ID F0UAE1_AJEC8 Unreviewed; 974 AA.
AC F0UAE1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Bromeodomain-containing protein {ECO:0000313|EMBL:EGC42860.1};
GN ORFNames=HCEG_02075 {ECO:0000313|EMBL:EGC42860.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; DS990637; EGC42860.1; -; Genomic_DNA.
DR AlphaFoldDB; F0UAE1; -.
DR STRING; 544711.F0UAE1; -.
DR VEuPathDB; FungiDB:I7I53_09302; -.
DR HOGENOM; CLU_007728_0_0_1; -.
DR OMA; MRDMDLM; -.
DR Proteomes; UP000008142; 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; IPR037382; Rsc/polybromo.
DR InterPro; IPR048047; RSC1/2_bromodom.
DR PANTHER; PTHR16062:SF21; CHROMATIN STRUCTURE-REMODELING COMPLEX SUBUNIT RSC1-RELATED; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008142}.
FT DOMAIN 111..162
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 296..358
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 381..504
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..222
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..699
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..727
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..776
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 111158 MW; E8077DCBA8C80DCE CRC64;
MAAESAQSEF QRASTSGSAD APAPETETEI QESTDLIQQL SEQAGQLAEQ SDQLSQHSRT
SHPFETPQPQ MTAIADSKEN EDNNPEHQVT DEQWRAMFDV VLAIYDYREP DGYDPSRLFH
RSVNKRNVPD YYDVIKEPMA LSVLKQKIKN KSYCNFAEFI RDCALDVFIS EFRKLVEQGI
ISSETAELPD LGEIPDADPL PVEEDEEEEE EDDEEDDEAE DSDDEVGRRR QKRPNRGSSK
REGAKDDQNK INDPELRKKR GRPPRVDTPM EARIKAVLKG IRKFKDSTGQ LKVRHFERLP
DKAAYPDYFS EVKDPMAIDL IKRKSKRKKY NSVDHFMKDM DLMFNNAKAY NQVDSQIYKD
AAALQTEARK LADQEKKKPD SEYLMEDGRL PLPNGILHEG ELWKVGDWIY RTWQDVEGQK
WVNACWYYRP EQTVHQYEKH FYPNEVVKTG QYRDHRIGEV VDRCFVMFFT RYNRGRPRGL
APDKQVYVCE ARYNEEKHKL NKIKTWASCL PDEVREKDYE MDLFDAPRKI KKIPSPIKHL
LKEDAKETDD VPKPTWGAEN APPIVGAVHR RPREENVIIF YFYLSYQLYE SPPPEPTPSP
PPQLPAPPVV PLAPQRQMSI NRAPTRQSID SQSDYRMSAS PLHSLPARSA GQPTPHAPPA
VAPQQAPIPL TRMQQSFPPL SANPTSATPV YPPGYPNHRP GPQFASQTPQ STPIYQQPPP
PQPYSAPHNF PSYQASRYHP HPPHIPQAHL QQQSQLLPHP QSQPQPVLPP NIYNPNAPRP
VETFILSDNT NAAIPEEIRG QFHCDEKGHV LFFTSPPLDV VQPAEQTGLG HSLRYLAAKE
ERAKIIEKRG IEREQMDKER AMKRLKTTMT TITNTDACSK DNNATLAKTD RNMLCELAVM
AAVAQMKQAD QDWYLMRYGE NNAVKAKEAD RERFMRILGE KEKADAMRES LDVREPVDVV
PVLSLAAGEG GAAV
//