ID   YR400_MIMIV             Reviewed;         467 AA.
AC   Q5UQJ6;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Putative serine/threonine-protein kinase R400;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=MIMI_R400;
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; AAV50669.1; -; Genomic_DNA.
DR   RefSeq; YP_003986904.1; NC_014649.1.
DR   PRIDE; Q5UQJ6; -.
DR   GeneID; 9925021; -.
DR   KEGG; vg:9925021; -.
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   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
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..467
FT                   /note="Putative serine/threonine-protein kinase R400"
FT                   /id="PRO_0000247403"
FT   DOMAIN          99..467
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          443..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        272
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         105..113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   467 AA;  54371 MW;  AC64F874E44B951F CRC64;
     MMNKKNNKYK SDSLDSKEDK VDLYQDAMIS NLISVNNKST SDSDAKKPTE NRIELLKNAY
     KGGTLKPMID FDDHNTETFM DKRITKNLLD ARSLFLSMGV KLIYIKSGTT GHTFKAISRS
     NKNVVFAVKV CAYPKDDYGG IKSSSRPENV EIRMLKILSY FVVNRLTPHL VLPIGTFHTD
     IEKFINIPEG VIDLKDEKND MYKKFIERYH DGEFEKFVSV LISEWCNGGD LLDYIRKNYD
     SMTLETWTVV IFQLLFTLAL IHEKFPAFRH NDMKANNILV EKTDNKHEGP DKWYRYSLGS
     HVFIIPGIGI QIKIWDFDFA SIDGIVENKK VNADWTKKIN ISKKKNMYYD MHYFFNTLIS
     KRFFPQFYEG GVPQEIVDFV HRIVPEEFRN GSDNINKKGR ILVDVEYTTP FKVIMTDPLF
     EKYRYNQYYF HPQRNMAPKK SILFQQGNGS KQPVPKKSTG QKPTKKV