Skip Header

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

Q3ITK1 (DNLJ_NATPD) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 48. 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:NP0882A
OrganismNatronomonas pharaonis (strain DSM 2160 / ATCC 35678) [Complete proteome] [HAMAP]
Taxonomic identifier348780 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Natronomonas

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_0000313530

Regions

Domain607 – 69185BRCT
Nucleotide binding56 – 605NAD By similarity
Nucleotide binding104 – 1052NAD By similarity

Sites

Active site1411N6-AMP-lysine intermediate By similarity
Metal binding4291Zinc By similarity
Metal binding4321Zinc By similarity
Metal binding4451Zinc By similarity
Metal binding4511Zinc By similarity
Binding site1391NAD By similarity
Binding site1621NAD By similarity
Binding site1981NAD By similarity
Binding site3141NAD By similarity
Binding site3381NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3ITK1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 586ED6C56413F9BC

FASTA69175,706
        10         20         30         40         50         60 
MEEPEDNPYI RDPPLDFEPV DELDAASATR QVETLREAIR FHDYRYYQLA DPVISDRAYD 

        70         80         90        100        110        120 
QLFERLERLE SKFDRSSATS PTQRVGGEPL DELETVEHVA PMRSIESSVE VDDIRDFDTR 

       130        140        150        160        170        180 
IQERLAAAGY EGPVRYLCEP KFDGLSVELV YEEGELSRAA TRGDGQEGDD VTANVRTIRS 

       190        200        210        220        230        240 
VPLTLDGDCP SFLAVRGEIF MPKDAFQEYN RERLERGEEP FSNPRNAAAG TLRQLDPSVT 

       250        260        270        280        290        300 
AERPLDCFVF DILDDGGRGF ETRMAEHEAV ESWGFQVDDH TARVDDIEAA IAFREEMLDG 

       310        320        330        340        350        360 
RASLDYEIDG IVIKLDRKDA CALLGATARA PRWAYAYKFP ARTEETTVRD IVLQVGRTGR 

       370        380        390        400        410        420 
LTPVALLDPV EVSGVEVSRA TLHNPQQIAE LGVGIGDRVT LKRAGDVIPY IEAVVDSERE 

       430        440        450        460        470        480 
AHFEFPDRCP VCESPLERDG PLAYCTGGVA CPAQLRRAVE HYASRSGLDI EGLGESAVDQ 

       490        500        510        520        530        540 
LVDAGLVERL PDLYDLSVAD VAELDGWGRT SAENLLEELE ASTEPPLPAF LSALGIPGVG 

       550        560        570        580        590        600 
TTTAADIARE FGTLDAVMDA TAEELRAVDG IGPTLGGEIA EFFDSDRNQQ VIEQLRKRGV 

       610        620        630        640        650        660 
DPEPAETAGD ALSGQTFVFT GSLDGLTREE AHELVETSGG TATGSVSGNT DYLVVGDSPG 

       670        680        690 
QRKREAANEH GVETLSQSDF ESLLESHGIE I

« Hide

References

[1]"Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis."
Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J., Oesterhelt D.
Genome Res. 15:1336-1343(2005) [PubMed: 16169924] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2160 / ATCC 35678.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR936257 Genomic DNA. Translation: CAI48532.1.
RefSeqYP_326101.1. NC_007426.1.

3D structure databases

ProteinModelPortalQ3ITK1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3ITK1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3702885.
GenomeReviewsGene locus NP0882A in contig CR936257_GR.
KEGGnph:NP0882A.
NMPDRfig|348780.3.peg.495.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG06741.
HOGENOMHBG620317.
OMAENVRTIR.
PhylomeDBQ3ITK1.
ProtClustDBPRK14351.

Enzyme and pathway databases

BioCycNPHA348780:NP0882A-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_NATPD
AccessionPrimary (citable) accession number: Q3ITK1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 8, 2005
Last modified: November 16, 2011
This is version 48 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