharide [GO:0071222]; dendritic cell antigen processing and presentation [GO:0002468]; Fc receptor-mediated immune complex endocytosis [GO:0160006]; natural killer cell degranulation [GO:0043320]; neutrophil activation [GO:0042119]; positive regulation of bone resorption [GO:0045780]

cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]

IgE binding [GO:0019863]; IgE receptor activity [GO:0019767]; IgG binding [GO:0019864]; IgG receptor activity [GO:0019770]; immune receptor activity [GO:0140375]

PF13895;PF13927;

2.60.40.10;

PTM: N-glycosylated. {ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:18949059}.; PTM: Phosphorylated following receptor ligation. {ECO:0000269|PubMed:17558411}.

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411, ECO:0000269|PubMed:28389502}; Single-pass type I membrane protein {ECO:0000255}.

FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG) (PubMed:16039578). Binds with intermediate affinity to both IgG2a and IgG2b (PubMed:16039578, PubMed:17558411, PubMed:19795417). Can bind to IgG2a and IgG2b monomers (PubMed:18949059). Does not display binding to IgG1 or IgG3 (PubMed:16039578). Recognizes neutralizing virus-specific IgGs displayed on the cell surface of infected cells and triggers antibody-dependent cellular cytotoxicity (ADCC). Confers protection to lethal influenza virus infection (PubMed:24412922). On splenic dendritic cells, uptakes antigen immune complexes and efficiently divert them into MHC class I and II antigen presentation pathways to provide for superior priming of CD4-positive and CD8-positive T cell immune responses (PubMed:28389502). Mediates neutrophil activation by IgG complexes redundantly with FCGR2A (PubMed:18097064). Plays a role in promoting bone resorption by enhancing osteoclast differentiation following binding to IgG2a (PubMed:25824719). Also acts as a receptor for the Fc region of immunoglobulin epsilon (IgE) (PubMed:17558411, PubMed:18949059). Binds with low affinity to both the a and b allotypes of IgE (PubMed:18949059). Has also been shown to bind to IgE allotype a only but not to allotype b (PubMed:17558411). Binds aggregated IgE but not the monomeric form and bound monomeric IgG is readily displaced by IgE complexes (PubMed:18949059). Binding to IgE promotes macrophage-mediated phagocytosis, antigen presentation to T cells, production of pro-inflammatory cytokines and the late phase of cutaneous allergic reactions (PubMed:17558411, PubMed:18949059). Mediates enhanced ADCC in response to afucosylated IgGs (PubMed:34485821). {ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411, ECO:0000269|PubMed:18097064, ECO:0000269|PubMed:18949059, ECO:0000269|PubMed:19795417, ECO:0000269|PubMed:24412922, ECO:0000269|PubMed:25824719, ECO:0000269|PubMed:28389502, ECO:0000269|PubMed:34485821}.

Mus musculus (Mouse)

A0A0B4J1N3

GP15L_MOUSE

MRLLALSGLLCMLLLCFCIFSSEGRRHPAKSLKLRRCCHLSPRSKLTTWKGNHTRPCRLCRNKLPVKSWVVPGALPQI

defense response to fungus [GO:0050832]; defense response to Gram-positive bacterium [GO:0050830]; G protein-coupled receptor signaling pathway [GO:0007186]; lymphocyte chemotaxis [GO:0048247]; mast cell degranulation [GO:0043303]; negative regulation of cell cycle G1/S phase transition [GO:1902807]; negative regulation of cell division [GO:0051782]; regulation of keratinocyte proliferation [GO:0010837]; regulation of T cell migration [GO:2000404]; T cell homeostasis [GO:0043029]

extracellular space [GO:0005615]

chemokine activity [GO:0008009]; G protein-coupled receptor binding [GO:0001664]; receptor ligand activity [GO:0048018]

PF15854;

SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6UWK7}.

FUNCTION: Highly cationic protein that has multiple functions. Acts as a chemotactic factor that mediates lymphocytes recruitment to epithelia through binding and activation of the G-protein coupled receptor GPR15 (PubMed:28900043, PubMed:28936214). May be a tumor suppressor; together with SUSD2 has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest (By similarity). May regulate keratinocyte proliferation. In addition, through activation of Mas-related G protein-coupled receptors (MRGPRs) contributes to pruritogenesis by activating itch-selective sensory neurons and mast cells degranulation (PubMed:35704588). {ECO:0000250|UniProtKB:Q6UWK7, ECO:0000269|PubMed:28900043, ECO:0000269|PubMed:28936214, ECO:0000269|PubMed:35704588}.; FUNCTION: Has antimicrobial activity against Gram-positive bacteria, including Staphylococcus aureus and Actinomyces spec., and Mycoplasma hominis and lentivirus. {ECO:0000250|UniProtKB:Q6UWK7}.

Mus musculus (Mouse)

A0A0B4J2F0

PIOS1_HUMAN

MFRRLTFAQLLFATVLGIAGGVYIFQPVFEQYAKDQKELKEKMQLVQESEEKKS

regulation of endoplasmic reticulum unfolded protein response [GO:1900101]; response to unfolded protein [GO:0006986]

mitochondrial outer membrane [GO:0005741]

SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:31653868}; Single-pass membrane protein {ECO:0000255}.

FUNCTION: Plays a role in regulation of the unfolded protein response triggered by endoplasmic reticulum (ER) stress resulting from the presence of unfolded proteins in the ER lumen. {ECO:0000269|PubMed:31653868}.

Homo sapiens (Human)

A0A0B4J2F2

SIK1B_HUMAN

MVIMSEFSADPAGQGQGQQKPLRVGFYDIERTLGKGNFAVVKLARHRVTKTQVAIKIIDKTRLDSSNLEKIYREVQLMKLLNHPHIIKLYQVMETKDMLYIVTEFAKNGEMFDYLTSNGHLSENEARKKFWQILSAVEYCHDHHIVHRDLKTENLLLDGNMDIKLADFGFGNFYKSGEPLSTWCGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGSLPFDGPNLPTLRQRVLEGRFRIPFFMSQDCESLIRRMLVVDPARRITIAQIRQHRWMRAEPCLPGPACPAFSAHSYTSNLGDYDEQALGIMQTLGVDRQRTVESLQNSSYNHFAAIYYLLLERLKEYRNAQCARPGPARQPRPRSSDLSGLEVPQEGLSTDPFRPALLCPQPQTLVQSVLQAEMDCELQSSLQWPLFFPVDASCSGVFRPRPVSPSSLLDTAISEEARQGPGLEEEQDTQESLPSSTGRRHTLAEVSTRLSPLTAPCIVVSPSTTASPAEGTSSDSCLTFSASKSPAGLSGTPATQGLLGACSPVRLASPFLGSQSATPVLQAQGGLGGAVLLPVSFQEGRRASDTSLTQGLKAFRQQLRKTTRTKGFLGLNKIKGLARQVCQVPASRASRGGLSPFHAPAQSPGLHGGAAGSREGWSLLEEVLEQQRLLQLQHHPAAAPGCSQAPQPAPAPFVIAPCDGPGAAPLPSTLLTSGLPLLPPPLLQTGASPVASAAQLLDTHLHIGTGPTALPAVPPPRLARLAPGCEPLGLLQGDCEMEDLMPCSLGTFVLVQ

2.7.11.1

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

intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]

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

ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]

PF00069;

1.10.510.10;

Protein kinase superfamily, CAMK Ser/Thr protein kinase family, AMPK subfamily

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:0000250|UniProtKB:P57059}; 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:0000250|UniProtKB:P57059};

FUNCTION: Probable serine/threonine-protein kinase. {ECO:0000250|UniProtKB:P57059}.

Homo sapiens (Human)

A0A0B4K692

NEP2_DROME

MQTVIQNPNWWRRRNKLEKSLLVSLGIMFVVLATGFGLWIGKVLRTSPPSNPQATALHGDSTTINQVPTGTASKGKSGDSGDVCLTQECIHTASTVLRKMKPEVEPCDNFYEFACGTYLEEENIPDDKVSISTFSVISDKLQEQLKDIITAERPETEPKHFRLPNLLYKACMNKTLIETLGPEPITRVAERLGGWPLIKGDSWNADDSWTWQEQVKKFRTAGFSMDYIIDFSIGVDLQNSTKRLIDLDQSSLALSREYLVKGFNETLVTAYYKYMVDIAVLFGANRDLAKTELLLSLEFEMALANISWPNEKRRNSSELYNLRTPAQLQAAYPYVQWVDYMNALLPEGLNVAEDEMINLSVPSFFEDLGKLLAKTPKRVIANYMFWRIHGFSVGFLSEEFRKRQLQYATALSGRQEQEARWKECVDIATSSMDEVCEDDFDSLGISVGSLYVGKHFHKDSKANALEMVNEIRNVFNDILDEVNWMDAKTKKEAKLKLHSMATHIGYPDEMLDNEKLAAYYAKLDIDPDKYFESFLGMNIFGTDYSFNKLRLPVNKTDWVRHARPAIVNAFYSSLENSIQFPAGILQGHFFNAQRPKYMNFGAIGYVIGHEITHGFDDQGRQFDVKGNLRDWWHPDTQKAYLAKAKCIIEQYGNYTERATGLNLNGINTQGENIADNGGVKESYIAYRRWAEKHGPEAKLPGLDYTPEQMFWVAAGQTWCAKYRKESLKMRITTGVHSPSEFRVLGSLSNMKDFAKDFHCPEGSPMNPVQKCEVW

3.4.24.11

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P08473}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08473};

protein processing [GO:0016485]; proteolysis [GO:0006508]; sperm competition [GO:0046692]

extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]

endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]

PF01431;PF05649;

3.40.390.10;1.10.1380.10;

Peptidase M13 family

PTM: N-glycosylated. {ECO:0000269|PubMed:17157960}.; PTM: The soluble form is probably produced by proteolytic cleavage. {ECO:0000305|PubMed:15554877, ECO:0000305|PubMed:17157960}.

SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960}. Note=A secreted form exists that is probably produced by proteolytic cleavage (Probable). In embryos, adult Malpighian tubules and testes, detected in the soluble fraction but is not detected in the membrane fraction (PubMed:15554877, PubMed:17157960). {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960, ECO:0000305|PubMed:15554877, ECO:0000305|PubMed:17157960}.

CATALYTIC ACTIVITY: Reaction=Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.; EC=3.4.24.11; Evidence={ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-7.5 at 35 degrees Celsius. {ECO:0000269|PubMed:17157960};

FUNCTION: Metalloendoprotease which cleaves peptides such as tachykinin peptide TK-2 at the amino side of hydrophobic residues (PubMed:15554877, PubMed:17157960). Functions in female fertility, embryogenesis and memory formation (PubMed:24395329, PubMed:27629706). Required in females for normal patterns of egg laying, probably due to its function in sperm retention and preventing sperm displacement by rival ejaculates (PubMed:24395329). Also required for normal patterns of hatching due to its important role in early embryonic development (PubMed:24395329). Required in the dorsal paired medial neurons for the proper formation of middle-term memory (PubMed:27629706). Also required in the mushroom body neurons where it functions redundantly with neprilysins Nep3 and Nep4 in normal long-term memory formation (PubMed:27629706). {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960, ECO:0000269|PubMed:24395329, ECO:0000269|PubMed:27629706}.

