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Q5ZKE7 (KCY_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UMP-CMP kinase

EC=2.7.4.14
Alternative name(s):
Deoxycytidylate kinase
Short name=CK
Short name=dCMP kinase
Nucleoside-diphosphate kinase
EC=2.7.4.6
Uridine monophosphate/cytidine monophosphate kinase
Short name=UMP/CMP kinase
Short name=UMP/CMPK
Gene names
Name:CMPK
Synonyms:CMPK1
ORF Names:RCJMB04_11f2
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity By similarity. HAMAP-Rule MF_03172

Catalytic activity

ATP + (d)CMP = ADP + (d)CDP. HAMAP-Rule MF_03172

ATP + UMP = ADP + UDP. HAMAP-Rule MF_03172

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. HAMAP-Rule MF_03172

Cofactor

Binds 1 magnesium ion per monomer By similarity. HAMAP-Rule MF_03172

Subunit structure

Monomer By similarity. HAMAP-Rule MF_03172

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Note: Predominantly nuclear By similarity. HAMAP-Rule MF_03172

Domain

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis By similarity. HAMAP-Rule MF_03172

Sequence similarities

Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196UMP-CMP kinase HAMAP-Rule MF_03172
PRO_0000292024

Regions

Nucleotide binding13 – 186ATP By similarity
Nucleotide binding61 – 633NMP By similarity
Nucleotide binding93 – 964NMP By similarity
Region33 – 6331NMPbind By similarity
Region133 – 14311LID By similarity

Sites

Binding site391NMP By similarity
Binding site1001CMP By similarity
Binding site1341ATP By similarity
Binding site1401NMP By similarity
Binding site1511NMP By similarity
Binding site1791ATP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5ZKE7 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: AF93779E27A247FA

FASTA19622,172
        10         20         30         40         50         60 
MKPVVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGDLLRD ERKRPGSQYG ELIENYIKEG 

        70         80         90        100        110        120 
EIVPVEITIS LLKRAMDQTM AANSQKNKFL IDGFPRNEDN LQGWNKTMDG KADVSFVLFF 

       130        140        150        160        170        180 
DCDNEICIGR CLERGKSSGR SDDNRESLEK RIHTYLQSTR PIIDLYERMG KVRRVDASKS 

       190 
VDEVFEKVVQ IFDKEG 

« Hide

References

[1]"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis."
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.
Genome Biol. 6:R6.1-R6.9(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: CB.
Tissue: Bursa of Fabricius.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ720137 mRNA. Translation: CAG31796.1.
RefSeqNP_001026735.1. NM_001031564.1.
UniGeneGga.19231.

3D structure databases

ProteinModelPortalQ5ZKE7.
SMRQ5ZKE7. Positions 3-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000017049.

Proteomic databases

PaxDbQ5ZKE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000017068; ENSGALP00000017049; ENSGALG00000010481.
GeneID429100.
KEGGgga:429100.

Organism-specific databases

CTD51727.

Phylogenomic databases

eggNOGCOG0563.
GeneTreeENSGT00390000016215.
HOGENOMHOG000238771.
HOVERGENHBG108060.
InParanoidQ5ZKE7.
KOK13800.
OMAKRPGSQY.
OrthoDBEOG7X0VJ0.
PhylomeDBQ5ZKE7.
TreeFamTF354283.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00235. Adenylate_kinase_Adk.
MF_03172. Adenylate_kinase_UMP_CMP_kin.
InterProIPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
IPR006266. UMP_CMP_kinase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PRINTSPR00094. ADENYLTKNASE.
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20829926.
PROQ5ZKE7.

Entry information

Entry nameKCY_CHICK
AccessionPrimary (citable) accession number: Q5ZKE7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: November 23, 2004
Last modified: April 16, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families