ID A0A059J476_TRIIM Unreviewed; 975 AA.
AC A0A059J476;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE RecName: Full=Bromo domain-containing protein {ECO:0000259|PROSITE:PS50014};
GN ORFNames=H109_05469 {ECO:0000313|EMBL:KDB22599.1};
OS Trichophyton interdigitale (strain MR816).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB22599.1, ECO:0000313|Proteomes:UP000024533};
RN [1] {ECO:0000313|EMBL:KDB22599.1, ECO:0000313|Proteomes:UP000024533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR816 {ECO:0000313|EMBL:KDB22599.1,
RC ECO:0000313|Proteomes:UP000024533};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Trichophyton interdigitale MR816.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KDB22599.1}.
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DR EMBL; AOKY01000345; KDB22599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059J476; -.
DR STRING; 1215338.A0A059J476; -.
DR HOGENOM; CLU_006198_0_0_1; -.
DR OMA; CHKISLI; -.
DR Proteomes; UP000024533; 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; 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; PS50014; BROMODOMAIN_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Reference proteome {ECO:0000313|Proteomes:UP000024533}.
FT DOMAIN 342..412
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 975 AA; 108338 MW; B71156357FF4612A CRC64;
MSLNHHHTWL PPGHLRPPDD LFDTHSSING LSRTPSRPRT PQLRSRATLE SMPSGMSISE
IDPAPEEDPR IVAFRNSYQE SEAKINSLFS GKPKIPDSSL PSAESRDTNA AEAGSESAQP
APQIAPRKPA RNLDEDDYDE YDDEGGSDSG GQGPSPPKSK SAPTPPEPKH ATQSPPRLSS
QPGSASENPK DAKKESAEDI RKRLEQDKKA TEEAARQSFH TIFYTLENDR DAMLDQQRLE
ESERQVEAEM SSQNNANNDS TATQGPGHGT LSSANLGASS LTLKNLIARI DMKRHEVQAS
DAELRSLMSE VRKNRSKWAS EEKIGQEELY EALEKVLSEL KAQTEHSSAF LTKVNRRDAP
DYVNIIKRPM DLGTMTKKLK AIQYKSKQEF VDDLNLIWAN CLKYNANPEH FLRKHALYMR
KETEKLVPLI PDIVIRDRAE VEAEERRLQL ADLDGAEESD DEPIMSSRGR KAPGKKSKKG
TSTTRTAPET KSETTSVTDS RPQVQEPPIA RQDSFLEGSQ NDSSTPPPGT LTPLTLNNSG
LPATQGDSMD IDCIGPPPAG QCAALLGLGS EFEDPEFKVW KLVTKKDRAL VAAERHRLFK
GDKINPEEQA LLRTKPGMRR WIRNRRATPG EIDKPEAAPS QEKAGPSGET LAEGIEEEED
KMLPDYYDVM SAIPDLPENL HWTEDAEGNV VEHSEEFLRV LPSGLFTAPV SKFSKKLDAN
VRQMQETRKA CSKISIVKQM QQQSQMYQNQ FQKYQPERLI EQDIAPHVMN GEGPVINPWV
CRAALQRSIG KILYHTGFEE YQPSALDAIT DVASDFFTKI GQTLKSYMEA PKVPASETSS
DQTGTSEWKL PYTSEEMILH TLQAVGTDVD TLETYVKDDI DRHGAKLAVI HERLKSHLTE
LLRPAFADTS GDGSGAFNDG SEQFVGGDFA DDIDEDFFGF KELGLDKEFG LASLSVPLHL
LQNRMFNAHQ AQNAK
//
