O86820 (END8B_STRCO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable endonuclease 8 2

Alternative name(s):
DNA glycosylase/AP lyase Nei 2
EC=3.2.2.-
DNA-(apurinic or apyrimidinic site) lyase Nei 2
EC=4.2.99.18
Endonuclease VIII 2

Gene names

Name:	nei
Ordered Locus Names:	SCO5760
ORF Names:	SC7C7.15c

Organism

Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]

Taxonomic identifier

100226 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › Streptomyces coelicolor

Protein attributes

Sequence length	276 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 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.
Catalytic activity	Removes damaged bases from DNA, leaving an abasic site. 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.
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 Reference proteome
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	DNA-(apurinic or apyrimidinic site) lyase activity Inferred from electronic annotation. Source: EC damaged DNA binding Inferred from electronic annotation. Source: InterPro hydrolase activity, hydrolyzing N-glycosyl compounds Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 276	275	Probable endonuclease 8 2		PRO_0000170902
Regions
	Zinc finger	222 – 260	39	FPG-type
Sites
	Active site	2	1	Schiff-base intermediate with DNA By similarity
	Active site	3	1	Proton donor By similarity
	Active site	51	1	Proton donor; for beta-elimination activity By similarity
	Active site	250	1	Proton donor; for delta-elimination activity By similarity
	Binding site	165	1	DNA By similarity

Sequences

	Sequence		Length	Mass (Da)
	O86820 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 01106CD65EF94DE9	FASTA	276	30,408
	10 20 30 40 50 60 MPEGDTVWQA ARRLHDALAG RVLTRSDFRV PRYATVDLTG RTVLDVTPRG KHLLTRVEGG 70 80 90 100 110 120 LTVHSHLRMD GSWKVFAPGQ RWSGGPAHQI RVILGTADRT AVGYRLPVLD ILRTAEEQRA 130 140 150 160 170 180 VGHLGPDLLG PDWDPERALD NLRADPPRAL GEALLDQRNL AGIGNVYKSE LCFLLGVTPW 190 200 210 220 230 240 LPVGELPADR AARLPTLAKK LLEANRDRPV RRTTGLRGQD LFVYGRAPRP CLRCGTSVRV 250 260 270 ADQGDGSRER PTYWCPTCQA GPAPRPGGRT GVRPRR

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL939125 Genomic DNA. Translation: CAA19861.1.
PIR	T35693.
RefSeq	NP_629885.1. NC_003888.3.
3D structure databases
ProteinModelPortal	O86820.
ModBase	Search...
Protein-protein interaction databases
STRING	100226.SCO5760.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1101202.
KEGG	sco:SCO5760.
PATRIC	23741404. VBIStrCoe124346_5849.
Phylogenomic databases
eggNOG	COG0266.
HOGENOM	HOG000020880.
KO	K05522.
OMA	WFAFPEL.
ProtClustDB	CLSK520654.
Family and domain databases
InterPro	IPR015886. DNA_glyclase/AP_lyase_DNA-bd. IPR015887. DNA_glyclase_Znf_dom_DNA_BS. IPR012319. DNA_glycosylase/AP_lyase_cat. IPR010979. Ribosomal_S13-like_H2TH. IPR000214. Znf_DNA_glyclase/AP_lyase. [Graphical view]
Pfam	PF01149. Fapy_DNA_glyco. 1 hit. PF06831. H2TH. 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

END8B_STRCO

Accession

Primary (citable) accession number: O86820

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program