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A0JUH2 (DNLJ_ARTS2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:Arth_1298
OrganismArthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]
Taxonomic identifier290399 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length790 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 – 790790DNA ligase HAMAP MF_01588
PRO_0000313117

Regions

Domain679 – 76890BRCT
Nucleotide binding79 – 835NAD By similarity
Nucleotide binding128 – 1292NAD By similarity

Sites

Active site1661N6-AMP-lysine intermediate By similarity
Metal binding4611Zinc By similarity
Metal binding4641Zinc By similarity
Metal binding4801Zinc By similarity
Metal binding4861Zinc By similarity
Binding site1641NAD By similarity
Binding site1871NAD By similarity
Binding site2241NAD By similarity
Binding site3401NAD By similarity
Binding site3641NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A0JUH2 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 8771FABBDF3747E2

FASTA79085,847
        10         20         30         40         50         60 
MRLEPDNVGD LGQDRSVSTG NTAADTDTQS MTGAGTREAD TASERVPSGA VREEYENLVE 

        70         80         90        100        110        120 
EVRKHRFAYY QEDAPIISDA EFDELFRRLE TIEAMHPELV ANDSPTQEVG GEVSAAFAAV 

       130        140        150        160        170        180 
EHLQRMYSLE DVFSLEELES WIAKAEASVA KLGNGTAGPA WLTELKIDGL AVNLLYRDGK 

       190        200        210        220        230        240 
LVRAATRGDG YTGEDITHNV LTIKEIPQQL TGGNYPAEME VRGEVFIPSK AFAEYNEALI 

       250        260        270        280        290        300 
EAGKAPLANP RNAAAGSLRQ KDPAETAKRP LRMYVHGIGA REGLRTVSQS DTYRQLAEWG 

       310        320        330        340        350        360 
LPTSPYFEVL GSLKDILDFI KRYGDKRHSL THEIDGIVVK VDDFATQRAL GYTSRVPRWA 

       370        380        390        400        410        420 
VAYKYPPEEV HTKLLDIAVN VGRTGRVTPF GIMEPVKVAG STVGMATLHN QDVVKAKGVK 

       430        440        450        460        470        480 
IGDIVVLRKA GDVIPEIVGP VLALRDQQDP PVRDFVMPTE CPACGTPLAP GKEGDVDIRC 

       490        500        510        520        530        540 
PNSRSCPAQL RERVFHVASR GAFDIEALGW EAAIALTQPA EPVTPPLTSE ANLFRLTRED 

       550        560        570        580        590        600 
LADVRIRREK RSKGVATGEF ELVPYFYTKG TAKSPSKPTA TTEKLFTELE KAKSQPLWRV 

       610        620        630        640        650        660 
LVALSIRHVG PRASRALATA FGSMDAIREA SEEELAHVDG VGPVIAAALK EWFAEDWHRE 

       670        680        690        700        710        720 
IVDTWAEDGV RMEDEQDEST PRTLEGLTVV VTGSLEGFSR DEAKEAILIR GGKASGSVSK 

       730        740        750        760        770        780 
NTSYVVAGEN AGTKLDKAEQ LGVPVLDEDG FRALLANGPA ASADSADASA DDDDAGVGDR 

       790 
PEDHQEEPAE

« Hide

References

[1]"Complete sequence of chromosome 1 of Arthrobacter sp. FB24."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FB24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000454 Genomic DNA. Translation: ABK02692.1.
RefSeqYP_830792.1. NC_008541.1.

3D structure databases

ProteinModelPortalA0JUH2.
SMRA0JUH2. Positions 50-368.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0JUH2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4446222.
GenomeReviewsGene locus Arth_1298 in contig CP000454_GR.
KEGGart:Arth_1298.
PATRIC20997877. VBIArtSp72239_1651.
TIGRArth_1298.

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBCLSK959647.

Enzyme and pathway databases

BioCycASP1667:ARTH_1298-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_ARTS2
AccessionPrimary (citable) accession number: A0JUH2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: January 25, 2012
This is version 43 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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