ID   A0A2K5JKY5_COLAP        Unreviewed;       503 AA.
AC   A0A2K5JKY5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000029525.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000029525.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O
CC         = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-
CC         glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-
CC         COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623;
CC         Evidence={ECO:0000256|ARBA:ARBA00029302};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC         Evidence={ECO:0000256|ARBA:ARBA00029302};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   RefSeq; XP_011781627.1; XM_011926237.1.
DR   AlphaFoldDB; A0A2K5JKY5; -.
DR   STRING; 336983.ENSCANP00000029525; -.
DR   Ensembl; ENSCANT00000052695.1; ENSCANP00000029525.1; ENSCANG00000038386.1.
DR   GeneID; 105500647; -.
DR   CTD; 84871; -.
DR   OMA; LRLWFNF; -.
DR   OrthoDB; 168164at2759; -.
DR   Proteomes; UP000233080; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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   CDD; cd06908; M14_AGBL4_like; 1.
DR   Gene3D; 2.60.40.3120; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR040626; Pepdidase_M14_N.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR12756:SF9; CYTOSOLIC CARBOXYPEPTIDASE 6; 1.
DR   Pfam; PF18027; Pepdidase_M14_N; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233080}.
FT   DOMAIN          169..421
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
FT   REGION          459..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  58287 MW;  5852643335477B0C CRC64;
     MAEGSQTAPE AGNDMGNDDA IGGNVSKYIV LPTGYCGQPK KGHLLFDACF ESGNLGRVDQ
     VSEFEYDLFI RPDTCNPRFR VWFNFTVENV KESQRVIFNI VNFSKTKSLY RDGMAPMVKS
     TSRPKWQRLP PKNVYYYRCP DHRKNYVMSF AFCFDREEDT YQFAYCYPYT YTRFQHYLDS
     LQKRNMDYFF REQLGQSVQQ RQLDLLTITS PDNLREGAEQ KVVFITGRVH PGETPSSFVC
     QGIIDFLVSQ HPIARVLREY LVFKIAPMLN PDGVYLGNYR CSLMGFDLNR HWLDPSPWVH
     PTLHGVKQLI VQMYNDPKTS LEFYIDIHAH STMMNGFMYG NIFEDEERFQ RQAIFPKLLC
     QNAEDFSYSS TSFNRDAVKA GTGRRFLGGL LDHTSYCYTL EVSFYSYIIS GTTAAVPYTE
     EAYMKLGRNV ARTFLDYYRL NPMVEKVAIP MPRLRNKEIE VQRRKEKSPP YKHPLLRGPA
     SNYPNGKGDK KSSVNHKDPS TPF
//