ID   M28P2_ARTGP             Reviewed;         500 AA.
AC   E4URG0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Probable zinc metalloprotease MGYG_02393;
DE            EC=3.4.-.-;
DE   Flags: Precursor;
GN   ORFNames=MGYG_02393;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
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; DS989823; EFQ99382.1; -; Genomic_DNA.
DR   RefSeq; XP_003174865.1; XM_003174817.1.
DR   AlphaFoldDB; E4URG0; -.
DR   SMR; E4URG0; -.
DR   PRIDE; E4URG0; -.
DR   EnsemblFungi; EFQ99382; EFQ99382; MGYG_02393.
DR   GeneID; 10030166; -.
DR   eggNOG; ENOG502R701; Eukaryota.
DR   HOGENOM; CLU_047420_0_0_1; -.
DR   InParanoid; E4URG0; -.
DR   OMA; NNDMIGN; -.
DR   OrthoDB; 607736at2759; -.
DR   Proteomes; UP000002669; 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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..500
FT                   /note="Probable zinc metalloprotease MGYG_02393"
FT                   /id="PRO_0000411757"
FT   DOMAIN          414..500
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   500 AA;  54844 MW;  C5F16365D68A35E9 CRC64;
     MHLSMGGLLP GLALLASANA LALALPLESS VYTVQVTNPF HESLFSCPAA SWPKVKLGSE
     NRSQEPSKDL KKILSQISPK RIEATIRKLV SFGTRHTLST QTNATYGIGA ARDWIESEFQ
     RYANASDGRL TVAVVGYDQQ PDGRRIPFPV RISDVVATLK GEGDPERVYL VSGHYDSRNS
     DALDYKGIAP GANDDASGVA VSLELARVMS QRGLPRPKAT IVFAAVAGEE QGLYGATFLA
     QSYRNSSANI EGMFTNDIIG SSTADDGTRE PHVVRLFAQG IPPLNVEDQA MRERRIMIGG
     DNDTPARQLA RFVKETAENK HTDMEVSVIY RLDRYLRGGD HRPFLEAGYP AARFTEPNEN
     FAHQHQDIRI DKDPKTGMDI QYGDLPEFCD FDYISRVGKV NAAALWNLAM SPGMPRNVRV
     NTSDLTNDSK FTWDPPAGGN ALVGGYEIVW RSTNAPFWTH KMDVGMVQEA TIDLSKDNVI
     FGIRARGKNG ERGVAVLPFP