ID   H1_TETPY                Reviewed;         165 AA.
AC   P12305;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Histone H1;
GN   Name=HHO;
OS   Tetrahymena pyriformis.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5908;
RN   [1]
RP   PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-83 AND THR-117.
RX   PubMed=3117783; DOI=10.1093/oxfordjournals.jbchem.a122063;
RA   Hayashi T., Hayashi H., Iwai K.;
RT   "Tetrahymena histone H1. Isolation and amino acid sequence lacking the
RT   central hydrophobic domain conserved in other H1 histones.";
RL   J. Biochem. 102:369-376(1987).
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 (By similarity). Is additionally phosphorylated on either Ser-
CC       33, Thr-34 or Thr-35, and on either Thr-39 or Ser-40. {ECO:0000250,
CC       ECO:0000269|PubMed:3117783}.
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DR   PIR; A27195; A27195.
DR   AlphaFoldDB; P12305; -.
DR   iPTMnet; P12305; -.
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.
FT   CHAIN           1..165
FT                   /note="Histone H1"
FT                   /id="PRO_0000195989"
FT   REGION          1..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..155
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         48
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         54
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:3117783"
FT   MOD_RES         117
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:3117783"
SQ   SEQUENCE   165 AA;  17942 MW;  6786E338F9772002 CRC64;
     GKQSTSKSVT REKKDVKKTV APKKAIKKVT KKSTTPVKTS KAAPASTTPI KDTTPVKADA
     KKIHRTKTMK ESVSDAKKTV HKSAGDKKLS RSQKPAKREA AKKIVHPAKK AAAKPKTAKK
     EVKKDTKPVK KDAKKDTKPV KKDAKKDTKP AKKDTKKATK GSKKN