ID   MOS_MSVTS               Reviewed;         342 AA.
AC   P10421;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Serine/threonine-protein kinase-transforming protein mos;
DE            EC=2.7.11.1;
GN   Name=V-MOS;
OS   Myeloproliferative sarcoma virus (isolate ts159).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Moloney murine sarcoma virus.
OX   NCBI_TaxID=11814;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3027415; DOI=10.1128/jvi.61.3.889-897.1987;
RA   Friel J., Stocking C., Stacey A., Ostertag W.;
RT   "A temperature-sensitive mutant of the myeloproliferative sarcoma virus,
RT   altered by a point mutation in the mos oncogene, has been modified as a
RT   selectable retroviral vector.";
RL   J. Virol. 61:889-897(1987).
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; M15424; AAA46581.1; -; Genomic_DNA.
DR   PIR; A26592; TVMVM9.
DR   SMR; P10421; -.
DR   BRENDA; 2.7.10.2; 3536.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd13979; STKc_Mos; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR23257:SF706; PROTO-ONCOGENE SERINE_THREONINE-PROTEIN KINASE MOS; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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..342
FT                   /note="Serine/threonine-protein kinase-transforming protein
FT                   mos"
FT                   /id="PRO_0000086363"
FT   DOMAIN          63..338
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        198
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         69..77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   342 AA;  37971 MW;  83D16BA59DF8CE76 CRC64;
     MPSPLSLCRY LPRELSPSVD SRSCSIPLVA PRKAGKLFLG TTPPRAPGLP RRLAWFSIDW
     EQVCLMHRLG SGGFGSVYKA TYHGVPVAIK QVNKCTKDLR ASQRSFWAEL NIARLRHDNI
     VRVVAASTRT PEDSNSLGTI IMEFGGNVTL HQVIYGATRS PEPLSCREQL SLGKCLKYSL
     DVVNGLLFLH SQSILHLDLK PANILISEQD VCKISDFGCS QKLQDLRCRQ SPHHIGGTYT
     HQAPEILKGE IATPKADIYS FGITLWQMTT REVPYSGEPQ YVQYAVVAYN LRPSLTGAVF
     TASLTRKTLQ NIIQNCWEAR ALQRPGAELL QRDLKAFRGA LG
//