ID   H1_TETTS                Reviewed;         164 AA.
AC   P10156;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Histone H1;
GN   Name=HHO; ORFNames=TTHERM_00823720;
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-29 AND 70-81.
RX   PubMed=3464976; DOI=10.1073/pnas.83.22.8674;
RA   Wu M., Allis C.D., Richman R., Cook R.G., Gorovsky M.A.;
RT   "An intervening sequence in an unusual histone H1 gene of Tetrahymena
RT   thermophila.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:8674-8678(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210;
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
RN   [3]
RP   PHOSPHORYLATION AT THR-47 AND THR-54.
RC   STRAIN=CU427, and CU428;
RX   PubMed=3204116; DOI=10.1083/jcb.107.6.2473;
RA   Roth S.Y., Schulman I.G., Richman R., Cook R.G., Allis C.D.;
RT   "Characterization of phosphorylation sites in histone H1 in the amitotic
RT   macronucleus of Tetrahymena during different physiological states.";
RL   J. Cell Biol. 107:2473-2482(1988).
CC   -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC       chains into higher-order structures.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Macronuclei.
CC   -!- PTM: Cell-growth/division-associated phosphorylation by a CDC2-like
CC       kinase. {ECO:0000269|PubMed:3204116}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAR83811.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; M14854; AAA30119.1; -; Genomic_DNA.
DR   EMBL; GG662466; EAR83811.2; ALT_SEQ; Genomic_DNA.
DR   PIR; A26490; A26490.
DR   RefSeq; XP_001031474.2; XM_001031474.3.
DR   AlphaFoldDB; P10156; -.
DR   iPTMnet; P10156; -.
DR   EnsemblProtists; EAR83811; EAR83811; TTHERM_00823720.
DR   GeneID; 7842709; -.
DR   KEGG; tet:TTHERM_00823720; -.
DR   HOGENOM; CLU_1622325_0_0_1; -.
DR   OMA; TREKKDH; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Chromosome; Direct protein sequencing; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3464976"
FT   CHAIN           2..164
FT                   /note="Histone H1"
FT                   /id="PRO_0000195990"
FT   REGION          1..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         47
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:3204116"
FT   MOD_RES         54
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:3204116"
SQ   SEQUENCE   164 AA;  17779 MW;  45BB0C091929FB48 CRC64;
     MAPRSSTSKS ATREKKDHKK APIKKAIAKK DTKPTPTKGK AASASTTPVK KDVTPVKADT
     KKKIHKTKTM KETVSDAKKT VHAAAGDKKL SKKRPAKEAA KKAINPGKKA AAQPKSTKKE
     VKKDNKTAKK ETKKDHKPAK KEAKKETKPA KKDAKKSSKP AKKN