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C0QJ86 (DNLJ_DESAH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 40. 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:
DNA ligase

EC=6.5.1.2
Alternative name(s):
Polydeoxyribonucleotide synthase [NAD(+)]
Gene names
Name:ligA
Ordered Locus Names:HRM2_28100
OrganismDesulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2) [Complete proteome] [HAMAP]
Taxonomic identifier177437 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfobacterium

Protein attributes

Sequence length685 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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

Keywords
   Biological processDNA damage
DNA repair
DNA replication
   LigandMagnesium
Manganese
Metal-binding
NAD
Zinc
   Molecular functionLigase
   Technical termComplete proteome
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: UniProtKB-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 – 685685DNA ligase HAMAP-Rule MF_01588
PRO_0000380361

Regions

Domain606 – 68580BRCT
Nucleotide binding39 – 435NAD By similarity
Nucleotide binding88 – 892NAD By similarity

Sites

Active site1211N6-AMP-lysine intermediate By similarity
Metal binding4201Zinc By similarity
Metal binding4231Zinc By similarity
Metal binding4381Zinc By similarity
Metal binding4431Zinc By similarity
Binding site1191NAD By similarity
Binding site1421NAD By similarity
Binding site1821NAD By similarity
Binding site3021NAD By similarity
Binding site3261NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
C0QJ86 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 3B0C000032505C3C

FASTA68575,284
        10         20         30         40         50         60 
MIDPSSSFDR IKKEARLLRE QLHVHNINYH VKDDPVISDG EYDRMMQRLI AIETQFPELS 

        70         80         90        100        110        120 
TPDSPTRRIG AKALTAFETA EHAIPMQSLD NAFSDQDVID FHNRTAKILN TSDIRYTVEP 

       130        140        150        160        170        180 
KLDGVAVELR YEQGSLTLAL TRGDGTMGEV ITDNARTIPS VPLKLAPAGN GTIPDVLEVR 

       190        200        210        220        230        240 
GEVIINSKDF EGLNKKRLAT GEPLFANPRN AAAGSLRQLD SRVTAKRPLE IFVYGVGRAQ 

       250        260        270        280        290        300 
ELMANFDIGS HSALLESLKR LGFRINPLIR SGLSLTEVLD RFKAFETMRQ DLDYEIDGMV 

       310        320        330        340        350        360 
IKVDDIVFQE RLGTKARSPR WAIAYKFPAM EETTVINDII VQVGRTGTLT PVAILEPVNI 

       370        380        390        400        410        420 
GGVMVARASL HNQDEIQNKD IRINDTVLVK RAGDVIPKVV KPVTALRTGS ERVFVMPTHC 

       430        440        450        460        470        480 
PVCHSPVRRL DNEAAVKCIN ASCKAQLKQR LKHFVSKGGF DMEGLGTKLI DQLVDRTLVG 

       490        500        510        520        530        540 
SFADLFTLDR ETLAAMDRMG EKSATNIVQA IERSKRIPLK RFLFALGMAH TGESAAQLLS 

       550        560        570        580        590        600 
STFFTLEALL KASAEALGAI EGVGPKTADS VVAFFANPDN QETIARMMEN GVVIENHTVV 

       610        620        630        640        650        660 
ESAALDNATF FSEKRVVLTG TLGTLTRSEA KQRLEEQGAR VVSSVSKNTD ILVAGEASGS 

       670        680 
KLVKARSLGV TIMDEQTFLE HLDRG 

« Hide

References

[1]"Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate reducer oxidizing organic carbon completely to carbon dioxide."
Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S., Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A., Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O., Meyerdierks A., Gottschalk G., Amann R.
Environ. Microbiol. 11:1038-1055(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43914 / DSM 3382 / HRM2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001087 Genomic DNA. Translation: ACN15899.1.
RefSeqYP_002604063.1. NC_012108.1.

3D structure databases

ProteinModelPortalC0QJ86.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING177437.HRM2_28100.

Proteomic databases

PRIDEC0QJ86.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACN15899; ACN15899; HRM2_28100.
GeneID7501340.
KEGGdat:HRM2_28100.
PATRIC21685323. VBIDesAut25181_2920.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHOG000218459.
KOK01972.
OMAFTAKSPR.
OrthoDBEOG6TTVM9.

Enzyme and pathway databases

BioCycDAUT177437:GHLR-2809-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. 2 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.
PS01056. DNA_LIGASE_N2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDNLJ_DESAH
AccessionPrimary (citable) accession number: C0QJ86
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 40 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