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Reviewed, UniProtKB/Swiss-Prot A8FAQ1 (DNLJ_BACP2)

Last modified February 9, 2010. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: BPUM_0626
OrganismBacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]
Taxonomic identifier315750 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length668 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 668668DNA ligase HAMAP MF_01588
PRO_0000340328

Regions

Domain590 – 66879BRCT
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
A8FAQ1-1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: A140C45364E650CB

FASTA66874,781
        10         20         30         40         50         60 
MDKEAAKRRI EELHEILNQY NYEYHTLDRP SVPDAEYDAR MRELISLEEE HPDLKAADSP 

        70         80         90        100        110        120 
SQRVGGAVLD AFQKVRHGTP MLSLGNAFNE QDLLDFDRRV RQAVGDDIAY NVELKIDGLA 

       130        140        150        160        170        180 
VSLRYENGVF VRGATRGDGT TGEDITENLK TIRSIPLKIK RPLSIEVRGE AFMPKPSFEA 

       190        200        210        220        230        240 
LNEKRLQNEE EPFANPRNAA AGSLRQLDTK IAAKRNLDIF VYSIAELDEI GVESQSEGLD 

       250        260        270        280        290        300 
LLDELGFKTN KERRTCQTIE EVIELIETLK TKRADFSYEI DGIVIKVDSL AQQEELGFTA 

       310        320        330        340        350        360 
KSPRWAVAYK FPAEEVVTKL LDIELSVGRT GVITPTAILE PVKVAGTTVQ RASLHNEDLI 

       370        380        390        400        410        420 
KEKDIRLLDQ VIVKKAGDII PEVAGVLIDQ RTGEEKPFHM PTECPECHSE LVRIEGEVAL 

       430        440        450        460        470        480 
RCINPECPAQ IREGLIHFVS RNAMNIDGLG ERVITQLFKE QLVSRVSDLY RLTKEELIQL 

       490        500        510        520        530        540 
ERMGEKSVEN LLRSIEQSKE NSLERLLFGL GIRFIGSKAA KTLALHFGDI DQLKQATKEQ 

       550        560        570        580        590        600 
LLEVDEIGEK MADAVVTYFE KEEILNLLNE LKELGVNMTY TGPKPVKVEE SDSYFAGKTI 

       610        620        630        640        650        660 
VLTGKLEEMA RNDAKAAIEA LGGKLAGSVS KKTDLVIAGE AAGSKLTKAE ELNIEIWDEV 


KMLEELKK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000813 Genomic DNA. Translation: ABV61318.1.
RefSeqYP_001485878.1.

3D structure databases

SMRA8FAQ1. Positions 1-580, 576-666.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8FAQ1.

Genome annotation databases

GeneID5619874.
GenomeReviewsGene locus BPUM_0626 in contig CP000813_GR.
KEGGbpu:BPUM_0626.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAIKHFASR.

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.
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]
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_BACP2
AccessionPrimary (citable) accession number: A8FAQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: November 13, 2007
Last modified: February 9, 2010
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents