ID CDKA1_ORYSJ Reviewed; 294 AA. AC P29618; Q10SL8; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 24-JAN-2024, entry version 156. DE RecName: Full=Cyclin-dependent kinase A-1; DE Short=CDKA;1; DE EC=2.7.11.22; DE EC=2.7.11.23; DE AltName: Full=CDC2Os-1; DE AltName: Full=Cell division control protein 2 homolog 1; GN Name=CDKA-1; Synonyms=CDC2-1; GN OrderedLocusNames=Os03g0118400, LOC_Os03g02680; 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 [MRNA]. RC STRAIN=cv. Nipponbare; RX PubMed=1376401; DOI=10.1007/bf00587555; RA Hashimoto J., Hirabayashi T., Hayano Y., Hata S., Ohashi Y., Suzuka I., RA Utsugi T., Toh-e A., Kikuchi Y.; RT "Isolation and characterization of cDNA clones encoding cdc2 homologues RT from Oryza sativa: a functional homologue and cognate variants."; RL Mol. Gen. Genet. 233:10-16(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16109971; DOI=10.1101/gr.3869505; RG The rice chromosome 3 sequencing consortium; RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K., RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J., RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., RA Jin W., Lee H.R., Jiang J., Jackson S.; RT "Sequence, annotation, and analysis of synteny between rice chromosome 3 RT and diverged grass species."; RL Genome Res. 15:1284-1291(2005). RN [3] 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 [4] 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 [5] 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 [6] RP DEVELOPMENTAL STAGE. RX PubMed=9076986; DOI=10.1046/j.1365-313x.1997.11020181.x; RA Sauter M.; RT "Differential expression of a CAK (cdc2-activating kinase)-like protein RT kinase, cyclins and cdc2 genes from rice during the cell cycle and in RT response to gibberellin."; RL Plant J. 11:181-190(1997). RN [7] RP INDUCTION. RX PubMed=9880342; DOI=10.1104/pp.119.1.21; RA Lorbiecke R., Sauter M.; RT "Adventitious root growth and cell-cycle induction in deepwater rice."; RL Plant Physiol. 119:21-30(1999). RN [8] RP TISSUE SPECIFICITY. RX PubMed=9880343; DOI=10.1104/pp.119.1.31; RA Umeda M., Umeda-Hara C., Yamaguchi M., Hashimoto J., Uchimiya H.; RT "Differential expression of genes for cyclin-dependent protein kinases in RT rice plants."; RL Plant Physiol. 119:31-40(1999). RN [9] RP PHOSPHORYLATION AT THR-161, AND MUTAGENESIS OF THR-161. RX PubMed=11029700; DOI=10.1046/j.1365-313x.2000.00846.x; RA Yamaguchi M., Fabian T., Sauter M., Bhalerao R.P., Schrader J., RA Sandberg G., Umeda M., Uchimiya H.; RT "Activation of CDK-activating kinase is dependent on interaction with H- RT type cyclins in plants."; RL Plant J. 24:11-20(2000). RN [10] 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 -!- TISSUE SPECIFICITY: Expressed in the dividing region of the root apex CC and in differentiated cells such as those in the sclerenchyma, CC pericycle and parenchyma of the central cylinder. CC {ECO:0000269|PubMed:9880343}. CC -!- DEVELOPMENTAL STAGE: Expressed throughout the cell cycle. CC {ECO:0000269|PubMed:9076986}. CC -!- INDUCTION: By submergence. Down-regulated by cytokinin. CC {ECO:0000269|PubMed:17443292, ECO:0000269|PubMed:9880342}. CC -!- PTM: Phosphorylated at Thr-161 by CDKD-1. CC {ECO:0000269|PubMed:11029700}. 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; X60374; CAA42922.1; -; mRNA. DR EMBL; DP000009; ABF93669.1; -; Genomic_DNA. DR EMBL; AP008209; BAF10686.1; -; Genomic_DNA. DR EMBL; AP014959; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; S22440; S22440. DR RefSeq; XP_015631633.1; XM_015776147.1. DR AlphaFoldDB; P29618; -. DR SMR; P29618; -. DR STRING; 39947.P29618; -. DR iPTMnet; P29618; -. DR PaxDb; 39947-P29618; -. DR GeneID; 4331415; -. DR KEGG; osa:4331415; -. DR eggNOG; KOG0594; Eukaryota. DR InParanoid; P29618; -. DR OrthoDB; 244018at2759; -. DR PlantReactome; R-OSA-9640760; G1 phase. DR PlantReactome; R-OSA-9640887; G1/S transition. DR Proteomes; UP000000763; Chromosome 3. DR Proteomes; UP000059680; Chromosome 3. DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0030332; F:cyclin binding; IBA:GO_Central. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central. DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central. DR GO; GO:0051445; P:regulation of meiotic cell cycle; IBA:GO_Central. DR GO; GO:0010033; P:response to organic substance; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd07835; STKc_CDK1_CdkB_like; 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 PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF549; CYCLIN-DEPENDENT KINASE A-1; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 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. PE 1: Evidence at protein level; KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..294 FT /note="Cyclin-dependent kinase A-1" FT /id="PRO_0000085755" FT DOMAIN 4..287 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 127 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 10..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 14 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" FT MOD_RES 15 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250" FT MOD_RES 161 FT /note="Phosphothreonine; by CAK" FT /evidence="ECO:0000269|PubMed:11029700" FT MUTAGEN 161 FT /note="T->A: Loss of phosphorylation by CDKD-1." FT /evidence="ECO:0000269|PubMed:11029700" SQ SEQUENCE 294 AA; 34071 MW; 51322D93AEF4C131 CRC64; MEQYEKEEKI GEGTYGVVYR ARDKVTNETI ALKKIRLEQE DEGVPSTAIR EISLLKEMHH GNIVRLHDVI HSEKRIYLVF EYLDLDLKKF MDSCPEFAKN PTLIKSYLYQ ILRGVAYCHS HRVLHRDLKP QNLLIDRRTN ALKLADFGLA RAFGIPVRTF THEVVTLWYR APEILLGSRQ YSTPVDMWSV GCIFAEMVNQ KPLFPGDSEI DELFKIFRVL GTPNEQSWPG VSSLPDYKSA FPKWQAQDLA TIVPTLDPAG LDLLSKMLRY EPNKRITARQ ALEHEYFKDL EMVQ //