ID A0A0D2TAQ1_GOSRA Unreviewed; 772 AA.
AC A0A0D2TAQ1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=B456_007G075400 {ECO:0000313|EMBL:KJB40730.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB40730.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB40730.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; CM001746; KJB40728.1; -; Genomic_DNA.
DR EMBL; CM001746; KJB40729.1; -; Genomic_DNA.
DR EMBL; CM001746; KJB40730.1; -; Genomic_DNA.
DR RefSeq; XP_012489517.1; XM_012634063.1.
DR RefSeq; XP_012489518.1; XM_012634064.1.
DR AlphaFoldDB; A0A0D2TAQ1; -.
DR EnsemblPlants; KJB40728; KJB40728; B456_007G075400.
DR EnsemblPlants; KJB40729; KJB40729; B456_007G075400.
DR EnsemblPlants; KJB40730; KJB40730; B456_007G075400.
DR GeneID; 105802432; -.
DR Gramene; KJB40728; KJB40728; B456_007G075400.
DR Gramene; KJB40729; KJB40729; B456_007G075400.
DR Gramene; KJB40730; KJB40730; B456_007G075400.
DR KEGG; gra:105802432; -.
DR eggNOG; KOG0610; Eukaryota.
DR OMA; HSCKTAY; -.
DR OrthoDB; 1217077at2759; -.
DR Proteomes; UP000032304; Chromosome 7.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd05574; STKc_phototropin_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45637; FLIPPASE KINASE 1-RELATED; 1.
DR PANTHER; PTHR45637:SF19; SERINE_THREONINE-PROTEIN KINASE D6PKL3; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 379..716
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 85401 MW; 6728BA8604133130 CRC64;
MDSLAISSSK NQNLGSGIGN NDPPSTSGMP RRPSRPPLPK QSENEGLSSA YHGVRTVQHH
DGSIGSQKHS CKTAYDNLVC EEMPNMAKHY YDSSKMKSEL TGKILAVASK SSFKHPIDDH
KSSNSTASLE YEQTVSGVHY YDSSKVKSES VGKILTTASK SSSKHPIDDH KTSDSIASLE
YEKPVPGAHY YDSSKVKSES VRSKSSFKHP IDDHKSSNSF RSLQSEKTVP GVHYYDSSKV
KSESVGKIST TASKSSFKHP VDEKLVPSAI QLNNHIVSQS EPSICVSPSS SMCTRSLYAE
AKQSFTNTEV SECASSDESG EVSRKTSINR GSNCSDISEE SSSSCSISAI YKPHQANDIR
WAAIQAVRSR KGELGFKHFR VLRKLGCGDI GSVYQSELTG TNTYFAMKVM DKALLASRKK
LLRAQTEREI LQSLDHPFLP TLYTHFETEK LSCLVMEFCP GGDLHALRQR QPGKYFSEQA
ARFYVAEVLL ALEYLHMLGI IYRDLKPENV LVREDGHIML SDFDLSLRCS VSPTLVKSSN
STLASKHSVY CAQPACLQPT CVMQPDCIQP ACFGPRLFPS KSKKEKKSKI KSETNQQVSP
LPELIAEPTN ARSMSFVGTH EYLAPEIIKG QGHGSAVDWW TFGIFLYELL FGKTPFKGAE
NRATLFNVIG QPLRFPEYPN VSFAAKDLIR GLLVKEPQHR LAYRRGATEV KQHPFFQSVN
WALIRCANPP EVPKPSMTDF FAGTNMSKAP TNNMVPGLDV KPSGNYLEID FF
//
