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P00969 (DNLI_BPT7) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
DNA ligase

EC=6.5.1.1
Alternative name(s):
DNA ligase gp1.3
Gene product 1.3
Short name=Gp1.3
Gene names
Ordered Locus Names:1.3
OrganismEnterobacteria phage T7 (Bacteriophage T7) [Reference proteome]
Taxonomic identifier10760 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7likevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair in an ATP-dependent reaction. Binds specifically to DNA nicks containing a 3'-OH and a 5'-phosphate group. Ref.5

Catalytic activity

ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m). Ref.6

Cofactor

Divalent metal cations By similarity.

Sequence similarities

Belongs to the ATP-dependent DNA ligase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359DNA ligase
PRO_0000059598

Regions

Nucleotide binding32 – 354ATP
Nucleotide binding55 – 573ATP

Sites

Active site341N6-AMP-lysine intermediate By similarity
Metal binding2171Divalent metal cation By similarity
Binding site391ATP
Binding site931ATP
Binding site2321ATP
Binding site2381ATP Probable

Experimental info

Mutagenesis2381K → A: Complete loss of transadenylation activity. Ref.5
Mutagenesis2401K → A: About 99% loss of transadenylation activity. Ref.5

Secondary structure

......................................................... 359
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00969 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 43DA453B71BDF8DC

FASTA35941,133
        10         20         30         40         50         60 
MMNIKTNPFK AVSFVESAIK KALDNAGYLI AEIKYDGVRG NICVDNTANS YWLSRVSKTI 

        70         80         90        100        110        120 
PALEHLNGFD VRWKRLLNDD RCFYKDGFML DGELMVKGVD FNTGSGLLRT KWTDTKNQEF 

       130        140        150        160        170        180 
HEELFVEPIR KKDKVPFKLH TGHLHIKLYA ILPLHIVESG EDCDVMTLLM QEHVKNMLPL 

       190        200        210        220        230        240 
LQEYFPEIEW QAAESYEVYD MVELQQLYEQ KRAEGHEGLI VKDPMCIYKR GKKSGWWKMK 

       250        260        270        280        290        300 
PENEADGIIQ GLVWGTKGLA NEGKVIGFEV LLESGRLVNA TNISRALMDE FTETVKEATL 

       310        320        330        340        350 
SQWGFFSPYG IGDNDACTIN PYDGWACQIS YMEETPDGSL RHPSFVMFRG TEDNPQEKM 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements."
Dunn J.J., Studier F.W.
J. Mol. Biol. 166:477-535(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to the beginning of gene 4."
Dunn J.J., Studier F.W.
J. Mol. Biol. 148:303-330(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcription termination site at the end of the early region of bacteriophage T7 DNA."
Dunn J.J., Studier F.W.
Nucleic Acids Res. 8:2119-2132(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-359.
[4]"Nucleotide sequence of the primary origin of bacteriophage T7 DNA replication: relationship to adjacent genes and regulatory elements."
Saito H., Tabor S., Tamanoi F., Richardson C.C.
Proc. Natl. Acad. Sci. U.S.A. 77:3917-3921(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
[5]"Nick recognition by DNA ligases."
Doherty A.J., Dafforn T.R.
J. Mol. Biol. 296:43-56(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-238 AND LYS-240.
[6]"Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7."
Subramanya H.S., Doherty A.J., Ashford S.R., Wigley D.B.
Cell 85:607-615(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ATP, CATALYTIC ACTIVITY, DNA-BINDING.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01124 Genomic DNA. Translation: CAA24322.1.
V01126 Genomic DNA. Translation: CAA24326.1.
V01127 Genomic DNA. Translation: CAA24336.1.
V01146 Genomic DNA. Translation: CAA24393.1.
PIRLQBP37. E94615.
RefSeqNP_041963.1. NC_001604.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0IX-ray2.60A3-349[»]
ProteinModelPortalP00969.
SMRP00969. Positions 2-349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1513817.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1261055.

Phylogenomic databases

ProtClustDBPHA0454.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
InterProIPR012310. DNA_ligase_ATP-dep_cent.
IPR016059. DNA_ligase_ATP-dep_CS.
IPR016306. DNA_ligase_ATP-dep_T3.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamPF01068. DNA_ligase_A_M. 1 hit.
[Graphical view]
PIRSFPIRSF001600. DNA_ligase_phage_T3. 1 hit.
SUPFAMSSF50249. SSF50249. 1 hit.
PROSITEPS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00969.

Entry information

Entry nameDNLI_BPT7
AccessionPrimary (citable) accession number: P00969
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references