MPG1_MAGO7
ID MPG1_MAGO7 Reviewed; 112 AA.
AC P52751; A4QQK2; G4NK02; Q2KEE7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Hydrophobin-like protein MPG1;
DE Flags: Precursor;
GN Name=MPG1; ORFNames=MGCH7_ch7g1089, MGG_10315;
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 [GENOMIC DNA].
RC STRAIN=Guyane 11;
RX PubMed=8312740; DOI=10.2307/3869740;
RA Talbot N.J., Ebbole D.J., Hamer J.E.;
RT "Identification and characterization of MPG1, a gene involved in
RT pathogenicity from the rice blast fungus Magnaporthe grisea.";
RL Plant Cell 5:1575-1590(1993).
RN [2]
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: Involved in pathogenicity, may have a role in the elaboration
CC of infective structure.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall.
CC -!- SIMILARITY: Belongs to the fungal hydrophobin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAQ71682.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L20685; AAA20128.1; -; Genomic_DNA.
DR EMBL; CM000230; EAQ71682.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM001237; EHA45770.1; -; Genomic_DNA.
DR RefSeq; XP_003720513.1; XM_003720465.1.
DR PDB; 2N4O; NMR; -; A=19-112.
DR PDBsum; 2N4O; -.
DR AlphaFoldDB; P52751; -.
DR BMRB; P52751; -.
DR SMR; P52751; -.
DR EnsemblFungi; MGG_10315T0; MGG_10315T0; MGG_10315.
DR GeneID; 2681967; -.
DR KEGG; mgr:MGG_10315; -.
DR VEuPathDB; FungiDB:MGG_10315; -.
DR eggNOG; ENOG502T10M; Eukaryota.
DR HOGENOM; CLU_164195_0_0_1; -.
DR InParanoid; P52751; -.
DR OMA; AEVYCCN; -.
DR OrthoDB; 1513191at2759; -.
DR PHI-base; PHI:15; -.
DR Proteomes; UP000009058; Chromosome 7.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:InterPro.
DR GO; GO:0005199; F:structural constituent of cell wall; IEA:InterPro.
DR InterPro; IPR001338; Hydrophobin.
DR InterPro; IPR019778; Hydrophobin_CS.
DR Pfam; PF01185; Hydrophobin; 1.
DR SMART; SM00075; HYDRO; 1.
DR PROSITE; PS00956; HYDROPHOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Disulfide bond; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..112
FT /note="Hydrophobin-like protein MPG1"
FT /id="PRO_0000013510"
FT DISULFID 36..94
FT /evidence="ECO:0000250"
FT DISULFID 44..88
FT /evidence="ECO:0000250"
FT DISULFID 45..68
FT /evidence="ECO:0000250"
FT DISULFID 95..107
FT /evidence="ECO:0000250"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:2N4O"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:2N4O"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:2N4O"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2N4O"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2N4O"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2N4O"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2N4O"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:2N4O"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2N4O"
SQ SEQUENCE 112 AA; 11639 MW; 9785E179929214FD CRC64;
MFSLKTVVLA LAAAAFVQAI PAPGEGPSVS MAQQKCGAEK VVSCCNSKEL KNSKSGAEIP
IDVLSGECKN IPINILTINQ LIPINNFCSD TVSCCSGEQI GLVNIQCTPI LS