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
//