HARB_PYRFU
ID HARB_PYRFU Reviewed; 67 AA.
AC O59627;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Archaeal histone B;
DE AltName: Full=Archaeal histone A2;
GN OrderedLocusNames=PF1722;
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 [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RA Kanai A., Oida H., Hasegawa A., Doi H.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25805.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB013081; BAA25805.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE009950; AAL81846.1; -; Genomic_DNA.
DR RefSeq; WP_011012868.1; NZ_CP023154.1.
DR AlphaFoldDB; O59627; -.
DR SMR; O59627; -.
DR STRING; 186497.PF1722; -.
DR EnsemblBacteria; AAL81846; AAL81846; PF1722.
DR GeneID; 41713553; -.
DR KEGG; pfu:PF1722; -.
DR PATRIC; fig|186497.12.peg.1790; -.
DR eggNOG; arCOG02144; Archaea.
DR HOGENOM; CLU_192667_0_0_2; -.
DR OMA; ELPVAPC; -.
DR OrthoDB; 127272at2157; -.
DR PhylomeDB; O59627; -.
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 B"
FT /id="PRO_0000155000"
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; 7282 MW; FC599CFA66FCC70B CRC64;
MGELPIAPVD RLIRKAGAQR VSEQAAKVLA EHLEEKAIEI AKKAVDLAKH AGRKTVKVED
IKLAIKS