ID   MCPA_ARTOC              Reviewed;         422 AA.
AC   C5FVN6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Metallocarboxypeptidase A;
DE            Short=MCPA;
DE            EC=3.4.17.-;
DE   AltName: Full=Carboxypeptidase M14A;
DE   Flags: Precursor;
GN   Name=MCPA; ORFNames=MCYG_06789;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS995706; EEQ33970.1; -; Genomic_DNA.
DR   RefSeq; XP_002844825.1; XM_002844779.1.
DR   AlphaFoldDB; C5FVN6; -.
DR   SMR; C5FVN6; -.
DR   STRING; 63405.XP_002844825.1; -.
DR   MEROPS; M14.014; -.
DR   PRIDE; C5FVN6; -.
DR   EnsemblFungi; EEQ33970; EEQ33970; MCYG_06789.
DR   GeneID; 9222215; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   HOGENOM; CLU_019326_1_1_1; -.
DR   OMA; KVHIANM; -.
DR   OrthoDB; 524270at2759; -.
DR   Proteomes; UP000002035; 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; Reference proteome; Secreted; Signal; Virulence;
KW   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_0000384101"
FT   CHAIN           113..422
FT                   /note="Metallocarboxypeptidase A"
FT                   /id="PRO_0000384102"
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;  47096 MW;  9EE43D35376FB699 CRC64;
     MRSVLSFALL AANVVSAAVL APFDYSGYKV VRVPTQKGNV KEVQRIITDL NLDTWKYPKA
     EGQNADIVIP PSQIPSFMER ISGMDREIMH EDLGMSISNE TTFEAYSAGY APDINWFKSY
     HSYQDHLSYL QDLQGLFRTR SEYVDAGKSH EGRTIPALHL WGKGGKNSKP AIIFHGTIHA
     REWITTMVTE YMAWSFLSEY NKNADITSIV DNFDIWIFPI VNPDGFAYTQ TSNRLWRKNR
     QPNPGARCPG RDLNRNYPYQ WVGPGSSSNP CSDIYRGAEA GDGTEIKVHI ANMKKIAAYK
     GIAMFVDWHS YGQLFMSPYG YSCTARPPTD ARHQELSRIF AQALKAVHGT PYKTGPICST
     IYQVNGDSVD WALEVLKVKL SLTAELRDTG ARGFVLPADQ ILPSGEETLA GTVAMLKAVI
     KG