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B1MDV2 (DNLJ_MYCA9) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:MAB_3345c
OrganismMycobacterium abscessus (strain ATCC 19977 / DSM 44196) [Complete proteome] [HAMAP]
Taxonomic identifier561007 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium abscessus

Protein attributes

Sequence length681 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 – 681681DNA ligase HAMAP MF_01588
PRO_0000380424

Regions

Domain599 – 68183BRCT
Nucleotide binding33 – 375NAD By similarity
Nucleotide binding83 – 842NAD By similarity

Sites

Active site1151N6-AMP-lysine intermediate By similarity
Metal binding4101Zinc By similarity
Metal binding4131Zinc By similarity
Metal binding4291Zinc By similarity
Metal binding4351Zinc By similarity
Binding site1131NAD By similarity
Binding site1361NAD By similarity
Binding site1761NAD By similarity
Binding site2921NAD By similarity
Binding site3161NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
B1MDV2 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 8169DCA503CB9A57

FASTA68174,083
        10         20         30         40         50         60 
MDSDIQRQWG ELAEEVRGHQ FRYYVKDAPV ISDGQFDELL RRLTALEEQY PELRTPDSPT 

        70         80         90        100        110        120 
QLVGGAGFVT EFRSVDHLER MLSLDNAFSS DELTAWDARV RGDIGQEPEY LCELKIDGVA 

       130        140        150        160        170        180 
LSLVYENGVL VRGATRGDGR SGEDVTLNAR TIEDVPERLA KSEKYPIPAL LEVRGEVFFR 

       190        200        210        220        230        240 
LEDFEALNAS LVEESKPPFA NPRNSAAGSL RQKNPAITAR RRLRMICHGL GRAEGFSPES 

       250        260        270        280        290        300 
LHDAYLALGE WGLPVSTHTT KVRGIAKVQE RVNYWAEHRH DVEHEIDGVV VKVDTVALQR 

       310        320        330        340        350        360 
RLGSTSRAPR WAIAYKYPPE EATTELLDIR VSVGRTGRVT PFAYMTPVKV AGSTVSLATL 

       370        380        390        400        410        420 
HNASEVKRKG VLIGDTVVIR KAGDVIPEVL GPVADLRNGN EREFVMPTAC PECGTTLAHE 

       430        440        450        460        470        480 
KEGDADIRCP NSRSCPAQLR ERVFHVAGRG AFDIEALGYE AAIALLAAGV IEDEGDLFGL 

       490        500        510        520        530        540 
TADDLLRTDL FKTKSGALSA NGARLLDNLD KAKQQPLWRV LVALSIRHVG PTAARALATE 

       550        560        570        580        590        600 
FGDLEAIEGA SVEQLAAVEG VGATIAAAVV DWFSVDWHRA IVDKWRAAGV RTADERDDSI 

       610        620        630        640        650        660 
PRNLEGLSIV VTGSLPGFSR DEAKEAIIAR GGKSASSVSK KTAFVVVGDS PGSKYDKAVE 

       670        680 
LGVTILDEDG FRALLADGPP A

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References

[1]"Acquisition of foreign virulence genes by the cystic fibrosis pathogen Mycobacterium abscessus."
Genoscope
Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., Gaillard J.L.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19977 / DSM 44196.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU458896 Genomic DNA. Translation: CAM63421.1.
RefSeqYP_001704075.1. NC_010397.1.

3D structure databases

ProteinModelPortalB1MDV2.
SMRB1MDV2. Positions 4-320.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1MDV2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000004138; EBMYCP00000004077; EBMYCG00000004136.
GeneID5965845.
GenomeReviewsGene locus MAB_3345c in contig CU458896_GR.
KEGGmab:MAB_3345c.
PATRIC17978472. VBIMycAbs55940_3407.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000016652.
HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycMABS561007:MAB_3345C-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_MYCA9
AccessionPrimary (citable) accession number: B1MDV2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 31 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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