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Database: UniProt
Entry: A0A0N4WI42_HAEPC
LinkDB: A0A0N4WI42_HAEPC
Original site: A0A0N4WI42_HAEPC 
ID   A0A0N4WI42_HAEPC        Unreviewed;       331 AA.
AC   A0A0N4WI42;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Peptidase_M14 domain-containing protein {ECO:0000313|WBParaSite:HPLM_0001060201-mRNA-1};
GN   ORFNames=HPLM_LOCUS10594 {ECO:0000313|EMBL:VDO40595.1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Trichostrongyloidea; Haemonchidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001060201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0001060201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO40595.1, ECO:0000313|Proteomes:UP000268014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHpl1 {ECO:0000313|EMBL:VDO40595.1,
RC   ECO:0000313|Proteomes:UP000268014};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   EMBL; UZAF01017338; VDO40595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4WI42; -.
DR   STRING; 6290.A0A0N4WI42; -.
DR   WBParaSite; HPLM_0001060201-mRNA-1; HPLM_0001060201-mRNA-1; HPLM_0001060201.
DR   OMA; LVSMHTH; -.
DR   Proteomes; UP000038042; Unplaced.
DR   Proteomes; UP000268014; 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; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF59; PEPTIDASE_M14 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022645};
KW   Protease {ECO:0000256|ARBA:ARBA00022645};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268014};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..331
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5033230858"
FT   DOMAIN          29..294
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   331 AA;  38353 MW;  07F3DFE12713774B CRC64;
     MITYNTCLYL FTLIMTVGGE TPFFDLTRYN DFPEIEEYVR GVAKMNPEFV SLRLIGHSRE
     DRPLLGLKIT ADLQSKNISE TSEWPSFSIG IMLVQKYKID DKITAYVDSL DIYIFPVLNP
     DGFIFSRTST RAIIRQWRKN RAPENCTGSV GYLEDICCEG VDLNRNYDLG EPETRSVVEF
     CEIYGRLHAL VSMHTHGQLW ILPYNHHKRT YPEDFKELEK LAARAAQKVY SYRETKYRIG
     TAADMLGTAT GGATDWIKKN TPTKYVYVLE LPPDMSTWFA FQIKPHWLIP IGKETWMGIK
     VILDQVIEET ITERKRRMTQ NTSHISSRAR F
//
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