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Q9YE60 (AGOG_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:
N-glycosylase/DNA lyase
Alternative name(s):
8-oxoguanine DNA glycosylase
EC=3.2.2.-
AGOG
DNA-(apurinic or apyrimidinic site) lyase
Short name=AP lyase
EC=4.2.99.18
Gene names
Ordered Locus Names:APE_0710.1
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates By similarity. HAMAP-Rule MF_01168

Catalytic activity

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. HAMAP-Rule MF_01168

Domain

Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif). HAMAP-Rule MF_01168

Sequence similarities

Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family.

Ontologies

Keywords
   Biological processDNA damage
DNA excision
DNA repair
   Molecular functionHydrolase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processbase-excision repair

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionDNA-(apurinic or apyrimidinic site) lyase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

oxidized base lesion DNA N-glycosylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 288288N-glycosylase/DNA lyase HAMAP-Rule MF_01168
PRO_0000185108

Regions

Region134 – 20370Helix-hairpin-helix HAMAP-Rule MF_01168

Sites

Active site1601Schiff-base intermediate with DNA By similarity
Active site1911 Potential
Binding site3518-oxoguanine By similarity
Binding site6218-oxoguanine; via carbonyl oxygen By similarity
Binding site7318-oxoguanine By similarity
Binding site16418-oxoguanine By similarity
Binding site18918-oxoguanine; via carbonyl oxygen By similarity
Binding site23818-oxoguanine By similarity
Binding site24218-oxoguanine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9YE60 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: A57E5A1F0A2786C3

FASTA28831,443
        10         20         30         40         50         60 
MAQRVRWERV ERVAEAFSRL SIGEVLGFEE QVDPQYKLVS RLAGEIGAGK AALSALLVGL 

        70         80         90        100        110        120 
ASYRLAMRGE EWWLCFYRHM RSSLPRAEGL RGVLRAVEGF LTSCSGAAIG REAKLRRVRR 

       130        140        150        160        170        180 
AASAAEVLGE VLDNPLVLVE RPSEVLEALR VALGEKGFRK TTVFSVKIAY YAVRPLAGRK 

       190        200        210        220        230        240 
PLTLDVPIPV DVRVACASIS SEMVEAPSYR EVVARPEAAQ RAWGRVARSS GIPVLHIDSI 

       250        260        270        280 
LWVTGWAPRE LPPGEAREAV AGILSRALDR GKAVLLASEL VRRPCPGG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000002 Genomic DNA. Translation: BAA79686.2.
PIRF72660.
RefSeqNP_147435.2. NC_000854.2.

3D structure databases

ProteinModelPortalQ9YE60.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272557.APE_0710.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA79686; BAA79686; APE_0710.1.
GeneID1444838.
KEGGape:APE_0710.1.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4047.
HOGENOMHOG000033850.
KOK01741.
ProtClustDBPRK13280.

Enzyme and pathway databases

BioCycAPER272557:GJD6-517-MONOMER.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPMF_01168. AGOG.
InterProIPR011257. DNA_glycosylase.
IPR023170. HTH_base_excis_C.
IPR015254. N-Glyclase/DNA_lyase-like_arc.
IPR016544. N-Glyclase/DNA_lyase_arc.
[Graphical view]
PfamPF09171. DUF1886. 1 hit.
[Graphical view]
PIRSFPIRSF008955. AGOG. 1 hit.
SUPFAMSSF48150. SSF48150. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAGOG_AERPE
AccessionPrimary (citable) accession number: Q9YE60
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 26, 2007
Last modified: February 19, 2014
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families