CDKG2_ORYSI
ID CDKG2_ORYSI Reviewed; 710 AA.
AC A2XUW1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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; ORFNames=OsI_015854;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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 -!- 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; CM000129; EAY94621.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XUW1; -.
DR SMR; A2XUW1; -.
DR STRING; 39946.A2XUW1; -.
DR iPTMnet; A2XUW1; -.
DR PRIDE; A2XUW1; -.
DR EnsemblPlants; BGIOSGA016643-TA; BGIOSGA016643-PA; BGIOSGA016643.
DR Gramene; BGIOSGA016643-TA; BGIOSGA016643-PA; BGIOSGA016643.
DR HOGENOM; CLU_000288_91_2_1; -.
DR OMA; DSGGRTH; -.
DR Proteomes; UP000007015; Chromosome 4.
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:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 3: Inferred from homology;
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_0000296113"
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
