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A6VR16 (DNLJ_ACTSZ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 33. 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:Asuc_2067
OrganismActinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]
Taxonomic identifier339671 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length672 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 – 672672DNA ligase HAMAP MF_01588
PRO_0000340323

Regions

Domain592 – 67281BRCT
Nucleotide binding32 – 365NAD By similarity
Nucleotide binding81 – 822NAD By similarity

Sites

Active site1161N6-AMP-lysine intermediate By similarity
Metal binding4091Zinc By similarity
Metal binding4121Zinc By similarity
Metal binding4271Zinc By similarity
Metal binding4331Zinc By similarity
Binding site1141NAD By similarity
Binding site1371NAD By similarity
Binding site1741NAD By similarity
Binding site2911NAD By similarity
Binding site3151NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A6VR16 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 03C6470823FEE503

FASTA67274,733
        10         20         30         40         50         60 
MTDIQNQINQ LRNTLRHHEY QYHVLDNPEI PDSEYDRLFH RLKALEQQHP ELISADSPTQ 

        70         80         90        100        110        120 
RVGAKPLAGF AQITHELPML SLDNVFSDEE FYAFVKRIQE RLITLPDNLE FCCEPKLDGL 

       130        140        150        160        170        180 
AVSILYENGR LVQAATRGDG TTGEDITLNI RTIRNIPLQL LTDNPPVRLE VRGEVFMPQE 

       190        200        210        220        230        240 
GFDRLNEAAL ARGEKTFANP RNAAAGSLRQ LDPKITSQRP LVWNAYSIGI AEGADLPPTH 

       250        260        270        280        290        300 
YERLQWLKSI GIPVNGEIRL CRGAENVLKF YRTIQEKRPE LGYDIDGTVL KVNEIALQER 

       310        320        330        340        350        360 
LGFISKAPRW AIAYKFPAQE EMTVLNDVEF QVGRTGAITP VAKLQPVFVA GVTVSNATLH 

       370        380        390        400        410        420 
NGDEIARLDI AIGDTVIVRR AGDVIPQIIG VVHDRRPPNA EPIIFPTLCP VCHSAIVRIE 

       430        440        450        460        470        480 
GEAVARCTGG LFCDAQRKES LKHFVSRRAM DIDGVGAKLI EQLVDRELIR TPADLFKLDL 

       490        500        510        520        530        540 
ITLMRLERMG EKSAQKALDS LEKAKKTTLA RFIFALGIRE VGEATALNLA NFFKNLTALQ 

       550        560        570        580        590        600 
TADLEQLQAV SDVGEVVANR IYVFWREQHN IDVVNDLIAQ GVHWDDVEEK QVNENPFKEK 

       610        620        630        640        650        660 
TVVLTGTLSQ MGRNEAKALL QQMGAKVAGS VSAKTHIVIA GDSAGSKLSK AQDLGVAVMS 

       670 
EAEFLEIVNS FS

« Hide

References

[1]"Complete sequence of Actinobacillus succinogenes 130Z."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 55618 / 130Z.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000746 Genomic DNA. Translation: ABR75413.1.
RefSeqYP_001345348.1. NC_009655.1.

3D structure databases

ProteinModelPortalA6VR16.
SMRA6VR16. Positions 1-584.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6VR16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5347710.
GenomeReviewsGene locus Asuc_2067 in contig CP000746_GR.
KEGGasu:Asuc_2067.
PATRIC20762614. VBIActSuc117883_2170.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBPRK07956.

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. 4 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_ACTSZ
AccessionPrimary (citable) accession number: A6VR16
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: August 21, 2007
Last modified: December 14, 2011
This is version 33 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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