ID   RT106_AJECN             Reviewed;         483 AA.
AC   A6R7F0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Histone chaperone RTT106;
GN   Name=RTT106; ORFNames=HCAG_05558;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476659; EDN09059.1; -; Genomic_DNA.
DR   RefSeq; XP_001540091.1; XM_001540041.1.
DR   AlphaFoldDB; A6R7F0; -.
DR   SMR; A6R7F0; -.
DR   STRING; 339724.A6R7F0; -.
DR   EnsemblFungi; EDN09059; EDN09059; HCAG_05558.
DR   GeneID; 5446350; -.
DR   KEGG; aje:HCAG_05558; -.
DR   VEuPathDB; FungiDB:HCAG_05558; -.
DR   HOGENOM; CLU_033828_0_0_1; -.
DR   OMA; AMPEAHR; -.
DR   OrthoDB; 1283058at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
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..483
FT                   /note="Histone chaperone RTT106"
FT                   /id="PRO_0000320480"
FT   REGION          382..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..417
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..455
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  52755 MW;  284E93403B22B436 CRC64;
     MSPDTVNNAV IDKAFEDNAP LRKRVYSAIA STPEYTSLFE DIAKYATTLR SGLGRDASSA
     CSQVRVAATG EGPAAKKRKL INGSEGAVAG TGAGSANDAA LLAGLTADAE LQFYVQDLSF
     AIPQRKKLRL ELTRLVSSAA GAREGYLRAR NQASNEVEFG IPMSRIQHIL CLPVPEKTQR
     QFNFCIIPEH GDGISPVPDH QLAFEPIVWT IPDGPPRTAY LGSGTPALES ANLAETYESY
     LKRMLDDNLR HTKVICPSEK EFVSPTPEAH RKGDKAYHVK AFRGSKEGFL FFLSTGIFFG
     FKKPLVFFAL ENIDTISYTS VLQRTFNLNI TARSPAKPDE VQEFELSMID QSNHPGIDAY
     IKKHGLQDAS LAEARRAKRL NINGVKGGDG GTDSAANHAG ESEEEESELV KAQRELEDRE
     DEEEEDYDPG SEGDSDGSGS SSEEEDQDGD GQEDYDGEGK DLVKEELGKM ISPKPQYQQT
     YNG