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Database: UniProt
Entry: A0A3Q3WHT8_MOLML
LinkDB: A0A3Q3WHT8_MOLML
Original site: A0A3Q3WHT8_MOLML 
ID   A0A3Q3WHT8_MOLML        Unreviewed;       438 AA.
AC   A0A3Q3WHT8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00132, ECO:0000259|PROSITE:PS00133};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000011782.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000011782.1}
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; A0A3Q3WHT8; -.
DR   STRING; 94237.ENSMMOP00000011782; -.
DR   Ensembl; ENSMMOT00000011982.1; ENSMMOP00000011782.1; ENSMMOG00000009048.1.
DR   OMA; DTIYSWM; -.
DR   Proteomes; UP000261620; 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:UniProtKB-KW.
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:SF155; CARBOXYPEPTIDASE A4-RELATED; 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   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:UP000261620};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          189..211
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
FT   DOMAIN          325..335
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
SQ   SEQUENCE   438 AA;  49827 MW;  E1E9E930F6BE0CAF CRC64;
     MALQSIIVSL QQSKKTDKTR FDLHFAVNSN VSLRDGFLSR DQVIRINAQS QEQIQLLQVL
     GTRQQEEELD FWLHPVSTEL PVDIRVPRSS LTFVKEYLHI HGIPYSVMIN DLQELLDEEK
     AEMEMNQMKE RSTRSFNFGA YHPLETIYSW MDTLVAKNPN LVTKQEIGKS YEGRPMYVLK
     FSTGGNKRPA IWIDTGIHSR EWVSQATGVW TANKIATDYG TDPSLTSLLS TMDIYLLILA
     NPDGYAYTHN KDRMWRKTRS KNPGSQCMGV DPNRNWDADF AGPGASKDPC SESYHGPSVH
     SEMEVLNVVN LIKNHGNIKS FISVHAYSQL LLYPYGYCCR NIDDQVELEA VGQAAVQKLT
     SLYGTRYKVG SICNTIYPAS GSSIDWSYDL GIKYSYAFEL RDTGRYGFIL PANQIIPTAS
     ETWLALKHIM EHVRDHPY
//
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