ID   ALBA2_METKA             Reviewed;          93 AA.
AC   Q8TWE6;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=DNA/RNA-binding protein Alba 2;
GN   Name=albA2; OrderedLocusNames=MK1089;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009439; AAM02302.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TWE6; -.
DR   SMR; Q8TWE6; -.
DR   STRING; 190192.MK1089; -.
DR   EnsemblBacteria; AAM02302; AAM02302; MK1089.
DR   KEGG; mka:MK1089; -.
DR   PATRIC; fig|190192.8.peg.1144; -.
DR   HOGENOM; CLU_110989_1_0_2; -.
DR   OMA; ITRHKFI; -.
DR   Proteomes; UP000001826; 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..93
FT                   /note="DNA/RNA-binding protein Alba 2"
FT                   /id="PRO_0000151700"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   93 AA;  10142 MW;  E11D650FD5F63169 CRC64;
     MAEENVIYVG NKPVTNYVLA VMTQFSEGAD EVKLVARGRA ISRAVDVAEF IRNNVMPEVE
     VKDIEIGTEE IETEEGDTIS VSTIAITLAK PSE