MOS_MSVTS
ID MOS_MSVTS Reviewed; 342 AA.
AC P10421;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, 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 Myeloproliferative sarcoma virus (isolate ts159).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11814;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3027415; DOI=10.1128/jvi.61.3.889-897.1987;
RA Friel J., Stocking C., Stacey A., Ostertag W.;
RT "A temperature-sensitive mutant of the myeloproliferative sarcoma virus,
RT altered by a point mutation in the mos oncogene, has been modified as a
RT selectable retroviral vector.";
RL J. Virol. 61:889-897(1987).
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; M15424; AAA46581.1; -; Genomic_DNA.
DR PIR; A26592; TVMVM9.
DR SMR; P10421; -.
DR BRENDA; 2.7.10.2; 3536.
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..342
FT /note="Serine/threonine-protein kinase-transforming protein
FT mos"
FT /id="PRO_0000086363"
FT DOMAIN 63..338
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 69..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 342 AA; 37971 MW; 83D16BA59DF8CE76 CRC64;
MPSPLSLCRY LPRELSPSVD SRSCSIPLVA PRKAGKLFLG TTPPRAPGLP RRLAWFSIDW
EQVCLMHRLG SGGFGSVYKA TYHGVPVAIK QVNKCTKDLR ASQRSFWAEL NIARLRHDNI
VRVVAASTRT PEDSNSLGTI IMEFGGNVTL HQVIYGATRS PEPLSCREQL SLGKCLKYSL
DVVNGLLFLH SQSILHLDLK PANILISEQD VCKISDFGCS QKLQDLRCRQ SPHHIGGTYT
HQAPEILKGE IATPKADIYS FGITLWQMTT REVPYSGEPQ YVQYAVVAYN LRPSLTGAVF
TASLTRKTLQ NIIQNCWEAR ALQRPGAELL QRDLKAFRGA LG
