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A0QJE3 (DNLJ_MYCA1) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 38. 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:MAV_3868
OrganismMycobacterium avium (strain 104) [Complete proteome] [HAMAP]
Taxonomic identifier243243 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium avium complex (MAC)

Protein attributes

Sequence length693 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 – 693693DNA ligase HAMAP MF_01588
PRO_0000313310

Regions

Domain607 – 69387BRCT
Nucleotide binding41 – 455NAD By similarity
Nucleotide binding91 – 922NAD By similarity

Sites

Active site1231N6-AMP-lysine intermediate By similarity
Metal binding4181Zinc By similarity
Metal binding4211Zinc By similarity
Metal binding4371Zinc By similarity
Metal binding4431Zinc By similarity
Binding site1211NAD By similarity
Binding site1441NAD By similarity
Binding site1841NAD By similarity
Binding site3001NAD By similarity
Binding site3241NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QJE3 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: DC1BB9F2A8797C21

FASTA69375,258
        10         20         30         40         50         60 
MSSAEADSVP PEVRRQWQEL AETVREHQFR YYIKDAPIIS DAEFDALFNE LLALEERHPE 

        70         80         90        100        110        120 
LRVADSPTQL VGGAGFATDF AEAAHLERML SLDDVFDTDE LIAWSNRVEN EIGKDPHYLC 

       130        140        150        160        170        180 
ELKIDGVALS LVYRDGRLER AATRGDGRVG EDVTLNARTI DDVPERLSPS DDFPVPALLE 

       190        200        210        220        230        240 
VRGEVFFLLA DFEALNASLV EDGKAPFANP RNSAAGSLRQ KNPAVTARRK LRMICHGIGR 

       250        260        270        280        290        300 
TEGFSPKTQH EAYTALSVWG LPVAEQTARV RGLAAVQERI GYWGEHRYEL QHEIDGVVVK 

       310        320        330        340        350        360 
VDDVALQRRL GATSRAPRWA VAYKYPPQEA QTKLLDIRVN VGRTGRVTPF AFMTPVKVAG 

       370        380        390        400        410        420 
STVGLATLHN AAEVKRKGVL IGDTVMIRKA GDVIPEVLGP VVDLRDGTER EFVMPTTCPE 

       430        440        450        460        470        480 
CGTPLAPAKE GDADIRCPNA RSCPAQLRER VFHVAGRGAL DIEGLGYEAA TALLKAGVIA 

       490        500        510        520        530        540 
DEGDLFALTE DDLLRTELFR TKAGTLSANG TRLLQNLQKA KKVALWRVLV ALSIRHVGPT 

       550        560        570        580        590        600 
AARALATEFG DLDSIMSAST ERLAAVEGVG PTIAAALTEW FTVDWHRAIV DKWRGAGVRM 

       610        620        630        640        650        660 
ADERDASVPR TLEGLTVVVT GSLAGFSRDD AKEAILARGG KAAGSVSKKT DYVVAGDSPG 

       670        680        690 
SKYDKAVELG VPILDEDGFR KLLAEGPPET PAD

« Hide

References

[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 104.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000479 Genomic DNA. Translation: ABK67454.1.
RefSeqYP_883031.1. NC_008595.1.

3D structure databases

ProteinModelPortalA0QJE3.
SMRA0QJE3. Positions 11-328.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0QJE3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000012422; EBMYCP00000012308; EBMYCG00000012420.
GeneID4527291.
GenomeReviewsGene locus MAV_3868 in contig CP000479_GR.
KEGGmav:MAV_3868.
PATRIC17989421. VBIMycAvi38287_3788.
TIGRMAV_3868.

Phylogenomic databases

eggNOGCOG0272.
GeneTreeEBGT00050000016652.
HOGENOMHBG620317.
OMAPEYICEL.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycMAVI243243:MAV_3868-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. 3 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_MYCA1
AccessionPrimary (citable) accession number: A0QJE3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 38 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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