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Protein

DNA/RNA-binding protein Alba 1

Gene

albA1

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. May be involved in DNA compaction. May bind rRNA and mRNA, playing a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA condensation

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-913-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA/RNA-binding protein Alba 1
Alternative name(s):
Sso10b
Gene namesi
Name:albA1
Synonyms:sso10b
Ordered Locus Names:SSO0962
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001974 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161K → A or V: Unable to repress transcription. 1 Publication
Mutagenesisi17 – 171K → A or V: Unable to repress transcription. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 9796DNA/RNA-binding protein Alba 1PRO_0000151712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei17 – 171N6-acetyllysine1 Publication

Post-translational modificationi

Acetylated. Deacetylation by the SIR2-homolog deacetylase increases its DNA-binding affinity, thereby repressing transcription. Regulation of DNA-based activities is therefore achieved at the chromatin level.1 Publication

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

DIPiDIP-48444N.
STRINGi273057.SSO0962.

Structurei

Secondary structure

1
97
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 133Combined sources
Helixi19 – 3113Combined sources
Beta strandi36 – 427Combined sources
Helixi45 – 5915Combined sources
Turni62 – 643Combined sources
Beta strandi65 – 7915Combined sources
Beta strandi84 – 9613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H0XX-ray2.60A/B1-97[»]
1H0YX-ray2.80A1-97[»]
2BKYX-ray1.70A/B1-97[»]
4R3LX-ray1.84B2-7[»]
ProteinModelPortaliP60849.
SMRiP60849. Positions 9-97.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60849.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone-like Alba family.Curated

Phylogenomic databases

eggNOGiarCOG01753. Archaea.
COG1581. LUCA.
HOGENOMiHOG000105803.
InParanoidiP60849.
KOiK03622.
OMAiYVIATVM.

Family and domain databases

Gene3Di3.30.110.20. 1 hit.
HAMAPiMF_01122. AlbA.
InterProiIPR013795. DNA/RNA-bd_Alba.
IPR002775. DNA/RNA-bd_Alba-like.
[Graphical view]
PfamiPF01918. Alba. 1 hit.
[Graphical view]
PIRSFiPIRSF028732. Alba. 1 hit.
SUPFAMiSSF82704. SSF82704. 1 hit.
TIGRFAMsiTIGR00285. TIGR00285. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P60849-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSGTPTPSN VVLIGKKPVM NYVLAALTLL NQGVSEIVIK ARGRAISKAV
60 70 80 90
DTVEIVRNRF LPDKIEIKEI RVGSQVVTSQ DGRQSRVSTI EIAIRKK
Length:97
Mass (Da):10,585
Last modified:January 23, 2007 - v2
Checksum:i22C1BC9CCDB6B013
GO

Sequence cautioni

The sequence AAK41236.1 differs from that shown. Reason: Erroneous initiation. Curated

Mass spectrometryi

Molecular mass is 10538 Da from positions 2 - 97. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ298830 Genomic DNA. Translation: CAC12668.1.
AE006641 Genomic DNA. Translation: AAK41236.1. Different initiation.
PIRiE90247.
RefSeqiWP_009992406.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK41236; AAK41236; SSO0962.
GeneIDi8761191.
KEGGisso:SSO0962.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ298830 Genomic DNA. Translation: CAC12668.1.
AE006641 Genomic DNA. Translation: AAK41236.1. Different initiation.
PIRiE90247.
RefSeqiWP_009992406.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H0XX-ray2.60A/B1-97[»]
1H0YX-ray2.80A1-97[»]
2BKYX-ray1.70A/B1-97[»]
4R3LX-ray1.84B2-7[»]
ProteinModelPortaliP60849.
SMRiP60849. Positions 9-97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48444N.
STRINGi273057.SSO0962.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK41236; AAK41236; SSO0962.
GeneIDi8761191.
KEGGisso:SSO0962.

Phylogenomic databases

eggNOGiarCOG01753. Archaea.
COG1581. LUCA.
HOGENOMiHOG000105803.
InParanoidiP60849.
KOiK03622.
OMAiYVIATVM.

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-913-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP60849.

Family and domain databases

Gene3Di3.30.110.20. 1 hit.
HAMAPiMF_01122. AlbA.
InterProiIPR013795. DNA/RNA-bd_Alba.
IPR002775. DNA/RNA-bd_Alba-like.
[Graphical view]
PfamiPF01918. Alba. 1 hit.
[Graphical view]
PIRSFiPIRSF028732. Alba. 1 hit.
SUPFAMiSSF82704. SSF82704. 1 hit.
TIGRFAMsiTIGR00285. TIGR00285. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Thermostable DNA-binding proteins from extremophilic Archaea, characterization and heterologous expression of 10kDa proteins from Sulfolobus solfataricus and Sulfolobus shibatae."
    Wu X.Q., Oppermann M., Knapp S., Berndt K.D., Bergman T., Joernvall H., Oppermann U.C.T.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  3. "The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation."
    Bell S.D., Botting C.H., Wardleworth B.N., Jackson S.P., White M.F.
    Science 296:148-151(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT SER-2 AND LYS-17, REGULATION OF ACTIVITY, MASS SPECTROMETRY, MUTAGENESIS OF LYS-16 AND LYS-17.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  4. "Structure of Alba: an archaeal chromatin protein modulated by acetylation."
    Wardleworth B.N., Russell R.J.M., Bell S.D., Taylor G.L., White M.F.
    EMBO J. 21:4654-4662(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.

Entry informationi

Entry nameiALBA1_SULSO
AccessioniPrimary (citable) accession number: P60849
Secondary accession number(s): P74761, Q97ZF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.