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A6L5G8 (DNLJ_BACV8) 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
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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:BVU_3306
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]
Taxonomic identifier435590 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length665 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 binding

Inferred from electronic annotation. Source: InterPro

DNA 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 – 665665DNA ligase HAMAP MF_01588
PRO_0000313133

Regions

Domain587 – 66579BRCT
Nucleotide binding31 – 355NAD By similarity
Nucleotide binding80 – 812NAD By similarity

Sites

Active site1121N6-AMP-lysine intermediate By similarity
Metal binding4031Zinc By similarity
Metal binding4061Zinc By similarity
Metal binding4211Zinc By similarity
Metal binding4271Zinc By similarity
Binding site1101NAD By similarity
Binding site1331NAD By similarity
Binding site1701NAD By similarity
Binding site2851NAD By similarity
Binding site3091NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A6L5G8 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: EA68EB368601CE89

FASTA66575,172
        10         20         30         40         50         60 
MTEIERIDQL REELHRHNYN YYVLNAPEIT DQEFDKLMRE LQDLEEKHPE HRDENSPSMR 

        70         80         90        100        110        120 
VGSDINKNFT QVVHKYPMLS LANTYSETEV TEFYDRVKKS LNEDFEICCE MKYDGTSISL 

       130        140        150        160        170        180 
TYENGKLVRA VTRGDGVQGD DVTGNVKTIR SIPLVLHGKG YPETFEIRGE ILMPWVVFEE 

       190        200        210        220        230        240 
LNKEREAREE PLFANPRNAA SGTLKLQNSA IVASRKLDAY LYYLLGDNLP CDGHYENLKE 

       250        260        270        280        290        300 
AEKWGFKISD LTRKCKTLQE VFDFIKYWDV ERKNLPVATD GIVLKVNSLR QQRNLGFTAK 

       310        320        330        340        350        360 
SPRWAIAYKF QAEQALTRLN KVTYQVGRTG AVTPVANLDP IQLSGTVVKR ASLHNADIIE 

       370        380        390        400        410        420 
GLDLHIGDMV YVEKGGEIIP KIVGVDKDAR IMIGDKVKFI THCPECGSKL VRYEGEAAYY 

       430        440        450        460        470        480 
CTNDAACPPQ IKGKIEHFIS RRAMNIDGLG PETVDQFYQE GLIRDVADLY TLKTSDIINL 

       490        500        510        520        530        540 
ERMGEKSAEN IIKGIEQSKE VPFERVLFAL GIRFVGETVA KKVAKSFKSM DALADASLDN 

       550        560        570        580        590        600 
LIHVDEIGEK IAQSILLYFA NPKNRDIIER LRVAGVRLEA DEEDTSEHTD KLAGKSIVIS 

       610        620        630        640        650        660 
GVFAHHSRDE YKELIEKHGG KNVGSISSKT SFILAGDNMG PSKLEKAQKL GVTIVSEEEF 


LQMIE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000139 Genomic DNA. Translation: ABR40932.1.
RefSeqYP_001300554.1. NC_009614.1.

3D structure databases

ProteinModelPortalA6L5G8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6L5G8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5304267.
GenomeReviewsGene locus BVU_3306 in contig CP000139_GR.
KEGGbvu:BVU_3306.
NMPDRfig|435590.6.peg.3082.
PATRIC21071642. VBIBacVul85104_3402.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBCLSK2516787.

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.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR010994. RuvA_2-like.
IPR004149. Znf_DNAligase_C4.
[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.
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]
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. False negative.
PS01056. DNA_LIGASE_N2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDNLJ_BACV8
AccessionPrimary (citable) accession number: A6L5G8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 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

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