ID   RMIL_AVEVR              Reviewed;         450 AA.
AC   P27966;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Serine/threonine-protein kinase-transforming protein Rmil;
DE            EC=2.7.11.1;
GN   Name=V-RMIL;
OS   Avian rous-associated virus type 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=11950;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1645786; DOI=10.1128/jvi.65.7.3633-3640.1991;
RA   Felder M.-P., Eychene A., Barnier J.V., Calogeraki I., Calothy G., Marx M.;
RT   "Common mechanism of retrovirus activation and transduction of c-mil and c-
RT   Rmil in chicken neuroretina cells infected with Rous-associated virus type
RT   1.";
RL   J. Virol. 65:3633-3640(1991).
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 Rmil-Env polyprotein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. RAF subfamily. {ECO:0000305}.
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DR   EMBL; M62407; AAA42549.1; -; Genomic_RNA.
DR   PIR; A40341; TVFVMR.
DR   SMR; P27966; -.
DR   BRENDA; 2.7.11.1; 599.
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..450
FT                   /note="Serine/threonine-protein kinase-transforming protein
FT                   Rmil"
FT                   /id="PRO_0000086616"
FT   DOMAIN          83..343
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        202
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         89..97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   450 AA;  50313 MW;  6581AAF2253CB622 CRC64;
     MEAVIKDLIR DQGVRGEGGS TAGLSATPPA SLPGSLTNVK ALQKSPGPQR ERKSSSSSED
     RNRMKTLGRR DSSDDWEIPD GQITVGQRIG SGSFGTVYKG KWHGDVAVKM LNVTAPTPQQ
     LQAFKNEVGV LRKTRHVNIL LFMGYSTKPQ LAIVTQWCEG SSLYHHLHII ETKFEMIKLI
     DIARQTAQGM DYLHAKSIIH RDLKSNNIFL HEDLTVKIGD FGLATVKSRW SGSHQFEQLS
     GSILWMAPEV IRMQDKNPYS FQSDVYAFGI VLYELMTGQL PYSNINNRDQ IIFMVGRGYL
     SPDLSKVRSN CPKAMKRLMA ECLKKKRDER PLFPQILASI ELLARSLPKI HRSASEPSLN
     RAGFQTEDFS LYACASPKTP IQAGGIGEWA VHLLKGLLLG LVVILLLVVC LPCLLQCVSS
     SIRKMIDNSL GYREEYKKLQ EAYKQPERRA