Skip Header

Contribute Send feedback
Read comments (?) or add your own

A7GKJ1 (DNLJ_BACCN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 35. 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
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:Bcer98_0286
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length669 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 – 669669DNA ligase HAMAP MF_01588
PRO_0000340327

Regions

Domain591 – 66979BRCT
Nucleotide binding34 – 385NAD By similarity
Nucleotide binding83 – 842NAD By similarity

Sites

Active site1161N6-AMP-lysine intermediate By similarity
Metal binding4051Zinc By similarity
Metal binding4081Zinc By similarity
Metal binding4231Zinc By similarity
Metal binding4281Zinc By similarity
Binding site1141NAD By similarity
Binding site1371NAD By similarity
Binding site1711NAD By similarity
Binding site2871NAD By similarity
Binding site3111NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A7GKJ1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: D7DB9AF24A370B8E

FASTA66974,934
        10         20         30         40         50         60 
MSKEAVQQRI EELRDLLNTF NYQYHVLDNP SVSDAEYDRN MQELIKLETE NPEFITEDSP 

        70         80         90        100        110        120 
SVRVGGAVLD IFEKVTHKSP MLSLGNAFNE GDLRDFDRRV RQGIDGVNVR YICELKIDGL 

       130        140        150        160        170        180 
AVSLHYEKGR FIQGSTRGDG ITGEDITQNL KTIKAIPLRL QEEVTLEVRG EAYMPKRSFV 

       190        200        210        220        230        240 
KLNEEKEQNG EAVFANPRNA AAGSLRQLDP KIAAKRNLSM FVYGLADIEG KTITSHSEAL 

       250        260        270        280        290        300 
DFLGELGFKT NPNRRICETI EEVIAYVEEW QEKRPNLDYE IDGIVIKVDD VTLQERLGTT 

       310        320        330        340        350        360 
AKSPRWAIAY KFPAEEVVTR LTGIELSVGR TGVVTPTAEL EPVRVAGTIV RRASLHNEDL 

       370        380        390        400        410        420 
IREKDIRIGD YVVVKKAGDI IPEVVNVVFD KRTGKEEAYH MPTHCPTCDS GLVRLEEEVA 

       430        440        450        460        470        480 
LRCINPACPA QIREGLIHFV SRNAMNIDGL GERVITQLFE ANYIRTFADL YGLTKDQLLQ 

       490        500        510        520        530        540 
LDRFGEKSAS NLVQAIEASK ENSLERLLFG LGIRHVGAKA ARTLAEHFET MDNLVKAGEE 

       550        560        570        580        590        600 
ELKAINEIGE KMAQSIVTYF DNEDVLHLIQ QFKDYGVNMT YKGIKRADLQ NIASYFAGKT 

       610        620        630        640        650        660 
VVLTGKLEVM GRSEAKKKIE ALGGKVTGSV SKSTDLVIAG EAAGSKLAQA EKHNIEIWNE 


ERFLQELNK

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NVH 391-98.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000764 Genomic DNA. Translation: ABS20649.1.
RefSeqYP_001373644.1. NC_009674.1.

3D structure databases

ProteinModelPortalA7GKJ1.
SMRA7GKJ1. Positions 1-315.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7GKJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000038784; EBBACP00000037835; EBBACG00000038775.
GeneID5344721.
GenomeReviewsGene locus Bcer98_0286 in contig CP000764_GR.
KEGGbcy:Bcer98_0286.
PATRIC18928846. VBIBacCyt128034_0311.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
GeneTreeEBGT00050000002892.
HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycBCER315749:BCER98_0286-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. 3 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_BACCN
AccessionPrimary (citable) accession number: A7GKJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: September 11, 2007
Last modified: December 14, 2011
This is version 35 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents