ID A0A194R1R1_PAPMA Unreviewed; 510 AA.
AC A0A194R1R1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=calcium/calmodulin-dependent protein kinase {ECO:0000256|ARBA:ARBA00012434};
DE EC=2.7.11.17 {ECO:0000256|ARBA:ARBA00012434};
GN ORFNames=RR48_15098 {ECO:0000313|EMBL:KPJ11459.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ11459.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ11459.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ11459.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ11459.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
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=2.7.11.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000902};
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=2.7.11.17; Evidence={ECO:0000256|ARBA:ARBA00000517};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000256|ARBA:ARBA00005354}.
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DR EMBL; KQ460883; KPJ11459.1; -; Genomic_DNA.
DR RefSeq; XP_014363729.1; XM_014508243.1.
DR AlphaFoldDB; A0A194R1R1; -.
DR STRING; 76193.A0A194R1R1; -.
DR GeneID; 106715049; -.
DR KEGG; pmac:106715049; -.
DR InParanoid; A0A194R1R1; -.
DR OMA; ECAQSVP; -.
DR OrthoDB; 1121238at2759; -.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14086; STKc_CaMKII; 1.
DR Gene3D; 3.10.450.50; -; 1.
DR Gene3D; 6.10.140.620; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032710; NTF2-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; PTHR24347:SF441; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT GAMMA; 1.
DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08332; CaMKII_AD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54427; NTF2-like; 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; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Kinase {ECO:0000313|EMBL:KPJ11459.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW Transferase {ECO:0000313|EMBL:KPJ11459.1}.
FT DOMAIN 17..275
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 320..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 510 AA; 57578 MW; 0E75F94301EEFD7E CRC64;
MANPNRESVS TRFSDNYDLK EELGKGAFSI VRRAVQKSTG YEFAAKIINT KKLSARDFQK
LEREARICRK LQHPNIVRLH DSIQEEHFHY LVFDLVTGGE LFEDIVAREF YSEADASHCI
QQILESVHHC HHNGVVHRDL KPENLLLASK AKGAAVKLAD FGLAIEVQGD QQAWFGFAGT
PGYLSPEVLK KEPYGKPVDI WACGVILYIL LVGYPPFWDE DQHRLYGQIK AGAYDYPSPE
WDTVTPEAKS LINQMLTVNP SKRITASEAL KHPWICHRER VASVMHRQET VDCLKKFNAR
RKLKGAILTT MLATRNFSGK SMVNKKGDGS QVKESTDSST TLEDEDLDKD KKGVDRACTV
ISKDHEEEAL TKADSFGKAR GDSNASLRRA EVIKVTEVLI DAVNNGDYDT YSKLCDPNVT
AFDPDALGNL VEGVEFHKFF IDNTPTHVKT NTTILNPRVH LLGDDVAVIA YVCLTQSVDA
EGRRETHQSQ ETRIWHKRHN KWIAVHFHRS
//
