P60849 · ALBA1_SACS2
- ProteinDNA/RNA-binding protein Alba 1
- GenealbA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds double-stranded DNA tightly but without sequence specificity (PubMed:11935028, PubMed:12198167, PubMed:20082605).
Involved in DNA compaction (PubMed:16004869, PubMed:23271660, PubMed:35454068).
Possesses DNA endonuclease activity (PubMed:36947546).
Prevents transcription after DNA binding (PubMed:11935028).
Binds single-stranded DNA and RNA in vitro (PubMed:20082605).
Binds rRNA and mRNA in vivo (By similarity).
May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).
Binds double-stranded RNA (dsRNA) and exhibits RNA chaperone activity (By similarity).
Required for normal growth (By similarity).
Involved in DNA compaction (PubMed:16004869, PubMed:23271660, PubMed:35454068).
Possesses DNA endonuclease activity (PubMed:36947546).
Prevents transcription after DNA binding (PubMed:11935028).
Binds single-stranded DNA and RNA in vitro (PubMed:20082605).
Binds rRNA and mRNA in vivo (By similarity).
May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).
Binds double-stranded RNA (dsRNA) and exhibits RNA chaperone activity (By similarity).
Required for normal growth (By similarity).
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 16 | RNA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 17 | RNA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Site | 17 | Not acetylated by pat acetylase | ||||
Sequence: K | ||||||
Binding site | 22 | RNA (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 42 | RNA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 44 | RNA (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | cytoplasm | |
Molecular Function | double-stranded DNA binding | |
Molecular Function | identical protein binding | |
Molecular Function | nuclease activity | |
Molecular Function | RNA binding | |
Biological Process | chromosome condensation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA/RNA-binding protein Alba 1
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Saccharolobus
Accessions
- Primary accessionP60849
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2 | Decreases acetylation. | ||||
Sequence: S → A, E, G, L, T, P, or V | ||||||
Mutagenesis | 16 | Decreases DNA binding affinity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 16 | Decreases DNA binding affinity. Unable to repress transcription. Abolishes acetylation. | ||||
Sequence: K → E | ||||||
Mutagenesis | 17 | Decreases DNA binding affinity. Unable to repress transcription. | ||||
Sequence: K → A | ||||||
Mutagenesis | 17 | Decreases DNA binding affinity. No significant effect on acetylation. | ||||
Sequence: K → E | ||||||
Mutagenesis | 60 | Decreases DNA binding affinity and cooperative side-by-side binding between homodimers. | ||||
Sequence: F → A |
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine; by ard1 acetylase | ||||
Sequence: S | ||||||
Chain | PRO_0000151712 | 2-97 | DNA/RNA-binding protein Alba 1 | |||
Sequence: SSGTPTPSNVVLIGKKPVMNYVLAALTLLNQGVSEIVIKARGRAISKAVDTVEIVRNRFLPDKIEIKEIRVGSQVVTSQDGRQSRVSTIEIAIRKK | ||||||
Modified residue | 16 | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 16 | N6,N6-dimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 16 | N6-acetyllysine; by pat acetylase; alternate | ||||
Sequence: K | ||||||
Modified residue | 16 | N6-methyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 31 | Deamidated asparagine; partial | ||||
Sequence: N | ||||||
Modified residue | 32 | Deamidated glutamine; partial | ||||
Sequence: Q | ||||||
Modified residue | 40 | N6-methyllysine; partial | ||||
Sequence: K | ||||||
Modified residue | 48 | N6-acetyllysine; partial | ||||
Sequence: K | ||||||
Modified residue | 51 | Aspartate methyl ester; partial | ||||
Sequence: D | ||||||
Modified residue | 58 | Deamidated asparagine; partial | ||||
Sequence: N | ||||||
Modified residue | 64 | N6-acetyllysine; alternate; partial | ||||
Sequence: K | ||||||
Modified residue | 64 | N6-methyllysine; alternate; partial | ||||
Sequence: K | ||||||
Modified residue | 68 | N6-acetyllysine; partial | ||||
Sequence: K | ||||||
Modified residue | 69 | Glutamate methyl ester (Glu); partial | ||||
Sequence: E | ||||||
Modified residue | 75 | N5-methylglutamine; partial | ||||
Sequence: Q | ||||||
Modified residue | 81 | Aspartate methyl ester; partial | ||||
Sequence: D | ||||||
Modified residue | 97 | N6-methyllysine; partial | ||||
Sequence: K |
Post-translational modification
Acetylated (PubMed:11935028).
Acetylation at Lys-16 by the Pat acetylase decreases DNA-binding affinity (PubMed:15824122).
Deacetylation at Lys-16 by the CobB deacetylase increases DNA-binding affinity (PubMed:11935028).
Acetylation at Ser-2 is involved in the regulation of the turnover of the protein (By similarity).
Acetylation at Lys-16 by the Pat acetylase decreases DNA-binding affinity (PubMed:15824122).
Deacetylation at Lys-16 by the CobB deacetylase increases DNA-binding affinity (PubMed:11935028).
Acetylation at Ser-2 is involved in the regulation of the turnover of the protein (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer; homodimers assemble cooperatively on DNA with consecutive dimers binding end-to-end (PubMed:12198167, PubMed:20082605, PubMed:23271660).
May form higher order oligomers, e.g. homotetramers (By similarity).
Interacts with Alba 2; heterodimers lack cooperative DNA-binding behavior and result in more compact chromatin structures compared to Alba 1 homodimers (PubMed:16004869, PubMed:23271660, PubMed:35454068).
May form higher order oligomers, e.g. homotetramers (By similarity).
Interacts with Alba 2; heterodimers lack cooperative DNA-binding behavior and result in more compact chromatin structures compared to Alba 1 homodimers (PubMed:16004869, PubMed:23271660, PubMed:35454068).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P60849 | albA1 P60849 | 2 | EBI-9021190, EBI-9021190 | |
BINARY | P60849 | albA2 Q97ZF4 | 6 | EBI-9021190, EBI-9021196 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length97
- Mass (Da)10,585
- Last updated2007-01-23 v2
- Checksum22C1BC9CCDB6B013
Sequence caution
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ298830 EMBL· GenBank· DDBJ | CAC12668.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE006641 EMBL· GenBank· DDBJ | AAK41236.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |