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Database: UniProt
Entry: G0RHN6_HYPJQ
LinkDB: G0RHN6_HYPJQ
Original site: G0RHN6_HYPJQ 
ID   G0RHN6_HYPJQ            Unreviewed;      1609 AA.
AC   G0RHN6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=TRIREDRAFT_60051 {ECO:0000313|EMBL:EGR49513.1};
OS   Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN   [1] {ECO:0000313|EMBL:EGR49513.1, ECO:0000313|Proteomes:UP000008984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QM6a {ECO:0000313|EMBL:EGR49513.1,
RC   ECO:0000313|Proteomes:UP000008984};
RX   PubMed=18454138; DOI=10.1038/nbt1403;
RA   Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA   Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA   Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA   Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA   Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA   Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA   Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA   Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT   "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT   reesei (syn. Hypocrea jecorina).";
RL   Nat. Biotechnol. 26:553-560(2008).
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=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. GCN2 subfamily. {ECO:0000256|ARBA:ARBA00037982}.
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DR   EMBL; GL985062; EGR49513.1; -; Genomic_DNA.
DR   RefSeq; XP_006964653.1; XM_006964591.1.
DR   STRING; 431241.G0RHN6; -.
DR   EnsemblFungi; EGR49513; EGR49513; TRIREDRAFT_60051.
DR   GeneID; 18486565; -.
DR   KEGG; tre:TRIREDRAFT_60051; -.
DR   VEuPathDB; FungiDB:TRIREDRAFT_60051; -.
DR   eggNOG; KOG1035; Eukaryota.
DR   HOGENOM; CLU_001222_2_0_1; -.
DR   OrthoDB; 8734at2759; -.
DR   Proteomes; UP000008984; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR   CDD; cd14012; PK_eIF2AK_GCN2_rpt1; 1.
DR   CDD; cd14046; STKc_EIF2AK4_GCN2_rpt2; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR016255; Gcn2.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR024435; HisRS-related_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR006575; RWD-domain.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR11042:SF160; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE 1; 1.
DR   PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR   Pfam; PF12745; HGTP_anticodon2; 1.
DR   Pfam; PF00069; Pkinase; 3.
DR   Pfam; PF05773; RWD; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 1.
DR   SMART; SM00591; RWD; 1.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50908; RWD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000660-
KW   2}; Initiation factor {ECO:0000313|EMBL:EGR49513.1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGR49513.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000660-2};
KW   Protein biosynthesis {ECO:0000313|EMBL:EGR49513.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008984};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          44..154
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          268..546
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          596..972
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          666..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..741
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..756
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        826
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT   BINDING         602..610
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT   BINDING         625
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT   BINDING         626
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1609 AA;  181487 MW;  03F3DA21E0C6A23F CRC64;
     MAWKKPGILT GPPKNPKDDS SFPGLKPTGT DATTKIEYEE LQRNEIFALE AIYGDDFIQH
     TAAHSAWKKS DPSFDIRIKA PSDEELAVTV GFTLTATYPK TPPLMTLKGQ QYLREVTAFK
     IQKFMETQPR IFAKEAEEMI YKIVEGIQDI LEDAAQAKAS GKQLPSLEEE RDRHEAALAK
     LAQEQKEKEK QLEEEELKEK EKAAAEELQQ ELQRQKQKAR ESRFSRRSNG LSPHRPSSSS
     VSNGETIEFD QFCTMTDRMG NALTFRSVTG KSDPRAGEAS TVYTVRPVLS HGQGNQQLAL
     KEVVLRPNGK DQKEFKKQLQ SLESRLQDLK IGNKVHHRHL VDILDFKVES GVAADRPTAN
     AWTVRVLTPL AERGSLEELL ELAGHLEIGK VRSWTRDLLD ALNFLHNKNI AHQDIHSRNI
     LLFRESTGEI IPKISDASYQ REILNLGSKK QGPPGLATAK SAYWLPPEIA AATKPQYTSK
     SDIWDFGIVF VQMVFGLDVL RKYSSPKNLM ESVMLSHPLQ ELVSRFFKDD RQKRPRAFEL
     GASEFLATDA PVLFEDSSAM LAHSPSVNSL QALPVRLRRD SMTTRSLAVS RYTEDFVEEG
     RLGKGGFGEV VKARKKLDGQ IYAIKKITQR SQASLTEILK EVRLLSQLSH PAVVRYYNTW
     VEEIPDSTDT EGETSTEDYT EDTRDTGNES AGIDIQFATS TGGLDFISSN AAADFDYDSD
     EDEDDDEDHD LSDDEEDDDG SSIMDSAGHR DKNQEKERLA AIQRRTRMHR SYRTVLYISM
     EYCEKRTLRD LIARKLYKNT PEVWRLFRQI LEGLSHIHSL SIVHRDLKPE NIFIASSADG
     VDNVKIGDFG LATSGQFSVD RATANGYEAD DMTRSIGTAY YSAPEVRSAS NGMYSTKVDM
     YSLGIIFFEM CYMPMMGMQK ADVLGQLRRP VPVLPSDFRP TDKTQTEIVL SLVNHNPKER
     PSSADLLKSG KLPVQMESET IRRTLAGLAD PNSPYYQKML ATLFARPVEA AKNFAWDMNG
     VTPSAAELLN QSIVKNALVA IFRRHGALEA TRTSIYPKSS HYADNAVRLL DSNGTVLQLP
     YDLTMGHARM LAKHSQSHPL QRTYTFGSVF RDKQDTGQPQ MFGEVDFDIV TTDTLDLALK
     EAEVLKVLDE ILHTFPSLSA SQMCFHIGHS DILQLIFEYC GIPTSSRRAA ADVLSRLNIH
     NHTWQKIRME LRSPAVGISA TSIDELQRFD FRDTPNKAFA KLKLVFEGSD MYQRASSTIA
     HLKEVVEYTK RLGIDTKIYI NPLNSLKEAF YTGGILFSCI YDRKAKDVFA AGGRYDHLIN
     EQRPKIGGQF EKRHAVGFSL AWERLAKTPK SGGYSFLRKA EEDVSSIFSS KRCDILVASF
     DPATLRSSGI EVLRLLWSHD VSAELARDSR SPEDLMSKHR DESYSWIIII KQDSMLKIKT
     VGKKDVPDVD LPMAQLISWL KPEIRDRDIK AAAKFRGAPE SAPHGEKEHE QEVKILVAQT
     KSKKFNRRTV VEQAQITAAS LMNSFLEGPI LAVETSDHLM ELVQNTKLSD PESWRKAEHS
     VSTSEKKNVR EIHDQLDTWR YKYEKKNGSK HSFLYNFRSG TCMYYDLSG
//
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