Drosophila melanogaster (Fruit fly)

A0A0B4K7J2

RBP2_DROME

MFTTRKEVDAHVHKMLGKLQPGRERDIKGLAVARLYMKVQEYPKAIEYLNGYLRVRDDAVGHNMIATCYSRLNPPDVTEALQHYQRSIQIDPRQSEVVIDACELLVKENNASITECARYWLDQANSLDLSGNKQVFNLRMRVNLADSNGERDDTSGGDGEQNTLEILMYKELQARPQDVNIRIQLLRSYVEKMKIDQAFNYALKTELESKNCTSQSNEWYEQIWMVLFKIEMAKDVKKNWRFWHFALHTLDRLVQLSLEGSGLADSSKQLFRLDQYLFKFSTSIERSGDAPQRDLHQACIDHFTGQLLLHAVTLIFKREVLANKNKWMSTLRSALPLLLLGYQVRPIDDSSTNQWIKHCDAEQKQLIQMWRPQGAFRCAQLGRTLLGCLDRSQMEIKNDRENAEFDENKNSGNSMPGLFADSEELLASAHQQCLDKSWRSQIYQQLFTHAEHKLKDTSSHLVRNLRLQLPLFEWPNLAHIENYELQALVLPPHSLAQHVYLALGTDPNKLGDAPRVVFYEGFQRDVKQNLNYCGQDSISQVDVDLYLYATTIQTRRKLQIQREVYDSSNLGNRNAAARPHMMPFANLVGQLGAPEQSNWWDLVVRLNSNQLITEGNRAEQRAQLQHGLEAVRGVNGPKADAIIIFQLGKILNSRSDRSSLEARIDTLYRQGFSILRHQHNQQMESYVRVFKYGSAGSTAAWQDLQSLAEEAVTYFSEKMFRIGQYEQFLDEVRGLHLPMAYFLQSEACHHLEESSKLPRTSRDRYSERRRECLQKTQKLIKNDDKHPLIAAMHRHQQDRNSRGIDNSFGSPDVHNNSSAYEDAEDDFYSHAAFSANRSRRQLEVTPVTPIVMAQPSQEMEQAVKQISKSLCVLKDDVSVGMEAMRQDIKVLTEKFTGLEDLLKKIKISSRDTPTRDVDPAAALGLDDLFIIEDALAEHQQQQQHQQQQSHNQGAIHPVVPNPYTSGFYNGMPNTPSAQERFLQGPYGSPMFNQNQMYNYYAAQAQAQAQAQFLRTPPAPGSIPPPNMFGPRNPNFGLPSMFPPPTVPSVAPYIDAMGNFTQPPPSLIPPPAQPAAPPAPLNILESKPVVALPTPGFFNTTTPVFGASPIQVPQSKPLTVPTVPIPSTAPAPPIAGTVNPPATTAVPPPVHIPQVAPSVPAQPPAPAPVSVPSMFNRALNNQPVEKEPPANVVITSSDPLPKPTTASVQPTLSVTIPAQHIKPSLVQAPEQPAQSAQPAQPSVSGVGSLSFNFGSKSSESPFSFKTQVAKAAAEKQKEQEEAEQNQSGATDPNKTLPQDTSADDYDPRPDFKPIIPLPDEVEVRTGEEGEDIKFTSRAKLFRYVDKEWKERGTGVIKILCDKATGVSRVLMRRDQTHKVCANHTITADITINVANQDKDKKSLLWAANDFADEQVTLERFLVRFKTGELAEEFRVAFTKASEAAKSKETVKPTVNTAEKGSTATAPAAFKSFVTSTPAANSLINKPQEQTKTQPNPDPPATAAKSLFGTLSVSAAPATSAPASATPFASFSFTPNGSSGFGTSTASPFGNLSFGTASAVGSGNNTTLFTTALIKDNTVQGKTLQQESQLNKSNSSDAEEEYVPTAQFVPVIALPDIVEVVTGEENEDVLFEHRAKLLRWDKEANEWKERGLGNMKLLRDRTDPNKVRLLMRREQVHKLCCNQRLLPETKFTYATNCKAAVTWGAQDYSDEELTTALLAVRFKSQDICQQFLEAVQKAQQSIGNEPKKEEVPSAAGEKEKPIKGFGDAFKPKAGSWNCQACYTNNGQDQLYCLACQEPKDATVPPKQSGLDQGNALNLTTSSSNKFSFGFASSATLPATGGFSFGGATQPKEKPAVAVVTASASAPTSVQTAALGFGKSSMTSGFGDAFKPAVGSWSCSACYVNNPGESLYCSACDAPKNDTVPQKEKSLGSGLNLPPTSKFSFGFGAAAAGDKDQAGDGATFNFAAMPAAVAPTTSIGSSSFTFSMTKPKPDQQQPNSTAAKEDEDNDSQEVEEEENNTYFSPVIPLPDKIDVKTGEEDEELLYVHKAKLYRLNESDWKERGLGDVKILRHRQTKKLRVVMRREQVFKICLNHVLNENVVYREKTETSWMFAVHDFSEGESVLERFTLRFKNKEVAQGFMEAIKNALNETAKPIEDSPVVGSVSQSTEANKPSQKNDGAAKSRGGESEVLDVGKTSSVRPTTHEVIPPLPMTLPLLTLPQPLAKPNDYQTPATILFKGSSLSRNNSSASEASKTPSSAFIFGSTDKSEPGKDAGPLANLQKLASGEGQGNVLGSIFRSGSSNENSSDGSVKFFFGGGNKAAEQQKKDSSESVFGGNKADSQSPATQEAPKLAFGGIAAPVFGDANPFGGHKVNLQKSDGKEEPKSIIGGTPLLFGGSNAFGIPKIETQSPAKDFVFGSAPAFGQMATFSFTAAKNEKEKDITSNNTTDLKAEGKEKKELVPETTSTFADLAKTGSTFADLASNPGGTFADLANKTGNDFANLSANSQGTTVGFNKSAGGGFYNLTHQNAFKNFESPQATEECDDDGDATTDDNYDPHYDAIVELPDEIVVTTGEENETKLFGERAKLYRYDAESKQWKERGVGEIKVLEHPELQTFRLIMRQEQIHKLVLNMNISASLQMDYMNAQMKSFLWAGYNYAVDAEGKVDTEGVLERLACRFAKEEIASEFLNTVNSCIKRAKALQGDEENKNDDAPEEQASS

2.3.2.-

germ cell development [GO:0007281]; juvenile hormone mediated signaling pathway [GO:0035626]; mRNA transport [GO:0051028]; NLS-bearing protein import into nucleus [GO:0006607]; nuclear pore complex assembly [GO:0051292]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of RNA export from nucleus [GO:0046833]; protein import into nucleus [GO:0006606]; regulation of protein localization [GO:0032880]; ventral cord development [GO:0007419]

annulate lamellae [GO:0005642]; cytoplasm [GO:0005737]; nuclear pore [GO:0005643]

GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; SUMO transferase activity [GO:0019789]

PF00638;PF00641;

2.30.29.30;1.25.40.10;4.10.1060.10;

RanBP2 E3 ligase family

SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49792}. Note=Localizes to annulate lamellae, stacked membrane sheets of the endoplasmic reticulum. Localizes to granules which travel from nurse cells into the ooplasm through ring canals connecting the cytoplasm of the two cell types. {ECO:0000269|PubMed:31626769}.

FUNCTION: E3 SUMO-protein ligase (By similarity). Component of the nuclear pore complex (NPC), a complex required for trafficking across the nuclear envelope (PubMed:17682050). Required for nuclear import of nuclear localization signal (NLS)-containing proteins in an importin alpha/importin beta-dependent manner, but also for the nuclear import of specific proteins such as phosphorylated Mad or the sesquiterpenoid juvenile hormone receptor Met as part of the juvenile hormone signal transduction pathway (PubMed:17682050, PubMed:27979731). Plays a role in nuclear mRNA export by recruiting the mRNA transport complex composed of Nxt1 and sbr/Nxf1 to the NPC (PubMed:14729961). Essential during germline development for transposon silencing and piRNA biogenesis probably by regulating piwi localization to the nucleus (PubMed:29735528). During oogenesis, required to form granules that modulate the biogenesis of annulate lamellae containing nuclear pore complex components (PubMed:31626769). {ECO:0000250|UniProtKB:P49792, ECO:0000269|PubMed:14729961, ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:27979731, ECO:0000269|PubMed:29735528, ECO:0000269|PubMed:31626769}.

Drosophila melanogaster (Fruit fly)

A0A0B4KEE4

KOI_DROME

MSENTYQIETRRRSRSKTPFLRSSCDHENCEHAGEEGHVHHLKRKSAAPNVQTIIEEHIVESSISKKTRAKAFAQLTSDYSSDDMTPDAKRKQNSITATVTSILTKRSGGATSTPRNRSQLETTQNTLNSAQEKLNQSNGNLSSGNVSDYLAYIEYRDAGEYWNKTPKTDYTYSELSPHRRQLAPGIVAMPNMSRKSLENHNDRVNYMVQQNPAQEEFIRRRYQSKYTQQVNYDSADELDATFGQQKQSWWLIRLIQLVVSSITTVWSRVTNLSATETTAYQNYHAKRQQSQQVGLWWKIVQTIGGGLASLLRYLYVFIGSVLSLDTWLLRSSDAENKSKKRFLIFLLILLPLLLLSGWLLLQEDQRSAYVQRAEALLPLPLSIFGSLRSRFSNAGATLKSWMEVPTVRSPQREAEAIKVNMASIEQNIQKALTAEEYENILNHVNSYVQQLVELKMQQHSKELAPQQIELFVKLMKENLKQIMYKTELSEKDLSDLAIKLKLELQSSGGWQDGAKLSQANLEEITKLIKAEVHLHESHYTIQLDRIDFASLLERILAAPALADFVDARISLRVGELEPKESSGSSDAEVQIERLNREIAFIKLALSDKQAENADLHQSISNLKLGQEDLLERIQQHELSQDRRFHGLLAEIENKLSALNDSQFALLNKQIKLSLVEILGFKQSTAGGSAGQLDDFDLQTWVRSMFVAKDYLEQQLLELNKRTNNNIRDEIERSSILLMSDISQRLKREILLVVEAKHNESTKALKGHIREEEVRQIVKTVLAIYDADKTGLVDFALESAGGQILSTRCTESYQTKSAQISVFGIPLWYPTNTPRVAISPNVQPGECWAFQGFPGFLVLKLNSLVYVTGFTLEHIPKSLSPTGRIESAPRNFTVWGLEQEKDQEPVLFGDYQFEDNGASLQYFAVQNLDIKRPYEIVELRIETNHGHPTYTCLYRFRVHGKPPAT

double-strand break repair via homologous recombination [GO:0000724]; nuclear migration [GO:0007097]; nucleus localization [GO:0051647]

meiotic nuclear membrane microtubule tethering complex [GO:0034993]; microtubule organizing center [GO:0005815]; nuclear envelope [GO:0005635]; nuclear periphery [GO:0034399]; perinuclear region of cytoplasm [GO:0048471]

protein-membrane adaptor activity [GO:0043495]

PF07738;

2.60.120.260;

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:32066907}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18820457, ECO:0000269|PubMed:32066907}. Note=Lam is required for perinuclear localization of Koi (PubMed:18820457). In the fat body, localizes to a perinuclear non-centrosomal microtubule-organizing centers (ncMTOCs) (PubMed:32066907). {ECO:0000269|PubMed:18820457, ECO:0000269|PubMed:32066907}.

