ID A2QY26_ASPNC Unreviewed; 906 AA.
AC A2QY26;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Contig An11c0400, genomic contig {ECO:0000313|EMBL:CAK40906.1};
GN ORFNames=An11g11080 {ECO:0000313|EMBL:CAK40906.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK40906.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK40906.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AM270257; CAK40906.1; -; Genomic_DNA.
DR RefSeq; XP_001395065.2; XM_001395028.2.
DR AlphaFoldDB; A2QY26; -.
DR EnsemblFungi; CAK40906; CAK40906; An11g11080.
DR GeneID; 4985325; -.
DR VEuPathDB; FungiDB:An11g11080; -.
DR HOGENOM; CLU_007728_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
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:UP000006706}.
FT DOMAIN 74..144
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 279..341
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..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..206
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..654
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 102759 MW; E0B7853CB9601540 CRC64;
MPDRGGGGKG GGAAWNMEPE PSQAQPQPAP EEPVKSIEND GQTDSQAPTD GITDEQWRSM
MNVVLAIYEF REEDGHDPSR LFQRSVNKRN VPDYYDIIKE PMALSILKQK INKREYKSFS
EFVRDCALIP HNAQTYNRPK SQAYEDALVI KDVFIAEFRK LVDQGIITAE EAELPDLGEI
PEADPLPEEE EEEDEDEEDE EDEEDSDDES RRKKKRGPRP GGKRDGGKDD GQKSNDPELR
KKRGRPPRVD TPMEARIKAV LKGIRKLKGP GSQLKVRHFE RLPDKATYPD YYMEIREPIA
IDIIKRKSKR KKYNSVDHFM RDMDLMFNNA KAYNQPESQI YKDAVDLQLE ARKLAEHEKK
KPDSEYLMED GRLPLPDGIL HKSELWKVGD WVHIQNPNDV TKPIVAQIYR TWQDSEGEKW
INACWYYRPE QTVHHFEKHF YPNEVVKTGQ YRDHRVEEIV DRCFVMFFTR YNRGRPRGLP
PDKDVYVCEA RYNEEKHKLN KIKTWASCLP DEVREKDYEM DLFDAPRRIK KIPSPIKHLL
KSDAKETDDL PKPTWGADNA PPVVGAVHRR PRDENESPPP EPTPSPPPSL PPPTLPPAPP
RQPSIPQSSG RPSIDNQSTG ATAGTAAAVR SPAAPIPPAQ SSPAPVPPVN FHQPQIPPTQ
AYQPALQKRA SAFVPQTPHP ATYQASALSH PYTAAQQTPY NLYSSGRLPV PPMGMYNPNA
PRPIEVFHLS DSANAAIPAD IREQFHCDDQ GRVLFFSSPP LDIVPSVQQK LGHSLKYLAA
KEERRKLVEA KKRKENDELA EREAGAKRQR ADDETTLAAR VDALTTRAVE NLTSQITQGT
SQLYEILYQD QAGSIRQTDT KAHERRLLAD HMSQQETARI LANSQPPSYI SLRGNAMYLS
DIGPKA
//
