Q6HDN3 (END4_BACHK) 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:	BT9727_4024

Organism

Bacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]

Taxonomic identifier

281309 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › Bacillus thuringiensis › Bacillus thuringiensis subsp. konkukian

Protein attributes

Sequence length	298 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 – 298	298	Probable endonuclease 4 HAMAP-Rule MF_00152		PRO_0000190823
Sites
	Metal binding	69	1	Zinc 1 By similarity
	Metal binding	111	1	Zinc 1 By similarity
	Metal binding	146	1	Zinc 1 By similarity
	Metal binding	146	1	Zinc 2 By similarity
	Metal binding	180	1	Zinc 2 By similarity
	Metal binding	183	1	Zinc 3 By similarity
	Metal binding	215	1	Zinc 2 By similarity
	Metal binding	228	1	Zinc 3 By similarity
	Metal binding	230	1	Zinc 3 By similarity
	Metal binding	260	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6HDN3 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: CD37009827F26C08	FASTA	298	32,910
	10 20 30 40 50 60 MLKIGSHVSM SGKKMLLAAS EEAVSYGATT FMIYTGAPQN TRRKPIEELN IEAGRKHMEQ 70 80 90 100 110 120 NGIEEIIVHA PYIINVGNTT KPETFQLGVD FLRMEIERTS ALGVAKQIVL HPGAHVGAGA 130 140 150 160 170 180 DAGIQQIIKG LNEVLTPDQT VNIALETMAG KGTECGRSFE EIAKIIDGVK YNEKLSVCFD 190 200 210 220 230 240 TCHTHDAGYD IVNDFDGVLN EFDKIVGIDR LQVLHINDSK NVRGAGKDRH ENIGFGHIGY 250 260 270 280 290 KALHHIVHHP QLTHVPKILE TPYVGEDKKD KKPPYKLEIE MLKNGTFDEG LLEKIKAQ

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT63495.1.
RefSeq	YP_038343.1. NC_005957.1.
3D structure databases
ProteinModelPortal	Q6HDN3.
SMR	Q6HDN3. Positions 2-298.
ModBase	Search...
Protein-protein interaction databases
STRING	281309.BT9727_4024.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT63495; AAT63495; BT9727_4024.
GeneID	2855869.
KEGG	btk:BT9727_4024.
PATRIC	18989135. VBIBacThu119411_4292.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0648.
HOGENOM	HOG000224895.
KO	K01151.
OMA	INLGHPD.
ProtClustDB	PRK01060.
Enzyme and pathway databases
BioCyc	BTHU281309:GJID-4098-MONOMER.
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_BACHK

Accession

Primary (citable) accession number: Q6HDN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program