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Q65MR2 (DNLJ_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. 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:BLi00716, BL00589
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length667 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 – 667667DNA ligase HAMAP MF_01588
PRO_0000313127

Regions

Domain589 – 66779BRCT
Nucleotide binding34 – 385NAD By similarity
Nucleotide binding83 – 842NAD By similarity

Sites

Active site1141N6-AMP-lysine intermediate By similarity
Metal binding4031Zinc By similarity
Metal binding4061Zinc By similarity
Metal binding4211Zinc By similarity
Metal binding4261Zinc By similarity
Binding site1121NAD By similarity
Binding site1351NAD By similarity
Binding site1691NAD By similarity
Binding site2851NAD By similarity
Binding site3091NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65MR2 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: ED7DC31F8AFAA80E

FASTA66774,782
        10         20         30         40         50         60 
MEKEAAKRRV EQLHALINKY NYEYHTLDDP SVPDSEYDKL MKELIALEEE HPDLKTPDSP 

        70         80         90        100        110        120 
SQRVGGAVLD AFQKVQHKTP MLSLGNAFNE EDLRDFDRRV RQAVGDVEYN VEFKIDGLAV 

       130        140        150        160        170        180 
SLRYENGVFV RGATRGDGTT GEDITENLKT IRNIPLRMKR DLSIEVRGEA FMPKRSFELL 

       190        200        210        220        230        240 
NKARIERDEE PFANPRNAAA GSLRQLDPKI AAKRNLDIFV YSIAELDEMG VETQSQGLDF 

       250        260        270        280        290        300 
LDELGFKTNH ERKKCSTIEE VIEIVEELKT KRADLPYEID GIVIKVDSLD QQEELGFTAK 

       310        320        330        340        350        360 
SPRWAIAYKF PAEEVVTTLL DIELSVGRTG AVTPTAILEP VKVAGTTVQR ASLHNEDLIK 

       370        380        390        400        410        420 
EKDIRLLDKV VVKKAGDIIP EVVNVLVEQR TGKEKEFNMP KECPECGSEL VRIEGEVALR 

       430        440        450        460        470        480 
CINPECPAQI REGLIHFVSR NAMNIDGLGE RVITQLFRED LVHNVADLYK LTREQLINLE 

       490        500        510        520        530        540 
RMGEKSTDNL LNSIEKSKKN SLERLLFGLG IRFIGAKAAK TLAMHFETLD KLKKATKEEL 

       550        560        570        580        590        600 
IEVDEIGDKM ADALVTYFEK EEILKLLDEL EELGVNTVYK GPKKAAAEAS DSYFAGKTIV 

       610        620        630        640        650        660 
LTGKLSEMSR NDAKAEIEAL GGKITGSVSK KTDLVIAGEA AGSKLAKAED LNIEVWDEAR 


LISELKK

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000002 Genomic DNA. Translation: AAU22302.1.
AE017333 Genomic DNA. Translation: AAU39652.1.
RefSeqYP_077940.1. NC_006270.3.
YP_090345.1. NC_006322.1.

3D structure databases

HSSPHSSP built from PDB template 1B04 based on UniProtKB O87703.
ProteinModelPortalQ65MR2.
SMRQ65MR2. Positions 1-313.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65MR2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000054283; EBBACP00000052814; EBBACG00000054274.
EBBACT00000061994; EBBACP00000060427; EBBACG00000061985.
GeneID3031245.
3098899.
GenomeReviewsGene locus BLi00716 in contig AE017333_GR.
Gene locus BL00589 in contig CP000002_GR.
KEGGbld:BLi00716.
bli:BL00589.
NMPDRfig|279010.5.peg.1023.
PATRIC18946959. VBIBacLic203714_0704.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
GeneTreeEBGT00050000002892.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBQ65MR2.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI00716-MONOMER.
BLIC279010:BL00589-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_BACLD
AccessionPrimary (citable) accession number: Q65MR2
Secondary accession number(s): Q62Y56
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 64 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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