Skip Header

Contribute Send feedback
Read comments (?) or add your own

O87703 (DNLJ_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. 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
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
Synonyms:lig
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length670 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.

Sequence similarities

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

Contains 1 BRCT domain.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
DNA replication
   LigandMagnesium
Manganese
Metal-binding
NAD
Zinc
   Molecular functionLigase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

DNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA ligase (NAD+) activity

Inferred from electronic annotation. Source: HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 670670DNA ligase HAMAP-Rule MF_01588
PRO_0000161737

Regions

Domain589 – 67082BRCT
Nucleotide binding34 – 385NAD By similarity
Nucleotide binding83 – 842NAD By similarity

Sites

Active site1141N6-AMP-lysine intermediate
Metal binding4031Zinc By similarity
Metal binding4061Zinc By similarity
Metal binding4211Zinc By similarity
Metal binding4261Zinc By similarity
Binding site1121NAD By similarity
Binding site1351NAD By similarity
Binding site1691NAD By similarity
Binding site2851NAD By similarity
Binding site3091NAD By similarity

Secondary structure

1 ........................................... 670
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O87703 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: B52462314CF9ACF5

FASTA67074,231
        10         20         30         40         50         60 
MDRQQAERRA AELRELLNRY GYEYYVLDRP SVPDAEYDRL MQELIAIEEQ YPELKTSDSP 

        70         80         90        100        110        120 
TQRIGGPPLE AFRKVAHRVP MMSLANAFGE GDLRDFDRRV RQEVGEAAYV CELKIDGLAV 

       130        140        150        160        170        180 
SVRYEDGYFV QGATRGDGTT GEDITENLKT IRSLPLRLKE PVSLEARGEA FMPKASFLRL 

       190        200        210        220        230        240 
NEERKARGEE LFANPRNAAA GSLRQLDPKV AASRQLDLFV YGLADAEALG IASHSEALDY 

       250        260        270        280        290        300 
LQALGFKVNP ERRRCANIDE VIAFVSEWHD KRPQLPYEID GIVIKVDSFA QQRALGATAK 

       310        320        330        340        350        360 
SPRWAIAYKF PAEEVVTTLI GIEVNVGRTG VVTPTAILEP VRVAGTTVQR ATLHNEDFIR 

       370        380        390        400        410        420 
EKDIRIGDAV IIKKAGDIIP EVVGVVVDRR DGDETPFAMP THCPECESEL VRLEGEVALR 

       430        440        450        460        470        480 
CLNPNCPAQL RERLIHFASR AAMNIEGLGE KVVTQLFNAG LVRDVADLYC LTKEQLVGLE 

       490        500        510        520        530        540 
RMGEKSAANL LAAIEASKQN SLERLLFGLG IRYVGAKAAQ LLAEHFETME RLERATKEEL 

       550        560        570        580        590        600 
MAVPEIGEKM ADAITAFFAQ PEATELLQEL RAYGVNMAYK GPKRSAEAPA DSAFAGKTVV 

       610        620        630        640        650        660 
LTGKLASMSR NEAKEQIERL GGRVTGSVSR STDLVIAGED AGSKLEKAQQ LGIEIWDESR 

       670 
FLQEINRGKR

« Hide

References

[1]"Nucleotide sequence, heterologous expression and novel purification of DNA ligase from Bacillus stearothermophilus."
Brannigan J.A., Ashford S.R., Doherty A.J., Timson D.J., Wigley D.B.
Biochim. Biophys. Acta 1432:413-418(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
[2]"Structure of the adenylation domain of an NAD+-dependent DNA ligase."
Singleton M.R., Hakansson K., Timson D.J., Wigley D.B.
Structure 7:35-42(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-318.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ011676 Genomic DNA. Translation: CAA09732.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B04X-ray2.80A/B1-318[»]
ProteinModelPortalO87703.
SMRO87703. Positions 1-313.
ModBaseSearch...

Proteomic databases

PRIDEO87703.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.50.140. 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.
IPR000445. HhH_motif.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR012340. NA-bd_OB-fold.
IPR010994. RuvA_2-like.
IPR004149. Znf_DNAligase_C4.
[Graphical view]
PANTHERPTHR11107:SF5. PTHR11107:SF5. 1 hit.
PfamPF00533. BRCT. 1 hit.
PF01653. DNA_ligase_aden. 1 hit.
PF03120. DNA_ligase_OB. 1 hit.
PF03119. DNA_ligase_ZBD. 1 hit.
PF00633. HHH. 1 hit.
[Graphical view]
PIRSFPIRSF001604. LigA. 1 hit.
SMARTSM00292. BRCT. 1 hit.
SM00278. HhH1. 3 hits.
SM00532. LIGANc. 1 hit.
[Graphical view]
SUPFAMSSF52113. BRCT. 1 hit.
SSF50249. Nucleic_acid_OB. 1 hit.
SSF47781. RuvA_2_like. 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

EvolutionaryTraceO87703.

Entry information

Entry nameDNLJ_GEOSE
AccessionPrimary (citable) accession number: O87703
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: April 3, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents