NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Flower;
DOI=10.1105/tpc.8.9.1465; PubMed=8837502 [NCBI, ExPASy, EBI, Israel, Japan]
Fobert P.R., Gaudin V., Lunness P., Coen E.S., Doonan J.H.;
"Distinct classes of cdc2-related genes are differentially expressed during the cell division cycle in plants.";
Plant Cell 8:1465-1476(1996).

Comments

FUNCTION: Plays a key role in the control of the eukaryotic cell cycle.
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
DEVELOPMENTAL STAGE: Expression specific to the G2 and M phases.
SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X97640; CAA66236.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T17118; T17118.

3D structure databases

HSSP

P24941; 1H06. [HSSP ENTRY / PDB]

ModBase

Q38775.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004693;	Molecular function: cyclin-dependent protein kinase activity (inferred from electronic annotation from EC).
GO:0008353;	Molecular function: RNA polymerase subunit kinase activity (inferred from electronic annotation from EC).
GO:0051301;	Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0007067;	Biological process: mitosis (inferred from electronic annotation from UniProtKB-KW).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.

Pfam

PF00069; Pkinase; 1.
Pfam graphical view of domain structure.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q38775.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cell cycle; Cell division; Kinase; Mitosis; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 312`	`312`	`Cell division control protein 2 homolog D.`	`PRO_0000085748`
`DOMAIN`	`14 304`	`291`	`Protein kinase.`
`NP_BIND`	`20 28`	`9`	`ATP (By similarity).`
`ACT_SITE`	`145 145`		`Proton acceptor (By similarity).`
`BINDING`	`43 43`		`ATP (By similarity).`
`MOD_RES`	`24 24`		`Phosphothreonine (By similarity).`
`MOD_RES`	`25 25`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`179 179`		`Phosphothreonine; by CAK (By similarity).`

Sequence information

Length: 312 AA [This is the length of the unprocessed precursor]

Molecular weight: 35503 Da [This is the MW of the unprocessed precursor]

CRC64: A38D2177EBF70210 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAEEKSKSSA MDAFVKLEKV GEGTYGKVYR AMEKSTGKIV ALKKTRLHED EEGVPPTTLR 

        70         80         90        100        110        120 
EVSLLRMLSR DPHVVRLLDV KQGQNKEGKT VLYLVFEYMD TDLKKYIRSF KQTGESIAPM 

       130        140        150        160        170        180 
NVKSLMYQLC KGVAFCHGHG VLHRDLKPHN LLMDRKTMML KIADLGLARA YTLPIKKYTH 

       190        200        210        220        230        240 
EILTLWYRAP EVLLGATHYS PAVDMWSVAC IFAELVTQKA LFPGDSELQQ LLHIFRLLGT 

       250        260        270        280        290        300 
PNEEIWPGVS TLVDWHEYPQ WTAQPISSAV PGLDEKGLNL LSEMLHYEPS RRISAKKAME 

       310 
HPYFDELDKS GL

Q38775 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools