ID   VF380_IIV6              Reviewed;         528 AA.
AC   Q91FE4;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Probable serine/threonine-protein kinase 380R;
DE            EC=2.7.11.1;
GN   ORFNames=IIV6-380R;
OS   Invertebrate iridescent virus 6 (IIV-6) (Chilo iridescent virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Betairidovirinae; Iridovirus.
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=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; AF303741; AAK82240.1; -; Genomic_DNA.
DR   RefSeq; NP_149843.1; NC_003038.1.
DR   GeneID; 1733084; -.
DR   KEGG; vg:1733084; -.
DR   OrthoDB; 10019at10239; -.
DR   Proteomes; UP000001359; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR014901; 2-cysteine_adaptor.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   Pfam; PF08793; 2C_adapt; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..528
FT                   /note="Probable serine/threonine-protein kinase 380R"
FT                   /id="PRO_0000376912"
FT   DOMAIN          156..507
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          70..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..93
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        302
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         162..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   528 AA;  59952 MW;  C3D7381E12E96BA3 CRC64;
     MNFDKEKCDE WEKIRLNSSP KNPFTKRNVK KDGPTYKKID LICKHNVVGG NVVDLNKLCL
     KWLKDNHPNV KIPKSKSPPK VKSPKRKKSP VRRRVSSPLL TDDEDDVLNL QYDYLLSYRS
     VASEEITNYL RQTINDKTIT AGNACMSNTK TLLKYFTNVK AVGKGSFGTV YIGNINIKNN
     VFSIAIKEGQ ISGLEANRAK KLQFPVEYLF NQMMNNILNN KMCPSFNYTY CIHFCDHCEV
     VSAIFKNPKT KSKITTCSVT MVEKADSDLI GLTSLDAQLS ALFQILAAVH CIHKLYGIQH
     CDIKIENVLK KNIPKQANEY FRYSLDGVNY FVPNTGFVAI LNDFGVSFST SPKISTSYFG
     VRNAKVVFNN NSYKFQSFTT QRYPQENKWG KIETLSPPPR LRGPGGAKLT LNKFMKNFDS
     KPSIFVDLED FQKFPTFGMY QDIQDVVRMF VGGKQTVQPG SHTEMRGLQP QAKKAILPFV
     EKLAPTSIWP EDKVELFLAN VLIHKIFTQF GYTNAPPNAI ILETYKLP
//