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Q6MRL9 (DNLJ_BDEBA) 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:Bd0057
OrganismBdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) [Complete proteome] [HAMAP]
Taxonomic identifier264462 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Bdellovibrionales › Bdellovibrionaceae › Bdellovibrio

Protein attributes

Sequence length684 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 – 684684DNA ligase HAMAP MF_01588
PRO_0000313138

Regions

Domain609 – 68476BRCT
Nucleotide binding48 – 525NAD By similarity
Nucleotide binding97 – 982NAD By similarity

Sites

Active site1311N6-AMP-lysine intermediate By similarity
Metal binding4291Zinc By similarity
Metal binding4321Zinc By similarity
Metal binding4471Zinc By similarity
Metal binding4521Zinc By similarity
Binding site1291NAD By similarity
Binding site1521NAD By similarity
Binding site1891NAD By similarity
Binding site3101NAD By similarity
Binding site3341NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MRL9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 13D2D1EA6E27D60D

FASTA68476,371
        10         20         30         40         50         60 
MPDAFCRDWT SEMGANYSMS KKRHEELKKI ISEHDHNYHV LDKPTITDYE YDQLFAELLD 

        70         80         90        100        110        120 
IEKNPKGLDL SDSPSQRVGG TVLEGFTKAQ HRLPMLSLAN SYSPEDIFEF DERVRKFLNT 

       130        140        150        160        170        180 
EDPVEYLCEL KFDGLSMELI YENGQLVRAI TRGDGTVGED VTHNIKTIKS IPLKLSHKNP 

       190        200        210        220        230        240 
PPLLEVRGEV LMFKEDFARL NETQQENGQQ TFANPRNAAA GTVRQLDSRI AASRPLRFFG 

       250        260        270        280        290        300 
YALGAVEGET FNTQKNIQEY FNDHGIPTVL PYKEDLLVVA KGPEEVVKYY HHIEKVRPKL 

       310        320        330        340        350        360 
PFDIDGVVIK VNSLRLQEDL GLVARSPRWA TAAKFKPEQA QTTVEDIVVQ VGRTGALTPV 

       370        380        390        400        410        420 
AIMKPVKVGG VTVTNATLHN QDEITRKDIR IGDTVIIQRA GDVIPEVVEV VNPDKRPADR 

       430        440        450        460        470        480 
LPYSIPERCP ACDSVAVKAE GEVVTRCVNP LCIAVVKESL KHFVARRAMN IDKVGDRLIE 

       490        500        510        520        530        540 
TLVDNKLLTR FSDFYRLTKE QILSLERQGD KSADNIIKSI ENSKNPTLAR FIFALGIRFV 

       550        560        570        580        590        600 
GEQTGKHLAD HFLTIDKFLE ASEEELLQVP EIGAKVAKSI RDWTGNPKLV DEVKAMIELG 

       610        620        630        640        650        660 
VKIAGPVRAQ EGSLSGMSFL ITGTLPVKRD DAKDLIERNG GKILGSVSSK LNYLVVGDDP 

       670        680 
GSKVEKAQGL GVKIISWEEL QAMI

« Hide

References

[1]"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
Science 303:689-692(2004) [PubMed: 14752164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15356 / DSM 50701 / NCIB 9529 / HD100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842646 Genomic DNA. Translation: CAE77738.1.
RefSeqNP_967084.1. NC_005363.1.

3D structure databases

HSSPHSSP built from PDB template 1B04 based on UniProtKB O87703.
ProteinModelPortalQ6MRL9.
SMRQ6MRL9. Positions 610-684.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2734257.
GenomeReviewsGene locus Bd0057 in contig BX842601_GR.
KEGGbba:Bd0057.
NMPDRfig|264462.1.peg.54.
PATRIC21074916. VBIBdeBac73187_0053.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG620317.
OMAPEYICEL.
PhylomeDBQ6MRL9.

Enzyme and pathway databases

BioCycBBAC264462:BD0057-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_BDEBA
AccessionPrimary (citable) accession number: Q6MRL9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 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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