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Q2KUU5 (DNLJ_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:BAV1072
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length695 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 – 695695DNA ligase HAMAP MF_01588
PRO_0000313143

Regions

Domain617 – 69579BRCT
Nucleotide binding36 – 405NAD By similarity
Nucleotide binding85 – 862NAD By similarity

Sites

Active site1251N6-AMP-lysine intermediate By similarity
Metal binding4361Zinc By similarity
Metal binding4391Zinc By similarity
Metal binding4541Zinc By similarity
Metal binding4601Zinc By similarity
Binding site1231NAD By similarity
Binding site1461NAD By similarity
Binding site1821NAD By similarity
Binding site3181NAD By similarity
Binding site3421NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2KUU5 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: D36526671877F754

FASTA69575,425
        10         20         30         40         50         60 
MSAFEQAARE QAARLRAEIA QHNIRYYVYD EPSITDADYD ALMRELMALE AQHPELVTPD 

        70         80         90        100        110        120 
SPTQRVGAAP LAEFGSVRHA VPMLSLGNGF EDEDVLAFDK RVSDTLREAG LLGPAEQAHY 

       130        140        150        160        170        180 
FCELKLDGLA ISLRYENGEL VQAATRGDGQ EGEDVTANIR TIRAIPLQLR AGAPAVLEVR 

       190        200        210        220        230        240 
GEVLMNRADF EKLNQKQAAR GEKIFVNPRN AAAGSLRQLD PRVTAQRPLR FFAYSWGEVQ 

       250        260        270        280        290        300 
GLSRDDAPAF DEASPGLVST LPRDTHGGML DWLAGLGLPV NVRFNHKAQG AEGLLAFYRR 

       310        320        330        340        350        360 
IGAERGSLPY DIDGLVYKVD ALAAQRVLGY VARAPRWALA HKFPAEEATT ELLDIEVQVG 

       370        380        390        400        410        420 
RTGAITPVAR LKPVFVGGVT VTNATLHNED EIRRKDVRIG DRVIVRRAGD VIPEVVGPVL 

       430        440        450        460        470        480 
EKRSGELPQF VMPTHCPICG SAIERLVDEA IARCTGGLFC PAQRKQTLLH AAGRKALDIE 

       490        500        510        520        530        540 
GLGEKLVEQL VDNGSLKTLA DVFRLNAFEL AALDRMGKKS ADNLVAAIDQ ARRPSLGRLL 

       550        560        570        580        590        600 
FALGIRHVGE TTARDVARHF GNIDAIMDAD EAALLAVPDV GPVVAGSIHR FFQEAHNREV 

       610        620        630        640        650        660 
IRELEKQGVH PQAEAQLQSG DLAGKTFVLT GTMPTWSRDE ATRHILAAGG KVSGSVSKKT 

       670        680        690 
AYVVAGEEAG SKLVKARELG VTILDEDGLK ALLSQ

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM167904 Genomic DNA. Translation: CAJ48681.1.
RefSeqYP_785595.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2KUU5.
SMRQ2KUU5. Positions 7-613.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2KUU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6265152.
GenomeReviewsGene locus BAV1072 in contig AM167904_GR.
KEGGbav:BAV1072.
NMPDRfig|521.1.peg.665.
PATRIC21128350. VBIBorAvi43433_1099.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBCLSK2516705.

Enzyme and pathway databases

BioCycABAU360910:BAV1072-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_BORA1
AccessionPrimary (citable) accession number: Q2KUU5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 47 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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