Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B4SZD3 (END8_SALNS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 42. 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:
Endonuclease 8
Alternative name(s):
DNA glycosylase/AP lyase Nei
EC=3.2.2.-
EC=4.2.99.18
DNA-(apurinic or apyrimidinic site) lyase Nei
Endonuclease VIII
Gene names
Name:nei
Ordered Locus Names:SNSL254_A0788
OrganismSalmonella newport (strain SL254) [Complete proteome] [HAMAP]
Taxonomic identifier423368 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates By similarity. HAMAP-Rule MF_01253

Catalytic activity

Removes damaged bases from DNA, leaving an abasic site. HAMAP-Rule MF_01253

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_01253

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01253

Sequence similarities

Belongs to the FPG family.

Contains 1 FPG-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 263262Endonuclease 8 HAMAP-Rule MF_01253
PRO_1000139944

Regions

Zinc finger229 – 26335FPG-type HAMAP-Rule MF_01253

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site531Proton donor; for beta-elimination activity By similarity
Active site2531Proton donor; for delta-elimination activity By similarity
Binding site701DNA By similarity
Binding site1251DNA By similarity
Binding site1691DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
B4SZD3 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 8D66AA1C9236E787

FASTA26329,861
        10         20         30         40         50         60 
MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF AQLKPYESQL TGQLVTRIET RGKALLTHFS 

        70         80         90        100        110        120 
NGLTLYSHNQ LYGVWRVIDT GEIPQTTRIL RVRLQTADKT ILLYSASDIE MLTAEQLTTH 

       130        140        150        160        170        180 
PFLQRVGPDV LDARLTPEEV KARLLSPRFR NRQFSGLLLD QAFLAGLGNY LRVEILWQVG 

       190        200        210        220        230        240 
LTGQHKAKDL NEAQLNALSH ALLDIPRLSY TTRGQADENK HHGALFRFKV FHRDGEVCER 

       250        260 
CGGIIEKTTL SSRPFYWCPH CQK 

« Hide

References

[1]"Complete genome of Salmonella newport strain SL254."
Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., Leclerc J., Cebula T., Sebastian Y.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SL254.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001113 Genomic DNA. Translation: ACF65550.1.
RefSeqYP_002039966.1. NC_011080.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING423368.SNSL254_A0788.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF65550; ACF65550; SNSL254_A0788.
PATRIC18519998. VBISalEnt114557_0910.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020882.
OMAGPDVLDM.
OrthoDBEOG6QP131.
ProtClustDBPRK10445.

Enzyme and pathway databases

BioCycSENT423368:GHJB-779-MONOMER.

Family and domain databases

HAMAPMF_01253. Endonuclease_8.
InterProIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR023713. Endonuclease-VIII.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PfamPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
SMARTSM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
PROSITEPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEND8_SALNS
AccessionPrimary (citable) accession number: B4SZD3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: April 16, 2014
This is version 42 of the entry and version 1 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