ID A0A0V1PDH7_9BILA Unreviewed; 431 AA.
AC A0A0V1PDH7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Carboxypeptidase A6 {ECO:0000313|EMBL:KRZ94247.1};
DE Flags: Fragment;
GN Name=CPA6 {ECO:0000313|EMBL:KRZ94247.1};
GN ORFNames=T08_15528 {ECO:0000313|EMBL:KRZ94247.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ94247.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ94247.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ94247.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ94247.1}.
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DR EMBL; JYDM01000019; KRZ94247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1PDH7; -.
DR STRING; 92180.A0A0V1PDH7; -.
DR Proteomes; UP000054924; 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 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:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-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.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:KRZ94247.1};
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:UP000054924};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 133..415
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
FT NON_TER 431
FT /evidence="ECO:0000313|EMBL:KRZ94247.1"
SQ SEQUENCE 431 AA; 50323 MW; 66D9CEB5A12D7AA0 CRC64;
MFAEVSLFWT FIFASIFSAW NLNLYENYQL LQIQLLSQDD VNVLQKIVDV ESLEMDFWTP
LTDLDNYDKP IIAFVPPSSV NLLIESLETS KISYSNITDV FRKNFNNHVQ MLKDKKHKMK
TSKILSTFTL NEYHTLAEIH WYMQALSRKH PQIVKLINIG YSSEGRPLLA VKVGRKFTKN
SIWIDAGMHA REWIAPATAV YLLHELAENY ENTKEIQFIL NKYSFYILPV VNPDGYDYSW
KSERFWRKSR SKHNCTFWSC CVGVDLDRNF NISIDLRGHP CRPDYPGPFP FSESETRAVS
KFLSENQQHI LLAISLHSFG KLLTVPYSFK SDEVENSNFQ TYTARHFLQA TAFKNEFYTL
TQAYENYKFS IGQEMDWIRL FTNIPLAYSI KLPPTPNEPY GFLLPEDHIV PVSIQAFEGI
LNMVKSLNYV Y
//
