RT106_VANPO
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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