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A9WTZ3 (DNLJ_RENSM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:RSal33209_2942
OrganismRenibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235) [Complete proteome] [HAMAP]
Taxonomic identifier288705 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Renibacterium

Protein attributes

Sequence length758 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 – 758758DNA ligase HAMAP MF_01588
PRO_0000340372

Regions

Domain660 – 74990BRCT
Nucleotide binding60 – 645NAD By similarity
Nucleotide binding109 – 1102NAD By similarity

Sites

Active site1501N6-AMP-lysine intermediate By similarity
Metal binding4421Zinc By similarity
Metal binding4451Zinc By similarity
Metal binding4611Zinc By similarity
Metal binding4671Zinc By similarity
Binding site1481NAD By similarity
Binding site1711NAD By similarity
Binding site2081NAD By similarity
Binding site3241NAD By similarity
Binding site3481NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A9WTZ3 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 4C06F2A4A53029F4

FASTA75882,589
        10         20         30         40         50         60 
MPENFGAMRQ DGLVSTSESD SPAPAATPAA TLRAEYSKLV EDIRHYRFAY YNEAESLVSD 

        70         80         90        100        110        120 
AEFDVLFRRL EEIEALHPEL ISNDSPTQEV GGEVSAAFTP VQHTSQIYSL EDVFSIEELQ 

       130        140        150        160        170        180 
SWIIKAQANA EKLAGSIVAE RPLRWLTELK IDGLAVNLLY RNGQLVRAAT RGDGITGEDI 

       190        200        210        220        230        240 
THNVLTIQEI PRQLRGENLP EEVEIRGEVF IASKDFLALN EQIVGTGRAP FANPRNAAAG 

       250        260        270        280        290        300 
SLRQKDPADT AKRPLSMLVH GIGSRIGLDV ASQSESYALL KAWGLPTSPY FKVLTGYQEV 

       310        320        330        340        350        360 
LDYINHYGEH RHDLLHEIDG IVIKIDDFAS QNALGFTSRV PRWAVAYKYP PEEVHTKLLD 

       370        380        390        400        410        420 
ILVNVGRTGR VTPFGVMEPV KVAGSTVEMA TLHNQDVVKA KGVLIGDTVV LRKAGDVIPE 

       430        440        450        460        470        480 
IVGPVLALRD GREREFVMPT ECPSCGTALA PAKEGDVDIR CPNAKSCPDQ LRERVFHLAG 

       490        500        510        520        530        540 
RGAFDIEALG WEAAIALTQP AEPELAPVRN EAQIFNLVAE DLALVKIKRE KKVKGVLSGV 

       550        560        570        580        590        600 
HELVPYFYSK GTEEKPSEPT SNTVKLFIEL EKAKAQPLWR VLVALSIRHV GPTASRALAT 

       610        620        630        640        650        660 
AFGSMAAIRA ASEPELAEVD GVGPTIAAAL IEWFAEDWHR EIIDAWAADG VRMADERDES 

       670        680        690        700        710        720 
VRRTLAGLTI VVTGSLEKFN RDQAKEAIIN RGGKSAGSVS KNTDYVVAGE NAGTKLDKAE 

       730        740        750 
KLGVTVLDEA GFETLLAHGP DHSAEAEENE SEGSTTND

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References

[1]"Genome sequence of the fish pathogen Renibacterium salmoninarum suggests reductive evolution away from an environmental Arthrobacter ancestor."
Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.
J. Bacteriol. 190:6970-6982(2008) [PubMed: 18723615] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000910 Genomic DNA. Translation: ABY24664.1.
RefSeqYP_001626078.1. NC_010168.1.

3D structure databases

ProteinModelPortalA9WTZ3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9WTZ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5824062.
GenomeReviewsGene locus RSal33209_2942 in contig CP000910_GR.
KEGGrsa:RSal33209_2942.
PATRIC23079317. VBIRenSal21953_3064.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBCLSK959647.

Enzyme and pathway databases

BioCycRSAL288705:RSAL33209_2942-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. 1 hit.
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_RENSM
AccessionPrimary (citable) accession number: A9WTZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 31 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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