ID   ALBA_PICTO              Reviewed;          90 AA.
AC   Q6KZR7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=DNA/RNA-binding protein Alba {ECO:0000255|HAMAP-Rule:MF_01122};
GN   Name=albA {ECO:0000255|HAMAP-Rule:MF_01122}; OrderedLocusNames=PTO1200;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC   -!- FUNCTION: Binds double-stranded DNA tightly but without sequence
CC       specificity. It is distributed uniformly and abundantly on the
CC       chromosome, suggesting a role in chromatin architecture. However, it
CC       does not significantly compact DNA. Binds rRNA and mRNA in vivo. May
CC       play a role in maintaining the structural and functional stability of
CC       RNA, and, perhaps, ribosomes. {ECO:0000255|HAMAP-Rule:MF_01122}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01122}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01122}.
CC       Chromosome {ECO:0000255|HAMAP-Rule:MF_01122}.
CC   -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may
CC       regulate its activity. {ECO:0000255|HAMAP-Rule:MF_01122}.
CC   -!- SIMILARITY: Belongs to the histone-like Alba family.
CC       {ECO:0000255|HAMAP-Rule:MF_01122}.
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DR   EMBL; AE017261; AAT43785.1; -; Genomic_DNA.
DR   RefSeq; WP_011178001.1; NC_005877.1.
DR   AlphaFoldDB; Q6KZR7; -.
DR   SMR; Q6KZR7; -.
DR   STRING; 263820.PTO1200; -.
DR   EnsemblBacteria; AAT43785; AAT43785; PTO1200.
DR   GeneID; 2844576; -.
DR   KEGG; pto:PTO1200; -.
DR   PATRIC; fig|263820.9.peg.1247; -.
DR   eggNOG; arCOG01753; Archaea.
DR   HOGENOM; CLU_110989_1_0_2; -.
DR   OMA; ITRHKFI; -.
DR   OrthoDB; 111461at2157; -.
DR   Proteomes; UP000000438; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.110.20; -; 1.
DR   HAMAP; MF_01122; AlbA; 1.
DR   InterPro; IPR036882; Alba-like_dom_sf.
DR   InterPro; IPR013795; DNA/RNA-bd_Alba.
DR   InterPro; IPR002775; DNA/RNA-bd_Alba-like.
DR   Pfam; PF01918; Alba; 1.
DR   PIRSF; PIRSF028732; Alba; 1.
DR   SUPFAM; SSF82704; SSF82704; 1.
DR   TIGRFAMs; TIGR00285; TIGR00285; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chromosome; Cytoplasm; DNA-binding; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..90
FT                   /note="DNA/RNA-binding protein Alba"
FT                   /id="PRO_1000065262"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01122"
SQ   SEQUENCE   90 AA;  10056 MW;  EB83F8C602283D04 CRC64;
     MAEENVIFVG KKPTMNYVLA IVTQFNNNST SRIVIKARGK AISKAVDIAE ITRHKFIQDA
     KYDEIKLDTE SLQGEKGESN VSSIEIVLTR