FUNCTION: Component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (By similarity). Is required to nuclear migration in eye and to anchor klar in the nuclear membrane (PubMed:18820457). {ECO:0000250|UniProtKB:O94901, ECO:0000269|PubMed:18820457}.

Drosophila melanogaster (Fruit fly)

A0A0B4KGY6

NOVA_DROME

MESIMKVAMDKAAEQLIQQFGFDYLQQQLQLQHQNQHNSSPQQPQHQQLEPENEHLTYQYQQSKPTHMQQLACNYQPRHSTTTSSPSSTHSLASGGGSSSNSSNSSSSDSSSINISHISNISNISNIGNISNSNHSNAAYSLAVHSYQKQIESPANPSHVPHHQMDLSPLSENGSPNGTPGAQTPTATASGNTAAALASAAAAAAAATSGGNGSSITNCNSNNSSSSSNAQQQLQLGNYKTNSCWCYGESVCSGIEVEIENNNNNHIHHGETTYHMKILVPAVASGAIIGKGGETIASLQKDTGARVKMSKSHDFYPGTTERVCLITGSTEAIMVVMEFIMDKIREKPDLTNKIVDTDSKQTQERDKQVKILVPNSTAGMIIGKGGAFIKQIKEESGSYVQISQKPTDVSLQERCITIIGDKENNKNACKMILSKIVEDPQSGTCLNVSYADVSGPVANFNPTGSPYATNQNAINSSTASLNSTLGTTIGGANSAASLLVNGTGINLSINLGSPNPAPNLAVATQLLEHIKVAMRGSGYSETVTNEVVAALSVLAKYGVLGMGVGVSHTNGAHSTLGNFLGVTTLDQQTAAAASAATASNVFGAVGQVNLEQYAAAVASAAAASRPTQSQLDAAAVQFDPFRHLGSATAPAATPVSLNNNSFGLTATTGTATTAQLGGLSKSPTPGDLSSKDSKNVEVPEVIIGAILGPSGRSLVEIQHVSGANVQISKKGIFAPGTRNRIVTITGQPSAIAKAQYLIEQKINEEETKRARQIPLTTVVN

3'-UTR-mediated mRNA stabilization [GO:0070935]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of RNA splicing [GO:0033120]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]

mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA binding [GO:0003729]; pre-mRNA intronic binding [GO:0097157]

PF00013;

3.30.1370.10;

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11784037, ECO:0000269|PubMed:28525754}. Cytoplasm {ECO:0000269|PubMed:28525754}. Note=Localizes to synaptoneuropil region of neurons. {ECO:0000269|PubMed:28525754}.

FUNCTION: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion (By similarity). Plays a role in long-term memory formation by processing the unspliced Orb2-isoform A (Orb2A) mRNA and thereby controlling Orb2A protein abundance (PubMed:28525754). {ECO:0000250|UniProtKB:Q9JKN6, ECO:0000269|PubMed:28525754}.

Drosophila melanogaster (Fruit fly)

A0A0B4LFY9

STING_DROME

MAIASNVVEAGNAVRAEKGRKYFYFRKMIGDYIDTSIRIVATVFLADLLLRLYRCVVEYGSNGRYYLPEDRLWIILRRSCTYNNRSIYLIVGFLLVAFFRISVTGNYRNVMPTTLFLFQMPLYWIWSFTDMDQSTLSYSHWIRDSHGLDYAAGMASNYFHGYLKLSLPERKDDGLKHRLAMYEDKNNVTFGIKRLVILIPDEMFVNGVLESHLLDKAEPLETQFINRAGVYRPFKHDVYRMNKKVNGRTYYFAVEGATPMISFFDATYSNLSGTWQMQELKREIWIKFYKHLKELITTWPETRDLVELIIYNSHDSKGNLVDVGELLVAHMQNKTKTIDEISN

antiviral innate immune response [GO:0140374]; autophagosome assembly [GO:0000045]; cellular response to virus [GO:0098586]; cGAS/STING signaling pathway [GO:0140896]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of antimicrobial peptide biosynthetic process [GO:0002807]; positive regulation of macroautophagy [GO:0016239]; positive regulation of type I interferon production [GO:0032481]; reticulophagy [GO:0061709]

autophagosome [GO:0005776]; endoplasmic reticulum membrane [GO:0005789]

2',3'-cyclic GMP-AMP binding [GO:0061507]; 3',2'-cyclic GMP-AMP binding [GO:0140704]; cyclic-di-GMP binding [GO:0035438]

PF15009;

3.40.50.12100;

STING family

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30119996}; Multi-pass membrane protein {ECO:0000255}.

FUNCTION: Facilitator of innate immune signaling that binds cyclic dinucleotides produced in response to infection by bacteria and/or viruses, and promotes the activation of the NF-kappa-B transcription factor Rel (Relish) (PubMed:29924997, PubMed:29934091, PubMed:30119996, PubMed:33262294, PubMed:34261127, PubMed:34261128). Recognizes and binds cyclic di-GMP (c-di-GMP), a cyclic dinucleotide messenger produced by bacteria such as L.monocytogenes, leading to activation of the peptidoglycan recognition protein (IMD) signaling pathway and activation of Rel (Relish) (PubMed:29924997). Innate immune response is triggered in response to double-stranded RNA from viruses delivered to the cytoplasm: Sting acts by specifically binding cyclic dinucleotides 3',2'-cGAMP and 2',3'-cGAMP produced by cGlr1 and cGlr2 in response to RNA virus in the cytosol (PubMed:34261127, PubMed:34261128). Has a strong preference for 3',2'-cGAMP compared to other cyclic dinucleotides such as 2',3'-cGAMP or 3'3'-c-di-GMP (PubMed:34261127). Upon binding to 3',2'-cGAMP, activates an antiviral immune response, leading to the activation of Rel (Relish) (PubMed:34261127, PubMed:34261128). Activated in brain in response to Zika virus infection, leading to autophagy (PubMed:29934091). {ECO:0000269|PubMed:29924997, ECO:0000269|PubMed:29934091, ECO:0000269|PubMed:30119996, ECO:0000269|PubMed:33262294, ECO:0000269|PubMed:34261127, ECO:0000269|PubMed:34261128}.

Drosophila melanogaster (Fruit fly)

A0A0B4U9L8

VMF1_VIPAA

MLQVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPQKLTALLKGAIQQPEQKYEDAMQYEFKVNGKPVVLHLEKNKGLFSEDYSETHYSPDGREITTNPPVEDHCYYHGHIQNDAHLTASISACNGLKGHFQLRGETYLIEPLKIPDSEAHAVYKYENVEKEDEGPKKCGVTQTNWKSDEPIKASQFILTPEQRAYMNANKYIKLAIVVDNVMFRKYTGNFTAIRTRIYEIVNTLNLIYTILNIHIALVFLEIWSKGDSINVQSVVDVTLNSFGEWRERDLLNRKRHDNAQLLTGINFNGDTIGFGFVGSMCIPKKSVGIVQDHSKTHLLVATTMAHELGHNLGINHDGDSCTCQANSCIMAAKLSHQPSYQFSDCSINELWMYLISHTPRCILNEPLTTDVVSPAVCGNYVVEEGEECDCGSLWYCRNPCCDAATCKLKPGAECGDGVCCYQCRFVTAGTVCRPARSECDIPEYCSGQSVECPMDHIQKNGKPCLMNHGYCYNGRCPIMIHQCIALWGPGTTVSSDVCFQRNESGQGYSYCRRENNQNIPCAPQDVKCGRLYCKFHNVNTLPCNFKYSDFAPDYGLVDHGTKCGDGKVCNSNRQCVDVNTAY

3.4.24.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9DGB9}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9DGB9};

envenomation resulting in modulation of blood coagulation in another organism [GO:0044468]; envenomation resulting in modulation of process in another organism [GO:0035738]; proteolysis [GO:0006508]

extracellular region [GO:0005576]; extraorganismal space [GO:0043245]; plasma membrane [GO:0005886]

metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270]

PF08516;PF00200;PF01562;PF01421;

3.40.390.10;4.10.70.10;

Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily

PTM: N-glycosylated. {ECO:0000269|PubMed:25549999}.; PTM: The N-terminus is blocked. {ECO:0000269|PubMed:25549999}.

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25549999}.

FUNCTION: Zinc metalloprotease that has fibrinogenolytic activity. Does not have hemorrhagic activity in rats. Cleaves insulin B chain at '38-Ala-|-Leu-39' and '40-Tyr-|-Leu-41' bonds. Hydrolyzes only partially and weakly isolated extracellular matrix (ECM) bovine fibronectin and basal membrane (BM) protein human collagen IV in vitro. Murine laminin is not hydrolyzed, neither isolated nor in a solubilized BM preparation. Nidogen is hydrolyzed at '350-Ser-|-Phe-351' bond in a solubilized BM preparation. Hydrolyzes plasma proteins involved in blood coagulation in vitro. Has alpha-fibrinogenase activity cleaving human fibrinogen alpha chain at '432-Lys-|-Leu-433' bond, but does not cleave beta or gamma chains. Does not cleave fibrin. Hydrolyzes only partially bovine prothrombin at '200-Ser-|-Gly-201' bond, factor X (FX) heavy chain, and very slowly, FX light chain and plasminogen in vitro, without activating any of them. Has no effect in plasma thrombin generation. Does not inhibit platelet aggregation induced by collagen in vitro. May have a delayed pathological action as an anticoagulant in envenomed patients after they received serotherapy as it is not recognized by the venom antiserum. {ECO:0000269|PubMed:25549999}.

