ID   ALBA_THEAC              Reviewed;          89 AA.
AC   Q9HJQ5;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=DNA/RNA-binding protein Alba {ECO:0000255|HAMAP-Rule:MF_01122};
GN   Name=albA {ECO:0000255|HAMAP-Rule:MF_01122}; OrderedLocusNames=Ta0912;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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; AL445065; CAC12041.1; -; Genomic_DNA.
DR   RefSeq; WP_010901321.1; NC_002578.1.
DR   AlphaFoldDB; Q9HJQ5; -.
DR   SMR; Q9HJQ5; -.
DR   STRING; 273075.Ta0912; -.
DR   EnsemblBacteria; CAC12041; CAC12041; CAC12041.
DR   GeneID; 1456447; -.
DR   KEGG; tac:Ta0912; -.
DR   eggNOG; arCOG01753; Archaea.
DR   HOGENOM; CLU_110989_1_0_2; -.
DR   OMA; ITRHKFI; -.
DR   OrthoDB; 111461at2157; -.
DR   Proteomes; UP000001024; 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..89
FT                   /note="DNA/RNA-binding protein Alba"
FT                   /id="PRO_0000151716"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01122"
SQ   SEQUENCE   89 AA;  9938 MW;  1EEC773A27A3FAB9 CRC64;
     MAEENIIFVG KKPTMNYVLA VVTQFNNNAN KIIIKARGKT ISKAVDVAEI TRHKFIPDAK
     YEEIKLDTET LQGERGSSNV SSIEITLSR