Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q3MGE7 (DNLJ_ANAVT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Ava_0313
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena

Protein attributes

Sequence length676 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 – 676676DNA ligase HAMAP MF_01588
PRO_0000313110

Regions

Domain599 – 67678BRCT
Nucleotide binding35 – 395NAD By similarity
Nucleotide binding84 – 852NAD By similarity

Sites

Active site1171N6-AMP-lysine intermediate By similarity
Metal binding4141Zinc By similarity
Metal binding4171Zinc By similarity
Metal binding4321Zinc By similarity
Metal binding4371Zinc By similarity
Binding site1151NAD By similarity
Binding site1381NAD By similarity
Binding site1771NAD By similarity
Binding site2961NAD By similarity
Binding site3201NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3MGE7 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: F939ACC379EA541C

FASTA67675,547
        10         20         30         40         50         60 
MVQTHSEVKR VEELRRLLQQ ASYAYYVLDA PVMEDAVYDQ LYRELQQLEI QHPELVTPDS 

        70         80         90        100        110        120 
PTQRIGERPA TQFLSVRHNI PLYSLENAFN VEELQAWDQR WRRQVAPTEA EYVAELKIDG 

       130        140        150        160        170        180 
SAIALTYENG ILVRGATRGD GVTGEDITQN VRTIRSIPLR LSFDGIENIG KVEVRGEAFL 

       190        200        210        220        230        240 
PLEVFKQINE ERQKAGEQLF ANPRNAAAGT LRQLDSKIVA RRRLDFFAYT LHISGMDDAS 

       250        260        270        280        290        300 
IANTQWEALE LLQKMGFRVN SQHQLCQSLA EVADYYRYWD TERLNLPYMT DGVVLKLNSF 

       310        320        330        340        350        360 
KLQEQLGFTQ RFPRWAVALK YPAEEAPTRV ENIAVNVGRT GALTPLAQMR PVQLAGTTVS 

       370        380        390        400        410        420 
RATLHNSDRI AQLDIRIGDT VIVRKAGEII PEVVRVLKEL RPVDTQPFIM PTHCPVCGQP 

       430        440        450        460        470        480 
VVRETGEAVT RCVNASCAAI LKGSIEHWVS RDALDIKGVG EKLVHQLVDK ELVHSVADLY 

       490        500        510        520        530        540 
SLTNEQLFVL ERMGEKSAQK LIEAIAQSKN QPWSRVLYGL GIRHVGSVNA QLLSEKYRAV 

       550        560        570        580        590        600 
AELSSAKQSD IAGIYGIGAE IAQSVYQWFR ISANQRLIER LQAAGLQFAN TEEISAVDNA 

       610        620        630        640        650        660 
NLKLVGKTFV ITGTLPTLKR DEAKALIQKA GGKITESVSK KTDYLVVGED AGSKLEKAQT 

       670 
LGIKQLSEAE LLKILA

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000117 Genomic DNA. Translation: ABA19939.1.
RefSeqYP_320834.1. NC_007413.1.

3D structure databases

ProteinModelPortalQ3MGE7.
SMRQ3MGE7. Positions 7-322, 603-675.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3MGE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3682785.
GenomeReviewsGene locus Ava_0313 in contig CP000117_GR.
KEGGava:Ava_0313.
NMPDRfig|240292.3.peg.808.
PATRIC35420933. VBIAnaVar43351_1040.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0272.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBQ3MGE7.
ProtClustDBPRK07956.

Enzyme and pathway databases

BioCycAVAR240292:AVA_0313-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_ANAVT
AccessionPrimary (citable) accession number: Q3MGE7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2005
Last modified: January 25, 2012
This is version 47 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

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