Vipera ammodytes ammodytes (Western sand viper)

A0A0B5A051

PT1L_HUMLU

MELSSVSSFSLGTNPFISIPHNNNNNLKVSSYCCKSKSRVINSTNSKHCSPNNNNNNNTSNKTTHLLGLYGQSRCLLKPLSIFSCKDQRGNSIRASAQIEDRPPESGNLSALTNVKDFVSVCWEYVRPYTAKGVIICSSCLFGRELLENPNLFSWPLIFRALLGMLAILGSCFYTAGINQIFDMDIDRINKPDLPLVSGRISVESAWLLTLSPAIIGFILILKLNSGPLLTSLYCLAILSGTIYSVPPFRWKKNPITAFLCILMIHAGLNFSVYYASRAALGLAFVWSPSFSFITAFITFMTLTLASSKDLSDINGDRKFGVETFATKLGAKNITLLGTGLLLLNYVAAISTAIIWPKAFKSNIMLLSHAILAFSLFFQARELDRTNYTPEACKSFYEFIWILFSAEYVVYLFI

2.5.1.136

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:E5RP65};

chloroplast membrane [GO:0031969]

prenyltransferase activity [GO:0004659]

PF01040;

1.10.357.140;

UbiA prenyltransferase family

SUBCELLULAR LOCATION: Plastid {ECO:0000269|PubMed:25564559}. Plastid, chloroplast membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: [2-acylphloroglucinol 4-prenyltransferase]: Reaction=2',4,4',6'-tetrahydroxychalcone + dimethylallyl diphosphate = desmethylxanthohumol + diphosphate; Xref=Rhea:RHEA:51876, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:77645, ChEBI:CHEBI:134302; EC=2.5.1.136; Evidence={ECO:0000269|PubMed:29760092}; CATALYTIC ACTIVITY: Reaction=a 2-acylphloroglucinol + dimethylallyl diphosphate = a 2-acyl-4-prenylphloroglucinol + diphosphate; Xref=Rhea:RHEA:51752, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:134371, ChEBI:CHEBI:134386; EC=2.5.1.136; Evidence={ECO:0000269|PubMed:25564559};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.74 uM for naringenin chalcone {ECO:0000269|PubMed:29760092}; KM=75.12 uM for dimethylallyl diphosphate {ECO:0000269|PubMed:29760092}; KM=5.01 uM for naringenin chalcone (in the presence of CHIL2) {ECO:0000269|PubMed:29760092}; KM=62.78 uM for dimethylallyl diphosphate (in the presence of CHIL2) {ECO:0000269|PubMed:29760092}; KM=1.36 uM for phlorisovalerophenone {ECO:0000269|PubMed:25564559}; KM=5.1 uM for phlorisobutyrophenone {ECO:0000269|PubMed:25564559}; KM=43.52 uM for dimethylallyl diphosphate {ECO:0000269|PubMed:25564559}; KM=5.7 uM for geranyl diphosphate {ECO:0000269|PubMed:25564559}; Vmax=0.1 umol/min/g enzyme with naringenin chalcone as substrate {ECO:0000269|PubMed:29760092}; Vmax=0.13 umol/min/g enzyme with dimethylallyl diphosphate as substrate {ECO:0000269|PubMed:29760092}; Vmax=0.12 umol/min/g enzyme with naringenin chalcone as substrate (in the presence of CHIL2) {ECO:0000269|PubMed:29760092}; Vmax=0.23 umol/min/g enzyme with dimethylallyl diphosphate as substrate (in the presence of CHIL2) {ECO:0000269|PubMed:29760092};

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:30468448}.

FUNCTION: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the first prenylation step in the beta-bitter acid pathway (PubMed:25564559). Uses dimethylallyl diphosphate (DMAPP) as the prenyl donor (PubMed:25564559). {ECO:0000269|PubMed:25564559, ECO:0000305|PubMed:30468448}.

Humulus lupulus (European hop)

A0A0B5A886

GP_SFTSV

MMKVIWFSSLICLVIQCSGDSGPIICAGPIHSNKSAGIPHLLGYSEKICQIDRLIHVSSWLRNHSQFQGYVGQRGGRSQVSYYPAENSYSRWSGLLSPCDADWLGMLVVKKAKESDMIVPGPSYKGKVFFERPTFDGYVGWGCGSGKSRTESGELCSSDSGTSSGLLPSDRVLWIGDVACQPMTPIPEETFLELKSFSQSEFPDICKIDGIVFNQCEGESLPQPFDVAWMDVGHSHKIIMREHKTKWVQESSSKDFVCYKEGTGPCSESEEKACKTSGSCRGDMQFCKVAGCEHGEEASEAKCRCSLVHKPGEVVVSYGGMRVRPKCYGFSRMMATLEVNPPEQRIGQCTGCHLECINGGVRLITLTSELRSATVCASHFCSSASSGKKSTEIHFHSGSLVGKTAIHVKGALVDGTEFTFEGSCMFPDGCDAVDCTFCREFLKNPQCYPAKKWLFIIIVILLGYAGLMLLTNVLKAIGVWGSWVIAPVKLMFAIIKKLMRTVSCLVGKLMDRGRQVIHEEIGENGEGNQDDVRIEMARPRRVRHWMYSPVILTILAIGLAEGCDEMVHADSKLVSCRQGSGNMKECITTGRALLPAVNPGQEACLHFTAPGSPDSKCLKIKVKRINLKCKKSSSYFVPDARSRCTSVRRCRWAGDCQSGCPPHFTSNSFSDDWAGKMDRAGLGFSGCSDGCGGAACGCFNAAPSCIFWRKWVENPHGIIWKVSPCAAWVPSAVIELTMPSGEVRTFHPMSGIPTQVFKGVSVTYLGSDMEVSGLTDLCEIEELKSKKLALAPCNQAGMGVVGKVGEIQCSSEESARTIKKDGCIWNADLVGIELRVDDAVCYSKITSVEAVANYSAIPTTIGGLRFERSHDSQGKISGSPLDITAIRGSFSVNYRGLRLSLSEITATCTGEVTNVSGCYSCMTGAKVSIKLHSSKNSTAHVRCKGDETAFSVLEGVHSYIVSLSFDHAVVDEQCQLNCGGHESQVTLKGNLIFLDVPKFVDGSYMQTYHSTVPTGANIPSPTDWLNALFGNGLSRWILGVIGVLLGGLALFFLIMFLLKLGTKQVFRSRTKLA

entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host endosome membrane [GO:0039654]; symbiont entry into host cell [GO:0046718]

host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; virion membrane [GO:0055036]

PF19019;PF07243;PF07245;

2.60.40.3770;2.60.98.50;

Phlebovirus envelope glycoprotein family

PTM: [Envelopment polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins including glycoprotein C and glycoprotein N. {ECO:0000269|PubMed:27855227}.; PTM: [Glycoprotein N]: The cytoplasmic tail is Palmitoylated. {ECO:0000250|UniProtKB:P09613}.; PTM: [Glycoprotein N]: Glycosylated. {ECO:0000250|UniProtKB:P09613}.; PTM: [Glycoprotein C]: Palmitoylated. {ECO:0000250|UniProtKB:P09613}.; PTM: [Glycoprotein C]: Glycosylated. {ECO:0000250|UniProtKB:P09613}.

SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane {ECO:0000269|PubMed:27855227, ECO:0000269|PubMed:29467349}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:27855227, ECO:0000269|PubMed:29467349}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N and Glycoprotein C is essential for proper targeting of Glycoprotein C to the Golgi complex, where virion budding occurs. {ECO:0000269|PubMed:27855227}.; SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane {ECO:0000269|PubMed:27855227, ECO:0000269|PubMed:29467349}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:27855227, ECO:0000269|PubMed:29467349}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N and Glycoprotein C is essential for proper targeting of Glycoprotein C to the Golgi complex, where virion budding occurs. {ECO:0000269|PubMed:27855227}.

FUNCTION: [Glycoprotein N]: Structural component of the virion that interacts with glycoprotein C (By similarity). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (By similarity). Plays a role in the packaging of ribonucleoproteins and polymerase during virus assembly (PubMed:29467349). {ECO:0000250|UniProtKB:P09613, ECO:0000250|UniProtKB:P21401, ECO:0000250|UniProtKB:R4V2Q5, ECO:0000269|PubMed:29467349}.; FUNCTION: [Glycoprotein C]: Structural component of the virion that interacts with glycoprotein N (By similarity). Acts as a class II fusion protein that is activated upon acidification and subsequent repositioning of the glycoprotein N (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (By similarity). {ECO:0000250|UniProtKB:P09613, ECO:0000250|UniProtKB:P21401, ECO:0000250|UniProtKB:R4V2Q5}.

SFTS phlebovirus (isolate SFTSV/Human/China/HB29/2010) (Severe fever with thrombocytopenia virus)

A0A0B5A8P4

INS3A_CONGE

MTTSFYFLLVALGLLLYVCQSSFGNQHTRNSDTPKHRCGSELADQYVQLCHGKRNDAGKKRGRASPLWQRQGFLSMLKAKRNEAFFLQRDGRGIVEVCCDNPCTVATLRTFCH

glucose metabolic process [GO:0006006]

extracellular region [GO:0005576]

hormone activity [GO:0005179]; toxin activity [GO:0090729]

PF00049;

1.10.100.10;

Insulin family

PTM: It is noteworthy that in this dimer, in contrast to Con-Ins G1, the chain B is amidated and not the chain A. {ECO:0000269|PubMed:25605914}.

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25605914}.

FUNCTION: This venom insulin, from a fish-hunting cone snail, facilitates prey capture by rapidly inducing hypoglycemic shock (PubMed:30747102). It is one of the smallest known insulin found in nature and lacks the C-terminal segment of the B chain that, in human insulin, mediates engagement of the insulin receptor (INSR) and assembly of the hormone's hexameric storage form (By similarity). Despite lacking this segment, it both binds and activates human insulin receptor (long isoform (HIR-B)) with a high potency (EC(50)=242 nM) (PubMed:30747102). In vivo, intraperitoneal injection of this peptide into zebrafish lowers blood glucose with a lower potency than human insulin (PubMed:30747102). In addition, when applied to water, this peptide reduces overall locomotor activity of zebrafish larvae, observed as a significant decrease in the percentage of time spent swimming and movement frequency (By similarity). When tested on a mouse model of diabetes, this insulin also lowers blood glucose with a 10-fold lower potency than human insulin (By similarity). {ECO:0000250|UniProtKB:A0A0B5AC95, ECO:0000269|PubMed:30747102}.

Conus geographus (Geography cone) (Nubecula geographus)

A0A0B5AC19

NSS_SFTSV

MSLSKCSNVDLKSVAMNANTVRLEPSLGEYPTLRRDLVECSCSVLTLSMVKRMGKMTNTVWLFGNPKNPLHQLEPGLEQLLDMYYKDMRCYSQRELSALRWPSGKPSVWFLQAAHMFFSIKNSWAMETGRENWRGLFHRITKGQKYLFEGDMILDSLEAIEKRRLRLGLPEILITGLSPILDVALLQIESLARLRGMSLNHHLFTSPSLRKPLLDCWDFFIPVRKKKTDGSYSVLDEDDEPGVLHGYPHLMAHYLNRCPFHNLIRFDEELRTAALNTIWGRDWPAIGDLPKEV

symbiont-mediated arrest of host cell cycle during G2/M transition [GO:0039592]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity [GO:0039540]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity [GO:0039723]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]

host cell cytoplasmic vesicle [GO:0044161]

Bandavirus NS-S protein family

SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:24478431}. Host cytoplasmic vesicle {ECO:0000269|PubMed:24335286, ECO:0000269|PubMed:28680969, ECO:0000269|PubMed:30598516}. Note=Localizes to the viral cytoplasmic occlusion bodies. {ECO:0000269|PubMed:24335286, ECO:0000269|PubMed:27226560, ECO:0000269|PubMed:28680969, ECO:0000269|PubMed:30598516}.

