ID   CDKD1_ARATH             Reviewed;         398 AA.
AC   Q9C9U2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Cyclin-dependent kinase D-1;
DE            Short=CDKD;1;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
DE   AltName: Full=CDK-activating kinase 3-At;
DE            Short=CAK3-At;
GN   Name=CDKD-1; OrderedLocusNames=At1g73690; ORFNames=F25P22.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=12527363; DOI=10.1016/s0014-5793(02)03780-8;
RA   Shimotohno A., Matsubayashi S., Yamaguchi M., Uchimiya H., Umeda M.;
RT   "Differential phosphorylation activities of CDK-activating kinases in
RT   Arabidopsis thaliana.";
RL   FEBS Lett. 534:69-74(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11971144; DOI=10.1105/tpc.010445;
RA   Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.;
RT   "Genome-wide analysis of core cell cycle genes in Arabidopsis.";
RL   Plant Cell 14:903-916(2002).
RN   [6]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-40.
RX   PubMed=15486101; DOI=10.1105/tpc.104.025601;
RA   Shimotohno A., Umeda-Hara C., Bisova K., Uchimiya H., Umeda M.;
RT   "The plant-specific kinase CDKF;1 is involved in activating phosphorylation
RT   of cyclin-dependent kinase-activating kinases in Arabidopsis.";
RL   Plant Cell 16:2954-2966(2004).
RN   [7]
RP   REVIEW.
RX   PubMed=17094738; DOI=10.1146/annurev.genet.40.110405.090431;
RA   Inze D., de Veylder L.;
RT   "Cell cycle regulation in plant development.";
RL   Annu. Rev. Genet. 40:77-105(2006).
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15486101}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in suspension cell culture,
CC       but not in plant organs. {ECO:0000269|PubMed:12527363}.
CC   -!- PTM: Autophosphorylated.
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; AB047275; BAB62844.1; -; mRNA.
DR   EMBL; AC012679; AAG52081.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35498.1; -; Genomic_DNA.
DR   EMBL; AY063843; AAL36199.1; -; mRNA.
DR   EMBL; AY091227; AAM14166.1; -; mRNA.
DR   PIR; A96764; A96764.
DR   RefSeq; NP_177510.1; NM_106028.4.
DR   AlphaFoldDB; Q9C9U2; -.
DR   SMR; Q9C9U2; -.
DR   BioGRID; 28923; 19.
DR   IntAct; Q9C9U2; 2.
DR   STRING; 3702.Q9C9U2; -.
DR   PaxDb; 3702-AT1G73690-1; -.
DR   ProteomicsDB; 222811; -.
DR   EnsemblPlants; AT1G73690.1; AT1G73690.1; AT1G73690.
DR   GeneID; 843704; -.
DR   Gramene; AT1G73690.1; AT1G73690.1; AT1G73690.
DR   KEGG; ath:AT1G73690; -.
DR   Araport; AT1G73690; -.
DR   TAIR; AT1G73690; CDKD1.
DR   eggNOG; KOG0659; Eukaryota.
DR   HOGENOM; CLU_000288_181_0_1; -.
DR   InParanoid; Q9C9U2; -.
DR   OMA; CLESEYF; -.
DR   OrthoDB; 244018at2759; -.
DR   PhylomeDB; Q9C9U2; -.
DR   PRO; PR:Q9C9U2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C9U2; baseline and differential.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0070985; C:transcription factor TFIIK complex; IEA:InterPro.
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:0030154; P:cell differentiation; TAS:TAIR.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051726; P:regulation of cell cycle; TAS:TAIR.
DR   CDD; cd07841; STKc_CDK7; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR037770; CDK7.
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:SF0; CYCLIN-DEPENDENT KINASE 7; 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.
DR   Genevisible; Q9C9U2; AT.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..398
FT                   /note="Cyclin-dependent kinase D-1"
FT                   /id="PRO_0000293119"
FT   DOMAIN          11..291
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          296..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        133
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         17..25
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         22
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P24100"
FT   MOD_RES         160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C9M7"
FT   MOD_RES         166
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C9M7"
FT   MUTAGEN         40
FT                   /note="K->R: Prevents autophosphorylation."
FT                   /evidence="ECO:0000269|PubMed:15486101"
SQ   SEQUENCE   398 AA;  45138 MW;  32BA95E61E6D2C45 CRC64;
     MEQPKKVADR YLKREVLGQG TYGVVFKATD TKNGETVAIK KIRLGKEKEG VNVTALREIK
     LLKELKHPHI IELIDAFPHK ENLHIVFEFM ETDLEAVIRD RNLYLSPGDV KSYLQMILKG
     LEYCHGKWVL HRDMKPNNLL IGPNGQLKLA DFGLARIFGS PGRKFTHQVF ARWYRAPELL
     FGAKQYDGAV DVWAAGCIFA ELLLRRPFLQ GNSDIDQLSK IFAAFGTPKA DQWPDMICLP
     DYVEYQFVPA PSLRSLLPTV SEDALDLLSK MFTYDPKSRI SIQQALKHRY FTSAPSPTDP
     LKLPRPVSKQ DAKSSDSKLE AIKVLSPAHK FRRVMPDRGK SGNGFKDQSV DVMRQASHDG
     QAPMSLDFTI LAERPPNRPT ITSADRSHLK RKLDLEFL
//