ID   HARB_PYRAB              Reviewed;          67 AA.
AC   Q9V1F5; G8ZGH6;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Archaeal histone B;
DE   AltName: Full=Archaeal histone A2;
GN   OrderedLocusNames=PYRAB04720; ORFNames=PAB3117;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248284; CAB49394.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69855.1; -; Genomic_DNA.
DR   PIR; C75164; C75164.
DR   RefSeq; WP_010867596.1; NC_000868.1.
DR   AlphaFoldDB; Q9V1F5; -.
DR   SMR; Q9V1F5; -.
DR   STRING; 272844.PAB3117; -.
DR   EnsemblBacteria; CAB49394; CAB49394; PAB3117.
DR   GeneID; 1495368; -.
DR   KEGG; pab:PAB3117; -.
DR   PATRIC; fig|272844.11.peg.499; -.
DR   eggNOG; arCOG02144; Archaea.
DR   HOGENOM; CLU_192667_0_0_2; -.
DR   OMA; ELPVAPC; -.
DR   PhylomeDB; Q9V1F5; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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.
FT   CHAIN           1..67
FT                   /note="Archaeal histone B"
FT                   /id="PRO_0000154999"
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;  7338 MW;  00B8DB475FAFE54A CRC64;
     MAELPIAPVD RLIRKAGAQR VSEKAAKLLA EHLEEKALEI AKKAVDLAKH AGRKTVKVED
     IKLAIRS