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Q1BAU4 (DNLJ_MYCSS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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:Mmcs_1881
OrganismMycobacterium sp. (strain MCS) [Complete proteome] [HAMAP]
Taxonomic identifier164756 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length701 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 – 701701DNA ligase HAMAP MF_01588
PRO_0000313315

Regions

Domain616 – 70186BRCT
Nucleotide binding50 – 545NAD By similarity
Nucleotide binding100 – 1012NAD By similarity

Sites

Active site1321N6-AMP-lysine intermediate By similarity
Metal binding4271Zinc By similarity
Metal binding4301Zinc By similarity
Metal binding4461Zinc By similarity
Metal binding4521Zinc By similarity
Binding site1301NAD By similarity
Binding site1531NAD By similarity
Binding site1931NAD By similarity
Binding site3091NAD By similarity
Binding site3331NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1BAU4 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: FC4714A2EEB824E5

FASTA70175,899
        10         20         30         40         50         60 
MSAKSTPDAG PQEQATEAEA ELRHRWQALA DEVRDHQFRY YVRDAPVISD ADFDKLFQQL 

        70         80         90        100        110        120 
EALEAEHPEL RAPDSPTQLV GGAGFATDFT PAEHLERMLS LDDVFNVDEL TAWSSRVRAE 

       130        140        150        160        170        180 
VGDDAAYLCE LKVDGLALAL VYRDGRLERA ATRGDGRVGE DVTLNARTLD DVPERLTPSD 

       190        200        210        220        230        240 
EFPHPAVLEV RGEVFFRVAD FEALNAGLVA EGKPPFANPR NSAAGSLRQK NPAVTARRPL 

       250        260        270        280        290        300 
RMVCHGIGYT EGFSPTSLHE AYGALRAWGL PVSDHTTRVQ GMDAVRERIA YWGEHRHDIE 

       310        320        330        340        350        360 
HEIDGVVVKL DQIALQRRLG ATSRAPRWAV AYKYPPEEAQ TKLLDIRVNV GRTGRVTPFA 

       370        380        390        400        410        420 
YMEPVKVAGS TVGLATLHNA SEVKRKGVLI GDTVVIRKAG DVIPEVLGPV VDLRDGTERE 

       430        440        450        460        470        480 
FVMPTHCPEC GTELAPAKEG DADIRCPNSR TCPAQLRERV FHVAGRGAFD IEGLGYEAAI 

       490        500        510        520        530        540 
ALLQAGVITD EGDLFTLTED DLLRTELFTT KGGAVSANGR RLLANLGKAK AQPLWRVLVA 

       550        560        570        580        590        600 
LSIRHVGPTA ARALATEFGS LDAIIEASED QLAAVEGVGP TIAAAVKEWF TVDWHCAIVE 

       610        620        630        640        650        660 
KWRAAGVRMA DERDASIART LEGLSIVVTG SLAGFSRDEA KEAIIARGGK AAGSVSKKTA 

       670        680        690        700 
YVVAGDSPGS KYDKAIDLGV PVLDEDGFRN LLENGPQAPE G

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium sp. MCS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000384 Genomic DNA. Translation: ABG07990.1.
RefSeqYP_639046.1. NC_008146.1.

3D structure databases

ProteinModelPortalQ1BAU4.
SMRQ1BAU4. Positions 17-337, 619-698.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1BAU4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000060797; EBMYCP00000058964; EBMYCG00000060792.
GeneID4110715.
GenomeReviewsGene locus Mmcs_1881 in contig CP000384_GR.
KEGGmmc:Mmcs_1881.
PATRIC18113935. VBIMycSp106721_1923.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
GeneTreeEBGT00050000016652.
HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycMSP164756:MMCS_1881-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_MYCSS
AccessionPrimary (citable) accession number: Q1BAU4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: January 25, 2012
This is version 46 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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