ID A0A238FFF2_9BASI Unreviewed; 546 AA.
AC A0A238FFF2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=BQ2448_3495 protein {ECO:0000313|EMBL:SCV70733.1};
GN ORFNames=BQ2448_3495 {ECO:0000313|EMBL:SCV70733.1};
OS Microbotryum intermedium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV70733.1, ECO:0000313|Proteomes:UP000198372};
RN [1] {ECO:0000313|Proteomes:UP000198372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; FMSP01000006; SCV70733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238FFF2; -.
DR STRING; 269621.A0A238FFF2; -.
DR OrthoDB; 1425644at2759; -.
DR Proteomes; UP000198372; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR15741; BASIC HELIX-LOOP-HELIX ZIP TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR15741:SF37; LD38259P; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000198372};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 427..520
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 89..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..262
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..413
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 56909 MW; 4F169558C5ECF9DA CRC64;
MHTAIGIVPT NFEFSSPFDF GFFPSTSAHP TGLDSLTTLP QEHRYHHHAA AAGGNHAESS
SAASLLGVSG LSSHSNLFNS NPFSPQNLAS PPSHFSSLTS PPSTAAPSTS SNALFATSSS
SSSSSLPPHR PFPSSAPHHP TPSLNAPHPS TSLNPSPLFD DSESALLSSF LTTLDVDPFF
LFNPVLPPGM PSPPPSFPLD EQAQSERDRL GAGLGKIKLE KEGGWGKWAK RVEAAAAEGG
GQDGPDVEEE EQHDELEEDD EDSTPKDRAS SSGVVVGTGG KRASGNLGAG QRGRGGLTKG
KKARRVSMHE SAEDVEMGEV TVASSTMTAP SRGARSARSM KGSAAGTSSG RLSSGTKSKD
TGRSITPLGA PSAGRDERPA TEEATKEGGD EQRPQEAEEA EEDEEEEEDD NDDDSKNNGK
APLTDTQKRS NHIASEQKRR NAIRSGFKDL VDLLAAGETA SGIVVAPPEP EGGNDASGNG
GKKKRASKGT GRGRGRKGEV AAGGSKSVVL EKAAAYILWL ERGNQALAAE VQRMEVNMRQ
IGIGTV
//
