ID A0A0D7AD45_9AGAR Unreviewed; 502 AA.
AC A0A0D7AD45;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Histone chaperone RTT106/FACT complex subunit SPT16-like middle domain-containing protein {ECO:0000259|SMART:SM01287};
GN ORFNames=FISHEDRAFT_73585 {ECO:0000313|EMBL:KIY48615.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY48615.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY48615.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY48615.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II. {ECO:0000256|ARBA:ARBA00025370}.
CC -!- SIMILARITY: Belongs to the RTT106 family.
CC {ECO:0000256|ARBA:ARBA00006159}.
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DR EMBL; KN881832; KIY48615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7AD45; -.
DR OrthoDB; 1660359at2759; -.
DR Proteomes; UP000054144; Unassembled WGS sequence.
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:UP000054144}.
FT DOMAIN 258..359
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 360..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..435
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 54198 MW; 900845F41960F7BC CRC64;
MSLSTSKTPI INAIAPLLPN EMASGLAELT TNSPQAVFFE TFIRFVTGGD RDASTSISSS
VWTQKQGPVI NTINSLTRPA KRTRENDDEN NEELGTKRAR TAHDVQDDKV LFTLHSISAT
CPIRKKVHIL VCENSVRMIN PSSKAVEAVI SRDSITRSFL LPTRNKTKAH WTVVLLSSDA
GKSAAEQVIF GVDAVAASTT KVTEGGDAEL PISKGQDMHP ILKSFLRHVG APIHQPTSRV
FKSACPTHVG ISADAGGIPG VEAYRAAKAG TLWFMEEGVL WGESKPCEFW SVQDLHSRSD
GVRLISATGR TCTVIFKRHA AVENDEDADA GEETEFSMVD GREQQSINNW VMQYRDSFGG
EKSKGKVGQD RHAARALPSG PITIHQLVAE SDSEDDDFTD SDARSGSVVS SLGGSDSDEE
SGSDGDDGEE SAAETDDEIM AQREDEKLDP RHHPLLREGA MPRMSKGLVE AVVAMVENDF
DGGPASVSEG EDGMEEVDEL DD
//