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Database: UniProt
Entry: A0A0L8G698_OCTBM
LinkDB: A0A0L8G698_OCTBM
Original site: A0A0L8G698_OCTBM 
ID   A0A0L8G698_OCTBM        Unreviewed;       316 AA.
AC   A0A0L8G698;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=OCBIM_22039473mg {ECO:0000313|EMBL:KOF72408.1};
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:KOF72408.1};
RN   [1] {ECO:0000313|EMBL:KOF72408.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF72408.1};
RC   TISSUE=Gonad {ECO:0000313|EMBL:KOF72408.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
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   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; KQ423675; KOF72408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L8G698; -.
DR   EnsemblMetazoa; Ocbimv22039475m; Ocbimv22039475m.p; Ocbimv22039473m.g.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
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   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          184..316
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   316 AA;  35399 MW;  A65F698030412A5F 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 QTLEQV
//
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