ID   MOS_MSVMO               Reviewed;         374 AA.
AC   P00538;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 103.
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 (MoMSV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11809;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6173134; DOI=10.1016/0092-8674(81)90364-0;
RA   van Beveren C., van Straaten F., Galleshaw J.A., Verma I.M.;
RT   "Nucleotide sequence of the genome of a murine sarcoma virus.";
RL   Cell 27:97-108(1981).
RN   [2]
RP   SEQUENCE REVISION TO 256.
RA   van Beveren C., van Straaten F., Galleshaw J.A., Verma I.M.;
RL   Submitted (OCT-1982) to the PIR data bank.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7045395; DOI=10.1128/jvi.42.2.538-546.1982;
RA   Donoghue D.J.;
RT   "Demonstration of biological activity and nucleotide sequence of an in
RT   vitro synthesized clone of the Moloney murine sarcoma virus mos gene.";
RL   J. Virol. 42:538-546(1982).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6170110; DOI=10.1126/science.6170110;
RA   Reddy E.P., Smith M.J., Aaronson S.A.;
RT   "Complete nucleotide sequence and organization of the Moloney murine
RT   sarcoma virus genome.";
RL   Science 214:445-450(1981).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=Ref.4; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; V01180; CAA24503.1; -; Genomic_DNA.
DR   PIR; A00647; TVMVM.
DR   SMR; P00538; -.
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..374
FT                   /note="Serine/threonine-protein kinase-transforming protein
FT                   mos"
FT                   /id="PRO_0000086361"
FT   DOMAIN          94..370
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        229
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         100..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   374 AA;  40977 MW;  56702CF0BE08609B CRC64;
     MAHSTPCSQT SLAVPNHFSL VSHVTVPSEG VMPSPLSLCR YLPRELSPSV DSRSCSIPLV
     APRKAGKLFL GTTPPRAPGL PRRLAWFSID WEQVCLMHRL GSGGFGSVYK ATYHGVPVAI
     KQVNKCTEDL RASQRSFWAE LNIAGLRHDN IVRVVAASTR TPEDSNSLGT IIMEFGGNVT
     LHQVIYDATR SPEPLSCRKQ LSLGKCLKYS LDVVNGLLFL HSQSILHLDL KPANILISEQ
     DVCKISDFGC SQKLQDLRGR QASPPHIGGT YTHQAPEILK GEIATPKADI YSFGITLWQM
     TTREVPYSGE PQYVQYAVVA YNLRPSLAGA VFTASLTGKA LQNIIQSCWE ARGLQRPSAE
     LLQRDLKAFR GTLG
//