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Database: UniProt
Entry: H6BU47_EXODN
LinkDB: H6BU47_EXODN
Original site: H6BU47_EXODN 
ID   H6BU47_EXODN            Unreviewed;       579 AA.
AC   H6BU47;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Histone chaperone RTT106/FACT complex subunit SPT16-like middle domain-containing protein {ECO:0000259|SMART:SM01287};
GN   ORFNames=HMPREF1120_03754 {ECO:0000313|EMBL:EHY55624.1};
OS   Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS   yeast) (Wangiella dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY55624.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|EMBL:EHY55624.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY55624.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00037550}.
CC   -!- SUBUNIT: Interacts with histones H3 and H4.
CC       {ECO:0000256|ARBA:ARBA00038654}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC   -!- SIMILARITY: Belongs to the RTT106 family.
CC       {ECO:0000256|ARBA:ARBA00006159}.
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DR   EMBL; JH226132; EHY55624.1; -; Genomic_DNA.
DR   RefSeq; XP_009156085.1; XM_009157837.1.
DR   AlphaFoldDB; H6BU47; -.
DR   STRING; 858893.H6BU47; -.
DR   GeneID; 20308393; -.
DR   VEuPathDB; FungiDB:HMPREF1120_03754; -.
DR   eggNOG; ENOG502R9PE; Eukaryota.
DR   HOGENOM; CLU_033828_0_0_1; -.
DR   InParanoid; H6BU47; -.
DR   OMA; AMPEAHR; -.
DR   OrthoDB; 1359279at2759; -.
DR   Proteomes; UP000007304; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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   Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT   DOMAIN          280..385
FT                   /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT                   like middle"
FT                   /evidence="ECO:0000259|SMART:SM01287"
FT   REGION          46..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..457
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..555
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..573
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   579 AA;  62977 MW;  A1ED9A8B1C2D71CD CRC64;
     MSDSSVIDRA FAQDKQLRKR VFDAIQTSPQ HAPLFEDIAR YHLTHTSNGT GDATDNDSEP
     ASKKRKLVNG SSVSTSQPPS TTLSKQNRQV LLEARDVSFS IPQRKKLHLG IAQYTGGGED
     KNKSATGNTT PSTHTLFARN PATSSIEFEV DLNQFAYALR LPVPEKATKQ YNFCLLPRST
     STSTSNSTST NSTYTNSGST STVEPIIWTV NHGPLKSLQI SDPKLTKIIS DSDSEPDQTF
     SIALNHILQT ATRGNVSLTY PTETEFASAK PESHRKSDKA YHVKAFRGSK DGFLFFLENG
     IFFGFKKPLA FFAFDDIVSI SYTSVLQRTF NLNVAYRPSS SGDAATTIPN GDEDVQEIEF
     SMLDQADFPG IDAYVKRHGL QDASLAESRR AAAAAAKKAG GGGGVAGSTG GGVNTATSGV
     DDGGEEEEDT RTELEKAQQQ LEDEEDELEE DYDPGSEGES DGSGGSSESD ADDDNDDGHD
     QRASGRKKKA NNHSGQNRDL VAEELGSEAE DVSITEDEVE EQEGHEDNEA DPDGGEQHAA
     EEEEYDEDED EVEDEHYDDH KNTWAHEAGM PDPDDEDQL
//
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