Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endonuclease V

Gene

nfi

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.UniRule annotation

Catalytic activityi

Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate.UniRule annotation

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi46MagnesiumUniRule annotation1
Metal bindingi116MagnesiumUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU36170-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Endonuclease VUniRule annotation (EC:3.1.21.7UniRule annotation)
Alternative name(s):
Deoxyinosine 3'endonucleaseUniRule annotation
Deoxyribonuclease VUniRule annotation
Short name:
DNase VUniRule annotation
Gene namesi
Name:nfiUniRule annotation
Synonyms:ywqL
Ordered Locus Names:BSU36170
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001596581 – 238Endonuclease VAdd BLAST238

Proteomic databases

PaxDbiP96724.
PRIDEiP96724.

Interactioni

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei86Interaction with target DNAUniRule annotation1

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019556.

Structurei

Secondary structure

1238
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 25Combined sources12
Helixi36 – 38Combined sources3
Beta strandi40 – 52Combined sources13
Beta strandi55 – 66Combined sources12
Turni67 – 69Combined sources3
Beta strandi72 – 81Combined sources10
Beta strandi86 – 89Combined sources4
Helixi91 – 94Combined sources4
Helixi96 – 105Combined sources10
Beta strandi113 – 117Combined sources5
Beta strandi119 – 122Combined sources4
Helixi128 – 136Combined sources9
Beta strandi140 – 146Combined sources7
Beta strandi165 – 170Combined sources6
Beta strandi173 – 179Combined sources7
Beta strandi188 – 196Combined sources9
Helixi198 – 207Combined sources10
Helixi217 – 235Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GA2X-ray2.10A1-238[»]
ProteinModelPortaliP96724.
SMRiP96724.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP96724.

Family & Domainsi

Sequence similaritiesi

Belongs to the endonuclease V family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105Y7X. Bacteria.
COG1515. LUCA.
HOGENOMiHOG000229135.
InParanoidiP96724.
KOiK05982.
OMAiDLAYWEQ.
PhylomeDBiP96724.

Family and domain databases

CDDicd06559. Endonuclease_V. 1 hit.
HAMAPiMF_00801. Endonuclease_5. 1 hit.
InterProiIPR007581. Endonuclease-V.
[Graphical view]
PfamiPF04493. Endonuclease_5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P96724-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVFDVHKFD MKKEQDFLQV QFNLKNRINL SPTIHPDSIN TCAGVDLAYW
60 70 80 90 100
EQDGEPYGVC CIIVIDADTK EVIEKVHSMG RISVPYVSGF LAFRELPLII
110 120 130 140 150
EAAKKLETEP DVFLFDGNGY LHYNHMGVAT HAAFFLGKPT IGIAKTYLKI
160 170 180 190 200
KGCDFVTPEI EVGAYTDIII DGEVYGRALR TRRDVKPIFL SCGNYIDLDS
210 220 230
SYQITMSLIN QESRLPIPVR LADLETHVLR TFYQKNHV
Length:238
Mass (Da):27,023
Last modified:July 28, 2009 - v2
Checksum:i87A59F090CF0047F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti42C → G in CAB07450 (PubMed:9353933).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z92952 Genomic DNA. Translation: CAB07450.1.
AL009126 Genomic DNA. Translation: CAB15634.2.
PIRiG70067.
RefSeqiNP_391498.2. NC_000964.3.
WP_003243213.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15634; CAB15634; BSU36170.
GeneIDi936894.
KEGGibsu:BSU36170.
PATRICi18979252. VBIBacSub10457_3788.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z92952 Genomic DNA. Translation: CAB07450.1.
AL009126 Genomic DNA. Translation: CAB15634.2.
PIRiG70067.
RefSeqiNP_391498.2. NC_000964.3.
WP_003243213.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GA2X-ray2.10A1-238[»]
ProteinModelPortaliP96724.
SMRiP96724.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019556.

Proteomic databases

PaxDbiP96724.
PRIDEiP96724.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15634; CAB15634; BSU36170.
GeneIDi936894.
KEGGibsu:BSU36170.
PATRICi18979252. VBIBacSub10457_3788.

Phylogenomic databases

eggNOGiENOG4105Y7X. Bacteria.
COG1515. LUCA.
HOGENOMiHOG000229135.
InParanoidiP96724.
KOiK05982.
OMAiDLAYWEQ.
PhylomeDBiP96724.

Enzyme and pathway databases

BioCyciBSUB:BSU36170-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP96724.

Family and domain databases

CDDicd06559. Endonuclease_V. 1 hit.
HAMAPiMF_00801. Endonuclease_5. 1 hit.
InterProiIPR007581. Endonuclease-V.
[Graphical view]
PfamiPF04493. Endonuclease_5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNFI_BACSU
AccessioniPrimary (citable) accession number: P96724
Secondary accession number(s): Q795B8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: July 28, 2009
Last modified: November 2, 2016
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.