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Protein

UMP-CMP kinase 1

Gene

C29F7.3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication

Catalytic activityi

ATP + (d)CMP = ADP + (d)CDP.UniRule annotation1 Publication
ATP + UMP = ADP + UDP.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per monomer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381NMPUniRule annotation
Binding sitei95 – 951CMPUniRule annotation
Binding sitei129 – 1291ATPUniRule annotation
Binding sitei133 – 1331NMPUniRule annotation
Binding sitei144 – 1441NMPUniRule annotation
Binding sitei172 – 1721ATP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 176ATPUniRule annotation
Nucleotide bindingi60 – 623NMPUniRule annotation
Nucleotide bindingi88 – 914NMPUniRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cytidylate kinase activity Source: UniProtKB-HAMAP
  • UMP kinase activity Source: WormBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-CEL-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Names & Taxonomyi

Protein namesi
Recommended name:
UMP-CMP kinase 1UniRule annotation (EC:2.7.4.14UniRule annotation)
Alternative name(s):
Deoxycytidylate kinase 1UniRule annotation
Short name:
CK 1UniRule annotation
Short name:
dCMP kinase 1UniRule annotation
Uridine monophosphate/cytidine monophosphate kinase 1UniRule annotation
Short name:
UMP/CMP kinase 1UniRule annotation
Short name:
UMP/CMPK 1UniRule annotation
Gene namesi
ORF Names:C29F7.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome X

Organism-specific databases

WormBaseiC29F7.3; CE08444; WBGene00007812.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Confers resistance to 5-fluorouracil.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191UMP-CMP kinase 1PRO_0000422252Add
BLAST

Proteomic databases

EPDiO17622.
PaxDbiO17622.
PRIDEiO17622.

Expressioni

Tissue specificityi

Expressed in the hypodermis, intestine, and pharynx.1 Publication

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi6239.C29F7.3.

Structurei

3D structure databases

ProteinModelPortaliO17622.
SMRiO17622. Positions 4-185.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 6231NMPbindUniRule annotationAdd
BLAST
Regioni128 – 1369LIDUniRule annotation

Domaini

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 disassembling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis (By similarity).By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3079. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00390000016215.
HOGENOMiHOG000238771.
InParanoidiO17622.
KOiK13800.
OMAiIEYYNAK.
OrthoDBiEOG7X0VJ0.
PhylomeDBiO17622.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03172. Adenylate_kinase_UMP_CMP_kin.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
IPR006266. UMP_CMP_kinase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O17622-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYNVVFVLGP PGSGKGTICT QIHENLGYVH LSAGDLLRAE RERAGSEYGA
60 70 80 90 100
LIEGHIKNGS IVPVEITCAL LENAMIASKD ANGFLIDGFP RNEDNWSGWN
110 120 130 140 150
KQMGGKVNEQ FVLFLSCPVD VCIDRCLHRG QGRTDDNVES LKKRVETYNQ
160 170 180 190
STFPIIEHFE KVGMVREVNS ERPVTEVYED VVKVFAAANQ K
Length:191
Mass (Da):21,202
Last modified:January 1, 1998 - v1
Checksum:i8920CE3F444FBC60
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z92827 Genomic DNA. Translation: CAB07328.1.
PIRiT19573.
RefSeqiNP_510236.1. NM_077835.3.
UniGeneiCel.11285.

Genome annotation databases

EnsemblMetazoaiC29F7.3; C29F7.3; WBGene00007812.
GeneIDi181464.
KEGGicel:CELE_C29F7.3.
UCSCiC29F7.3. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z92827 Genomic DNA. Translation: CAB07328.1.
PIRiT19573.
RefSeqiNP_510236.1. NM_077835.3.
UniGeneiCel.11285.

3D structure databases

ProteinModelPortaliO17622.
SMRiO17622. Positions 4-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.C29F7.3.

Proteomic databases

EPDiO17622.
PaxDbiO17622.
PRIDEiO17622.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC29F7.3; C29F7.3; WBGene00007812.
GeneIDi181464.
KEGGicel:CELE_C29F7.3.
UCSCiC29F7.3. c. elegans.

Organism-specific databases

CTDi181464.
WormBaseiC29F7.3; CE08444; WBGene00007812.

Phylogenomic databases

eggNOGiKOG3079. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00390000016215.
HOGENOMiHOG000238771.
InParanoidiO17622.
KOiK13800.
OMAiIEYYNAK.
OrthoDBiEOG7X0VJ0.
PhylomeDBiO17622.

Enzyme and pathway databases

ReactomeiR-CEL-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

PROiO17622.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03172. Adenylate_kinase_UMP_CMP_kin.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
IPR006266. UMP_CMP_kinase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "Functional analysis of pyrimidine biosynthesis enzymes using the anticancer drug 5-fluorouracil in Caenorhabditis elegans."
    Kim S., Park D.H., Kim T.H., Hwang M., Shim J.
    FEBS J. 276:4715-4726(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiKCY1_CAEEL
AccessioniPrimary (citable) accession number: O17622
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2013
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.