Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A7Z6S8 (END4_BACA2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable endonuclease 4

EC=3.1.21.2
Alternative name(s):
Endodeoxyribonuclease IV
Endonuclease IV
Gene names
Name:nfo
Ordered Locus Names:RBAM_023440
OrganismBacillus amyloliquefaciens subsp. plantarum (strain DSM 23117 / BGSC 10A6 / FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP-Rule MF_00152

Sequence similarities

Belongs to the AP endonuclease 2 family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   LigandMetal-binding
Zinc
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentintracellular

Inferred from electronic annotation. Source: InterPro

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

deoxyribonuclease IV (phage-T4-induced) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Probable endonuclease 4 HAMAP-Rule MF_00152
PRO_1000011288

Sites

Metal binding691Zinc 1 By similarity
Metal binding1101Zinc 1 By similarity
Metal binding1451Zinc 1 By similarity
Metal binding1451Zinc 2 By similarity
Metal binding1791Zinc 2 By similarity
Metal binding1821Zinc 3 By similarity
Metal binding2141Zinc 2 By similarity
Metal binding2271Zinc 3 By similarity
Metal binding2291Zinc 3 By similarity
Metal binding2591Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A7Z6S8 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: C8A3FC59BE4E4DEE

FASTA29732,792
        10         20         30         40         50         60 
MLKIGSHVSM SGKHMLLAAS KEAVSYGANT FMIYTGAPQN TRRKKIEDLN IEAGRAHMKE 

        70         80         90        100        110        120 
NGIDEIVVHA PYIINIGNTT NPATFELGVD FLRSEIERTA AIGARQIVLH PGAHVGAGAE 

       130        140        150        160        170        180 
TGIKKIIEGL NEVIVPGQNV QIALETMAGK GSECGRSFEE LAEIIAGVTH NEHLSVCFDT 

       190        200        210        220        230        240 
CHTHDAGYDV ANDFDGVLNE FDKIVGIDRI KVLHVNDSKN IKGARKDRHE NIGFGEIGFD 

       250        260        270        280        290 
ALQYIVHHEQ LADIPKILET PYVGEDKKNK KPPYRFEIEM LKEKQFDKEL LEKISAQ 

« Hide

References

[1]"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42."
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.
Nat. Biotechnol. 25:1007-1014(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 23117 / BGSC 10A6 / FZB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000560 Genomic DNA. Translation: ABS74704.1.
RefSeqYP_001421935.1. NC_009725.1.

3D structure databases

ProteinModelPortalA7Z6S8.
SMRA7Z6S8. Positions 2-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326423.RBAM_023440.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS74704; ABS74704; RBAM_023440.
GeneID5461457.
KEGGbay:RBAM_023440.
PATRIC18749784. VBIBacAmy31356_2367.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0648.
HOGENOMHOG000224895.
KOK01151.
OMAINLGHPD.
OrthoDBEOG6Z0QCM.
ProtClustDBPRK01060.

Enzyme and pathway databases

BioCycBAMY326423:GCM4-2342-MONOMER.

Family and domain databases

Gene3D3.20.20.150. 1 hit.
HAMAPMF_00152. Nfo.
InterProIPR001719. AP_endonuc_2.
IPR018246. AP_endonuc_F2_Zn_BS.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PANTHERPTHR21445. PTHR21445. 1 hit.
PfamPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
SMARTSM00518. AP2Ec. 1 hit.
[Graphical view]
SUPFAMSSF51658. SSF51658. 1 hit.
TIGRFAMsTIGR00587. nfo. 1 hit.
PROSITEPS00729. 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]
ProtoNetSearch...

Entry information

Entry nameEND4_BACA2
AccessionPrimary (citable) accession number: A7Z6S8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: April 16, 2014
This is version 47 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