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Q29561 (KCY_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. 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:CMPK1
Synonyms:CMPK, UCK
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. 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_0000158951

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

Amino acid modifications

Modified residue431N6-acetyllysine By similarity
Modified residue551N6-acetyllysine By similarity
Modified residue1061N6-succinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q29561 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3780384E43900797

FASTA19622,279
        10         20         30         40         50         60 
MRPKVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG ELIEKYIKDG 

        70         80         90        100        110        120 
KIVPVEITIS LLRREMDQTM AANAQKNKFL IDGFPRNQDN LQGWNKTMDG KADVSFVLFF 

       130        140        150        160        170        180 
DCNNEICIER CLERGKSSGR SDDNRESLEK RIQTYLQSTK PIIDLYEEMG KVKKIDASKS 

       190 
VDEVFDEVVK IFDKEG 

« Hide

References

[1]"Cloning, sequencing, and expression in Escherichia coli of cDNA encoding porcine brain UMP-CMP kinase."
Okajima T., Goto S., Tanizawa K., Tagaya M., Shimofuruya H., Suzuki J., Fukui T.
J. Biochem. 117:980-986(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D29655 Genomic DNA. Translation: BAA06130.1.
PIRJC4181.

3D structure databases

ProteinModelPortalQ29561.
SMRQ29561. Positions 3-196.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ29561.
PRIDEQ29561.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000004297; ENSSSCP00000004197; ENSSSCG00000003885.

Phylogenomic databases

eggNOGCOG0563.
GeneTreeENSGT00390000016215.
HOGENOMHOG000238771.
HOVERGENHBG108060.
OMAKRPGSQY.
OrthoDBEOG7X0VJ0.
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...

Entry information

Entry nameKCY_PIG
AccessionPrimary (citable) accession number: Q29561
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 83 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