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P57172 (DNLJ_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Synonyms:lig
Ordered Locus Names:BU067
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)
Taxonomic identifier107806 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length675 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
Reference 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 – 675675DNA ligase HAMAP MF_01588
PRO_0000161740

Regions

Domain595 – 67581BRCT
Nucleotide binding32 – 365NAD By similarity
Nucleotide binding81 – 822NAD By similarity

Sites

Active site1151N6-AMP-lysine intermediate By similarity
Metal binding4091Zinc By similarity
Metal binding4121Zinc By similarity
Metal binding4271Zinc By similarity
Metal binding4331Zinc By similarity
Binding site1131NAD By similarity
Binding site1361NAD By similarity
Binding site1731NAD By similarity
Binding site2911NAD By similarity
Binding site3151NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
P57172 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 3C77E54F6F0ADC24

FASTA67577,536
        10         20         30         40         50         60 
MTSTKDKIEK LRKILLKYEY FYHTLNQSII SDAEYDYLFR QLYELELKNK ELIPSDSPTQ 

        70         80         90        100        110        120 
KVGSHILQKF KKIKHFSPML SLENTFDVNG YLNFKKRIKK SIHNNEPLSF CCELKLDGVA 

       130        140        150        160        170        180 
ISIIYEEGIF VRAATRGDGF EGENITSNAR MIDSIPLKLK GIDIPKRLEI RGEVFMLKSN 

       190        200        210        220        230        240 
FIKLNKKYKL NQNKYFSNPR NAAAGSLRHI DPNITAERKL IFSCHGCDFF VKTNKELTTH 

       250        260        270        280        290        300 
YQRLMKCLSW GIPVNKEIVI CSSDIEIIQF YKKIAQKRNF LDFDIDGIVI KVNSLELQKK 

       310        320        330        340        350        360 
IGSTTKSPRW AIAFKFSPKE RITTLNDVKF QVGRTGVITP VAYFNPVYIS GVMISKASLH 

       370        380        390        400        410        420 
NKNEIERLNL HFNDTITICR SGDVIPRLLN VIEIRRCDNA KKIIFPSFCP VCNTELLENI 

       430        440        450        460        470        480 
EEKLIRCHSG LTCDAQKKQA LYHFFSKKSL YVVGLGPKII NELVEKGLVK NPIDFFYLKD 

       490        500        510        520        530        540 
IDLIQLKNVG KRKSIKIINS IKKCKKTTLK CFIYALGIPG VGEVVAGKIA NYFIKLDKLM 

       550        560        570        580        590        600 
NSNILELNCI SGVGKIISNN IFNYFSTISN REMVVKLIKQ AGIFLNDQEI HKINSEKTYF 

       610        620        630        640        650        660 
FNKKIVLTGV FKSFSRIELK TILLSLGAKI SNNISRKTDF LIYGNNFGSK FFRAKDLDVK 

       670 
IINQEELNSL IRIKE

« Hide

References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed: 10993077] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000003 Genomic DNA. Translation: BAB12790.1.
RefSeqNP_239904.1. NC_002528.1.

3D structure databases

ProteinModelPortalP57172.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000003097; EBBUCP00000002873; EBBUCG00000003097.
GeneID1109474.
GenomeReviewsGene locus BU067 in contig BA000003_GR.
KEGGbuc:BU067.
PATRIC21243640. VBIBucAph127364_0076.

Phylogenomic databases

GeneTreeEBGT00050000007874.
HOGENOMHBG620317.
OMATQKVGAT.
PhylomeDBP57172.
ProtClustDBCLSK2516823.

Enzyme and pathway databases

BioCycBSP107806:BU067-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_BUCAI
AccessionPrimary (citable) accession number: P57172
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents