CDKG1_ORYSJ
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 03-AUG-2022, entry version 118.
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}.
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; 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; 4530.OS02T0602100-02; -.
DR PaxDb; Q6K5F8; -.
DR PRIDE; 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; 925637at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q6K5F8; baseline and differential.
DR Genevisible; Q6K5F8; OS.
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; 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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR CDD; cd07843; STKc_CDC2L1; 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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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
