Uracil-DNA glycosylase

Details

Name
Uracil-DNA glycosylase
Synonyms
  • 3.2.2.27
  • UDG
  • UNG
Gene Name
Not Available
UniProtKB Entry
P10186Swiss-Prot
Organism
HHV-1
NCBI Taxonomy ID
10299
Amino acid sequence
>lcl|BSEQ0011378|Uracil-DNA glycosylase
MKRACSRSPSPRRRPSSPRRTPPRDGTPPQKADADDPTPGASNDASTETRPGSGGEPAAC
RSSGPAALLAALEAGPAGVTFSSSAPPDPPMDLTNGGVSPAATSAPLDWTTFRRVFLIDD
AWRPLMEPELANPLTAHLLAEYNRRCQTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPY
HHPGQAHGLAFSVRANVPPPPSLRNVLAAVKNCYPEARMSGHGCLEKWARDGVLLLNTTL
TVKRGAAASHSRIGWDRFVGGVIRRLAARRPGLVFMLWGTHAQNAIRPDPRVHCVLKFSH
PSPLSKVPFGTCQHFLVANRYLETRSISPIDWSV
Number of residues
334
Molecular Weight
36327.865
Theoretical pI
9.61
GO Classification
Functions
uracil DNA N-glycosylase activity
Processes
base-excision repair
General Function
Uracil dna n-glycosylase activity
Specific Function
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or deamination of cytosine. Therefore may reduce deleterious uracil incorporation into the viral genome, particularly, in terminally differentiated neurons which lack DNA repair enzymes.
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0011379|Uracil-DNA glycosylase
ATGAAGCGGGCCTGCAGCCGAAGCCCCTCACCACGCCGCCGCCCATCATCGCCACGTCGG
ACCCCACCCCGCGACGGGACGCCGCCACAAAAAGCAGACGCCGACGACCCCACTCCCGGC
GCCTCTAACGATGCCTCGACGGAAACCCGTCCGGGTTCGGGGGGCGAACCGGCCGCCTGT
CGCTCGTCAGGGCCGGCGGGCGCTCCTCGCCGCCCTAGAGGCTGTCCCGCTGGTGTGACG
TTTTCCTCGTCCGCGCCCCCCGACCCTCCCATGGATTTAACAAACGGGGGGGTGTCGCCT
GCGGCGACCTCGGCGCCTCTGGACTGGACCACGTTTCGGCGTGTGTTTCTGATCGACGAC
GCGTGGCGGCCCCTGATGGAGCCTGAGCTGGCGAACCCCTTAACCGCCCACCTCCTGGCC
GAATATAATCGTCGGTGCCAGACCGAAGAGGTGCTGCCGCCGCGGGAGGATGTGTTTTCG
TGGACTCGTTATTGCACCCCCGACGAGGTGCGCGTGGTTATCATCGGCCAGGACCCATAT
CACCACCCCGGCCAGGCGCACGGACTTGCGTTTAGCGTGCGCGCGAACGTGCCGCCTCCC
CCGAGTCTTCGGAATGTCTTGGCGGCCGTCAAGAACTGTTATCCCGAGGCACGGATGAGC
GGCCACGGTTGCCTGGAAAAGTGGGCGCGGGACGGCGTCCTGTTACTAAACACGACCCTG
ACCGTCAAGCGCGGGGCGGCGGCGTCCCACTCTAGAATCGGTTGGGACCGCTTCGTGGGC
GGAGTTATCCGCCGGTTGGCCGCGCGCCGCCCCGGCCTGGTGTTTATGCTCTGGGGCACA
CACGCCCAGAATGCCATCAGGCCGGACCCTCGGGTCCATTGCGTCCTCAAGTTTTCGCAC
CCGTCGCCCCTCTCCAAGGTTCCGTTCGGAACCTGCCAGCATTTCCTCGTGGCGAACCGA
TACCTCGAGACCCGGTCGATTTCACCCATCGACTGGTCGGTTTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP10186
UniProtKB Entry NameUNG_HHV11
GenBank Protein ID59502
GenBank Gene IDX14112
PDB ID(s)1LAU, 1UDG, 1UDH, 1UDI, 2C53, 2C56, 4L5N
KEGG IDvg:2703370
NCBI Gene ID2703370
General References
  1. McGeoch DJ, Dalrymple MA, Davison AJ, Dolan A, Frame MC, McNab D, Perry LJ, Scott JE, Taylor P: The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. J Gen Virol. 1988 Jul;69 ( Pt 7):1531-74. [Article]
  2. Ushijima Y, Luo C, Goshima F, Yamauchi Y, Kimura H, Nishiyama Y: Determination and analysis of the DNA sequence of highly attenuated herpes simplex virus type 1 mutant HF10, a potential oncolytic virus. Microbes Infect. 2007 Feb;9(2):142-9. Epub 2006 Dec 12. [Article]
  3. Savva R, McAuley-Hecht K, Brown T, Pearl L: The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature. 1995 Feb 9;373(6514):487-93. [Article]
  4. Savva R, Pearl LH: Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycosylase inhibitor protein complex. Nat Struct Biol. 1995 Sep;2(9):752-7. [Article]
  5. Krusong K, Carpenter EP, Bellamy SR, Savva R, Baldwin GS: A comparative study of uracil-DNA glycosylases from human and herpes simplex virus type 1. J Biol Chem. 2006 Feb 24;281(8):4983-92. Epub 2005 Nov 22. [Article]

Associated Data

Bio-Entities
Bio-EntityType
Uracil-DNA glycosylase (HHV-1)protein
primary
Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Uracilexperimental, investigationalunknowntargetDetails