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Q0S2J2 (DNLJ_RHOSR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:RHA1_ro06469
OrganismRhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP]
Taxonomic identifier101510 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length696 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 – 696696DNA ligase HAMAP MF_01588
PRO_0000313397

Regions

Domain608 – 69689BRCT
Nucleotide binding43 – 475NAD By similarity
Nucleotide binding92 – 932NAD By similarity

Sites

Active site1241N6-AMP-lysine intermediate By similarity
Metal binding4191Zinc By similarity
Metal binding4221Zinc By similarity
Metal binding4381Zinc By similarity
Metal binding4441Zinc By similarity
Binding site1221NAD By similarity
Binding site1451NAD By similarity
Binding site1851NAD By similarity
Binding site3011NAD By similarity
Binding site3251NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0S2J2 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 29620AE6EBDE98AE

FASTA69675,730
        10         20         30         40         50         60 
MSESTEAPTP APGHVREHWN ELAEEVRQHQ FRYYVRDAPI ISDGEFDVLL GELNDLENQY 

        70         80         90        100        110        120 
PDLRTPDSPT QLVGGGFSTD FASADHLERM LSLDNVFATD ELRTWISRVE QETGPDLHYL 

       130        140        150        160        170        180 
CEVKIDGVAL NLVYENGRLD RAATRGDGRT GEEVTLNART IDDIPEKLTG TDEYPIPALL 

       190        200        210        220        230        240 
EVRGEVFFRL EDFAALNAAL VEEGKAPFAN PRNSAAGSLR QKNPAVTARR RLGMICHGLG 

       250        260        270        280        290        300 
RSEGFEPVSQ YDAYTALAAW GLPVSTHTAR VTGADAVVDR VQYWGEHRHD VEHEIDGLVV 

       310        320        330        340        350        360 
KVDETSLQRR LGSTSRAPRW AIAYKYPPEE ATTKLLDIRV NVGRTGRVTP FAYMEPVTVA 

       370        380        390        400        410        420 
GSTVSLATLH NGSEVKRKGV LIGDTVVLRK AGDVIPEVLG PVVDARTGDE YEFVMPTHCP 

       430        440        450        460        470        480 
ECDTPLAPAK EGDADIRCPN QQYCPAQLRE RVFHVAGRGA FDIEVLGYEA ATSLLEAKAI 

       490        500        510        520        530        540 
GDEGDLFSLT EDDLLKTSLF RTKAGGLSAN GRRLLDNLDS AKDKPLWRVL VALSIRHVGP 

       550        560        570        580        590        600 
TAARALAGEF GSLARIRESS VEELAAVDGV GGTIAAAVAE WFGVDWHQQI VEKWSAAGVR 

       610        620        630        640        650        660 
MEDERDESIP RNLEGLSIVV TGSLETFSRD QAKEAILIRG GKAAGSVSKK TAFVVVGESP 

       670        680        690 
GSKHDKAVEL GVPVLDEDGF RRLLEGGPDA VAESGV

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000431 Genomic DNA. Translation: ABG98244.1.
RefSeqYP_706402.1. NC_008268.1.

3D structure databases

ProteinModelPortalQ0S2J2.
SMRQ0S2J2. Positions 11-329.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0S2J2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4224020.
GenomeReviewsGene locus RHA1_ro06469 in contig CP000431_GR.
KEGGrha:RHA1_ro06469.
PATRIC23211897. VBIRhoJos26306_6522.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycRSP101510:RHA1_RO06469-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. 2 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_RHOSR
AccessionPrimary (citable) accession number: Q0S2J2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: January 25, 2012
This is version 44 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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