FUNCTION: Sequesters host STAT2 into viral inclusion bodies (Probable) (PubMed:29886262). Impairs IFN-stimulated phosphorylation and nuclear translocation of host STAT2, thereby suppressing type-I IFN antiviral signaling (Probable) (PubMed:28680969, PubMed:29886262). Sequesters host TRIM25, RIGI, TBK1/IKK complex components (TBK1, IKBKE/IKKE, and IRF3) and IRF7 into viral inclusion bodies, thereby inhibiting the IFN responses (Probable). Inhibits TRIM25-mediated ubiquitination of the RIGI (PubMed:32471869). The sequestration of IKBKE/IKKE, and IRF3 occurs via the interaction with TBK1 (PubMed:24335286). Sequestration and inhibition of host TBK1 probably participates to the cytokine storm induced by the virus (PubMed:33288641). Also inhibits the phosphorylation of host TBK1 (PubMed:28680969). Interacts with host TNIP2 and promotes TPL2-TNIP2-p105 complex formation leading to IL-10 induction (PubMed:30617349). By interacting with CDK1, induces host cell arrest at the G2/M transition to promote viral replication (PubMed:31852787). Requested for the formation of the viral cytoplasmic inclusion bodies (PubMed:24335286, PubMed:27226560). {ECO:0000269|PubMed:24335286, ECO:0000269|PubMed:27226560, ECO:0000269|PubMed:28680969, ECO:0000269|PubMed:29886262, ECO:0000269|PubMed:30617349, ECO:0000269|PubMed:31852787, ECO:0000269|PubMed:32471869, ECO:0000269|PubMed:33288641, ECO:0000305|PubMed:24478431, ECO:0000305|PubMed:24706939, ECO:0000305|PubMed:25631085, ECO:0000305|PubMed:30021900, ECO:0000305|PubMed:30598516}.

SFTS phlebovirus (isolate SFTSV/Human/China/HB29/2010) (Severe fever with thrombocytopenia virus)

A0A0B5AC95

INS1A_CONGE

MTTSSYFLLMALGLLLYVCQSSFGNQHTRTFDTPKHRCGSEITNSYMDLCYRKRNDAGEKRGRASPLWQRRGSLSKLKARAKRNGAFHLPRDGRGVVEHCCHRPCSNAEFKKYCG

glucose metabolic process [GO:0006006]

extracellular region [GO:0005576]

hormone activity [GO:0005179]; toxin activity [GO:0090729]

PF00049;

1.10.100.10;

Insulin family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25605914}.

FUNCTION: This venom insulin, from a fish-hunting cone snail, facilitates prey capture by rapidly inducing hypoglycemic shock (PubMed:25605914, PubMed:27617429). It is one of the smallest known insulin found in nature and lacks the C-terminal segment of the B chain that, in human insulin, mediates engagement of the insulin receptor (INSR) and assembly of the hormone's hexameric storage form (PubMed:27617429). Despite lacking this segment, it both binds and activates human insulin receptor (long isoform (HIR-B)) with a high potency (EC(50)=16.28 nM) (PubMed:27617429, PubMed:30747102). In vivo, intraperitoneal injection of this peptide into zebrafish lowers blood glucose with the same potency than human insulin (PubMed:25605914, PubMed:30747102). In addition, when applied to water, this peptide reduces overall locomotor activity of zebrafish larvae, observed as a significant decrease in the percentage of time spent swimming and movement frequency (PubMed:25605914). When tested on a mouse model of diabetes, this insulin also lowers blood glucose with a 10-fold lower potency than human insulin (PubMed:30747102). {ECO:0000269|PubMed:25605914, ECO:0000269|PubMed:27617429, ECO:0000269|PubMed:30747102}.

Conus geographus (Geography cone) (Nubecula geographus)

A0A0B5KYT4

MPDE2_PENBR

MESLSLTWITAIAVVLYLVQRYVRSYWRLKDIPGPVLAKLTDLQRVWWVKTGRAHEFHRDMHAMYGPIVRFGPNMVSVSDPRVIPTIYPSRPGFPKGDFYRTQKPYTRNKGAMPAVFNTQDEDLHKQLRSPIASLYSMTNVVRLEPLVDETLTVLSKQLDERFVGTNDKPFDLGDWLQYFAFDSMGTLTFSRRYGFLEQGRDMHGILQEIWNFMTRVAVMGQIPWFDEIWNKNSFITLFKRPTGFGVLKVVDNFISQRVSSRENDEKADEKDMLSQFLNIQASNPHSIMPWAPRAWTFSNVMAGSDSTANVMRTMMYNLLVDRDTLKSLRAELLEAESSNGLSRSLPSWDGVRSLPYLDACVLEALRLHPPFCLPFERVVPEGGITVCETYLPAGTVVGISPYLANRDKQTFGDDADKWRPSRWLDLSREDRVKLENSILTFGAGRRTCLGKNIAILEIKKLFPMLLLNYEIEIVNPENYQTTNAWFFRQWGLHAVIRKLPAPERDDTIEQKASIPPALNIPPSSSTVDVRIIDSGTLLDLRPDLFWTPDLPGLLKVTAPTYCFLISNGSRHVLFDLAVRQDWENLPPSIVAMIKSQTVIQEPRNISDVLDSDESSLGIRSKDIEAIIWSHAHFDHIGDPSTFPPSTELVVGPGIRDTHWPGFPTNPDAINLNTDIQGRNVREISFEKTQKGATKIGSFDAMDYFGDGSFYLLDAAGHSVGHIGALARVTTSPDSFVFMGGDSCHHAGVLRPTKYLPCPLDSGDTSLPCKSDSVFTLSPALPTDYTAALRTVENIKELDACEDVFVVLAHDATLKGKVDFYPSKINDWKAKEYGKKTKWLFYKDIENAIEGQK

1.-.-.-

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

mycophenolic acid biosynthetic process [GO:0140722]; terpenoid biosynthetic process [GO:0016114]

endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; polyketide synthase activity [GO:0016218]

PF00753;PF00067;

1.10.630.10;3.60.15.10;

Cytochrome P450 family

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31209052}; Single-pass membrane protein {ECO:0000255}.

CATALYTIC ACTIVITY: Reaction=5-methylorsellinate + O2 + reduced [NADPH--hemoprotein reductase] = 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:66668, 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:146172, ChEBI:CHEBI:167385; Evidence={ECO:0000269|PubMed:31209052}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66669; Evidence={ECO:0000269|PubMed:31209052}; CATALYTIC ACTIVITY: Reaction=4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoate + H(+) = 5,7-dihydroxy-4-methylphthalide + H2O; Xref=Rhea:RHEA:66672, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:68194, ChEBI:CHEBI:167385; Evidence={ECO:0000269|PubMed:31209052}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66673; Evidence={ECO:0000269|PubMed:31209052};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:31209052}.

FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893 (PubMed:31209052). MpaDE' is an endoplasmic reticulum-bound enzyme that catalyzes the conversion of 5-methylorsellinic acid (5MOA) into the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) (PubMed:31209052). MpaDE' first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB), and then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP (PubMed:31209052). The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable) (PubMed:31209052). {ECO:0000269|PubMed:31209052, ECO:0000305|PubMed:31209052}.

Penicillium brevicompactum

A0A0B5LB55

MPAH2_PENBR

MSTEKFTITEHLVPGSHIREYPGSTVNQEDVLKIHVKQYTPKREGPVPDDAITFIATHGVGLPKELYEPLWDELLDQASGFHIRAIWMADVASMNQSGIHNEDKLSMDCSWMDHARDLLLMINHFRDQMPRPLVGIGHSFGGNIITNLAYLHPRLFTTLLLLDPLIQLSPPSLGFGTDAPSAINYTLWRDDVWPSREVAIRANRAIMQGMDPRCLDRMTKHFFRDLPTPLYPDVEAIKALFGTTADSTTTPVTLTTPKYHELVAQIRQNFNARDPKTGRIEVPRDTHADMDPLVAYIPLYRPEPRSTFRRLETLRPSCLWVIAGATFLNIDEIREGVKICGSGIGGSGGVPDGRVREVVLPGFGHLMPFQEVKTVAETCIVWLQQEMDRFRQTERQWKEDRDGKSHLAVEENWYKVLKPIPSGRKKRNDKGKL

3.1.1.-

mycophenolic acid biosynthetic process [GO:0140722]; terpenoid biosynthetic process [GO:0016114]

peroxisomal matrix [GO:0005782]

fatty acyl-CoA hydrolase activity [GO:0047617]; hydrolase activity [GO:0016787]; polyketide synthase activity [GO:0016218]

PF12697;

3.40.50.1820;

AB hydrolase superfamily, MpaH hydrolase family

SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:31209052}. Note=The mpaH' location in peroxisomes is required for the unique cooperation between biosynthetic and beta-oxidation catabolism machineries to produce final MPA. {ECO:0000269|PubMed:31209052}.

CATALYTIC ACTIVITY: Reaction=H2O + mycophenolyl-CoA = CoA + H(+) + mycophenolate; Xref=Rhea:RHEA:66704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:62932, ChEBI:CHEBI:167447; Evidence={ECO:0000269|PubMed:31209052, ECO:0000269|PubMed:33843134}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66705; Evidence={ECO:0000269|PubMed:31209052, ECO:0000269|PubMed:33843134};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=722.3 uM for acetyl-CoA {ECO:0000269|PubMed:31209052}; KM=351.5 uM for propionyl-CoA {ECO:0000269|PubMed:31209052}; KM=76.37 uM for malonyl-CoA {ECO:0000269|PubMed:31209052}; KM=201.9 uM for isobutyryl-CoA {ECO:0000269|PubMed:31209052}; KM=780.83 uM for isovaleryl-CoA {ECO:0000269|PubMed:31209052}; KM=217.9 uM for benzoyl-CoA {ECO:0000269|PubMed:31209052}; KM=143 uM for N-decanoyl-CoA {ECO:0000269|PubMed:31209052}; KM=260.2 uM for lauroyl-CoA {ECO:0000269|PubMed:31209052}; KM=577 uM for palmitoyl-CoA {ECO:0000269|PubMed:31209052}; KM=316.6 uM for arachidonoyl-CoA {ECO:0000269|PubMed:31209052}; KM=382.6 uM for DMMPA-CoA {ECO:0000269|PubMed:31209052}; KM=117.5 uM for MPA-CoA {ECO:0000269|PubMed:31209052}; Note=The kcat values are 54.98 min(-1) for acetyl-CoA, 24.58 min(-1) for propionyl-CoA, 12.94 min(-1) for malonyl-CoA, 7.688 min(-1) for isobutyryl-CoA, 5.718 min(-1) for isovaleryl-CoA, 3.891 min(-1) for benzoyl-CoA, 136.5 min(-1) for N-decanoyl-CoA, 99.11 min(-1) for lauroyl-CoA, 23.19 min(-1) for palmitoyl-CoA, 47.35 min(-1) for arachidonoyl-CoA, 4438 min(-1) for DMMPA-CoA and 9578 min(-1) for MPA-CoA. {ECO:0000269|PubMed:31209052};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:31209052, ECO:0000269|PubMed:33843134}.

FUNCTION: Type I acyl-CoA thioesterase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893 (PubMed:31209052, PubMed:33843134). MpaH' acts as a peroxisomal acyl-CoA hydrolase that converts MPA-CoA into the final product MPA (PubMed:31209052, PubMed:33843134). The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable) (PubMed:31209052). {ECO:0000269|PubMed:31209052, ECO:0000269|PubMed:33843134, ECO:0000305|PubMed:31209052}.

