ID   ALBA1_SULTO             Reviewed;          99 AA.
AC   Q971T8; F9VP01;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=DNA/RNA-binding protein Alba 1;
GN   Name=albA1; OrderedLocusNames=STK_12895; ORFNames=STS141;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome
CC       {ECO:0000250}.
CC   -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may
CC       regulate its activity (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone-like Alba family. {ECO:0000305}.
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DR   EMBL; BA000023; BAK54509.1; -; Genomic_DNA.
DR   RefSeq; WP_010979310.1; NC_003106.2.
DR   AlphaFoldDB; Q971T8; -.
DR   SMR; Q971T8; -.
DR   STRING; 273063.STK_12895; -.
DR   EnsemblBacteria; BAK54509; BAK54509; STK_12895.
DR   GeneID; 42801073; -.
DR   KEGG; sto:STK_12895; -.
DR   PATRIC; fig|273063.9.peg.1448; -.
DR   eggNOG; arCOG01753; Archaea.
DR   OMA; QFNEGAK; -.
DR   OrthoDB; 111461at2157; -.
DR   Proteomes; UP000001015; 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..99
FT                   /note="DNA/RNA-binding protein Alba 1"
FT                   /id="PRO_0000151714"
FT   MOD_RES         18
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   99 AA;  10772 MW;  52A2CF6612E52787 CRC64;
     MSSTATPTPS NVVLVGKKPV MNYVLAALTL LNQGVSEIII KARGRAISKA VDTVEIVRNR
     FLPDKIEVKE IRIGSQVVTS QDGRQSRVST IEIAIRKKA