ID   MOS_MSVMH               Reviewed;         374 AA.
AC   P07331;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, 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   Moloney murine sarcoma virus (strain HT-1) (MoMSV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Moloney murine sarcoma virus.
OX   NCBI_TaxID=11810;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2993645; DOI=10.1128/jvi.56.1.144-152.1985;
RA   Seth A., Vande Woude G.F.;
RT   "Nucleotide sequence and biochemical activities of the Moloney murine
RT   sarcoma virus strain HT-1 mos gene.";
RL   J. Virol. 56:144-152(1985).
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; M11909; AAA46496.1; -; mRNA.
DR   PIR; A25318; TVMVHT.
DR   SMR; P07331; -.
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   2: Evidence at transcript level;
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_0000086359"
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;  41094 MW;  B124C62202DCBB0C CRC64;
     MARSTPCSQT SLAVPTHFSL VSHVTVPSEG VMPSPLSLCR YLPRELSPSV DSRSCSIPLV
     APRKAGKLFL GTTPPRAPGL PRRLAWFSID WEQVCLMHRL GSGGFGSVYK ATYHGVPVAI
     KQVNKCTKDL RASQRSFWAE LNIARLRHDN IVRVVAASTR TPEDSNSLGT IIMEFGGNVT
     LHQVIYGATR SPEPLSCREQ LSLGKCLKYS LDVVNGLLFL HSQSILHLDL KPANILISEQ
     DVCKISDFGC SQKLQDLRCR QASPHHIGGT YTHQAPEILK GEIATPKADI YSFGITLWQM
     TTREVPYSGE PQYVQYAVVA YNLRPSLAGA VFTASLTGKT LQNIIQSCWE ARALQRPGAE
     LLQRDLKAFR GALG
//