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Q7ZWE9 (KCY_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. 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
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

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 caution

The sequence AAH49446.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196UMP-CMP kinase HAMAP-Rule MF_03172
PRO_0000292025

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
Q7ZWE9 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: C86279CB8E589811

FASTA19622,423
        10         20         30         40         50         60 
MKPQVVFVLG GPGAGKGTQC ARIVENYSYT HLSAGDLLRE ERSRTDSEFG QLIDSYIKEG 

        70         80         90        100        110        120 
KIVPVQITIN LLRKAMEETM KADEKKFRFL IDGFPRNQDN LQGWNTEMDG KADVKFVLFF 

       130        140        150        160        170        180 
DCSNEVCIDR CLERGKSSGR TDDNRESLEK RIQTYLQSTR PIIELYEKQG KVQRIDASRS 

       190 
VDEVFADVKN ILEKDD 

« Hide

References

[1]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC049446 mRNA. Translation: AAH49446.1. Different initiation.
UniGeneDr.24327.

3D structure databases

ProteinModelPortalQ7ZWE9.
SMRQ7ZWE9. Positions 3-195.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

ZFINZDB-GENE-040426-2113. cmpk.

Phylogenomic databases

eggNOGCOG0563.
HOVERGENHBG108060.
InParanoidQ7ZWE9.

Gene expression databases

BgeeQ7ZWE9.

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

NextBio20817993.
PROQ7ZWE9.

Entry information

Entry nameKCY_DANRE
AccessionPrimary (citable) accession number: Q7ZWE9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 74 of the entry and version 2 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