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A1TR21 (DNLJ_ACIAC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. 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:Aave_2841
OrganismAcidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length732 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 – 732732DNA ligase HAMAP MF_01588
PRO_0000313099

Regions

Domain653 – 73280BRCT
Nucleotide binding47 – 515NAD By similarity
Nucleotide binding96 – 972NAD By similarity

Sites

Active site1351N6-AMP-lysine intermediate By similarity
Metal binding4701Zinc By similarity
Metal binding4731Zinc By similarity
Metal binding4881Zinc By similarity
Metal binding4941Zinc By similarity
Binding site1331NAD By similarity
Binding site1561NAD By similarity
Binding site1961NAD By similarity
Binding site3171NAD By similarity
Binding site3411NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A1TR21 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 08C13A1C2A6C3C19

FASTA73278,897
        10         20         30         40         50         60 
MAEHPDLFSA PAQEAPEDLG LRAAALRAQL HQWAHQYYVL DAPTVPDAEY DRVFQALQAL 

        70         80         90        100        110        120 
ETAHPELVTP DSPTQRVIGA VMEGLTPVRH TVPMLSIRTE TDTEASGAET FDARVRRELK 

       130        140        150        160        170        180 
LAPDAPPVEY VAEPKFDGLA MSLRYENGRL VQAATRGDGE VGEDVTHNIR TIRQIPLTLP 

       190        200        210        220        230        240 
TGGRYGVPPV LEVRGEVYMR RADFDRLNER QREAGGKTFV NPRNAAAGAV RQLDSGIAAQ 

       250        260        270        280        290        300 
RPLSFFAYGL GDITPAAEGG PDFATHFDML RQLKAWGFPV AAQVRTARGA SELVAFHQEV 

       310        320        330        340        350        360 
GASRDQLPYD IDGVVYKVNS LALQRQLGFV TREPRWAVAH KYPAQEMVTR VEGIDVQVGR 

       370        380        390        400        410        420 
TGKLTPVARL APVFVGGVTV TNATLHNLFE IRKKGVRVGD QVIVRRAGDV IPEVVGTVPA 

       430        440        450        460        470        480 
ALLPVAGALQ GSDALADAAS GADGTAPGAD AARAAPRSPY VPNFRMPRQC PICGSTVVRE 

       490        500        510        520        530        540 
KGEANHRCTG GLFCPAQRKE ALLHFAQRRA MDIEGLGEKL VDQLVEGQVI RTLPDLYRLG 

       550        560        570        580        590        600 
LTALSSLDRM AEKSAQNVLA ALEKSKHTTL PRFLFGLGIR HVGEATAKDL ARHFGGLDAI 

       610        620        630        640        650        660 
MDASVEQLLE VNDVGPVVAE AIHTFFAQPH NREVVEQLRA CGVTWKEGPP AERATLPLAG 

       670        680        690        700        710        720 
KTFVLTGTLP TLSREDAKDR LEAAGAKVAG SVSRKTHYVV AGEEAGSKLA KAQELGVPVL 

       730 
DEAGMLALLQ GR

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References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AAC00-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000512 Genomic DNA. Translation: ABM33409.1.
RefSeqYP_971183.1. NC_008752.1.

3D structure databases

ProteinModelPortalA1TR21.
SMRA1TR21. Positions 19-647.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1TR21.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4667429.
GenomeReviewsGene locus Aave_2841 in contig CP000512_GR.
KEGGaav:Aave_2841.
NMPDRfig|397945.5.peg.2415.
PATRIC20680811. VBIAciCit38535_2885.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBA1TR21.
ProtClustDBCLSK951442.

Enzyme and pathway databases

BioCycAAVE397945:AAVE_2841-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_ACIAC
AccessionPrimary (citable) accession number: A1TR21
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 40 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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