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B1VG01 (DNLJ_CORU7) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. 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:cu0730
OrganismCorynebacterium urealyticum (strain ATCC 43042 / DSM 7109) [Complete proteome] [HAMAP]
Taxonomic identifier504474 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length712 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 – 712712DNA ligase HAMAP MF_01588
PRO_0000380349

Regions

Domain624 – 71289BRCT
Nucleotide binding53 – 575NAD By similarity
Nucleotide binding104 – 1052NAD By similarity

Sites

Active site1311N6-AMP-lysine intermediate By similarity
Metal binding4261Zinc By similarity
Metal binding4291Zinc By similarity
Metal binding4451Zinc By similarity
Metal binding4511Zinc By similarity
Binding site1291NAD By similarity
Binding site1521NAD By similarity
Binding site1921NAD By similarity
Binding site3081NAD By similarity
Binding site3321NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
B1VG01 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: B827F1FDE886F32B

FASTA71277,277
        10         20         30         40         50         60 
MSTQYDSDSS PAASNSGSAD PALAELAQQW QSLADQVRHH REVYYYGNPE ISDAEFDALL 

        70         80         90        100        110        120 
TRLQEFENSH PEAVTGPSPT TEVAPSPPES SPFRNVDHQE PMLSLDNVFD TEQLSSWLDR 

       130        140        150        160        170        180 
TPAKTYLTEL KIDGASINLL YRNGVLELAL TRGDGTTGED ITHNARTLSD IPARLQPSED 

       190        200        210        220        230        240 
FPVPEIVEIR GEVFIRVEDF AKMNAQRQAE GQKMFANPRN AAAGAMRQKD PAETARRPLR 

       250        260        270        280        290        300 
LICHGIGARE GFTPASQHAA YEALAAWGLP VSPYTKQVHS AKEVLEQVAY WADHRHDADH 

       310        320        330        340        350        360 
EMDGLVIKVD DTESQQRLGT TSRAPRWAIA YKYPPEEART RLHDIRLGIG RTGRATPYAV 

       370        380        390        400        410        420 
MEPKYVAGST VTMATLHNPS EAHRKGVRLG DEIMIRKAGE VIPEVLGPVE DARNGAEREF 

       430        440        450        460        470        480 
LFSSLCPECG TPLAPARGDD ADWRCPNTRY CPGQLHTRLT YIAGRGAFDI DALGEKAAYD 

       490        500        510        520        530        540 
LIHSGVLPDE TGLFSLTEED LRRTDAYTTK SGALNKQGET LLTTLAAAKE VDLWRVIVAL 

       550        560        570        580        590        600 
SIRHVGPTAA KALANHYGSI PDVAAADVET MSTVDGVGPI IAESVRDWFA VSWHQEIVDA 

       610        620        630        640        650        660 
WAAAGVRMEQ DVTEQPSADA AGSIQADLLA GLSIVVTGTL EDFDRSSAKE AIESRGGKAT 

       670        680        690        700        710 
GSVSKKTDYL VAGAKAGSKL TKAEELGIPV LDEAGFHKLL SEGPGKGDAE ED

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References

[1]"The lifestyle of Corynebacterium urealyticum derived from its complete genome sequence established by pyrosequencing."
Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A., Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J., Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M., Puehler A.
J. Biotechnol. 136:11-21(2008) [PubMed: 18367281] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43042 / DSM 7109.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM942444 Genomic DNA. Translation: CAQ04690.1.
RefSeqYP_001800124.1. NC_010545.1.

3D structure databases

ProteinModelPortalB1VG01.
SMRB1VG01. Positions 25-336.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1VG01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6184981.
GenomeReviewsGene locus cu0730 in contig AM942444_GR.
KEGGcur:cur_0730.
PATRIC21521184. VBICorUre58120_0731.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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. 2 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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDNLJ_CORU7
AccessionPrimary (citable) accession number: B1VG01
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 32 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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