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A6W7L4 (DNLJ_KINRD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:Krad_1315
OrganismKineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216) [Complete proteome] [HAMAP]
Taxonomic identifier266940 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Kineosporiineae › Kineosporiaceae › Kineococcus

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_0000340355

Regions

Domain603 – 69290BRCT
Nucleotide binding41 – 455NAD By similarity
Nucleotide binding90 – 912NAD By similarity

Sites

Active site1221N6-AMP-lysine intermediate By similarity
Metal binding4141Zinc By similarity
Metal binding4171Zinc By similarity
Metal binding4331Zinc By similarity
Metal binding4391Zinc By similarity
Binding site1201NAD By similarity
Binding site1431NAD By similarity
Binding site1801NAD By similarity
Binding site2961NAD By similarity
Binding site3201NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A6W7L4 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: AF020832164917D8

FASTA69675,120
        10         20         30         40         50         60 
MDTVDGGDVP SEARHRWEDL VAQIEAARFA YYVRNSSPLS DGQYDALERE LRALEEQHPQ 

        70         80         90        100        110        120 
LRTPDSPTQT VGGTFSTEFT TVDHPERMLS LDNAFSTDEL SAWAARVERE VGAGARYLCE 

       130        140        150        160        170        180 
PKIDGLAIDL VYEDGRLVRG VTRGDGRTGE DVTFNVRTVE DVPHRLTGAD VPEFLEVRGE 

       190        200        210        220        230        240 
VFFHLDGFAA INAGLVEAGK PPFANPRNAA AGSLRQKDPR VTATRPLRML VHGVGARRGM 

       250        260        270        280        290        300 
ENDTQSGAYE KLAAWGLPTS PRVKVVDTLD EVAEYVRFYG EHRHDVEHEI DGVVVKVDQV 

       310        320        330        340        350        360 
PLQRRLGSTS RAPRWAIAYK YPPEEVTTSL LDIQVNVGRT GRVTPFAVLE PVKVAGSTVA 

       370        380        390        400        410        420 
MATLHNASEV VRKGVLIGDT VVVRKAGDVI PEVLGPVVES RTGAEREFVM PTVCPECGTP 

       430        440        450        460        470        480 
LAHQRADDVD IRCPNSRSCP AQLRERVFHL AGRGSFDVEA LGDKAAAALL QAGVIADEGD 

       490        500        510        520        530        540 
LFTLTEDDLV GVPLFTTKAG TVSANGRRLL ANLHDRKDQP LWRVLVGLSI RHVGPTAARA 

       550        560        570        580        590        600 
LADRFGSMEA IEAATAEDIA SAEGVGPTIA EAVVEWLAVD WHRDVVRKWR EAGVRMADER 

       610        620        630        640        650        660 
DESTPRTLEG LTIVVTGSLS GFSRDEAKEA VLSRGGKASS AVSKKTSFVV VGEAAGSKAD 

       670        680        690 
KAEQLGVPVL DEEGFVALLE GGPDAVARPA EEPGQG

« Hide

References

[1]"Complete sequence of chromosome of Kineococcus radiotolerans SRS30216."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J., Fliermans C., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-149 / DSM 14245 / SRS30216.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000750 Genomic DNA. Translation: ABS02803.1.
RefSeqYP_001361067.1. NC_009664.2.

3D structure databases

ProteinModelPortalA6W7L4.
SMRA6W7L4. Positions 12-324.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6W7L4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5334394.
GenomeReviewsGene locus Krad_1315 in contig CP000750_GR.
KEGGkra:Krad_1315.
NMPDRfig|266940.1.peg.1242.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.

Enzyme and pathway databases

BioCycKRAD266940:KRAD_1315-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_KINRD
AccessionPrimary (citable) accession number: A6W7L4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: August 21, 2007
Last modified: January 25, 2012
This is version 35 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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