Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q29561

- KCY_PIG

UniProt

Q29561 - KCY_PIG

Protein

UMP-CMP kinase

Gene

CMPK1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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-SubCell
    2. nucleus Source: UniProtKB-SubCell

    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.
    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

    MRPKVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG    50
    ELIEKYIKDG KIVPVEITIS LLRREMDQTM AANAQKNKFL IDGFPRNQDN 100
    LQGWNKTMDG KADVSFVLFF DCNNEICIER CLERGKSSGR SDDNRESLEK 150
    RIQTYLQSTK PIIDLYEEMG KVKKIDASKS VDEVFDEVVK IFDKEG 196
    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.
    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 1, 2014
    This is version 84 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