Penicillium brevicompactum

A0A0B6CGH9

F7ODM_OCIBA

MRITLQYIKLESKNTKERDMAESKAIGRSLEVPNVQELAKGKLASVPARYVRYSDRENTTLPPLTQIPVIDMQALLHPNSFEAELNSLHKACKQWGFFQLINHGVEAAVMEKMKLEMQEFFNLPLEEKQKFRQSADDMEGYGQSFVVSDEQKLDWADGFSVISLPTYLRKPHLIPKLPAPFRDAIDAYGAQLKELAIKILGFMAEALGMDPHEMTALFEEGIQALRMNYYPPCPQPEMVSGLCPHSDAGGLTILMQVNEVEGLQVRKDGGWVPVSPLPDAFIINLGDILEIVTNGEYFSVEHQATVNGDKERLSVAAFLNPKMEDNIGPAASFISGETPAKFKTITAAEYFKGLFSKELDGKSYLDLMRIQN

1.14.13.-

COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q94LP4};

coumarin biosynthetic process [GO:0009805]; response to molecule of fungal origin [GO:0002238]

cytoplasm [GO:0005737]

2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; metal ion binding [GO:0046872]

PF03171;PF14226;

Iron/ascorbate-dependent oxidoreductase family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q94LP4}.

CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + gardenin B + O2 = CO2 + formaldehyde + H(+) + nevadensin + succinate; Xref=Rhea:RHEA:73443, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:79628, ChEBI:CHEBI:192756; Evidence={ECO:0000269|PubMed:25378691}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73444; Evidence={ECO:0000269|PubMed:25378691}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 8-hydroxysalvigenin + O2 = CO2 + formaldehyde + pilosin + succinate; Xref=Rhea:RHEA:73511, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:174456, ChEBI:CHEBI:192704; Evidence={ECO:0000269|PubMed:25378691}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73512; Evidence={ECO:0000269|PubMed:25378691};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.46 uM for gardenin B {ECO:0000269|PubMed:25378691}; KM=20.98 uM for 2-oxoglutarate {ECO:0000269|PubMed:25378691}; KM=4.02 uM for Fe(2+) {ECO:0000269|PubMed:25378691}; KM=7.651 uM for ascorbate {ECO:0000269|PubMed:25378691}; Vmax=1.267 pmol/sec/mg enzyme with gardenin B as substrate {ECO:0000269|PubMed:25378691}; Vmax=1.087 pmol/sec/mg enzyme with 2-oxoglutarate as substrate {ECO:0000269|PubMed:25378691}; Vmax=1.153 pmol/sec/mg enzyme with Fe(2+) as substrate {ECO:0000269|PubMed:25378691}; Vmax=1.047 pmol/sec/mg enzyme with ascorbate as substrate {ECO:0000269|PubMed:25378691}; Note=kcat is 5.38x10(2) sec(-1) with gardenin B as substrate (PubMed:25378691). kcat is 4.62x10(2) sec(-1) with 2-oxoglutarate as substrate (PubMed:25378691). kcat is 4.96x10(2) sec(-1) with Fe(2+) as substrate (PubMed:25378691). kcat is 84.56x10(2) sec(-1) with ascorbate as substrate (PubMed:25378691). {ECO:0000269|PubMed:25378691};

PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}.

FUNCTION: Oxoglutarate-dependent dioxygenase (2-ODD) acting as a flavonoid 7-O-demethylase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects (PubMed:25378691). Catalyzes the 7-O-demethylation of methoxylated flavones; mediates the conversion of 8-hydroxysalvigenin (8-OH-SALV) to pilosin (PIL) and of gardenin B (GARD B) to nevadensin (NEV) (PubMed:25378691). {ECO:0000269|PubMed:25378691}.

Ocimum basilicum (Sweet basil)

A0A0B7P3V8

YP41B_YEAST

MATPVRDETRNVIDDNISARIQSKVKTNDTVRQTPSSLRKVSIKDEQVKQYQRNLNRFKTILNGLKAEEEKLSETDDIQMLAEKLLKLGETIDKVENRIVDLVEKIQLLETNENNNILHEHIDATGTYYLFDTLTSTNKRFYPKDCVFDYRTNNVENIPILLNNFKKFIKKYQFDDVFENDIIEIDPRENEILCKIIKEGLGESLDIMNTNTTDIFRIIDGLKNKYRSLHGRDVRIRAWEKVLVDTTCRNSALLMNKLQKLVLMEKWIFSKCCQDCPNLKDYLQEAIMGTLHESLRNSVKQRLYNIPHNVGINHEEFLINTVIETVIDLSPIADDQIENSCMYCKSVFHCSINCKKKPNRELRPDSTNFSKTYYLQGAQRQQQLKSSAKEQKSWNKTQKKSNKVYNSKKLVIIDTGSGVNITNDKTLLHNYEDSNRSTRFFGIGKNSSVSVKGYGYIKIKNGHNNTDNKCLLTYYVPEEESTIISCYDLAKKTKMVLSRKYTRLGNKIIKIKTKIVNGVIHVKMNELIERPSDDSKINAIKPTSSPGFKLNKRSITLEDAHKRMGHTGIQQIENSIKHNHYEESLDLIKEPNEFWCQTCKISKATKRNHYTGSMNNHSTDHEPGSSWCMDIFGPVSSSNADTKRYMLIMVDNNTRYCMTSTHFNKNAETILAQIRKNIQYVETQFDRKVREINSDRGTEFTNDQIEEYFISKGIHHILTSTQDHAANGRAERYIRTIVTDATTLLRQSNLRVKFWEYAVTSATNIRNCLEHKSTGKLPLKAISRQPVTVRLMSFLPFGEKGIIWNHNHKKLKPSGLPSIILCKDPNSYGYKFFIPSKNKIVTSDNYTIPNYTMDGRVRNTQNIYKSHQFSSHNDNEEDQIETVTNLCEALENYEDDNKPITRLEDLFTEEELSQIDSNAKYPSPSNNLEGDLDYVFSDVEESGDYDVESELSTTNTSISTDKNKILSNKDFNSELASTEISISEIDKKGLINTSHIDEDKYDEKVHRIPSIIQEKLVGSKNTIKINDENRISDRIRSKNIGSILNTGLSRCVDITDESITNKDESMHNAKPELIQEQFNKTNHETSFPKEGSIGTKCKIPKYRQ

2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.-

DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; transposition [GO:0032196]

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

aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]

PF00665;

3.30.420.10;

PTM: Proteolytically processed into capsid protein (CA), Ty4 protease (PR), integrase (IN) and reverse transcriptase/ribonuclease H (RT) proteins (By similarity). Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein, and this cleavage is a prerequisite for subsequent processing at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs. {ECO:0000250}.

SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.

CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;

FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. {ECO:0000250}.; FUNCTION: The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP. {ECO:0000250}.; FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends. {ECO:0000250}.; FUNCTION: Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome. {ECO:0000250}.

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

A0A0B7P9G0

UEX_DROME

MNTYFISFITIIIFANGINGTSVDTSNKLLLQKANDFNLSQNLSSSRTRRTIANSFRIVGIRLEDETVETKNGIPTVLVDKEQQFRVFGSGLEENTAITFTNEKNDYGGPCLKPATDLFTPIEVSSNGFSALYSVKFPSFINEFFICAKTAEKTTNHSKAATTTPLEHQGNSDFLKIKTFEPLIPVWLAIIIIVTCLGFSALFSGLNLGLMSMDRTELKILRNTGTEKEKKYASKIAPVRDQGNYLLCSILLGNVLVNSTFTILLDGLTSGLFAVIFSTLAIVLFGEITPQAVCSRHGLAIGAKTILVTKTVMAITAPLSYPVSRILDKLLGEEIGNVYNRERLKELVRVTNDVNDLDKNEVNIISGALELRKKTVADVMTHINDAFMLSLDALLDFETVSEIMNSGYSRIPVYDGDRKNIVTLLYIKDLAFVDTDDNTPLKTLCEFYQNPVHFVFEDYTLDIMFNQFKEGTIGHIAFVHRVNNEGDGDPFYETVGLVTLEDVIEELIQAEIVDETDVFVDNRTKTRRNRYKKADFSAFAERREVQTVRISPQLTLATFQYLSTAVDAFKKDVISELILRRLLNQDVFHNIKTKGKSKDDPSLYIFTQGKAVDFFVLILEGRVEVTIGKEALMFESGPFTYFGTQALVPNVVIDSPTQMGSLQSLNMDSKIRQSFVPDYSVRAISDVIYITIKRVLYLTAKKATLLEKSRKSGTFSSETFDDEVERLLHSITENEKPSCFAQNQSTRRLSNRSINSSPTNMNRSPDFVYNSVDEAIQDDTKLKNIKHADNVTTSISLVAAELEDLHSGEQDTTAASMPLLPKLDDKFESKQSKP

cellular response to carbon dioxide [GO:0071244]; export across plasma membrane [GO:0140115]; intracellular manganese ion homeostasis [GO:0030026]; intracellular monoatomic ion homeostasis [GO:0006873]; long-term memory [GO:0007616]; magnesium ion homeostasis [GO:0010960]; magnesium ion transmembrane transport [GO:1903830]

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

magnesium ion transmembrane transporter activity [GO:0015095]; transmembrane transporter activity [GO:0022857]

PF01595;

3.10.580.10;2.60.120.10;

ACDP family

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31404830}; Multi-pass membrane protein {ECO:0000255}.

FUNCTION: Probable metal transporter (By similarity). Acts downstream of PRL-1 and protects the nervous system against olfactory carbon dioxide stimulation (PubMed:31404830). {ECO:0000250|UniProtKB:Q3TWN3, ECO:0000269|PubMed:31404830}.

Drosophila melanogaster (Fruit fly)

A0A0C3RR82

PGMA1_PHLG1

MSSASSDSNTGSLTIAGSGIASVRHMTLETLAHVQEADIVFYVVADPVTEAYIKKNARGPCKDLEVLFDKDKVRYDTYVQMAETMLNAVREGQKVLGIFYGHPGVFVSPSRRALSIARKEGYQAKMLPGISSEDYMFADLEFDPAVHGCCAYEATQLLLREVSLDTAMSNIIWQVGGVGVSKIDFENSKVKLLVDRLEKDFGPDHHVVHYIGAVLPQSATVQDVLKISDLRKEEIVAQFNSCSTLYVPPLTHANKFSGNMVKQLFGQDVTEVSSALCPTPKWAAGSHLGDVVEYGPREKAAVDALVEHTVPADYRVLGGSLAFQQFMIDLALRPAIQANYKENPRALVDATKGLTTVEQAALLLRQPGAVFGVMKLRASEVANEQGHPVAPASLDHVAFTAPSPASLDHVAFSAPNPASLDHVAFIAPTPASLDHVAFSAPTPASLDHVSFGTPTSASLDHVAFEAPVPASLDHVAFAAPVPASLDHVAFAAPTPASLDHVAFAAPTPASLDHVAFAVPVPASLDHIAFSVPTPASLDHVAFAVPVPDHVAGIPCM

2.1.1.-

methylation [GO:0032259]

methyltransferase activity [GO:0008168]

PF00590;

Precorrin methyltransferase family

PTM: PgiMA1 automethylates at Asp-421, Asp-434, Asp-447, Asp-460, Asp-473, Asp-486, Asp-499, Asp-512, Asp-525 and Asp-538 before being processed, probably by the M64 family peptidase found in the genes surrounding PgiMA1, to release methylated peptides which then undergos macrocyclization with the N-terminus of the modified core peptides (PubMed:31117659). Peptide backbone alpha-N-methylations change the physicochemical properties of amide bonds to provide structural constraints and other favorable characteristics including biological membrane permeability to peptides (Probable). {ECO:0000269|PubMed:31117659, ECO:0000305}.

PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:31117659}.

FUNCTION: Fusion protein of the methyltransferase pgiM1 and 12 type II borosin core peptides; part of the gene cluster that mediates the biosynthesis of a type II borosin, a highly methylated cyclic peptide with potent biological activities (PubMed:31117659). Type II borosins derive from the C-terminus of the fusion protein, and it is the same protein that methylates its own C-terminus using S-adenosyl methionine (SAM) (PubMed:31117659). The C-terminus is subsequently cleaved off and macrocyclized by a prolyloligopeptidase to give the final product (By similarity). {ECO:0000250|UniProtKB:A0A2R2JFI5, ECO:0000269|PubMed:31117659}.

Phlebiopsis gigantea (strain 11061_1 CR5-6) (White-rot fungus) (Peniophora gigantea)

A0A0C3VJP4

SCP1_MEDTR

MEKVSLYACLILNLSLLVIFPYSKASQADKLNEFILSRKSQNPPKTLSWEEGDALKTLFSSAAYVAPPQEELRLADKIVTLPGQPYGVNFDQYSGYVTVDPETGRELFYYFVESPCNSSTKPLVLWLNGGPGCSSLGYGAFQELGPFRVNSDGKTLYRNPYAWNEVANVLFLESPAGIGFSYSNTTSDYDKSGDKSTAKDSYVFLINWLERFPQYKTRDFYISGESYAGHYVPQLASTILHNNKLYKNTIINLKGISLGNAWIDDATSLKGLYDNLWTHALNSDQTHELIEKYCDFTKQNYSAICTNAMNMSMIEKGKIDSFNIYAPLCHDSTLKNGSTGYVSNDLDPCSDYYGTAYLNRPEVQKALHAKPTNWSHCSDSINLNWKDSPITILPTIKYLIDNGIKLWIYSGDTDAVGVTISRYPINTLKLPIDSTWRPWYSGKEIGGYVVGYKGLTFVTVRGAGHLVPSWQPERALTLISSFLYGILPASVSPSN

3.4.16.-

arbuscular mycorrhizal association [GO:0036377]; proteolysis [GO:0006508]; response to symbiotic fungus [GO:0009610]

apoplast [GO:0048046]; extracellular space [GO:0005615]; vacuole [GO:0005773]

serine-type carboxypeptidase activity [GO:0004185]

PF00450;

3.40.50.11320;6.10.250.940;3.40.50.1820;

Peptidase S10 family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23662629}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:23662629}.

FUNCTION: Carboxypeptidase that, together with KPI106, controls mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis). {ECO:0000269|PubMed:23662629}.

Medicago truncatula (Barrel medic) (Medicago tribuloides)

A0A0C5B5G6

MOTSC_HUMAN

MRWQEMGYIFYPRKLR

activation of protein kinase activity [GO:0032147]; negative regulation of phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity [GO:2001145]; osteoblast differentiation [GO:0001649]; osteoblast proliferation [GO:0033687]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; purine-containing compound biosynthetic process [GO:0072522]; regulation of carbohydrate utilization [GO:0043610]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal muscle tissue growth [GO:0048630]

extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleus [GO:0005634]

DNA binding [GO:0003677]; DNA-binding transcription factor binding [GO:0140297]

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25738459}. Mitochondrion {ECO:0000269|PubMed:29983246}. Nucleus {ECO:0000269|PubMed:29983246, ECO:0000269|PubMed:33473109}. Note=Translocates to the nucleus in response to metabolic stress in an AMPK-dependent manner. {ECO:0000269|PubMed:29983246}.

FUNCTION: Regulates insulin sensitivity and metabolic homeostasis (PubMed:25738459, PubMed:33468709). Inhibits the folate cycle, thereby reducing de novo purine biosynthesis which leads to the accumulation of the de novo purine synthesis intermediate 5-aminoimidazole-4-carboxamide (AICAR) and the activation of the metabolic regulator 5'-AMP-activated protein kinase (AMPK) (PubMed:25738459). Protects against age-dependent and diet-induced insulin resistance as well as diet-induced obesity (PubMed:25738459). In response to metabolic stress, translocates to the nucleus where it binds to antioxidant response elements (ARE) present in the promoter regions of a number of genes and plays a role in regulating nuclear gene expression in an NFE2L2-dependent manner and increasing cellular resistance to metabolic stress (PubMed:29983246). Increases mitochondrial respiration and levels of CPT1A and cytokines IL1B, IL6, IL8, IL10 and TNF in senescent cells (PubMed:29886458). Increases activity of the serine/threonine protein kinase complex mTORC2 and reduces activity of the PTEN phosphatase, thus promoting phosphorylation of AKT (PubMed:33554779). This promotes AKT-mediated phosphorylation of transcription factor FOXO1 which reduces FOXO1 activity, leading to reduced levels of MSTN and promotion of skeletal muscle growth (PubMed:33554779). Promotes osteogenic differentiation of bone marrow mesenchymal stem cells via the TGFB/SMAD pathway (PubMed:30468456). Promotes osteoblast proliferation and osteoblast synthesis of type I collagens COL1A1 and COL1A2 via the TGFB/SMAD pathway (PubMed:31081069). {ECO:0000269|PubMed:25738459, ECO:0000269|PubMed:29886458, ECO:0000269|PubMed:29983246, ECO:0000269|PubMed:30468456, ECO:0000269|PubMed:31081069, ECO:0000269|PubMed:33468709, ECO:0000269|PubMed:33554779}.

Homo sapiens (Human)

A0A0C5CJR8

APRA_PSEMA

MSKAKDKAIVSAAQASTAYSQIDSFSHLYDRGGNLTINGKPSYTVDQAATQLLRDGAAYRDFDGNGKIDLTYTFLTSASSSTMNKHGISGFSQFNAQQKAQAALAMQSWSDVANVTFTEKASGGDGHMTFGNYSSGQDGAAAFAYLPGTGAGYDGTSWYLTNNSYTPNKTPDLNNYGRQTLTHEIGHTLGLAHPGDYNAGEGAPTYNDATYGQDTRGYSLMSYWSESNTNQNFSKGGVEAYASGPLIDDIAAIQKLYGANYNTRAGDTTYGFNSNTGRDFLSATSNADKLVFSVWDGGGNDTLDFSGFTQNQKINLNEASFSDVGGLVGNVSIAKGVTIENAFGGAGNDLIIGNNAANVIKGGAGNDLIYGAGGADQLWGGAGNDTFVFGASSDSKPGAADKIFDFTSGSDKIDLSGITKGAGLTFVNAFTGHAGDAVLTYAAGTNLGTLAVDFSGHGVADFLVTTVGQAAVSDIVA

3.4.24.-

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q03023}; Note=Binds 8 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:Q03023}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q03023}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q03023};

collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]

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

calcium ion binding [GO:0005509]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270]

PF00353;PF00413;PF08548;

3.40.390.10;2.150.10.10;

Peptidase M10B family

SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|Ref.1};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. At higher temperatures, the activity decreases rapidly. Shows high enzyme activity with casein as a substrate under the storage conditions of UHT milk. Is highly thermostable. Withstands general ultra-high temperature (UHT) processing (138 degrees Celsius for 18 seconds) in skim milk, with 88% of the initial enzyme activity remaining after heating. The milk matrix has a protective effect on the enzyme activity during the thermal process. {ECO:0000269|Ref.1};

FUNCTION: Peptidase able to cleave azocasein and the milk substrates beta-casein and Na-caseinate. Can withstand UHT processing of milk, and is able to spoil UHT milk over the storage period. {ECO:0000269|Ref.1}.

Pseudomonas marginalis (Pseudomonas panacis)

A0A0C5PHQ7

ELOV5_TACFU

MEILNQRLNQQFDSWMGPRDPRVRGWLLLDNYLPTLSFTIIYLLIVWMGPKYMRNRQPVSCRGILVVYNMALTLLSLYMFYELVTAVWQGGYNFFCQDTHSGGEADNRVINVLWWYYFSKLIEFMDTFFFILRKNNHQITFLHIYHHFTMLNIWWFVMNWVPCGHSYFGATFNSFIHVLMYSYYGLSAIPAIQPYLWWKKYITQGQLVQFVLTMIQTSCAVVWPCGFPKGWLYFQISYMITLIILFSNFYIQTYKKKGTAAKKDPRHNGIKSVNGHSNGASHTNAVKNRKARTD

2.3.1.199

fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; sphingolipid biosynthetic process [GO:0030148]; unsaturated fatty acid biosynthetic process [GO:0006636]; very long-chain fatty acid biosynthetic process [GO:0042761]

dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]

fatty acid elongase activity [GO:0009922]

PF01151;

ELO family, ELOVL5 subfamily

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03205}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000255|HAMAP-Rule:MF_03205}. Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. {ECO:0000255|HAMAP-Rule:MF_03205}.

CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000255|RuleBase:RU361115}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA = (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35379, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57363, ChEBI:CHEBI:57384, ChEBI:CHEBI:71481; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35380; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36523, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:74034, ChEBI:CHEBI:74054; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(11Z)-octadecenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39675, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:61540, ChEBI:CHEBI:76555; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = (11Z)-3-oxoicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36511, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:57387, ChEBI:CHEBI:74011; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; CATALYTIC ACTIVITY: Reaction=(11Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(13Z)-eicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39679, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:75121, ChEBI:CHEBI:76559; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39680; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z)-3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36503, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:57384, ChEBI:CHEBI:74012; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + H(+) + malonyl-CoA = (8Z,11Z,14Z,17Z)-3-oxoicosatetraenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35391, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:71489, ChEBI:CHEBI:71491; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35392; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H(+) + malonyl-CoA = (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36475, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57384, ChEBI:CHEBI:73852; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + H(+) + malonyl-CoA = (7Z,10Z,13Z,16Z,19Z)-3-oxodocosapentaenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36483, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:73862, ChEBI:CHEBI:73863; Evidence={ECO:0000250|UniProtKB:Q9NYP7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36484; Evidence={ECO:0000250|UniProtKB:Q9NYP7};

PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03205}.

FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate in the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators (By similarity). In conditions where the essential linoleic and alpha linoleic fatty acids are lacking it is also involved in the synthesis of Mead acid from oleic acid (By similarity). {ECO:0000250|UniProtKB:Q8BHI7, ECO:0000255|HAMAP-Rule:MF_03205}.

