ID   HARB_PYRHO              Reviewed;          67 AA.
AC   O74092;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Archaeal histone B;
DE   AltName: Full=Archaeal histone A2;
GN   OrderedLocusNames=PH1701.1; ORFNames=PHS046;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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 (By
CC       similarity). {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA30815.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000001; BAA30815.1; ALT_INIT; Genomic_DNA.
DR   PIR; H71177; H71177.
DR   RefSeq; WP_048053461.1; NC_000961.1.
DR   AlphaFoldDB; O74092; -.
DR   SMR; O74092; -.
DR   STRING; 70601.3258132; -.
DR   EnsemblBacteria; BAA30815; BAA30815; BAA30815.
DR   GeneID; 1442548; -.
DR   KEGG; pho:PHS046; -.
DR   eggNOG; arCOG02144; Archaea.
DR   OMA; ELPVAPC; -.
DR   Proteomes; UP000000752; 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   GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR003958; CBFA_NFYB_domain.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR   Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR   SMART; SM00803; TAF; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
PE   3: Inferred from homology;
KW   Chromosome; Cytoplasm; DNA-binding.
FT   CHAIN           1..67
FT                   /note="Archaeal histone B"
FT                   /id="PRO_0000155001"
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;  7366 MW;  00A04ACE5FAFE54A CRC64;
     MAELPIAPVD RLIRKAGAQR VSEKAAKLLA EHLEEKALEI ARKAVDLAKH AGRKTVKVED
     IKLAIRS