ID   MCPA_TRITO              Reviewed;         422 AA.
AC   B6V865;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Metallocarboxypeptidase A;
DE            Short=MCPA;
DE            EC=3.4.17.-;
DE   AltName: Full=Carboxypeptidase M14A;
DE   Flags: Precursor;
GN   Name=MCPA;
OS   Trichophyton tonsurans (Scalp ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=34387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Preuett B.L., Abdel-Rahman S.M.;
RT   "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT   and Trichophyton equinum.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular metalloprotease that contributes to
CC       pathogenicity. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; FJ267688; ACJ06656.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6V865; -.
DR   SMR; B6V865; -.
DR   MEROPS; M14.014; -.
DR   PRIDE; B6V865; -.
DR   VEuPathDB; FungiDB:TESG_00263; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 1.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   Pfam; PF02244; Propep_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Disulfide bond; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..112
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000384107"
FT   CHAIN           113..422
FT                   /note="Metallocarboxypeptidase A"
FT                   /id="PRO_0000384108"
FT   ACT_SITE        385
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         179..182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         254..255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         310..311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        248..271
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   422 AA;  47180 MW;  DF0B9F316A8F1CD4 CRC64;
     MRSVLSLALL AANVVTAAVV SPFDYSGYKV IRVPTQKDNV KEVQRIITDL NLDTWKYPKS
     EGQNADIVVP PSQITSFMER ISGMSMEMMH EDLGMSISNE TSFEAYSAGY APDINWFKSY
     HSYQDHISYL QDLQGLFRTR SEYVDAGKSH EGRTIPALHI WGSGGKNSKP AIIFHGTIHA
     REWITTMVTE YLAWSLLSQY NKNADITSIV DNFDIWVFPI VNPDGFAFTQ TSNRLWRKNR
     QPNPNARCPG RDLNRNYPYQ WVGPGSSSNP CSDTYRGAQP GDGTEIKVHI ANMKRIASYH
     GIAMFVDWHS YGQLFMSPYG YSCTARPPTD ARHQELSRIF AQALRAVHGT PYRTGPICNT
     IYQVNGDSVD YALEVLKVKL SLTAELRDTG ARGFVLPADQ IVPSGEETLA GTVAMLKAVI
     RG