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Q8NR20 (DNLJ_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. 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:Cgl1244, cg1401
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length680 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
Reference 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 – 680680DNA ligase HAMAP MF_01588
PRO_0000313206

Regions

Domain597 – 68084BRCT
Nucleotide binding35 – 395NAD By similarity
Nucleotide binding86 – 872NAD By similarity

Sites

Active site1131N6-AMP-lysine intermediate By similarity
Metal binding4081Zinc By similarity
Metal binding4111Zinc By similarity
Metal binding4271Zinc By similarity
Metal binding4331Zinc By similarity
Binding site1111NAD By similarity
Binding site1341NAD By similarity
Binding site1741NAD By similarity
Binding site2901NAD By similarity
Binding site3141NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NR20 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: F96FB7AE7F6D01C4

FASTA68074,706
        10         20         30         40         50         60 
MTEDNAQLRR TWNDLAEKVR YHRDRYYNEQ PEIPDADFDA LFKQLQQLEE DHPELAVPDS 

        70         80         90        100        110        120 
PTMVVGAPVA EQSSFDNVEH LERMLSLDNV FDEQELRDWL GRTPAKQYLT ELKIDGLSID 

       130        140        150        160        170        180 
LVYRNGQLER AATRGDGRVG EDITANARVI EDIPHQLQGT DEYPVPAVLE IRGEVFITVE 

       190        200        210        220        230        240 
DFPEVNAQRI ADGGKPFANP RNAAAGSLRQ KNIEDVKKRR LRMISHGIGF TEGFSPASQH 

       250        260        270        280        290        300 
DAYLALAAWG LPTSPYTEAV TDPEDVVKKV SYWADHRHDA LHEMDGLVIK VDDIASQRAL 

       310        320        330        340        350        360 
GSTSRAPRWA IAYKYPPEEV TTKLLDIQVG VGRTGRVTPF AVMEPVLVAG STVSMATLHN 

       370        380        390        400        410        420 
QSEVKRKGVL IGDTVVIRKA GEVIPEVLGP VVELRDGTER EYIFPTLCPE CGTRLAPAKA 

       430        440        450        460        470        480 
DDVDWRCPNM QSCPGQLSTR LTYLAGRGAF DIEALGEKGA EDLIRTGILL DESGLFDLTE 

       490        500        510        520        530        540 
DDLLSSNVYT TNAGKVNASG KKLLDNLQKS KQTDLWRVLV ALSIRHVGPT AARALAGRYH 

       550        560        570        580        590        600 
SIQALIDAPL EELSETDGVG TIIAQSFKDW FEVDWHKAIV DKWAAAGVTM EEEVGEVAEQ 

       610        620        630        640        650        660 
TLEGLTIVVT GGLEGFTRDS VKEAIISRGG KASGSVSKKT DYVVIGENAG SKATKAEELG 

       670        680 
LRILDEAGFV RLLNTGSADE 

« Hide

References

[1]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB98637.1.
BX927151 Genomic DNA. Translation: CAF19947.1.
RefSeqNP_600467.1. NC_003450.3.
YP_225533.1. NC_006958.1.

3D structure databases

HSSPHSSP built from PDB template 1ZAU based on UniProtKB P63973.
ProteinModelPortalQ8NR20.
SMRQ8NR20. Positions 7-318.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1019226.
3344018.
GenomeReviewsGene locus Cgl1244 in contig BA000036_GR.
Gene locus cg1401 in contig BX927147_GR.
KEGGcgb:cg1401.
cgl:NCgl1196.
PATRIC21494530. VBICorGlu203724_1221.

Phylogenomic databases

HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBQ8NR20.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycCGLU196627:CG1401-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.
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.
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_CORGL
AccessionPrimary (citable) accession number: Q8NR20
Secondary accession number(s): Q6M5U1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 67 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