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Database: UniProt
Entry: A0A251VCG7_HELAN
LinkDB: A0A251VCG7_HELAN
Original site: A0A251VCG7_HELAN 
ID   A0A251VCG7_HELAN        Unreviewed;      1215 AA.
AC   A0A251VCG7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OTG32846.1};
GN   Name=GCN2 {ECO:0000313|EMBL:OTG32846.1};
GN   ORFNames=HannXRQ_Chr03g0091131 {ECO:0000313|EMBL:OTG32846.1},
GN   HanXRQr2_Chr03g0134751 {ECO:0000313|EMBL:KAF5816481.1};
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG32846.1, ECO:0000313|Proteomes:UP000215914};
RN   [1] {ECO:0000313|EMBL:KAF5816481.1, ECO:0000313|Proteomes:UP000215914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5816481.1};
RX   PubMed=28538728; DOI=10.1038/nature22380;
RA   Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA   Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA   Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA   Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA   Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA   Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA   Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA   Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA   Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA   Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA   Vincourt P., Rieseberg L.H., Langlade N.B.;
RT   "The sunflower genome provides insights into oil metabolism, flowering and
RT   Asterid evolution.";
RL   Nature 546:148-152(2017).
RN   [2] {ECO:0000313|EMBL:OTG32846.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaves {ECO:0000313|EMBL:OTG32846.1};
RA   Langlade N., Munos S.;
RT   "Sunflower complete genome.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF5816481.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5816481.1};
RA   Gouzy J., Langlade N., Munos S.;
RT   "Helianthus annuus Genome sequencing and assembly Release 2.";
RL   Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-
CC         histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665,
CC         Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001137};
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};
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DR   EMBL; MNCJ02000318; KAF5816481.1; -; Genomic_DNA.
DR   EMBL; CM007892; OTG32846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251VCG7; -.
DR   STRING; 4232.A0A251VCG7; -.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr03g0134751; mRNA:HanXRQr2_Chr03g0134751; HanXRQr2_Chr03g0134751.
DR   Gramene; mRNA:HanXRQr2_Chr03g0134751; mRNA:HanXRQr2_Chr03g0134751; HanXRQr2_Chr03g0134751.
DR   InParanoid; A0A251VCG7; -.
DR   OMA; ADEAWND; -.
DR   OrthoDB; 8734at2759; -.
DR   Proteomes; UP000215914; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:EnsemblPlants.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IEA:EnsemblPlants.
DR   GO; GO:0009635; P:response to herbicide; IEA:EnsemblPlants.
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; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR006575; RWD_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR11476; HISTIDYL-TRNA SYNTHETASE; 1.
DR   PANTHER; PTHR11476:SF10; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF05773; RWD; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   SMART; SM00591; RWD; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50908; RWD; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000215914};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|EMBL:KAF5816481.1}.
FT   DOMAIN          36..145
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          399..703
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..288
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         429
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1215 AA;  136951 MW;  FB39F3D77C7EDA21 CRC64;
     MGHSSKKKKK RAGTGRRRPP SDHTSIDGVG GELLSDELTA LCAILQEDYD VVSESPPQIK
     IKLRPYSQDS GYEDVDVSAF LSIRFLPGYP YKYPKLTIIP EKGLSKSDAD NLLSLLHDQA
     NLNAREGRVM IYNLVEAAQE FLSEVVTIDQ PHLSRKNATV SCDRPSKGPF VYGFLDLFIG
     SGESWHWGLS VEESNSTIVA LDNLNNGAQP SWEKVNPTLK MGVIEGGQLK VKSTERLDIL
     EEDDSKSTDS LASQSAEPVE NVSVGEDYPL AEDTEEETDY DETESDILES ASSVDHHQIS
     HTVERDLILA HLLRLACAPK GPLADALTDV TSELVNLGIV SDRVADLATG SSSLFDRSFN
     QAFGNRMVAS KISNFWKTAA DSKGQHTSPT LSSRYLNDFE ELQPIGHGGF GHVVLCKNKL
     DGRQYAVKKI RLKDKSQPLD DRILREVATL SRLQHQHVVR YYQAWFETGD AGFYDDATWG
     SRTAASSSYS YIDHTSTDVI GQDNKVGTYL YIQMEYCPRT LRQMFESYSH FDKKDAWHLF
     RQIVEGLAHI HSQGIIHRDL TPNNIFFDAR SDIKIGDFGL AKFLKLEQLD QDVDPAETTG
     VSVDGTGQIG TYFYTAPEIE QRWPKINEKA DMYSLGIVFF ELWHPFSTGM ERHIVLSDLK
     KKGELPSDWV AEFPEQAALL RRMMSSSPSD RPSANELLQH ACPPRMESEL LDNILRTMHN
     SEDTSIYDKV VNAIFSEEIL STKIQDNDTE TLKLGRNVTS SIQHTDLDTE IRDLVSEVSA
     AVFRLHCAKH LETIPMRLLG DSVQFNRNNV KLLTNGGDML ELCHELRLPF INWVVLNQKS
     TFKRFEIGYV YRRSIGHSPP NRYLQGDFDV IGGDSAITEA EVIKATMDII TRFFHPESCD
     IHLNHGDLLE AIWSWIGIKA DHRQKVAELL SLLGSLRPQS TERKTKWVVI RRQLRQELNI
     TEGAVNKLQT VGLRFCGSAD HALPRLRGAL PSDTLTRKAL DELSQLFNYL RIWKIDKHVF
     IDPLMPPTEG YHRDSFFQIY LRKDNTLGSH TEGTLLAVGG RYDYLLHRMW QSEYKSNPPG
     AVGTSLALET IIHHSSVDVY RPFRNDSSRS VLVCSRGGGG LLEKRMELVT ELREDDIKAE
     FVPTLDPSLT EQYEYANEND IKCLIIISDT GVSQNGSVKI RHLELKKEKE VSRESLANFL
     SDAMASQFRN PSIWN
//
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