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P00814 (DCTD_BPT2) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Deoxycytidylate deaminase

EC=3.5.4.12
Alternative name(s):
dCMP deaminase
Gene names
Name:CD
OrganismEnterobacteria phage T2 (Bacteriophage T2)
Taxonomic identifier10664 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Supplies the nucleotide substrate for thymidylate synthetase.

Catalytic activity

dCMP + H2O = dUMP + NH3.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Enzyme regulation

Allosteric enzyme whose activity is greatly influenced by the end products of its metabolic pathway, dCTP and dTTP.

Subunit structure

Homohexamer.

Sequence similarities

Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termAllosteric enzyme
Direct protein sequencing
Gene Ontology (GO)
   Biological_processnucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiondCMP deaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 188188Deoxycytidylate deaminase
PRO_0000171700

Sites

Active site1061Proton donor By similarity
Metal binding191Zinc 1; structural By similarity
Metal binding491Zinc 1; structural By similarity
Metal binding941Zinc 1; structural By similarity
Metal binding1021Zinc 2; catalytic By similarity
Metal binding1041Zinc 2; catalytic By similarity
Metal binding1321Zinc 2; catalytic By similarity
Metal binding1351Zinc 2; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
P00814 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: A13EAF89D5CEB14A

FASTA18820,599
        10         20         30         40         50         60 
MKASTVLQIA YLVSQESKCC SWKVGAVIEK NGRIISTGYN GSPAGGVNCD NYAAIEGWLL 

        70         80         90        100        110        120 
NKPKHTIIQG HKPECVSFGT SDRFVLAKEH RSAHSEWSSK NEIHAELNAI LFAARNGSSI 

       130        140        150        160        170        180 
EGATMYVTLS PCPDCAKAIA QSGIKKLVYC ETYDKNKPGW DDILRNAGIE VFNVPKLNWE 


NISEFCGE 

« Hide

References

[1]"Complete amino acid sequence of an allosteric enzyme, T2 bacteriophage deoxycytidylate deaminase."
Maley G.F., Guarino D.U., Maley F.
J. Biol. Chem. 258:8290-8297(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRDUBPC2. A01011.

3D structure databases

ProteinModelPortalP00814.
SMRP00814. Positions 1-188.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR015517. Cyt_deaminase.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
[Graphical view]
PANTHERPTHR11086. PTHR11086. 1 hit.
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
PIRSFPIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMSSF53927. SSF53927. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDCTD_BPT2
AccessionPrimary (citable) accession number: P00814
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 16, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families