Endonuclease 8 - Salmonella typhi

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Q8Z8D2 (END8_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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:	STY0771, t2148

Organism

Salmonella typhi [Complete proteome] [HAMAP]

Taxonomic identifier

90370 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length	263 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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.
Sequence similarities	Belongs to the FPG family. Contains 1 FPG-type zinc finger.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Glycosidase Hydrolase Lyase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological_process	base-excision repair Inferred from electronic annotation. Source: InterPro nucleotide-excision repair Inferred from electronic annotation. Source: InterPro
Molecular_function	damaged DNA binding Inferred from electronic annotation. Source: InterPro endonuclease activity Inferred from electronic annotation. Source: InterPro oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 263

262

Endonuclease 8 HAMAP-Rule MF_01253

PRO_0000170897

Regions

Zinc finger

229 – 263

FPG-type HAMAP-Rule MF_01253

Sites

Active site

Schiff-base intermediate with DNA By similarity

Active site

Proton donor By similarity

Active site

Proton donor; for beta-elimination activity By similarity

Active site

253

Proton donor; for delta-elimination activity By similarity

Binding site

DNA By similarity

Binding site

125

DNA By similarity

Binding site

169

DNA By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8Z8D2 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 63257D84FF59BEE2
Show »

FASTA

263

29,865

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

        70         80         90        100        110        120 
NGLTLYSHNQ LYGVWRVIDT GEIPQTTRIL RVRLQTADKI ILLYSASDIE MLTAEQLMTH 

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

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

       250        260 
CGGIIEKTTL SSRPFYWCAH CQK

« Hide

References

[1]

"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P.

Barrell B.G.
Nature 413:848-852(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.

[2]

"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL627268 Genomic DNA. Translation: CAD05190.1. AE014613 Genomic DNA. Translation: AAO69762.1.
RefSeq	NP_805902.1. NC_004631.1.
3D structure databases
ProteinModelPortal	Q8Z8D2.
SMR	Q8Z8D2. Positions 2-262.
ModBase	Search...
Protein-protein interaction databases
STRING	220341.STY0771.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1067263.
KEGG	stt:t2148.
PATRIC	18539403. VBISalEnt120419_0776.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0266.
HOGENOM	HOG000020882.
KO	K05522.
OMA	WFAFPEL.
ProtClustDB	PRK10445.
Family and domain databases
HAMAP	MF_01253. Endonuclease_8.
InterPro	IPR015886. 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]
Pfam	PF01149. Fapy_DNA_glyco. 1 hit. PF06831. H2TH. 1 hit. PF06827. zf-FPG_IleRS. 1 hit. [Graphical view]
SMART	SM00898. Fapy_DNA_glyco. 1 hit. [Graphical view]
SUPFAM	SSF81624. Form_DNAglyc_cat. 1 hit. SSF46946. Ribosomal_H2TH. 1 hit.
PROSITE	PS51068. FPG_CAT. 1 hit. PS01242. ZF_FPG_1. 1 hit. PS51066. ZF_FPG_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

END8_SALTI

Accession

Primary (citable) accession number: Q8Z8D2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 85 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents