RT106_PHANO
ID RT106_PHANO Reviewed; 439 AA.
AC Q0UTL2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Histone chaperone RTT106;
GN Name=RTT106; ORFNames=SNOG_04902;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(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; CH445331; EAT87293.2; -; Genomic_DNA.
DR RefSeq; XP_001795315.1; XM_001795263.1.
DR AlphaFoldDB; Q0UTL2; -.
DR SMR; Q0UTL2; -.
DR STRING; 13684.SNOT_04902; -.
DR EnsemblFungi; SNOT_04902; SNOT_04902; SNOG_04902.
DR GeneID; 5972190; -.
DR KEGG; pno:SNOG_04902; -.
DR eggNOG; ENOG502R9PE; Eukaryota.
DR HOGENOM; CLU_033828_0_0_1; -.
DR InParanoid; Q0UTL2; -.
DR OrthoDB; 1283058at2759; -.
DR Proteomes; UP000001055; 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 GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
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..439
FT /note="Histone chaperone RTT106"
FT /id="PRO_0000320498"
FT REGION 66..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..439
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 439 AA; 47585 MW; C55F759821DA30FC CRC64;
MVFTSMNTQV RVPQPPPVPA AVVNPTVVTP AGPHPEEIDE AFASSHELRK RTSLFRDIST
FILGQASQPS AEPAAKKRKL EEKTTSQSAP AAPGGSLVSS ATKAWRTYPG VSFSIPQRKK
FTLELLDKKD GGIRAIGASG NVEFSIAWKD VDQVFCLPIP EKAKKQHNFV VIPVHGDGIN
PLPEHLQGAA PEPIIWTFEE ATGKNIVEGE DPGPGPMAEA IHHCLIQAGT GKQVIFPDAE
EFASATPESH RKGDKAYHVK AHRGSKEGYL FFTSVGILYG YKKPLAYFDF ASVNSIAYAA
VLRNTFNLVI TTQTQEIEFG MLDQADYAGI NDYVQKHGLQ DASLAAARRA KKLNVNKPKD
KSNGTAPPDA DDAEEEEGEL QKAERELQDQ EDEEEEDYDP GSEGESEGSG SDSEDEDGGG
GYDEGDGDEV EADDDEMEE
