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A1A200 (DNLJ_BIFAA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 37. 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:BAD_0952
OrganismBifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) [Complete proteome] [HAMAP]
Taxonomic identifier367928 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length892 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 – 892892DNA ligase HAMAP MF_01588
PRO_0000313139

Regions

Domain810 – 89283BRCT
Nucleotide binding99 – 1035NAD By similarity
Nucleotide binding148 – 1492NAD By similarity

Sites

Active site1841N6-AMP-lysine intermediate By similarity
Metal binding4901Zinc By similarity
Metal binding4931Zinc By similarity
Metal binding5091Zinc By similarity
Metal binding5151Zinc By similarity
Binding site1821NAD By similarity
Binding site2051NAD By similarity
Binding site2441NAD By similarity
Binding site3691NAD By similarity
Binding site3931NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A1A200 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 1A613B1510FC9098

FASTA89297,284
        10         20         30         40         50         60 
MTMTNRDDSE QLAWDFDAPE SDGSSAAVVA DEGLASLTPG SERWIAALQP TDADAMRLDK 

        70         80         90        100        110        120 
VDVASMSAEA AARLWARVAA WVESDQIAYY IDDAPVSSDA AYDARLRCLQ SLEAQFPSLD 

       130        140        150        160        170        180 
SPQSPTHRVG GTFSNDFASV RHPSRMMSLD DVFSIEELRE WYDGVLRGLD WPESKPLPMT 

       190        200        210        220        230        240 
CEVKIDGLAL NLIYRNGVLE QGLTRGDGVT GEDITLNVRT ISTIPQNLAG PEEDIPEFVE 

       250        260        270        280        290        300 
IRGEVFMRWD DFNKLNAENE DAGRAPFANP RNAAAGSLRQ KDPRITATRR LSFYAHGIGS 

       310        320        330        340        350        360 
LRWGAGHAGN GHDVVNDQSE AYELYKKWGV PVSPHNREVT SFKEILDMID YYGEHRGDIE 

       370        380        390        400        410        420 
HALDGIVVKV DDLGLQRSLG ATSRAPRWAI AYKYPPEEVN TELLDITVQV GRTGRVTPVA 

       430        440        450        460        470        480 
VLKPVYVAGS TVSRTTLHNP FEVERKGVLI GDTVVVRKAG DVIPELVGPV LERRKGREGE 

       490        500        510        520        530        540 
LRRFVMPTRC PSCGAELAPA KEGDKDIRCP NVESCPAQLT ERIINLASRK AFDIEHLGDQ 

       550        560        570        580        590        600 
SAIALTNPEE DRPDSIDTYA PNITEIVVKP GEEPEPYEPV AGLELPPMQT PVLSSEAGLF 

       610        620        630        640        650        660 
SLTSADLKDV RVWREAPIIE IHETVGSNGK IKKVRKRVGG SGLWHQVPAF WTAPTAARKR 

       670        680        690        700        710        720 
KEADIDETAE YPQYVVPDDA VVIREEIKVS RGGTSSVQPV YIRPAENTRK MLDEMDKARH 

       730        740        750        760        770        780 
ADLWRVLVAL SIRRLGPPTA RTIASAFGTL DAIEHASVDE LSQIDGIGSE IAESVVTWFT 

       790        800        810        820        830        840 
AAREPGNWRG AVLDAWKAAG VGVGQAQASG LPQTLAGKTV VVTGSLEGFS RDSAKEAIVL 

       850        860        870        880        890 
RGGKAAGSVS KKTDWVVVGE NAGSKAAKAE ELGIPMLNED QFKQLLDTGT VE

« Hide

References

[1]"Bifidobacterium adolescentis complete genome sequence."
Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S., Tanaka K., Watanabe K.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15703 / DSM 20083 / NCTC 11814 / E194a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009256 Genomic DNA. Translation: BAF39733.1.
RefSeqYP_909815.1. NC_008618.1.

3D structure databases

ProteinModelPortalA1A200.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1A200.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4556290.
GenomeReviewsGene locus BAD_0952 in contig AP009256_GR.
KEGGbad:BAD_0952.
NMPDRfig|1680.3.peg.1221.
PATRIC21101337. VBIBifAdo27973_1032.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
ProtClustDBCLSK572471.

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]
SMARTSM00292. BRCT. 1 hit.
SM00278. HhH1. 2 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_BIFAA
AccessionPrimary (citable) accession number: A1A200
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 37 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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