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Database: UniProt
Entry: P01104
LinkDB: P01104
Original site: P01104 
ID   MYB_AVIMB               Reviewed;         382 AA.
AC   P01104; Q83871; Q90954;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   29-SEP-2021, entry version 119.
DE   RecName: Full=Transforming protein Myb;
GN   Name=V-MYB;
OS   Avian myeloblastosis virus.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=11866;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=6297766; DOI=10.1016/0092-8674(82)90138-6;
RA   Klempnauer K.-H., Gonda T.J., Bishop J.M.;
RT   "Nucleotide sequence of the retroviral leukemia gene v-myb and its cellular
RT   progenitor c-myb: the architecture of a transduced oncogene.";
RL   Cell 31:453-463(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6283631; DOI=10.1126/science.6283631;
RA   Rushlow K.E., Lautenberger J.A., Papas T.S., Baluda M.A., Perbal B.,
RA   Chirikjian J.G., Reddy E.P.;
RT   "Nucleotide sequence of the transforming gene of avian myeloblastosis
RT   virus.";
RL   Science 216:1421-1423(1982).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8084581;
RA   Baluda M.A., Reddy E.P.;
RT   "Anatomy of an integrated avian myeloblastosis provirus: structure and
RT   function.";
RL   Oncogene 9:2761-2774(1994).
CC   -!- FUNCTION: DNA-binding protein that specifically recognizes the sequence
CC       5'-YAAC[GT]G-3'. The v-Myb oncogene transforms immature myelomonocytic
CC       avian cells in culture and induces myeloblastosis (myeloid leukemia) in
CC       chickens.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}.
CC   -!- DOMAIN: The absence of the N- and/or C-terminal may prevent homodimer
CC       formation, leading to DNA-binding and its increased transactivation
CC       activity.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA42553.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAC15907.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; J02012; AAA42553.1; ALT_INIT; Genomic_RNA.
DR   EMBL; S74099; AAB31930.2; -; Genomic_RNA.
DR   EMBL; J02013; AAC15907.1; ALT_INIT; Genomic_DNA.
DR   PIR; A36314; QOYV.
DR   PDB; 1H8A; X-ray; 2.23 A; C=1-122.
DR   PDBsum; 1H8A; -.
DR   BMRB; P01104; -.
DR   SMR; P01104; -.
DR   IntAct; P01104; 2.
DR   EvolutionaryTrace; P01104; -.
DR   Proteomes; UP000235313; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00167; SANT; 2.
DR   InterPro; IPR015395; C-myb_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR012642; Tscrpt_reg_Wos2-domain.
DR   Pfam; PF09316; Cmyb_C; 1.
DR   Pfam; PF07988; LMSTEN; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 2.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS51294; HTH_MYB; 2.
DR   PROSITE; PS50090; MYB_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Host nucleus; Oncogene; Repeat.
FT   CHAIN           1..382
FT                   /note="Transforming protein Myb"
FT                   /id="PRO_0000197053"
FT   DOMAIN          1..15
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT   DOMAIN          16..71
FT                   /note="HTH myb-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          72..122
FT                   /note="HTH myb-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        44..67
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        95..118
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          119..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..256
FT                   /note="Transcriptional activation domain"
FT                   /evidence="ECO:0000250"
FT   REGION          257..376
FT                   /note="Negative regulatory domain (incomplete)"
FT                   /evidence="ECO:0000250"
FT   REGION          305..326
FT                   /note="Leucine-zipper"
FT   HELIX           26..38
FT                   /evidence="ECO:0007829|PDB:1H8A"
FT   HELIX           44..50
FT                   /evidence="ECO:0007829|PDB:1H8A"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:1H8A"
FT   HELIX           56..65
FT                   /evidence="ECO:0007829|PDB:1H8A"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:1H8A"
FT   HELIX           78..91
FT                   /evidence="ECO:0007829|PDB:1H8A"
FT   HELIX           95..98
FT                   /evidence="ECO:0007829|PDB:1H8A"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:1H8A"
FT   HELIX           107..115
FT                   /evidence="ECO:0007829|PDB:1H8A"
FT   TURN            116..119
FT                   /evidence="ECO:0007829|PDB:1H8A"
SQ   SEQUENCE   382 AA;  43061 MW;  1459BACAD29EC971 CRC64;
     NRTDVQCQHR WQKVLNPELN KGPWTKEEDQ RVIEHVQKYG PKRWSDIAKH LKGRIGKQCR
     ERWHNHLNPE VKKTSWTEEE DRIIYQAHKR LGNRWAEIAK LLPGRTDNAV KNHWNSTMRR
     KVEQEGYPQE SSKAGPPSAT TGFQKSSHLM AFAHNPPAGP LPGAGQAPLG SDYPYYHIAE
     PQNVPGQIPY PVALHINIIN VPQPAAAAIQ RHYTDEDPEK EKRIKELELL LMSTENELKG
     QQALPTQNHT ANYPGWHSTT VADNTRTSGD NAPVSCLGEH HHCTPSPPVD HGCLPEESAS
     PARCMIVHQS NILDNVKNLL EFAETLQLID SFLNTSSNHE NLNLDNPALT STPVCGHKMS
     VTTPFHKDQT FTEYRKMHGG AV
//
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