ID   YR517_MIMIV             Reviewed;         450 AA.
AC   Q5UQ78; Q5UQ77;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Putative serine/threonine-protein kinase R517/R518;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=MIMI_R517, MIMI_R518;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
RN   [2]
RP   SEQUENCE REVISION.
RA   Audic S.;
RL   Submitted (SEP-2007) to UniProtKB.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAV50781.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAV50782.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY653733; AAV50781.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY653733; AAV50782.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; YP_003987031.1; NC_014649.1.
DR   SMR; Q5UQ78; -.
DR   PRIDE; Q5UQ78; -.
DR   GeneID; 9925150; -.
DR   KEGG; vg:9925150; -.
DR   Proteomes; UP000001134; Genome.
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; IPR045269; Atg1-like.
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   PANTHER; PTHR24348; PTHR24348; 1.
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; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..450
FT                   /note="Putative serine/threonine-protein kinase R517/R518"
FT                   /id="PRO_0000253439"
FT   DOMAIN          9..290
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         15..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   450 AA;  51879 MW;  1AE60AD2F2144583 CRC64;
     MEIINSRYKM TDTVLGKGGF SEVFLGTDMY TDNKVAIKKI NITGKNSSDI KFLNKLDFEI
     RTMQILNHPN IVAYYDVMKT ENYWYIVMEY CNFGTLNDVI KFNKNKGISS LDLEKNTHYY
     LNQLRDALNY IINMGYIHRD IKPMNILLTK SISENNENNE NTNYDRSNSL ILKLADFGLT
     KKCSENEEDI MNTICGSPLY MAPELFFNQH YNSQSDIWSF GIIMYQLLFH DHPINATNYS
     QLKNGLKNQK INFPKNNMFS NYCFDLLSKT LAKDPKNRLN WSELFHHYWF IHWSEQHCPK
     NKSDDSNNKK IPDKSQFNEI LSSTKSPLIS LRQFGQLGQS NLSKFKNNGA INCSIDFPKY
     TNNFPSAVNQ SIKIGLSGSS SPINIPVRNN SSKKINYDDI ELISNGNIFP ETLYGSISPV
     DSIINKETRN KTNNPSSLNL SEFVLSDYEI