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A0PPW9 (DNLJ_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 39. 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:MUL_1933
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length683 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 – 683683DNA ligase HAMAP MF_01588
PRO_0000313317

Regions

Domain595 – 68389BRCT
Nucleotide binding29 – 335NAD By similarity
Nucleotide binding79 – 802NAD By similarity

Sites

Active site1111N6-AMP-lysine intermediate By similarity
Metal binding4061Zinc By similarity
Metal binding4091Zinc By similarity
Metal binding4251Zinc By similarity
Metal binding4311Zinc By similarity
Binding site1091NAD By similarity
Binding site1321NAD By similarity
Binding site1721NAD By similarity
Binding site2881NAD By similarity
Binding site3121NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PPW9 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 1EDB4814BCF1B519

FASTA68374,625
        10         20         30         40         50         60 
MLRQWQELAE QVREHQFRYY VRDAPVITDA EFDELLRRLE ALEEQYPELR TPDSPTQLVG 

        70         80         90        100        110        120 
GAGFATEFEP VEHLERMLSL DNAFNTEELT AWAGRIHADV GDSAAYLCEL KIDGVALSLV 

       130        140        150        160        170        180 
YEGGRLTRAS TRGDGRTGED VTLNARTIED VPERLSHSED HRMPEVLEVR GEVFFRVADF 

       190        200        210        220        230        240 
QALNASLVEE GKAPFANPRN SAAGSLRQKD PAVTARRRLR MICHGLGHTE GFRPATLHQA 

       250        260        270        280        290        300 
YLALQAWGLP VSQHTTLVAD LAEVQARIDY WGEHRHEVDH EIDGVVVKVD DVALQRRLGS 

       310        320        330        340        350        360 
TSRAPRWAIA YKYPPEEAQT KLLDIRVNVG RTGRVTPFAF MTPVKVAGST VAQATLHNAS 

       370        380        390        400        410        420 
EVKRKGVLIG DTVVIRKAGD VIPEVLGPVV DLRDGSEREF VMPTTCPECG TPLAPEKEGD 

       430        440        450        460        470        480 
ADIRCPNTRS CPGQLRERVF HVSSRNALDI EMLGYEAGAA LLSARVIGDE GDLFGLTEEE 

       490        500        510        520        530        540 
LLRTDLFRTK AGDLSANGRR LLANLDKAKA APLWRVLVAL SIRHVGPTAA RALATEFGSI 

       550        560        570        580        590        600 
DAIVAATTEQ LAAVEGVGPT IASAVSEWFT VDWHREIVER WRAAGVRMAD ERDDSVPRTL 

       610        620        630        640        650        660 
AGVTVVVTGS LPGFSRDEAK EAIVTRGGKA AGSVSKKTSY VVAGDAPGSK YDKAVELGVP 

       670        680 
ILDEDGFRKL LEQGPPAEAG EPT

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed: 17210928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000325 Genomic DNA. Translation: ABL04388.1.
RefSeqYP_905859.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PPW9.
SMRA0PPW9. Positions 1-316.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0PPW9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000074479; EBMYCP00000072484; EBMYCG00000074474.
GeneID4551274.
GenomeReviewsGene locus MUL_1933 in contig CP000325_GR.
KEGGmul:MUL_1933.
PATRIC18170901. VBIMycUlc37413_2301.

Organism-specific databases

GenoListMUL_1933.
CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
GeneTreeEBGT00050000016652.
HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBPRK07956.

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_MYCUA
AccessionPrimary (citable) accession number: A0PPW9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 39 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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