ID A0A1Y2VEZ3_9PEZI Unreviewed; 1150 AA.
AC A0A1Y2VEZ3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=Bromo domain-containing protein {ECO:0000259|PROSITE:PS50014};
GN ORFNames=M434DRAFT_221134 {ECO:0000313|EMBL:OTA95268.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA95268.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA95268.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA95268.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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DR EMBL; KZ112445; OTA95268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2VEZ3; -.
DR STRING; 1001938.A0A1Y2VEZ3; -.
DR Proteomes; UP000194361; 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:UP000194361}.
FT DOMAIN 350..420
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..140
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1150 AA; 127454 MW; 463B2B2ED72940B5 CRC64;
MSIMNGQNSW PPPQQHHVVG KRPFRNIDDA PGRSTDAMDN SVASVPEASD TDDERMRAHF
AELYRRCEAR IAQMFAPDGS INRDVVESWR RPISPSAAPP PTTDHSAIEE RPVKRVKRVI
DEDDYGDDDD EDEDDEEEIS NNTTTIPPPK SKTASAAAAA SKGLPSPSKS GSSPIASASS
PDKLYDRAKE DASQGSQGSQ AQASNSEDAR KQLEEARKDI EEAAKRSFHT LIYTLENDRA
AMLEQQQLEE SEKQLQAEMD KNTNNNASGG NSGENYGSLS SANLGASSLT LKHLIARIDM
KRDMVRASDA ELRSLMNEVR KNRSKWASED NVNQEELYEA LEKVLTELKA HTEYSTPFLQ
RVNKKDAPDY YNFIKQPMDL GTMTKKLKSL TYKSKADFVT DLNLIWDNCL RYNQDMNHPL
RRMANGMRKE AEKLIPLIPD LVIRPRAEVE AEERRKQNGG EDDGGDDSDD EPIMSSRGRI
AGGAKGTKSR KTHSDHKEGT PGGDQKPTLQ LNGLLAKARE GSELDGSNGF ATPPIGGSLT
PSGVNGHSGM ASNADAMDID GPELNGTALG QALNEAAQQA YEDEEYKIWK QVTKKDRALI
TKARYQLFNN KKLNIDEPAL LRSRAGMRRF MRGRKQAEAL GLLGHTQDSS SPSNKEAKAT
ETLAEGMEED EEKVIPDYYE PQTIIPDIPS KFQWIEDSDG QVINQHEEFL HTLPPGYFTA
PKSSLTQKFD ANLRQMQETR KICSKIGVIK QMQLQTQVYA NQFPKYNPEP FHELDVEPHV
VCGDDIVMAP EVCRAGLQRS VAKIFYHAGF EELQPSAMDT ITDIAADYFG KFIQTFKNYT
EIEMKDPSPE MFQRGYTAQP RYNAEEAILH TLSEGGYTVE ALESYAKDEV ERLGHKLTGI
HERMKSHLSD LLRPAVTEST QDGAAAFDDG SEQFIGGDFA EELGEDFFGF KELGLAGEMG
GMLSVPLHLL QSRVRNQYQV QNPTQGPTDA VLFEDLPPPE PVTKENIQEQ IGLVKNFFLA
KLHANGDSPL VEDEDLPVKQ RRPRPRLGAT GKIVSPQKRP PKEQNAINKK KKKMEAQAAE
ASKAANQSPE KGGAKKGKSI PIPNGTSQTN GVSLPVAPPM ERVESTQSQG NNSQTDKDDT
GMMSPESMER
//
