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Q6NHQ4 (DNLJ_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:DIP1077
OrganismCorynebacterium diphtheriae [Complete proteome] [HAMAP]
Taxonomic identifier1717 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length677 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 – 677677DNA ligase HAMAP MF_01588
PRO_0000313205

Regions

Domain596 – 67782BRCT
Nucleotide binding35 – 395NAD By similarity
Nucleotide binding85 – 862NAD By similarity

Sites

Active site1121N6-AMP-lysine intermediate By similarity
Metal binding4071Zinc By similarity
Metal binding4101Zinc By similarity
Metal binding4261Zinc By similarity
Metal binding4321Zinc By similarity
Binding site1101NAD By similarity
Binding site1331NAD By similarity
Binding site1731NAD By similarity
Binding site2891NAD By similarity
Binding site3131NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NHQ4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: A3DB72254B796666

FASTA67774,766
        10         20         30         40         50         60 
MTDNFADLRR QWDDLAEQVR HHRDAYYNHT PEISDAEFDQ LFRQLQQLEQ EHPELAVPES 

        70         80         90        100        110        120 
PTLRVGAPVE QSSFDNVEHL ERMLSLDNVF DAAELDDWLQ RTPSATYLTE LKIDGLSIDL 

       130        140        150        160        170        180 
VYRSGRLERA ATRGDGRVGE DVTANAKVIE DIPHRLQHSD AYPVPELVEI RGEVFIAVED 

       190        200        210        220        230        240 
FALVNEQRQK EGGKPFANPR NAAAGSLRQK DTEAVRKRRL KMICHGIGAS EGFEADTQFD 

       250        260        270        280        290        300 
AYKALEAWGL PVSPYTKRVH SAQEVQERVT YWAQHRHDAT HEMDGLVIKI DSFAEQRALG 

       310        320        330        340        350        360 
STARAPRWAI AYKYPPEEVT TKLLDIQVGV GRTGRVTPFA VMDPVFVAGS TVEMATLHNQ 

       370        380        390        400        410        420 
TEVKRKGVLI GDTVVIRKAG EVIPEVLGPV VEKRDGSERE FIFPTLCPAC GTRLAPQKED 

       430        440        450        460        470        480 
DADWRCPNSQ SCPAQLSSRL TYLAGRGAFD IEALGEKGAE DLIASGVLID EAQLFNLTED 

       490        500        510        520        530        540 
DLKRTKVYTT KAGALNATGE KLLANLESAK HTDLWRVLVA LSIRHVGPTA ARALAVRYRS 

       550        560        570        580        590        600 
LEALRAADVE DIANTEGVGA IIAQSFAQWF DVPWHRNIVE VWADAGVTMA DSEADIPDQV 

       610        620        630        640        650        660 
LEGLTIVVTG SLVDFSRDSA KEAIVSRGGK ASGSVSKKTS YVVVGENAGS KETKARDLGL 

       670 
RILNEDEFKQ LLANGTV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248357 Genomic DNA. Translation: CAE49600.1.
RefSeqNP_939438.1. NC_002935.2.

3D structure databases

HSSPHSSP built from PDB template 1ZAU based on UniProtKB P63973.
ProteinModelPortalQ6NHQ4.
SMRQ6NHQ4. Positions 6-317.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2649337.
GenomeReviewsGene locus DIP1077 in contig BX248353_GR.
KEGGcdi:DIP1077.
NMPDRfig|257309.1.peg.1029.
PATRIC21483337. VBICorDip47633_1061.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBQ6NHQ4.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycCDIP257309:DIP1077-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_CORDI
AccessionPrimary (citable) accession number: Q6NHQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 53 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