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Q837V6 (DNLJ_ENTFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. 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=6.5.1.2
Alternative name(s):
Polydeoxyribonucleotide synthase [NAD(+)]
Gene names
Name:ligA
Ordered Locus Names:EF_0722
OrganismEnterococcus faecalis (strain ATCC 700802 / V583) [Reference proteome] [HAMAP]
Taxonomic identifier226185 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

Protein attributes

Sequence length676 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA By similarity. HAMAP-Rule MF_01588

Catalytic activity

NAD+ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D-ribonucleotide + (deoxyribonucleotide)(n+m). HAMAP-Rule MF_01588

Cofactor

Magnesium or manganese By similarity. HAMAP-Rule MF_01588

Sequence similarities

Belongs to the NAD-dependent DNA ligase family. LigA subfamily.

Contains 1 BRCT domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 676676DNA ligase HAMAP-Rule MF_01588
PRO_0000313228

Regions

Domain595 – 67682BRCT
Nucleotide binding39 – 435NAD HAMAP-Rule MF_01588
Nucleotide binding88 – 914NAD HAMAP-Rule MF_01588

Sites

Active site1201N6-AMP-lysine intermediate
Metal binding4091Zinc By similarity
Metal binding4121Zinc By similarity
Metal binding4271Zinc By similarity
Metal binding4321Zinc By similarity
Binding site1181NAD
Binding site1411NAD
Binding site1751NAD
Binding site2911NAD
Binding site3151NAD

Secondary structure

.................................................. 676
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q837V6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 9B6B93FD8DBB8E3B

FASTA67675,584
        10         20         30         40         50         60 
MEQQPLTLTA ATTRAQELRK QLNQYSHEYY VKDQPSVEDY VYDRLYKELV DIETEFPDLI 

        70         80         90        100        110        120 
TPDSPTQRVG GKVLSGFEKA PHDIPMYSLN DGFSKEDIFA FDERVRKAIG KPVAYCCELK 

       130        140        150        160        170        180 
IDGLAISLRY ENGVFVRGAT RGDGTVGENI TENLRTVRSV PMRLTEPISV EVRGECYMPK 

       190        200        210        220        230        240 
QSFVALNEER EENGQDIFAN PRNAAAGSLR QLDTKIVAKR NLNTFLYTVA DFGPMKAKTQ 

       250        260        270        280        290        300 
FEALEELSAI GFRTNPERQL CQSIDEVWAY IEEYHEKRST LPYEIDGIVI KVNEFALQDE 

       310        320        330        340        350        360 
LGFTVKAPRW AIAYKFPPEE AETVVEDIEW TIGRTGVVTP TAVMAPVRVA GTTVSRASLH 

       370        380        390        400        410        420 
NADFIQMKDI RLNDHVIIYK AGDIIPEVAQ VLVEKRAADS QPYEMPTHCP ICHSELVHLD 

       430        440        450        460        470        480 
EEVALRCINP KCPAQIKEGL NHFVSRNAMN IDGLGPRVLA QMYDKGLVKD VADLYFLTEE 

       490        500        510        520        530        540 
QLMTLDKIKE KSANNIYTAI QGSKENSVER LIFGLGIRHV GAKAAKILAE HFGDLPTLSR 

       550        560        570        580        590        600 
ATAEEIVALD SIGETIADSV VTYFENEEVH ELMAELEKAQ VNLTYKGLRT EQLAEVESPF 

       610        620        630        640        650        660 
KDKTVVLTGK LAQYTREEAK EKIENLGGKV TGSVSKKTDI VVAGEDAGSK LTKAESLGVT 

       670 
VWNEQEMVDA LDASHF 

« Hide

References

« Hide 'large scale' references
[1]"Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis."
Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin S.A. expand/collapse author list , Kolonay J.F., Madupu R., Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.
Science 299:2071-2074(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700802 / V583.
[2]"Structural rearrangement accompanying NAD+ synthesis within a bacterial DNA ligase crystal."
Gajiwala K.S., Pinko C.
Structure 12:1449-1459(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-325 IN COMPLEXES WITH NAD AND NICOTINAMIDE NUCLEOTIDE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016830 Genomic DNA. Translation: AAO80542.1.
RefSeqNP_814472.1. NC_004668.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TA8X-ray1.80A1-325[»]
1TAEX-ray2.70A/B/C/D1-324[»]
3BA8X-ray1.90A1-324[»]
3BA9X-ray1.90A1-324[»]
3BAAX-ray1.90A1-324[»]
3BABX-ray2.50A1-324[»]
4EEQX-ray2.10A1-323[»]
4EFBX-ray2.20A1-323[»]
4EFEX-ray2.00A1-323[»]
4LH6X-ray1.65A1-323[»]
4LH7X-ray1.90A1-323[»]
DisProtDP00326.
ProteinModelPortalQ837V6.
SMRQ837V6. Positions 4-324.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226185.EF0722.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO80542; AAO80542; EF_0722.
GeneID1199621.
KEGGefa:EF0722.
PATRIC21851834. VBIEntFae7065_0667.

Phylogenomic databases

eggNOGCOG0272.
KOK01972.
OMAFTAKSPR.
OrthoDBEOG6TTVM9.

Enzyme and pathway databases

BioCycEFAE226185:GHI1-709-MONOMER.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.40.50.10190. 1 hit.
HAMAPMF_01588. DNA_ligase_A.
InterProIPR001357. BRCT_dom.
IPR018239. DNA_ligase_AS.
IPR004150. DNA_ligase_OB.
IPR001679. DNAligase.
IPR013839. DNAligase_adenylation.
IPR013840. DNAligase_N.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR012340. NA-bd_OB-fold.
IPR010994. RuvA_2-like.
IPR004149. Znf_DNAligase_C4.
[Graphical view]
PfamPF00533. BRCT. 1 hit.
PF01653. DNA_ligase_aden. 1 hit.
PF03120. DNA_ligase_OB. 1 hit.
PF03119. DNA_ligase_ZBD. 1 hit.
[Graphical view]
PIRSFPIRSF001604. LigA. 1 hit.
SMARTSM00292. BRCT. 1 hit.
SM00278. HhH1. 3 hits.
SM00532. LIGANc. 1 hit.
[Graphical view]
SUPFAMSSF47781. SSF47781. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF52113. SSF52113. 1 hit.
TIGRFAMsTIGR00575. dnlj. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS01055. DNA_LIGASE_N1. 1 hit.
PS01056. DNA_LIGASE_N2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ837V6.

Entry information

Entry nameDNLJ_ENTFA
AccessionPrimary (citable) accession number: Q837V6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 86 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references