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Protein

Deoxycytidylate deaminase

Gene

CD

Organism
Enterobacteria phage T2 (Bacteriophage T2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Supplies the nucleotide substrate for thymidylate synthetase.

Catalytic activityi

dCMP + H2O = dUMP + NH3.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi19 – 191Zinc 1; structuralBy similarity
Metal bindingi49 – 491Zinc 1; structuralBy similarity
Metal bindingi94 – 941Zinc 1; structuralBy similarity
Metal bindingi102 – 1021Zinc 2; catalyticBy similarity
Metal bindingi104 – 1041Zinc 2; catalyticBy similarity
Active sitei106 – 1061Proton donorBy similarity
Metal bindingi132 – 1321Zinc 2; catalyticBy similarity
Metal bindingi135 – 1351Zinc 2; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxycytidylate deaminase (EC:3.5.4.12)
Alternative name(s):
dCMP deaminase
Gene namesi
Name:CD
OrganismiEnterobacteria phage T2 (Bacteriophage T2)
Taxonomic identifieri10664 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostiEscherichia coli [TaxID: 562]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Deoxycytidylate deaminasePRO_0000171700Add
BLAST

Interactioni

Subunit structurei

Homohexamer.

Structurei

3D structure databases

ProteinModelPortaliP00814.
SMRiP00814. Positions 1-188.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 171171CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
IPR015517. dCMP_deaminase-rel.
[Graphical view]
PANTHERiPTHR11086. PTHR11086. 1 hit.
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
PIRSFiPIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00814-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKASTVLQIA YLVSQESKCC SWKVGAVIEK NGRIISTGYN GSPAGGVNCD
60 70 80 90 100
NYAAIEGWLL NKPKHTIIQG HKPECVSFGT SDRFVLAKEH RSAHSEWSSK
110 120 130 140 150
NEIHAELNAI LFAARNGSSI EGATMYVTLS PCPDCAKAIA QSGIKKLVYC
160 170 180
ETYDKNKPGW DDILRNAGIE VFNVPKLNWE NISEFCGE
Length:188
Mass (Da):20,599
Last modified:July 21, 1986 - v1
Checksum:iA13EAF89D5CEB14A
GO

Sequence databases

PIRiA01011. DUBPC2.

Cross-referencesi

Sequence databases

PIRiA01011. DUBPC2.

3D structure databases

ProteinModelPortaliP00814.
SMRiP00814. Positions 1-188.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
IPR015517. dCMP_deaminase-rel.
[Graphical view]
PANTHERiPTHR11086. PTHR11086. 1 hit.
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
PIRSFiPIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiDCTD_BPT2
AccessioniPrimary (citable) accession number: P00814
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 1, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.