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Q87SC6 (END4_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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:VP0498
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length295 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 – 295295Probable endonuclease 4 HAMAP-Rule MF_00152
PRO_0000190885

Sites

Metal binding781Zinc 1 By similarity
Metal binding1181Zinc 1 By similarity
Metal binding1541Zinc 1 By similarity
Metal binding1541Zinc 2 By similarity
Metal binding1881Zinc 2 By similarity
Metal binding1911Zinc 3 By similarity
Metal binding2251Zinc 2 By similarity
Metal binding2381Zinc 3 By similarity
Metal binding2401Zinc 3 By similarity
Metal binding2701Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87SC6 [UniParc].

Last modified May 23, 2003. Version 1.
Checksum: 784D0378858E3E0C

FASTA29533,017
        10         20         30         40         50         60 
MTNMKNKFGN KLIGAHVSAA GGVDQAPLRA REIGANAFAL FTKNQRQWVA KPLEAKTISA 

        70         80         90        100        110        120 
FKANCKMLGF GAEHILPHDS YLINLGAPEA EKLDKSRAAF IDEMERCNQL GLTLLNFHPG 

       130        140        150        160        170        180 
SHLKKVSEQE CLATIAESIN LAHKTVPDVV AVIENTAGQG TNLGWKFEHL AEIIEQVEDK 

       190        200        210        220        230        240 
DRVGVCIDTC HTFTAGYDLR TKEDCERTFA EFDRIVGMHY LRAMHLNDSK VEFASKVDRH 

       250        260        270        280        290 
HSLGKGEIGW DCFEYIAKDS RFDGIPLILE TIDPDIWQQE INTLRQFHLA AINNQ 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC58761.1.
RefSeqNP_796877.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87SC6.
SMRQ87SC6. Positions 11-285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP0498.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC58761; BAC58761; BAC58761.
GeneID1187966.
KEGGvpa:VP0498.
PATRIC20139202. VBIVibPar50997_0475.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0648.
HOGENOMHOG000224893.
KOK01151.
OMADEINWIN.
OrthoDBEOG6Z0QCM.

Enzyme and pathway databases

BioCycVPAR223926:GHK4-510-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_VIBPA
AccessionPrimary (citable) accession number: Q87SC6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: May 14, 2014
This is version 74 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