ID A0A0L8G5U4_OCTBM Unreviewed; 445 AA. AC A0A0L8G5U4; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 03-MAY-2023, entry version 21. DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687}; GN ORFNames=OCBIM_22039473mg {ECO:0000313|EMBL:KOF72407.1}; OS Octopus bimaculoides (California two-spotted octopus). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda; OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus. OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF72407.1, ECO:0000313|Proteomes:UP000053454}; RN [1] {ECO:0000313|Proteomes:UP000053454} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Albertin C.B., Simakov O., Mitros T., Wang Z.Y., Pungot J.R., RA Edsinger-Gonzalez E., Brenner S., Ragsdale C.W., Rokhsar D.S.; RT "WGS assembly of Octopus bimaculoides."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + L-phenylalanine = H2O + N- CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-phenylalanine; CC Xref=Rhea:RHEA:51312, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, CC ChEBI:CHEBI:58095, ChEBI:CHEBI:134022; CC Evidence={ECO:0000256|ARBA:ARBA00034626}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51313; CC Evidence={ECO:0000256|ARBA:ARBA00034626}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51314; CC Evidence={ECO:0000256|ARBA:ARBA00034626}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-octadecenoate + L-phenylalanine = H2O + N-(9Z- CC octadecenoyl)-L-phenylalanine; Xref=Rhea:RHEA:51300, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:58095, CC ChEBI:CHEBI:134020; Evidence={ECO:0000256|ARBA:ARBA00034630}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51301; CC Evidence={ECO:0000256|ARBA:ARBA00034630}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51302; CC Evidence={ECO:0000256|ARBA:ARBA00034630}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-octadecenoate + glycine = H2O + N-(9Z- CC octadecenoyl)glycine; Xref=Rhea:RHEA:51316, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57305, ChEBI:CHEBI:133992; CC Evidence={ECO:0000256|ARBA:ARBA00034640}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51318; CC Evidence={ECO:0000256|ARBA:ARBA00034640}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-L- CC phenylalanine = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + L- CC phenylalanine; Xref=Rhea:RHEA:64132, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:58095, ChEBI:CHEBI:77016, ChEBI:CHEBI:149701; CC Evidence={ECO:0000256|ARBA:ARBA00034635}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64133; CC Evidence={ECO:0000256|ARBA:ARBA00034635}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine = CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycine; Xref=Rhea:RHEA:64108, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:57305, CC ChEBI:CHEBI:59002; Evidence={ECO:0000256|ARBA:ARBA00034637}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64109; CC Evidence={ECO:0000256|ARBA:ARBA00034637}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64110; CC Evidence={ECO:0000256|ARBA:ARBA00034637}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-serine = CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-serine; Xref=Rhea:RHEA:64116, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:149697; Evidence={ECO:0000256|ARBA:ARBA00034616}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64117; CC Evidence={ECO:0000256|ARBA:ARBA00034616}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64118; CC Evidence={ECO:0000256|ARBA:ARBA00034616}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-asparagine = (9Z)-octadecenoate + CC L-asparagine; Xref=Rhea:RHEA:64136, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:58048, ChEBI:CHEBI:149730; CC Evidence={ECO:0000256|ARBA:ARBA00034627}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64137; CC Evidence={ECO:0000256|ARBA:ARBA00034627}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-glutamine = (9Z)-octadecenoate + CC L-glutamine; Xref=Rhea:RHEA:51356, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:58359, ChEBI:CHEBI:134033; CC Evidence={ECO:0000256|ARBA:ARBA00034643}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51357; CC Evidence={ECO:0000256|ARBA:ARBA00034643}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-leucine = (9Z)-octadecenoate + L- CC leucine; Xref=Rhea:RHEA:51360, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:57427, ChEBI:CHEBI:134035; CC Evidence={ECO:0000256|ARBA:ARBA00034652}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51361; CC Evidence={ECO:0000256|ARBA:ARBA00034652}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51362; CC Evidence={ECO:0000256|ARBA:ARBA00034652}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-lysine = (9Z)-octadecenoate + L- CC lysine; Xref=Rhea:RHEA:64192, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:32551, ChEBI:CHEBI:149731; CC Evidence={ECO:0000256|ARBA:ARBA00034633}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64193; CC