ID   HOG1_ALTBR              Reviewed;         355 AA.
AC   Q52PH6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Mitogen-activated protein kinase HOG1;
DE            Short=MAP kinase HOG1;
DE            EC=2.7.11.24;
GN   Name=HOG1;
OS   Alternaria brassicicola (Dark leaf spot agent).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Brassicicola.
OX   NCBI_TaxID=29001;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Abra43;
RA   Simoneau P., Sellam A., Bataille-Simoneau N.;
RT   "Characterization of a HOG1 homolog from Alternaria brassicicola.";
RL   Submitted (MAR-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 osmolarity of
CC       the extracellular environment. Controls osmotic regulation of
CC       transcription of target genes (By similarity). {ECO:0000250}.
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, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; 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 {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. {ECO:0000250}.
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}.
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DR   EMBL; AY987486; AAX86000.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q52PH6; -.
DR   SMR; Q52PH6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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   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   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   3: Inferred from homology;
KW   Activator; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..355
FT                   /note="Mitogen-activated protein kinase HOG1"
FT                   /id="PRO_0000289671"
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   355 AA;  40787 MW;  BB0B46747C3591EA CRC64;
     MAEFVRAQIF GTTFEITSRY TDLQPVGMGA FGLVCSAKDQ LTSQAVAIKK IMKPFSTPVL
     SKRTYRELKL LKHLRHENII SLSDIFISPL EDIYFVTELL GTDLHRLLTS RPLEKQFIQY
     FLYQILRGLK YVHSAGVVHR DLKPSNILVN ENCDLKICDF GLARIQDPQM TGYVSTRYYR
     APEIMLTWQK YDVEVDIWSA GCIFAEMLEG KPLFPGKDHV NQFSIITELL GTPPDDVIQT
     ICSENTLRFV QSLPKRERQP LSNKFKNAEP QAVDLLENML VFDPKKRVRA EQALAHPYLA
     PYHDPTDEPI AEEKFDWSFN DADLPVDTWK IMMYSEILDY HNVDAAAQEQ ENNGS