ID   A0A0N1I7A9_PAPMA        Unreviewed;       969 AA.
AC   A0A0N1I7A9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN   ORFNames=RR48_05857 {ECO:0000313|EMBL:KPJ09994.1};
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:KPJ09994.1, ECO:0000313|Proteomes:UP000053240};
RN   [1] {ECO:0000313|EMBL:KPJ09994.1, ECO:0000313|Proteomes:UP000053240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ09994.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPJ09994.1};
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=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001436};
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DR   EMBL; KQ461033; KPJ09994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1I7A9; -.
DR   STRING; 76193.A0A0N1I7A9; -.
DR   InParanoid; A0A0N1I7A9; -.
DR   Proteomes; UP000053240; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 6.10.250.780; -; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR11920:SF462; GUANYLATE CYCLASE; 1.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          521..839
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          913..964
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          850..881
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   969 AA;  105634 MW;  C81267EC20763E18 CRC64;
     MCGRESRWRD EGRPRPHGAC ARAMTPADMR APQLLLALLA ATAARASSAQ PAPSEHPAPP
     ALLVLRSACS ARDPVYFKAD GLRAYVHAVN KSLPWREFSI LSFNETCGDD WRMSVVQSAA
     RALAGGGVVL LAGRAGLAAC ALRELRPPAA LALPSYCAAP HGLAAVVGAL ASRLRWQSAL
     LPPHAACAHL APFVAHELTA AGLFVSRNPL SRVEIDKRPH VIILCSSETE SVRGAARLQV
     ACARAGAALL LLRLAPDAGP DVVAPDAGPD ATAHDADRDA AAPDSGPDAA APDAAHYITN
     MKSLYYDRQL PQSMNISKRS GSTNTSLDES AKHFERPEIT SNRQSRFLND KKKHFQKYST
     ARGRRWPRLT LLLSDEPPGG RPRADVYAEV LRAIERNAEE ANVGVEIAHN EYFLYEETSE
     PNRSWVPVGQ LVATSLRPPD GRHEWLTFVE VVDPAGEFQR WLAAAAAETS VGWVQNAWSA
     VVSAAALLTL AATCALCCHR VRARAPALSA PVLSAADFSF PAEERRVGEG MESMASWLQR
     LPGCGAPLPA APSSTCSVTR LASDGRTLYK GEPVHVRAVP DGAGGAGGSL RRRAADLLLV
     LQALRHDNVN PFIGWLAEAR GVRGVRGALV FAACARGSLE DVLVADDIPL DWTFRLSLLT
     DLVRGMRYLH ASPLRVHGRL SSRNCVVDAR WVLRVTDYGV PAFAHAQALP LPTRSARGAQ
     SISTIRRYCS GRMQKSRPEL LWTAPELLRS GGNAGGTQAG DVFSFAIIMQ EVIVRGEPYC
     MLQLTPEEIV EKLRRGPPLV RPSVSLGAAP PDAVRAMRQC WAESPAMRPD FARLYHQFRL
     MHRGRKINIV DSMFEMLEKY SNNLEELIKE RTEQLDLEKK KTEQLLNRML PRPVAERLVL
     GLRVPPEEFE EVTIYFSDIV GFTELAARST PVQVVDLLND LYSSFDAAIE RYGVYKVRFC
     LDSISLTDL
//