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Q5WJ30 (DNLJ_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. 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:ABC1087
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length671 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 – 671671DNA ligase HAMAP MF_01588
PRO_0000313126

Regions

Domain590 – 67182BRCT
Nucleotide binding34 – 385NAD By similarity
Nucleotide binding83 – 842NAD By similarity

Sites

Active site1151N6-AMP-lysine intermediate By similarity
Metal binding4041Zinc By similarity
Metal binding4071Zinc By similarity
Metal binding4221Zinc By similarity
Metal binding4271Zinc By similarity
Binding site1131NAD By similarity
Binding site1361NAD By similarity
Binding site1701NAD By similarity
Binding site2861NAD By similarity
Binding site3101NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WJ30 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 3ECBA04BDCF5F403

FASTA67174,638
        10         20         30         40         50         60 
MDKHQAEKRL KELRLLLEDY GYHYYVLDTP KVPDSEYDRL MNELLQLEAD YPDLVTEDSP 

        70         80         90        100        110        120 
SVRIGGPPAP SFKKVAHRVP MMSLSNAFNE EDLRAFDRRV RQAVGEHVSY VCELKFDGLA 

       130        140        150        160        170        180 
VSLTYENGKL VRGATRGDGT IGEDITNNLR TVPAIPLRLK QPYSIEVRGE AYMPKASFER 

       190        200        210        220        230        240 
LNEAKEQAGE EKFANPRNAA AGSLRQLDPK IAAKRNLSLF AYSIGEVEGK NVQTHFDSLM 

       250        260        270        280        290        300 
FLKELGFKVN EEAAECETIE DVIAYTEKWS ERRHELPYEI DGVVVKVNSL ADHEKLGFTA 

       310        320        330        340        350        360 
KSPRWATAFK FPAEEVLTVL RDIELNVGRT GVVTPTALLD PVLVAGTTVR RASLHNEDLI 

       370        380        390        400        410        420 
REKDVKLGDT VIVKKAGDII PEVVGVLTDK RTGEEVDFHM PTECPECHSV LERLEGEVAL 

       430        440        450        460        470        480 
RCLNPKCPAQ IREGLIHFVS RNAMNIDGLG EKVISQLFLH QLIADVADLY LLEREELLQL 

       490        500        510        520        530        540 
ERMGEKSVDN LLAAIEASKE NSLERLLFGL GIRFVGAKAA KTLAYEFETM ERLQEATFEQ 

       550        560        570        580        590        600 
LLAVNEIGEK MADSIVSYFQ KPEVATLLEK LANAGVNMTY TGPKKAAIAE EAGVFAGKTV 

       610        620        630        640        650        660 
VLTGKLSQWT RKEAQEKIEA LGGTVTGSVS KKTDLVVAGE DAGSKQKKAE SIGIEIWTEE 

       670 
QFTQAVEQSE Q

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References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KSM-K16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP006627 Genomic DNA. Translation: BAD63625.1.
RefSeqYP_174586.1. NC_006582.1.

3D structure databases

HSSPHSSP built from PDB template 1B04 based on UniProtKB O87703.
ProteinModelPortalQ5WJ30.
SMRQ5WJ30. Positions 1-314.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5WJ30.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000048996; EBBACP00000047757; EBBACG00000048987.
GeneID3204072.
GenomeReviewsGene locus ABC1087 in contig AP006627_GR.
KEGGbcl:ABC1087.
NMPDRfig|66692.3.peg.651.
PATRIC18921550. VBIBacCla58185_1163.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
GeneTreeEBGT00050000002892.
HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycBCLA66692:ABC1087-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_BACSK
AccessionPrimary (citable) accession number: Q5WJ30
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 23, 2004
Last modified: January 25, 2012
This is version 55 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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