Reviewed,
UniProtKB/Swiss-Prot Q8FZQ3 (DNLJ_BRUSU)
Last modified
February 9, 2010.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: DNA ligase EC=6.5.1.2 Alternative name(s): Polydeoxyribonucleotide synthase [NAD+] | ||||
| Gene names |
| ||||
| Organism | Brucella suis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 29461 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 719 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: HAMAP magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW zinc 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 – 719 | 719 | DNA ligase HAMAP MF_01588 | PRO_0000313156 | |||||
Regions | |||||||||
| Domain | 640 – 719 | 80 | BRCT | ||||||
| Nucleotide binding | 42 – 46 | 5 | NAD By similarity | ||||||
| Nucleotide binding | 92 – 93 | 2 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 128 | 1 | N6-AMP-lysine intermediate By similarity | ||||||
| Metal binding | 430 | 1 | Zinc By similarity | ||||||
| Metal binding | 433 | 1 | Zinc By similarity | ||||||
| Metal binding | 448 | 1 | Zinc By similarity | ||||||
| Metal binding | 454 | 1 | Zinc By similarity | ||||||
| Binding site | 126 | 1 | NAD By similarity | ||||||
| Binding site | 149 | 1 | NAD By similarity | ||||||
| Binding site | 185 | 1 | NAD By similarity | ||||||
| Binding site | 301 | 1 | NAD By similarity | ||||||
| Binding site | 325 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | "The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330 / Biovar 1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014291 Genomic DNA. Translation: AAN30333.1. |
| RefSeq | NP_698418.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1B04 based on UniProtKB O87703. |
| SMR | Q8FZQ3. Positions 14-629, 643-718. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1167102. |
| GenomeReviews | Gene locus BR1420 in contig AE014291_GR. |
| KEGG | bms:BR1420. |
| TIGR | BR1420. |
Phylogenomic databases | |
| HOGENOM | HBG620317. |
| OMA | IKHFASR. |
| PhylomeDB | Q8FZQ3. |
Enzyme and pathway databases | |
| BioCyc | BSUI204722:BR_1420-MONOMER. |
| BRENDA | 6.5.1.2. 281610. |
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. |
| 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. 2 hits. SM00532. LIGANc. 1 hit. [Graphical view] |
| 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_BRUSU | ||||||||
| Accession | Primary (citable) accession number: Q8FZQ3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Brucella suis Brucella suis (strain 1330): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


