ID C5YNQ9_SORBI Unreviewed; 588 AA.
AC C5YNQ9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SORBI_3008G097900 {ECO:0000313|EMBL:EES15978.1};
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:EES15978.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EES15978.1, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00649}.
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DR EMBL; CM000767; EES15978.1; -; Genomic_DNA.
DR RefSeq; XP_002442140.1; XM_002442095.1.
DR AlphaFoldDB; C5YNQ9; -.
DR STRING; 4558.C5YNQ9; -.
DR EnsemblPlants; EES15978; EES15978; SORBI_3008G097900.
DR GeneID; 8063264; -.
DR Gramene; EES15978; EES15978; SORBI_3008G097900.
DR KEGG; sbi:8063264; -.
DR eggNOG; KOG1886; Eukaryota.
DR HOGENOM; CLU_027180_0_0_1; -.
DR InParanoid; C5YNQ9; -.
DR OMA; PASNHTH; -.
DR OrthoDB; 419101at2759; -.
DR Proteomes; UP000000768; Chromosome 8.
DR ExpressionAtlas; C5YNQ9; baseline.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR PANTHER; PTHR45707; C2 CALCIUM/LIPID-BINDING PLANT PHOSPHORIBOSYLTRANSFERASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR45707:SF79; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00509; TFS2N; 1.
DR SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00649}; Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 45..344
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 494..575
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51319"
FT REGION 368..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 588 AA; 66448 MW; 5DF902322C58C55D CRC64;
MAGRCDGVTH GVTPTGGQLH SGSTCHGGFG KVYELEDLQN ITNNFSEERL LGEGGFGKVY
KGLLPNGDII AVKKLTSTMP GIKDRQFDNE AWHLMRLSHP NIVQLVGYCS HTEEILVLHQ
GKYVYAEKSE RLLCLEYQPK GSLHEHLSDE SSGLDWDSRY KIIEGICNGL HYLHEKWQAS
TPIIHMDLKP KNILLDDNMV PKIADFGLSR LFGEEQTRTC TASRDGTLGY MAPEYLNRGI
ITKKLDIFSL GVIIIEIVTG HKDYPDETDT SSQEFIELVL KNWRNRLEKT PGYTTAFSIF
PSFCREIDYQ RIRRCIQIGL ACVKLNRAKR PTTLEVLNML HKSEGAECSN GKEDYTNERP
EEVNGPLYNK AEDRLNGTQN FGSSKGKKRE RDERGIDPAK LHRDSLHNIY DSEPGSFKLD
DMESKIAKIK KGGLANVEAV EELLHLMKLD QTEQRIDLSG RVILADVIAA TEKPDILHVF
MESKGLLVLD SWLQEAHKWR SDDGSSPKEA DKPIGPGEFF LAMLRALARL PINLSALQRC
SIGKSVNRLR GHKNVEIQKK SRLLIEDGKR RIDAEMKLGR VWLRTKQN
//
