ID G9MW46_HYPVG Unreviewed; 356 AA. AC G9MW46; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 03-AUG-2022, entry version 66. 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: 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. {ECO:0000256|ARBA:ARBA00025247}. 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; Evidence={ECO:0000256|RuleBase:RU361165}; 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: 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 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; YTDLNPV; -. DR OrthoDB; 683132at2759; -. DR Proteomes; UP000007115; Unassembled WGS sequence. 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: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; 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 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 {ECO:0000256|ARBA:ARBA00023159}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; 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:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, 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 //