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Q1LU20 (DNLJ_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:BCI_0066
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length671 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 – 671671DNA ligase HAMAP MF_01588
PRO_0000313137

Regions

Domain592 – 67180BRCT
Nucleotide binding32 – 365NAD By similarity
Nucleotide binding81 – 822NAD By similarity

Sites

Active site1161N6-AMP-lysine intermediate By similarity
Metal binding4101Zinc By similarity
Metal binding4131Zinc By similarity
Metal binding4281Zinc By similarity
Metal binding4341Zinc By similarity
Binding site1141NAD By similarity
Binding site1371NAD By similarity
Binding site1751NAD By similarity
Binding site2921NAD By similarity
Binding site3161NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LU20 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 49FF168A2406494F

FASTA67176,271
        10         20         30         40         50         60 
MKQIEQYIEQ LRQQLRYWNF LYYAKDAPEV SDVEYDWLMM KLRELERQWP DLKTADSPTQ 

        70         80         90        100        110        120 
HIGYKAQSKF RKVIHEVPML SLDHIFNDTS FLAFDRRIRN RLQYGNNYLT YCCELKFDGI 

       130        140        150        160        170        180 
AVSLLYKHGK LIRAATRGDG HIGEDVTDNI RTICSIPLQL KDDGHIPRLI EIRGEVIMSE 

       190        200        210        220        230        240 
DAFRHLNETA KKNKSKRFAN PRNAAAGSLR QVDPSITATR LLSFFCYGVG RIDSKKIPAA 

       250        260        270        280        290        300 
HLELLQQFKI WGLPVSNYRR YCVGHQEVLD FYSYVSKVRS KLGFNIDGIV IKVNALVQQQ 

       310        320        330        340        350        360 
QLGFVARAPR WAIAYKLPAN EQLTEIQNID FQVGRTGIIT PVARLKPVYI SGAYISNASL 

       370        380        390        400        410        420 
HSFAEIKRLG LRIGDTVVIR LAGNIIPQIV NVVVSKRSIK TSPVLYPLYC PVCGSKVKQN 

       430        440        450        460        470        480 
NKEKTIICTA GMICSAQLKE ALKHFVSRRA MNIYGMGGKI IDQLVDLKII QNPVDLFRLN 

       490        500        510        520        530        540 
QDQLTCLKNM GQKKTKKLLD AIEYAKKTTF ARFLYAIGIR EIGETKAAYL ADYYKHIDAL 

       550        560        570        580        590        600 
MAADIESLTK IQDIGIIVAT NVLNFFHNKH NIAIIEELCS PKIGIKFLST LEKNNYFSGK 

       610        620        630        640        650        660 
NIVFTGTLAF LSREEAIDML IALGARIRSS VSSKIDLLIA GKNTGFKLTK AKQLQIKIIE 

       670 
EAEFYQILGI R

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000238 Genomic DNA. Translation: ABF14158.1.
RefSeqYP_588544.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LU20.
SMRQ1LU20. Positions 1-588.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LU20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4056211.
GenomeReviewsGene locus BCI_0066 in contig CP000238_GR.
KEGGbci:BCI_0066.
PATRIC21073621. VBIBauCic75062_0067.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBQ1LU20.

Enzyme and pathway databases

BioCycBCIC186490:BCI_0066-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_BAUCH
AccessionPrimary (citable) accession number: Q1LU20
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 44 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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