Uracil-DNA glycosylase
Details
- Name
- Uracil-DNA glycosylase
- Synonyms
- 3.2.2.27
- UDG
- UNG
- Gene Name
- Not Available
- Organism
- HHV-1
- 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
- Functionsuracil DNA N-glycosylase activityProcessesbase-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
- UDG (PF03167)
- 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
Resource Link UniProtKB ID P10186 UniProtKB Entry Name UNG_HHV11 GenBank Protein ID 59502 GenBank Gene ID X14112 - General References
- 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]
- 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]
- 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]
- 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]
- 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]