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Protein

Cell division control protein 2 homolog

Gene

CRK2

Organism
Plasmodium vivax
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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

Enzyme regulationi

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-158 activates it.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei32 – 321ATPPROSITE-ProRule annotation
Active sitei125 – 1251Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 189ATPPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 2 homolog (EC:2.7.11.22, EC:2.7.11.23)
Alternative name(s):
Pvcrk2
Gene namesi
Name:CRK2
OrganismiPlasmodium vivax
Taxonomic identifieri5855 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Plasmodium)

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 288288Cell division control protein 2 homologPRO_0000232671Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphothreonineBy similarity
Modified residuei15 – 151PhosphotyrosineBy similarity
Modified residuei158 – 1581Phosphothreonine; by CAKBy similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin.By similarity

Protein-protein interaction databases

STRINGi5855.PVX_114825.

Structurei

3D structure databases

ProteinModelPortaliQ9XZD6.
SMRiQ9XZD6. Positions 1-286.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 284281Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9XZD6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKYHGLEKI GEGTYGVVYK AQNNYGETFA LKKIRLEKED EGIPSTAIRE
60 70 80 90 100
ISILKELKHS NIVKLYDVIH TKKRLILVFE HLDQDLKKLL DVCDGGLESV
110 120 130 140 150
TAKSFLLQLL SGIAYCHEHR VLHRDLKPQN LLINREGELK IADFGLARAF
160 170 180 190 200
GIPVRKYTHE VVTLWYRAPD ILMGSKKYST PIDMWSVGCI FAEMVNGRPL
210 220 230 240 250
FPGVSETDQL MRIFRILGTP NSENWPNVTE LPKYDPDFMV YEPLPWETFL
260 270 280
KGLDDTGIDL LSKMLRLDPN QRITAKQALE HAYFKESN
Length:288
Mass (Da):33,094
Last modified:November 1, 1999 - v1
Checksum:i16A484C4B6CD313C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136377 Genomic DNA. Translation: AAD29423.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136377 Genomic DNA. Translation: AAD29423.1.

3D structure databases

ProteinModelPortaliQ9XZD6.
SMRiQ9XZD6. Positions 1-286.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5855.PVX_114825.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0515.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure of the Plasmodium vivax crk2 gene and interference of the yeast cell cycle upon its conditional expression."
    Speranca M.A., Vinkenoog R., Ocampos M., Fischer K., Janse C.J., Waters A.P., del Portillo H.A.
    Exp. Parasitol. 97:119-128(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiCDC2H_PLAVI
AccessioniPrimary (citable) accession number: Q9XZD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.