ID   G9MW46_HYPVG            Unreviewed;       356 AA.
AC   G9MW46;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   07-SEP-2016, entry version 32.
DE   RecName: Full=Mitogen-activated protein kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574127};
DE            EC=2.7.11.24 {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574127};
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;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   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.,
RA   Antal Z., Atanasova L., Cervantes-Badillo M.G., Challacombe J.,
RA   Chertkov O., McCluskey K., Coulpier F., Deshpande N., von Doehren H.,
RA   Ebbole D.J., 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
RT   the ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574132}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361165};
CC   -!- ENZYME REGULATION: Activated by threonine and tyrosine
CC       phosphorylation. {ECO:0000256|RuleBase:RU361165}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. MAP kinase subfamily.
CC       {ECO:0000256|RuleBase:RU361165}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000256|RuleBase:RU361165}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {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   EnsemblFungi; EHK21342; EHK21342; TRIVIDRAFT_83666.
DR   GeneID; 25798469; -.
DR   InParanoid; G9MW46; -.
DR   OMA; LSHEYLA; -.
DR   OrthoDB; EOG092C2FL8; -.
DR   Proteomes; UP000007115; Unassembled WGS sequence.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR003527; MAP_kinase_CS.
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   ATP-binding {ECO:0000256|RuleBase:RU361165,
KW   ECO:0000256|SAAS:SAAS00574094};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007115};
KW   Kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574086,
KW   ECO:0000313|EMBL:EHK21342.1};
KW   Magnesium {ECO:0000256|RuleBase:RU361165};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361165,
KW   ECO:0000256|SAAS:SAAS00574135};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361165,
KW   ECO:0000256|SAAS:SAAS00574114};
KW   Transferase {ECO:0000256|RuleBase:RU361165,
KW   ECO:0000256|SAAS:SAAS00574095}.
FT   DOMAIN       20    299       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
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
//