ID   P20D1_ARTOC             Reviewed;         455 AA.
AC   C5FXY7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Probable carboxypeptidase MCYG_07204;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein MCYG_07204;
DE   Flags: Precursor;
GN   ORFNames=MCYG_07204;
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR   EMBL; DS995707; EEQ34385.1; -; Genomic_DNA.
DR   RefSeq; XP_002843421.1; XM_002843375.1.
DR   AlphaFoldDB; C5FXY7; -.
DR   SMR; C5FXY7; -.
DR   STRING; 63405.XP_002843421.1; -.
DR   EnsemblFungi; EEQ34385; EEQ34385; MCYG_07204.
DR   GeneID; 9225495; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   OMA; VSGHKGM; -.
DR   OrthoDB; 1432382at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Protease; Reference proteome;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..455
FT                   /note="Probable carboxypeptidase MCYG_07204"
FT                   /id="PRO_0000411226"
FT   ACT_SITE        202
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   455 AA;  49061 MW;  637027D245829EA2 CRC64;
     MQKTYLLALL VSSLASVRSL ADQTRLDLGG SFDSTDSADG GSDNVMIQKS EMNEVIASSE
     LLSLHRSLVE IKSISDNEQA VGEFLIDYLD SKNFTVEMQY VDFDDDTGKT IRSPRRFNIF
     AYPGNNASPG IILTSHIDTV PPFIPYSLSH PASTSLKRDD ILISGRGTVD DKASVACQVI
     AAMDHLEKHP DIPIGLLFVV SEEVGGKGMS TFSNSRLNSG TYHTIIFGEP TEGALVAGHK
     GMVSFTLRVH GKPAHSGYPW LGRSAVSEII PILAEVDRLG DIPVSQGGLP SSEKYGRTTL
     NIGFMSGGVA SNVVAEEAVA KVAVRLAAGD PEDAKDIIFR AIRNVATKNR NDATVVLSNG
     HERPKGDIEI IFGLEAYGVI DLDSDVDGFN VTTVNYGTDV PHWKIYGDNV KRYLYGPGTI
     FVAHGKNEAL TVGEMEAGLE GYKKLVAKAV ERERP