MOS_MSVMH
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 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 HT-1) (MoMSV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
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: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 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
