ID   RT106_NEUCR             Reviewed;         469 AA.
AC   Q7S4I9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Histone chaperone rtt-106;
GN   Name=rtt-106; ORFNames=NCU08161;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002242; EAA30417.1; -; Genomic_DNA.
DR   RefSeq; XP_959653.1; XM_954560.2.
DR   AlphaFoldDB; Q7S4I9; -.
DR   SMR; Q7S4I9; -.
DR   STRING; 5141.EFNCRP00000008353; -.
DR   EnsemblFungi; EAA30417; EAA30417; NCU08161.
DR   GeneID; 3875809; -.
DR   KEGG; ncr:NCU08161; -.
DR   VEuPathDB; FungiDB:NCU08161; -.
DR   HOGENOM; CLU_033828_0_0_1; -.
DR   InParanoid; Q7S4I9; -.
DR   OMA; AMPEAHR; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR013719; DUF1747.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   Pfam; PF08512; Rtt106; 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..469
FT                   /note="Histone chaperone rtt-106"
FT                   /id="PRO_0000320497"
FT   REGION          54..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..469
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   469 AA;  50909 MW;  517ADC54153EF5EC CRC64;
     MAAKLDSQLL GLVFQSRPDI LKGIQEAADS PARIDLFNNI ASFVYERIAD NTSEEPATKR
     RRVEAQTSGP NGAAHPIAGS QAAVLGADAA AAEPVLLEIK DISVSVPQRK KYDLCFTKNF
     LYARASGSPV PVQGIVYPWK DIEHAFYLPV PDKSQVQHNY VLLPRNSYLP TTKSQQSADQ
     QTQQQTSAPL EPLVFTIPST APKPGTITGP SAAAAAPVSD SYATLFHWAL TTSLHAAGNH
     ACELVSSDPK VFHSVARQAY RPQEKAVHVK AFRGSKDGFL FFLPTGILWG FKKPLLFLPL
     DKIVAISYTS VLQRTFNIVV ELEGGGEGSE EGGQEIEFSM LDQEDYAGID QSYVRRHGLA
     DRSMAEQRKA KKQLAENAKK AAANGEEGEG GEGGEAGDGL TELERAQKEE EQRLQDEEDE
     EEEDYDPGSE GESEGSGSSS EEEEEEEDGE GEGDEDDDED MGEGLEGEE