ID   ALBA1_AERPE             Reviewed;          94 AA.
AC   Q9YAW1;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=DNA/RNA-binding protein Alba 1;
GN   Name=albA1; OrderedLocusNames=APE_1832a.1; ORFNames=APES060;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA80837.2; -; Genomic_DNA.
DR   PIR; H72568; H72568.
DR   AlphaFoldDB; Q9YAW1; -.
DR   SMR; Q9YAW1; -.
DR   STRING; 272557.APE_1832a.1; -.
DR   EnsemblBacteria; BAA80837; BAA80837; APE_1832a.1.
DR   KEGG; ape:APE_1832a.1; -.
DR   eggNOG; arCOG01753; Archaea.
DR   Proteomes; UP000002518; 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.
PE   3: Inferred from homology;
KW   Acetylation; Chromosome; Cytoplasm; DNA-binding; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..94
FT                   /note="DNA/RNA-binding protein Alba 1"
FT                   /id="PRO_0000151694"
FT   MOD_RES         16
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   94 AA;  10336 MW;  59FDE158644669F5 CRC64;
     MSIEPQKPNT ILVGRKPTIN YVMAALKLLN EEGAPEVVIK ARGRNICNAV DTVEMLKNLF
     IKNLVIKKVN IYSESLDSEG KKKVSAIEIV VAKG