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P60848

- ALBA1_SULSH

UniProt

P60848 - ALBA1_SULSH

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Protein

DNA/RNA-binding protein Alba 1

Gene

albA1

Organism
Sulfolobus shibatae
Status
Reviewed - Annotation score: 4 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. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.

Temperature dependencei

Highly active above 45 degrees Celsius. Poorly active at 25 degrees Celsius.

GO - Molecular functioni

  1. double-stranded DNA binding Source: UniProtKB-HAMAP
  2. RNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. chromosome condensation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

DNA condensation

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA/RNA-binding protein Alba 1
Alternative name(s):
Ssh10b
Gene namesi
Name:albA1
Synonyms:ssh10b
OrganismiSulfolobus shibatae
Taxonomic identifieri2286 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Subcellular locationi

Cytoplasm 1 Publication. Chromosome 1 Publication

GO - Cellular componenti

  1. chromosome Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81P → A: No effect on cis-trans isomerization of dimer. 1 Publication
Mutagenesisi62 – 621P → A: Loss of cis-trans isomerization of dimer. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 9796DNA/RNA-binding protein Alba 1PRO_0000151711Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei17 – 171N6-acetyllysineBy similarity

Post-translational modificationi

Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity).By similarity

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

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.

Structurei

Secondary structure

1
97
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 135Combined sources
Helixi19 – 3113Combined sources
Beta strandi36 – 427Combined sources
Helixi45 – 5915Combined sources
Turni62 – 643Combined sources
Beta strandi65 – 7612Combined sources
Beta strandi80 – 823Combined sources
Beta strandi86 – 9611Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y9XNMR-A/B1-97[»]
3WBMX-ray2.00A/B/C/D1-97[»]
ProteinModelPortaliP60848.
SMRiP60848. Positions 9-97.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60848.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone-like Alba family.Curated

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.

P60848-1 [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 databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98420 Genomic DNA. Translation: CAA67066.1.
PIRiT29101.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98420 Genomic DNA. Translation: CAA67066.1 .
PIRi T29101.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Y9X NMR - A/B 1-97 [» ]
3WBM X-ray 2.00 A/B/C/D 1-97 [» ]
ProteinModelPortali P60848.
SMRi P60848. Positions 9-97.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P60848.

Family and domain databases

Gene3Di 3.30.110.20. 1 hit.
HAMAPi MF_01122. AlbA.
InterProi IPR013795. DNA/RNA-bd_Alba.
IPR002775. DNA/RNA-bd_Alba-like.
[Graphical view ]
Pfami PF01918. Alba. 1 hit.
[Graphical view ]
PIRSFi PIRSF028732. Alba. 1 hit.
SUPFAMi SSF82704. SSF82704. 1 hit.
TIGRFAMsi TIGR00285. TIGR00285. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiALBA1_SULSH
AccessioniPrimary (citable) accession number: P60848
Secondary accession number(s): P74761, Q97ZF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 61 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

Documents

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

External Data

Dasty 3