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Reviewed, UniProtKB/Swiss-Prot Q1IHJ4 (DNLJ_ACIBL)

Last modified February 9, 2010. Version 33. 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: Acid345_4656
OrganismAcidobacteria bacterium (strain Ellin345) [Complete proteome] [HAMAP]
Taxonomic identifier204669 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaCandidatus Koribacter

Protein attributes

Sequence length673 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 – 673673DNA ligase HAMAP MF_01588
PRO_0000313097

Regions

Domain595 – 67379BRCT
Nucleotide binding35 – 395NAD By similarity
Nucleotide binding84 – 852NAD By similarity

Sites

Active site1171N6-AMP-lysine intermediate By similarity
Metal binding4151Zinc By similarity
Metal binding4181Zinc By similarity
Metal binding4331Zinc By similarity
Metal binding4381Zinc By similarity
Binding site1151NAD By similarity
Binding site1381NAD By similarity
Binding site1801NAD By similarity
Binding site2961NAD By similarity
Binding site3201NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1IHJ4-1 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 5FB4E95B477B6B86

FASTA67374,926
        10         20         30         40         50         60 
MSRTKDPAKQ AEDLREKLRY HEHRYYVLDD PEISDADYDV MMNELKALEA KHPELLTPDS 

        70         80         90        100        110        120 
PTQRVGGKPR EGFVKVAHSA PMLSLDNAYN EEELRDWARR VEELSGKAEI EYECELKLDG 

       130        140        150        160        170        180 
LSMALRYQDA RFVLAVTRGD GSIGEDVTLN LRTVKSVPLG VSSATLKKTH MLGDFEVRGE 

       190        200        210        220        230        240 
VIFPTKSFEK MNEDREKQGL AKFANPRNAA AGAVRVLEPN ITAQRRLDFY AYFLLVDGRV 

       250        260        270        280        290        300 
HIDRQSEALD TLEKLGFKVN SNRAVFKSID DVLKFIHKKE EDREKLPYEI DGVVIKVNST 

       310        320        330        340        350        360 
ALWQRLGFTG KAPRWAIAYK YAARAAVTQV EDILVQVGRT GKLTPVAALK PVPIGGTTVS 

       370        380        390        400        410        420 
RATLHNMDEI DRLGLLIGDW VQVERGGDVI PKVVKVIDDK DHPRGKKKFK MPERCPECGG 

       430        440        450        460        470        480 
HVVRTEGEAD HRCVNANCPA KLRESILHFA SRGVMNIEGM GDSLVNQLVD RGLVKNVADI 

       490        500        510        520        530        540 
YELDEEKLLS LERMGKKSAQ NILDEIKGTK KLPLERVIYG LGIRMVGERT AQFLAEHFGS 

       550        560        570        580        590        600 
LDGVMKATEE ELLEVEEVGP RIAQSIHEFF AEPSNRELVK RLEAAGLQFK GVKKERGTAL 

       610        620        630        640        650        660 
AGQTFVLTGS LPTYSRDEAK KLIEDAGGKV SGSVSKKTNY VVAGEEAGSK LDKARDLGVA 

       670 
VIDEDALKKL LGK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000360 Genomic DNA. Translation: ABF43656.1.
RefSeqYP_593730.1.

3D structure databases

SMRQ1IHJ4. Positions 6-323, 8-590, 596-671.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1IHJ4.

Genome annotation databases

GeneID4070813.
GenomeReviewsGene locus Acid345_4656 in contig CP000360_GR.
KEGGaba:Acid345_4656.
NMPDRfig|204669.6.peg.4633.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAIKHFASR.
PhylomeDBQ1IHJ4.

Enzyme and pathway databases

BioCycABAC204669:ACID345_4656-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.
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. False negative.
PS01056. DNA_LIGASE_N2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDNLJ_ACIBL
AccessionPrimary (citable) accession number: Q1IHJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 13, 2006
Last modified: February 9, 2010
This is version 33 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