ID   HFO2_METFO              Reviewed;          68 AA.
AC   P48783;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Archaeal histone A2;
GN   Name=hfoA2;
OS   Methanobacterium formicicum.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX   NCBI_TaxID=2162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP   SUBUNIT.
RC   STRAIN=JF-1;
RX   PubMed=7836329; DOI=10.1128/jb.177.3.858-860.1995;
RA   Darcy T.J., Sandman K.M., Reeve J.N.;
RT   "Methanobacterium formicicum, a mesophilic methanogen, contains three HFo
RT   histones.";
RL   J. Bacteriol. 177:858-860(1995).
CC   -!- FUNCTION: Binds and compact DNA (95 to 150 base pairs) to form
CC       nucleosome-like structures that contain positive DNA supercoils.
CC       Increases the resistance of DNA to thermal denaturation (in vitro).
CC       {ECO:0000305|PubMed:7836329}.
CC   -!- SUBUNIT: Homodimer or heterodimer with another histone
CC       (PubMed:7836329). Dimers then assemble into higher oligomers, with the
CC       DNA wrapped around the protein core (By similarity).
CC       {ECO:0000250|UniProtKB:P19267, ECO:0000305|PubMed:7836329}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Chromosome
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the archaeal histone HMF family. {ECO:0000305}.
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DR   EMBL; U12931; AAA67722.1; -; Genomic_DNA.
DR   RefSeq; WP_004031856.1; NZ_CP017767.1.
DR   AlphaFoldDB; P48783; -.
DR   SMR; P48783; -.
DR   STRING; 2162.BRM9_1489; -.
DR   PRIDE; P48783; -.
DR   GeneID; 35125170; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR003958; CBFA_NFYB_domain.
DR   InterPro; IPR009072; Histone-fold.
DR   Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Cytoplasm; Direct protein sequencing; DNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..68
FT                   /note="Archaeal histone A2"
FT                   /id="PRO_0000154985"
FT   REGION          20..22
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P19267"
FT   REGION          54..57
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P19267"
FT   SITE            14
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P19267"
SQ   SEQUENCE   68 AA;  7195 MW;  93AFCAA3A34F4886 CRC64;
     MAELPIAPVG RIIKNAGAQR ISDDAKEALA KALEENGEEL AKKAVELAKH AGRKTVKAED
     IEMAVKSA