ID C1G1I2_PARBD Unreviewed; 1203 AA.
AC C1G1I2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Bromo domain-containing protein {ECO:0000259|PROSITE:PS50014};
GN ORFNames=PADG_00722 {ECO:0000313|EMBL:EEH44433.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH44433.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH44433.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH44433.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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DR EMBL; KN275957; EEH44433.2; -; Genomic_DNA.
DR RefSeq; XP_010755950.1; XM_010757648.1.
DR AlphaFoldDB; C1G1I2; -.
DR STRING; 502780.C1G1I2; -.
DR GeneID; 22580516; -.
DR KEGG; pbn:PADG_00722; -.
DR VEuPathDB; FungiDB:PADG_00722; -.
DR eggNOG; KOG1472; Eukaryota.
DR HOGENOM; CLU_006198_0_0_1; -.
DR InParanoid; C1G1I2; -.
DR OMA; YRRSEAK; -.
DR OrthoDB; 142354at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0000124; C:SAGA complex; IEA:InterPro.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR CDD; cd05510; Bromo_SPT7_like; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037782; Spt7.
DR PANTHER; PTHR47343; TRANSCRIPTIONAL ACTIVATOR SPT7; 1.
DR PANTHER; PTHR47343:SF1; TRANSCRIPTIONAL ACTIVATOR SPT7; 1.
DR Pfam; PF07524; Bromo_TP; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT DOMAIN 341..411
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1203 AA; 130858 MW; 5A0409052DCFEDBC CRC64;
MSLGQHHTWL PPGHLRPPDD HHDSHPVVNG LSKVPSRPRT PQFRFRASTD GAQPGNMISE
AETTPEDDPR IATFRDCYQK GEAKIGALFT FVKASDTGDN DAEASEGAAV GATAADSQAQ
SSAPPRKAAR KLDDDDYDDY DDEEESDGAP PVSSPLKSKL PAARPDSHSL PFPPQKQAIT
LTSSSDTSKD SKKESLEDIR KKLEDDKKAI EETAKRSFRS LFYTLENDRD AMLDQQRLEE
SERQVEAEMS SQGANNANPA HATTSGHGTL SSANLGASSL TLKNLIARID MKRSEVQASD
AELRSLMSEV RKNRSKWASE EKVGQEELYE AAEKVLSELK AMTEHSSAFL TRVNKREAPD
YYNIIKRPMD LGTMTKKLKA VQYKSKQEFV EDLNLIWSNC LKYNANPEHF LRKHALYMRK
ETEKLVPLIP DIVIRDRAEV EAEERRLQLA ELDGAEESDD EPIMSSRGRK APGMKSKKGT
GTGRVTIGSG TEATPGADTK PQGAATVRAE SDAAVDGSQN GFSTPPPGTL TPLGSNGLGT
GAPGSQGDSM DIDSFGVSVN STTLSRPMIE FEDPEYKIWK QVTKKDRALL AAERHRLFSG
DKLNSDEPAL LRTKAGMRRW LRNQRQATDE VDGLAVAGPQ SREAETTGET LAEGIEEEED
KMLPDYYDTM SGIPDLPEQL HWTEDSEGNV VDPSEEFLRI LPKGYFTAPK SKFTQKMDAN
LRQMQETRKI CSKIGIVKQM QLQSQMYQNQ FQKYNPEPFV ERDVPTHVMN DNGPVISPWV
CRAALQRSVG KIFYSAGFEE YQPSALDAIT DVAADFFYKI GSTLKTYMES PKVPRTEQST
ASSQWKSPYT AEKMILHTLQ SVGTDVESLE SYVKEDVDRL GQKLGVLHER MKSHLTELLR
PAFNDTGGDG SSAFHDGSEQ FVGGDFAEDI DEDFFGFKEL GLDKEFGLAS LSVPLHLLQN
RMYSAHQAQN TNAAQTSAAL FPPPPPYPRI SLQTLSSQIG LVQNFFLAKL HANNDEPLVE
DLELPPKQRP TAARPRVPAS GKIPQALLGA GVSSSPQKRP APPAGPGGSK FGASEPSKKK
SKKNSGTAGP SNAETGNDES ANLAKGSTSA KTLGKQKVGS ISFDEKAATI SSMKGKPEAA
VDGIIAESDS EMPPSASNAN NDIKLNGSSS ALVNGADAPD HAAGGSSTSG GGAMLSPESI
STQ
//
