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A8IGY0 (DNLJ_AZOC5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. 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:AZC_0149
OrganismAzorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / ORS 571) [Complete proteome] [HAMAP]
Taxonomic identifier438753 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Xanthobacteraceae › Azorhizobium

Protein attributes

Sequence length739 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 – 739739DNA ligase HAMAP MF_01588
PRO_0000340326

Regions

Domain662 – 73978BRCT
Nucleotide binding51 – 555NAD By similarity
Nucleotide binding100 – 1012NAD By similarity

Sites

Active site1361N6-AMP-lysine intermediate By similarity
Metal binding4401Zinc By similarity
Metal binding4431Zinc By similarity
Metal binding4641Zinc By similarity
Metal binding4701Zinc By similarity
Binding site1341NAD By similarity
Binding site1571NAD By similarity
Binding site1941NAD By similarity
Binding site3111NAD By similarity
Binding site3351NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A8IGY0 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: C74D235705EB8134

FASTA73980,556
        10         20         30         40         50         60 
MTANRPALPT RDKAVSDLSA TEASDEHAAL SQEIASHDAR YYQEDAPVIS DADYDRLRRR 

        70         80         90        100        110        120 
YEDIEARFPA LKNDDSLSRK VGAAPSAKFA KVVHQVPMLS LQNAFSDEEV EEFVARVRRF 

       130        140        150        160        170        180 
LNLAESAELA FTAEPKIDGL SCSLRYEGGV LVRAATRGDG TQGEDVTANV RTIAEIPHRL 

       190        200        210        220        230        240 
TGAGVPDIID IRGEVYMGKA DFLALNARQE EAGKPVFANP RNAAAGSLRQ LDPEITRSRP 

       250        260        270        280        290        300 
LRFFAYAWGQ AEPGPPGASQ HEVVDAFRRF GLPTNPLTIR VTDAAGLLAH YRKIGAERAS 

       310        320        330        340        350        360 
LGYDIDGVVY KVDSLALQER LGFVSRSPRW AIAHKFAAEQ ATTVIEAIEI QVGRTGALTP 

       370        380        390        400        410        420 
VAKLTPVTVG GVVVSNATLH NEDYIRAIGG NGEEIREGID IRVGDTVVVQ RAGDVIPQVV 

       430        440        450        460        470        480 
SVVLDKRPAG ATAYQFPHHC PVCNSQAVRE VDPKTGKQDA VRRCTGGLIC PAQAVERLRH 

       490        500        510        520        530        540 
FVSRNAFDIE GLGEKQAHAF YEWKLIAEPA DIFRLQARNE QSLSKLENRE GWGRTSAQNL 

       550        560        570        580        590        600 
FAAIEARRTI ALDRFIFALG IRHVGETNAK RLARHYGSVE ALRDAAIGAE MPTEMEEASE 

       610        620        630        640        650        660 
ETPPTRRRKP QGNEVWQEMT DIDGIGAVVA EAVVEFFREP HNRQVVEELL KEVTPQPLEA 

       670        680        690        700        710        720 
VASTSPVSGK TVVFTGSLER MTRDEAKAMA ERLGAKVAGS VSGKTDLLVA GPGAGSKLEK 

       730 
ARSLGVKTIT EDEWFDLVG

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References

[1]"Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium caulinodans ORS571."
Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43989 / DSM 5975 / ORS 571.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009384 Genomic DNA. Translation: BAF86147.1.
RefSeqYP_001523065.1. NC_009937.1.

3D structure databases

ProteinModelPortalA8IGY0.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8IGY0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5691128.
GenomeReviewsGene locus AZC_0149 in contig AP009384_GR.
KEGGazc:AZC_0149.
PATRIC21016737. VBIAzoCau17976_0153.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBCLSK979523.

Enzyme and pathway databases

BioCycACAU438753:AZC_0149-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_AZOC5
AccessionPrimary (citable) accession number: A8IGY0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: December 4, 2007
Last modified: January 25, 2012
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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