RT106_KLULA
ID RT106_KLULA Reviewed; 459 AA.
AC Q6CQ86;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Histone chaperone RTT106;
GN Name=RTT106; OrderedLocusNames=KLLA0D18986g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382124; CAH00999.1; -; Genomic_DNA.
DR RefSeq; XP_453903.1; XM_453903.1.
DR AlphaFoldDB; Q6CQ86; -.
DR SMR; Q6CQ86; -.
DR STRING; 28985.XP_453903.1; -.
DR EnsemblFungi; CAH00999; CAH00999; KLLA0_D18986g.
DR GeneID; 2892814; -.
DR KEGG; kla:KLLA0_D18986g; -.
DR eggNOG; ENOG502R9PE; Eukaryota.
DR HOGENOM; CLU_040939_1_0_1; -.
DR InParanoid; Q6CQ86; -.
DR OMA; TRLTFNV; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0031507; P:heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
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_0000320493"
FT REGION 289..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..396
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..459
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 52711 MW; 36CC794FA76D6FF7 CRC64;
MPNFLEKLSE SLREKVLHIV SKEPDSISIF QEVYNCGKDS QDEDIDNKKR KLTTTDTLSV
NDENVVFELQ DVSVLSPLRK KLTVLIAVDE RDQSPMISFN KNNNVEYVIN NIKQSVKFST
FLPFPEKKNL VYLYMNYERD GSNADPVLIT LNKEQILKQF KERNLLKAED SDFQLCVDYM
RRQAILTGFR ISDPFSKSVM DSHHSFFVDC HRGSKEGTLF FLPEHIIFGF KKPILLFESK
QIDAITYSSI TRLTFNVTLI TKDGERFEFS MIDQNKFSEI DEYVKKKQVE DKSMSDELKA
KTPKSGQTSD QSALKEALEE SGTLDTMNGE SDDEDDQNFE EESDLSDGSG SGDDDEDDDD
DDDDEDDDSI EKGDDGEEEE DDNEEEEQEE EEKEEQEQEQ NRQILNRASP NAAPSNHFSM
EIDEIPDLLD ENGLIQDIPI TMDDDNDEEE EEGSGVEYD