D3RWK7 (D3RWK7_FERPA) Unreviewed, UniProtKB/TrEMBL
Last modified
May 29, 2013.
Version 24.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: NAD-dependent protein deacylase HAMAP-Rule MF_01121 EC=3.5.1.- HAMAP-Rule MF_01121 Alternative name(s): Regulatory protein SIR2 homolog HAMAP-Rule MF_01121 | ||||
| Gene names |
| ||||
| Organism | Ferroglobus placidus (strain DSM 10642 / AEDII12DO) [Complete proteome] [HAMAP] EMBL ADC64870.1 | ||||
| Taxonomic identifier | 589924 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Ferroglobus › ![]() |
Protein attributes
| Sequence length | 235 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form. Deacetylates the N-terminal lysine residue of Alba, the major archaeal chromatin protein and that, in turn, increases Alba's DNA binding affinity, thereby repressing transcription. May also have NAD-dependent lysine demalonylase and desuccinylase activity By similarity. HAMAP-Rule MF_01121 |
| Catalytic activity | NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein. HAMAP-Rule MF_01121 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_01121. |
| Domain | In contrast to class I sirtuins, class III sirtuins have only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr-61 and Arg-64) that bind to malonylated and succinylated substrates and define the specificity By similarity. HAMAP-Rule MF_01121 |
| Sequence similarities | Belongs to the sirtuin family. Class III subfamily. HAMAP-Rule MF_01121 Contains 1 deacetylase sirtuin-type domain. HAMAP-Rule MF_01121 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation HAMAP-Rule MF_01121 |
| Cellular component | Cytoplasm HAMAP-Rule MF_01121 |
| Ligand | NAD HAMAP-Rule MF_01121 |
| Molecular function | Hydrolase HAMAP-Rule MF_01121 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | peptidyl-lysine demalonylation Inferred from electronic annotation. Source: GOC peptidyl-lysine desuccinylationInferred from electronic annotation. Source: GOC |
| Molecular_function | NAD+ binding Inferred from electronic annotation. Source: InterPro protein-malonyllysine demalonylase activityInferred from electronic annotation. Source: InterPro protein-succinyllysine desuccinylase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Nucleotide binding | 17 – 36 | 20 | NAD By similarity HAMAP-Rule MF_01121 | ||||||
| Nucleotide binding | 95 – 98 | 4 | NAD By similarity HAMAP-Rule MF_01121 | ||||||
| Nucleotide binding | 176 – 178 | 3 | NAD By similarity HAMAP-Rule MF_01121 | ||||||
| Nucleotide binding | 202 – 204 | 3 | NAD By similarity HAMAP-Rule MF_01121 | ||||||
Sites | |||||||||
| Active site | 113 | 1 | Proton acceptor By similarity HAMAP-Rule MF_01121 | ||||||
| Metal binding | 124 | 1 | Zinc By similarity HAMAP-Rule MF_01121 | ||||||
| Metal binding | 140 | 1 | Zinc By similarity HAMAP-Rule MF_01121 | ||||||
| Binding site | 61 | 1 | Substrate By similarity HAMAP-Rule MF_01121 | ||||||
| Binding site | 64 | 1 | Substrate By similarity HAMAP-Rule MF_01121 | ||||||
| Binding site | 220 | 1 | NAD; via amide nitrogen By similarity HAMAP-Rule MF_01121 | ||||||
Sequences
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References
| [1] | "Complete sequence of Ferroglobus placidus DSM 10642." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D. Woyke T.Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 10642 / AEDII12DO. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001899 Genomic DNA. Translation: ADC64870.1. |
| RefSeq | YP_003435145.1. NC_013849.1. |
3D structure databases | |
| ProteinModelPortal | D3RWK7. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ADC64870; ADC64870; Ferp_0700. |
| GeneID | 8778204. |
| KEGG | fpl:Ferp_0700. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000085950. |
| KO | K12410. |
| OMA | VLHMHGE. |
Enzyme and pathway databases | |
| BioCyc | FPLA589924:GHX0-714-MONOMER. |
Family and domain databases | |
| Gene3D | 3.30.1600.10. 2 hits. |
| HAMAP | MF_01121. Sirtuin_ClassIII. |
| InterPro | IPR003000. Sirtuin. IPR026591. Sirtuin_cat_small_dom. IPR027546. Sirtuin_ClassIII. IPR026590. Ssirtuin_cat_dom. [Graphical view] |
| PANTHER | PTHR11085. PTHR11085. 1 hit. |
| Pfam | PF02146. SIR2. 1 hit. [Graphical view] |
| PROSITE | PS50305. SIRTUIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | D3RWK7_FERPA | ||||||||
| Accession | Primary (citable) accession number: D3RWK7 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
