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Q5PCL7 (END8_SALPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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 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:SPA2015
OrganismSalmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP]
Taxonomic identifier295319 [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_1000067208

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
Q5PCL7 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 0B2ADF746F14F35B

FASTA26329,847
        10         20         30         40         50         60 
MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF AQLKPYESQL TGQIITRIET 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 FHRDGEACER 

       250        260 
CGGIIEKTTL SSRPFYWCPH CQK 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000026 Genomic DNA. Translation: AAV77918.1.
RefSeqYP_151230.1. NC_006511.1.

3D structure databases

ProteinModelPortalQ5PCL7.
SMRQ5PCL7. Positions 2-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295319.SPA2015.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV77918; AAV77918; SPA2015.
PATRIC32353457. VBISalEnt134188_2147.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020882.
OMAGPDVLDM.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycSENT295319:GJBZ-2015-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_SALPA
AccessionPrimary (citable) accession number: Q5PCL7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 67 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