ID G9MW46_HYPVG Unreviewed; 356 AA. AC G9MW46; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-NOV-2024, entry version 76. DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|RuleBase:RU361165}; DE EC=2.7.11.24 {ECO:0000256|RuleBase:RU361165}; GN Name=tmk3 {ECO:0000313|EMBL:EHK21342.1}; GN ORFNames=TRIVIDRAFT_83666 {ECO:0000313|EMBL:EHK21342.1}; OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens) OS (Trichoderma virens). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma. OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK21342.1, ECO:0000313|Proteomes:UP000007115}; RN [1] {ECO:0000313|EMBL:EHK21342.1, ECO:0000313|Proteomes:UP000007115} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115}; RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40; RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A., RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A., RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z., RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O., RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J., RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F., RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R., RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E., RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M., RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E., RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S., RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M., RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.; RT "Comparative genome sequence analysis underscores mycoparasitism as the RT ancestral life style of Trichoderma."; RL Genome Biol. 12:R40.1-R40.15(2011). CC -!- FUNCTION: Proline-directed serine/threonine-protein kinase involved in CC a signal transduction pathway that is activated by changes in the CC osmolarity of the extracellular environment. Controls osmotic CC regulation of transcription of target genes. CC {ECO:0000256|ARBA:ARBA00046173}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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 Evidence={ECO:0000256|ARBA:ARBA00045064}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; CC Evidence={ECO:0000256|ARBA:ARBA00045064}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; CC Evidence={ECO:0000256|ARBA:ARBA00045089}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; CC Evidence={ECO:0000256|ARBA:ARBA00045089}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|RuleBase:RU361165}; CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine CC phosphorylation. {ECO:0000256|RuleBase:RU361165}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. MAP kinase subfamily. {ECO:0000256|RuleBase:RU361165}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EHK21342.1}. 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; ABDF02000072; EHK21342.1; -; Genomic_DNA. DR RefSeq; XP_013955538.1; XM_014100063.1. DR AlphaFoldDB; G9MW46; -. DR STRING; 413071.G9MW46; -. DR EnsemblFungi; EHK21342; EHK21342; TRIVIDRAFT_83666. DR GeneID; 25798469; -. DR VEuPathDB; FungiDB:TRIVIDRAFT_83666; -. DR eggNOG; KOG0660; Eukaryota. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; G9MW46; -. DR OMA; NRYTDLN; -. DR OrthoDB; 158564at2759; -. DR Proteomes; UP000007115; Unassembled WGS sequence. 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-UniRule. DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:TreeGrafter. DR GO; GO:0007231; P:osmosensory signaling pathway; IEA:TreeGrafter. 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 FunFam; 1.10.510.10:FF:000049; Mitogen-activated protein kinase; 1. DR FunFam; 3.30.200.20:FF:000050; Mitogen-activated protein kinase; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR050117; MAP_kinase. DR InterPro; IPR003527; MAP_kinase_CS. 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; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF158; MITOGEN-ACTIVATED PROTEIN KINASE P38A-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 {ECO:0000256|ARBA:ARBA00023159}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361165}; KW Magnesium {ECO:0000256|RuleBase:RU361165}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Reference proteome {ECO:0000313|Proteomes:UP000007115}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|RuleBase:RU000304}; KW Transcription {ECO:0000256|ARBA:ARBA00023015}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}; KW Transferase {ECO:0000256|RuleBase:RU361165}. FT DOMAIN 20..299 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 50 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 356 AA; 41083 MW; 3C7AFEDA24185FE7 CRC64; MAEFVRAQIF GTTFEITSRY SDLQPVGMGA FGLVCSARDQ LTNQNVAVKK IMKPFSTPVL AKRTYRELKL LKHLRHENVI SLSDIFISPL EDIYFVTELL GTDLHRLLTS RPLEKQFIQY FLYQIMRGLK YVHSAGVVHR DLKPSNILVN ENCDLKICDF GLARIQDPQM TGYVSTRYYR APEIMLTWQK YDVEVDIWSA GCIFAEMLEG KPLFPGKDHV NQFSIITELL GTPPDDVINT IASENTLRFV KSLPKRERQP LRNKFKNADD SAIDLLERML VFDPKKRVTA TQALAHEYLQ PYHDPTDEPV ADEKFDWSFN DADLPVDTWK IMMYSEILDY HNVEGAPNME EQFATQ //