ID A0A2A4J0W2_HELVI Unreviewed; 676 AA.
AC A0A2A4J0W2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=B5V51_9594 {ECO:0000313|EMBL:PCG65164.1};
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG65164.1, ECO:0000313|Proteomes:UP000218220};
RN [1] {ECO:0000313|EMBL:PCG65164.1, ECO:0000313|Proteomes:UP000218220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HvINT- {ECO:0000313|EMBL:PCG65164.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:PCG65164.1};
RA Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA Gould F.;
RT "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT response to modern agricultural practices.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCG65164.1}.
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DR EMBL; NWSH01004393; PCG65164.1; -; Genomic_DNA.
DR STRING; 7102.A0A2A4J0W2; -.
DR Proteomes; UP000218220; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05146; RIO3_euk; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR PANTHER; PTHR45723:SF1; SERINE_THREONINE-PROTEIN KINASE RIO3; 1.
DR Pfam; PF01163; RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01245; RIO1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 226..470
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
SQ SEQUENCE 676 AA; 78152 MW; DF0A1F89B6D199DF CRC64;
MSNPWKKIAA PAEVQDLSDI MSEELARGLQ VKEEIKFAEQ FSEQLSDQHV STSNDIPPEI
LHEIEASNVK EYCNSDAIIA KVLQCQFDRE YDDELKVVEK KRNGDAKVSV SYDNYFNVPK
HLIYDSESDD EDYEREKKDW DRFETNEKEF ASLPKRGYVM KDGEMVTKHD SVINGRRNAC
RVMAFPPEVC TGDGAGFDMK LSNSVFNHLR EQTRHHQTRK HKMLDRKESH ATAEMGLDEP
TRLILFKLIN NELLEDINGI ISTGKESIVL HANGNTNYPD LTVPKECAIK VFKTTLNEFK
TRDKYIEADY RFKDRFSKQN PRKIVHMWAE KEMHNMLRLK KIGLNCPDMV CLKKHILVMS
FIGKDNKPAP KLRDVILKPE KWQSVYNEVV ESVHKMYNTG HMIHADLSEY NILWWDNKCW
FIDVSQSVQP DHPNGLEFLL RDCRNIANFF EKKGVADMKS GEDLFKSITG FDEIDVNFLE
GVHTTYNSLS SRFEVAPDDN RNVSYPFEYC WQKTSEGKLK SDKSADEEDD DDEEDEFEEM
WSHSLQNKAV VDTAADFGNE VIVQEGSSRD NXHEIWNVSY PFEYCWQKTS EGKLKSDKSA
DEEDDDDEED EFEEMWSHSL QNKAVVDTAA DFGNEVIVKE GSSRDNVVLD REVNFGKELG
VVIPKMDEIS STDKKS
//
