ID A0A158PA16_ANGCA Unreviewed; 400 AA.
AC A0A158PA16;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidase_M14 domain-containing protein {ECO:0000313|WBParaSite:ACAC_0000888501-mRNA-1};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000888501-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0000888501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) 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; A0A158PA16; -.
DR STRING; 6313.A0A158PA16; -.
DR WBParaSite; ACAC_0000888501-mRNA-1; ACAC_0000888501-mRNA-1; ACAC_0000888501.
DR Proteomes; UP000035642; Unassembled WGS sequence.
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; cd03860; M14_CP_A-B_like; 1.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF139; PEPTIDASE_M14 DOMAIN-CONTAINING PROTEIN; 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.
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:UP000035642};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 144..166
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
SQ SEQUENCE 400 AA; 45925 MW; 814D5635118D7B78 CRC64;
MRDFNGTLHL KATQRRRLLI DVWGMPSKRN PATDVLVAPE FLETFLNMLE KRGIHRVEML
KDDISRDILR ERRHLERSSR RAKRSFSAME FDVENYHSYN EMVDFMRKIA GERPDLVKLL
NISRSFEGRP LYGVKISASN SFKPAIFVDA GVHAREWIAP AAALYIIKKL VSEYGKDPTI
TSSLNRFDWY IIPQVNPDGY EYSRISDRLW RKTRSRNITI NKWCVGADAN RNWGHRWGEA
GANRSPCSNI YAGSRPFSEP EIVGLRDLVT WQIPNLVIYI SLHSYGQLLL SPWGYTQARP
DNYADQRRAA RIAVEAMRNA TGAIYNYGTI AELMYPASGT SIDYMQDRGV PYIFGVELRP
LDAYDTYAFS LPPRFIRPTG EEMLAGLIAL GDYATVHKKL
//
