G4NEB8 · MST7_PYRO7
- ProteinMitogen-activated protein kinase kinae MST7
- GeneMST7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids415 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mitogen-activated protein kinase kinase; part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth (PubMed:15749760, PubMed:21283781, PubMed:23454094, PubMed:27059015).
The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the cell surface sensors MDB2 and SHO1 that recognize various surface signals such as surface hydrophobicity, cutin monomers, and rice leaf waxes (PubMed:21283781).
MST7 acts as the upstream MAPKK that directly phosphorylates MAP kinase PMK1 (PubMed:15749760).
The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the cell surface sensors MDB2 and SHO1 that recognize various surface signals such as surface hydrophobicity, cutin monomers, and rice leaf waxes (PubMed:21283781).
MST7 acts as the upstream MAPKK that directly phosphorylates MAP kinase PMK1 (PubMed:15749760).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]This reaction proceeds in the forward direction.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | MAP kinase activity | |
Molecular Function | MAP kinase kinase activity | |
Biological Process | MAPK cascade | |
Biological Process | positive regulation of appressorium formation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitogen-activated protein kinase kinae MST7
- EC number
- Short namesMAPKK MST7
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Magnaporthales > Pyriculariaceae > Pyricularia
Accessions
- Primary accessionG4NEB8
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Produces much less aerial hyphae and conidia and shows weakened cell walls and higher sensitivity to cell wall-degrading enzymes (PubMed:15749760).
Impairs the formation of appressoria and the ability to infect rice plants (PubMed:15749760, PubMed:23454094).
Impairs the formation of appressoria and the ability to infect rice plants (PubMed:15749760, PubMed:23454094).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 114 | Does not affect appressorium formation and plant infection. | ||||
Sequence: C → A | ||||||
Mutagenesis | 136 | Does not affect appressorium formation and plant infection. | ||||
Sequence: C → A | ||||||
Mutagenesis | 201 | Does not affect appressorium formation and plant infection. | ||||
Sequence: C → A | ||||||
Mutagenesis | 212 | Leads to constitutive activity; when associated with Glu-216. | ||||
Sequence: S → D | ||||||
Mutagenesis | 216 | Leads to constitutive activity; when associated with Asp-212. | ||||
Sequence: T → E | ||||||
Mutagenesis | 305 | Impairs appressorium formation and pathogenicity. | ||||
Sequence: C → A |
Miscellaneous
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000453095 | 1-415 | Mitogen-activated protein kinase kinae MST7 | |||
Sequence: MADPFAPRTMKRRNVKGLALTPAAPKPPPTAENAPIHRDSDQHAQLEIGIEFNLDLRPEDLEVIKDLGSGNGGTVSKVRHIPTNTVMARKVIHVEAKREMRKRIVRELQIMHSCNSEYIVTFYGAFLNENNDVIMCMEYADVGSLDRVSRVFGPIRVDVLGKIAEATLGGLTYLYAKHHIMHRDIKPSNILVNSRGSIKLCDFGVSGELINSIADTFVGTSTYMAPERIQGEKYTVKSDVWSFGLSIMELAIGKFPFAASEQLSDAESAPAGILDLLQQIVHEPAPKLPKSDAFPQILEDMIQKCLYKNPDDRPTPEELFERDPFVQAAKRTPVDLREWAFGLMERDNRKSHLAPQLSPATADLLRSSDSPTATYHGDDRPLETPTSAYRVDPRRGPAEGSAGLADQVDRLYIRD |
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-37 | Disordered | ||||
Sequence: MADPFAPRTMKRRNVKGLALTPAAPKPPPTAENAPIH | ||||||
Domain | 61-326 | Protein kinase | ||||
Sequence: LEVIKDLGSGNGGTVSKVRHIPTNTVMARKVIHVEAKREMRKRIVRELQIMHSCNSEYIVTFYGAFLNENNDVIMCMEYADVGSLDRVSRVFGPIRVDVLGKIAEATLGGLTYLYAKHHIMHRDIKPSNILVNSRGSIKLCDFGVSGELINSIADTFVGTSTYMAPERIQGEKYTVKSDVWSFGLSIMELAIGKFPFAASEQLSDAESAPAGILDLLQQIVHEPAPKLPKSDAFPQILEDMIQKCLYKNPDDRPTPEELFERDPFV | ||||||
Region | 363-409 | Disordered | ||||
Sequence: DLLRSSDSPTATYHGDDRPLETPTSAYRVDPRRGPAEGSAGLADQVD |
Sequence similarities
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length415
- Mass (Da)46,171
- Last updated2011-12-14 v1
- ChecksumF9036A416DB661EB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM001235 EMBL· GenBank· DDBJ | EHA48601.1 EMBL· GenBank· DDBJ | Genomic DNA |