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P60848

- ALBA1_SULSH

UniProt

P60848 - ALBA1_SULSH

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
  1. 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

    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-SubCell
    2. cytoplasm Source: UniProtKB-SubCell

    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 – 135
    Helixi19 – 3113
    Beta strandi36 – 427
    Helixi45 – 5915
    Turni62 – 643
    Beta strandi65 – 7612
    Beta strandi80 – 823
    Beta strandi86 – 9611

    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

    MSSGTPTPSN VVLIGKKPVM NYVLAALTLL NQGVSEIVIK ARGRAISKAV   50
    DTVEIVRNRF LPDKIEIKEI RVGSQVVTSQ DGRQSRVSTI EIAIRKK 97
    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 1, 2014
    This is version 60 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