Reviewed, UniProtKB/Swiss-Prot Q7RM49 (CDC2H_PLAYO)

Names and origin

Protein names

Recommended name:
    Cell division control protein 2 homolog
    EC=2.7.11.22
    EC=2.7.11.23

Gene names

Name:	CRK2
ORF Names:	PY02339

Organism

Plasmodium yoelii yoelii [Complete proteome]

Taxonomic identifier

73239 [NCBI]

Taxonomic lineage

Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Vinckeia)

Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Plays a key role in the control of the eukaryotic cell cycle. It is required in higher cells for entry into S-phase and mitosis. Component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
Enzyme regulation	Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-159 activates it By similarity.
Subunit structure	Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase subunit kinase activity Inferred from electronic annotation. Source: EC cyclin-dependent protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 289	289	Cell division control protein 2 homolog		PRO_0000232672
Regions
	Domain	4 – 285	282	Protein kinase
	Nucleotide binding	10 – 18	9	ATP By similarity
Sites
	Active site	126	1	Proton acceptor By similarity
	Binding site	32	1	ATP By similarity
Amino acid modifications
	Modified residue	14	1	Phosphothreonine By similarity
	Modified residue	15	1	Phosphotyrosine By similarity
	Modified residue	159	1	Phosphothreonine; by CAK By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7RM49-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 701FCFCEEA4F5CA3	FASTA	289	33,121
	10 20 30 40 50 60 MEKYHGLEKI GEGTYGVVYK AQNSDGESFA LKKIRLEKED EGIPSTVSIR EISILKELRH 70 80 90 100 110 120 SNIVKLYDVI HAKKRLILVF EHLDQDLKKL IDVCDGGLES VTAKSFLLQL LNGIAYCHEH 130 140 150 160 170 180 RVLHRDLKPQ NLLINREGEL KIADFGLARA FGIPARRYTH EVVTLWYRAP DILMGSKKYS 190 200 210 220 230 240 TPIDIWSVGC IFAEMVNGRP LFPGVSETDQ LMRIFKILGT PNSQNWPDVF KLPKYDPNFP 250 260 270 280 VYEPLPWETF IKGLDDTGID LLSKMLKLDP NQRITAKQAI EHPYFKETN

References

[1]

"Genome sequence and comparative analysis of the model rodent malaria parasite Plasmodium yoelii yoelii." Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C., Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M., Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E., Riedmuller S.B. , Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M., Shoaibi A., Cummings L.M., Florens L., Yates J.R. III, Raine J.D., Sinden R.E., Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B., van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R., Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J., Carucci D.J. Nature 419:512-519(2002) [PubMed: 12368865] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 17XNL.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AABL01000639 Genomic DNA. Translation: EAA21777.1.
RefSeq	XP_730212.1.
3D structure databases
HSSP	HSSP built from PDB template 1OB3 based on UniProtKB Q07785.
SMR	Q7RM49. Positions 1-287.
ModBase	Search...
Genome annotation databases
GeneID	3807518.
KEGG	pyo:PY02339.
Enzyme and pathway databases
BRENDA	2.7.11.22. 288785. 2.7.11.23. 288785.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CDC2H_PLAYO

Accession

Primary (citable) accession number: Q7RM49

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	December 15, 2003
Last modified:	June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)