ID K7Z8U6_9VIRU Unreviewed; 563 AA.
AC K7Z8U6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Putative serine/threonine-protein kinase {ECO:0000313|EMBL:AFX92931.1};
GN ORFNames=CE11_00905 {ECO:0000313|EMBL:AFX92931.1};
OS Megavirus courdo11.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Megamimivirinae; Megavirus; Megavirus chilense.
OX NCBI_TaxID=1128140 {ECO:0000313|EMBL:AFX92931.1, ECO:0000313|Proteomes:UP000241137};
RN [1] {ECO:0000313|EMBL:AFX92931.1, ECO:0000313|Proteomes:UP000241137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24293219; DOI=10.1007/s11262-013-1016-x;
RA Yoosuf N., Pagnier I., Fournous G., Robert C., La Scola B., Raoult D.,
RA Colson P.;
RT "Complete genome sequence of Courdo11 virus, a member of the family
RT Mimiviridae.";
RL Virus Genes 48:218-223(2014).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily.
CC {ECO:0000256|ARBA:ARBA00006485}.
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DR EMBL; JX975216; AFX92931.1; -; Genomic_DNA.
DR Proteomes; UP000241137; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
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 PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00292; CYCLINS; 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 {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFX92931.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 280..560
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 563 AA; 66021 MW; 4E004D1A8BC174F4 CRC64;
MSLCCIHQII NTVVNPMSYF SYHPHLTQGL RSSIVDWLVL VSDEVNLKST TFNLGISIMD
RYLAKKSNIS RDKMQAISIC SLNLASKIED FVTIGIENCR HFINYNYDIQ YLIELEYDII
ITLKCDLRIP TIVEHIKEIG FKRGNNITQQ FFAHYLIDIL LVTIDYIYYD PKTLAEAIIN
FSREIKNSMD FSESNFEIFV NGNIIYQYIY CKWFDYNAGK YREINNKYGH KRFYTIAKTI
VPTIICDWKP INFPDCFNSC YQINNNRNYY VYNNYELSIM PKNEILGKGT YGTVVKSTFM
DHDIALKSTI CDEEIETFTL RELCHLVKLK HENIVDIYGF GMNNKTSLFY ISLELGLSSI
FQKIFIKHET INEEDKIKYI IQLLSAIDYM HQNKIMHRDL SVANIIIDKD NNLKVCDLGL
SKFFYNFDFC KYSTGVCTIT SRPIELLLNY EKYNEKIDIW SCACIIGVIL RNSAIFEANT
EQEAINEIYH ILGTPTELQQ SKADYLRESM IDIDPKIRTG FVDLEKKYPE ETQIIYDMLD
YDIKKRLTAS EALDRFQNIY KKK
//
