ID   RT106_ASPNC             Reviewed;         458 AA.
AC   A2RBA1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Histone chaperone rtt106;
GN   Name=rtt106; ORFNames=An18g06020;
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(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}.
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DR   EMBL; AM270411; CAK43325.1; -; Genomic_DNA.
DR   RefSeq; XP_001399053.1; XM_001399016.1.
DR   AlphaFoldDB; A2RBA1; -.
DR   SMR; A2RBA1; -.
DR   EnsemblFungi; CAK43325; CAK43325; An18g06020.
DR   GeneID; 4990168; -.
DR   KEGG; ang:An18g06020; -.
DR   VEuPathDB; FungiDB:An18g06020; -.
DR   HOGENOM; CLU_033828_0_0_1; -.
DR   OrthoDB; 1359279at2759; -.
DR   Proteomes; UP000006706; Chromosome 8L.
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   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   PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1.
DR   PANTHER; PTHR45849:SF3; HISTONE CHAPERONE RTT106; 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..458
FT                   /note="Histone chaperone rtt106"
FT                   /id="PRO_0000320484"
FT   REGION          71..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..440
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  50310 MW;  053AEFE3FBD85B59 CRC64;
     MAFATINSSV PSSIPAIEDA FAAEPALKKR VYDAIAHTPQ HGLLFEDIAK YTSSLLARTA
     TAPVRPVEVV SDGPAMKKRK LQNGNATSAQ SSGDLKSDTS LQFYMQDVSF AVPQRKKLTL
     EVTAGFLRAR NQTSKEVEFG VPLDNIQHVL CLPVPEKNQR QFNFCIIPQY ADGVNSPPEG
     VAAPDAIVWT VNDGPPKAAF SGNGQQLGTD NEETADKLVQ RILNDSLPRT KVVRPDEREF
     VSAMPEAHRK GEKAFHVKAF RGSKEGYLFL LSTGILFGFK KPLVFFAFEN VDSISYTSVL
     QRTFNLNVVA RPTSSEETQE FEFSMIDQAD FSGIDGYIKK HGLQDASLAE ARRAKRYNVN
     GAKGEDEAAA NEEGAVEEES ELQKAQRELE DQEDEDEEDY DPGSDSDSDG SGSSSEEDDD
     DDEEDDEGDM EEDDEEGDRN LVAEELGSEA EDVPAEEL
//