Q92BR0 (END4_LISIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable endonuclease 4
EC=3.1.21.2

Alternative name(s):
Endodeoxyribonuclease IV
Endonuclease IV

Gene names

Name:	nfo
Ordered Locus Names:	lin1487

Organism

Listeria innocua serovar 6a (strain CLIP 11262) [Complete proteome] [HAMAP]

Taxonomic identifier

272626 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria › Listeria innocua

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin By similarity. HAMAP-Rule MF_00152
Catalytic activity	Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products. HAMAP-Rule MF_00152
Cofactor	Binds 3 zinc ions By similarity.
Sequence similarities	Belongs to the AP endonuclease 2 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Ligand	Metal-binding Zinc
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: HAMAP nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro deoxyribonuclease IV (phage-T4-induced) 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
	Chain	1 – 297	297	Probable endonuclease 4 HAMAP-Rule MF_00152		PRO_0000190846
Sites
	Metal binding	69	1	Zinc 1 By similarity
	Metal binding	110	1	Zinc 1 By similarity
	Metal binding	145	1	Zinc 1 By similarity
	Metal binding	145	1	Zinc 2 By similarity
	Metal binding	179	1	Zinc 2 By similarity
	Metal binding	182	1	Zinc 3 By similarity
	Metal binding	214	1	Zinc 2 By similarity
	Metal binding	227	1	Zinc 3 By similarity
	Metal binding	229	1	Zinc 3 By similarity
	Metal binding	259	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92BR0 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: E2AAA1025C402002	FASTA	297	32,843
	10 20 30 40 50 60 MLRLGSHVSM SGKKMLLGAS EEAASYGSNT FMIYTGAPQN TRRKPIEELN IEAGLEHMKA 70 80 90 100 110 120 HDMADIVVHA PYIINIGNSV KPETFELGVN FLQSEIERTR ALGAKQIVLH PGAHVGEGAD 130 140 150 160 170 180 KGIKQIIQGL NEALIHDQDV QIALETMAGK GSECGRTFEE LAQIIDGVTH NELLSVTFDT 190 200 210 220 230 240 CHTHDAGYDI VNDFDGVLNE FDKIIGIDRL KVLHINDSKN ERGAHKDRHA NIGFGHIGFD 250 260 270 280 290 ALHYIVHHPQ LSNIPKILET PYVGEDKASK KAPYKWEIAM LRNGEFDPDL LNKIQNS

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIP 11262.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL596168 Genomic DNA. Translation: CAC96718.1.
PIR	AF1618.
RefSeq	NP_470823.1. NC_003212.1.
3D structure databases
ProteinModelPortal	Q92BR0.
SMR	Q92BR0. Positions 2-295.
ModBase	Search...
Protein-protein interaction databases
STRING	272626.lin1487.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC96718; CAC96718; CAC96718.
GeneID	1130094.
KEGG	lin:lin1487.
PATRIC	20299707. VBILisInn102668_1520.
Organism-specific databases
GenoList	LIN1487.
CMR	Search...
Phylogenomic databases
eggNOG	COG0648.
HOGENOM	HOG000224895.
KO	K01151.
OMA	INLGHPD.
ProtClustDB	PRK01060.
Family and domain databases
Gene3D	3.20.20.150. 1 hit.
HAMAP	MF_00152. Nfo.
InterPro	IPR018246. AP_endonuc_F2_Zn_BS. IPR001719. Endodeoxyribonuclease_IV. IPR013022. Xyl_isomerase-like_TIM-brl. [Graphical view]
PANTHER	PTHR21445. PTHR21445. 1 hit.
Pfam	PF01261. AP_endonuc_2. 1 hit. [Graphical view]
SMART	SM00518. AP2Ec. 1 hit. [Graphical view]
SUPFAM	SSF51658. Xyl_isomerase-like_TIM-brl. 1 hit.
TIGRFAMs	TIGR00587. nfo. 1 hit.
PROSITE	PS00729. AP_NUCLEASE_F2_1. 1 hit. PS00730. AP_NUCLEASE_F2_2. 1 hit. PS00731. AP_NUCLEASE_F2_3. 1 hit. PS51432. AP_NUCLEASE_F2_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

END4_LISIN

Accession

Primary (citable) accession number: Q92BR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program