ID   MOS_SIBNE               Reviewed;         193 AA.
AC   Q8AX00;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Serine/threonine-protein kinase mos;
DE            EC=2.7.11.1;
DE   AltName: Full=Oocyte maturation factor mos;
DE   Flags: Fragment;
GN   Name=MOS;
OS   Sibon nebulatus (Cloudy snail-eating snake) (Coluber sibon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Dipsadidae; Sibon.
OX   NCBI_TaxID=211651;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12487103; DOI=10.1016/s1631-0691(02)01510-x;
RA   Vidal N., Hedges S.B.;
RT   "Higher-level relationships of snakes inferred from four nuclear and
RT   mitochondrial genes.";
RL   C. R. Biol. 325:977-985(2002).
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; AF544736; AAO13459.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8AX00; -.
DR   SMR; Q8AX00; -.
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   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.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           <1..>193
FT                   /note="Serine/threonine-protein kinase mos"
FT                   /id="PRO_0000086356"
FT   DOMAIN          47..>193
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         53..61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NON_TER         1
FT   NON_TER         193
SQ   SEQUENCE   193 AA;  20915 MW;  DDAFE80F62DEED49 CRC64;
     SSVNARPCSS PLVCPAKGEK FFGVGSASRI RQLPPRLAWC SIDWDQLCLL HLLGSGGFGS
     VYKATYHGAT VAVKQVKKCS KNHLASRQSF WAELNVACLD HNNVVHIVAA STCTPTSQDS
     LGTIIMEYAG NCTLHHVIYG IGYLTGNNDG LKRDHEFLST AQAVVYSCDI VAGLMFLHSQ
     LIVHLDLKPA NIF