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Q2INT9 (DNLJ_ANADE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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:Adeh_0693
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

Protein attributes

Sequence length687 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 – 687687DNA ligase HAMAP MF_01588
PRO_0000313111

Regions

Domain609 – 68779BRCT
Nucleotide binding34 – 385NAD By similarity
Nucleotide binding83 – 842NAD By similarity

Sites

Active site1191N6-AMP-lysine intermediate By similarity
Metal binding4161Zinc By similarity
Metal binding4191Zinc By similarity
Metal binding4341Zinc By similarity
Metal binding4391Zinc By similarity
Binding site1171NAD By similarity
Binding site1401NAD By similarity
Binding site1821NAD By similarity
Binding site2981NAD By similarity
Binding site3221NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2INT9 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: E65AAA74C69A1EDF

FASTA68776,280
        10         20         30         40         50         60 
MKKADAAARA RDLRERIRAA DHAYYVLDQP VLADAEYDRL MHELQAIEAE HPELVTADSP 

        70         80         90        100        110        120 
TQRVSGAPSE RFERVVHREP MLSLGNVQSD DELHEFDARV RRLLGLPEGE AVGYVVEPKL 

       130        140        150        160        170        180 
DGLAVELVYR DGAFTGGSTR GDGVNGEDVT ANLRVVGGLG ANRGVPHALE GTPPPRVEVR 

       190        200        210        220        230        240 
GEVLLFKEHF EAMNRQLVRA GDEPFANPRN AAAGTLRQLD WRVTARRPLS FVAYEALVPG 

       250        260        270        280        290        300 
GDPWRTHWEK LEALAAWGFE TNPENRRCRG LGEVLAYRDR MAERRFELPY DTDGIVVKVD 

       310        320        330        340        350        360 
DLDWRRRLGA ASKFPRWAVA FKYPPQEEAT RIRRIWASVG RTGVLTPVVD FDPVRLSGAM 

       370        380        390        400        410        420 
VARATLHNED EMRRKDILEG DWVLVRRAGE VIPEVVKPLP ERRTGEERPF RFPAECPVCG 

       430        440        450        460        470        480 
ARVVREEGEK VYRCTGAACP AQLVGRICHF AQRRALDIEG LGEKLAAGLV ERGQVKDFAD 

       490        500        510        520        530        540 
LYAVPFEVWQ QLFSRPRKEQ DAGAARELPE KSAQNMVAAL ERSRSTTLRR FLFALGIPQV 

       550        560        570        580        590        600 
GEATAATLAR HFGDLARILD ADEEALKGVR DVGPETASEI RAWTQEPQNR RVVERLLAAG 

       610        620        630        640        650        660 
VRPEPEVVEA RGPFAGKTVV LTGGLSAMSR DDAKAEVERR GGKVSGSVSR KTDLVVAGEE 

       670        680 
AGSKLEKARS LGVRVVGEEE FVRLLKE

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References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000251 Genomic DNA. Translation: ABC80469.1.
RefSeqYP_463906.1. NC_007760.1.

3D structure databases

ProteinModelPortalQ2INT9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2INT9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3886813.
GenomeReviewsGene locus Adeh_0693 in contig CP000251_GR.
KEGGade:Adeh_0693.
PATRIC20917433. VBIAnaDeh31384_0717.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBQ2INT9.
ProtClustDBCLSK945187.

Enzyme and pathway databases

BioCycADEH290397:ADEH_0693-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. 3 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_ANADE
AccessionPrimary (citable) accession number: Q2INT9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 46 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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