ID C5X896_SORBI Unreviewed; 1214 AA.
AC C5X896;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=SORBI_3002G155400 {ECO:0000313|EMBL:EER96489.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER96489.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EER96489.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; CM000761; EER96489.1; -; Genomic_DNA.
DR RefSeq; XP_002459968.1; XM_002459923.1.
DR AlphaFoldDB; C5X896; -.
DR STRING; 4558.C5X896; -.
DR EnsemblPlants; EER96489; EER96489; SORBI_3002G155400.
DR GeneID; 8062054; -.
DR Gramene; EER96489; EER96489; SORBI_3002G155400.
DR KEGG; sbi:8062054; -.
DR eggNOG; ENOG502QQ5H; Eukaryota.
DR HOGENOM; CLU_000288_22_4_1; -.
DR InParanoid; C5X896; -.
DR OMA; SHAHPKK; -.
DR OrthoDB; 385706at2759; -.
DR Proteomes; UP000000768; Chromosome 2.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.310; -; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR045381; BRI1_island_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45974:SF272; LRR RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE FLS2; 1.
DR PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR Pfam; PF20141; Island; 1.
DR Pfam; PF00560; LRR_1; 7.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 2.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1214
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002958783"
FT TRANSMEM 827..847
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 912..1196
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 941
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1214 AA; 129234 MW; 3BEDC9D620261D80 CRC64;
MAASTTAAAW FLVAVVLVLL HATAPAIAGA EDEAAALLAF RRASVADDPR GALSGWAMAN
ATAAAPCSWA GVSCAPPPDG RVVAINLTGM ALVGELRLDA LLALPALQRL DLRGNAFYGN
LSHAHAAASA SPCALVEVDM SSNTFNGTLP AAFLATCGAL QSLNLSRNAL VGGGFPFAPS
LRSLDLSRNH LADVGLLNYS FAGCHGLRYL NLSANQFVGR LPELATCSAV SVLDVSWNHM
SGALPAGFMA AAPPNLTHLS IAGNNFSGDV SAYDFGGCAN LTVLDWSFNG LSSSELPPSL
ANCGRLEMLD VSGNKLLGGP IPTFLTGFSS LKRLALAGNE FSGTIPDELS QLCGRIVELD
LSSNRLVGGL PASFAKCRSL EVLDLSGNQL SGSFVDSVVS TISSLRELRL SFNNITGQNP
LPVLAAGCPL LEVIDLGSNE LDGEIMEDLC SSLPSLRKLF LPNNYLKGTV PKSLGNCANL
ESIDLSFNFL VGQIPKEIIL LPKLIDLVMW ANGLSGEIPD MLCSNGTTLE TLVLSYNNFT
GGIPPSITRC VNLIWVSFSG NHLIGSVPHG FGKLQKLAIL QLNKNQLSGP VPAELGSCIN
LIWLDLNSNS FTGIIPPELA SQTGLIPGGI VSGKQFAFLR NEAGNICPGA GVLFEFFGIR
PERLAAFPTV HLCPSTRIYV GTMDYKFQSN GSMIFLDLSY NRLTGTIPAG LGNMMFLEVM
NLGHNDLNGT IPYEFSGLKL VGAMDLSNNH LTGGIPPGLG TLSFLADLDV SSNNLSGPIP
LTGQLSTFPQ SRYANNPGLC GIPLPPCGHD PGQGSVPSAS SGRRKTVGGS ILVGIALSML
ILLLLLVTLC KLRKNQKTEE IRTGYIESLP TSGTSSWKLS GVHEPLSINV ATFEKPLRKL
TFAHLLEATD GFSAETLIGS GGFGEVYKAK LKDGTVVAIK KLIHFTGQGD REFTAEMETI
GKIKHRNLVP LLGYCKIGDE RLLVYEYMKH GSLDVVLHDQ AKAGVKLDWA ARKKIAIGSA
RGLAFLHHSC IPHIIHRDMK SSNVLLDSNL DARVSDFGMA RLMNALDTHL SVSTLAGTPG
YVPPEYYQSF RCTTKGDVYS YGVVLLELLS GKKPIDPTEF GDNNLVGWVK QMVKENRSSE
IFDPTLTNTK SGEAELYQSL KIARECLDDR PNQRPTMIQV MAMFKELQLD SDSDFLDGFS
INSSTIDESA EKSS
//
