ID   ALBA_METST              Reviewed;          90 AA.
AC   Q2NHL8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=DNA/RNA-binding protein Alba {ECO:0000255|HAMAP-Rule:MF_01122};
GN   Name=albA {ECO:0000255|HAMAP-Rule:MF_01122}; OrderedLocusNames=Msp_0198;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC56615.1; -; Genomic_DNA.
DR   RefSeq; WP_011405814.1; NC_007681.1.
DR   AlphaFoldDB; Q2NHL8; -.
DR   SMR; Q2NHL8; -.
DR   STRING; 339860.Msp_0198; -.
DR   EnsemblBacteria; ABC56615; ABC56615; Msp_0198.
DR   GeneID; 41324771; -.
DR   KEGG; mst:Msp_0198; -.
DR   eggNOG; arCOG01753; Archaea.
DR   HOGENOM; CLU_110989_1_0_2; -.
DR   OMA; QFNEGAK; -.
DR   OrthoDB; 111461at2157; -.
DR   Proteomes; UP000001931; 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_1000073040"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01122"
SQ   SEQUENCE   90 AA;  9795 MW;  7655E3F106016136 CRC64;
     MAEENIVYIG NKPVMNYVLA VVTQMNSGVT EVILKARGRA ISRAVDVAEI VRNRFISDVD
     VKSIDISTEE IVGNEGTSSN VSAIEIRLSK