ID A0A3B6GTX3_WHEAT Unreviewed; 411 AA.
AC A0A3B6GTX3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=CFC21_046668 {ECO:0000313|EMBL:KAF7035882.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS3D02G154400.1};
RN [1] {ECO:0000313|EMBL:KAF7035882.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7035882.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS3D02G154400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS3D02G154400.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS3D02G154400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7035882.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7035882.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196}.
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DR EMBL; CM022219; KAF7035882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6GTX3; -.
DR SMR; A0A3B6GTX3; -.
DR STRING; 4565.A0A3B6GTX3; -.
DR PaxDb; 4565-Traes_3DS_36B61656A-2; -.
DR EnsemblPlants; TraesCS3D02G154400.1; TraesCS3D02G154400.1; TraesCS3D02G154400.
DR Gramene; TraesCAD_scaffold_006429_01G000500.1; TraesCAD_scaffold_006429_01G000500.1; TraesCAD_scaffold_006429_01G000500.
DR Gramene; TraesCLE_scaffold_035969_01G000200.1; TraesCLE_scaffold_035969_01G000200.1; TraesCLE_scaffold_035969_01G000200.
DR Gramene; TraesCS3D02G154400.1; TraesCS3D02G154400.1; TraesCS3D02G154400.
DR Gramene; TraesCS3D03G0326800.1; TraesCS3D03G0326800.1.CDS; TraesCS3D03G0326800.
DR Gramene; TraesPAR_scaffold_043856_01G000100.1; TraesPAR_scaffold_043856_01G000100.1; TraesPAR_scaffold_043856_01G000100.
DR Gramene; TraesRN3D0100345800.1; TraesRN3D0100345800.1; TraesRN3D0100345800.
DR Gramene; TraesROB_scaffold_015556_01G000200.1; TraesROB_scaffold_015556_01G000200.1; TraesROB_scaffold_015556_01G000200.
DR Gramene; TraesWEE_scaffold_045661_01G000100.1; TraesWEE_scaffold_045661_01G000100.1; TraesWEE_scaffold_045661_01G000100.
DR OMA; KREACKT; -.
DR Proteomes; UP000019116; Chromosome 3D.
DR Proteomes; UP000815260; Chromosome 3D.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR PANTHER; PTHR45723:SF2; SERINE_THREONINE-PROTEIN KINASE RIO1; 1.
DR Pfam; PF01163; RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01245; RIO1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..165
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 279..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 46990 MW; F167FD7F513E053A CRC64;
MPLSAYHAHL SNHTHTALPV GLHVWRVGPL FPCPLHHQWD AGVTPLLLRL HVLVMEFIGK
GGWAAPRLKD AALSDDKLRE TYFEIVTTMR TLYQKCKLVH GDLSEYNILY FEGHLYIIDV
SQSVDLDHPS ALDFLKEDCL HVNDFFKKQG VAVMTVTELF NFVVDQNIAD EDVDDYLEKV
QQKILENGDT AADDDAIAPT VLVQTLDYVK QCEAEIVSMS MMQRPSIGYE PTADKLYDQP
LLGFVRTINE HTENQEAQSA QNTPEEPLDL QTKCCSLENK EEDESGDSES CSSSDEDGSW
HESTKMGPEE RKAYRKENKK KVKEEKRETR KTKIPKADKK KRKKMAKAKC KLSTATCLEN
QRNCHHTVNM IMPLHWSAIF RFVCILQTSM SPSLTRSRME LKRLLMCLIF L
//
