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Database: UniProt
Entry: M2QEG5_CERS8
LinkDB: M2QEG5_CERS8
Original site: M2QEG5_CERS8 
ID   M2QEG5_CERS8            Unreviewed;       610 AA.
AC   M2QEG5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=BHLH domain-containing protein {ECO:0000259|PROSITE:PS50888};
GN   ORFNames=CERSUDRAFT_96544 {ECO:0000313|EMBL:EMD35428.1};
OS   Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS   subvermispora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Gelatoporiaceae; Gelatoporia.
OX   NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD35428.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD35428.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD35428.1,
RC   ECO:0000313|Proteomes:UP000016930};
RX   PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA   Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA   Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA   Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA   Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA   Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA   Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA   Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA   Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA   Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA   Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA   Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA   Martinez A.T., Vicuna R., Cullen D.;
RT   "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT   chrysosporium provide insight into selective ligninolysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KB445800; EMD35428.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2QEG5; -.
DR   STRING; 914234.M2QEG5; -.
DR   HOGENOM; CLU_020171_0_0_1; -.
DR   OrthoDB; 1334653at2759; -.
DR   Proteomes; UP000016930; 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   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   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          453..534
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   REGION          230..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          531..558
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        328..344
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..509
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   610 AA;  64125 MW;  5557AFED11BC9D4C CRC64;
     MNLDSAQQDS QQKDFLQSFY SQETAREHGD LFHAGPSASQ ASMTFPPSLP SMPVGMDVLE
     SLMAMQNNAG QQQVPMHAQT TPQALIDQQM ARLTQLQQLQ QLQNQIFQQQ MEILSSQGSL
     SSLLPNPMDR SKEQSHYNAP PTPMSSAELR AQQSTDFVSP MILHSNNSSL ASNQQLLQNY
     LPQGMLPSAP HSAPANIVFQ QQSALPLPSP AELDFNDFSP LTSPWLGAYG ASAGTSGRPA
     PPPAKNKRRP VSSSGDESAA AAAPARKRQS PASGSTAKPP PPARRTGARG SRSANSTPLF
     QASARRAEGA GGAGGAGGAG DAPADTPSPI EIPMPPPAHP PPAPQAASVI AVQQPAPPNA
     QQQQGRGPSP IVPVTPASIM KLGRLGAGAA EGAGASGSGA SGRSRAASRG ESSKAKGNLS
     LVSPGLKPIR PAGSTGALSP TSPAAPFAQP LQFRKSSHKA AEQKRRDSLK TSFDDLRVLL
     PPIPLPSEDG FPDEPLLPGQ MPPRGPPKGN ADGPNRGVSK LQLLRCGNEY IKVLKARIDR
     RDEEVEKLRR EVARLRVLVP EEERGEELEM EKDLDACEAA YGGIFARTQA AYASMGIQEG
     DEADEEGGGE
//
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