ID M1WIB7_CLAP2 Unreviewed; 876 AA.
AC M1WIB7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Related to member of RSC complex {ECO:0000313|EMBL:CCE34199.1};
GN ORFNames=CPUR_08131 {ECO:0000313|EMBL:CCE34199.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE34199.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE34199.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE34199.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCE34199.1}.
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DR EMBL; CAGA01000079; CCE34199.1; -; Genomic_DNA.
DR AlphaFoldDB; M1WIB7; -.
DR STRING; 1111077.M1WIB7; -.
DR VEuPathDB; FungiDB:CPUR_08131; -.
DR eggNOG; KOG1827; Eukaryota.
DR HOGENOM; CLU_007728_0_0_1; -.
DR OrthoDB; 1334586at2759; -.
DR PhylomeDB; M1WIB7; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
DR GO; GO:0016586; C:RSC-type complex; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:UniProt.
DR CDD; cd04717; BAH_polybromo; 1.
DR CDD; cd05522; Bromo_Rsc1_2_II; 1.
DR CDD; cd04369; Bromodomain; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 2.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR037382; Rsc/polybromo.
DR InterPro; IPR048047; RSC1/2_bromodom.
DR PANTHER; PTHR16062:SF19; PROTEIN POLYBROMO-1; 1.
DR PANTHER; PTHR16062; SWI/SNF-RELATED; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; Bromodomain; 2.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Reference proteome {ECO:0000313|Proteomes:UP000016801}.
FT DOMAIN 67..137
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 272..342
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 384..503
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..206
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..591
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 876 AA; 99521 MW; 36D75A644A4FFC27 CRC64;
MSMHDDGSMC DVAGSIKAQD GEPDAAVKDN SPSGHPGSES EAPEGEEHDA LRHIQTLTTY
LSSVQEDGED LAAGFQRIPN RRVLPDYFDV INHPIAFSTI RSKIQKKQYS TFSEFVKDVA
QICHNAQVYN RPSAPIFSAA VRLRDVFGSE LGKLAAKGSI SSDDAKLPHL GDLPPMEEFI
QRSGDDDRGD DDDDEGEGEE EDGGSTDEDD GNRKRRIRRD PRHKGLAVRK EREDDLDDET
YKRRGRPPMV QTPMEARISS ILRGLRRFKD REGNLMVLPF EKLPDKVTMP DYYSIIHKPI
ALDNIKRKAK RKKYCDVDEL QKDLELMFEN ARIYNEDDSA VHEAATELRM QSRILLEQEK
AKPDENFRDE DGKLALSEVQ YDGQTWKVGD WVHIRNANDL AKPIIAQIFR VWQDRAGQQW
LNACWYYRPE QTVHRYEKHF FEHEVVKTGQ YRDHQTSELL DRCFVMFVTR FNKGRPRGLP
SDKSVYICES RYNEEKFRFN KIKTWASCVP DEVRDKDYEM DLFDAPRRVR KVPSPIKHLL
REDAKASDEL PRPIWGSPNA PPIIGAVHRR PPEMNDSPPP ELTPSPDIPS GPVPRHSESS
LTSNMPVDFI AKNHYGGFAG PCFESSPPSL AQHSVAPADR FSSATSGLIG QHVQQTPVPV
PHPPQAISDS QVSLRPIQCQ QQQAGYASKA SMHSQPISSY NHNHSVTNHG AVQYDQQHAH
TRTQMKSNGT SAKNIYNPPR PPEVYTLLES VNDTLYKSIR QTFQQDVAGR VVFFAGPPLD
RPVKRVSPRN LGVEHSVKYL AGRNRWLVDR EKKRRWRHRL QSTSPQLESH DIRSVKTASA
ARATSAIQKW VQAFSDGAVE WRQKAQLDGW MVPASD
//
