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P60848 (ALBA1_SULSH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA/RNA-binding protein Alba 1
Alternative name(s):
Ssh10b
Gene names
Name:albA1
Synonyms:ssh10b
OrganismSulfolobus shibatae
Taxonomic identifier2286 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length97 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes. HAMAP-Rule MF_01122

Subunit structure

Homodimer. Two forms exist in solution due to isomerization of the Leu-61/Pro-62 peptide bond. The trans (T) form of the dimer dominates at higher temperatures, whereas the population of the cis (C) form increases at lower temperatures. The T form causes DNA to adopt a supercoiled conformation.

Subcellular location

Cytoplasm. Chromosome Ref.4.

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity By similarity. HAMAP-Rule MF_01122

Sequence similarities

Belongs to the histone-like Alba family.

Biophysicochemical properties

Temperature dependence:

Highly active above 45 degrees Celsius. Poorly active at 25 degrees Celsius. HAMAP-Rule MF_01122

Ontologies

Keywords
   Biological processDNA condensation
   Cellular componentChromosome
Cytoplasm
   LigandDNA-binding
RNA-binding
   PTMAcetylation
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processchromosome condensation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

double-stranded DNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 9796DNA/RNA-binding protein Alba 1 HAMAP-Rule MF_01122
PRO_0000151711

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue171N6-acetyllysine By similarity

Experimental info

Mutagenesis81P → A: No effect on cis-trans isomerization of dimer. Ref.3
Mutagenesis621P → A: Loss of cis-trans isomerization of dimer. Ref.3

Secondary structure

................ 97
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60848 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 22C1BC9CCDB6B013

FASTA9710,585
        10         20         30         40         50         60 
MSSGTPTPSN VVLIGKKPVM NYVLAALTLL NQGVSEIVIK ARGRAISKAV DTVEIVRNRF 

        70         80         90 
LPDKIEIKEI RVGSQVVTSQ DGRQSRVSTI EIAIRKK 

« Hide

References

[1]"Reverse gyrase gene from Sulfolobus shibatae B12: gene structure, transcription unit and comparative sequence analysis of the two domains."
Jaxel C., Bouthier de la Tour C., Duguet M., Nadal M.
Nucleic Acids Res. 24:4668-4675(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12.
[2]"An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion."
Xue H., Guo R., Wen Y., Liu D., Huang L.
J. Bacteriol. 182:3929-3933(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12.
[3]"Two conformations of archaeal Ssh10b. The origin of its temperature-dependent interaction with DNA."
Cui Q., Tong Y., Xue H., Huang L., Feng Y., Wang J.
J. Biol. Chem. 278:51015-51022(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF DIMER CONFORMATIONS, MUTAGENESIS OF PRO-8 AND PRO-62.
[4]"Ssh10b, a conserved thermophilic archaeal protein, binds RNA in vivo."
Guo R., Xue H., Huang L.
Mol. Microbiol. 50:1605-1615(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING TO RNA, SUBCELLULAR LOCATION.
[5]"The two faces of Alba: the evolutionary connection between proteins participating in chromatin structure and RNA metabolism."
Aravind L., Iyer L.M., Anantharaman V.
Genome Biol. 4:R64.1-R64.10(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98420 Genomic DNA. Translation: CAA67066.1.
PIRT29101.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y9XNMR-A/B2-96[»]
3WBMX-ray2.00A/B/C/D1-97[»]
ProteinModelPortalP60848.
SMRP60848. Positions 9-97.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.110.20. 1 hit.
HAMAPMF_01122. AlbA.
InterProIPR013795. DNA/RNA-bd_Alba.
IPR002775. DNA/RNA-bd_Alba-like.
[Graphical view]
PfamPF01918. Alba. 1 hit.
[Graphical view]
PIRSFPIRSF028732. Alba. 1 hit.
SUPFAMSSF82704. SSF82704. 1 hit.
TIGRFAMsTIGR00285. TIGR00285. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP60848.

Entry information

Entry nameALBA1_SULSH
AccessionPrimary (citable) accession number: P60848
Secondary accession number(s): P74761, Q97ZF6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references