Q5NYU3 (DNLJ_AROAE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 54.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: DNA ligase EC=6.5.1.2 Alternative name(s): Polydeoxyribonucleotide synthase [NAD+] | ||||||
| Gene names |
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| Organism | Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 76114 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum |
Protein attributes
| Sequence length | 681 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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 process | DNA damage DNA repair DNA replication |
| Ligand | Magnesium Manganese Metal-binding NAD Zinc |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replicationInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | intracellular Inferred from electronic annotation. Source: InterPro |
| Molecular function | DNA binding Inferred from electronic annotation. Source: InterPro DNA ligase (NAD+) activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 681 | 681 | DNA ligase HAMAP MF_01588 | PRO_0000313120 | |||||
Regions | |||||||||
| Domain | 601 – 681 | 81 | BRCT | ||||||
| Nucleotide binding | 35 – 39 | 5 | NAD By similarity | ||||||
| Nucleotide binding | 84 – 85 | 2 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 123 | 1 | N6-AMP-lysine intermediate By similarity | ||||||
| Metal binding | 418 | 1 | Zinc By similarity | ||||||
| Metal binding | 421 | 1 | Zinc By similarity | ||||||
| Metal binding | 436 | 1 | Zinc By similarity | ||||||
| Metal binding | 442 | 1 | Zinc By similarity | ||||||
| Binding site | 121 | 1 | NAD By similarity | ||||||
| Binding site | 144 | 1 | NAD By similarity | ||||||
| Binding site | 180 | 1 | NAD By similarity | ||||||
| Binding site | 300 | 1 | NAD By similarity | ||||||
| Binding site | 324 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1." Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R. Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: EbN1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR555306 Genomic DNA. Translation: CAI09771.1. |
| RefSeq | YP_160672.1. NC_006513.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1L7B based on UniProtKB P26996. |
| ProteinModelPortal | Q5NYU3. |
| SMR | Q5NYU3. Positions 8-595. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q5NYU3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3182930. |
| GenomeReviews | Gene locus AZOSEA36460 in contig CR555306_GR. |
| KEGG | eba:ebA6380. |
| NMPDR | fig|76114.4.peg.3651. |
| PATRIC | 20973499. VBIAroAro98752_3667. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0272. |
| HOGENOM | HBG620317. |
| OMA | ENVRTIR. |
| ProtClustDB | CLSK767052. |
Enzyme and pathway databases | |
| BioCyc | ASP76114:EBA6380-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01588. DNA_ligase_A. [Tree] |
| InterPro | IPR001357. 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] |
| Gene3D | G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. |
| KO | K01972. |
| Pfam | PF00533. BRCT. 1 hit. PF01653. DNA_ligase_aden. 1 hit. PF03120. DNA_ligase_OB. 1 hit. PF03119. DNA_ligase_ZBD. 1 hit. [Graphical view] |
| PIRSF | PIRSF001604. LigA. 1 hit. |
| SMART | SM00292. BRCT. 1 hit. SM00278. HhH1. 4 hits. SM00532. LIGANc. 1 hit. [Graphical view] |
| SUPFAM | SSF52113. BRCT. 1 hit. SSF50249. Nucleic_acid_OB. 1 hit. SSF47781. RuvA_2_like. 1 hit. |
| TIGRFAMs | TIGR00575. Dnlj. 1 hit. |
| PROSITE | PS50172. BRCT. 1 hit. PS01055. DNA_LIGASE_N1. 1 hit. PS01056. DNA_LIGASE_N2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DNLJ_AROAE | ||||||||
| Accession | Primary (citable) accession number: Q5NYU3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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