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Q875L0

- HOG1_CRYPA

UniProt

Q875L0 - HOG1_CRYPA

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Protein

Mitogen-activated protein kinase HOG1

Gene
HOG1
Organism
Cryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes By similarity. Involved in the virulence and conidia formation. Mediates tannic acid-induced laccase expression and cryparin expression.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium By similarity.

Enzyme regulationi

Activated by tyrosine and threonine phosphorylation By similarity. Hypoviruses like CHV1-EP713 induce inactivation by lowering the degree of phosphorylation in response to various environmental stresses.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491ATP By similarity
Active sitei141 – 1411Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 349ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase HOG1 (EC:2.7.11.24)
Short name:
MAP kinase HOG1
Gene namesi
Name:HOG1
OrganismiCryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
Taxonomic identifieri5116 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeDiaporthalesCryphonectriaceaeCryphonectria-Endothia complexCryphonectria

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Mitogen-activated protein kinase HOG1PRO_0000289686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei171 – 1711Phosphothreonine By similarity
Modified residuei173 – 1731Phosphotyrosine By similarity

Post-translational modificationi

Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme By similarity. Phosphorylated in response of osmotic stress.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ875L0.

Structurei

3D structure databases

ProteinModelPortaliQ875L0.
SMRiQ875L0. Positions 3-343.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 299280Protein kinaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi171 – 1733TXY

Domaini

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similaritiesi

Phylogenomic databases

OMAiPDDVIHT.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q875L0-1 [UniParc]FASTAAdd to Basket

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MAEFVRAQIF GTTFEITSRY SDLQPVGMGA FGLVCSARDQ LTNQNVAIKK    50
IMKPFSTPVL AKRTYRELKL LKHLRHENII SLSDIFISPL EDIYFVTELL 100
GTDLHRLLTS RPLEKQFIQY FLYQIMRGLK YVHSAGVVHR DLKPSNILVN 150
ENCDLKICDF GLARIQDPQM TGYVSTRYYR APEIMLTWQK YDVEVDIWSA 200
GCIFAEMLEG KPLFPGKDHV NQFSIITELL GTPPDDVINT IASENTLRFV 250
KSLPKRERQP LASKFKNADE QAVDLLERML VFDPKKRITA SDALAHEYLA 300
PYHDPTDEPV AEEKFDWSFN DADLPVDTWK IMMYSEILDY HNVDASGASA 350
AMGEFNGQ 358
Length:358
Mass (Da):40,945
Last modified:June 1, 2003 - v1
Checksum:iD4B52064CF00B7C3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY166687 Genomic DNA. Translation: AAO27796.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY166687 Genomic DNA. Translation: AAO27796.1 .

3D structure databases

ProteinModelPortali Q875L0.
SMRi Q875L0. Positions 3-343.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q875L0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

OMAi PDDVIHT.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01773. P38MAPKINASE.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of HOG1 homologue, CpMK1, from Cryphonectria parasitica and evidence for hypovirus-mediated perturbation of its phosphorylation in response to hypertonic stress."
    Park S.-M., Choi E.-S., Kim M.-J., Cha B.-J., Yang M.-S., Kim D.-H.
    Mol. Microbiol. 51:1267-1277(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION, ENZYME REGULATION.
    Strain: ATCC 38755 / EP155.

Entry informationi

Entry nameiHOG1_CRYPA
AccessioniPrimary (citable) accession number: Q875L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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