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Reviewed, UniProtKB/Swiss-Prot Q5PBN8 (DNLJ_ANAMM)

Last modified November 3, 2009. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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: AM152
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

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Protein attributes

Sequence length673 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

Catalytic activity

NAD+ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide + (deoxyribonucleotide)(n+m). HAMAP MF_01588

Cofactor

Magnesium or manganese By similarity.

Sequence similarities

Belongs to the NAD-dependent DNA ligase family. LigA subfamily.

Contains 1 BRCT domain.

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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 ligase (NAD+) activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 673673DNA ligase HAMAP MF_01588
PRO_0000313113

Regions

Domain592 – 67382BRCT
Nucleotide binding33 – 375NAD By similarity
Nucleotide binding83 – 842NAD By similarity

Sites

Active site1191N6-AMP-lysine intermediate By similarity
Metal binding4001Zinc By similarity
Metal binding4031Zinc By similarity
Metal binding4181Zinc By similarity
Metal binding4241Zinc By similarity
Binding site1171NAD By similarity
Binding site1401NAD By similarity
Binding site1751NAD By similarity
Binding site2821NAD By similarity
Binding site3061NAD By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5PBN8-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 2E49722792DB9B65

FASTA67374,628
        10         20         30         40         50         60 
MLEQARRRLA GLNAKLRHHD VLYHGLDAPE VTDHQYDLLV QEKKRLLDEF PDISQYDDYA 

        70         80         90        100        110        120 
DVVGTPKIDS RFPKVQHLEP MLSLENAFTV QDVEKFITRV RRFLELQPDD ILELSCELKM 

       130        140        150        160        170        180 
DGMSFSALYH GGKLTRVATR GNGHFGEDIT TNAMVLRGLP HQLDSAPEVL EVRGEIYMHH 

       190        200        210        220        230        240 
EDFEKLRGSC NFANPRNAAA GSIRQLNQKI VEERNLSYVA YSAVNSTFAT QQEILKQLDE 

       250        260        270        280        290        300 
WGFHTNKQVL FTDKIEEAIA FYNSVYTTRS ALGYDIDGVV YKVNSTNFQK LLGATGKSPR 

       310        320        330        340        350        360 
WAIAHKFPST EARTKLLDIT VQVGRTGVVT PIAELEPINI GGVMVSRASL HNLNEIERKD 

       370        380        390        400        410        420 
VRIGDLVIVK RAGEVIPQVV DVDKTLRSSG TQKFVFPSHC PSCGSKLHRE PGEVALRCVA 

       430        440        450        460        470        480 
ELSCKAQALE RVKHFVSRDG LNIMGLGAKQ IEFFCNHGLI GSIADIFSLE EKLHGINLDT 

       490        500        510        520        530        540 
EHGWGEKSVA NLIAAIRNSA TVRLSNFIFA LGIRFIGVGA AKLVAEHYRS YKNWHQAMLA 

       550        560        570        580        590        600 
LTETHDTVQI RGLGEKSISS LKAFFSVQGN LEVLESLSAK LNILDEASPA QRGSSAISGK 

       610        620        630        640        650        660 
TVVFTGTLES MSRTEAKLQA ESLGAKVANS VSANTWLLVA GSNPGSKHEK ALSLNVRVID 

       670 
EQTWVKMVED ARS

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References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000030 Genomic DNA. Translation: AAV86291.1.
RefSeqYP_153546.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5PBN8.

Genome annotation databases

GeneID3171105.
GenomeReviewsGene locus AM152 in contig CP000030_GR.
KEGGama:AM152.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5PBN8.
OMARFAIAYK.

Enzyme and pathway databases

BioCycAMAR234826:AM152-MON.

Family and domain databases

HAMAPMF_01588.
[Tree]
InterProIPR001357. BRCT.
IPR018239. DNA_ligase_AS.
IPR004150. DNA_ligase_OB.
IPR001679. DNAligase.
IPR013839. DNAligase_adenylation.
IPR013840. DNAligase_N.
IPR012340. NA-bd_OB-fold.
IPR004149. Znf_DNAligase_C4.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
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.
ProDomPD003944. DNAligase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00292. BRCT. 1 hit.
SM00532. LIGANc. 1 hit.
[Graphical view]
TIGRFAMsTIGR00575. dnlj. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS01055. DNA_LIGASE_N1. 1 hit.
PS01056. DNA_LIGASE_N2. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDNLJ_ANAMM
AccessionPrimary (citable) accession number: Q5PBN8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 4, 2005
Last modified: November 3, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents