ID   HARA_PYRFU              Reviewed;          67 AA.
AC   P61882; P58298; Q9V1T0;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Archaeal histone A;
DE   AltName: Full=Archaeal histone A1;
GN   OrderedLocusNames=PF1831;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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:0000250|UniProtKB:P19267}.
CC   -!- SUBUNIT: Homodimer or heterodimer with another histone. Dimers then
CC       assemble into higher oligomers, with the DNA wrapped around the protein
CC       core (By similarity). {ECO:0000250|UniProtKB:P19267}.
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; AE009950; AAL81955.1; -; Genomic_DNA.
DR   RefSeq; WP_010867469.1; NZ_CP023154.1.
DR   AlphaFoldDB; P61882; -.
DR   SMR; P61882; -.
DR   STRING; 186497.PF1831; -.
DR   PRIDE; P61882; -.
DR   EnsemblBacteria; AAL81955; AAL81955; PF1831.
DR   GeneID; 41713650; -.
DR   KEGG; pfu:PF1831; -.
DR   PATRIC; fig|186497.12.peg.1902; -.
DR   eggNOG; arCOG02144; Archaea.
DR   HOGENOM; CLU_192667_0_0_2; -.
DR   OMA; CKHAGRK; -.
DR   OrthoDB; 127272at2157; -.
DR   PhylomeDB; P61882; -.
DR   Proteomes; UP000001013; Chromosome.
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   3: Inferred from homology;
KW   Chromosome; Cytoplasm; DNA-binding; Reference proteome.
FT   CHAIN           1..67
FT                   /note="Archaeal histone A"
FT                   /id="PRO_0000154995"
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"
SQ   SEQUENCE   67 AA;  7406 MW;  D0B1353EB0CECC68 CRC64;
     MGELPIAPVD RLIRKAGAER VSEQAAKVLA EYLEEYAIEV AKKAVEFARH AGRKTVKVED
     IKLAIKS