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Q0VR01 (DNLJ_ALCBS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:ABO_0949
OrganismAlcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]
Taxonomic identifier393595 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length777 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 – 777777DNA ligase HAMAP MF_01588
PRO_0000313107

Regions

Domain691 – 77787BRCT
Nucleotide binding35 – 395NAD By similarity
Nucleotide binding84 – 852NAD By similarity

Sites

Active site1181N6-AMP-lysine intermediate By similarity
Metal binding4111Zinc By similarity
Metal binding4141Zinc By similarity
Metal binding4291Zinc By similarity
Metal binding4351Zinc By similarity
Binding site1161NAD By similarity
Binding site1391NAD By similarity
Binding site1761NAD By similarity
Binding site2931NAD By similarity
Binding site3171NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0VR01 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 0A60F808E9D10703

FASTA77784,628
        10         20         30         40         50         60 
MTNNNDPSLQ AQSLRDQLND WSYRYYVQDD PAVPDAEYDR VFRALKDLEA QYPDLVTADS 

        70         80         90        100        110        120 
PTQRVGDVPL DAFEQVQHEV PMLSLDNAFD DEELWAFDKR IRERLDVSEI IDYVAEPKLD 

       130        140        150        160        170        180 
GLAVSLLYEN GELVRAATRG DGQTGENITV NARTIRSVPL KLRGNDVPKR LEVRGEVVMP 

       190        200        210        220        230        240 
HAGFEELNAR QQEAGLKLFA NPRNAAAGSL RQLDSRITAS RPLEFYAYSM AQLEGWEHPP 

       250        260        270        280        290        300 
THSAMLDALR DWGLRVNPEI RVCHGVEALL RFYQGILEKR EHLDYDIDGV VYKVNRFDWQ 

       310        320        330        340        350        360 
DDLGFVSRAP RWAIAHKFPA QEELTVLNGV DWQVGRTGAL TPVARLEPVH VGGVIVSNAT 

       370        380        390        400        410        420 
LHNIDEIQRL DIRIGDTVVV YRAGDVIPKV VRALPERRPA NAQGIALPSS CPVCGSEILR 

       430        440        450        460        470        480 
GHDQVVARCT GGLICGDQRR EAIKHFASRR AMDIDGLGDK LVDALVDQEL ITTVADLYRL 

       490        500        510        520        530        540 
KAEQVAGLER MGEKSADNLI AALEASKTVG LGRFLFALGI LQIGEETAKN LADCFGDLDS 

       550        560        570        580        590        600 
IRHAPLLLLL AVPDVGLEVA KAIGAFFAES DNEAVIDGLL AQGVSPQASG VPSAAFVKSL 

       610        620        630        640        650        660 
TLAQLLKSAK RLGMNLEGIG DKSLDILGSH FRTVTELSAA AAEGAGAEPK GVRSGVMTQL 

       670        680        690        700        710        720 
AKALAENDWR GRLQDAEKKV ADMAARAPQE MESQPLEGQT WVLTGTLEQF TRNQAKQALQ 

       730        740        750        760        770 
QLGAKVAGSV SKNTRMVVAG ASAGSKLAKA ESLGIEVCDE AALLSLLNQH GIDPGAL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM286690 Genomic DNA. Translation: CAL16397.1.
RefSeqYP_692669.1. NC_008260.1.

3D structure databases

ProteinModelPortalQ0VR01.
SMRQ0VR01. Positions 9-588.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0VR01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4211547.
GenomeReviewsGene locus ABO_0949 in contig AM286690_GR.
KEGGabo:ABO_0949.
NMPDRfig|393595.12.peg.949.
PATRIC20839605. VBIAlcBor124741_0995.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBQ0VR01.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycABOR393595:ABO_0949-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_ALCBS
AccessionPrimary (citable) accession number: Q0VR01
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: January 25, 2012
This is version 44 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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