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Database: UniProt
Entry: C6HRD6_AJECH
LinkDB: C6HRD6_AJECH
Original site: C6HRD6_AJECH 
ID   C6HRD6_AJECH            Unreviewed;      1203 AA.
AC   C6HRD6;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Bromodomain-containing protein {ECO:0000313|EMBL:EER37070.1};
GN   ORFNames=HCDG_08521 {ECO:0000313|EMBL:EER37070.1};
OS   Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544712 {ECO:0000313|EMBL:EER37070.1, ECO:0000313|Proteomes:UP000002624};
RN   [1] {ECO:0000313|Proteomes:UP000002624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA   Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA   Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain H143.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG692436; EER37070.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HRD6; -.
DR   STRING; 544712.C6HRD6; -.
DR   VEuPathDB; FungiDB:HCDG_08521; -.
DR   eggNOG; KOG1472; Eukaryota.
DR   HOGENOM; CLU_006198_0_0_1; -.
DR   OMA; YRRSEAK; -.
DR   Proteomes; UP000002624; 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:UP000002624}.
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          91..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1019..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        248..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1083..1119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1129..1144
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1151..1175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1203 AA;  131346 MW;  406A3BB83BFBE606 CRC64;
     MSIGQHHNWL LPGHLRPPDD HHDPHPSING LSKVPSRPRT PQLRFRGIAD GSQSGNMISD
     ADTIPEEDPR IASFRDCYQK GEAKISALFN FGKASDPGNN EPGAIQGAEE TGIAADGQVQ
     SSAPARKAAR KLDEDDYDDY DDDDESESAP PAPSPLIISK PAPARSEPNT LPSPPQKPSI
     ALKTSETQKD PKKHSLEDIR KKLEEDKKAT EEAARRNFHT VFYTLENDRD AMLDQQMLEE
     SERQVEAEMS GQGANSANSA NATTSGHGTL SSANLGASSL TLKNLIARID MKRSEVQASD
     AELRSLMSEV RKNRSKWASE EKVGQEELYE AAEKVLSELK AMTEHSSAFL TRVNKREAPD
     YYNIIKRPMD LGTMTKKLKA VQYKSKQEFV EDLNLIWTNC LKYNANPEHF LRKHALYMRK
     ETEKLVPLIP DIVIRDRAEV EAEERRLQLA ELDGAEESDD EPIMSSRGRK APGMKSKKGI
     GTGRTAPGSR PEATPGAENK TQGGTAVGAE SDTALEGSQN GFSTPPPGTL TPLGSNGLGP
     GAAGSQGDAM DIDAFGVPVN SSALSRPMIE FEDPEYKIWK QVTKKDRALL AAERHRLFKG
     DKLNADEPAL LRSKAGMRRW LRNQRPATEE ADRLDIAGPQ SKEVETTGET LAEGIEVEED
     KMLPDYYDTM SGIPDLPEQL RWIEDSEGNV VDHSEEFLRI LPKGYFTSPK SKFSKKMDAN
     MRQMQETRKV CSKIGIVKQM QLQSQMYQNQ FQKYNPEPFV EQDVPTHVMN DDGPVISPWV
     CRAALQRSVG KIFYNAGFEE YQPSALDAVT DVAADFFYKI GSTLKTYMES PKIPRTEQST
     VSSEWKSPYM AEEMILHTLQ SVGTDVESLE SYVKEDVDRL GQKLSIIHER MKSHLTELLR
     PAFSDTTGDG SSAFNDGSEQ FVGGDFAEDI DEDFFGFKEL GLDKEFGLAS LSVPLHLLQN
     RMYSAHQAQN TSSSQASAAL FPPPPPYPRI SLQTLPSQIG LVQNFFLAKL HANNDEPLVE
     DLELPPKQRP TAARPRVPAS GKIPHAPLGT GLNSSPQKRP APPAGTGGSK PGAPEPSKKK
     SKKNNGTAGP SNAELGNDES SNQTKSSTSA KTLGKQKVSS TVADDKAAVI SPKKSRHESS
     ADGVVAESDS EIILSANNGN NDIKMNGSTS ATVNGADPPD LAVGGSSAIS GGGILSPESM
     STR
//
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