ID A0A097F6X4_9NEOP Unreviewed; 681 AA. AC A0A097F6X4; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 27-NOV-2024, entry version 35. DE SubName: Full=PKG {ECO:0000313|EMBL:AIT18204.1}; DE Flags: Fragment; OS Sesamia calamistis. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea; OC Noctuidae; Amphipyrinae; Sesamia. OX NCBI_TaxID=134397 {ECO:0000313|EMBL:AIT18204.1}; RN [1] {ECO:0000313|EMBL:AIT18204.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sc-mtito {ECO:0000313|EMBL:AIT18204.1}; RX PubMed=25274324; DOI=10.1242/jeb.108258; RA Chardonnet F., Capdevielle-Dulac C., Chouquet B., Joly N., Harry M., RA Le Ru B., Silvain J.F., Kaiser L.; RT "Food searching behaviour of a Lepidoptera pest species is modulated by the RT foraging gene polymorphism."; RL J. Exp. Biol. 217:3465-3473(2014). 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; KM017967; AIT18204.1; -; mRNA. DR AlphaFoldDB; A0A097F6X4; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW. DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IEA:InterPro. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR CDD; cd00038; CAP_ED; 2. DR CDD; cd12085; DD_cGKI-alpha; 1. DR CDD; cd05572; STKc_cGK; 1. DR FunFam; 3.30.200.20:FF:000005; cAMP-dependent protein kinase catalytic subunit; 1. DR FunFam; 2.60.120.10:FF:000035; cGMP-dependent protein kinase; 1. DR FunFam; 2.60.120.10:FF:000064; cGMP-dependent protein kinase, isozyme; 1. DR FunFam; 1.10.510.10:FF:000571; Maternal embryonic leucine zipper kinase; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 2. DR Gene3D; 1.20.5.490; Single helix bin; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR002374; cGMP_dep_kinase. DR InterPro; IPR018488; cNMP-bd_CS. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR018490; cNMP-bd_dom_sf. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR035014; STKc_cGK. DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1. DR PANTHER; PTHR24353:SF111; PROTEIN KINASE CGMP-DEPENDENT 1; 1. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF00069; Pkinase; 1. DR PIRSF; PIRSF000559; cGMP-dep_kinase; 1. DR PRINTS; PR00104; CGMPKINASE. DR SMART; SM00100; cNMP; 2. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF51206; cAMP-binding domain-like; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00888; CNMP_BINDING_1; 2. DR PROSITE; PS00889; CNMP_BINDING_2; 2. DR PROSITE; PS50042; CNMP_BINDING_3; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000559- KW 2}; cGMP {ECO:0000256|ARBA:ARBA00022535}; KW cGMP-binding {ECO:0000256|ARBA:ARBA00022992}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Kinase {ECO:0000256|ARBA:ARBA00022777}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRSR:PIRSR000559-2}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 177..292 FT /note="Cyclic nucleotide-binding" FT /evidence="ECO:0000259|PROSITE:PS50042" FT DOMAIN 295..418 FT /note="Cyclic nucleotide-binding" FT /evidence="ECO:0000259|PROSITE:PS50042" FT DOMAIN 433..681 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 124..148 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 89..116 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 557 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000559-1" FT BINDING 439..447 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2" FT BINDING 463 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2, FT ECO:0000256|PROSITE-ProRule:PRU10141" FT NON_TER 681 FT /evidence="ECO:0000313|EMBL:AIT18204.1" SQ SEQUENCE 681 AA; 77481 MW; 9E8EA793FBC3807D CRC64; MRVCFDTLCF GSSQRTAADD EPRAIVNTGG GALTVAPTVN GDRRALNETY REIELNGIMG TPSAMNADSE NCVANATMSN DMQPLIERIR ELEALLKQRD QEMLELRSQL DKLQSVFPYQ QYARGSRAPR KQRAQGISAE PQTSSSLQDL THQTFPTFDK SEVSRELIKS AILDNDFMKN LEMTQIREIV DCMYPVEYAA GSLIIKEGDV GSIVYVMEEG RVEVSRENKY LSTMAPGKVF GELAILYNCK RTATIKAATD CRLWAIERQC FQTIMMRTGL IRQAEYTDFL KSVPIFKDLP EDTLIKISDV LEETHYQNGD YIIRQGARGD TFFIISKGQV KVTQKPPNSN DEKFIRTLTK GDFFGEKALQ GDDLRTANII CDSPEGTTCL VIDRETFNQL ISALDEIRTK YKDEGDSRQR LNEEFANLRL SDLRIIATLG IGGFGRVELV QIQSDSSRSF ALKQMKKAQI VETRQQQHIM SEKEIMSEMN CEFIVKLYKT FKDRKYLYML METCLGGELW TILRDRGQFD DATTRFYTAC VVEAFHYLHS RNIIYRDLKP ENLLLDSKGY VKLVDFGFSK KLQASRKTWT FCGTPEYVAP EVIMNRGHDI SADYWSLGVL MFELLTGSPP FTGTDPMKTY NKILKGIDAV EFPRCITRNA ANLIKKLCRD NPAERLGYQR G //