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Q68W27 (DNLJ_RICTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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
Synonyms:lig
Ordered Locus Names:RT0706
OrganismRickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]
Taxonomic identifier257363 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length693 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 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 – 693693DNA ligase HAMAP-Rule MF_01588
PRO_0000280948

Regions

Domain610 – 69384BRCT
Nucleotide binding40 – 445NAD By similarity
Nucleotide binding89 – 902NAD By similarity

Sites

Active site1231N6-AMP-lysine intermediate By similarity
Metal binding4131Zinc By similarity
Metal binding4161Zinc By similarity
Metal binding4311Zinc By similarity
Metal binding4371Zinc By similarity
Binding site1211NAD By similarity
Binding site1441NAD By similarity
Binding site1791NAD By similarity
Binding site2951NAD By similarity
Binding site3191NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q68W27 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 80BE9C9493DF658B

FASTA69378,483
        10         20         30         40         50         60 
MQNIDLISEK EAKKLLEELA DKIAMYNHAY YIEDNPLVSD SEYDQLFNLN LKLENTFPHL 

        70         80         90        100        110        120 
VLSNSPSKKI GAKITNKFAK VIHQAPMLSL SNAFDEEDIR DFLERIKNFL RINEFTPIFC 

       130        140        150        160        170        180 
EPKIDGLSFS AIYKHGLFIT GATRGDGYVG EDITINIKTI KNFPHKIDNA PEFLEVRGEI 

       190        200        210        220        230        240 
YIEKQDFVNL NKEQEAQNRG KFANPRNAAA GSIRQLDVAI TAQRPLKYFI YSGGVTEKNL 

       250        260        270        280        290        300 
ASTQEQLLAK LKALSFSVNE ISKLASSEEE IFAFYEYLKT NRHNLPYEID GVVYKLNNFA 

       310        320        330        340        350        360 
MQNRMGFIAR SPRFAIAHKF PAIIGQTKLL SITVQVGRTG MLTPVAELDP LEIGGVVVSR 

       370        380        390        400        410        420 
ATLHNFQDIA RKDVRIKDYV FLQRAGDVIP QITGVDISKR SNDTVKFDTP VFCPSCNSKL 

       430        440        450        460        470        480 
RYVSEDIIIR CDNGLNCPAQ NYERICHFVS KNAMDIAGLG RKQVAFLIDK RLISNPLDIF 

       490        500        510        520        530        540 
FLKKKNETNL IRLENMDGWG KKSVANLWQN IEKSQKISLQ RFIYALGIRH IGEQNAKLLA 

       550        560        570        580        590        600 
REFVSYNNFI AQMELLSKND SDVYQKLNDL EGIGDKMLVD IIDFFYVKEN IQLIKKLGAV 

       610        620        630        640        650        660 
LNIEDYKETR EQNILTGKIL VFTGSLKTIS RVEAKEIAEK LGAKVASSVS SNTDLLIVGV 

       670        680        690 
NGGSKLKKAK ELNIKIIDEA EWLAFIKCLE KEV 

« Hide

References

[1]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017197 Genomic DNA. Translation: AAU04165.1.
RefSeqYP_067647.1. NC_006142.1.

3D structure databases

ProteinModelPortalQ68W27.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257363.RT0706.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU04165; AAU04165; RT0706.
GeneID2959338.
KEGGrty:RT0706.
PATRIC17910662. VBIRicTyp34752_0726.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHOG000218458.
KOK01972.
OMAKEYYVDS.
OrthoDBEOG6TTVM9.

Enzyme and pathway databases

BioCycRTYP257363:GJEQ-743-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.
IPR001679. DNAligase.
IPR013839. DNAligase_adenylation.
IPR013840. DNAligase_N.
IPR012340. NA-bd_OB-fold.
IPR004150. NAD_DNA_ligase_OB.
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.
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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDNLJ_RICTY
AccessionPrimary (citable) accession number: Q68W27
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 66 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

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names