ID   A0A016SZX5_9BILA        Unreviewed;       367 AA.
AC   A0A016SZX5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
GN   Name=Acey_s0154.g2972 {ECO:0000313|EMBL:EYB95982.1};
GN   Synonyms=Acey-W01A8.6 {ECO:0000313|EMBL:EYB95982.1};
GN   ORFNames=Y032_0154g2972 {ECO:0000313|EMBL:EYB95982.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB95982.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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:EYB95982.1}.
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DR   EMBL; JARK01001490; EYB95982.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016SZX5; -.
DR   MEROPS; M14.A27; -.
DR   Proteomes; UP000024635; 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:InterPro.
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   PRINTS; PR00765; CRBOXYPTASEA.
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:UP000024635};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..367
FT                   /note="Peptidase M14 carboxypeptidase A domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001490152"
FT   DOMAIN          29..331
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   367 AA;  42302 MW;  AD7FE193AE19946A CRC64;
     MRRLLAVLVV VFPPLVAAGE TPFFDLTRYN DFPEFESYIR GVARMNPDIV HMRLIGFSRE
     HRPLLGLKIG RPANHTKPAV WLDGGNHARE WPAFHVAVYF IEELIHNYGI DEKITSYINL
     LDIYVFPVLN PDGFIFSRTS RKSMIRQWRK NRAPTNCSGY TALAKNICCE GVDLNRNYDL
     GFSQKNYPFN NPCSDEFQGP FPFSEPESRA VRDFVLSHEI YGRLHALVSM HTHGQLWILP
     YNHHKRTYPE DFRELESLAT RAADKVYSYR ETKYRIGTAA DMLGTATGGA TDWIKKNTPT
     KYVYVLELPP DMSTWFAFQI KPHWLIPIGK ETWMGIKVIL DQVIEETINE PRRRVAAAAA
     TTFRVSN
//