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A0LSQ7 (DNLJ_ACIC1) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. 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:Acel_0694
OrganismAcidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]
Taxonomic identifier351607 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Acidothermaceae › Acidothermus

Protein attributes

Sequence length695 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 – 695695DNA ligase HAMAP MF_01588
PRO_0000313098

Regions

Domain605 – 69490BRCT
Nucleotide binding44 – 485NAD By similarity
Nucleotide binding93 – 942NAD By similarity

Sites

Active site1251N6-AMP-lysine intermediate By similarity
Metal binding4181Zinc By similarity
Metal binding4211Zinc By similarity
Metal binding4361Zinc By similarity
Metal binding4421Zinc By similarity
Binding site1231NAD By similarity
Binding site1461NAD By similarity
Binding site1841NAD By similarity
Binding site3001NAD By similarity
Binding site3241NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A0LSQ7 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: A5483913137AE471

FASTA69575,300
        10         20         30         40         50         60 
MSPARNTGIP ASAADAARRH AELVKEIEEH AYRYYVLDAP TISDAEYDAL MRELEEIENA 

        70         80         90        100        110        120 
YPELRTPDSP TQKVQGAPAA HFAPVEHLER MLSLDNVFTE GELRAWIARV EKEVGTDAAY 

       130        140        150        160        170        180 
LCEPKVDGLA VDLVYEDGVL VRGATRGDGR VGEDVTANIK AIRNVPHRLH RDGNLPALLE 

       190        200        210        220        230        240 
VRGEVYFPVA DFAELNAGLV AAGKAPFANP RNAAAGSLRQ KDPRVTASRP LRLVVHGIGA 

       250        260        270        280        290        300 
HQGLAAARQS EAYVALAAWG LPVSERAKVA TTTKEILDYI AYYAEHRHDL EHEIDGVVVK 

       310        320        330        340        350        360 
VDQFALQRRL GATAKAPRWA VAYKYPPEEV TTKLLDIQVN VGRTGRVTPF AVMEPVRVAG 

       370        380        390        400        410        420 
STVTNATLHN ADEIKRKGVL IGDTVVVRKA GDVIPEVVGP VVALRDGSER EFVFPSHCPA 

       430        440        450        460        470        480 
CGTPLVRENG GVDIRCPNAR SCPAQLRERL FHIASRGALD IESLGYEAAN ALLESKLLAD 

       490        500        510        520        530        540 
EGDLFLLTPE KLRTVPFFTK KDGELSANAV KLLENLESAK TRPLWRVLVA LSIRHVGPTA 

       550        560        570        580        590        600 
ARALAREFGS IDAIRNASVD ELAAVEGVGR VIAESIRDWF AVDWHQEIVA KWSAAGVRMA 

       610        620        630        640        650        660 
EEQRSAAKPL AGITVVVTGT LSRWSRDSAI EAIQDAGGRA AGSVSKKTDF VVVGENPGSK 

       670        680        690 
YDKARQLGIP ILDEEGFATL LTKGPDAARS MAQRP

« Hide

References

[1]"Complete sequence of Acidothermus cellulolyticus 11B."
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., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43068 / 11B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000481 Genomic DNA. Translation: ABK52467.1.
RefSeqYP_872453.1. NC_008578.1.

3D structure databases

ProteinModelPortalA0LSQ7.
SMRA0LSQ7. Positions 12-328.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0LSQ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4486002.
GenomeReviewsGene locus Acel_0694 in contig CP000481_GR.
KEGGace:Acel_0694.
PATRIC20671782. VBIAciCel132453_0736.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBA0LSQ7.

Enzyme and pathway databases

BioCycACEL351607:ACEL_0694-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_ACIC1
AccessionPrimary (citable) accession number: A0LSQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: December 14, 2011
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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