ID   CDKG1_ORYSJ             Reviewed;         693 AA.
AC   Q6K5F8; B7F3X5;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Cyclin-dependent kinase G-1;
DE            Short=CDKG;1;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
GN   Name=CDKG-1; OrderedLocusNames=Os02g0602100, LOC_Os02g39010;
GN   ORFNames=OJ1669_F01.7, OJ1791_B03.45;
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 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}.
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DR   EMBL; AP004124; BAD19341.1; -; Genomic_DNA.
DR   EMBL; AP005385; BAD22167.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF09269.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS79623.1; -; Genomic_DNA.
DR   EMBL; AK111593; BAG99322.1; -; mRNA.
DR   RefSeq; XP_015625437.1; XM_015769951.1.
DR   AlphaFoldDB; Q6K5F8; -.
DR   SMR; Q6K5F8; -.
DR   STRING; 39947.Q6K5F8; -.
DR   PaxDb; 39947-Q6K5F8; -.
DR   EnsemblPlants; Os02t0602100-02; Os02t0602100-02; Os02g0602100.
DR   GeneID; 4329899; -.
DR   Gramene; Os02t0602100-02; Os02t0602100-02; Os02g0602100.
DR   KEGG; osa:4329899; -.
DR   eggNOG; KOG0663; Eukaryota.
DR   HOGENOM; CLU_000288_91_2_1; -.
DR   InParanoid; Q6K5F8; -.
DR   OMA; HEENDYH; -.
DR   OrthoDB; 313344at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   ExpressionAtlas; Q6K5F8; 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:SF403; CYCLIN-DEPENDENT KINASE G-1; 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; Q6K5F8; 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..693
FT                   /note="Cyclin-dependent kinase G-1"
FT                   /id="PRO_0000296110"
FT   DOMAIN          349..640
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..684
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        473
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         355..363
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         378
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         359
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         360
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         500
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         506
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   693 AA;  78720 MW;  E6AB21552A7826A6 CRC64;
     MAAGSHGGYR GYEVAREREH DVGVSRRSKE HYHHRHPSRH RDSERRRDGG RSGGRELSNG
     YSHRRDSPRP PPRRRPSEGR TEDREPGEVS GGSGSERSGE RPMKTGEPRE NGVTRVSKEE
     AKMSPSKKRK QSPVIWDRNG SKRQARDPVR GIREVDAVVA EIIMHQSHSL PVMSSLSSIG
     DGHSPMILDV SVDKVQEYEK NRIVDEEEEG YPTMRNILTS RWADAGDEEE NVFVPKKKKS
     VSPVDSIERG STKKVTSPES GEVLVYNSVR SSSRSSDSGV LQGSANRDLE VEKGDNIDVE
     EAADDDYPAG HLLDSDFEGE DCRSETPECT RSPRRCINML QGCRSVDEFE RLNTINEGTY
     GVVFRVRDKR TGEIVALKKV KMEKEREGFP LTSLREMNIL LSFHHPSIVE VKEVVVGSND
     RDIFMVMEYM EHDLKGVMET MKQPYSQSEV KCLMLQLLEG VKYLHDNWVL HRDLKTSNLL
     LNNRGELKIC DFGLSRQYGS PLKPYTQLVV TLWYRAPELL LGAKDYSTAI DMWSLGCIMG
     ELLSKGPLFN GKSEIDQLDK IFRTLGTPDE NIWPGYSKLP GATVKFGKQT HNRLRDKFRA
     VSFTGGPMLS EAGFDLLNRL LTYDPEKRIS AEDALNHEWF RELPLPRSKD FMPTFPALNE
     QDRRFKKHMK SPDPLEEQRM KEQGNNGDRG LFG
//