ID A0A194W6V1_9PEZI Unreviewed; 977 AA.
AC A0A194W6V1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Chromatin structure-remodeling complex subunit RSC1 {ECO:0000313|EMBL:KUI72209.1};
GN ORFNames=VM1G_07846 {ECO:0000313|EMBL:KUI72209.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI72209.1};
RN [1] {ECO:0000313|EMBL:KUI72209.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI72209.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; CM003105; KUI72209.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194W6V1; -.
DR OrthoDB; 1334586at2759; -.
DR Proteomes; UP000078559; Chromosome 8.
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; 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; PS50014; BROMODOMAIN_2; 2.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035}.
FT DOMAIN 126..196
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 336..398
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 440..559
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..271
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 977 AA; 111941 MW; EF9CF8A0C16FF374 CRC64;
MAPRARDEIM VHDSIEAKGD EDVDMEDVQV DGNGNNRNDV ADAPTGADTN GEVNVEVEVD
ADGEADTDGA ADAEGQADDG EPADTSTVRR GKGGGRGRWR SVEDPHKELR QLIDDTQKYL
CTYKEDGEQI CDPFQRIPRK NIMPEYHEVI TNPVAFSTVR SKLVRKEYTA FSQFVHDVAQ
IFRNAQVFNR PNSLIFKYSV RLLDVFKDKL QELIEDGSIQ AQDAELPDFG ELPPVEDSPS
PDPEDEEIEE EDEEEEEEEE EEEEDDDDDS DDEGGRRRGR RRGRTFKKDA DDDDDYHKKR
GRPPKVFTPT EARIHAILKG LRKPKNEDGN LRILHFERLP DKQLNKEYYQ TIENPIALDQ
IKRNAKRKKY RNVDELLADI ELMFENAMQY NEEGSDIYDD AVELQKVARQ LVDLEKGKSD
DAFRDEEGKL PLSEVQHNGE TWKVGDWVHI RNMNDLQKPI VAQIYRLWQD EAGKKWINAC
WYYRPEQTVH RVSKRFYKNE VMKTGQYRDH LVEDIVDRCF VMFHTRYHKG RPRGFSPDKE
IYVCEARYNE EKYTFNRIKT WTSCLPDEVR EKDYEMDLFD IPRKIKKEPT PIAHLLAPDA
RETDPLPRPN WGAKDAPPII GGVHIRPRET NDSPSPEPTP EPPAVPPPST TADPIRRQSV
PMPMPMPMAP ASTAFHPGAP GPMQSPSPAH AHHFQQSHFV PPRPIATTPS AISIQPMQQQ
QQQQQQQQLQ HHPVPSPAHV AQSPHFAPQH NQGYGHHPQQ PHFVPSPSPV GHHHHLPNNT
YATQSFTPSA VPVHQQPRMP MAPTASNTAI PHANANANMY NPPRPVEVYH LRDDIDAAIP
AEVREQYQTD DKGHVLFFTA PPLNRPYHGV AEEHATLGHS VRYLSDIAKH RAERERKRKE
RDEALERERA ETAAREKEIR EQQEREMGAV AGQMLGDYFL GLQRGNERMA KELEPVRADK
AAWEAEKKAM RQQQQLQ
//
