HARB_THEKO
ID HARB_THEKO Reviewed; 67 AA.
AC Q9Y8I2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Archaeal histone B;
DE AltName: Full=Archaeal histone A2;
GN Name=hpkB; OrderedLocusNames=TK2289;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=10329402; DOI=10.1006/bbrc.1999.0533;
RA Higashibata H., Fujiwara S., Takagi M., Imanaka T.;
RT "Analysis of DNA compaction profile and intracellular contents of archaeal
RT histones from Pyrococcus kodakaraensis KOD1.";
RL Biochem. Biophys. Res. Commun. 258:416-424(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Binds and compacts DNA (about 120 base pairs per nucleosome,
CC corresponding to four histone dimers) to form nucleosome-like
CC structures. {ECO:0000269|PubMed:10329402}.
CC -!- SUBUNIT: Homodimer or heterodimer. Dimers then assemble into higher
CC oligomers, with the DNA wrapped around the protein core. Higher order
CC oligomerization of these structures can give rise to long, superhelical
CC fibers (in vitro). {ECO:0000250|UniProtKB:Q9Y8I1}.
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; AB016004; BAA77576.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD86478.1; -; Genomic_DNA.
DR RefSeq; WP_011251239.1; NC_006624.1.
DR AlphaFoldDB; Q9Y8I2; -.
DR SMR; Q9Y8I2; -.
DR STRING; 69014.TK2289; -.
DR EnsemblBacteria; BAD86478; BAD86478; TK2289.
DR GeneID; 34863161; -.
DR KEGG; tko:TK2289; -.
DR PATRIC; fig|69014.16.peg.2244; -.
DR eggNOG; arCOG02144; Archaea.
DR HOGENOM; CLU_192667_0_0_2; -.
DR InParanoid; Q9Y8I2; -.
DR OMA; ELPVAPC; -.
DR OrthoDB; 127272at2157; -.
DR PhylomeDB; Q9Y8I2; -.
DR Proteomes; UP000000536; 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; Reference proteome.
FT CHAIN 1..67
FT /note="Archaeal histone B"
FT /id="PRO_0000155002"
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; 7167 MW; E0231457521F85EE CRC64;
MAELPIAPVD RLIRKAGAAR VSEEAAKVLA EHLEEKALEI AKKAVALAQH AGRKTVKAED
IKLAIKS
