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A1T6X7 (DNLJ_MYCVP) 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:Mvan_2112
OrganismMycobacterium vanbaalenii (strain DSM 7251 / PYR-1) [Complete proteome] [HAMAP]
Taxonomic identifier350058 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length707 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 – 707707DNA ligase HAMAP MF_01588
PRO_0000313318

Regions

Domain622 – 70786BRCT
Nucleotide binding53 – 575NAD By similarity
Nucleotide binding103 – 1042NAD By similarity

Sites

Active site1351N6-AMP-lysine intermediate By similarity
Metal binding4331Zinc By similarity
Metal binding4361Zinc By similarity
Metal binding4521Zinc By similarity
Metal binding4581Zinc By similarity
Binding site1331NAD By similarity
Binding site1561NAD By similarity
Binding site1961NAD By similarity
Binding site3151NAD By similarity
Binding site3391NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A1T6X7 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: F50ADAD49E26A1FF

FASTA70776,838
        10         20         30         40         50         60 
MSSKATQDPE AVLAEQSDDA TEAGLRRQWQ ELADEVRDHQ FRYYVRDAPI ITDAEFDAML 

        70         80         90        100        110        120 
RRLEALEEAH PELRTPDSPT QLVGGAGFAT DFTAAEHLER MLSLDNVFTP DELAAWAARI 

       130        140        150        160        170        180 
RTEIGADAQY LCELKIDGVA LSLVYRDGRL ERGATRGDGR TGEDVTLNAR TIEDVPEKLT 

       190        200        210        220        230        240 
GTEEFPLPSV LEVRGEVFFR IADFEDLNAG LVAEGKPPFA NPRNSAAGSL RQKNPAVTAR 

       250        260        270        280        290        300 
RRLRMICHGL GHIEDAAGFP FRTLHDAYRA LQAWGLPVSP HTAQVTGLDA VTERIAYWGE 

       310        320        330        340        350        360 
HRHDVEHEID GVVVKVDEVA LQRRLGATSR APRWAVAYKY PPEEAQTKLL DIRVNVGRTG 

       370        380        390        400        410        420 
RVTPFAYMEP VKIAGSTVGL ATLHNGSEVK RKGVLIGDTV VIRKAGDVIP EVLGPVVDLR 

       430        440        450        460        470        480 
DGSEREFVMP THCPECGTEL APAKEGDADI RCPNSRTCPA QLRERVFHVA GRGAFDIEGL 

       490        500        510        520        530        540 
GYEAAIALLQ ARVITDEGDL FTLTADDLLR TDLFTTKAGE LSANGKRLLT NLGKAKAQPL 

       550        560        570        580        590        600 
WRVLVALSIR HVGPTAARAL ATEFGSLDAI VAASEEELAA VEGVGPTIAA AVTDWFTVDW 

       610        620        630        640        650        660 
HRTIVDKWRA AGVRMADERD ASIERTLDGL SIVVTGSLTG YSRDEAKEAI IARGGKAAGS 

       670        680        690        700 
VSKKTAYVVA GDSPGSKYDK AIELGVPVLD EDGFRRLLEN GPDTPDS

« Hide

References

[1]"Complete sequence of Mycobacterium vanbaalenii PYR-1."
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., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.J., Miller C., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 7251 / PYR-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000511 Genomic DNA. Translation: ABM12927.1.
RefSeqYP_952933.1. NC_008726.1.

3D structure databases

ProteinModelPortalA1T6X7.
SMRA1T6X7. Positions 27-343.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1T6X7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000081346; EBMYCP00000079299; EBMYCG00000081341.
GeneID4647288.
GenomeReviewsGene locus Mvan_2112 in contig CP000511_GR.
KEGGmva:Mvan_2112.
PATRIC18182455. VBIMycVan31953_2156.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
GeneTreeEBGT00050000016652.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBA1T6X7.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycMVAN350058:MVAN_2112-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_MYCVP
AccessionPrimary (citable) accession number: A1T6X7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 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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