ID C5YL32_SORBI Unreviewed; 655 AA.
AC C5YL32;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=SORBI_3007G132300 {ECO:0000313|EMBL:EES15012.1};
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:EES15012.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EES15012.1, 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).
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DR EMBL; CM000766; EES15012.1; -; Genomic_DNA.
DR RefSeq; XP_002445517.1; XM_002445472.1.
DR AlphaFoldDB; C5YL32; -.
DR EnsemblPlants; EES15012; EES15012; SORBI_3007G132300.
DR GeneID; 8075388; -.
DR Gramene; EES15012; EES15012; SORBI_3007G132300.
DR KEGG; sbi:8075388; -.
DR eggNOG; ENOG502QSFF; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; C5YL32; -.
DR OMA; LGMDCTE; -.
DR OrthoDB; 395327at2759; -.
DR Proteomes; UP000000768; Chromosome 7.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR48010:SF24; INACTIVE RECEPTOR KINASE-RELATED; 1.
DR PANTHER; PTHR48010; OS05G0588300 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..655
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002960272"
FT TRANSMEM 259..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 361..635
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 655 AA; 69737 MW; A6CC91D1B6DE0449 CRC64;
MARQRRPVGG ARVAVLFVVV ALLAAALPGL VAQDLAGDRL ALLALRDALD RGRLLPWNTA
DPTPCKWRGV LCSNQTGQGV PQRVVELRLP GKRLIGTIPL GTVGNLTALQ ALSLRHNGIT
GGIPADIGNC DQLTVVNLTR NQFAGAVPEG FFSLAVLRNV DLSRNRLAGG VSQEFNRLKQ
LDTLFLDNND FAGALPPGFY LPSLSRFNVS FNAQLTGPVP ASLAGMPASA FQGTALCGGP
LLACPNSPGG EKKKRLSRWA IVGIIAGAAL VLLLIVGLVA CLRRRQVASA ASAGRPTETA
AAANVRETTT PITVTLARTD RDAVKQSHAP PLAPVMISEG KKLVFLGSAP DRPYDLETLL
RASAEVLGKG QHGTTYRATL DGGEPVLAVK RLREVHLSEN EFRHRATALG ALHHGNLTRL
RAYFYSKEEK LLVYDFVGAG SLSALLHDGS LEGRARLDFT ARARIALAAA RGVAFIHQGG
AKSSHGNLKS SNIVVTATRD GAYVSDYGIA QVTGAAAPPP RRGAGYHAPE VTDARSVPQS
ADVYSFGVVV LELLSGRAPQ HALPEGADGV DLPRWVRSVV QEEWTSEVFD AAIANEPRVE
GEMMRLLQLG IECTEQRPDR RPTMAEVEAR IERIVEDTCR KDDFSSTDGS RSVSA
//