Detail Information for IndEnz0015000069
IED ID IndEnz0015000069
Enzyme Type ID laccase000069
Protein Name Mitogen-activated protein kinase HOG1
MAP kinase HOG1
EC 2.7.11.24
Gene Name HOG1
Organism Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Diaporthales Cryphonectriaceae Cryphonectria-Endothia species complex Cryphonectria Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica)
Enzyme Sequence MAEFVRAQIFGTTFEITSRYSDLQPVGMGAFGLVCSARDQLTNQNVAIKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPLEDIYFVTELLGTDLHRLLTSRPLEKQFIQYFLYQIMRGLKYVHSAGVVHRDLKPSNILVNENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVINTIASENTLRFVKSLPKRERQPLASKFKNADEQAVDLLERMLVFDPKKRITASDALAHEYLAPYHDPTDEPVAEEKFDWSFNDADLPVDTWKIMMYSEILDYHNVDASGASAAMGEFNGQ
Enzyme Length 358
Uniprot Accession Number Q875L0
Absorption
Active Site ACT_SITE 141; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027"
Activity Regulation ACTIVITY REGULATION: Activated by tyrosine and threonine phosphorylation (By similarity). Hypoviruses like CHV1-EP713 induce inactivation by lowering the degree of phosphorylation in response to various environmental stresses. {ECO:0000250, ECO:0000269|PubMed:14982623}.
Binding Site BINDING 49; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24;
DNA Binding
EC Number 2.7.11.24
Enzyme Function FUNCTION: Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes (By similarity). Involved in the virulence and conidia formation. Mediates tannic acid-induced laccase expression and cryparin expression. {ECO:0000250, ECO:0000269|PubMed:14982623}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 26..34; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159
Features Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (2); Motif (1); Nucleotide binding (1)
Keywords ATP-binding;Activator;Cytoplasm;Kinase;Nucleotide-binding;Nucleus;Phosphoprotein;Serine/threonine-protein kinase;Transcription;Transcription regulation;Transferase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Modified Residue MOD_RES 171; /note=Phosphothreonine; /evidence=ECO:0000250; MOD_RES 173; /note=Phosphotyrosine; /evidence=ECO:0000250
Post Translational Modification PTM: Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme (By similarity). Phosphorylated in response of osmotic stress. {ECO:0000250, ECO:0000269|PubMed:14982623}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 171..173; /note=TXY
Gene Encoded By
Mass 40,945
Kinetics
Metal Binding
Rhea ID RHEA:17989; RHEA:46608
Cross Reference Brenda