ID   ALBA2_ARCFU             Reviewed;          89 AA.
AC   O28323;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=DNA/RNA-binding protein Alba 2;
DE   AltName: Full=Af1;
GN   Name=albA2; OrderedLocusNames=AF_1956;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS), AND MUTAGENESIS OF ASN-10; LYS-11;
RP   LEU-18 AND PHE-54.
RX   PubMed=12730210; DOI=10.1074/jbc.m303666200;
RA   Zhao K., Chai X., Marmorstein R.;
RT   "Structure of a Sir2 substrate, Alba, reveals a mechanism for
RT   deacetylation-induced enhancement of DNA binding.";
RL   J. Biol. Chem. 278:26071-26077(2003).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Chromosome
CC       {ECO:0000305}.
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; AE000782; AAB89299.1; -; Genomic_DNA.
DR   PIR; C69494; C69494.
DR   RefSeq; WP_010879448.1; NC_000917.1.
DR   PDB; 1NFH; X-ray; 2.65 A; A/B=1-89.
DR   PDB; 1NFJ; X-ray; 2.00 A; A=1-89.
DR   PDBsum; 1NFH; -.
DR   PDBsum; 1NFJ; -.
DR   AlphaFoldDB; O28323; -.
DR   SMR; O28323; -.
DR   STRING; 224325.AF_1956; -.
DR   EnsemblBacteria; AAB89299; AAB89299; AF_1956.
DR   GeneID; 24795698; -.
DR   KEGG; afu:AF_1956; -.
DR   eggNOG; arCOG01753; Archaea.
DR   HOGENOM; CLU_110989_1_0_2; -.
DR   OMA; QFNEGAK; -.
DR   OrthoDB; 111461at2157; -.
DR   PhylomeDB; O28323; -.
DR   EvolutionaryTrace; O28323; -.
DR   Proteomes; UP000002199; 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   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chromosome; Cytoplasm; DNA-binding;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..89
FT                   /note="DNA/RNA-binding protein Alba 2"
FT                   /id="PRO_0000151697"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         10
FT                   /note="N->A: Slight decrease in ability to bind DNA."
FT                   /evidence="ECO:0000269|PubMed:12730210"
FT   MUTAGEN         11
FT                   /note="K->R,Q,M: Less stable tetramers; decreased ability
FT                   to bind DNA."
FT                   /evidence="ECO:0000269|PubMed:12730210"
FT   MUTAGEN         18
FT                   /note="L->R: Less stable tetramers; decreased ability to
FT                   bind DNA."
FT                   /evidence="ECO:0000269|PubMed:12730210"
FT   MUTAGEN         54
FT                   /note="F->R: Less stable tetramers; decreased ability to
FT                   bind DNA."
FT                   /evidence="ECO:0000269|PubMed:12730210"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:1NFJ"
FT   HELIX           13..25
FT                   /evidence="ECO:0007829|PDB:1NFJ"
FT   STRAND          29..36
FT                   /evidence="ECO:0007829|PDB:1NFJ"
FT   HELIX           39..53
FT                   /evidence="ECO:0007829|PDB:1NFJ"
FT   STRAND          59..69
FT                   /evidence="ECO:0007829|PDB:1NFJ"
FT   STRAND          79..88
FT                   /evidence="ECO:0007829|PDB:1NFJ"
SQ   SEQUENCE   89 AA;  9894 MW;  96071A4C48CB8ED7 CRC64;
     MAEHVVYVGN KPVMNYVLAT LTQLNEGADE VVIKARGRAI SRAVDVAEIV RNRFMPGVKV
     KEIKIDTEEL ESEQGRRSNV STIEIVLAK