ID   A0A0N5CHM3_STREA        Unreviewed;       182 AA.
AC   A0A0N5CHM3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Peptidase_M14 domain-containing protein {ECO:0000313|WBParaSite:SPAL_0001733700.1};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001733700.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0001733700.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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; A0A0N5CHM3; -.
DR   STRING; 174720.A0A0N5CHM3; -.
DR   WBParaSite; SPAL_0001733700.1; SPAL_0001733700.1; SPAL_0001733700.
DR   Proteomes; UP000046392; 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   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   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   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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..182
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005896093"
FT   DOMAIN          35..92
FT                   /note="Carboxypeptidase activation peptide"
FT                   /evidence="ECO:0000259|Pfam:PF02244"
FT   DOMAIN          124..181
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|Pfam:PF00246"
SQ   SEQUENCE   182 AA;  21572 MW;  D0E64E6E15987CCB CRC64;
     MFPSNILFIF LFFVETSCYV DYSNYSLFTI QIKDLKIYED LEKKFPDDKL DFWTKSRSSE
     IPIQLFTSPE STLKIKNYLK SQNYNFNVTT KNWNKISKPK TIRRLSSNLN NAFQHNIYHS
     YDEIINFLKL QANKNKDFVS VGIYGESHEK RLLHYVKIGY SNGKEKPQIV IDAGMHAREW
     VN
//