ID   YL232_MIMIV             Reviewed;         633 AA.
AC   Q5UQC1;
DT   13-SEP-2005, 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 L232;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=MIMI_L232;
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).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY653733; AAV50505.1; -; Genomic_DNA.
DR   RefSeq; YP_003986728.1; NC_014649.1.
DR   SMR; Q5UQC1; -.
DR   GeneID; 9924839; -.
DR   KEGG; vg:9924839; -.
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; IPR008266; Tyr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..633
FT                   /note="Putative serine/threonine-protein kinase L232"
FT                   /id="PRO_0000086847"
FT   DOMAIN          10..314
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        133
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         16..24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   633 AA;  76003 MW;  548A4B7DAEF58ACD CRC64;
     MSNNIFTNNY TIVDKLSEGT YGIVYKVEHI ESKKNFACKK FVIDNNFTYC NYNELIAHNE
     FNHSNLIEIY DILVDYGHDK CTYYVIMELC DGCLFDILFC DKVFLDESQR LDYLIQIIDG
     LEYMWSKGFV HNDLSLTNIL VKNNKIKIAD FGFMYNRFIK QDIYHRNTIY IQPPELISGH
     PRICDPNKID TWALGQIFYV MCYNSVLYNY SNKTDYYLDI ISKTNTPSLD IIDKLYLSDK
     YKKLYYNIFR KNIKKLTQNA INELVCYNKS TNKFSNDNLR KKTSSNKFIK KHMNWSVRHR
     PDIKQSRKLF YEILANKYPI YNSPIIQSII PSTISFREFS FHKLWSSMNN YDYLFKSNLL
     FGIHFEYKIR LHHRFDYQYN LIVKIMLLMG KIIRSCFSKY NKFKCLNKFI YPNNNYLLSS
     QISRLENSFD RFYSMGKIIY CHYPFFENYI FDYDTIKLSN SLEFQYHFID ILDKEIPCLD
     AYDIFLLSNC NKMYQKYFKY MYYLFVSSPN ATVFDNNIVY QSIMLIIISY KNSLIYKKLI
     NQFLKLNIST KIKYSREINH CFNDDIINVI EIDNDYGINL NYFTVDTIIT AYYIIHICRL
     ITNEKYNLLN INFAIESKFI KYLDKLVSVI DME