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A4YZJ3 (DNLJ_BRASO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. 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:BRADO5649
OrganismBradyrhizobium sp. (strain ORS278) [Complete proteome] [HAMAP]
Taxonomic identifier114615 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length716 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 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 – 716716DNA ligase HAMAP MF_01588
PRO_0000313151

Regions

Domain638 – 71679BRCT
Nucleotide binding49 – 535NAD By similarity
Nucleotide binding98 – 992NAD By similarity

Sites

Active site1341N6-AMP-lysine intermediate By similarity
Metal binding4371Zinc By similarity
Metal binding4391Zinc By similarity
Metal binding4611Zinc By similarity
Metal binding4671Zinc By similarity
Binding site1321NAD By similarity
Binding site1551NAD By similarity
Binding site1921NAD By similarity
Binding site3081NAD By similarity
Binding site3321NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A4YZJ3 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 6FF31B580BF4E0B7

FASTA71679,735
        10         20         30         40         50         60 
MAKTAKSKQS VDVADLTKAQ AKVEWKRLAL ELETHDRLYY QEDAPKISDA AYDELRRRFN 

        70         80         90        100        110        120 
AIEKRFPELV SRDSPSQTVG AAPSGRFKKV RHAVPMLSLD NAFAEEDVRD FVGRIARFLK 

       130        140        150        160        170        180 
LAEDDRIAFS AEPKIDGLSM SLRYEGGQLV TAATRGDGAE GEDVTANIRT LKDVPQKLHG 

       190        200        210        220        230        240 
RNLPDICEIR GEVYMTKQAF LALNERQKEA GDTIFANPRN SAAGSLRQKD PTITASRPLG 

       250        260        270        280        290        300 
FFAYAWGDMS AMPAETQSGM IKWFEHCGFT TNPLTKLCHS VEELIAFHRA IEEQRAELDY 

       310        320        330        340        350        360 
DIDGVVYKVD RIDWQERLGF VSRTPRWGIA HKFPAERAMT VLKDIEIQVG RTGSFTPVGK 

       370        380        390        400        410        420 
LEPVGVGGVI VQNVTLHNED YIKGIGNKGE VLREGRDIRI GDTVVIQRAG DVIPQVVDVL 

       430        440        450        460        470        480 
IDKRPADAEV FAFPRKCPCP LHTDVVREET AAGEEGSRAR CTGEFACPYQ KIEHLKLFAS 

       490        500        510        520        530        540 
RRAFDIDGLG EKQIQFFFDE GWVKEPADIF TLQKRNAKLK LEEVEGYGET SVRNLFNAIE 

       550        560        570        580        590        600 
ARREMALERF IYALGMRYVG ETTALALARG YGSWEAFHDA CLKVANGDEE AIAEMDALDQ 

       610        620        630        640        650        660 
IGETVIKSVA AYFGEDHNRG IVERLTREVK ILDAEKPKRN SPIATKTVVF TGTLEKMTRD 

       670        680        690        700        710 
EAKATAERLG AKVSGSVSKK TDYVVAGPGA GSKLKDAEKH GVKVLTEDEW LQLIGE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU234118 Genomic DNA. Translation: CAL79319.1.
RefSeqYP_001207536.1. NC_009445.1.

3D structure databases

ProteinModelPortalA4YZJ3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4YZJ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5115430.
GenomeReviewsGene locus BRADO5649 in contig CU234118_GR.
KEGGbra:BRADO5649.
PATRIC21227255. VBIBraSp122330_5424.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBCLSK2516592.

Enzyme and pathway databases

BioCycBSP376:BRADO5649-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.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR010994. RuvA_2-like.
[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.
[Graphical view]
PIRSFPIRSF001604. LigA. 1 hit.
SMARTSM00292. BRCT. 1 hit.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDNLJ_BRASO
AccessionPrimary (citable) accession number: A4YZJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: December 14, 2011
This is version 36 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