ID   M28P2_MAGO7             Reviewed;         502 AA.
AC   A4R017; G4MNP9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Probable zinc metalloprotease MGG_02107;
DE            EC=3.4.-.-;
DE   Flags: Precursor;
GN   ORFNames=MGG_02107;
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   -!- 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; CM001231; EHA56265.1; -; Genomic_DNA.
DR   RefSeq; XP_003708877.1; XM_003708829.1.
DR   AlphaFoldDB; A4R017; -.
DR   SMR; A4R017; -.
DR   EnsemblFungi; MGG_16033T0; MGG_16033T0; MGG_16033.
DR   GeneID; 12985700; -.
DR   KEGG; mgr:MGG_16033; -.
DR   VEuPathDB; FungiDB:MGG_16033; -.
DR   eggNOG; ENOG502R701; Eukaryota.
DR   HOGENOM; CLU_047420_0_0_1; -.
DR   InParanoid; A4R017; -.
DR   OMA; NNDMIGN; -.
DR   OrthoDB; 607736at2759; -.
DR   Proteomes; UP000009058; Chromosome 1.
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   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; PTHR12147; 1.
DR   Pfam; PF04389; Peptidase_M28; 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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..502
FT                   /note="Probable zinc metalloprotease MGG_02107"
FT                   /id="PRO_0000411760"
FT   DOMAIN          414..502
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          284..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        417
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   502 AA;  52930 MW;  DFAB3795D2D966D8 CRC64;
     MRSPPGAVAA LASVAAQLAT AALVPRDAAA PTTAAMPLPF PAQVGIDDSN LATCANANWP
     PPSSPVGEVI SAQLPDADLQ AALGEVDPAR IRAIVDKLVG FGTRHTLSTQ TDPTRGIGAA
     RDWIAEEMRG YAATAGGRME VTVPGYVQGV ASRISFPVKI SNVVATLKGD KDPDRVYVVS
     GHYDSRVTDV MNYEADAPGA NDDASGVALA MELARIFATR RPAATIVFTA VAGEEQGLYG
     SAFMAQTYRN ASVNVEGVLN NDIIGSSTGS RGEKDPHTVR VFCQGGSPAG ESKERAETRA
     SIGGENDSPA RELGRFIAEV GGNAFTDMKV ALVYRLDRYL RGGDHRSFLD AGYGSAVRFT
     EPNEDFNHQH QDVRNATDGT VLGDLAEFVD YDYVARVAKV NLAAAWSLAN APPQVRNVTV
     DTSTLSNDSG LSWAKIAGAG AALVKGYEVV WRPTTASLWT HQLYVGDVAS FRVPLTKDNV
     IFGVRSVGLN GYKSPATMPF PG