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
//