ID A0A072Q4N3_9EURO Unreviewed; 979 AA.
AC A0A072Q4N3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Chromatin structure-remodeling complex subunit RSC1/2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O9_00833 {ECO:0000313|EMBL:KEF62860.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF62860.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF62860.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF62860.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:KEF62860.1}.
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DR EMBL; AMGV01000001; KEF62860.1; -; Genomic_DNA.
DR RefSeq; XP_013265450.1; XM_013409996.1.
DR AlphaFoldDB; A0A072Q4N3; -.
DR STRING; 1182545.A0A072Q4N3; -.
DR GeneID; 25275784; -.
DR VEuPathDB; FungiDB:A1O9_00833; -.
DR HOGENOM; CLU_007728_0_0_1; -.
DR OrthoDB; 1334586at2759; -.
DR Proteomes; UP000027920; 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; 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 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:UP000027920}.
FT DOMAIN 81..151
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 302..364
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 407..526
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..225
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..617
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 111324 MW; 9B2A4557A17D2ED6 CRC64;
MADPSTTEEP ATAKSPDPVD SIEVVTEVKD EDAVDEKSDN EADAAEDEAG GERPVSNDQY
KALKNITEIL TNHKVKVKGD EDHYPSTLFR RIPNRRNLPD YHEIIKDPVA LSTLKGKIQR
KQYSGIPEFV RDFALIVHNA QVYNRPNSAP VRDVLELQGL FKAELQRLVE DGFLKAEEID
FPDLGEIPYA TPEPDPVSEE DDENEDDQDQ DQDEDDDDDD GDGDDSDDDR RKRKGRRGRP
SISGRKGRDD DDDDNKLNDA DIRKRRGRPP KVDTPMEARI KAILKGIRKP KDKAGNLRVR
HFERLPDKAE YPAYFIEIKE PIALDTIKKK AKRKKYQSLE HFMKDIDLLF NNAKDFNEDS
SEIYQDAIEL SAEALRLLDI EKAKPDEEYL MEDGRRPLPS GILHNNELWK VGDWVHIKNS
NDVTKPIVAQ IYRTWEDTDG QKWINACWYY RPEQTVHQYE KHFFPNEVVK TGQYRDHQIE
EVIDRCFVMF FTRFSRGRPR SLEPSKEVYV CEARYNEEKH RFNKIKTWAS CLPDEVRDKD
YEMDLFDTPR RIKKVPSPLK HLLKSDAKAT DVIPAPQWGH PNAPPLVGGI HKQPRDENQS
PPPEPTPPPP PTPPAQVVRQ PSTNSMSHQQ ARPSLDGRSS TGPGILPQLP RPSPSMAPQM
SPYQAQSLSP APQYIRQSSL SQTPAATHRT AAPQTPTQPL PLAYAANQQL HPTPALTAAH
PTSYAPAIPT VQPYARPSVP PTQSYNPYGA AMVAPTREQQ VFVLPDIANE SIPKSIRDQF
PQDSEGRVLF FSKPPVVADE AIYDMHASTK PKLLAHSEKY LAAKAERDKL ITARKRTIEE
QNVRDDHKRV KNDLVNGGEP NGTHSSRATA SHMQGSNGSQ GAQPKESGTD PITTGLTDTM
QNWIKNMSAQ TEIDYKTRYG DKWKEYFEED QLRRQERAKK EAEKQKAREE MFAKCHNPPT
YDTSFSRDIW SGGFKGERY
//
