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Q5UY84 (DNLJ_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 50. 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:rrnAC3049
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula

Protein attributes

Sequence length691 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 – 691691DNA ligase HAMAP MF_01588
PRO_0000313531

Regions

Domain608 – 69184BRCT
Nucleotide binding59 – 635NAD By similarity
Nucleotide binding107 – 1082NAD By similarity

Sites

Active site1391N6-AMP-lysine intermediate By similarity
Metal binding4261Zinc By similarity
Metal binding4291Zinc By similarity
Metal binding4421Zinc By similarity
Metal binding4481Zinc By similarity
Binding site1371NAD By similarity
Binding site1601NAD By similarity
Binding site1961NAD By similarity
Binding site3111NAD By similarity
Binding site3351NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5UY84 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 4F073DCB4249C59A

FASTA69175,738
        10         20         30         40         50         60 
MTTAEDVAGN PYISDPRTDF ESVEDVDAET AREQADQLRE ALRYHDYRYY VENDPVIGDR 

        70         80         90        100        110        120 
AYDALFSRLQ RLESAFNLDT DGSPTQRVGG EPLDELPDVE HVARMGSIDQ GGEEADVREF 

       130        140        150        160        170        180 
DSRVRNGLDG DVQYFCEPKF DGLSVEIVYE DGVYQRAATR GDGEVGEDVT ENVRTISSVP 

       190        200        210        220        230        240 
QRLRGDYPDF LAVRGEVYIP RDAFTTFNRE RVERGEDPFA NPRNAAAGTL RQLDPSVTAE 

       250        260        270        280        290        300 
RPLSIFFFGV LDASVDFESH SELHERFPEW GLRVCDRTAV VDDIDAAIDY RNEQQQARDD 

       310        320        330        340        350        360 
LDYEIDGVVI KVDDMDACDD LGSTARAPRW AFAYKFPARK EETTVRDIVV QVGRTGRLTP 

       370        380        390        400        410        420 
VALMDPVEVG GVTVSRASLH NPSLIADLGV DVGDRVRIKR AGDVIPDVVE VLDDDGDGHF 

       430        440        450        460        470        480 
EFPETCPACD SPVEHDGPMA FCTGGLTCPA QRERSVEHYA SRDALDIEGV GEKAVQQLLD 

       490        500        510        520        530        540 
AGLVSDPADL YDLTVEDLTG LEGWGETSAR NLVDGMDSAR EPPLADFLVA LGIPEVGTVT 

       550        560        570        580        590        600 
ARNLAQEFGT FEAILDAADE GDTDAFEAVP DVGQTVARSI VEFFEGEGNR AVIDRLLDHV 

       610        620        630        640        650        660 
EPQAAEETDG DALDGQTFVF TGSLDGYTRG EAQELVERND GSATSSVSGN TDYLVLGDNP 

       670        680        690 
GQRKQDDAAA HDVETLTEDE FEELLDDAGV L

« Hide

References

[1]"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea."
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.
Genome Res. 14:2221-2234(2004) [PubMed: 15520287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY596297 Genomic DNA. Translation: AAV47769.1.
RefSeqYP_137475.1. NC_006396.1.

3D structure databases

HSSPHSSP built from PDB template 1B04 based on UniProtKB O87703.
ProteinModelPortalQ5UY84.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3128232.
GenomeReviewsGene locus rrnAC3049 in contig AY596297_GR.
KEGGhma:rrnAC3049.
NMPDRfig|272569.1.peg.2765.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBQ5UY84.
ProtClustDBPRK14351.

Enzyme and pathway databases

BioCycHMAR272569:RRNAC3049-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. False negative.
PS01056. DNA_LIGASE_N2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDNLJ_HALMA
AccessionPrimary (citable) accession number: Q5UY84
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 7, 2004
Last modified: December 14, 2011
This is version 50 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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