GenomeNet

Database: UniProt
Entry: A0A318ZSW0_9EURO
LinkDB: A0A318ZSW0_9EURO
Original site: A0A318ZSW0_9EURO 
ID   A0A318ZSW0_9EURO        Unreviewed;       314 AA.
AC   A0A318ZSW0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=BHLH domain-containing protein {ECO:0000259|PROSITE:PS50888};
GN   ORFNames=BP01DRAFT_6057 {ECO:0000313|EMBL:PYH49785.1};
OS   Aspergillus saccharolyticus JOP 1030-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH49785.1, ECO:0000313|Proteomes:UP000248349};
RN   [1] {ECO:0000313|EMBL:PYH49785.1, ECO:0000313|Proteomes:UP000248349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH49785.1,
RC   ECO:0000313|Proteomes:UP000248349};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KZ821218; PYH49785.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A318ZSW0; -.
DR   STRING; 1450539.A0A318ZSW0; -.
DR   OrthoDB; 1369766at2759; -.
DR   Proteomes; UP000248349; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; PTHR47336:SF4; BHLH TRANSCRIPTION FACTOR (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR47336; TRANSCRIPTION FACTOR HMS1-RELATED; 1.
DR   Pfam; PF00010; HLH; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248349}.
FT   DOMAIN          221..279
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          269..296
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        161..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   314 AA;  34299 MW;  6C4B03C8141DD3A0 CRC64;
     MAYTRADTFT LPEDERMFLS QPSPLSRPND SFPKGPDPLS ANWNYDSAID LFSLNTMMPE
     TFPLNDMMTL DPKDFPTDFF APPPDISGFT ISNHSGEDAA SCGSLSSDLE SDDQSWSPTC
     RVSALDSMPM ELAKPASRTV KSAGRRKTAT ATRQQKVRDD MVTRWSSSPE ITPQDYPAAS
     VSPLPTPSSP VTTGRKTTRS MSGDSNASAG PTNTATGRNA AKRAAHNIIE KRYRTNMNAK
     FVALEKAMSG GIQKPTKGGS ASLKKSEILT NAIAFMQELQ EENKALQKEL TMMKQNMVPN
     GMWRHSKGTE AFHA
//
DBGET integrated database retrieval system