ID   HMVA_METJA              Reviewed;          96 AA.
AC   Q59041;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=DNA-binding protein HmvA;
GN   Name=hmvA; OrderedLocusNames=MJ1647;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   SUBUNIT.
RX   PubMed=10741836; DOI=10.1007/s007920050006;
RA   Li W.-T., Sandman K., Pereira S.L., Reeve J.N.;
RT   "MJ1647, an open reading frame in the genome of the hyperthermophile
RT   Methanococcus jannaschii, encodes a very thermostable archaeal histone with
RT   a C-terminal extension.";
RL   Extremophiles 4:43-51(2000).
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 (PubMed:10741836). Dimers then assemble into higher
CC       oligomers, with the DNA wrapped around the protein core (By
CC       similarity). {ECO:0000250|UniProtKB:P19267,
CC       ECO:0000269|PubMed:10741836}.
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; L77117; AAB99668.1; -; Genomic_DNA.
DR   PIR; E64505; E64505.
DR   RefSeq; WP_010871171.1; NC_000909.1.
DR   AlphaFoldDB; Q59041; -.
DR   SMR; Q59041; -.
DR   STRING; 243232.MJ_1647; -.
DR   EnsemblBacteria; AAB99668; AAB99668; MJ_1647.
DR   GeneID; 1452556; -.
DR   KEGG; mja:MJ_1647; -.
DR   eggNOG; arCOG02145; Archaea.
DR   HOGENOM; CLU_2340228_0_0_2; -.
DR   OMA; MKENTDM; -.
DR   OrthoDB; 110775at2157; -.
DR   Proteomes; UP000000805; 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   1: Evidence at protein level;
KW   Chromosome; Cytoplasm; DNA-binding; Reference proteome.
FT   CHAIN           1..96
FT                   /note="DNA-binding protein HmvA"
FT                   /id="PRO_0000155005"
FT   REGION          52..55
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P19267"
FT   SITE            12
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P19267"
SQ   SEQUENCE   96 AA;  11201 MW;  D64F2C5841855C42 CRC64;
     MLPKATVKRI MKQHTDFNIS AEAVDELCNM LEEIIKITTE VAEQNARKEG RKTIKARDIK
     QCDDERLKRK IMELSERTDK MPILIKEMLN VITSEL