MOS_MSVMM
ID MOS_MSVMM Reviewed; 376 AA.
AC P00537;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 m1) (MoMSV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11811;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6319757; DOI=10.1128/jvi.49.2.579-582.1984;
RA Brow M.A.D., Sen A., Sutcliffe J.G.;
RT "Nucleotide sequence of the transforming gene of m1 murine sarcoma virus.";
RL J. Virol. 49:579-582(1984).
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; K02728; AAA46497.1; -; Genomic_DNA.
DR PIR; A00646; TVMV1M.
DR SMR; P00537; -.
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..376
FT /note="Serine/threonine-protein kinase-transforming protein
FT mos"
FT /id="PRO_0000086360"
FT DOMAIN 94..376
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 376 AA; 41331 MW; 8A1988EF20003323 CRC64;
MARSTPCSQT SLAVPNHFSL VSHVTVPSEG VMPSPLSLCR CLPRELSPSV DSRSCSIPLV
APRRAGKLFL 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
LLQRDLKALA DSIEPM
