ID W7I0H0_9PEZI Unreviewed; 414 AA.
AC W7I0H0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Histone chaperone RTT106/FACT complex subunit SPT16-like middle domain-containing protein {ECO:0000259|SMART:SM01287};
GN ORFNames=DRE_05055 {ECO:0000313|EMBL:EWC45718.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC45718.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC45718.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC45718.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) 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; KI966424; EWC45718.1; -; Genomic_DNA.
DR AlphaFoldDB; W7I0H0; -.
DR HOGENOM; CLU_033828_0_0_1; -.
DR Proteomes; UP000024837; 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:UP000024837}.
FT DOMAIN 216..308
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 50..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..364
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 414 AA; 45889 MW; 2FD6A11CC409EFCE CRC64;
MALPIDAAFP DAPLLQKDIL DHVATYPPSL DLLRRISHYV LELRSQLPDL DNGPSSKRRK
LDPPSDPSDL ASEMSSDPSL LRLPDISFSI PQRKKFTLLL TASALAALGP TGSVEFGFFF
KDIDYVACLP VPEKAARQSN FCIFVKNSHG VSQSESDPLL FTVPDGPQKA NPSAYPDLKQ
TVVQTLNRLL PIAVVEPDPE TFKSLSTNAY RKTDASYHTK AHLGTKEGFL FFLKDAIIWG
FKKPMYCFLF ESVESSSYSN ITQRTFSLTI RTLEHYGGKE IEFSMIDQAE HPAIDDYLRR
NQLKDASLTE ARRARLPPSL VKENAGKKSE LRAAQDEIAG IDPEHDAANY DDDDDDDDDD
YKADSDSDSN SVSSSSSEGS KPDSTTHRKS ASKNLAEDEL GSELEDVELT DDEE
//
