ID   YR679_MIMIV             Reviewed;         694 AA.
AC   Q5UNT7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Putative serine/threonine-protein kinase R679;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=MIMI_R679;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA   Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H.,
RA   Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT   "Mimivirus giant particles incorporate a large fraction of anonymous and
RT   unique gene products.";
RL   J. Virol. 80:11678-11685(2006).
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   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16971431}.
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; AY653733; AAV50940.1; -; Genomic_DNA.
DR   RefSeq; YP_003987203.1; NC_014649.1.
DR   GeneID; 9925327; -.
DR   KEGG; vg:9925327; -.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   SUPFAM; SSF56112; SSF56112; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Virion.
FT   CHAIN           1..694
FT                   /note="Putative serine/threonine-protein kinase R679"
FT                   /id="PRO_0000247411"
FT   DOMAIN          167..548
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        395
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         173..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   694 AA;  80144 MW;  AD36E1CF25002118 CRC64;
     MSTLIDNHIE HLSKLSDKKI CRILRIKPSK DIDKNDLITK LILDHYYGKP RLGNIIVIKS
     LQNGGVRNWE FNLEEIDSNN RQLDSTIPWN NDYSLREIQN TLNHRYNNIN QDLVDLLSVD
     DMNNSLNTDF LKKFYTYFYI GNYNRDKLCQ TMKTFAKSTK KVTSNGITKN KTVGKGAAGI
     AFLAETNSGS FEFVIKAMNN VKQYRNKSLD IGTILYKSEL PLRSNVKNNH LEYLATDVMR
     TVELRYPGYS GYNAFISNEG LLYLNSANDN FTNQTIMHIV LNRILTQYDN DHFIYQFDAF
     FCENRSGLKR GTSTLTNKIT LGKTNSTNVK QTDGYNIMEF ANAGSLDAIL DDWSKSINID
     SNYETLLFMF NDIFVQILKT LKILQQPKFA FVHGDLKTKN IFVKTDGQIN LPNGQVFPRY
     IYKIADYDKS SITWNGIRFH NSGNLGTNII GKLYDNLNTL DLTSTVDSNY YYLTNICPFI
     ESCTSIINGI ELESIPIRYL PIPFYSSIDV YSFVTSMLCH KIFHNFVDYC LVRSIDNEIT
     NILKHLFTET DLNIVMDHIN NTFNSNKKLD LTKYGKIISI IKNNHIGLRK NINKIYDIYG
     IKLHMKETRT VVPNIILSAD QNICLDKCKL NTCNIIQSTR YNRLSDQCYW KSTNSETQEL
     HISDSDQIDR EIDSDEQKQI IDNLFNDIKQ QSKK