ID   RT106_VANPO             Reviewed;         459 AA.
AC   A7TRU5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Histone chaperone RTT106;
GN   Name=RTT106; ORFNames=Kpol_400p6;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- FUNCTION: Histones H3 and H4 chaperone involved in the nucleosome
CC       formation and heterochromatin silencing. Required for the deposition of
CC       H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role
CC       in the transcriptional regulation of the cell-cycle dependent histone
CC       genes by creating a repressive structure at the core histone gene
CC       promoter (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with histones H3 and H4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RTT106 family. {ECO:0000305}.
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DR   EMBL; DS480488; EDO15012.1; -; Genomic_DNA.
DR   RefSeq; XP_001642870.1; XM_001642820.1.
DR   AlphaFoldDB; A7TRU5; -.
DR   SMR; A7TRU5; -.
DR   STRING; 436907.A7TRU5; -.
DR   EnsemblFungi; EDO15012; EDO15012; Kpol_400p6.
DR   GeneID; 5543059; -.
DR   KEGG; vpo:Kpol_400p6; -.
DR   eggNOG; ENOG502R9PE; Eukaryota.
DR   HOGENOM; CLU_040939_1_0_1; -.
DR   InParanoid; A7TRU5; -.
DR   OMA; TRLTFNV; -.
DR   OrthoDB; 1283058at2759; -.
DR   PhylomeDB; A7TRU5; -.
DR   Proteomes; UP000000267; 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   CDD; cd11604; RTT106_N; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 6.10.10.70; -; 1.
DR   InterPro; IPR013719; DUF1747.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR040993; Rtt106_N.
DR   InterPro; IPR044891; Rtt106_N_sf.
DR   InterPro; IPR040770; Rtt106_PH.
DR   Pfam; PF18469; PH_18; 1.
DR   Pfam; PF08512; Rtt106; 1.
DR   Pfam; PF18215; Rtt106_N; 1.
DR   SMART; SM01287; Rtt106; 1.
PE   3: Inferred from homology;
KW   Chaperone; Chromosome; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..459
FT                   /note="Histone chaperone RTT106"
FT                   /id="PRO_0000320500"
FT   REGION          304..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..402
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..425
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   459 AA;  52469 MW;  51220A87D0FEDC80 CRC64;
     MTDSFLDKLP AGLKSKVSTI IRALPSSKSV FQELYEFALN ENDDSKRKMS KNSPSDICAS
     LEPVHEEFTI FKIEDVTILS PIRKKLNLVL HISPTTKKPL LSLTNKDGGQ ELTIEDLNKN
     ISMATFLPVP EKKNIFYMFI NYKESVGSKY TEPVLITINK TNILEQFKKV GLIDLEIQDF
     TKCIEYIRKQ AILTGFRMSD PFFSVRQDSD SVPSFHVEGH RGTKEGTLYF LPDHIIFGFK
     KPILLFQSID IESITYSSIT RLTFNVTLIT KNDEKFEFSM IDQTEYSKID EYVKMRQVKD
     RSMSEELKAK TANKNQQSQN EDDEQISALE AAAQQMEKNM NINDIPVDSD DEEDDGNFEA
     ESDLSDGSDV EAEDDYAEDD EDDEDEEDEE DKEDEENDRF EHNEDQYEEK EASLLDIEHG
     DSVNYDDPGQ DGFSVDLGID DVPIELDEDD EEGSGVEYD