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P04418 (END5_BPT4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Endonuclease V
EC=3.1.25.1
Gene names
Name:denV
OrganismEnterobacteria phage T4 (Bacteriophage T4) [Reference proteome]
Taxonomic identifier10665 [NCBI]
Taxonomic lineageViruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › Tevenvirinae › T4likevirus ›
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length138 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme is a pyrimidine dimer DNA glycosylase. Excises pyrimidine dimers that are the major UV-lesion of a DNA duplex. It first hydrolyzes the glycosylic bond of the 5' pyrimidine of the dimer and then the intrapyrimidine phosphodiester bond.

Catalytic activity

Endonucleolytic cleavage near pyrimidine dimers to products with 5'-phosphate.

Subunit structure

Monomer.

Miscellaneous

Phage T4 deficient in the enzymes are extremely sensitive to UV.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 138138Endonuclease V
PRO_0000164934

Sites

Active site231Proton acceptor

Secondary structure

1 ...................... 138
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04418 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 90B889C8E6686697

FASTA13816,079
        10         20         30         40         50         60 
MTRINLTLVS ELADQHLMAE YRELPRVFGA VRKHVANGKR VRDFKISPTF ILGAGHVTFF 

        70         80         90        100        110        120 
YDKLEFLRKR QIELIAECLK RGFNIKDTTV QDISDIPQEF RGDYIPHEAS IAISQARLDE 

       130 
KIAQRPTWYK YYGKAIYA

« Hide

References

« Hide 'large scale' references
[1]"Identification, physical map location and sequence of the denV gene from bacteriophage T4."
Valerie K., Henderson E.E., Deriel J.K.
Nucleic Acids Res. 12:8085-8096(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence and analysis of the 58.3 to 65.5-kb early region of bacteriophage T4."
Valerie K., Stevens J., Lynch M., Henderson E.E., de Riel J.K.
Nucleic Acids Res. 14:8637-8654(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Physical mapping and complete nucleotide sequence of the denV gene of bacteriophage T4."
Radany E.H., Naumovski L., Love J.D., Gutekunst K.A., Hall D.H., Friedberg E.C.
J. Virol. 52:846-856(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Bacteriophage T4 genome."
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.
Microbiol. Mol. Biol. Rev. 67:86-156(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Site-directed deletion mutagenesis within the T4 endonuclease V gene: dispensable sequences within putative loop regions."
Dodson M.L., Prince M.A., Anderson W.F., Lloyd R.S.
Mutat. Res. 255:19-29(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[6]"Participation of glutamic acid 23 of T4 endonuclease V in the beta-elimination reaction of an abasic site in a synthetic duplex DNA."
Hori N., Doi T., Karaki Y., Kikuchi M., Ikehara M., Ohtsuka E.
Nucleic Acids Res. 20:4761-4764(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[7]"X-ray structure of T4 endonuclease V: an excision repair enzyme specific for a pyrimidine dimer."
Morikawa K., Matsumoto O., Tsujimoto M., Katayanagi K., Ariyoshi M., Doi T., Ikehara M., Inaoka T., Ohtsuka E.
Science 256:523-526(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X04567 Genomic DNA. Translation: CAA28215.1.
AF158101 Genomic DNA. Translation: AAD42563.1.
PIRNEBPT4. A93540.
RefSeqNP_049733.1. NC_000866.4.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ENIX-ray2.20A1-138[»]
1ENJX-ray1.80A1-138[»]
1ENKX-ray2.00A1-138[»]
1VASX-ray2.75A2-138[»]
2ENDX-ray1.45A1-138[»]
2FCCX-ray2.30A/B2-138[»]
ProteinModelPortalP04418.
SMRP04418. Positions 2-138.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1258606.

Phylogenomic databases

ProtClustDBCLSP2343276.

Family and domain databases

Gene3D1.10.440.10. 1 hit.
InterProIPR004260. Pyr-dimer_DNA_glycosylase.
IPR021143. Pyr-dimer_DNAGlyclase_EndonucV.
IPR024796. T4_endonuc_V_domain.
[Graphical view]
PfamPF03013. Pyr_excise. 1 hit.
[Graphical view]
PIRSFPIRSF001000. PDG_ENDV. 1 hit.
ProDomPD021350. Pyr-dimer_DNA_glycosylase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47077. Pyr-dimer_DNA_glycosylase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP04418.

Entry information

Entry nameEND5_BPT4
AccessionPrimary (citable) accession number: P04418
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents