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A4TDZ8 (DNLJ_MYCGI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Mflv_4248
OrganismMycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens (strain ATCC 700033 / PYR-GCK)) [Complete proteome] [HAMAP]
Taxonomic identifier350054 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length712 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 – 712712DNA ligase HAMAP MF_01588
PRO_0000340360

Regions

Domain622 – 71190BRCT
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
A4TDZ8 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: F99471D715F2D228

FASTA71277,282
        10         20         30         40         50         60 
MSPEAIPDPE SMLAEQAHDA LDPDLRRSWQ ELADEVREHQ FRYYIRDAPI ITDAEFDQLL 

        70         80         90        100        110        120 
RRLQALEDEY PELRTPDSPT QLVGGAGFAT DFTAAEHLER MLSLDNVFDL EELAAWAARI 

       130        140        150        160        170        180 
RTEIGADAQY LCELKIDGVA LALVYRDGRL ERAATRGDGR TGEDVTLNAR TIEDIPERLS 

       190        200        210        220        230        240 
GTNEFPLPTV VEVRGEVFFR VADFEDLNAG LVAEGKPPFA NPRNSAAGSL RQKNPAVTAR 

       250        260        270        280        290        300 
RRLRMICHGL GHVESSGGSP FPTLHDAYRA LKAWGLPVSD HTAQVTGLDA VTERIAYWGE 

       310        320        330        340        350        360 
HRHDVEHEID GVVVKVDAVA LQRRLGATSR APRWAVAYKY PPEEAQTRLL DIRVNVGRTG 

       370        380        390        400        410        420 
RVTPFAYMEP VKVAGSTVGL ATLHNASEVK RKGVLIGDTV VIRKAGDVIP EVLGPVVDLR 

       430        440        450        460        470        480 
DGSEREFVFP THCPECGSEL APAKEGDADI RCPNTRSCPA QLRERVFHVA GRGAFDIEGL 

       490        500        510        520        530        540 
GYEAATALLQ AGVIADEGDL FGLTADDLLR TELFTTKAGE LSANGKRLLA NLGKAKAQPL 

       550        560        570        580        590        600 
WRVLVALSIR HVGPTAARAL ATEFGSLEAI ETASEEQLAG TEGVGPTIAA AVIDWFTVDW 

       610        620        630        640        650        660 
HRAIVDKWRE AGVRMADERD ASIERTLEGL SIVVTGSLAG FSRDEAKEAI IARGGKAAGS 

       670        680        690        700        710 
VSKKTAYVVA GDAPGSKYDK AIELGVPVLD EDGFRRLLAE GPERDAEDGE PG 

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PYR-GCK.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000656 Genomic DNA. Translation: ABP46717.1.
RefSeqYP_001135505.1. NC_009338.1.

3D structure databases

ProteinModelPortalA4TDZ8.
SMRA4TDZ8. Positions 23-343.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4TDZ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000023580; EBMYCP00000023242; EBMYCG00000023575.
GeneID4975561.
GenomeReviewsGene locus Mflv_4248 in contig CP000656_GR.
KEGGmgi:Mflv_4248.
PATRIC18036722. VBIMycGil17082_4329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
GeneTreeEBGT00050000016652.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBA4TDZ8.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycMGIL350054:MFLV_4248-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_MYCGI
AccessionPrimary (citable) accession number: A4TDZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: May 15, 2007
Last modified: January 25, 2012
This is version 41 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