ID   MYC_AVIMD               Reviewed;         416 AA.
AC   P06295;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   23-FEB-2022, entry version 121.
DE   RecName: Full=Viral myc transforming protein;
DE            Short=v-Myc;
GN   Name=MYC;
OS   Avian myelocytomatosis virus HBI.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae.
OX   NCBI_TaxID=11915;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2999450; DOI=10.1128/jvi.56.3.969-977.1985;
RA   Smith D.R., Vennstrom B., Hayman M.J., Enrietto P.J.;
RT   "Nucleotide sequence of HBI, a novel recombinant MC29 derivative with
RT   altered pathogenic properties.";
RL   J. Virol. 56:969-977(1985).
CC   -!- FUNCTION: Transforms avian and murine macrophages and fibroblasts as
CC       well as murine B-lymphoid cells.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}.
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-vMyc chimeric
CC       protein. The sequence shown here corresponds to the Myc homolog
CC       fragment of the chimera.
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DR   EMBL; M11784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P06295; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR003327; Myc-LZ.
DR   InterPro; IPR002418; Tscrpt_reg_Myc.
DR   InterPro; IPR012682; Tscrpt_reg_Myc_N.
DR   Pfam; PF00010; HLH; 1.
DR   Pfam; PF02344; Myc-LZ; 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; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Host nucleus; Oncogene.
FT   CHAIN           1..416
FT                   /note="Viral myc transforming protein"
FT                   /id="PRO_0000127309"
FT   DOMAIN          331..383
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          144..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..411
FT                   /note="Leucine-zipper"
FT   COMPBIAS        153..171
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..244
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..336
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  46072 MW;  4D4D960E6FBEA7E2 CRC64;
     MPLSASLPSK NYDYDYDSVQ PYFYFEEEEE NFYLAAQQRG SELQPPAPSE DIWKKFELLP
     MPPLSPSRRS SLAAASCFPS TADQLEMVTE LLGGDMVNQS FICDPDDESF VKSIIIQDCM
     WSGFSAAAKL EKVVSEKLAT YQASRREGGP AAASRPGPPP SGPPPPPAGP AASAGLYLHD
     LGAAAADCID PSVVFPYPLS ERAPRAAPPG ANPAALLGVD TPPTTSSDSE EEQEEDEEID
     VVTLAEANES ESSTESSTEA SEEHCKPHHS PLVLKRCQVN IHQHNYAAPP STKVEYPAAK
     RLKLDSGRVL KQISNNRKCS SPRTLDSEEN DKRRTHNVLE RQRRNELKLR FFALRDQIPE
     VANNEKAPKV GILKKATEYV LSIQSDEHRL IAEKEQLRRR REQLKHNLEQ LKNSRA