Q4UN15 (DNLJ_RICFE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 48.
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 |
| ||||||
| Organism | Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 315456 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group |
Protein attributes
| Sequence length | 689 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. |
| Sequence caution | The sequence AAY61043.1 differs from that shown. Reason: Erroneous initiation. |
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 ligase (NAD+) activity Inferred 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 – 689 | 689 | DNA ligase HAMAP MF_01588 | PRO_0000280947 | |||||
Regions | |||||||||
| Domain | 610 – 689 | 80 | BRCT | ||||||
| Nucleotide binding | 40 – 44 | 5 | NAD By similarity | ||||||
| Nucleotide binding | 89 – 90 | 2 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 123 | 1 | N6-AMP-lysine intermediate By similarity | ||||||
| Metal binding | 413 | 1 | Zinc By similarity | ||||||
| Metal binding | 416 | 1 | Zinc By similarity | ||||||
| Metal binding | 431 | 1 | Zinc By similarity | ||||||
| Metal binding | 437 | 1 | Zinc By similarity | ||||||
| Binding site | 121 | 1 | NAD By similarity | ||||||
| Binding site | 144 | 1 | NAD By similarity | ||||||
| Binding site | 179 | 1 | NAD By similarity | ||||||
| Binding site | 295 | 1 | NAD By similarity | ||||||
| Binding site | 319 | 1 | NAD By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The genome sequence of Rickettsia felis identifies the first putative conjugative plasmid in an obligate intracellular parasite." Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., Parinello H., Claverie J.-M., Raoult D. PLoS Biol. 3:1-12(2005) [PubMed: 15984913] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-1525 / URRWXCal2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000053 Genomic DNA. Translation: AAY61043.1. Different initiation. |
| RefSeq | YP_246208.1. NC_007109.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1B04 based on UniProtKB O87703. |
| ProteinModelPortal | Q4UN15. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3400381. |
| GenomeReviews | Gene locus RF_0192 in contig CP000053_GR. |
| KEGG | rfe:RF_0192. |
| NMPDR | fig|315456.3.peg.26. |
| PATRIC | 17890754. VBIRicFel64634_0219. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG620317. |
| OMA | ENVRTIR. |
| ProtClustDB | PRK07956. |
Enzyme and pathway databases | |
| BioCyc | RFEL315456:RF_0192-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. 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. 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_RICFE | ||||||||
| Accession | Primary (citable) accession number: Q4UN15 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Rickettsia felis (Rickettsia azadi) Rickettsia felis (strain URRWXCal2): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with