ID E3RQR9_PYRTT Unreviewed; 454 AA.
AC E3RQR9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Histone chaperone RTT106/FACT complex subunit SPT16-like middle domain-containing protein {ECO:0000259|SMART:SM01287};
GN ORFNames=PTT_11078 {ECO:0000313|EMBL:EFQ91929.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ91929.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ91929.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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; GL534525; EFQ91929.1; -; Genomic_DNA.
DR RefSeq; XP_003299966.1; XM_003299918.1.
DR AlphaFoldDB; E3RQR9; -.
DR STRING; 861557.E3RQR9; -.
DR EnsemblFungi; EFQ91929; EFQ91929; PTT_11078.
DR KEGG; pte:PTT_11078; -.
DR eggNOG; ENOG502R9PE; Eukaryota.
DR HOGENOM; CLU_033828_0_0_1; -.
DR OrthoDB; 1359279at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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:UP000001067}.
FT DOMAIN 262..350
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 78..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..454
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 49171 MW; FECF61D90459E37E CRC64;
MAFTALNNKP SAPVVPVQVP APVPVPVPHP QEIDVAFASN HELRKRVHAA IDQNPAQSTL
FRDISTYILN QASQPVAEPA AKKRKLEEDG VPQNKAPATS GSLTGATTKA FKTFPGVSFS
IPQRKKFILE LLDKKDGGIR AIGTNGSVEF AIAWKDVDQV FCLPIPEKAK KQHNFVIIPI
HGDGVAPVPD ELKASPPEPI VWTFEEATGK NIVEGEDPGP GPMAEAIQHC LKHAGTGKQV
IFPDADEFAS AVPESHRKGE KAYHVKAHRG SKEGYLFFTE IGILYGFKKP LAFFDFAAIN
SISYTAVLRN TFNLVITTPT GDIEFGMLDQ ANFAGINDYV QKHGLQDASL ADDRRAKKLN
VNKVGGKKDA ANGTEPEATG EEEESELQKA ERELQDQEDD EEEDDDFDPG SEGESEGSGS
DSEDEEGEGG EGGYEEGDTV EGEYDEADGD EMEQ
//
