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Q7ZX23

- KCY_XENLA

UniProt

Q7ZX23 - KCY_XENLA

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Protein

UMP-CMP kinase

Gene

cmpk1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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.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

Mg2+UniRule annotationNote: Binds 1 Mg(2+) 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:cmpk1
Synonyms:cmpk
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-980044. cmpk1.

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 – 193193UMP-CMP kinasePRO_0000292026Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ7ZX23.
SMRiQ7ZX23. Positions 3-193.
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

HOVERGENiHBG108060.
KOiK13800.

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.

Q7ZX23-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKPLVVFVLG GPGAGKGTQC ERIVQKYGYT HLSAGDLLRD ERKKPDSQYG
60 70 80 90 100
ELIESYIRDG KIVPVEITIS LLQRAMERTM AFDANKHKFL IDGFPRNEDN
110 120 130 140 150
LQGWERTMNG KADVSFVLFF DCDNETCIER CLERGKSSGR SDDNRESLEK
160 170 180 190
RIQTYLQSTR PIIDLYEKRG KVRKVDASKS VDEVFTKVQN IFD
Length:193
Mass (Da):22,106
Last modified:June 26, 2007 - v2
Checksum:iB2BD9C8638D86360
GO

Sequence cautioni

The sequence AAH45275.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH54975.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161F → I in AAH54975. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC045275 mRNA. Translation: AAH45275.1. Different initiation.
BC054975 mRNA. Translation: AAH54975.2. Different initiation.
RefSeqiNP_001082709.1. NM_001089240.1.
UniGeneiXl.6001.

Genome annotation databases

GeneIDi398670.
KEGGixla:398670.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC045275 mRNA. Translation: AAH45275.1 . Different initiation.
BC054975 mRNA. Translation: AAH54975.2 . Different initiation.
RefSeqi NP_001082709.1. NM_001089240.1.
UniGenei Xl.6001.

3D structure databases

ProteinModelPortali Q7ZX23.
SMRi Q7ZX23. Positions 3-193.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 398670.
KEGGi xla:398670.

Organism-specific databases

CTDi 51727.
Xenbasei XB-GENE-980044. cmpk1.

Phylogenomic databases

HOVERGENi HBG108060.
KOi K13800.

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. NIH - Xenopus Gene Collection (XGC) project
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiKCY_XENLA
AccessioniPrimary (citable) accession number: Q7ZX23
Secondary accession number(s): Q7SY80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: November 26, 2014
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3