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A5FWJ5 (DNLJ_ACICJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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:Acry_0757
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Acidiphilium

Protein attributes

Sequence length682 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 – 682682DNA ligase HAMAP MF_01588
PRO_0000313528

Regions

Domain601 – 68282BRCT
Nucleotide binding42 – 465NAD By similarity
Nucleotide binding88 – 892NAD By similarity

Sites

Active site1231N6-AMP-lysine intermediate By similarity
Metal binding4091Zinc By similarity
Metal binding4121Zinc By similarity
Metal binding4271Zinc By similarity
Metal binding4331Zinc By similarity
Binding site1211NAD By similarity
Binding site1441NAD By similarity
Binding site1801NAD By similarity
Binding site2911NAD By similarity
Binding site3151NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A5FWJ5 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 1A2105E6C0E93630

FASTA68273,603
        10         20         30         40         50         60 
MTSPASGVPE PADPKARLAE LVERLAAADA AYYRDDAPIM DDAAYDALRR EAESLRAAHP 

        70         80         90        100        110        120 
DLAAALDQVG AAPSGAFGKV RHRLPMLSLD NVFEPADFVE FCASIRRFLG LGAAPLAFVA 

       130        140        150        160        170        180 
EPKIDGLSIS LTYENRRFVR GATRGDGTEG EDVTENLRTL RELPATLPDD APDFIEIRGE 

       190        200        210        220        230        240 
VYMTKTDFIT LNQGQARQFA NPRNAAAGSL RQLDPAVTAS RRLSLFAYAR GAASQAVGET 

       250        260        270        280        290        300 
HWDYLAILRR WGFPVNPLAE RVSEAGAEPF QRSIGERRAG LDYDIDGVVY KIDDLALQER 

       310        320        330        340        350        360 
LGFAGRAPRW AVAWKFPAER ALTTLLGIDI QVGRTGALTP RARLDPVNVG GVLVSHATLH 

       370        380        390        400        410        420 
NEDEIARKDV RIGDTVELQR AGDVIPQILR ALPERRPADS VPFVFPDHCP VCGALAIRPA 

       430        440        450        460        470        480 
GEVVRRCTGG LSCPAQVVER LIHFCSRLAF DIEGMGEKTV QEFHGLGWLE SPADIFTLRD 

       490        500        510        520        530        540 
REAAIAALEG WGEVSARKLI AAIDARRRIS LARFIYALGI RRIGEQNAKL LARHYSSYAV 

       550        560        570        580        590        600 
WRRQMEEAGV IGSDARLELG SISGIGPSIA EELAGFFAEP HNRDLLDRLV PMLTIEDEVA 

       610        620        630        640        650        660 
AAGGALAGKT IVFTGTLESL TRPEAKARAE ALGARVTESV SKKTDFVVVG ADAGSKAAKA 

       670        680 
ASLGVTVLSE AEFRSLAGLP PG

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
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., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000697 Genomic DNA. Translation: ABQ29977.1.
RefSeqYP_001233896.1. NC_009484.1.

3D structure databases

ProteinModelPortalA5FWJ5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5FWJ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5160952.
GenomeReviewsGene locus Acry_0757 in contig CP000697_GR.
KEGGacr:Acry_0757.
PATRIC20646498. VBIAciCry6074_1246.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBCLSK935936.

Enzyme and pathway databases

BioCycACRY349163:ACRY_0757-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. 4 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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDNLJ_ACICJ
AccessionPrimary (citable) accession number: A5FWJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: January 25, 2012
This is version 39 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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