Tachysurus fulvidraco (Yellow catfish) (Pimelodus fulvidraco)

A0A0C5Q4Y6

C76H2_ROSOF

MDSFPLLAALFFILAATWFISFRRPRNLPPGPFPYPIVGNMLQLGTQPHETFAKLSKKYGPLMSIHLGSLYTVIVSSPEMAKEIMHKYGQVFSGRTVAQAVHACGHDKISMGFLPVGGEWRDMRKICKEQMFSHQSMEDSQWLRKQKLQQLLEYAQKCSERGRAIDIREAAFITTLNLMSATLFSMQATEFDSKVTMEFKEIIEGVASIVGVPNFADYFPILRPFDPQGVKRRADVYFGRLLAIIEGFLNERVESRRTNPNAPKKDDFLETLVDTLQTNDNKLKTDHLTHLMLDLFVGGSETSTTEIEWIMWELLANPEKMAKMKAELKSVMGEEKVVDESQMPRLPYLQAVVKESMRLHPPGPLLLPRKAESDQVVNGYLIPKGAQVLINAWAIGRDHSIWKNPDSFEPERFLDQKIDFKGTDYELIPFGSGRRVCPGMPLANRILHTVTATLVHNFDWKLERPEASDAHRGVLFGFAVRRAVPLKIVPFKV

1.14.14.-; 1.14.14.175; 1.14.14.60

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q94IP1};

diterpenoid biosynthetic process [GO:0016102]

membrane [GO:0016020]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]

PF00067;

1.10.630.10;

Cytochrome P450 family

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

CATALYTIC ACTIVITY: Reaction=abieta-8,11,13-triene + O2 + reduced [NADPH--hemoprotein reductase] = ferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48080, 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:78274, ChEBI:CHEBI:86062; EC=1.14.14.175; Evidence={ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48081; Evidence={ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}; CATALYTIC ACTIVITY: Reaction=ferruginol + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxyferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55428, 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:78274, ChEBI:CHEBI:138942; EC=1.14.14.60; Evidence={ECO:0000269|PubMed:27703160}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55429; Evidence={ECO:0000269|PubMed:27703160}; CATALYTIC ACTIVITY: Reaction=miltiradiene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 11-oxomiltiradiene + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:66796, 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:65037, ChEBI:CHEBI:167496; Evidence={ECO:0000250|UniProtKB:A0A0S1TP26}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66797; Evidence={ECO:0000250|UniProtKB:A0A0S1TP26};

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

FUNCTION: Monooxygenase involved in the biosynthesis of labdane-related diterpenes natural products (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of abietatriene to produce ferruginol (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of ferruginol at C-12 to produce 11-hydroxyferruginol (PubMed:27703160). Ferruginol and 11-hydroxyferruginol are intermediates in the biosynthesis of carnosate, a potent antioxidant (PubMed:26020634, PubMed:27703160). May also convert miltiradiene into 11-oxomiltiradiene (By similarity). {ECO:0000250|UniProtKB:A0A0S1TP26, ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}.

Rosmarinus officinalis (Rosemary) (Salvia rosmarinus)

A0A0C5QRZ2

C76H2_SALFT

MDPFPLVAAALFIAATWFITFKRRRNLPPGPFPYPIVGNMLQLGSQPHETFAKLSKKYGPLMSIHLGSLYTVIISSPEMAKEIMHKYGQVFSGRTIAQAVHACDHDKISMGFLPVGAEWRDMRKICKEQMFSHQSMEDSQNLRKQKLQQLLEYAQKCSEEGRGIDIREAAFITTLNLMSATLFSMQATEFDSKVTMEFKEIIEGVASIVGVPNFADYFPILRPFDPQGVKRRADVYFGRLLGLIEGYLNERIEFRKANPNAPKKDDFLETLVDALDAKDYKLKTEHLTHLMLDLFVGGSETSTTEIEWIMWELLASPEKMAKVKAELKSVMGGEKVVDESMMPRLPYLQAVVKESMRLHPPGPLLLPRKAESDQVVNGYLIPKGAQVLINAWAMGRDPSLWKNPDSFEPERFLDQKIDFKGTDYELIPFGSGRRVCPGMPLANRILHTVTATLVHNFDWKLERPEASDAHKGVLFGFAVRRAVPLKIVPIKA

1.14.14.-; 1.14.14.175; 1.14.14.60

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q94IP1};

diterpenoid biosynthetic process [GO:0016102]

membrane [GO:0016020]

heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]

PF00067;

1.10.630.10;

Cytochrome P450 family

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

CATALYTIC ACTIVITY: Reaction=abieta-8,11,13-triene + O2 + reduced [NADPH--hemoprotein reductase] = ferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48080, 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:78274, ChEBI:CHEBI:86062; EC=1.14.14.175; Evidence={ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48081; Evidence={ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}; CATALYTIC ACTIVITY: Reaction=ferruginol + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxyferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55428, 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:78274, ChEBI:CHEBI:138942; EC=1.14.14.60; Evidence={ECO:0000269|PubMed:27703160}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55429; Evidence={ECO:0000269|PubMed:27703160}; CATALYTIC ACTIVITY: Reaction=miltiradiene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 11-oxomiltiradiene + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:66796, 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:65037, ChEBI:CHEBI:167496; Evidence={ECO:0000250|UniProtKB:A0A0S1TP26}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66797; Evidence={ECO:0000250|UniProtKB:A0A0S1TP26};

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

FUNCTION: Monooxygenase involved in the biosynthesis of labdane-related diterpenes natural products (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of abietatriene to produce ferruginol (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of ferruginol at C-12 to produce 11-hydroxyferruginol (PubMed:27703160). Ferruginol and 11-hydroxyferruginol are intermediates in the biosynthesis of carnosate, a potent antioxidant (PubMed:26020634, PubMed:27703160). May also convert miltiradiene into 11-oxomiltiradiene (By similarity). {ECO:0000250|UniProtKB:A0A0S1TP26, ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}.

Salvia fruticosa (Greek sage)

A0A0C5XL88

PART_SPHYB

MTTSFWRIATDARTYEADDLSGAGAKITGGRWNEVGVAIVYAASSRALACLETVVHLNSGGLPLNRYLVEIEVPDEVLASAEVATPGNLPVGWDAEPAGRVSISFGSQWAQSQRTALLLVPSVIVPEETNLLINPAHPDAKGIKARKVRKWLYDPRMIRKA

2.4.2.-

glycosyltransferase activity [GO:0016757]; nucleotidyltransferase activity [GO:0016779]

PF08808;

MbcT/ParT/Res family

PTM: Consumes NAD(+) and auto-ADP-ribosylates on the tryptic fragment Ala-47-Arg-66 in vitro. Also auto-ADP-ribosylates using NADP(+). {ECO:0000269|PubMed:30598453}.

FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Expression in E.coli inhibits cell growth; bacteriostasis is neutralized by expression of cognate antitoxin ParS. ADP-ribosylates E.coli ribose-phosphate pyrophosphokinase (RPPK, prs) using NAD(+) in vitro; ADP-ribosylates RPPK on 'Lys-182' and 'Ser-202'. Cannot use NADP(+). Also auto-ADP-ribosylates in vitro; in the presence of RPPK auto-ADP-ribosylation decreases. {ECO:0000269|PubMed:30598453}.

Sphingobium sp. (strain YBL2)

A0A0C6DRW4

DSZC1_RHOER

MTLSPEKQHVRPRDAADNDPVAVARGLAEKWRATAVERDRAGGSATAEREDLRASGLLSLLVPREYGGWGADWPTAIEVVREIAAADGSLGHLFGYHLTNAPMIELIGSQEQEEHLYTQIAQNNWWTGNASSENNSHVLDWKVRATPTEDGGYVLNGTKHFCSGAKGSDLLFVFGVVQDDSPQQGAIIAAAIPTSRAGVTPNDDWAAIGMRQTDSGSTDFHNVKVEPDEVLGAPNAFVLAFIQSERGSLFAPIAQLIFANVYLGIAHGALDAAREYTRTQARPWTPAGIQQATEDPYTIRSYGEFTIALQGADAAAREAAHLLQTVWDKGDALTPEDRGELMVKVSGVKALATNAALNISSGVFEVIGARGTHPRYGFDRFWRNVRTHSLHDPVSYKIADVGKHTLNGQYPIPGFTS

1.14.14.21

dibenzothiophene catabolic process [GO:0018896]; leucine catabolic process [GO:0006552]

cytoplasm [GO:0005737]

flavin adenine dinucleotide binding [GO:0050660]; isovaleryl-CoA dehydrogenase activity [GO:0008470]; monooxygenase activity [GO:0004497]

PF08028;PF02770;PF02771;

1.10.540.10;2.40.110.10;1.20.140.10;

DszC flavin monooxygenase family

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|Ref.2}.

CATALYTIC ACTIVITY: Reaction=dibenzothiophene + 2 FMNH2 + 2 O2 = dibenzothiophene 5,5-dioxide + 2 FMN + 2 H(+) + 2 H2O; Xref=Rhea:RHEA:49072, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23681, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90356; EC=1.14.14.21; Evidence={ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=dibenzothiophene + FMNH2 + O2 = dibenzothiophene 5-oxide + FMN + H(+) + H2O; Xref=Rhea:RHEA:49076, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23681, ChEBI:CHEBI:23683, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000305|Ref.2}; CATALYTIC ACTIVITY: Reaction=dibenzothiophene 5-oxide + FMNH2 + O2 = dibenzothiophene 5,5-dioxide + FMN + H(+) + H2O; Xref=Rhea:RHEA:49080, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23683, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90356; Evidence={ECO:0000305|Ref.2};

PATHWAY: Sulfur metabolism; dibenzothiophene degradation. {ECO:0000305|PubMed:25627402}.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|Ref.2};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|Ref.2};

FUNCTION: Catalyzes the first step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Sulfur dioxygenase which converts DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner (PubMed:11229908, Ref.2). Also acts on thioxanthen-9-one and 4,6-dimethyl DBT and 2,8-dimethyl DBT (Ref.2). {ECO:0000269|PubMed:11229908, ECO:0000269|Ref.2}.

Rhodococcus erythropolis (Arthrobacter picolinophilus)

A0A0D1DWQ2

CMU1_USTMA

MKLSVSIFVLLAVSAFGGGSAAAVSGKSEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGGRAPSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTRPLPPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPTNMDEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVLLGYPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLTDHKQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRLFQAYLIPITTQIEAAAILDHANKCT

5.4.99.5

aromatic amino acid family biosynthetic process [GO:0009073]; chorismate metabolic process [GO:0046417]; effector-mediated suppression of host salicylic acid-mediated innate immune signaling [GO:0140502]

extracellular region [GO:0005576]; host apoplast [GO:0140593]; host cell cytosol [GO:0044164]

chorismate mutase activity [GO:0004106]

1.10.590.10;

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21976020}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:21976020}. Note=Is translocated to host plant cells and spreads to neighboring tissue. The spreading is likely to occur through plasmodesmata. {ECO:0000269|PubMed:21976020}.

CATALYTIC ACTIVITY: Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000269|PubMed:21976020, ECO:0000269|PubMed:30651637}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898; Evidence={ECO:0000269|PubMed:21976020, ECO:0000269|PubMed:30651637};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 mM for chorismate {ECO:0000269|PubMed:30651637}; Vmax=40.8 umol/min/mg enzyme {ECO:0000269|PubMed:30651637}; Vmax=21.1 umol/min/mg enzyme (when bound to host KWL1) {ECO:0000269|PubMed:30651637};

FUNCTION: Secreted chorismate mutase that is one component of a cocktail of effectors shaping the host metabolome and acting as virulence factors. The enzyme is taken up by plant cells, can spread to neighboring cells where it affects the biosynthesis of the plant immune signal salicylic acid by channelling chorismate into the phenylpropanoid pathway (PubMed:21976020, PubMed:30651637). Interferes with the activity of host cytosolic chorismate mutase CM2 through heterodimerization (PubMed:21976020). {ECO:0000269|PubMed:21976020, ECO:0000269|PubMed:30651637}.

Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)