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Q28H12

- KCY_XENTR

UniProt

Q28H12 - KCY_XENTR

Protein

UMP-CMP kinase

Gene

cmpk1

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 2 (26 Jun 2007)
      Previous versions | rss
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    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.UniRule annotation

    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:cmpk1
    Synonyms:cmpk
    ORF Names:TEgg001e20.1
    OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
    Taxonomic identifieri8364 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
    ProteomesiUP000008143: Unplaced

    Organism-specific databases

    XenbaseiXB-GENE-980040. cmpk1.

    Subcellular locationi

    Cytoplasm UniRule annotation. Nucleus 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_0000292027Add
    BLAST

    Proteomic databases

    PaxDbiQ28H12.

    Expressioni

    Gene expression databases

    BgeeiQ28H12.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi8364.ENSXETP00000035667.

    Structurei

    3D structure databases

    ProteinModelPortaliQ28H12.
    SMRiQ28H12. 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.
    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.

    Q28H12-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPFVVFVLG GPGAGKGTQC ERIVQKYGYT HLSAGDLLRD ERKKPDSQYG    50
    ELIESYIRDG RIVPVEITIS LLQRAMEQTM ALDGNKHKFL IDGFPRNEDN 100
    LQGWERTMNG KADVSFVLFF DCDNETCIER CLERGKSSGR SDDNRESLEK 150
    RIQTYLQSTR PIIDLYEKTG KVKKVDASKS VDEVFTKVQD IFDREG 196
    Length:196
    Mass (Da):22,352
    Last modified:June 26, 2007 - v2
    Checksum:i1E1B1F9E771F8B7A
    GO

    Sequence cautioni

    The sequence CAJ82118.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR761111 mRNA. Translation: CAJ82118.1. Different initiation.
    UniGeneiStr.22202.

    Genome annotation databases

    EnsembliENSXETT00000035667; ENSXETP00000035667; ENSXETG00000016340.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR761111 mRNA. Translation: CAJ82118.1 . Different initiation.
    UniGenei Str.22202.

    3D structure databases

    ProteinModelPortali Q28H12.
    SMRi Q28H12. Positions 3-196.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 8364.ENSXETP00000035667.

    Proteomic databases

    PaxDbi Q28H12.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSXETT00000035667 ; ENSXETP00000035667 ; ENSXETG00000016340 .

    Organism-specific databases

    Xenbasei XB-GENE-980040. cmpk1.

    Phylogenomic databases

    eggNOGi COG0563.
    GeneTreei ENSGT00390000016215.
    HOGENOMi HOG000238771.
    HOVERGENi HBG108060.
    OrthoDBi EOG7X0VJ0.
    TreeFami TF354283.

    Gene expression databases

    Bgeei Q28H12.

    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. Sanger Xenopus tropicalis EST/cDNA project
      Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Egg.

    Entry informationi

    Entry nameiKCY_XENTR
    AccessioniPrimary (citable) accession number: Q28H12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 53 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3