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Database: UniProt
Entry: R7TAA2_CAPTE
LinkDB: R7TAA2_CAPTE
Original site: R7TAA2_CAPTE 
ID   R7TAA2_CAPTE            Unreviewed;       429 AA.
AC   R7TAA2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   13-SEP-2023, entry version 44.
DE   RecName: Full=BHLH domain-containing protein {ECO:0000259|PROSITE:PS50888};
GN   ORFNames=CAPTEDRAFT_166474 {ECO:0000313|EMBL:ELT88315.1};
OS   Capitella teleta (Polychaete worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Scolecida; Capitellidae; Capitella.
OX   NCBI_TaxID=283909 {ECO:0000313|EMBL:ELT88315.1};
RN   [1] {ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ELT88315.1, ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELT88315.1,
RC   ECO:0000313|Proteomes:UP000014760};
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:CapteP166474}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. {ECO:0000256|PIRNR:PIRNR001705}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR001705}.
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DR   EMBL; AMQN01003457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB311873; ELT88315.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7TAA2; -.
DR   STRING; 283909.R7TAA2; -.
DR   EnsemblMetazoa; CapteT166474; CapteP166474; CapteG166474.
DR   HOGENOM; CLU_052560_0_0_1; -.
DR   OMA; CEWTSEL; -.
DR   Proteomes; UP000014760; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd11400; bHLHzip_Myc; 1.
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   InterPro; IPR002418; Tscrpt_reg_Myc.
DR   InterPro; IPR012682; Tscrpt_reg_Myc_N.
DR   PANTHER; PTHR45851:SF3; MYC PROTEIN; 1.
DR   PANTHER; PTHR45851; MYC PROTO-ONCOGENE; 1.
DR   Pfam; PF00010; HLH; 1.
DR   Pfam; PF01056; Myc_N; 1.
DR   PIRSF; PIRSF001705; Myc_protein; 1.
DR   PRINTS; PR00044; LEUZIPPRMYC.
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, ECO:0000256|PIRNR:PIRNR001705};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR001705};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014760}.
FT   DOMAIN          342..394
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          384..425
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        42..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  47078 MW;  B3240A82767E8BF1 CRC64;
     MNRGRNSRAS LASELFDPCP SCVQNRHGHQ SKRHRIKSPS PAPSMTKHSL QSNTPLMEFD
     EVREGASAWS LSEVEFYGDM SSPNMDIWNK FEMGQPTPPA SPERDSSTDG DDFSSQSMWD
     SLLDSQLNFA HLNEPLNTKL IQDCMWSATQ PDPDKPRKPT NSAAASAAVN RSRTVSCSGD
     AANSLDCVDP TSVFPYPISA EAKTCLGSSN ALITAPSTLT ASSSVFDTPS PSESEDDEEI
     DVVTVPTSSI VRKSSRGPSS VARNLESASA QVAAMHNYSN VNHSAHSDHH YSQPYSTQSA
     PQSPQISAAS TGAVSVLKRS RPMSMPSSPQ PFKNSDSEEG EGKRAQHNVL ERKRRNDLKY
     SFCTLRACVP DISSAERTPK VTILKKASEH VISLKRRHNS LEVELARQKH RQEQLRAKLN
     HLKDNDLFL
//
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