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A1W7N4 (DNLJ_ACISJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 38. 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:Ajs_2083
OrganismAcidovorax sp. (strain JS42) [Complete proteome] [HAMAP]
Taxonomic identifier232721 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length731 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 – 731731DNA ligase HAMAP MF_01588
PRO_0000313100

Regions

Domain645 – 73187BRCT
Nucleotide binding47 – 515NAD By similarity
Nucleotide binding96 – 972NAD By similarity

Sites

Active site1351N6-AMP-lysine intermediate By similarity
Metal binding4621Zinc By similarity
Metal binding4651Zinc By similarity
Metal binding4801Zinc By similarity
Metal binding4861Zinc By similarity
Binding site1331NAD By similarity
Binding site1561NAD By similarity
Binding site1921NAD By similarity
Binding site3131NAD By similarity
Binding site3371NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A1W7N4 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: BB799A0FC0E9466B

FASTA73178,461
        10         20         30         40         50         60 
MTEQSDLFPA PAPKGSALVA TKIKALREQL NRWAHEYYVQ DTPSVPDAEY DRAFQQLQAL 

        70         80         90        100        110        120 
EGAYPDLVTP DSPTQRVLGA VLDGLTPVRH RVPMLSIRTE TDTEASGAQA FDARVRRELK 

       130        140        150        160        170        180 
LPPDAPPVEY VAEPKFDGLA MSLRYEGGRL VQAATRGDGE VGEDVTHNVR TIRQIPLSLP 

       190        200        210        220        230        240 
AGVPPVLEVR GEVYMRRADF DALNERQREK GDKTFVNPRN AAAGAVRQLD SGITAQRPLS 

       250        260        270        280        290        300 
FFAYGLGEVT PAAEGGPDFG THFGMLQQLK EWGFPVAAQV QIAQGASELI AFHQRVGAER 

       310        320        330        340        350        360 
DALPYDIDGV VYKVNSLALQ RQLGFVTREP RWAVAHKYPA QEMVTRVEGI DVQVGRTGKL 

       370        380        390        400        410        420 
TPVARLAPVF VGGVTVTNAT LHNLFELRRK KVRVGDQVIV RRAGDVIPEV VGVVPAGAGL 

       430        440        450        460        470        480 
AVLAGSDALV DAASSADGTA PAQPLAGPRQ PYVPNFRMPR QCPICGSAVV REPGEVNHRC 

       490        500        510        520        530        540 
SGGLFCPAQR KQAVLHFAQR RAMDIEGLGE KLVDQLVDGH VIRTLPDLYR LGLSSLAQLD 

       550        560        570        580        590        600 
RMAEKSAQNV LDALDKSKRT TLARFLFGLG IRHVGEATAK DLARHFGQLD AIMDAGVEQL 

       610        620        630        640        650        660 
LQVNDVGPVV AEAIHTFFAQ PHNREVVEQL RACGVTWDES EPAAAATLPL AGMTVVLTGT 

       670        680        690        700        710        720 
LPTLGRDAAK DLLESAGAKV AGSVSKKTHY VVAGADAGSK LAKAQELGIP VLDEDGLHAL 

       730 
LRGTPPNAGG A

« Hide

References

[1]"Complete sequence of chromosome 1 of Acidovorax sp. JS42."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000539 Genomic DNA. Translation: ABM42259.1.
RefSeqYP_986335.1. NC_008782.1.

3D structure databases

ProteinModelPortalA1W7N4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1W7N4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4671145.
GenomeReviewsGene locus Ajs_2083 in contig CP000539_GR.
KEGGajs:Ajs_2083.
PATRIC20689500. VBIAciSp27161_2284.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBA1W7N4.
ProtClustDBCLSK951442.

Enzyme and pathway databases

BioCycASP232721:AJS_2083-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. 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_ACISJ
AccessionPrimary (citable) accession number: A1W7N4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 38 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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