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A6Q6E1 (DCD_SULNB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:SUN_0090
OrganismSulfurovum sp. (strain NBC37-1) [Complete proteome] [HAMAP]
Taxonomic identifier387093 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaSulfurovum

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_1000009824

Sequences

Sequence LengthMass (Da)Tools
A6Q6E1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: AE4FFE58A74A5A00

FASTA18820,976
        10         20         30         40         50         60 
MGLKPDKWIR EKSLNEAMIT PFCEGLVGEG VVSYGLSSYG YDIRVSDEFK IFTNINAEVV 

        70         80         90        100        110        120 
DPKDFNENNV VDFKGDICIV PPNSFALART VEYFRMPKDT LAICLGKSTY ARCGIIVNVT 

       130        140        150        160        170        180 
PFEPGFEGHI TIEISNTTPL PAKIYANEGI AQVLFLEGDE QCETTYSDRK GKYQSQTGIT 


LPRILKQQ 

« Hide

References

[1]"Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBC37-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009179 Genomic DNA. Translation: BAF71050.1.
RefSeqYP_001357407.1. NC_009663.1.

3D structure databases

ProteinModelPortalA6Q6E1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING387093.SUN_0090.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF71050; BAF71050; SUN_0090.
GeneID5362028.
KEGGsun:SUN_0090.
PATRIC23773107. VBISulSp49917_0091.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSP387093:GH25-94-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_SULNB
AccessionPrimary (citable) accession number: A6Q6E1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 43 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