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C0ZXK3 (DNLJ_RHOE4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 21. 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:RER_23800
OrganismRhodococcus erythropolis (strain PR4 / NBRC 100887) [Complete proteome] [HAMAP]
Taxonomic identifier234621 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length700 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 – 700700DNA ligase HAMAP MF_01588
PRO_0000380455

Regions

Domain608 – 69790BRCT
Nucleotide binding43 – 475NAD By similarity
Nucleotide binding92 – 932NAD By similarity

Sites

Active site1241N6-AMP-lysine intermediate By similarity
Metal binding4191Zinc By similarity
Metal binding4221Zinc By similarity
Metal binding4381Zinc By similarity
Metal binding4441Zinc By similarity
Binding site1221NAD By similarity
Binding site1451NAD By similarity
Binding site1851NAD By similarity
Binding site3011NAD By similarity
Binding site3251NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
C0ZXK3 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 183EA4F46E276CF6

FASTA70076,277
        10         20         30         40         50         60 
MTETADAMQP APNEAREQWT ELAEEVRQHQ FRYYVRDAPV ISDGAFDTLL GQLNALEEQY 

        70         80         90        100        110        120 
PDLRTPDSPT QLVGGGFATD FTSVDHLERM LSLDNVFDES ELRGWIAKVE QETGPELHYL 

       130        140        150        160        170        180 
CEVKIDGVAL NLVYENGKLV RAATRGDGRT GELVTLNALT INDIPERLTA TDEFPIPTLL 

       190        200        210        220        230        240 
EVRGEVFFRL EDFAALNASL VEEGKAPFAN PRNSAAGSLR QKNPAVTARR RLGMICHGFG 

       250        260        270        280        290        300 
RMEGFEPASQ YDAYVALAAW GLPVSTHTSR VVGADAVVEK MKYWGEHRHD VEHEIDGLVV 

       310        320        330        340        350        360 
KVDEMSLHRR LGTTSRAPRW AIAYKYPPEE VTTKLLDIRV SVGRTGRVTP FAYMEPVTVA 

       370        380        390        400        410        420 
GSTVSLATLH NGSEVKRKGV LIGDTVVLRK AGDVIPEVLG PVADVRDGTE REFVMPTHCP 

       430        440        450        460        470        480 
ECGTLLAPAK EGDVDVRCPN QQHCPAQLRE RVFHVSGRGA FDIEVLGYEA ATGLLEAKVI 

       490        500        510        520        530        540 
GDEGDLFSLD AEKLIEVPIF RTNAGALSAN GKRLLANLDS AKDKPLWRVL VALSIRHVGP 

       550        560        570        580        590        600 
TAARALAGEF GSLQRIREAS VDELAAVDGV GSTIAAAVVE WFSVDWHQQI VDKWASAGVR 

       610        620        630        640        650        660 
MEDERDDSIP RNLEGLSIVV TGSLETYSRD QAKEAILVRG GKAAGSVSKK TAFVVVGEAP 

       670        680        690        700 
GSKHDKAVEL GVPVLDEDGF RRLLEDGPDA VAPTDLDVSE

« Hide

References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PR4 / NBRC 100887.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP008957 Genomic DNA. Translation: BAH33088.1.
RefSeqYP_002765827.1. NC_012490.1.

3D structure databases

ProteinModelPortalC0ZXK3.
ModBaseSearch...

Protein-protein interaction databases

STRINGC0ZXK3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7709909.
GenomeReviewsGene locus RER_23800 in contig AP008957_GR.
KEGGrer:RER_23800.
PATRIC23191178. VBIRhoEry66701_2883.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAENVRTIR.
ProtClustDBPRK07956.

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. 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_RHOE4
AccessionPrimary (citable) accession number: C0ZXK3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: January 25, 2012
This is version 21 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