GenomeNet

Database: UniProt
Entry: F0X7S7_GROCL
LinkDB: F0X7S7_GROCL
Original site: F0X7S7_GROCL 
ID   F0X7S7_GROCL            Unreviewed;       485 AA.
AC   F0X7S7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Negative regulator of DNA transposition protein {ECO:0000313|EMBL:EFX06425.1};
GN   ORFNames=CMQ_6746 {ECO:0000313|EMBL:EFX06425.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFX06425.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL629729; EFX06425.1; -; Genomic_DNA.
DR   RefSeq; XP_014175907.1; XM_014320432.1.
DR   AlphaFoldDB; F0X7S7; -.
DR   STRING; 655863.F0X7S7; -.
DR   GeneID; 25980213; -.
DR   eggNOG; ENOG502R9PE; Eukaryota.
DR   HOGENOM; CLU_033828_0_0_1; -.
DR   InParanoid; F0X7S7; -.
DR   OrthoDB; 1359279at2759; -.
DR   Proteomes; UP000007796; 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:UP000007796}.
FT   DOMAIN          267..361
FT                   /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT                   like middle"
FT                   /evidence="ECO:0000259|SMART:SM01287"
FT   REGION          64..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..397
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..435
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..485
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  51904 MW;  934CA19EEEAE7FF3 CRC64;
     MATGLDTERL RLAFETRPDL VTGIQKAADS PARVALFNSI ASFVCDRLQG DDEPAVKRRR
     VQANAAAASN THTNGGLPGR PATGADGGGV SAAGLATAAA AETPILEIKD ISLSMPQRKK
     LDLCFTQHYL YARAAGTTAP VQGIVYAWTD IEHVFCVPVP DKAQVQHSYV LLPRGQALAS
     LSKTTTTPNG TAGLPEPLVF TVPAAAPKPG SVGGTAAGEA ATVADAYNTL LHWALEGRLP
     SSSQIVRTDA KVFHSMARQA YRPSEKAVHV RAFRGSKDGF LFFLPTGILW GFKKPLLFLP
     LDRVEAVSYT NVLQRTFNVV VEVDVGGGRT EEVEFGMLDQ EDYGSIDEAY VRRHGLQDRS
     MAERRKAKRE LAENAKDGDG DGDEGEAEAE DEAEGGGTET TDGVKQEGTA ARPKTEQELQ
     DEEDEMEEDY DPGSDDDSGG SGSSDGSVDE DEDDGDGDEE DEDEDMEDGE EEEEEGFDVV
     GKAEE
//
DBGET integrated database retrieval system