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Q29561

- KCY_PIG

UniProt

Q29561 - KCY_PIG

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Protein

UMP-CMP kinase

Gene

CMPK1

Organism
Sus scrofa (Pig)
Status
Reviewed - 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. Also displays broad nucleoside diphosphate kinase activity.

Catalytic activityi

ATP + (d)CMP = ADP + (d)CDP.UniRule annotation
ATP + UMP = ADP + UDP.UniRule annotation
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.UniRule annotation

Cofactori

Binds 1 magnesium ion per monomer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391NMPUniRule annotation
Binding sitei100 – 1001CMPUniRule annotation
Binding sitei134 – 1341ATPUniRule annotation
Binding sitei140 – 1401NMPUniRule annotation
Binding sitei151 – 1511NMPUniRule annotation
Binding sitei179 – 1791ATP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 186ATPUniRule annotation
Nucleotide bindingi61 – 633NMPUniRule annotation
Nucleotide bindingi93 – 964NMPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cytidylate kinase activity Source: UniProtKB-HAMAP
  3. nucleoside diphosphate kinase activity Source: UniProtKB
  4. uridylate kinase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. nucleoside diphosphate phosphorylation Source: UniProtKB
  2. nucleoside triphosphate biosynthetic process Source: UniProtKB
  3. pyrimidine nucleotide biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
UMP-CMP kinaseUniRule annotation (EC:2.7.4.14UniRule annotation)
Alternative name(s):
Deoxycytidylate kinaseUniRule annotation
Short name:
CKUniRule annotation
Short name:
dCMP kinaseUniRule annotation
Nucleoside-diphosphate kinaseUniRule annotation (EC:2.7.4.6UniRule annotation)
Uridine monophosphate/cytidine monophosphate kinaseUniRule annotation
Short name:
UMP/CMP kinaseUniRule annotation
Short name:
UMP/CMPKUniRule annotation
Gene namesi
Name:CMPK1UniRule annotation
Synonyms:CMPKUniRule annotation, UCK
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Chromosome 6

Subcellular locationi

Nucleus UniRule annotation. Cytoplasm UniRule annotation
Note: Predominantly nuclear.UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
  2. nucleus Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196UMP-CMP kinasePRO_0000158951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-acetyllysineBy similarity
Modified residuei55 – 551N6-acetyllysineBy similarity
Modified residuei106 – 1061N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ29561.
PRIDEiQ29561.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ29561.
SMRiQ29561. Positions 3-196.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 6331NMPbindUniRule annotationAdd
BLAST
Regioni133 – 14311LIDUniRule annotationAdd
BLAST

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 dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.UniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0563.
GeneTreeiENSGT00390000016215.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiQ29561.
OMAiKRPGSQY.
OrthoDBiEOG7X0VJ0.
TreeFamiTF354283.

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.

Q29561-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRPKVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG
60 70 80 90 100
ELIEKYIKDG KIVPVEITIS LLRREMDQTM AANAQKNKFL IDGFPRNQDN
110 120 130 140 150
LQGWNKTMDG KADVSFVLFF DCNNEICIER CLERGKSSGR SDDNRESLEK
160 170 180 190
RIQTYLQSTK PIIDLYEEMG KVKKIDASKS VDEVFDEVVK IFDKEG
Length:196
Mass (Da):22,279
Last modified:November 1, 1996 - v1
Checksum:i3780384E43900797
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D29655 Genomic DNA. Translation: BAA06130.1.
PIRiJC4181.

Genome annotation databases

EnsembliENSSSCT00000004297; ENSSSCP00000004197; ENSSSCG00000003885.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D29655 Genomic DNA. Translation: BAA06130.1 .
PIRi JC4181.

3D structure databases

ProteinModelPortali Q29561.
SMRi Q29561. Positions 3-196.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q29561.
PRIDEi Q29561.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000004297 ; ENSSSCP00000004197 ; ENSSSCG00000003885 .

Phylogenomic databases

eggNOGi COG0563.
GeneTreei ENSGT00390000016215.
HOGENOMi HOG000238771.
HOVERGENi HBG108060.
InParanoidi Q29561.
OMAi KRPGSQY.
OrthoDBi EOG7X0VJ0.
TreeFami TF354283.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00235. Adenylate_kinase_Adk.
MF_03172. Adenylate_kinase_UMP_CMP_kin.
InterProi IPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
IPR006266. UMP_CMP_kinase.
[Graphical view ]
PANTHERi PTHR23359. PTHR23359. 1 hit.
PRINTSi PR00094. ADENYLTKNASE.
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiKCY_PIG
AccessioniPrimary (citable) accession number: Q29561
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3