MEP1_MAGO7
ID MEP1_MAGO7 Reviewed; 283 AA.
AC A4RGT4; G4MXP9;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Extracellular metalloprotease MGG_08041;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN ORFNames=MGG_08041;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
CC -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC proteinaceous substrates. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M43B family. {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; CM001232; EHA55186.1; -; Genomic_DNA.
DR RefSeq; XP_003714993.1; XM_003714945.1.
DR AlphaFoldDB; A4RGT4; -.
DR SMR; A4RGT4; -.
DR STRING; 318829.MGG_08041T0; -.
DR MEROPS; M43.008; -.
DR EnsemblFungi; MGG_08041T0; MGG_08041T0; MGG_08041.
DR GeneID; 2678331; -.
DR KEGG; mgr:MGG_08041; -.
DR VEuPathDB; FungiDB:MGG_08041; -.
DR eggNOG; ENOG502QQ7Z; Eukaryota.
DR HOGENOM; CLU_048726_0_0_1; -.
DR InParanoid; A4RGT4; -.
DR OMA; INETWAN; -.
DR OrthoDB; 1569419at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04275; ZnMc_pappalysin_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR008754; Peptidase_M43.
DR Pfam; PF05572; Peptidase_M43; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..283
FT /note="Extracellular metalloprotease MGG_08041"
FT /id="PRO_0000407202"
FT ACT_SITE 198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 233..260
FT /evidence="ECO:0000250"
SQ SEQUENCE 283 AA; 29953 MW; 241FB7E442A690BA CRC64;
MQINVVKTFL FALAASSVSA LAVDTEFRCG APEPSEELIE ASAIMAVAEA EAAANGTLAA
RQSALTIDTY VHVVATSTSA SAGYLSDATI QQQLRVMNED YAPSGIQFVL KGTDRTVNAN
WARDSGETAM KTALRKGTYK DLNLYFLSSI PGGILGYCYF PASATTSTVR LDGCTIASGT
VPGGSISRFN LGKTAVHEVG HWFGLYHTFQ GGCNGQGDLV DDTPAQASAS SGCPIGRDSC
PNQPGLDPIH NYMDYSDDSC YEEFTPGQNA RMSSMFAQFR AGK