ID   A0A1I8EX10_WUCBA        Unreviewed;       433 AA.
AC   A0A1I8EX10;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Peptidase_M14 domain-containing protein {ECO:0000313|WBParaSite:maker-PairedContig_5624-snap-gene-4.17-mRNA-1};
OS   Wuchereria bancrofti.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX   NCBI_TaxID=6293 {ECO:0000313|WBParaSite:maker-PairedContig_5624-snap-gene-4.17-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-PairedContig_5624-snap-gene-4.17-mRNA-1}
RP   IDENTIFICATION.
RC   STRAIN=pt0022
RC   {ECO:0000313|WBParaSite:maker-PairedContig_5624-snap-gene-4.17-mRNA-1};
RG   WormBaseParasite;
RL   Submitted (NOV-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}.
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   AlphaFoldDB; A0A1I8EX10; -.
DR   STRING; 6293.A0A1I8EX10; -.
DR   WBParaSite; maker-PairedContig_5624-snap-gene-4.17-mRNA-1; maker-PairedContig_5624-snap-gene-4.17-mRNA-1; maker-PairedContig_5624-snap-gene-4.17.
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   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..433
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009318444"
FT   DOMAIN          194..216
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
SQ   SEQUENCE   433 AA;  49406 MW;  D63408507C892D37 CRC64;
     MLAIFAVLFT VLHLRYMCSA IQQYRGYSLL RFPTATTDWL DQIEADSLVL NNANVINFLE
     PKRILVDIWA KPNMYRNHAD VLVAPEYLDS FLALLRMRGV SDIQIVANDI QKEIDRERRD
     LAYAMKYRSR RSVGDNSLAN FNLIAYHRYD EIVDYLRKLS RLHPNLAEIF NVTKTYEGRD
     LIGIKIGSRS SFKPAIFIDA GIHAREWIAP AVALYIITKL VTEYGKDSNL THMTDKFDWY
     IVPVANPDGY EYSMTTDRLW RKTRSRNVTV NKWCVGADAN RNWGYRWGEA GASRSPCSNI
     YPGSTAFSEV YVSLHSYGQL FLAPWGYTND RPNNYYDQKQ AASLAVEAIR KRTDPASGTS
     IDYMQDKGVP YIYGIELRPE DADNNFGFTI PARFIEPTGQ LVTSALALGK YVPFLDMSES
     IVGIIPKVST VRL
//