Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q6FDW0 (DNLJ_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:ACIAD0848
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length676 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 – 676676DNA ligase HAMAP MF_01588
PRO_0000313102

Regions

Domain595 – 67682BRCT
Nucleotide binding35 – 395NAD By similarity
Nucleotide binding84 – 852NAD By similarity

Sites

Active site1171N6-AMP-lysine intermediate By similarity
Metal binding4121Zinc By similarity
Metal binding4151Zinc By similarity
Metal binding4301Zinc By similarity
Metal binding4361Zinc By similarity
Binding site1151NAD By similarity
Binding site1381NAD By similarity
Binding site1771NAD By similarity
Binding site2941NAD By similarity
Binding site3181NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FDW0 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: D457CEA091C1C83B

FASTA67675,659
        10         20         30         40         50         60 
MMQPADIVAQ MRQLIQLIAK HNHAYYVMDQ PSITDNEYDQ LFHQLKALEA EYPELTQADT 

        70         80         90        100        110        120 
PTNRVGGQAL SKFETVTHAV PMLSLGNVFN QEDLFAFARR IEERLPNQQI QYDVELKLDG 

       130        140        150        160        170        180 
LAISLWYENG VLVRGVTRGD GETGEDITQN VKTIRNLPKH LQHHSVETPR FLEVRGEVLM 

       190        200        210        220        230        240 
PKQGFERLNA ANEAKGEKTF ANPRNAAAGS LRQLDPAIAA SRPLAFYAYG IAQCEPHHGL 

       250        260        270        280        290        300 
GSMHESLQWL TQLGFEIAER QFLCSSIQEV QQCYEQIQQE RPDLAVEIDG MVIKVDDLKQ 

       310        320        330        340        350        360 
QQQLGFLSRE PRWATAYKFP AEVAMTTVEN IDWQVGRTGT LTPVARLQPV FVGGVTVSNV 

       370        380        390        400        410        420 
TLHNIGEIHR LDVRVGDRVS VYRSGDVIPK VEKVWPEFRP ELAEIVQLPE QCPVCSSPVV 

       430        440        450        460        470        480 
MPEGEALARC SGGLYCAAQR IEAIRHFVSR KALDIEGLGD RWVESLLHLD LLKDVADIYH 

       490        500        510        520        530        540 
LHEHREQLLT IEKMGEKSVQ NLMDAIEASK KTTLARFIYA LGIRGVGETT ARMLANTFQT 

       550        560        570        580        590        600 
LDALKQADIE ALKKTPDVGD ITAEWIYDFF LAEHNIEVLD RLLAAGIHWD APLAPTRQPL 

       610        620        630        640        650        660 
NGESWVVTGT LETMGRDEAT QRLQALGARV SGSVSSKTKC VVAGEKAGSK LDKAEKLQIR 

       670 
VMNEQEFLAF LAQYSA 

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ADP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR543861 Genomic DNA. Translation: CAG67748.1.
RefSeqYP_045570.1. NC_005966.1.

3D structure databases

HSSPHSSP built from PDB template 1B04 based on UniProtKB O87703.
ProteinModelPortalQ6FDW0.
SMRQ6FDW0. Positions 6-592.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6FDW0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2881106.
GenomeReviewsGene locus ACIAD0848 in contig CR543861_GR.
KEGGaci:ACIAD0848.
NMPDRfig|62977.3.peg.760.
PATRIC20739588. VBIAciSp98416_0758.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAFGIDGIV.
PhylomeDBQ6FDW0.
ProtClustDBCLSK830527.

Enzyme and pathway databases

BioCycASP62977:ACIAD0848-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. 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_ACIAD
AccessionPrimary (citable) accession number: Q6FDW0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 57 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