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Q9LFT8 (CDKC1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.5

Tissue specificity

Highly expressed in flowers. Expressed in seedlings, roots, rosettes and stems. Ref.5

Sequence similarities

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

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

At3g15000Q9LKA52EBI-2025736,EBI-2025869
CYCT1-3Q8LBC04EBI-2025736,EBI-2025764

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

Sequences

Sequence LengthMass (Da)Tools
Q9LFT8 [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

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"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] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[5]"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] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INTERACTION WITH CYCT1-3.
[6]"Cell cycle regulation in plant development."
Inze D., de Veylder L.
Annu. Rev. Genet. 40:77-105(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL360334 Genomic DNA. Translation: CAB96683.1.
CP002688 Genomic DNA. Translation: AED91515.1.
AF375437 mRNA. Translation: AAK53021.1.
AY120690 mRNA. Translation: AAM52233.1.
IPIIPI00547326.
PIRT50815.
RefSeqNP_196589.1. NM_121065.2.
UniGeneAt.19998.

3D structure databases

ProteinModelPortalQ9LFT8.
SMRQ9LFT8. Positions 23-351.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9LFT8. 12 interactions.
STRING3702.AT5G10270.1-P.

Proteomic databases

PRIDEQ9LFT8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G10270.1; AT5G10270.1; AT5G10270.
GeneID830891.
KEGGath:AT5G10270.

Organism-specific databases

GeneFarm3283. 108.
TAIRAt5g10270.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
InParanoidQ9LFT8.
KOK08819.
OMAYEASHEF.
PhylomeDBQ9LFT8.
ProtClustDBCLSN2692317.

Gene expression databases

GenevestigatorQ9LFT8.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

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: May 29, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

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