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