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A9IW95 (DNLJ_BART1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:BT_1581
OrganismBartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]
Taxonomic identifier382640 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length719 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 – 719719DNA ligase HAMAP MF_01588
PRO_0000340329

Regions

Domain638 – 71982BRCT
Nucleotide binding42 – 465NAD By similarity
Nucleotide binding91 – 922NAD By similarity

Sites

Active site1271N6-AMP-lysine intermediate By similarity
Metal binding4291Zinc By similarity
Metal binding4321Zinc By similarity
Metal binding4471Zinc By similarity
Metal binding4531Zinc By similarity
Binding site1251NAD By similarity
Binding site1481NAD By similarity
Binding site1841NAD By similarity
Binding site3001NAD By similarity
Binding site3241NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A9IW95 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 40BE850BB0DC6D70

FASTA71980,428
        10         20         30         40         50         60 
MNKDGIKNLT VVEAERELEW LAKEIARHDV LYNRDDQPEI SDAEYDALRR RNAEIEALFP 

        70         80         90        100        110        120 
ELIRVDSPSH KIGAAISEKF EKSVHAQPML SLDNAFSAED VYEFVERIRR FLRLPETQVL 

       130        140        150        160        170        180 
EITAEPKIDG LSLSLRYEKG RLVRAATRGD GTVGENVTAN ARTIADIPQV LQGDFPDVIE 

       190        200        210        220        230        240 
VRGEVYMGRE DFQALNISQQ EKGKLTFANP RNAAAGSLRQ LDSRITASRK LQFFAYACGE 

       250        260        270        280        290        300 
VSEIFAESQM EMMTKLKEYG FVINPLTKVF KTVEDIISYY RDIEERRYSL NYDIDGIVYK 

       310        320        330        340        350        360 
VNDLMLQKRL GFVSRSPRWA IAHKFPAEKA MALLEDIDIQ VGRTGALTPV ARLTPITIGG 

       370        380        390        400        410        420 
VVVTNASLHN EDYIKGIGHK GEPIREGRDI RIGDTVIIQR AGDVIPQVVD IVLEKRQKDS 

       430        440        450        460        470        480 
SAFVFPDLCP ACGSHAVREV GEAVRRCTGG LICPAQAIER IRHFVARNAF DIEGLGKKQV 

       490        500        510        520        530        540 
EFFFHAQDEA LCIHTPADIF TLERRQEKSL IRLENIEGFG TVSVRKLYDA INARREIPLS 

       550        560        570        580        590        600 
RFLFALGIRH VGEVNARRLA RAYQTYTAFE TAAMEALMPC KQDNKEGNEA WMELTNIEGI 

       610        620        630        640        650        660 
GPQVGSAIVD FYQEAHNREV LAVLLEEITP LDEVPIMTAS SPIAEKIIVF TGTLAHMSRD 

       670        680        690        700        710 
EAKALAERLG AKTSGSLSKK TDLLVAGPGA GSKLTKAQEF GVQVIDEEAW MRLIKGHNI

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References

[1]"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed: 18037886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIP 105476 / IBS 506.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM260525 Genomic DNA. Translation: CAK01920.1.
RefSeqYP_001609915.1. NC_010161.1.

3D structure databases

ProteinModelPortalA9IW95.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9IW95.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5829496.
GenomeReviewsGene locus BT_1581 in contig AM260525_GR.
PATRIC20550988. VBIBarTri113218_1630.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycBTRI382640:BT_1581-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.
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. 1 hit.
PS01056. DNA_LIGASE_N2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDNLJ_BART1
AccessionPrimary (citable) accession number: A9IW95
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 31 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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