ID A0A2A4JS23_HELVI Unreviewed; 1007 AA.
AC A0A2A4JS23;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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_13233 {ECO:0000313|EMBL:PCG74488.1};
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:PCG74488.1, ECO:0000313|Proteomes:UP000218220};
RN [1] {ECO:0000313|EMBL:PCG74488.1, ECO:0000313|Proteomes:UP000218220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HvINT- {ECO:0000313|EMBL:PCG74488.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:PCG74488.1};
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. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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:PCG74488.1}.
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DR EMBL; NWSH01000740; PCG74488.1; -; Genomic_DNA.
DR EMBL; NWSH01000740; PCG74489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4JS23; -.
DR Proteomes; UP000218220; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
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; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 28..292
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 691..981
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 313..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1007 AA; 111588 MW; DD990D03391B6317 CRC64;
MAHQLAPSVN CSLDDIDLSA LKDPAGIFEL IEVVGNGTYG QVYKGRHTKT GQLAAIKVMD
VTQDEEEEIK LEINVLKKYS NHRNIATYYG AFIKKSPPGK DDQLWLVMEY CGAGSVTDLV
KSTKGQSLKE EWISYICREI LRGLSYLHSN KVIHRDIKGQ NVLLTDNAEV KLVDFGVSAQ
LDRTIGRRNT FIGTPYWMAP EVIACDENPD ATYDNRSDLW SLGITALEMA ESQPPLCDLH
PMRALFLIPR NPPPRLKSKK WAKKFHSFIE TVLVKDYHQR PYTEQLLKHA FIRDQPTERQ
VRIQLKDHID RCKKRKQDNS VREDYKYSGS EGEEEENAVA GEPSSIVHNA AAHQGGDTLR
RNFQQIQEGP RPTEAPQPQP PPKRNSKREE REEIPEPGPP ARPTIPQRLI VVPDPQAQQP
NRYRPLPPTP KSSGSSNSSG SNNGTPPASG PQPPQRGSHH MFKPMLPPRR PEDLDKLAAQ
LNELGVVSGN EPPNRPPRAP TNGQGPPVER NQPEPAFEDS DSDSDAEESG GRVRNDGTLL
ASDPPKPLPG LSAVSEDGGG GAGGGAPTRP LPPTPDDDDT HADRTLVMKR GRSSGTNEGS
GSRTSSVLPD LLSQAGQPTT PPRHDKSTSE EKQRSFLTFG FGAGSTGSGG TGGSGGNASR
RESHVNVNVT PTGHDLSSDT PEIRKYKKRF NSEILCAALW GVNLLIGTEN GLMLLDRSGQ
GKVYQLISRR RFQQMEVLEG QNILVTVSGK KNRVRVYYLS WLKSKILRTD GLSDQAERRN
GWINVGELQG AVHFRIVKYE RIKFLVIALK DSIEIYAWAP KPYHKFMAFK NFGELQHRPL
LVDLTIEDST RLKVIYGSAD GFHAVDLDTA TVYDIYIPKH TQGAIVPHCI VPLPNSNGVQ
LLLCYDNEGV YVNTYGRVSK NIVLQWGEMP TSVAYIGTGQ IMGWGNKAIE IRSVETGHLD
GVFMHKKAQR LKFLCERNDK VFFSSAKGGS SCQIYFMTLN KPGMANW
//
