ID HOG1_BOTFB Reviewed; 354 AA. AC A1IVT7; A0A384K4V3; A6RRX4; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-NOV-2024, entry version 103. DE RecName: Full=Mitogen-activated protein kinase hog1; DE Short=MAP kinase hog1; DE EC=2.7.11.24 {ECO:0000250|UniProtKB:P32485}; DE AltName: Full=BcSAK1; DE AltName: Full=Stress-activated mitogen-activated protein kinase; GN Name=hog1; Synonyms=sak1; ORFNames=BC1G_03001, BCIN_15g03580; OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis OS cinerea). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Botrytis. OX NCBI_TaxID=332648; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PHOSPHORYLATION. RX PubMed=17189492; DOI=10.1128/ec.00153-06; RA Segmueller N., Ellendorf U., Tudzynski B., Tudzynski P.; RT "BcSAK1, a stress-activated mitogen-activated protein kinase, is involved RT in vegetative differentiation and pathogenicity in Botrytis cinerea."; RL Eukaryot. Cell 6:211-221(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B05.10; RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230; RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.; RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia RT sclerotiorum and Botrytis cinerea."; RL PLoS Genet. 7:E1002230-E1002230(2011). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=B05.10; RX PubMed=23104368; DOI=10.1128/ec.00164-12; RA Staats M., van Kan J.A.L.; RT "Genome update of Botrytis cinerea strains B05.10 and T4."; RL Eukaryot. Cell 11:1413-1414(2012). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=B05.10; RX PubMed=26913498; DOI=10.1111/mpp.12384; RA van Kan J.A.L., Stassen J.H.M., Mosbach A., van der Lee T.A.J., Faino L., RA Farmer A.D., Papasotiriou D.G., Zhou S., Seidl M.F., Cottam E., Edel D., RA Hahn M., Schwartz D.C., Dietrich R.A., Widdison S., Scalliet G.; RT "A gapless genome sequence of the fungus Botrytis cinerea."; RL Mol. Plant Pathol. 18:75-89(2017). CC -!- FUNCTION: Proline-directed serine/threonine-protein kinase involved in CC a signal transduction pathway that is activated by changes in the CC osmolarity of the extracellular environment. Controls osmotic CC regulation of transcription of target genes (By similarity). Involved CC in vegetative and pathogenic development like conidia formation, CC sclerotial development, and in penetration into unwounded plant tissue. CC {ECO:0000250|UniProtKB:Q4WSF6, ECO:0000269|PubMed:17189492}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; CC Evidence={ECO:0000250|UniProtKB:P32485}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; CC Evidence={ECO:0000250|UniProtKB:P32485}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; CC Evidence={ECO:0000250|UniProtKB:P32485}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; CC Evidence={ECO:0000250|UniProtKB:P32485}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q16539}; CC -!- ACTIVITY REGULATION: Activated by tyrosine and threonine CC phosphorylation. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues CC whose phosphorylation activates the MAP kinases. CC -!- PTM: Dually phosphorylated on Thr-171 and Tyr-173, which activates the CC enzyme (By similarity). Phosphorylated under osmotic stress, specific CC fungicides, and oxidative stress mediated by H(2)O(2) and menadione. CC {ECO:0000250, ECO:0000269|PubMed:17189492}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. MAP kinase subfamily. HOG1 sub-subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. 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; AM236311; CAJ85638.1; -; Genomic_DNA. DR EMBL; CP009819; ATZ57828.1; -; Genomic_DNA. DR RefSeq; XP_001558337.1; XM_001558287.1. DR AlphaFoldDB; A1IVT7; -. DR SMR; A1IVT7; -. DR EnsemblFungi; Bcin15g03580.2; Bcin15p03580.2; Bcin15g03580. DR VEuPathDB; FungiDB:Bcin15g03580; -. DR OMA; NRYTDLN; -. DR OrthoDB; 158564at2759; -. DR PHI-base; PHI:1031; -. DR Proteomes; UP000001798; Chromosome bcin15. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:CACAO. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:TreeGrafter. DR GO; GO:0007231; P:osmosensory signaling pathway; IEA:TreeGrafter. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR GO; GO:0051403; P:stress-activated MAPK cascade; IEA:InterPro. DR CDD; cd07856; STKc_Sty1_Hog1; 1. DR FunFam; 1.10.510.10:FF:000049; Mitogen-activated protein kinase; 1. DR FunFam; 3.30.200.20:FF:000050; Mitogen-activated protein kinase; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR050117; MAP_kinase. DR InterPro; IPR003527; MAP_kinase_CS. DR InterPro; IPR008352; MAPK_p38-like. DR InterPro; IPR038783; MAPK_Sty1/Hog1. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF158; MITOGEN-ACTIVATED PROTEIN KINASE P38A-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01773; P38MAPKINASE. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS01351; MAPK; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW Activator; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; KW Transcription; Transcription regulation; Transferase. FT CHAIN 1..354 FT /note="Mitogen-activated protein kinase hog1" FT /id="PRO_0000289679" FT DOMAIN 20..299 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOTIF 171..173 FT /note="TXY" FT ACT_SITE 141 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 26..34 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 49 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 171 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" FT MOD_RES 173 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250" SQ SEQUENCE 354 AA; 40499 MW; 4C0DB95CE772A627 CRC64; MAEFVRAQIF GTTFEITSRY SDLQPVGMGA FGLVCSAKDN LTGSNVAVKK IMKPFSTPVL SKRTYRELKL LKHLKHENVI SLSDIFISPL EDIYFVTELL GTDLHRLLTS RPLEKQFIQY FLYQILRGLK YVHSAGVVHR DLKPSNILVN ENCDLKICDF GLARIQDPQM TGYVSTRYYR APEIMLTWQK YDVEVDVWSA GCIFAEMLEG KPLFPGKDHV NQFSIITELL GTPPDDVIHT IASENTLRFV QSLPKRERQP LASKFTQADP LAIDLLEKML VFDPRARIKA AEGLAHEYLS PYHDPTDEPA AEERFDWSFN DADLPVDTWK IMMYSEILDY HNVINDAQNL TESQ //