Evidence={ECO:0000256|ARBA:ARBA00034633}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-methionine = (9Z)-octadecenoate + CC L-methionine; Xref=Rhea:RHEA:64144, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57844, ChEBI:CHEBI:149732; CC Evidence={ECO:0000256|ARBA:ARBA00034645}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64145; CC Evidence={ECO:0000256|ARBA:ARBA00034645}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-serine = (9Z)-octadecenoate + L- CC serine; Xref=Rhea:RHEA:51352, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:33384, ChEBI:CHEBI:134031; CC Evidence={ECO:0000256|ARBA:ARBA00034646}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51353; CC Evidence={ECO:0000256|ARBA:ARBA00034646}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-tryptophan = (9Z)-octadecenoate + CC L-tryptophan; Xref=Rhea:RHEA:64176, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57912, ChEBI:CHEBI:149733; CC Evidence={ECO:0000256|ARBA:ARBA00034619}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64177; CC Evidence={ECO:0000256|ARBA:ARBA00034619}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(9Z-octadecenoyl)-L-tyrosine = (9Z)-octadecenoate + L- CC tyrosine; Xref=Rhea:RHEA:64184, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:58315, ChEBI:CHEBI:149734; CC Evidence={ECO:0000256|ARBA:ARBA00034625}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64185; CC Evidence={ECO:0000256|ARBA:ARBA00034625}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-hexadecanoyl-L-phenylalanine = hexadecanoate + L- CC phenylalanine; Xref=Rhea:RHEA:64124, ChEBI:CHEBI:7896, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:149699; CC Evidence={ECO:0000256|ARBA:ARBA00034620}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64125; CC Evidence={ECO:0000256|ARBA:ARBA00034620}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-octadecanoyl-L-phenylalanine = L-phenylalanine + CC octadecanoate; Xref=Rhea:RHEA:64128, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:25629, ChEBI:CHEBI:58095, ChEBI:CHEBI:149700; CC Evidence={ECO:0000256|ARBA:ARBA00034641}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64129; CC Evidence={ECO:0000256|ARBA:ARBA00034641}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha- CC amino acid; Xref=Rhea:RHEA:15565, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:29067, ChEBI:CHEBI:59869, ChEBI:CHEBI:59874; EC=3.5.1.14; CC Evidence={ECO:0000256|ARBA:ARBA00034644}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15566; CC Evidence={ECO:0000256|ARBA:ARBA00034644}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15567; CC Evidence={ECO:0000256|ARBA:ARBA00034644}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acyl-aromatic L-alpha-amino acid + H2O = a carboxylate + CC an aromatic L-alpha-amino acid; Xref=Rhea:RHEA:54184, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:84824, CC ChEBI:CHEBI:138093; EC=3.5.1.114; CC Evidence={ECO:0000256|ARBA:ARBA00034622}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54185; CC Evidence={ECO:0000256|ARBA:ARBA00034622}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54186; CC Evidence={ECO:0000256|ARBA:ARBA00034622}; CC -!- PATHWAY: Amino-acid metabolism. {ECO:0000256|ARBA:ARBA00034698}. CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism. CC {ECO:0000256|ARBA:ARBA00004872}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KQ423675; KOF72407.1; -; Genomic_DNA. DR RefSeq; XP_014783801.1; XM_014928315.1. DR AlphaFoldDB; A0A0L8G5U4; -. DR EnsemblMetazoa; Ocbimv22039474m; Ocbimv22039474m.p; Ocbimv22039473m.g. DR EnsemblMetazoa; XM_014928315.1; XP_014783801.1; LOC106878941. DR GeneID; 106878941; -. DR OrthoDB; 3672990at2759; -. DR Proteomes; UP000053454; Unassembled WGS sequence. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.150.900; -; 1. DR Gene3D; 3.30.70.360; -; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR InterPro; IPR036264; Bact_exopeptidase_dim_dom. DR InterPro; IPR047177; Pept_M20A. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1. DR PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF036696; ACY-1; 2. DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. PE 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000053454}. FT DOMAIN 184..325 FT /note="Peptidase M20 dimerisation" FT /evidence="ECO:0000259|Pfam:PF07687" SQ SEQUENCE 445 AA; 50429 MW; 4FFBB77CBF93E6E0 CRC64; MYVSVCLSKY RQRITDFKKR LSLETIYEAY PTVHKSPFVK YEVVANYSML YTVEGSDKKL LPYLLTSHLD VVPVTEENWK FDPFAAKLYQ GYIYGRGTLD VKCSVIGIME ALEHALKSGF KPKRSFFIAF GHDEEVTGYD GAYHIAQTLE SRGVQLEYLL DEGLAIVKDF FKGLHPVAMI GVVEKGQAIV KLSVNGTAGH SAIPPPESVI GILSTAIRRI ESNPQPDLFG TGAERAMFEH LAPKLPFLPR MVLSNLWLFR PVVSWVLSRQ PQTNALIRTV NAVTKFNAGI KDNVLSDSAE AVIDYRIHPS QTLEQLFDFH LKIINDDRVK TTLKNYIAPS LISPYDDASF GYHTVKNSIR EVFLDVLVVP GVTVGNTDTH HYKHLTKSIY RFTPSVLTPE STNMIHGDNE KISIWNYEKV VNFYHHVILN SDRDKMNFIN KHVEL //