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Database: UniProt
Entry: A0A2A4JT22_HELVI
LinkDB: A0A2A4JT22_HELVI
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ID   A0A2A4JT22_HELVI        Unreviewed;       528 AA.
AC   A0A2A4JT22;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-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_12135 {ECO:0000313|EMBL:PCG75161.1};
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:PCG75161.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG75161.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG75161.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG75161.1};
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:PCG75161.1}.
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DR   EMBL; NWSH01000630; PCG75161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4JT22; -.
DR   Proteomes; UP000218220; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd06612; STKc_MST1_2; 1.
DR   Gene3D; 4.10.170.10; p53-like tetramerisation domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024205; Mst1_SARAH_domain.
DR   InterPro; IPR036674; p53_tetramer_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR011524; SARAH_dom.
DR   PANTHER; PTHR48015:SF33; SERINE/THREONINE-PROTEIN KINASE HIPPO; 1.
DR   PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR   Pfam; PF11629; Mst1_SARAH; 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; PS50951; SARAH; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          63..314
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          474..521
FT                   /note="SARAH"
FT                   /evidence="ECO:0000259|PROSITE:PS50951"
FT   BINDING         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   528 AA;  59686 MW;  A149074D8DC15829 CRC64;
     MDSEGRLVFW KSGVWEGGAP TLNCNTCKKR RADRMSANDM QRPQGELKKL SEESLTRQPE
     EVFDIICKLG EGSYGSVYKA LHKESGQVLA IKQVPVDTDL QEIIKEISIM QQCDSPYVVK
     YYGSYFKNTD LWIVMEYCGA GSVSDIMRLR KKTLSEDEIA TILCDTLKGL EYLHRRRKIH
     RDIKAGNILL NTEGHAKLAD FGVAGQLTDT MAKRNTVIGT PFWMAPEVIQ EIGYDCVADI
     WSLGITALEM AEGKPPYGDI HPMRAIFMIP TKPPPSFREP DQWSPEFIDF VSQCLVKNPE
     ERATAEYLLT HEFIGNAKHP SILSTMIAEA REIRESQVFR NAQHHTNNAK TFAAGEGYEE
     ATMKQRGDGT LVPSRDATAD LAADLGTMVI NEPDADLATM KRHDTDPMDT NRPKYRPLFL
     EHFEKKEVNH VAANGTLTRM RTPADTADSV EGEAESEANP ALAFQRAFVE EGNFEFLGYL
     GERELEALVS RLDAEMEAEI EQLRARYTRK RQPILDAIHL KRKRQQNF
//
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