ID HOG1_BOTFB Reviewed; 354 AA. AC A1IVT7; A6RRX4; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 05-DEC-2018, entry version 81. DE RecName: Full=Mitogen-activated protein kinase hog1; DE Short=MAP kinase hog1; DE EC=2.7.11.24; DE AltName: Full=BcSAK1; DE AltName: Full=Stress-activated mitogen-activated protein kinase; GN Name=hog1; Synonyms=sak1; ORFNames=BC1G_03001; 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 RT involved in vegetative differentiation and pathogenicity in Botrytis RT 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., RA Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., RA Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., RA Pradier J.-M., Quevillon E., Sharon A., Simon A., ten Have A., RA Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., RA Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., RA Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., RA Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., RA Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., RA Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., RA Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., RA Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., RA 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). CC -!- FUNCTION: Mitogen-activated protein kinase involved in a signal CC 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). CC Involved in vegetative and pathogenic development like conidia CC formation, sclerotial development, and in penetration into CC unwounded plant tissue. {ECO:0000250, CC ECO:0000269|PubMed:17189492}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CC EC=2.7.11.24; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.24; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ACTIVITY REGULATION: Activated by tyrosine and threonine CC phosphorylation. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {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 CC the enzyme (By similarity). Phosphorylated under osmotic stress, CC specific fungicides, and oxidative stress mediated by H(2)O(2) and CC menadione. {ECO:0000250, ECO:0000269|PubMed:17189492}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein 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; CH476852; EDN18852.1; -; Genomic_DNA. DR RefSeq; XP_001558337.1; XM_001558287.1. DR ProteinModelPortal; A1IVT7; -. DR SMR; A1IVT7; -. DR PRIDE; A1IVT7; -. DR EuPathDB; FungiDB:Bcin15g03580; -. DR OMA; EITNRYT; -. 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:0051403; P:stress-activated MAPK cascade; IEA:InterPro. DR CDD; cd07856; STKc_Sty1_Hog1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. 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:SF247; PTHR24055:SF247; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01773; P38MAPKINASE. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 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; KW Nucleus; Phosphoprotein; Serine/threonine-protein kinase; KW Transcription; Transcription regulation; Transferase. FT CHAIN 1 354 Mitogen-activated protein kinase hog1. FT /FTId=PRO_0000289679. FT DOMAIN 20 299 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 26 34 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOTIF 171 173 TXY. FT ACT_SITE 141 141 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 49 49 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOD_RES 171 171 Phosphothreonine. {ECO:0000250}. FT MOD_RES 173 173 Phosphotyrosine. {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 //