GenomeNet

Database: UniProt
Entry: A0A3Q3AF34_KRYMA
LinkDB: A0A3Q3AF34_KRYMA
Original site: A0A3Q3AF34_KRYMA 
ID   A0A3Q3AF34_KRYMA        Unreviewed;       422 AA.
AC   A0A3Q3AF34;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Carboxypeptidase A1 {ECO:0000256|ARBA:ARBA00040642};
DE            EC=3.4.17.1 {ECO:0000256|ARBA:ARBA00039144};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000014740.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000014740.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid, but little or no action
CC         with -Asp, -Glu, -Arg, -Lys or -Pro.; EC=3.4.17.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00036253};
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}.
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   RefSeq; XP_017292307.1; XM_017436818.1.
DR   AlphaFoldDB; A0A3Q3AF34; -.
DR   STRING; 37003.ENSKMAP00000014740; -.
DR   Ensembl; ENSKMAT00000014954.1; ENSKMAP00000014740.1; ENSKMAG00000011054.1.
DR   GeneID; 108248203; -.
DR   KEGG; kmr:108248203; -.
DR   CTD; 93979; -.
DR   GeneTree; ENSGT00940000158082; -.
DR   OMA; SHGISYE; -.
DR   OrthoDB; 3540647at2759; -.
DR   Proteomes; UP000264800; Unplaced.
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; cd03870; M14_CPA; 1.
DR   Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR034248; CPA_M14_CPD.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF94; CARBOXYPEPTIDASE A1; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   Pfam; PF02244; Propep_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..422
FT                   /note="Carboxypeptidase A1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018598908"
FT   DOMAIN          173..195
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
FT   DOMAIN          309..319
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
FT   COILED          80..111
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   422 AA;  48131 MW;  6D0F7B72A62AFE22 CRC64;
     MMRGMLTFAA LFVVVLAKET FEGHQVLRII PKNDIQLSLI KDLEKMIEFE LDIWMRVTNI
     FSPVDVRVPS HTLQSFKSYL ENLNIEYATM IENLQAILDE EQEEMDSAAR VAQPKHTDSF
     DYTRYHPINE IYSFQNMLVA ENPNLVSKIV IGQSYEGRPL NVLKFSTGGT NHPAIWIDTG
     IHSREWVTQA SGIWFAKKIV KEYGRDPALT AILNNMDIFL EIVTNPDGYY YTHTSNRMWR
     KTRKPNSGSS CIGVDPNRNW DAGFGGPGAS SYPCSETYCG PRAHSESEVK SIVDFVKSHG
     NIKAFISIHS YSQMLMYPYG YTRTPVKDQA ELHQLAQKAI TDLASLYGTR YRYGSIINTI
     YQASGGTIDW TYNQGVKYSY TFELRDTGRY GFLLPANQIV PTAEETWLAL MAIMDHTYKN
     PY
//
DBGET integrated database retrieval system