ID   MOS_MSVMT               Reviewed;         354 AA.
AC   P32593;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Serine/threonine-protein kinase-transforming protein mos;
DE            EC=2.7.11.1;
GN   Name=V-MOS;
OS   Moloney murine sarcoma virus (strain ts110) (MoMSV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Moloney murine sarcoma virus.
OX   NCBI_TaxID=31691;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1501276; DOI=10.1128/jvi.66.9.5329-5337.1992;
RA   Huai L., Chiocca S.M., Gilbreth M.A., Ainsworth J.R., Bishop L.A.,
RA   Murphy E.C. Jr.;
RT   "Moloney murine sarcoma virus MuSVts110 DNA: cloning, nucleotide sequence,
RT   and gene expression.";
RL   J. Virol. 66:5329-5337(1992).
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 probably translated as a Gag-Mos
CC       polyprotein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M96854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; B42745; TVMVMU.
DR   SMR; P32593; -.
DR   BRENDA; 2.7.10.2; 3394.
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..354
FT                   /note="Serine/threonine-protein kinase-transforming protein
FT                   mos"
FT                   /id="PRO_0000086362"
FT   DOMAIN          74..350
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        209
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         80..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   354 AA;  38851 MW;  95F845823B748965 CRC64;
     VSHVTVPSEG VMPSPLSLCR YLPRELSPSV DSRSCSIPLV APRKAGKLFL GTTPPRAPGL
     PRRLAWFSID WEQVCLMHRL GSGGFGSVYK ATYHGVPVAI KQVNKCTEDL RASQRSFWAE
     LNIAGLRHDN IVRVVAASTR TPEDSNSLGT IIMEFGGNVT LHQVIYDATR SPEPLSCRKQ
     LSLGKCLKYS LDVVNGLLFL HSQSILHLDL KPANILISEQ DVCKISDFGC SQKLQVLRGR
     QASPPHIGGT YTHQAPEILK GEIATPKADI YSFGITLWQM TTREVPYSGE PQYVQYAVVA
     YNLRPSLAGA VFTASLTGKA LQNIIQSCWE ARGLQRPSAE LLQRDLKAFR GTLG
//