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A5EPJ2 (DNLJ_BRASB) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 37. 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:BBta_6162
OrganismBradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) [Complete proteome] [HAMAP]
Taxonomic identifier288000 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length716 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 MF_01588

Catalytic activity

NAD+ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide + (deoxyribonucleotide)(n+m). HAMAP MF_01588

Cofactor

Magnesium or manganese By similarity. HAMAP 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

   Cellular componentintracellular

Inferred from electronic annotation. Source: InterPro

   Molecular functionDNA ligase (NAD+) activity

Inferred from electronic annotation. Source: EC

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 – 716716DNA ligase HAMAP MF_01588
PRO_0000313150

Regions

Domain638 – 71679BRCT
Nucleotide binding49 – 535NAD By similarity
Nucleotide binding98 – 992NAD By similarity

Sites

Active site1331N6-AMP-lysine intermediate By similarity
Metal binding4371Zinc By similarity
Metal binding4391Zinc By similarity
Metal binding4611Zinc By similarity
Metal binding4671Zinc By similarity
Binding site1311NAD By similarity
Binding site1541NAD By similarity
Binding site1911NAD By similarity
Binding site3081NAD By similarity
Binding site3321NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A5EPJ2 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: DEF4A224F317F330

FASTA71679,657
        10         20         30         40         50         60 
MPKTAKPKKP VDVAELTKAQ AKVEWKRLAL ELEVHDRLYY QDDAPKISDA EYDELRRRFN 

        70         80         90        100        110        120 
AIETRFPELV SSESPSQKVG ASPSGRFKKV RHAVPMLSLD NAFAEEDVRD FVGRIARFLK 

       130        140        150        160        170        180 
LADDRIDFSA EPKIDGLSMS LRYEGGELVT AATRGDGAEG EDVTANIRTL KDVPQKLHGR 

       190        200        210        220        230        240 
NWPDVCEVRG EVYMTKQAFL ALNERQKEAG DTIFANPRNS AAGSLRQKDP AITASRPLGF 

       250        260        270        280        290        300 
FAYAWGEISG TPPAETQTGM IKWFEQCGFT TNPLTRLCHS VEELIAFHRS IEEQRAELDY 

       310        320        330        340        350        360 
DIDGVVYKVD RIDWQERLGF VSRTPRWAIA HKFPAERAMT VLKDIEIQVG RTGSLTPVGK 

       370        380        390        400        410        420 
LEPVGVGGVI VQNVTLHNED YIKGIGNKGE VLREGRDIRI GDTVVIQRAG DVIPQVVDVV 

       430        440        450        460        470        480 
IDKRPAQARP FHLPKTCPCP LHTDVVREET ATGEEGSRAR CTGEFACPYQ KIEHLKLFAS 

       490        500        510        520        530        540 
RRAFDIDGLG EKQIAFFFEQ GWVKEPADIF TLQKRNAGLK LEEIEGYGET SVRNLFNAID 

       550        560        570        580        590        600 
ARREIALERF IYALGMRHVG ETTALALARG YGSWDAFHEA CLKVAAGDEE AIAEMDALDQ 

       610        620        630        640        650        660 
IGDTVIKSVA AYFAEDHNRG IVERLTQEVK ILDAEKPKRH SPIATKTVVF TGTLEKMTRD 

       670        680        690        700        710 
EAKATAERLG AKVSGSVSKK TDYVVAGPGA GSKLKEAQKH GVQVLTEDEW LQLIAE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000494 Genomic DNA. Translation: ABQ38086.1.
RefSeqYP_001241992.1. NC_009485.1.

3D structure databases

ProteinModelPortalA5EPJ2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5EPJ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5155320.
GenomeReviewsGene locus BBta_6162 in contig CP000494_GR.
KEGGbbt:BBta_6162.
PATRIC21213003. VBIBraSp29847_6156.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMATQKVGAT.
ProtClustDBCLSK2516592.

Family and domain databases

HAMAPMF_01588. DNA_ligase_A.
[Tree]
InterProIPR001357. BRCT.
IPR018239. DNA_ligase_AS.
IPR004150. DNA_ligase_OB.
IPR001679. DNAligase.
IPR013839. DNAligase_adenylation.
IPR013840. DNAligase_N.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR010994. RuvA_2-like.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01972.
PfamPF00533. BRCT. 1 hit.
PF01653. DNA_ligase_aden. 1 hit.
PF03120. DNA_ligase_OB. 1 hit.
[Graphical view]
PIRSFPIRSF001604. LigA. 1 hit.
SMARTSM00292. BRCT. 1 hit.
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...

Entry information

Entry nameDNLJ_BRASB
AccessionPrimary (citable) accession number: A5EPJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: December 14, 2011
This is version 37 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