ID 389L_IIV6 Reviewed; 411 AA. AC Q91FD5; DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 02-SEP-2026, entry version 100. DE RecName: Full=Probable serine/threonine-protein kinase 389L; DE EC=2.7.11.1; GN ORFNames=IIV6-389L; OS Invertebrate iridescent virus 6 (IIV-6) (Chilo iridescent virus). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes; OC Pimascovirales; Pimascovirales incertae sedis; Iridoviridae; OC Betairidovirinae; Iridovirus; Iridovirus chilo1. OX NCBI_TaxID=176652; OH NCBI_TaxID=6997; Acheta domesticus (House cricket). OH NCBI_TaxID=168631; Chilo suppressalis (Asiatic rice borer moth). OH NCBI_TaxID=6999; Gryllus bimaculatus (Two-spotted cricket). OH NCBI_TaxID=58607; Gryllus campestris. OH NCBI_TaxID=7108; Spodoptera frugiperda (Fall armyworm). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11448171; DOI=10.1006/viro.2001.0963; RA Jakob N.J., Mueller K., Bahr U., Darai G.; RT "Analysis of the first complete DNA sequence of an invertebrate iridovirus: RT coding strategy of the genome of Chilo iridescent virus."; RL Virology 286:182-196(2001). RN [2] RP GENOME REANNOTATION. RX PubMed=17239238; DOI=10.1186/1743-422x-4-11; RA Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R.; RT "Comparative genomic analysis of the family Iridoviridae: re-annotating and RT defining the core set of iridovirus genes."; RL Virol. J. 4:11-11(2007). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; 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; AF303741; AAK82249.1; -; Genomic_DNA. DR RefSeq; NP_149852.1; NC_003038.1. DR SMR; Q91FD5; -. DR GeneID; 1733177; -. DR KEGG; vg:1733177; -. DR OrthoDB; 8674at10239; -. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR050235; CK1_Ser-Thr_kinase-like. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR11909; CASEIN KINASE-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. 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 Proteomes; UP000001359; Segment. DR AlphaFoldDB; Q91FD5; -. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..411 FT /note="Probable serine/threonine-protein kinase 389L" FT /id="PRO_0000376913" FT DOMAIN 126..410 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 262 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 132..140 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 162 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 411 AA; 47716 MW; 1C9A58A2542A1198 CRC64; MDLKDEFIQI IKKYSELSLK ESENETKKYI QEVFNVSLSE VFIKEPSKQE TLKQEPTQET NGCIYIFKKG KNIGQKCGSG KSKFCYKHKK NDLNIKVNQE RNIKKPIPKP IPTNKIETGS VINQNWFIGT SIGKGGFGEI YSAAKFNDHG NYKDDDFSFA IKIEPKSNGP LFVEMHFYKR VIVEKEIEKF KLQKNIQYLG LPKYYGSGLY NDYRYIVMEK YDSNIDKLFR NGDLNSSTIL QIGIQILNIV EYIHSKGYIH ADIKGENILL KENDTSHIYL VDFGLCSRYS NIYQPDPKKA HNGTLKYTSR DSHQGVESRR GDLEILGYNM IEWSGGILPW QHLCKKSAGK KILNEVSESK IKYMNDLSLF FNKVQFNDTN LKNKLQTYFE TIIKITFEEL PPYQLLHNIF N //