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Q57C89 (DNLJ_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BruAb1_1415
OrganismBrucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]
Taxonomic identifier262698 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

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-Rule MF_01588

Catalytic activity

NAD+ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D-ribonucleotide + (deoxyribonucleotide)(n+m). HAMAP-Rule MF_01588

Cofactor

Magnesium or manganese By similarity. HAMAP-Rule 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

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA ligase (NAD+) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

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-Rule MF_01588
PRO_0000313152

Regions

Domain640 – 71980BRCT
Nucleotide binding42 – 465NAD By similarity
Nucleotide binding92 – 932NAD By similarity

Sites

Active site1281N6-AMP-lysine intermediate By similarity
Metal binding4301Zinc By similarity
Metal binding4331Zinc By similarity
Metal binding4481Zinc By similarity
Metal binding4541Zinc By similarity
Binding site1261NAD By similarity
Binding site1491NAD By similarity
Binding site1851NAD By similarity
Binding site3011NAD By similarity
Binding site3251NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q57C89 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 122949D2FB8B1B79

FASTA71978,681
        10         20         30         40         50         60 
MSDISVEKLT ELEAAAELER LARAIAHHDE LYHAKDRPEI SDAAYDALKR RNEAIEAHFP 

        70         80         90        100        110        120 
ALVRDDSPSR RVGAAPALAT FAPVVHARPM LSLDNAFSDE DVRDFVGSVY RFLGQLPDDS 

       130        140        150        160        170        180 
IAFTAEPKID GLSMSIRYEN GILVSGATRG DGTTGENVTA NIRTIAEIPN RLPAGAPAVV 

       190        200        210        220        230        240 
EVRGEVYMAK SDFLTLNAQM EAEGKQTYVN PRNTAAGSLR QLDAKVTASR KLRFFAYAWG 

       250        260        270        280        290        300 
EMSDMPADTQ LGMVEVFRQW GFPVNPLMKR FNSVDGLLAH YRAIGMERPT LDYDIDGVVY 

       310        320        330        340        350        360 
KVDRLDLQTR LGFRSRSPRW AIAHKFPAEQ ALTILRGIDI QVGRTGALTP VARLEPITVG 

       370        380        390        400        410        420 
GVVVTNATLH NEDYIKGIGQ KGEPIREGRD IRIGDSVIVQ RAGDVIPQIV DVVLEEGKKR 

       430        440        450        460        470        480 
GEPYQFPHVC PACGSHAVRE EGEAVRRCTG GLICPAQAVE RIRHFVSRNA FDIEGLGEKQ 

       490        500        510        520        530        540 
VEFFFNAEDP ALCIRSPADI FTLKKRQENS LTKLQNIEGF GATSVKKLYD AIDARREIAL 

       550        560        570        580        590        600 
HRFLFGLGIR HVGEVNAKRL ARAYLSYAAF EKAALEAVPP KEGDRTDKGS EAWQDMLAVE 

       610        620        630        640        650        660 
GIGSIVAEAV VDFYGEPHNR EVLAALLAEV TPLDEEARVA TGSPVEGKTV VFTGSLERMS 

       670        680        690        700        710 
RDEAKAMAER HGAKTAGSVS KKTDLVVAGP GAGSKLAKAT ELGIEVINED DWFKLVGED 

« Hide

References

[1]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017223 Genomic DNA. Translation: AAX74745.1.
RefSeqYP_222106.1. NC_006932.1.

3D structure databases

ProteinModelPortalQ57C89.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262698.BruAb1_1415.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX74745; AAX74745; BruAb1_1415.
GeneID3340487.
KEGGbmb:BruAb1_1415.
PATRIC17824565. VBIBruAbo15061_1498.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHOG000218459.
KOK01972.
OMAFTAKSPR.
OrthoDBEOG6TTVM9.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycBABO262698:GJC2-1445-MONOMER.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.40.50.10190. 1 hit.
HAMAPMF_01588. DNA_ligase_A.
InterProIPR001357. BRCT_dom.
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.
IPR010994. RuvA_2-like.
IPR004149. Znf_DNAligase_C4.
[Graphical view]
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. 2 hits.
SM00532. LIGANc. 1 hit.
[Graphical view]
SUPFAMSSF47781. SSF47781. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF52113. SSF52113. 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_BRUAB
AccessionPrimary (citable) accession number: Q57C89
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 10, 2005
Last modified: April 16, 2014
This is version 67 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

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names