ID CDKF1_ORYSJ Reviewed; 479 AA. AC Q5Z754; A0A0P0WWF8; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 24-JAN-2024, entry version 128. DE RecName: Full=Cyclin-dependent kinase F-1; DE Short=CDKF;1; DE EC=2.7.11.22; DE EC=2.7.11.23; GN Name=CDKF-1; OrderedLocusNames=Os06g0334400, LOC_Os06g22820; GN ORFNames=OSJNBa0012F14.17; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). RN [5] RP INDUCTION, AND GENE FAMILY. RX PubMed=17443292; DOI=10.1007/s11103-007-9154-y; RA Guo J., Song J., Wang F., Zhang X.S.; RT "Genome-wide identification and expression analysis of rice cell cycle RT genes."; RL Plant Mol. Biol. 64:349-360(2007). 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=2.7.11.22; 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=2.7.11.22; CC -!- CATALYTIC ACTIVITY: CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho- CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA- CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, CC ChEBI:CHEBI:456216; EC=2.7.11.23; CC -!- INDUCTION: By auxin. Down-regulated by cytokinin. CC {ECO:0000269|PubMed:17443292}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP004784; BAD61885.1; -; Genomic_DNA. DR EMBL; AP008212; BAF19465.1; -; Genomic_DNA. DR EMBL; AP014962; BAS97580.1; -; Genomic_DNA. DR EMBL; AK120969; -; NOT_ANNOTATED_CDS; mRNA. DR RefSeq; XP_015644444.1; XM_015788958.1. DR AlphaFoldDB; Q5Z754; -. DR SMR; Q5Z754; -. DR STRING; 39947.Q5Z754; -. DR iPTMnet; Q5Z754; -. DR PaxDb; 39947-Q5Z754; -. DR EnsemblPlants; Os06t0334400-01; Os06t0334400-01; Os06g0334400. DR GeneID; 4340934; -. DR Gramene; Os06t0334400-01; Os06t0334400-01; Os06g0334400. DR KEGG; osa:4340934; -. DR eggNOG; KOG0594; Eukaryota. DR InParanoid; Q5Z754; -. DR OMA; VWPGCVK; -. DR OrthoDB; 1211503at2759; -. DR Proteomes; UP000000763; Chromosome 6. DR Proteomes; UP000059680; Chromosome 6. DR ExpressionAtlas; Q5Z754; baseline and differential. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0019912; F:cyclin-dependent protein kinase activating kinase activity; IBA:GO_Central. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC. DR GO; GO:0010078; P:maintenance of root meristem identity; IEA:EnsemblPlants. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF171; CYCLIN-DEPENDENT KINASE 20; 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. DR Genevisible; Q5Z754; OS. PE 2: Evidence at transcript level; KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..479 FT /note="Cyclin-dependent kinase F-1" FT /id="PRO_0000296105" FT DOMAIN 24..419 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 429..479 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 444..467 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 146 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 30..38 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 53 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 291 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" FT CONFLICT 253 FT /note="N -> D (in Ref. 4; AK120969)" FT /evidence="ECO:0000305" FT CONFLICT 394 FT /note="S -> G (in Ref. 4; AK120969)" FT /evidence="ECO:0000305" FT CONFLICT 450 FT /note="F -> L (in Ref. 4; AK120969)" FT /evidence="ECO:0000305" SQ SEQUENCE 479 AA; 52073 MW; 0FA906213F770759 CRC64; MAIGGGGGGG SWSIHGRPDV TSRYEVLGRA GSGAYADVYR GRRRSDGAPV ALKEVHDAVS ARREADALLA AAPSRHVVAL LDHFPGGDHD DDVLVLEWLP LDLSAVVRAA AAARPSALPA AQRKRWMLQV LEGVAACHSA GVVHRDLKPA NLLISEDGVL KVADLGQARI LQETGTYQGM HPYEQSSGVE PWVSQQRAVL HGVKENHPSH DSETQTGQEP ERLTAADYLH EMDQLRAKST HGDVDKMSLQ DGNASCLATC STADIDDDPF RASYSYDAEE GMLEEESGAF TSCVGTRWFR APELLYGSTN YGQEVDLWSL GCILAELFNL EPIFPGTSDI DQIGRIISVL GNITEETFPG CSNLPDYNKI FFNKVEKPIG LEACLPDRSA SEVSIIKRLL CYDPTKRASA ADLLNDPYFA EEPLPVPIEG LQVPESKDED DDSTEEWANF RGGDSDSDFD EFGSMDVTKT DKGFSIRFS //