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A0QUW7 (DNLJ_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 42. 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:MSMEG_2362
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length701 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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
Reference 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 – 701701DNA ligase HAMAP MF_01588
PRO_0000313312

Regions

Domain615 – 70187BRCT
Nucleotide binding49 – 535NAD By similarity
Nucleotide binding99 – 1002NAD By similarity

Sites

Active site1311N6-AMP-lysine intermediate By similarity
Metal binding4261Zinc By similarity
Metal binding4291Zinc By similarity
Metal binding4451Zinc By similarity
Metal binding4511Zinc By similarity
Binding site1291NAD By similarity
Binding site1521NAD By similarity
Binding site1921NAD By similarity
Binding site3081NAD By similarity
Binding site3321NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QUW7 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 3A37884B5D1DF931

FASTA70176,269
        10         20         30         40         50         60 
MSEKATGEVE AELPEHPDAD ERRRWQELAD EVREHQFRYY VKDAPIISDA EFDKLLRELQ 

        70         80         90        100        110        120 
ALEDAHPELR TPDSPTQLVG GAGFATEFAP AEHLERMLSL DNVFDSDELT AWAARISSET 

       130        140        150        160        170        180 
GDAAHFLCEL KIDGVALSLV YRDGRLERGA TRGDGRTGED VTLNARTIDD IPERLTPSDE 

       190        200        210        220        230        240 
FPVPAVLEVR GEVFFRVADF EELNAGLVAE GKPPFANPRN SAAGSLRQKN PAVTARRKLR 

       250        260        270        280        290        300 
MICHGIGYTE GFTPASLHDA YRALGAWGLP VSEHTTKVST VAEVAERIAY WGEHRHDVEH 

       310        320        330        340        350        360 
EIDGVVVKVD EVALQRRLGA TSRAPRWAVA YKYPPEEATT KLLDIRVNVG RTGRVTPFAY 

       370        380        390        400        410        420 
MEPVKVAGST VGLATLHNAS EVKRKGVLIG DTVVIRKAGD VIPEVLGPVV DLRDGTEREF 

       430        440        450        460        470        480 
EFPTHCPECG TELAPAKEGD ADIRCPNSRS CPAQLRERLF HLAGRGAFDI EGLGYEAATA 

       490        500        510        520        530        540 
LLAAQVIPDE GDLFTLTADD LLRTELFTTK KGELSANGKR LLANLTKAKE QPLWRVLVAL 

       550        560        570        580        590        600 
SIRHVGPTAA RALATEFGSL EAIEAASEEE LAAVEGVGPT IAAAVKDWFT VDWHRAIVDK 

       610        620        630        640        650        660 
WRAAGVRMAD ERDASIERTL EGLSIVVTGS LAGFSRDQAK EAIIARGGKA AGSVSKKTAY 

       670        680        690        700 
VVAGDAPGSK YDKAVELGVP VLDEDGFRRL LEQGPPVEPA E

« Hide

References

[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[2]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed: 18955433] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000480 Genomic DNA. Translation: ABK72497.1.
RefSeqYP_886705.1. NC_008596.1.

3D structure databases

ProteinModelPortalA0QUW7.
SMRA0QUW7. Positions 23-336.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0QUW7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000044174; EBMYCP00000042511; EBMYCG00000044169.
GeneID4535192.
GenomeReviewsGene locus MSMEG_2362 in contig CP000480_GR.
KEGGmsm:MSMEG_2362.
NMPDRfig|246196.1.peg.2361.
PATRIC18077148. VBIMycSme59918_2328.
TIGRMSMEG_2362.

Phylogenomic databases

eggNOGCOG0272.
GeneTreeEBGT00050000016652.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBA0QUW7.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycMSME246196:MSMEG_2362-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. 2 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_MYCS2
AccessionPrimary (citable) accession number: A0QUW7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 42 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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