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Q5LCI0 (DNLJ_BACFN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. 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:BF2485
OrganismBacteroides fragilis (strain ATCC 25285 / NCTC 9343) [Complete proteome] [HAMAP]
Taxonomic identifier272559 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length665 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 – 665665DNA ligase HAMAP MF_01588
PRO_0000313131

Regions

Domain587 – 66579BRCT
Nucleotide binding31 – 355NAD By similarity
Nucleotide binding80 – 812NAD By similarity

Sites

Active site1121N6-AMP-lysine intermediate By similarity
Metal binding4031Zinc By similarity
Metal binding4061Zinc By similarity
Metal binding4211Zinc By similarity
Metal binding4271Zinc By similarity
Binding site1101NAD By similarity
Binding site1331NAD By similarity
Binding site1701NAD By similarity
Binding site2851NAD By similarity
Binding site3091NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LCI0 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: BB108C3558699473

FASTA66575,329
        10         20         30         40         50         60 
MTVKEKIEQL RLQLHQHNYN YYVLNAPEIS DKEFDDLMRE LQDLEQEHPE YKDENSPTMR 

        70         80         90        100        110        120 
VGSDINKNFT QVAHKYPMLS LSNTYSENEV TDFYDRVRKA LNEDFEICCE MKYDGTSISL 

       130        140        150        160        170        180 
TYENGKLIRA VTRGDGEKGD DVTDNVKTIR SIPLVLHGDN YPEVFEIRGE ILMPWEVFEA 

       190        200        210        220        230        240 
LNREKEAREE PLFANPRNAA SGTLKLQNSA IVASRKLDAY LYYLLGDNLP TDGHYENLQE 

       250        260        270        280        290        300 
AAKWGFKISP LMRKCQTLQE VFDFINYWDV ERKNLNVATD GIVLKVNSLK QQRNLGFTAK 

       310        320        330        340        350        360 
SPRWAIAYKF QAERALTRLN MVTYQVGRTG AVTPVANLDP VQLSGTVVKR ASLHNADIIE 

       370        380        390        400        410        420 
GLDLHIGDMV YVEKGGEIIP KITGVDTSVR FMIGEKVKFI THCPECGSKL IRYEGEAAHY 

       430        440        450        460        470        480 
CPNETACPPQ IKGKIEHFIS RKAMNIDGLG PETVDMFYRL GLIHDTADLY QLTTDDIRGL 

       490        500        510        520        530        540 
DRMGDKSAEN IIKGIMQSKE VPFERVIFAL GIRFVGETVA KKIAKSFKDI EELENADLET 

       550        560        570        580        590        600 
LINIDEIGEK IARSILNYFA NESNRKLVDR LKTAGLQLYR PEEDLSGHTD KLAGQSIVIS 

       610        620        630        640        650        660 
GVFTHHSRDE YKDLIEKHGG KNVGSISSKT SFILAGDNMG PAKLEKASKL GIKIMNEEEF 


LKLIS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR626927 Genomic DNA. Translation: CAH08185.1.
RefSeqYP_212109.1. NC_003228.3.

3D structure databases

HSSPHSSP built from PDB template 1B04 based on UniProtKB O87703.
ProteinModelPortalQ5LCI0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5LCI0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3289219.
GenomeReviewsGene locus BF2485 in contig CR626927_GR.
KEGGbfs:BF2485.
PATRIC21041508. VBIBacFra29119_2491.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBCLSK2516787.

Enzyme and pathway databases

BioCycBFRA272559:BF2485-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. 4 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. False negative.
PS01056. DNA_LIGASE_N2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDNLJ_BACFN
AccessionPrimary (citable) accession number: Q5LCI0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 21, 2005
Last modified: January 25, 2012
This is version 49 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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