HOG1_CRYPA
ID HOG1_CRYPA Reviewed; 358 AA.
AC Q875L0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Mitogen-activated protein kinase HOG1;
DE Short=MAP kinase HOG1;
DE EC=2.7.11.24;
GN Name=HOG1;
OS Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Cryphonectriaceae;
OC Cryphonectria-Endothia species complex; Cryphonectria.
OX NCBI_TaxID=5116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION, AND ACTIVITY
RP REGULATION.
RC STRAIN=ATCC 38755 / EP155;
RX PubMed=14982623; DOI=10.1111/j.1365-2958.2004.03919.x;
RA Park S.-M., Choi E.-S., Kim M.-J., Cha B.-J., Yang M.-S., Kim D.-H.;
RT "Characterization of HOG1 homologue, CpMK1, from Cryphonectria parasitica
RT and evidence for hypovirus-mediated perturbation of its phosphorylation in
RT response to hypertonic stress.";
RL Mol. Microbiol. 51:1267-1277(2004).
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). Involved in the
CC virulence and conidia formation. Mediates tannic acid-induced laccase
CC expression and cryparin expression. {ECO:0000250,
CC ECO:0000269|PubMed:14982623}.
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 (By similarity). Hypoviruses like CHV1-EP713 induce
CC inactivation by lowering the degree of phosphorylation in response to
CC various environmental stresses. {ECO:0000250,
CC ECO:0000269|PubMed:14982623}.
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 in response of osmotic stress.
CC {ECO:0000250, ECO:0000269|PubMed:14982623}.
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; AY166687; AAO27796.1; -; Genomic_DNA.
DR AlphaFoldDB; Q875L0; -.
DR SMR; Q875L0; -.
DR OMA; YTDLNPV; -.
DR PHI-base; PHI:342; -.
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 1: Evidence at protein level;
KW Activator; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Serine/threonine-protein kinase; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..358
FT /note="Mitogen-activated protein kinase HOG1"
FT /id="PRO_0000289686"
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 358 AA; 40945 MW; D4B52064CF00B7C3 CRC64;
MAEFVRAQIF GTTFEITSRY SDLQPVGMGA FGLVCSARDQ LTNQNVAIKK IMKPFSTPVL
AKRTYRELKL LKHLRHENII SLSDIFISPL EDIYFVTELL GTDLHRLLTS RPLEKQFIQY
FLYQIMRGLK YVHSAGVVHR DLKPSNILVN ENCDLKICDF GLARIQDPQM TGYVSTRYYR
APEIMLTWQK YDVEVDIWSA GCIFAEMLEG KPLFPGKDHV NQFSIITELL GTPPDDVINT
IASENTLRFV KSLPKRERQP LASKFKNADE QAVDLLERML VFDPKKRITA SDALAHEYLA
PYHDPTDEPV AEEKFDWSFN DADLPVDTWK IMMYSEILDY HNVDASGASA AMGEFNGQ
