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MEP1_ARTOC
ID   MEP1_ARTOC              Reviewed;         639 AA.
AC   C5FYJ8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Extracellular metalloproteinase 1;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP1;
DE   Flags: Precursor;
GN   Name=MEP1; ORFNames=MCYG_07415;
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=EEQ34596.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS995707; EEQ34596.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002843632.1; XM_002843586.1.
DR   AlphaFoldDB; C5FYJ8; -.
DR   SMR; C5FYJ8; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EEQ34596; EEQ34596; MCYG_07415.
DR   GeneID; 9230808; -.
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..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..250
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000384077"
FT   CHAIN           251..639
FT                   /note="Extracellular metalloproteinase 1"
FT                   /id="PRO_0000384078"
FT   ACT_SITE        435
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         438
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        598
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   639 AA;  70672 MW;  F5CF28024C74051C CRC64;
     MHGLLLAAGL ISLPLHVLAH PQPSSTSLAG RAVDLNEYRI GHRSSYTSND EMMKQPSIAS
     FRAGTYVEVA TEMVKQTMPN MEFRLVDDHY IGQSGIGHVR FRQTMHGIDI DNSDFNVNAY
     DNFYQIGQDG KVLSHGNSFY TGPAPESSPV QKRDFSDPMQ ALHGVRKALN LPIKAEGATV
     ENMSEHKVMF KGTSGALSDP TAKLCYMAKE DGSLALTWRV ETDIGDNWLL SYMDAKDTGK
     VHNVVDYVAH ATFQVYKWGL ADPTEGNREI LTNPWNLQTS PLTWLADGQN NFTATRGNNA
     IAQYNPDGGN DYENNYRPSP KNLKFEYPYS ANMDPPKTYI DASVTQLFYT SNVCHDLYYM
     LGFNEKAGNF QVNNRGQGGK GNDYVILNAQ DGSGTNNANF ATPPDGQPGR MRAYIWTRAN
     PPRDASFEAG TIIHEYTHGL SNRLCGGPAN SRCLNAIESG GMGEGWGDFY ATAVRLKPKD
     TRKTNYVKGG WVNNSPKGVR MYPYSTDMSV NPLVYTSNNQ LNEVHAIGTV WATMLYELLW
     NLIDKHGKND GPVPIFKNGI PSDGKYLAMK IVMDGMAIQP CNPNFVQARD AILDADKNLT
     KASNKCEIWK AFAKRGLGVG AKFDPKNRIG SNEVPKECK
 
 
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