RT106_ASPNC
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 25-MAY-2022, entry version 70.
DE RecName: Full=Histone chaperone rtt106;
GN Name=rtt106; ORFNames=An18g06020;
OS Aspergillus niger (strain 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=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
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 PaxDb; A2RBA1; -.
DR EnsemblFungi; CAK43325; CAK43325; An18g06020.
DR GeneID; 4990168; -.
DR KEGG; ang:ANI_1_806164; -.
DR VEuPathDB; FungiDB:An18g06020; -.
DR HOGENOM; CLU_033828_0_0_1; -.
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; 2.30.29.30; -; 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..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