ID   MIL_AVIMH               Reviewed;         380 AA.
AC   P00531;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Serine/threonine-protein kinase-transforming protein mil;
DE            EC=2.7.11.1;
GN   Name=V-MIL; Synonyms=V-MHT;
OS   Avian retrovirus MH2.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=11870;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6325930; DOI=10.1038/309085a0;
RA   Sutrave P., Bonner T.I., Rapp U.R., Jansen H.W., Patschinsky T., Bister K.;
RT   "Nucleotide sequence of avian retroviral oncogene v-mil: homologue of
RT   murine retroviral oncogene v-raf.";
RL   Nature 309:85-88(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6328485; DOI=10.1073/pnas.81.10.3000;
RA   Kan N.C., Flordellis C.S., Mark G.E., Duesberg P.H., Papas T.S.;
RT   "Nucleotide sequence of avian carcinoma virus MH2: two potential onc genes,
RT   one related to avian virus MC29 and the other related to murine sarcoma
RT   virus 3611.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:3000-3004(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6320371; DOI=10.1126/science.6320371;
RA   Kan N.C., Flordellis C.S., Mark G.E., Duesberg P.H., Papas T.S.;
RT   "A common onc gene sequence transduced by avian carcinoma virus MH2 and by
RT   murine sarcoma virus 3611.";
RL   Science 223:813-816(1984).
CC   -!- FUNCTION: By itself the v-Mil oncogene has only weak transforming
CC       capacity but it abolishes the growth factor requirements of avian
CC       macrophages transformed by other oncogenes.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-Mht or Gag-Mil
CC       polyprotein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. RAF subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA25211.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X00534; CAA25211.1; ALT_INIT; Genomic_RNA.
DR   PIR; A00639; TVFVMM.
DR   SMR; P00531; -.
DR   BRENDA; 2.7.11.1; 597.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Oncogene;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..380
FT                   /note="Serine/threonine-protein kinase-transforming protein
FT                   mil"
FT                   /id="PRO_0000086328"
FT   DOMAIN          82..341
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        201
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         88..96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        211
FT                   /note="G -> E (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   380 AA;  42853 MW;  6498695FB7EBEE5D CRC64;
     PTMPVDSRII EDAIRNHSES ASPSASSGSP NNMSPTGWSQ PKTPVPAQRE RAPGTNTQEK
     NKIRPRGQRD SSYYWEIEAS EVLLSTRIGS GSFGTVYKGK WHGDVAVKIL KVVDPTPEQF
     QAFRNEVAVL RKTRHVNILL FMGYMTKDNL AIVTQWCEGS SLYKHLHVQE TKFQMFQLID
     IARQTAQGMD YLHAKNIIHR DMKSNNIFLH GGLTVKIGDF GLATVKSRWS GSQQVEQPTG
     SILWMAPEVI RMQDSNPFSF QSDVYSYGIV LYELMTGELP YSHINNRDQI IFMVGRGYAS
     PDLSKLYKNC PKAMKRLVAD CLKKVREERP LFPQILSSIA LLQHSLPKIN RSASEPSLHR
     ASHTEDINSC TLTSTRLPVF