ID   M28P2_ARTOC             Reviewed;         508 AA.
AC   C5FP82;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Probable zinc metalloprotease MCYG_04217;
DE            EC=3.4.-.-;
DE   Flags: Precursor;
GN   ORFNames=MCYG_04217;
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 M28 family. M28B subfamily.
CC       {ECO:0000305}.
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DR   EMBL; DS995704; EEQ31398.1; -; Genomic_DNA.
DR   RefSeq; XP_002846480.1; XM_002846434.1.
DR   AlphaFoldDB; C5FP82; -.
DR   SMR; C5FP82; -.
DR   EnsemblFungi; EEQ31398; EEQ31398; MCYG_04217.
DR   GeneID; 9224550; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_047420_0_0_1; -.
DR   OMA; NNDMIGN; -.
DR   OrthoDB; 607736at2759; -.
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:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; PTHR12147; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..508
FT                   /note="Probable zinc metalloprotease MCYG_04217"
FT                   /id="PRO_0000411758"
FT   DOMAIN          422..508
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   508 AA;  55828 MW;  EB72CA8DDC22E11B CRC64;
     MARPAAGPGG ISKFGNDFGL QRWRNTPRYD QTQPLEGSVC GYGLSNPFHE SLFSCPAASW
     PQAKLGRPNT PQEPSKDLKR ILSQISPKRI EATIRKLVSF GTRHTLSTQT NATHGIGAAR
     DWIASEFQRY ADASDGRLTV KVIGYEQQPD GSRVLFPVRI SDVVATLKGS EDPERVYVVS
     GHYDSRASDP LDYKTDAPGA NDDASGVAVS LEIARVMSQR NLPRPKATIV FAAVAGEEQG
     LLGSNFLAQT YRNSSTNVEG MFTNDIIGSS TADDGTKEPH VIRLFAQGVP PLNVENQAMR
     EKRLMIGGEN DTPARQLARF VKETAENKYT DMQVSVIYRL DRYLRGGDHR PFLEAGYPAA
     RFTEPNENYA HQHQNIRIEK DPKTGKDIQY GDLPEFCDFD FISRVGKVNA AALWNLAMSP
     GMPRNVRVDT SDLSNDSKFT WDPPAGGNAG VGGYEIVWRS TIAPFWTNVM DVGMVQAATI
     DLSKDNVIFG IRARGKNGER GVAVLPFP