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Q81IP2 (DNLJ_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. 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:BC_0341
OrganismBacillus cereus (strain ATCC 14579 / DSM 31)
Taxonomic identifier226900 [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
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 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_0000313124

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
Q81IP2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: AF60142EC4F0563E

FASTA66975,199
        10         20         30         40         50         60 
MSKEIAKKRI EELRDLLNTF NYQYHVLDNP SVSDAEYDRN MQELIKLEAE NPEFMSEDSP 

        70         80         90        100        110        120 
SVRVGGTVLD IFEKVTHKSP MLSLGNAFNE GDLRDFDRRV RQGIDGANVR YICELKIDGL 

       130        140        150        160        170        180 
AVSLHYEKGR FIQGATRGDG VTGEDITQNL KTIKAIPLRL NEEVTLEARG EAYMPKRSFV 

       190        200        210        220        230        240 
KLNEEKEQNG EDVFANPRNA AAGSIRQLDP KIAAKRNLSM FVYGLANVEE KTIPSHSESL 

       250        260        270        280        290        300 
DFLGELGFKT NPNRRTCETI EEVIAYVEEW QEKRPHLDYE IDGIVIKVDD VALQESLGTT 

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

       370        380        390        400        410        420 
IREKDIRIGD YVVVKKAGDI IPEVVNVIFD KRTGEEEEYR MPTHCPACES ELVRLEEEVA 

       430        440        450        460        470        480 
LRCINPTCPA QIREGLIHFV SRNAMNIDGL GERVITQLFD ADYIRTFADL YALTKEQLLQ 

       490        500        510        520        530        540 
LERFGEKSAT NLIQAIENSK ENSLERLLFG LGIRHVGAKA ARTFAEHFET MDELVKATEE 

       550        560        570        580        590        600 
ELKAINEIGE KMAQSVVTYF DNEDVLELLQ QFKEYGVNMT YKGIKIADLQ NVESYFAGKT 

       610        620        630        640        650        660 
VVLTGKLEVM GRSEAKKKIE ALGGKVTGSV SKSTDLVVAG EAAGSKLAQA EKHNVEVWNE 


ERFLQELNK

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016877 Genomic DNA. Translation: AAP07381.1.
RefSeqNP_830180.1. NC_004722.1.

3D structure databases

HSSPHSSP built from PDB template 1B04 based on UniProtKB O87703.
ProteinModelPortalQ81IP2.
SMRQ81IP2. Positions 1-315.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ81IP2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000033310; EBBACP00000032516; EBBACG00000033301.
GeneID1202694.
GenomeReviewsGene locus BC_0341 in contig AE016877_GR.
KEGGbce:BC0341.
PATRIC32596310. VBIBacCer54481_0312.

Phylogenomic databases

eggNOGCOG0272.
GeneTreeEBGT00050000002892.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBQ81IP2.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycBCER226900:BC_0341-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_BACCR
AccessionPrimary (citable) accession number: Q81IP2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 63 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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