ID   MEP5_ARTOC              Reviewed;         632 AA.
AC   C5FX29;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Extracellular metalloproteinase 5;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP5;
DE   Flags: Precursor;
GN   Name=MEP5; ORFNames=MCYG_07688;
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: Secreted metalloproteinase probably acting as a virulence
CC       factor. {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 M36 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEQ34869.1; Type=Frameshift; Evidence={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; DS995707; EEQ34869.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; XP_002843905.1; XM_002843859.1.
DR   AlphaFoldDB; C5FX29; -.
DR   SMR; C5FX29; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EEQ34869; EEQ34869; MCYG_07688.
DR   GeneID; 9228027; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.390.10; -; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR001842; Peptidase_M36.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF02128; Peptidase_M36; 1.
DR   PRINTS; PR00999; FUNGALYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000384085"
FT   CHAIN           245..632
FT                   /note="Extracellular metalloproteinase 5"
FT                   /id="PRO_0000384086"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         427
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        591
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        620
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   632 AA;  69546 MW;  E39A4963B743DEDB CRC64;
     MHGLLLAAGL LSLPLHVLAH PQPGTSLAGR AVDLNAYRMA DRASYMSSDE MQAQQPHIAS
     VSAGGYVETA TEVVKRVMPG MTFRLVDDHY VGVSGISHVY FRQTMHGMDI DNSDFNVNIG
     KDGKVLSYGN SFYTGPAPDK APMVKRDFSD PMQALHGVRK ALNLPITADK ATVKTVNEHE
     VTFMGTTGAL SDPSAKLCYM AKEDGSLALT WRVETDMGDN WLLSYVDAKS TDQVHNVVDY
     VSHATYQVYR WPIPDPTEGK REILENPWNL RTSPFTWISD GKNNYTTTRG NNAIAQANPD
     GGNEYLNNYR PNNKNLKFEY PYSPNMSPPK TYIDASITQL FYSANMVHDL YYMLGFTEKA
     GNFQVNNRGQ GGKGNDFVIL NAQDGSGTNN ANFATPPDGQ PGRMRVYIWT KAQPARDSSF
     EAGTVIHEYT HGLSNRLCGG PANSACLNGL ESGGMGEGWG DFFATAIRLK PNDNRNANYV
     HGEWVNNSPK GNRLFPYSTS LKTNPLVYTS CNKYNEVHAI GTVWASILYE VLWNLIDKHG
     KNDGPTPVFE NGVPKDGKYL SLKLVLDGMA IQPCKPNFVQ ARNAIIDADK NLTKGANKCE
     LWKAFAKRGL GTGAKYDPKN RTGSTAVPKE CQ