ID   MCPAL_ARTOC             Reviewed;         416 AA.
AC   C5FH26;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Metallocarboxypeptidase A-like protein MCYG_01475;
DE            EC=3.4.17.-;
DE   Flags: Precursor;
GN   ORFNames=MCYG_01475;
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}.
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DR   EMBL; DS995702; EEQ28656.1; -; Genomic_DNA.
DR   RefSeq; XP_002848541.1; XM_002848495.1.
DR   AlphaFoldDB; C5FH26; -.
DR   SMR; C5FH26; -.
DR   STRING; 63405.XP_002848541.1; -.
DR   MEROPS; M14.014; -.
DR   EnsemblFungi; EEQ28656; EEQ28656; MCYG_01475.
DR   GeneID; 9230679; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   HOGENOM; CLU_019326_1_1_1; -.
DR   OMA; SHGISYE; -.
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..113
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000390756"
FT   CHAIN           114..416
FT                   /note="Metallocarboxypeptidase A-like protein MCYG_01475"
FT                   /id="PRO_0000390757"
FT   REGION          264..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        381
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         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         250..251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         306..307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        244..267
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  45914 MW;  EAB1CB34FD949EA6 CRC64;
     MQPLLVLATL LGSALAGTIP LQSANYHGYK VVRLSGEDTS KISHIVSQLG LETWKFPKSA
     NANVDIVVPP KKIAEFEKMS HAAGLKKQIM HEDLGRSIAS EMSFRPYSYG GANDTWFQSY
     HKYEDHLKFM KDFQSAHAEN TEIVTSGKSH EGRDITGVHV WGSGGKGSKP AVVFHGTVHA
     REWITTMTVE YILNQLLEDK EAGAALLDKY DFYIFPITNP DGFVFSTDHD RMWRKNREQN
     EKGCYGTDLN RNWPYEWDGD GSTTDPCSET YRGPSPGSAP ETKASTSFIK GLADGAGVKM
     FVDWHSYSQL FMTPYGYSCS ARAPNDDVLQ EMASSFADAV KAVHGTSFTT GPICSTIYQA
     NGNSVDWVVD EIKGETAFAA ELRDTGMHGF VLPPDQIIPS GEETWAGVKA MFSKLK