ID   A0A3Q3MJZ7_9TELE        Unreviewed;       383 AA.
AC   A0A3Q3MJZ7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Carboxypeptidase O-like {ECO:0000313|Ensembl:ENSMAMP00000021234.1};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000021234.1, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000021234.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   AlphaFoldDB; A0A3Q3MJZ7; -.
DR   STRING; 205130.ENSMAMP00000021234; -.
DR   Ensembl; ENSMAMT00000021777.2; ENSMAMP00000021234.1; ENSMAMG00000014257.2.
DR   GeneTree; ENSGT00940000161508; -.
DR   InParanoid; A0A3Q3MJZ7; -.
DR   OrthoDB; 3540647at2759; -.
DR   Proteomes; UP000261640; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF19; CARBOXYPEPTIDASE O; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022645};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022645};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..383
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018572385"
FT   TRANSMEM        352..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          92..114
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
SQ   SEQUENCE   383 AA;  43489 MW;  5A764C3D2A15E124 CRC64;
     MKIMLRWWIL GFFLLLNQGL QTSHGSLEGL ESTWSYDYTK YHPMPEIYNW MEDVQRENPD
     LVSSVVYGHT YEGRNITLLK LGLQNPERRE KKAIWMDCGI HAREWIAPAF CQWFIKELVH
     SYKNKKKMKR MLQNLDIYVT PVVNVDGYIF TWANDTTRRW RKSRSLPPPD SSCYGVDLNR
     NFNANWGTVG VSFDSCENNY CGKSPGSEPE AKAVMDFVGS MVNQLLCFLT IHSAGQLILL
     PYGHPEVSAP NYIELVSVGK EAAAEMKKVH GMNYTVGTSP QILYPNSGSS RDWARLMGIP
     FSYTFELRDK GEFSHLLPED QIQPACEEAY IGALSIITYV HDKTFNNTIP NAAVTTVTGL
     ITISGVAVMI WSTMIVLTAR ILV
//