ID RT106_DEBHA Reviewed; 482 AA.
AC Q6BYP2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=Histone chaperone RTT106;
GN Name=RTT106; OrderedLocusNames=DEHA2A07986g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382133; CAG84633.2; -; Genomic_DNA.
DR RefSeq; XP_456677.2; XM_456677.1.
DR AlphaFoldDB; Q6BYP2; -.
DR SMR; Q6BYP2; -.
DR STRING; 284592.Q6BYP2; -.
DR GeneID; 2899653; -.
DR KEGG; dha:DEHA2A07986g; -.
DR VEuPathDB; FungiDB:DEHA2A07986g; -.
DR eggNOG; ENOG502R9PE; Eukaryota.
DR HOGENOM; CLU_040939_0_0_1; -.
DR InParanoid; Q6BYP2; -.
DR OMA; TRLTFNV; -.
DR OrthoDB; 1359279at2759; -.
DR Proteomes; UP000000599; Chromosome A.
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; cd13304; PH2-like_Rtt106; 1.
DR Gene3D; 2.30.29.120; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR InterPro; IPR040770; Rtt106_PH.
DR PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1.
DR PANTHER; PTHR45849:SF3; HISTONE CHAPERONE RTT106; 1.
DR Pfam; PF18469; PH_18; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
PE 3: Inferred from homology;
KW Chaperone; Chromosome; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..482
FT /note="Histone chaperone RTT106"
FT /id="PRO_0000320491"
FT REGION 47..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..456
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 53386 MW; D5D87974761F4226 CRC64;
MSNDQKWIKS LPSDLQNQVN ALVEAHPPSL TVIHKLCEYF KTNASEHEDK RRKLSSDPEI
KSEGHVPEAL SGPKSEVPGQ IHEQEIIFEL PQISFQSPIR KKLNLIFHLL VEPGQSPKPV
MSLALPTTYV PEISIHNLAS SIRLCVLLPI LGNSTNNTKR NIGLLCFWIH DDAASDPNKN
DPIICQVNFD QVKKQLIKAG KIPAEAETQL KEMNESNQSQ DGIKAINEAI INFLQKQFQL
CGIHMINYLP SSSATKNKLT INTDAGVAVS SNANSVNDLV MVEAYKGARD GAVLMLTANE
YNQPYIIFGF KKPILIFDIS KVQHVSYSNI TRLTYSMIVT VVNEKKDSKV ETLEFGMIDQ
KYFQIMDEFI KSQGINDNSF DEDLREKVTT NANSGEGEQA SEQAAPADSD DEEEDGTFQV
GQEEEGESSV DEEYDSNAGS DGDSDVGEEE DDTNENNEGA NPAASTEADD VVTQSKEEDD
EQ
//
