ID   ALBA_IGNH4              Reviewed;          97 AA.
AC   A8A8V6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=DNA/RNA-binding protein Alba {ECO:0000255|HAMAP-Rule:MF_01122};
GN   Name=albA {ECO:0000255|HAMAP-Rule:MF_01122}; OrderedLocusNames=Igni_0174;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
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; CP000816; ABU81358.1; -; Genomic_DNA.
DR   RefSeq; WP_011998210.1; NC_009776.1.
DR   AlphaFoldDB; A8A8V6; -.
DR   SMR; A8A8V6; -.
DR   STRING; 453591.Igni_0174; -.
DR   EnsemblBacteria; ABU81358; ABU81358; Igni_0174.
DR   GeneID; 5562396; -.
DR   KEGG; iho:Igni_0174; -.
DR   eggNOG; arCOG01753; Archaea.
DR   HOGENOM; CLU_110989_1_0_2; -.
DR   OMA; QFNEGAK; -.
DR   OrthoDB; 111461at2157; -.
DR   PhylomeDB; A8A8V6; -.
DR   Proteomes; UP000000262; 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..97
FT                   /note="DNA/RNA-binding protein Alba"
FT                   /id="PRO_1000073037"
FT   MOD_RES         16
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01122"
SQ   SEQUENCE   97 AA;  10711 MW;  6F09B614E4CC9F19 CRC64;
     MAAQIPQSNE VRVGKKPVMN YVLATLTLLN QGVDRIEIKA RGRAISKAVD TVEIVRNRFL
     PGQVRVAEIR IGSQTVTSAD GRQSRISTID IVLERVK