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B2UUI8 (DCD_HELPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxycytidine triphosphate deaminase

Short name=dCTP deaminase
EC=3.5.4.13
Gene names
Name:dcd
Ordered Locus Names:HPSH_05555
OrganismHelicobacter pylori (strain Shi470) [Complete proteome] [HAMAP]
Taxonomic identifier512562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Ontologies

Keywords
   Biological processNucleotide metabolism
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processdUMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

dUTP biosynthetic process

Inferred from electronic annotation. Source: InterPro

pyrimidine ribonucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functiondCTP deaminase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 188188Deoxycytidine triphosphate deaminase HAMAP-Rule MF_00146
PRO_1000096431

Sequences

Sequence LengthMass (Da)Tools
B2UUI8 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: BBFC0A31FBED4DAE

FASTA18820,901
        10         20         30         40         50         60 
MGLKADSWIK KMSLEHGMIS PFCEKQIGKD VISYGLSSYG YDIRVGSEFM LFDNKNALID 

        70         80         90        100        110        120 
PKNFDPNNTT KIDASKEGFF ILPANAFALA HTIEYFKMPK DTLAICLGKS TYARCGIIVN 

       130        140        150        160        170        180 
VTPFEPEFEG YITIEISNTT NLPAKVYANE GIAQVVFLQG DEVCEQSYKD RGGKYQGQVG 


ITLPKILK 

« Hide

References

[1]"Genome sequence of Helicobacter pylori from the remote Amazon: traces of Asian ancestry of the first Americans."
Kersulyte D., Kalia A., Gilman R.H., Berg D.E.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Shi470.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001072 Genomic DNA. Translation: ACD48520.1.
RefSeqYP_001910550.1. NC_010698.2.

3D structure databases

ProteinModelPortalB2UUI8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING512562.HPSH_05555.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD48520; ACD48520; HPSH_05555.
GeneID6297251.
KEGGhps:HPSH_05555.
PATRIC20613567. VBIHelPyl23559_1084.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0717.
HOGENOMHOG000228600.
KOK01494.
OMAMEYFRIP.
OrthoDBEOG67DPKR.
ProtClustDBPRK00416.

Enzyme and pathway databases

BioCycHPYL512562:GHHZ-1103-MONOMER.
UniPathwayUPA00610; UER00665.

Family and domain databases

HAMAPMF_00146. dCTP_deaminase.
InterProIPR011962. dCTP_deam.
IPR008180. dUTP_pyroPase.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR02274. dCTP_deam. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDCD_HELPS
AccessionPrimary (citable) accession number: B2UUI8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways