RT106_YEAS7
ID RT106_YEAS7 Reviewed; 455 AA.
AC A6ZRN4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Histone chaperone RTT106;
DE AltName: Full=Regulator of Ty1 transposition protein 106;
GN Name=RTT106; ORFNames=SCY_4595;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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 directly recruiting the SWI/SNF and RSC chromatin remodeling
CC complexes to the histone genes in a cell cycle dependent manner. In
CC cooperation with HIR and ASF1, creates a repressive structure at the
CC core histone gene promoter and contributes to their repression outside
CC of S phase. Involved in regulation of Ty1 transposition (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the SWI/SNF, RSC and HIR complexes. Interacts
CC with RLF2, SIR4, YTA7 and histones H3 and H4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- DOMAIN: The N-ter domain (residues 1-67) homodimerizes and interacts
CC with H3-H4 independently of acetylation while the double pleckstrin-
CC homology (PH) domain (residues 68-301) binds the 'Lys-56'-containing
CC region of H3. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RTT106 family. {ECO:0000305}.
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DR EMBL; AAFW02000067; EDN62616.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZRN4; -.
DR SMR; A6ZRN4; -.
DR PRIDE; A6ZRN4; -.
DR EnsemblFungi; EDN62616; EDN62616; SCY_4595.
DR HOGENOM; CLU_040939_1_0_1; -.
DR Proteomes; UP000007060; 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 GO; GO:0032196; P:transposition; 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 Acetylation; Chaperone; Chromosome; DNA-binding; Nucleus; Phosphoprotein;
KW Repeat; Transcription; Transcription regulation; Transposition.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P40161"
FT CHAIN 2..455
FT /note="Histone chaperone RTT106"
FT /id="PRO_0000320502"
FT DOMAIN 68..200
FT /note="PH 1"
FT DOMAIN 217..301
FT /note="PH 2"
FT REGION 2..67
FT /note="Dimeric region"
FT /evidence="ECO:0000250"
FT REGION 68..301
FT /note="Double PH domain"
FT /evidence="ECO:0000250"
FT REGION 305..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..396
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P40161"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40161"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40161"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40161"
SQ SEQUENCE 455 AA; 51563 MW; 7BA75A659A7F4F4D CRC64;
MSKLFLDELP ESLSRKIGTV VRVLPSSLEI FEELYKYALN ENSNDRSGRH KKPRIDVSSD
LLKTDEISET NTIFKLEGVS VLSPLRKKLD LVFYLSNVDG SPVITLLKGN DRELSIYQLN
KNIKMASFLP VPEKPNLIYL FMTYTSCEDN KFSEPVVMTL NKENTLNQFK NLGLLDSNVT
DFEKCVEYIR KQAILTGFKI SNPFVNSTLV DTDAEKINSF HLQCHRGTKE GTLYFLPDHI
IFGFKKPILL FDASDIESIT YSSITRLTFN ASLVTKDGEK YEFSMIDQTE YAKIDDYVKR
KQMKDKSMSE ELKAKSKSKG QATDGTADQP SILQEATRQM QDEKKAGVFS DDDEENDQNF
EAESDLSDGS GQESSDGAED GEEAEEDDEE DDEEEDKKGQ SALNRDNSFA SINGQPEQEL
QYKEFKEPLE LEDIPIEIGN DDDEDDEDGS GVEYD
