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O67539 (DCD_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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:aq_1607
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Ontologies

Keywords
   Biological processNucleotide metabolism
   Molecular functionHydrolase
   Technical termComplete proteome
Reference 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 – 180180Deoxycytidine triphosphate deaminase HAMAP-Rule MF_00146
PRO_0000155963

Sequences

Sequence LengthMass (Da)Tools
O67539 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: B2710421A2FA48D6

FASTA18020,545
        10         20         30         40         50         60 
MILSDRSIRE LIEKGELKVE PYEPSHVQCS SLDLRLGNQI ALYEGEGVID VKKGTKGVRI 

        70         80         90        100        110        120 
LEFEEYFDIM PKQFLLATTL EYISLPPYVT AFVEGRSSLG RLGLFIENAG WVDAGFEGQI 

       130        140        150        160        170        180 
TLELFNANDR PIRLYRGMRI CQLVFARLDR PPERVYSGKY KGQKGVVPSR IHMDEELKSE 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07499.1.
PIRA70439.
RefSeqNP_214104.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_1607.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07499; AAC07499; aq_1607.
GeneID1193162.
KEGGaae:aq_1607.
PATRIC20960256. VBIAquAeo85532_1241.

Phylogenomic databases

eggNOGCOG0717.
HOGENOMHOG000228601.
KOK01494.
OMAGWIDAGF.
OrthoDBEOG67DPKR.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-1146-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_AQUAE
AccessionPrimary (citable) accession number: O67539
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: February 19, 2014
This is version 83 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