ID   YL670_MIMIV             Reviewed;         539 AA.
AC   Q5UNT4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Putative serine/threonine-protein kinase L670;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=MIMI_L670;
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; AAV50931.1; -; Genomic_DNA.
DR   RefSeq; YP_003987192.1; NC_014649.1.
DR   SMR; Q5UNT4; -.
DR   GeneID; 9925316; -.
DR   KEGG; vg:9925316; -.
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   CDD; cd00043; CYCLIN; 1.
DR   InterPro; IPR013763; Cyclin-like.
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..539
FT                   /note="Putative serine/threonine-protein kinase L670"
FT                   /id="PRO_0000086850"
FT   DOMAIN          1..115
FT                   /note="Cyclin N-terminal"
FT   DOMAIN          258..519
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        375
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         264..272
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         285
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   539 AA;  62673 MW;  AC086BB26ADE7685 CRC64;
     MSLFNNHPEL DFTMREMLID WLINIYFDQN VEISNRSLVS GIMMIDRYIY LEKTSISRKM
     YQGIGVICLN LACKLDDTKI LGLDYCEYIC AGIYTADILS NLEKRILKVF KFGLHFKNIL
     HYIKLISIKE NVDDTVYVFA RLMLITILFK TNYLTIKTKS MAKNLMNFSK WFVNNKNVEI
     KNPIHIYFFT ELRRYITHPH FTSINRLAKE FRIFSLIKSR IPNIIYLEKP NVFSKEIIPI
     ELQNSLTIEY TENQLNNMNV IEKLGIGSFG LVNKVKFDNT EIALKTHHPD DSKEIIVESL
     REINNMIMLD HPNIIKMHGY YYSQGITHIG LELCDMPLYK KLDKGNLSPE LKKSFIIQLL
     CGLKYLHNNN IIHRDLTSSN VLIKGDTLKI CDFGCSRFVY DKKIIGNYSL DVCSVRYRAI
     EILNGILPYN EKIDIWSCAC LIAEILGEKF LFRGRNEIEV LDSINRLLGK TVGSGRVGFS
     MLEKHYPNET QIIYKMLDFD PSNRPNAKLV LKIFSECFVA QSELLVNNQK TTIDKNQIS