ID   ALBA_METMJ              Reviewed;          91 AA.
AC   A3CVI3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=DNA/RNA-binding protein Alba {ECO:0000255|HAMAP-Rule:MF_01122};
GN   Name=albA {ECO:0000255|HAMAP-Rule:MF_01122}; OrderedLocusNames=Memar_1454;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
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; CP000562; ABN57383.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3CVI3; -.
DR   SMR; A3CVI3; -.
DR   STRING; 368407.Memar_1454; -.
DR   EnsemblBacteria; ABN57383; ABN57383; Memar_1454.
DR   KEGG; mem:Memar_1454; -.
DR   eggNOG; arCOG01753; Archaea.
DR   HOGENOM; CLU_110989_1_0_2; -.
DR   OMA; ITRHKFI; -.
DR   Proteomes; UP000002146; 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; RNA-binding.
FT   CHAIN           1..91
FT                   /note="DNA/RNA-binding protein Alba"
FT                   /id="PRO_1000073038"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01122"
SQ   SEQUENCE   91 AA;  9928 MW;  D8F2BE96D1A060CA CRC64;
     MIKDNTVFVG NKPVMNYVLA VVTQFNNGAE EVAIKARGKA ISRAVDTAEI ALNRFLANVD
     KKEIFTSTEM IDTDTGKTNV SSIEIVLTHA K