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Reviewed, UniProtKB/Swiss-Prot Q9LFT8 (CDKC1_ARATH)

Last modified November 3, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cyclin-dependent kinase C-1
      Short name=CDKC;1
    EC=2.7.11.22
    EC=2.7.11.23
Gene names
Name: CDKC-1
Ordered Locus Names: At5g10270
ORF Names: F18D22.40
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Subunit structure

Interacts with CYCT1-3. Ref.4

Tissue specificity

Highly expressed in flowers. Expressed in seedlings, roots, rosettes and stems. Ref.4

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

At3g15000Q9LKA51EBI-2025736,EBI-2025869
CYCT1-3Q8LBC03EBI-2025736,EBI-2025764

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 505505Cyclin-dependent kinase C-1
PRO_0000293117

Regions

Domain26 – 325300Protein kinase
Nucleotide binding32 – 409ATP By similarity
Compositional bias417 – 49377Gly-rich

Sites

Active site1641Proton acceptor By similarity
Binding site551ATP By similarity

Amino acid modifications

Modified residue361Phosphothreonine By similarity
Modified residue371Phosphotyrosine By similarity
Modified residue1981Phosphothreonine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9LFT8-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 9159218AEB976361

FASTA50556,729
        10         20         30         40         50         60 
MAMASFGQLN LEEPPPIWGS RSVDCFEKLE QIGEGTYGQV YMAKEIKTGE IVALKKIRMD 

        70         80         90        100        110        120 
NEREGFPITA IREIKILKKL HHENVIQLKE IVTSPGRDRD DQGKPDNNKY KGGIYMVFEY 

       130        140        150        160        170        180 
MDHDLTGLAD RPGLRFTVPQ IKCYMKQLLT GLHYCHVNQV LHRDIKGSNL LIDNEGNLKL 

       190        200        210        220        230        240 
ADFGLARSYS HDHTGNLTNR VITLWYRPPE LLLGATKYGP AIDMWSVGCI FAELLHAKPI 

       250        260        270        280        290        300 
LPGKNEQEQL NKIFELCGSP DEKLWPGVSK MPWFNNFKPA RPLKRRVREF FRHFDRHALE 

       310        320        330        340        350        360 
LLEKMLVLDP AQRISAKDAL DAEYFWTDPL PCDPKSLPTY ESSHEFQTKK KRQQQRQNEE 

       370        380        390        400        410        420 
AAKRQKLQHP PLQHSRLPPL QHGGQSHAAP HWPAGPNHPT NNAPPQVPAG PSHNFYGKPR 

       430        440        450        460        470        480 
GPPGPNRYPP SGNQSGGYNQ SRGGYSSGSY PPQGRGAPYV AGPRGPSGGP YGVGPPNYTQ 

       490        500 
GGQYGGSGSS GRGQNQRNQQ YGWQQ

« Hide

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References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed: 11130714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"Genome-wide analysis of core cell cycle genes in Arabidopsis."
Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.
Plant Cell 14:903-916(2002) [PubMed: 11971144] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[4]"Novel complexes of cyclin-dependent kinases and a cyclin-like protein from Arabidopsis thaliana with a function unrelated to cell division."
Barroco R.M., de Veylder L., Magyar Z., Engler G., Inze D., Mironov V.
Cell. Mol. Life Sci. 60:401-412(2003) [PubMed: 12678503] [Abstract]
Cited for: TISSUE SPECIFICITY, INTERACTION WITH CYCT1-3.
[5]"Cell cycle regulation in plant development."
Inze D., de Veylder L.
Annu. Rev. Genet. 40:77-105(2006) [PubMed: 17094738] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AL360334 Genomic DNA. Translation: CAB96683.1.
AF375437 mRNA. Translation: AAK53021.1.
AY120690 mRNA. Translation: AAM52233.1.
IPIIPI00547326.
PIRT50815.
RefSeqNP_196589.1.
UniGeneAt.19998

3D structure databases

HSSPHSSP built from PDB template 1H00 based on UniProtKB P24941.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9LFT8. 5 interactions.
STRINGQ9LFT8.

Genome annotation databases

GeneID830891.
GenomeReviewsGene locus AT5G10270 in contig BA000015_GR.
KEGGath:AT5G10270.
NMPDRfig|3702.1.peg.23156.

Organism-specific databases

GeneFarm3283. 108.
TAIRAt5g10270.

Phylogenomic databases

OMAVYMAKET.

Enzyme and pathway databases

BRENDA2.7.11.22. 302.
2.7.11.23. 302.

Gene expression databases

GenevestigatorQ9LFT8.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCDKC1_ARATH
AccessionPrimary (citable) accession number: Q9LFT8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: October 1, 2000
Last modified: November 3, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents