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B0BQN6 (DNLJ_ACTPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. 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:APJL_1315
OrganismActinobacillus pleuropneumoniae serotype 3 (strain JL03) [Complete proteome] [HAMAP]
Taxonomic identifier434271 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length682 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 – 682682DNA ligase HAMAP MF_01588
PRO_0000340322

Regions

Domain603 – 68280BRCT
Nucleotide binding42 – 465NAD By similarity
Nucleotide binding91 – 922NAD By similarity

Sites

Active site1261N6-AMP-lysine intermediate By similarity
Metal binding4201Zinc By similarity
Metal binding4231Zinc By similarity
Metal binding4381Zinc By similarity
Metal binding4441Zinc By similarity
Binding site1241NAD By similarity
Binding site1471NAD By similarity
Binding site1841NAD By similarity
Binding site3021NAD By similarity
Binding site3261NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
B0BQN6 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: FB63414024FD3C13

FASTA68275,693
        10         20         30         40         50         60 
MPLLSQMQDQ SGTTFAQLEA LRQKLREYEY YYHVLDNPLV PDAEYDRLMN ELKNLEWQHP 

        70         80         90        100        110        120 
EWITADSPTQ RVGAKPLDGF AQVTHEIPML SLDNAFSDEE LDGFLRRMES YITEDPHTLA 

       130        140        150        160        170        180 
FCCEPKLDGL AVSILYVDGV LSQAATRGDG TTGEDITSNI RTVRNIPLKL NMDNPPARLE 

       190        200        210        220        230        240 
VRGEVFMPQK GFETLNERAL EKGEKTFANP RNAAAGSLRQ LDPKITRQRP LVLNAYGIGV 

       250        260        270        280        290        300 
YESDDELPAT HFERLQWLKS IGIPVNNEIR LATGREQLLA FYADIQAKRP TLGYDIDGTV 

       310        320        330        340        350        360 
LKVNDIGLQE QLGFISRSPR WAIAYKFPAQ EEMTVLNDVE FQVGRTGAIT PVAKLEPVFV 

       370        380        390        400        410        420 
AGVTVSNATL HNGDEIERLG IVIGDTVIIR RAGDVIPQIV GVVMERRPEN AKKIEFPTAC 

       430        440        450        460        470        480 
PVCESAVVRV EGEAVARCTG GLFCGAQRKE ALKHFVSRKA MDIDGVGEKL IEQLMERELV 

       490        500        510        520        530        540 
HTPADLFKLE HTTLMRLERM GGKSAQNALN SIEKAKNTTL ARFLFALGIR DVGEATAQNL 

       550        560        570        580        590        600 
ANHFHNLDAI RAATFEQLQE VQDVGEVVAN RIVRFWQEPH NVTVVEDLIS QGIHWQDVVQ 

       610        620        630        640        650        660 
VEIADNPLKG KSVVLTGTLT QLTRDQAKAL LQSFGCKVSG SVSSKTDYLI AGEKAGSKLA 

       670        680 
KAQELGVKVL TEQEFIALTG EN

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References

[1]"Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of serotype 3 prevalent in China."
Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W., Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T. expand/collapse author list , Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S., Zhao G.-P., Chen H.
PLoS ONE 3:E1450-E1450(2008) [PubMed: 18197260] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JL03.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000687 Genomic DNA. Translation: ABY69871.1.
RefSeqYP_001652315.1. NC_010278.1.

3D structure databases

ProteinModelPortalB0BQN6.
SMRB0BQN6. Positions 17-595.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0BQN6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5852592.
GenomeReviewsGene locus APJL_1315 in contig CP000687_GR.
KEGGapj:APJL_1315.
PATRIC20751886. VBIActPle136345_1308.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycAPLE434271:APJL_1315-MONOMER.

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. 4 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...

Entry information

Entry nameDNLJ_ACTPJ
AccessionPrimary (citable) accession number: B0BQN6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 32 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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