ID CDKG2_ORYSJ Reviewed; 710 AA. AC Q7XUF4; B7F3Y9; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2004, sequence version 2. DT 27-MAR-2024, entry version 128. DE RecName: Full=Cyclin-dependent kinase G-2; DE Short=CDKG;2; DE EC=2.7.11.22; DE EC=2.7.11.23; GN Name=CDKG-2; OrderedLocusNames=Os04g0488000, LOC_Os04g41100; GN ORFNames=OJ991113_30.14; 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=12447439; DOI=10.1038/nature01183; RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T., RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R., RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G., RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C., RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J., RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J., RA Li J., Hong G., Xue Y., Han B.; RT "Sequence and analysis of rice chromosome 4."; RL Nature 420:316-320(2002). RN [2] 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 [3] 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 [4] 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 [5] 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 [6] 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: Down-regulated by cytokinin. {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; AL662946; CAD41330.2; -; Genomic_DNA. DR EMBL; AP008210; BAF15061.1; -; Genomic_DNA. DR EMBL; AP014960; BAS89811.1; -; Genomic_DNA. DR EMBL; AK111619; BAG99336.1; -; mRNA. DR RefSeq; XP_015635720.1; XM_015780234.1. DR RefSeq; XP_015635721.1; XM_015780235.1. DR RefSeq; XP_015635722.1; XM_015780236.1. DR AlphaFoldDB; Q7XUF4; -. DR SMR; Q7XUF4; -. DR STRING; 39947.Q7XUF4; -. DR PaxDb; 39947-Q7XUF4; -. DR EnsemblPlants; Os04t0488000-01; Os04t0488000-01; Os04g0488000. DR EnsemblPlants; Os04t0488000-02; Os04t0488000-02; Os04g0488000. DR GeneID; 4336224; -. DR Gramene; Os04t0488000-01; Os04t0488000-01; Os04g0488000. DR Gramene; Os04t0488000-02; Os04t0488000-02; Os04g0488000. DR KEGG; osa:4336224; -. DR eggNOG; KOG0663; Eukaryota. DR HOGENOM; CLU_000288_91_2_1; -. DR InParanoid; Q7XUF4; -. DR OMA; PIKERDM; -. DR OrthoDB; 313344at2759; -. DR Proteomes; UP000000763; Chromosome 4. DR Proteomes; UP000059680; Chromosome 4. DR ExpressionAtlas; Q7XUF4; 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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central. DR CDD; cd07843; STKc_CDC2L1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR045267; CDK11/PITSLRE_STKc. 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:SF585; CYCLIN-DEPENDENT KINASE G-2; 1. DR Pfam; PF00069; Pkinase; 1. 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; Q7XUF4; 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..710 FT /note="Cyclin-dependent kinase G-2" FT /id="PRO_0000296112" FT DOMAIN 365..656 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..350 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 8..29 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 39..68 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 117..136 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 139..162 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 168..183 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 209..227 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 237..256 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 303..317 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 332..346 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 489 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 371..379 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 394 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 375 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" FT MOD_RES 376 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250" FT MOD_RES 516 FT /note="Phosphoserine" FT /evidence="ECO:0000250" FT MOD_RES 522 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" SQ SEQUENCE 710 AA; 79883 MW; C8A958D5DDA4EE91 CRC64; MAAGRHGGYR DYEARERELD AEASRRSKEQ QHHHHPSGRH QRGDSDPRCE ADRRRDGGRS RGGRELSNGY GHRRSPPPRS RLSARLGDRE PGEVLSGSAS DDSGGRPHRA RENGVSSSSR DGESVVAASA SSPSKKRKFS PIIWDRDSPK PMHSDVAKGK KAVDSVPTEL PLPPPPPLPP QDHIPERLAV EKSPMDVEPA VASESPEQLQ EHAESRVMEE EEEYSTMRNI STSRWAGAND DEEEGAPHRK KKSASPADSA ELGQRKKALS PELGEVVASD ISGGRTMSRS SDSGRLGADE NEDLEVDKDD YMDVDRDDDG NSDIANHQSG MDSEYEVRRS ETPEPVKPPH RCINMLQGCR SVDEFERLNK INEGTYGVVY RARDKKTGEI VALKKVKMEK EREGFPLTSL REINILLSFH HPSIVDVKEV VVGSSLDSIF MVMEYMEHDL KGVMEAMKQP YSQSEVKCLM LQLLEGVKYL HDNWVLHRDL KTSNLLLNNR GELKICDFGL SRQYGSPLKP YTQLVVTLWY RAPELLLGTK EYSTAIDMWS VGCIMAELLA KEPLFNGKTE FEQLDKIFRT LGTPNEKIWP GYAKLPGVKV NFVKQPYNRL RDKFPAASFS GRPILSEAGF DLLNNLLTYD PEKRLSADAA LQHEWFREVP LPKSKDFMPT FPALNELDRR TKRYLKSPDP LEEQRLKELQ GNIGNRGLFG //