ID   MLH_TETTS               Reviewed;         633 AA.
AC   P40631;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Micronuclear linker histone polyprotein;
DE            Short=MIC LH;
DE   Contains:
DE     RecName: Full=Micronuclear linker histone-alpha;
DE   Contains:
DE     RecName: Full=Micronuclear linker histone-beta;
DE   Contains:
DE     RecName: Full=Micronuclear linker histone-delta;
DE   Contains:
DE     RecName: Full=Micronuclear linker histone-gamma;
GN   Name=MLH; ORFNames=TTHERM_00471820;
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], PROTEIN SEQUENCE OF 22-44; 68-73;
RP   87-107; 131-162; 168-227; 400-424; 486-495 AND 559-568, AND PROTEOLYTIC
RP   PROCESSING.
RC   STRAIN=CU401;
RX   PubMed=8264578; DOI=10.1128/mcb.14.1.10-20.1994;
RA   Wu M., Allis C.D., Sweet M.T., Cook R.G., Thatcher T.H., Gorovsky M.A.;
RT   "Four distinct and unusual linker proteins in a mitotically dividing
RT   nucleus are derived from a 71-kilodalton polyprotein, lack p34cdc2 sites,
RT   and contain protein kinase A sites.";
RL   Mol. Cell. Biol. 14:10-20(1994).
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).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Micronuclei.
CC   -!- PTM: All four histones are processed from the precursor molecule.
CC       {ECO:0000269|PubMed:8264578}.
CC   -!- PTM: Phosphorylated in growing and dividing cells but not in nongrowing
CC       (starved) cells.
CC   -!- PTM: The N-terminus of MIC LH-alpha and MIC LH-delta is blocked.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAR85403.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M87306; AAC18874.1; -; Unassigned_DNA.
DR   EMBL; GG662622; EAR85403.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001033066.2; XM_001033066.3.
DR   AlphaFoldDB; P40631; -.
DR   SMR; P40631; -.
DR   EnsemblProtists; EAR85403; EAR85403; TTHERM_00471820.
DR   GeneID; 7832262; -.
DR   KEGG; tet:TTHERM_00471820; -.
DR   eggNOG; ENOG502RT0M; Eukaryota.
DR   HOGENOM; CLU_432478_0_0_1; -.
DR   InParanoid; P40631; -.
DR   OMA; ITHEDSP; -.
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.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 2.
DR   SUPFAM; SSF47095; SSF47095; 2.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Direct protein sequencing; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..399
FT                   /note="Micronuclear linker histone-alpha"
FT                   /id="PRO_0000013473"
FT   CHAIN           1..199
FT                   /note="Micronuclear linker histone-delta"
FT                   /id="PRO_0000013474"
FT   CHAIN           200..399
FT                   /note="Micronuclear linker histone-gamma"
FT                   /id="PRO_0000013475"
FT   CHAIN           400..633
FT                   /note="Micronuclear linker histone-beta"
FT                   /id="PRO_0000013476"
FT   DNA_BIND        12..74
FT                   /note="HMG box 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   DNA_BIND        96..164
FT                   /note="HMG box 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          170..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..311
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..348
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..405
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..435
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..495
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..520
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..626
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        554
FT                   /note="N -> P (in Ref. 1; AAC18874)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   633 AA;  70641 MW;  63A3FCDAB8DB3F15 CRC64;
     MELRTKTLNI QPPKKPFSNT YQAFVLEKKN ALGKNFDNKK VQADYNKLSN NEKERLQKLV
     DNAEEKYKEE LFHYNNHIQG KGKQKYVPQV KVPEKPKKPI GSFFRFLEEN RQKYAAKHKD
     LTNAKILKIM SEDFNNLPQK EVKVYEDAYQ KEYAQYLVEF KKWNEKYGQA AQKKQTKRKN
     STSKSRRSSS KGKSSVSKGR TKSTSSKRRA DSSASQGRSQ SSSSNRRKAS SSKDQKGTRS
     SSRKASNSKG RKNSTSNKRN SSSSSKRSSS SKNKKSSSSK NKKSSSSKGR KSSSSRGRKA
     SSSKNRKSSK SKDRKSSSSK GRKSSSSSKS NKRKASSSRG RKSSSSKGRK SSKSQERKNS
     HADTSKQMED EGQKRRQSSS SAKRDESSKK SRRNSMKEAR TKKANNKSAS KASKSGSKSK
     GKSASKSKGK SSSKGKNSKS RSASKPKSNA AQNSNNTHQT ADSSENASST TQTRTRGRQR
     EQKDMVNEKS NSKSSSKGKK NSKSNTRSKS KSKSASKSRK NASKSKKDTT NHGRQTRSKS
     RSESKSKSEA PNKNSNKMEV IEQPKEESSD RKRRESRSQS AKKTSDKKSK NRSDSKKMTA
     EDPKKNNAED SKGKKKSKEG KTGAYGKKAN KKQ