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Database: UniProt
Entry: A0A1B6QD81_SORBI
LinkDB: A0A1B6QD81_SORBI
Original site: A0A1B6QD81_SORBI 
ID   A0A1B6QD81_SORBI        Unreviewed;      1135 AA.
AC   A0A1B6QD81;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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_3002G239700 {ECO:0000313|EMBL:KXG35861.1};
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:KXG35861.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:KXG35861.1, 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; KXG35861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B6QD81; -.
DR   EnsemblPlants; KXG35861; KXG35861; SORBI_3002G239700.
DR   Gramene; KXG35861; KXG35861; SORBI_3002G239700.
DR   eggNOG; ENOG502QSU9; Eukaryota.
DR   InParanoid; A0A1B6QD81; -.
DR   OMA; LLRWKDT; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 5.
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; 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; PTHR27008; OS04G0122200 PROTEIN; 1.
DR   PANTHER; PTHR27008:SF486; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 7.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00369; LRR_TYP; 9.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF52047; RNI-like; 2.
DR   PROSITE; PS51450; LRR; 1.
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};
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   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          802..1090
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1090..1135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..42
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1116..1135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         831
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1135 AA;  119924 MW;  F0B969B976F7ACDE CRC64;
     MLARGATSQS QPSTALPPPL SSRHPPASAS PPRRAPPMPP RSRAAAPRLA FLVPLACALL
     LVSLSPCHCV NEQGQALLRW KDTLRPASGA LASWRAADAN PCRWTGVSCN ARGDVVGLSI
     TSVDLQGPLP ANLQPLAASL KTLELSGTNL TGAIPKEMGG YGELTTLDLS KNQLTGAIPD
     ELCRLAKLES LALNSNSLRG AIPDDIGNLT SLAYLTLYDN ELSGPIPPSI GNLKKLQVLR
     AGGNQGMKGP LPPEIGGCSN LTMLGLAETG VSGSLPETIG QLKKIQTIAI YTTLLSGRIP
     ESIGNCTELT SLYLYQNSLS GPIPAQLGQL KKLQTLLLWQ NQLVGAIPPE LGQCKELTLI
     DLSLNSLTGS IPASLGRLPN LQQLQLSTNQ LTGTIPPELS NCTSLTDIEV DNNLLSGEIS
     IDFPRLSNLT LFYAWKNRLT GGVPVSLAEA PSLQAVDLSY NNLTGPIPKA LFGLQNLTKL
     LLLNNELSGP IPPEIGNCTN LYRLRLNGNR LSGTIPAEIG NLKNLNFLDM SENHLVGPVP
     AAISGCASLE FLDLHSNALS GALPDTLPRS LQLIDVSDNQ LAGPLSSSIG SMPELTKLYM
     GNNRLTGGIP PELGSCEKLQ LLDLGGNAFS GDIPSELGLL PSLEISLNLS SNRLSGEIPS
     QFAGLDKLGS LDLSHNELSG SLEPLAALQN LVTLNISYNA FSGELPNTPF FQKLPLSDLA
     GNRHLVVGDG SDESSRRGAI SSLKIAMSVL ATVSALLLVS ATYMLARTHR RGGGRIIHGE
     GSWEVTLYQK LDITMDDVLR GLTSANMIGT GSSGAVYKVD TPNGYTLAVK KMWSSDEATS
     AAFRSEIAAL GSIRHRNIVR LLGWAANGGT RLLFYGYLPN GSLSGLLHGG HAGKGSPADE
     WGARYEIALG VAHAVAYLHH DCVPAILHGD VKSMNVLLGP AYEPYLADFG LARVLAAATS
     KLDTGKQPRI AGSYGYMAPE YASMQRISEK SDVYSFGVVL LEILTGRHPL DPTLSGGAHL
     VQWVREHVQA KRDAAELLDA RLRGRASEAD VHEMRQVLSV AALCVSRRAD DRPAMKDVVA
     LLKEIRRPAA VDDAKQPSPT ATGAAATPAP VSPVVSAHSR GQSSSCSFAV SEYSA
//
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