ID   YL268_MIMIV             Reviewed;         546 AA.
AC   Q5UPU3;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Putative serine/threonine-protein kinase L268;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=MIMI_L268;
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; AAV50540.1; -; Genomic_DNA.
DR   RefSeq; YP_003986766.1; NC_014649.1.
DR   SMR; Q5UPU3; -.
DR   GeneID; 9924877; -.
DR   KEGG; vg:9924877; -.
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; IPR008266; Tyr_kinase_AS.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; SSF47954; 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..546
FT                   /note="Putative serine/threonine-protein kinase L268"
FT                   /id="PRO_0000086848"
FT   DOMAIN          1..112
FT                   /note="Cyclin N-terminal"
FT   DOMAIN          260..544
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        389
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         266..274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         287
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   546 AA;  63372 MW;  2CC6B0E3846B58D2 CRC64;
     MVCFSKYSGI TLDMRLILID WLIEVHYEYE CIIDTLCLAI ILVDEFVDRI DKIDRKYFQC
     IGICCMNIAT KILEPEHIGS ENCNFISASQ YTTDVIISYE KNILQTLDFH LVRKTILDSL
     WSKIKDFSRQ KKNMGIFFTI VSMTSDKYKC FPCEKIADGI IKLVDLIDNY PIDSIDYTDE
     INTDTIMRYL WSQLTICTNK KLDGYTDLIK NLEIDFEFMK KLTSDIILKP KIVLFPSKNL
     ELYTPLRHCF QYNTEDISNI TVVKNLGEGT YGTVDLVTLN ASKAAIKTQK ELNEEISPDM
     VNEIVFLRIM DHPNIIKLYG YHLGSQTKLV LEPMESSLRR FIIDDTWNNL NKTLGITNNI
     FSDNQKIFYI KQLLEGLKYL HENRIVHGDL TCSNILISKS KLKICDFGSS KIIHPKNKLN
     YKTSKCSLWY RAIELLLEQN YDEKIDVWSV ACICGFILGD KLFDGDNESE IIENIFSHLG
     TPDPIIFESK TSINIPTKKY KFVGFEKLEE KYPDITSIIY RMLSYDSKMR ISASQTLEEF
     NKFNSD