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Q6FZ81 (DNLJ_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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:BQ08760
OrganismBartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier283165 [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_0000313136

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
Q6FZ81 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 096B443073BEBB42

FASTA71980,128
        10         20         30         40         50         60 
MNKDEIKNLT ALEAESELEW LAKEIARHDV LYNRDDQPEI SDAEYDALRR RNAEIEALFP 

        70         80         90        100        110        120 
ELIRSDSPSH KIGAPVSEKF EKSVHAQAML SLDNAFSSED ICEFIVRIRR FLRLPATQIL 

       130        140        150        160        170        180 
EMTAEPKIDG LSLSLRYEKG RLVCAATRGD GYIGENVTAN ARTISDIPKV LRGEFPDIIE 

       190        200        210        220        230        240 
VRGEVYMRRE NFQALNMSQQ EKGKFVFANP RNAAAGSLRQ LDPRITASRK LHFFAYACGE 

       250        260        270        280        290        300 
VSETFAASQM EMMKKLKEYG FFINPLTKSF KTLEEIISYY HDIEECRHSL SYDIDGIVYK 

       310        320        330        340        350        360 
VNDLKLQMRL GFVSRSPRWA VAHKFPAEKA MALLEGIDIQ VGRTGALTPV ARLAPITIGG 

       370        380        390        400        410        420 
VVVTNASLHN EDYIKGIGHK GESIREGRDI RVGDTVIVQR AGDVIPQIVD IIAEKRPKGA 

       430        440        450        460        470        480 
SAFVFPHLCP ACGSHAVREV GESVRRCTGG LICPAQAIER IRHFVSRNAF DIEGLGKKQV 

       490        500        510        520        530        540 
EFFFHIQDEA LCIHTPADIF TLQRRQEKAL VRLENMEGFG TVSVRKLYNA INMRRKVPLS 

       550        560        570        580        590        600 
RFLFALGIRH IGEVNARRLA HAYQNYTAFE TVAMAATMPY DKVGEEGNEA WLELTNIEGI 

       610        620        630        640        650        660 
GPQVGEAIID FYQEAHNREV LAALLREVTP LDEENVMTAS SPIAGKTIVF TGTLARMSRD 

       670        680        690        700        710 
EAKALAERLG AKTSGSLSKK TDLLVAGSAV GSKLAKAQGL GVEVIDEEAW LQLIEGSYI

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References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX897700 Genomic DNA. Translation: CAF26355.1.
RefSeqYP_032488.1. NC_005955.1.

3D structure databases

HSSPHSSP built from PDB template 1L7B based on UniProtKB P26996.
ProteinModelPortalQ6FZ81.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2866441.
GenomeReviewsGene locus BQ08760 in contig BX897700_GR.
KEGGbqu:BQ08760.
NMPDRfig|283165.1.peg.758.
PATRIC31953073. VBIBarQui58630_0952.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBQ6FZ81.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycBQUI283165:BQ08760-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_BARQU
AccessionPrimary (citable) accession number: Q6FZ81
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 54 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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