HMT1_METTH
ID HMT1_METTH Reviewed; 68 AA.
AC P50483;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=DNA-binding protein HMt-1.1;
DE AltName: Full=Archaeal histone A1;
GN Name=hmtA1; Synonyms=hmtA {ECO:0000303|PubMed:1459937};
GN OrderedLocusNames=MTH_821;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=1459937; DOI=10.1128/jb.174.24.7890-7895.1992;
RA Tabassum R., Sandman K.M., Reeve J.N.;
RT "HMt, a histone-related protein from Methanobacterium thermoautotrophicum
RT delta H.";
RL J. Bacteriol. 174:7890-7895(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Binds and compacts DNA (95 to 150 base pairs) to form
CC nucleosome-like structures that contain positive DNA supercoils.
CC {ECO:0000269|PubMed:1459937}.
CC -!- SUBUNIT: Homodimer or heterodimer with HmtB (PubMed:1459937). Dimers
CC then assemble into higher oligomers, with the DNA wrapped around the
CC protein core (By similarity). {ECO:0000250|UniProtKB:P19267,
CC ECO:0000305|PubMed:1459937}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:1459937}.
CC Chromosome {ECO:0000305|PubMed:1459937}.
CC -!- SIMILARITY: Belongs to the archaeal histone HMF family. {ECO:0000305}.
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DR EMBL; M90086; AAA73227.1; -; Genomic_DNA.
DR EMBL; AE000666; AAB85321.1; -; Genomic_DNA.
DR PIR; G69209; G69209.
DR RefSeq; WP_010876456.1; NC_000916.1.
DR AlphaFoldDB; P50483; -.
DR SMR; P50483; -.
DR STRING; 187420.MTH_821; -.
DR EnsemblBacteria; AAB85321; AAB85321; MTH_821.
DR GeneID; 24853954; -.
DR KEGG; mth:MTH_821; -.
DR PATRIC; fig|187420.15.peg.806; -.
DR HOGENOM; CLU_192667_0_0_2; -.
DR OMA; ELPVAPC; -.
DR Proteomes; UP000005223; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..68
FT /note="DNA-binding protein HMt-1.1"
FT /id="PRO_0000154991"
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"
FT SITE 14
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P19267"
SQ SEQUENCE 68 AA; 7283 MW; 9BB488EE1E2D1D86 CRC64;
MAELPIAPVG RIIKNAGAQR ISDDAKEALA KALEEMGEEI SRKAVELAKH AGRKTVKATD
IEMAAKQL
