ID   YL673_MIMIV             Reviewed;         545 AA.
AC   Q5UNT1;
DT   13-SEP-2005, 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 L673;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=MIMI_L673;
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}.
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DR   EMBL; AY653733; AAV50934.1; -; Genomic_DNA.
DR   RefSeq; YP_003987195.1; NC_014649.1.
DR   SMR; Q5UNT1; -.
DR   GeneID; 9925319; -.
DR   KEGG; vg:9925319; -.
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; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF47954; SSF47954; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 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..545
FT                   /note="Putative serine/threonine-protein kinase L673"
FT                   /id="PRO_0000086851"
FT   DOMAIN          13..125
FT                   /note="Cyclin N-terminal"
FT   DOMAIN          264..543
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        384
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         270..278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         291
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   545 AA;  63468 MW;  AB20207994278F81 CRC64;
     MDQYNKYITT NKRLGLVNWM LNVSRIFKLR SHTFQSAVNI MDSYFLKIDF EPNAEELSQT
     AVLCLKISSM ICEIRPLFMD DVLYLLDIDT DNEFTNNIIS SQLCTVELSI LEKLNYKVYY
     LTIWKYIKQF WAKRNLPEQY YHLAYSLANI LLSTNDYLRF DPKILADKII NICIVLEEDP
     ECYETLIEDE LEYQYIHLIW NRAYHKFKDY FNAVISTTLL SKHQVKVPPI QLSSNIKFPN
     SIFCTKIYPE KEFTMYSKKT VKKIDFQNKL GSGTYGSVYK ITYDDNQIAM KKIRNKSTFV
     IDSNMIREVN NLMILSGHPN IINIEGYYYW DLTSTMYIGL DLMDTSLAIY LTKNNISESL
     KIKYVLQLLE AINYMHSKGI MHRDLSASNI LIKGSTLKIG DFGSARFFSG DTLDTKYTRN
     VCSINYRAME LLMGIFPYNN KIDIWSCGCL ITEILTGKRI FNGLKEAEVI NKIHDILGVP
     DADSMNMSVF LSKSKIPLVT QGTLFTPLNL YPNQFPIIYQ MLDYNPYKRP NAENCLKKIK
     ESFDS