ID A0A397ISQ1_9GLOM Unreviewed; 779 AA.
AC A0A397ISQ1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=Bromo domain-containing protein {ECO:0000259|PROSITE:PS50014};
GN ORFNames=Glove_203g56 {ECO:0000313|EMBL:RHZ76124.1};
OS Diversispora epigaea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Diversisporaceae; Diversispora.
OX NCBI_TaxID=1348612 {ECO:0000313|EMBL:RHZ76124.1, ECO:0000313|Proteomes:UP000266861};
RN [1] {ECO:0000313|EMBL:RHZ76124.1, ECO:0000313|Proteomes:UP000266861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT104 {ECO:0000313|EMBL:RHZ76124.1,
RC ECO:0000313|Proteomes:UP000266861};
RA Sun X., Fei Z., Harrison M.;
RT "Genome and evolution of the arbuscular mycorrhizal fungus Diversispora
RT epigaea (formerly Glomus versiforme) and its bacterial endosymbionts.";
RL Submitted (AUG-2018) 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:RHZ76124.1}.
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DR EMBL; PQFF01000190; RHZ76124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397ISQ1; -.
DR STRING; 1348612.A0A397ISQ1; -.
DR Proteomes; UP000266861; 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 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 SMART; SM00576; BTP; 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:UP000266861}.
FT DOMAIN 69..139
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 221..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 89667 MW; 8153A229C57636AE CRC64;
MSTKMNNNKI KYLLEALEQK KREILMPKNE LKLLLSDIEA AGSKWKDQDR VGQAQLYEAA
EFVLNNLKGY TPYSEPFQRK VTPKEAPDYH KVIEHPMDLG QIFRKLRQHE YNNKQEFSDD
LYLIYSNCLR YNTNPEHIFR EYARAMKEKT DELLEKVPDI TIQSREEFLA SVDQEQEDEQ
KINQPITESQ PVTENQQVAD SLVLIDEAQE ENSQDLHDIN VPVPDEEQVG NDSIISSESD
NDEEAEIERE LQEILSNFDM PKFPDLWDPE IDNPDRDKFF EPGYDPSANN PTLDQYPQLQ
FPKRGTALMI ENNIQTLKRS RILHSKLMAA RQNIPLSHLG ITETAPEEQI TQIKPNIDPR
NLPPLMLNSE GAFESTKRVV AKLCQHAGFE ATSHTALTIL TEVAQDYFLN LGKTLRTYID
DYGKKMTPEE IVTHTLYENG VTSINKLESY VKNDIIRYGS KLRDIHNRLE TTYKEALASP
ENHETEEESF PDSEDAFMMG NFGEDLGDDF FGFRELGLGS LVIPQRLFLG TNKPKPQIKK
TNEETRKKSR YEPPPPWEPI NDPDSQIGLL REFFRNNMEE SGGKLIEDEF LPVKQRNQRP
KVPPTGKIPP QSKRLLKPQL TAAALLEKKR KRERDAQIAE EKERAKRIKA EERAKKQAEK
EEAKRLKQLE REAAKKAEME AKEQRKAEQE HQKRLAQEAK EARKAEAEAA KKAAMENKKR
KTSTKTGKSK TPQSEVSSTP VSRKLEPDDG SDSEMVPLAQ RKKRRAESSG RTGNKRPTN
//
