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Database: UniProt
Entry: A0A0L8GC35_OCTBM
LinkDB: A0A0L8GC35_OCTBM
Original site: A0A0L8GC35_OCTBM 
ID   A0A0L8GC35_OCTBM        Unreviewed;       406 AA.
AC   A0A0L8GC35;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=N-acyl-aliphatic-L-amino acid amidohydrolase {ECO:0000256|ARBA:ARBA00011913};
DE            EC=3.5.1.14 {ECO:0000256|ARBA:ARBA00011913};
DE   AltName: Full=N-acyl-L-amino-acid amidohydrolase {ECO:0000256|ARBA:ARBA00029656};
GN   ORFNames=OCBIM_22036825mg {ECO:0000313|EMBL:KOF74085.1};
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:KOF74085.1};
RN   [1] {ECO:0000313|EMBL:KOF74085.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF74085.1};
RC   TISSUE=Gonad {ECO:0000313|EMBL:KOF74085.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036696-2};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR036696-
CC       2};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; KQ422866; KOF74085.1; -; Genomic_DNA.
DR   RefSeq; XP_014782659.1; XM_014927173.1.
DR   AlphaFoldDB; A0A0L8GC35; -.
DR   STRING; 37653.A0A0L8GC35; -.
DR   EnsemblMetazoa; Ocbimv22036825m; Ocbimv22036825m.p; Ocbimv22036825m.g.
DR   EnsemblMetazoa; XM_014927173.1; XP_014782659.1; LOC106878078.
DR   GeneID; 106878078; -.
DR   KEGG; obi:106878078; -.
DR   OMA; GTDAKQF; -.
DR   OrthoDB; 158507at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004046; F:aminoacylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05646; M20_AcylaseI_like; 1.
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; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR010159; N-acyl_aa_amidohydrolase.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01880; Ac-peptdase-euk; 1.
DR   PANTHER; PTHR45892; AMINOACYLASE-1; 1.
DR   PANTHER; PTHR45892:SF1; AMINOACYLASE-1; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF036696; ACY-1; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036696-2};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR036696-2}.
FT   DOMAIN          192..302
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        86
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         377
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
SQ   SEQUENCE   406 AA;  46124 MW;  3E1DB8B432537E00 CRC64;
     MGSETERRNP SAEHQAVTNF RRYLRIKTVQ PEPDYDGAIK FLKEMAGELG LPYKVIEVSP
     GNPVFVMTVE GKDPSLPSLM LNSHIDVVPV DMDCWKVDPF SAEKMENGDI YARGSQDMKC
     VGIQYIEAIR QLLKDGKKML RNVHLTFMPD EEVGGKLGMQ LFIKREEFKQ MNIAFALDEG
     LANPTEHFTI FYGERSAWWA KIKCPGNPGH GSRFIENTAA EKFRNIINKL LSLRDEEEKR
     LKSNPNLVLG DVTSVNLTMV EGGLQHNVVP SRFTVCFDIR VPPSVDPVQF EEKLNNLCKE
     AGEGLTLEYV QKGCDNKLTS IDDGNIWWKT FSSTFENMNL KIKTEIFPAG TDIRYLRELG
     YPALGFSPMN FTPILLHDHN EFLNENIFLK GIDIYYNLIS NLANVK
//
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