MOS_MSVMT
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 03-AUG-2022, entry version 85.
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.
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}.
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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: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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 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..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