ID   CDKC1_ARATH             Reviewed;         505 AA.
AC   Q9LFT8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Cyclin-dependent kinase C-1;
DE            Short=CDKC;1;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
GN   Name=CDKC-1; OrderedLocusNames=At5g10270; ORFNames=F18D22.40;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH CYCT1-3.
RX   PubMed=12678503; DOI=10.1007/s000180300033;
RA   Barroco R.M., de Veylder L., Magyar Z., Engler G., Inze D., Mironov V.;
RT   "Novel complexes of cyclin-dependent kinases and a cyclin-like protein from
RT   Arabidopsis thaliana with a function unrelated to cell division.";
RL   Cell. Mol. Life Sci. 60:401-412(2003).
RN   [6]
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   -!- SUBUNIT: Interacts with CYCT1-3. {ECO:0000269|PubMed:12678503}.
CC   -!- INTERACTION:
CC       Q9LFT8; Q8LBC0: CYCT1-3; NbExp=4; IntAct=EBI-2025736, EBI-2025764;
CC       Q9LFT8; Q9LKA5: MORF8; NbExp=2; IntAct=EBI-2025736, EBI-2025869;
CC   -!- TISSUE SPECIFICITY: Highly expressed in flowers. Expressed in
CC       seedlings, roots, rosettes and stems. {ECO:0000269|PubMed:12678503}.
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; AL360334; CAB96683.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91515.1; -; Genomic_DNA.
DR   EMBL; AF375437; AAK53021.1; -; mRNA.
DR   EMBL; AY120690; AAM52233.1; -; mRNA.
DR   PIR; T50815; T50815.
DR   RefSeq; NP_196589.1; NM_121065.3.
DR   AlphaFoldDB; Q9LFT8; -.
DR   SMR; Q9LFT8; -.
DR   BioGRID; 16169; 16.
DR   IntAct; Q9LFT8; 12.
DR   STRING; 3702.Q9LFT8; -.
DR   iPTMnet; Q9LFT8; -.
DR   PaxDb; 3702-AT5G10270-1; -.
DR   ProteomicsDB; 224391; -.
DR   EnsemblPlants; AT5G10270.1; AT5G10270.1; AT5G10270.
DR   GeneID; 830891; -.
DR   Gramene; AT5G10270.1; AT5G10270.1; AT5G10270.
DR   KEGG; ath:AT5G10270; -.
DR   Araport; AT5G10270; -.
DR   TAIR; AT5G10270; CDKC.
DR   eggNOG; KOG0600; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; Q9LFT8; -.
DR   OMA; YTQGGQY; -.
DR   OrthoDB; 10753at2759; -.
DR   PhylomeDB; Q9LFT8; -.
DR   PRO; PR:Q9LFT8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LFT8; baseline and differential.
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:0016301; F:kinase activity; IDA:TAIR.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009615; P:response to virus; IEP:TAIR.
DR   CDD; cd07840; STKc_CDK9_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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:SF560; CYCLIN-DEPENDENT KINASE C-1; 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; Q9LFT8; AT.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..505
FT                   /note="Cyclin-dependent kinase C-1"
FT                   /id="PRO_0000293117"
FT   DOMAIN          26..325
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          336..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         32..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         37
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P24100"
FT   MOD_RES         198
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C9M7"
SQ   SEQUENCE   505 AA;  56729 MW;  9159218AEB976361 CRC64;
     MAMASFGQLN LEEPPPIWGS RSVDCFEKLE QIGEGTYGQV YMAKEIKTGE IVALKKIRMD
     NEREGFPITA IREIKILKKL HHENVIQLKE IVTSPGRDRD DQGKPDNNKY KGGIYMVFEY
     MDHDLTGLAD RPGLRFTVPQ IKCYMKQLLT GLHYCHVNQV LHRDIKGSNL LIDNEGNLKL
     ADFGLARSYS HDHTGNLTNR VITLWYRPPE LLLGATKYGP AIDMWSVGCI FAELLHAKPI
     LPGKNEQEQL NKIFELCGSP DEKLWPGVSK MPWFNNFKPA RPLKRRVREF FRHFDRHALE
     LLEKMLVLDP AQRISAKDAL DAEYFWTDPL PCDPKSLPTY ESSHEFQTKK KRQQQRQNEE
     AAKRQKLQHP PLQHSRLPPL QHGGQSHAAP HWPAGPNHPT NNAPPQVPAG PSHNFYGKPR
     GPPGPNRYPP SGNQSGGYNQ SRGGYSSGSY PPQGRGAPYV AGPRGPSGGP YGVGPPNYTQ
     GGQYGGSGSS GRGQNQRNQQ YGWQQ
//