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   03-MAR-2009, entry version 18.
DE   RecName: Full=Mitogen-activated protein kinase hog1;
DE            Short=MAP kinase hog1;
DE            EC=2.7.11.24;
DE   AltName: Full=Stress-activated mitogen-activated protein kinase;
DE   AltName: Full=BcSAK1;
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; Botryotinia.
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].
RA   Birren B.W., Galagan J.E., Lander E.S., Devon K., Nusbaum C.,
RA   Cuomo C., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Alvarado L.,
RA   Kodira C.D., Zeng Q., Yandava C., O'Leary S., Amedeo P., Briggs S.,
RA   Baker S., Goff S., Hohn T., Hutchison D., Lam S., Martin C.,
RA   Miguel T., Rose M., Turgeon B.G., Wu G., Yoder O., Zheng L.;
RT   "Annotation of the Botryotinia fuckeliana B05.10 genome.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by tyrosine and threonine
CC       phosphorylation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
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.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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; -.
DR   GeneID; 5438947; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004707; F:MAP kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR008352; MAPK_p38.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_bd_CS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   InterPro; IPR002290; Ser_thr_pkinase.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01773; P38MAPKINASE.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00220; S_TKc; 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; Complete proteome; Cytoplasm; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    354       Mitogen-activated protein kinase hog1.
FT                                /FTId=PRO_0000289679.
FT   DOMAIN       20    299       Protein kinase.
FT   NP_BIND      26     34       ATP (By similarity).
FT   MOTIF       171    173       TXY.
FT   ACT_SITE    141    141       Proton acceptor (By similarity).
FT   BINDING      49     49       ATP (By similarity).
FT   MOD_RES     171    171       Phosphothreonine (By similarity).
FT   MOD_RES     173    173       Phosphotyrosine (By similarity).
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
//