Q2KIW9 (KCY_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UMP-CMP kinase
EC=2.7.4.14

Alternative name(s):
Deoxycytidylate kinase
Short name=CK
Short name=dCMP kinase
Uridine monophosphate/cytidine monophosphate kinase
Short name=UMP/CMP kinase
Short name=UMP/CMPK

Gene names

Name:	CMPK1
Synonyms:	CMPK

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	196 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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
Cofactor	Binds 1 magnesium ion per monomer By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Note: Predominantly nuclear By similarity.
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 AAI12479.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cytidylate kinase activity Inferred from electronic annotation. Source: EC phosphotransferase activity, phosphate group as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 196	196	UMP-CMP kinase HAMAP-Rule MF_03172		PRO_0000292023
Regions
	Nucleotide binding	13 – 18	6	ATP By similarity
	Nucleotide binding	61 – 63	3	NMP By similarity
	Nucleotide binding	93 – 96	4	NMP By similarity
	Region	33 – 63	31	NMPbind By similarity
	Region	133 – 143	11	LID By similarity
Sites
	Binding site	39	1	NMP By similarity
	Binding site	100	1	CMP By similarity
	Binding site	134	1	ATP By similarity
	Binding site	140	1	NMP By similarity
	Binding site	151	1	NMP By similarity
	Binding site	179	1	ATP; via carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	55	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2KIW9 [UniParc]. Last modified June 26, 2007. Version 2. Checksum: 6011E45A8085D28A	FASTA	196	22,279
	10 20 30 40 50 60 MKPQVVFVLG 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 KVRKIDASKS 190 VDEVFDEVVK IFDKEG

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Testis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC112478 mRNA. Translation: AAI12479.1. Different initiation.
IPI	IPI00717207.
RefSeq	NP_001039509.1. NM_001046044.1.
UniGene	Bt.28263.
3D structure databases
HSSP	HSSP built from PDB template 2CDN based on UniProtKB P69440.
ProteinModelPortal	Q2KIW9.
SMR	Q2KIW9. Positions 3-196.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000026582.
Proteomic databases
PaxDb	Q2KIW9.
PRIDE	Q2KIW9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000026582; ENSBTAP00000026582; ENSBTAG00000019956.
GeneID	509965.
KEGG	bta:509965.
Organism-specific databases
CTD	51727.
Phylogenomic databases
eggNOG	COG0563.
GeneTree	ENSGT00390000016215.
HOGENOM	HOG000238771.
HOVERGEN	HBG108060.
InParanoid	Q2KIW9.
KO	K13800.
OMA	FFDCDNE.
OrthoDB	EOG4F1X45.
Family and domain databases
HAMAP	MF_00235. Adenylate_kinase_Adk. MF_03172. Adenylate_kinase_UMP_CMP_kin.
InterPro	IPR000850. Adenylate_kin. IPR006266. UMP_CMP_kinase. [Graphical view]
PANTHER	PTHR23359. PTHR23359. 1 hit.
Pfam	PF00406. ADK. 1 hit. [Graphical view]
PRINTS	PR00094. ADENYLTKNASE.
TIGRFAMs	TIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITE	PS00113. ADENYLATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20869218.

Entry information

Entry name

KCY_BOVIN

Accession

Primary (citable) accession number: Q2KIW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	June 26, 2007
Last modified:	May 1, 2013
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program