ID   MCPA_TRIVH              Reviewed;         422 AA.
AC   D4DL57;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Probable metallocarboxypeptidase A;
DE            Short=MCPA;
DE            EC=3.4.17.-;
DE   AltName: Full=Carboxypeptidase M14A;
DE   Flags: Precursor;
GN   Name=MCPA; ORFNames=TRV_07931;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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; ACYE01000493; EFE37398.1; -; Genomic_DNA.
DR   RefSeq; XP_003018043.1; XM_003017997.1.
DR   AlphaFoldDB; D4DL57; -.
DR   SMR; D4DL57; -.
DR   MEROPS; M14.014; -.
DR   EnsemblFungi; EFE37398; EFE37398; TRV_07931.
DR   GeneID; 9579170; -.
DR   KEGG; tve:TRV_07931; -.
DR   HOGENOM; CLU_019326_1_1_1; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
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_0000397760"
FT   CHAIN           113..422
FT                   /note="Probable metallocarboxypeptidase A"
FT                   /id="PRO_0000397761"
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;  47132 MW;  7BF1DC86643A9FC4 CRC64;
     MRSVLSLALL AVNVVTAAVV APFDYSGYKV IRVPTQKDNV KEVQRIITDL NLDTWKYPKS
     EGQNADIVVP PSQISSFMER ISGMNIEMMH EDLGLSIRNE TSFEAYSAGY APDINWFKSY
     HSYQDHLSYL QDLQGLFRTR SEYVDAGKSH EGRTIPALHI WGSGGKNSKP AIIFHGTIHA
     REWITTMVTE YMAWSFLSQY NKNADITSIV DNFDIWIFPI VNPDGFAFTQ TSNRLWRKNR
     QPNPNARCPG RDLNRNYPYQ WVGPGSSSNP CSDTYRGAQP GDGTEIKVHI ANMKKIAANK
     GIAMFVDWHS YGQLFMSPYG YSCTARPPTD ARHQELSRIF AQALKAVHGT PYKTGPICNT
     IYQVNGDSVD YALEVLKVKL SLTAELRDTG ARGFVLPADQ IIPSGEETLA GTVAMLKAVI
     QG