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Database: UniProt
Entry: A0A194PKE1_PAPXU
LinkDB: A0A194PKE1_PAPXU
Original site: A0A194PKE1_PAPXU 
ID   A0A194PKE1_PAPXU        Unreviewed;      1362 AA.
AC   A0A194PKE1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN   ORFNames=RR46_15064 {ECO:0000313|EMBL:KPI91560.1};
OS   Papilio xuthus (Asian swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI91560.1, ECO:0000313|Proteomes:UP000053268};
RN   [1] {ECO:0000313|EMBL:KPI91560.1, ECO:0000313|Proteomes:UP000053268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI91560.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPI91560.1};
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 = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001593};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   EMBL; KQ459606; KPI91560.1; -; Genomic_DNA.
DR   STRING; 66420.A0A194PKE1; -.
DR   Proteomes; UP000053268; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 2.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR009398; Adcy_conserved_dom.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR   PANTHER; PTHR45627:SF26; ADENYLATE CYCLASE TYPE 1; 1.
DR   Pfam; PF06327; Adcy_cons_dom; 1.
DR   Pfam; PF00211; Guanylate_cyc; 2.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        294..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        323..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        358..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        424..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        452..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        488..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..36
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          573..715
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          187..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1023..1075
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1146..1173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1186..1266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..783
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..836
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..880
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        913..942
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1058
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1198..1221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1222..1242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1362 AA;  149418 MW;  01F5D45BCABA42C3 CRC64;
     MRVGIHTGRV LCGVLGLRKW QYDVWSNDVT LANNMEAGGE PGRVHVTQAT LECLGGAYEV
     EPGHGGTRNA YLRDHSVQTY FIIPPPRRRK MCLSAGVGLG SGSRRKLSFK NVSNVVVQLL
     HSIKFNVDVP FSNMAASPQE LKANAARKEE GTGLGLCQVL DLRRALHAEP GSAEALRLAA
     LRGDDVSAPA APAAPAPAAP PPAAAPHHHT FDAVMQHHAL RTHPTNKVTE KFKRPLKKRH
     SSVYHQPTNR VNKYLAQAID ARSVHREKAT HVHLLTLCFK DAEKEAQYRA STDGGWAGSL
     GAALCALAAG GVLQAAILPR TTILLLLFVT AFAWSAAVLA LTLAARLRLI PCDVSRPFAL
     RNAITTFTIV LGYAVGQVNV VTCREIDVCR NLTENVTTMS EIRELRGGLA AALWSAGDHR
     ACPVPLYIAL GCCLAVLTVA VFLRLPILIK GILLAVITAG YVSVILAYHK DLFDCYDMMT
     DVGVVGSAWS MCLWSLLLAV GVLLHARQTE WTARLDFLWQ AQARDEKRDM DALQASNKRI
     LFNLLPAHVA THFLDNQFRT NMDLYHQSYQ RVGVVFASIT NYHEFYMELD GNNQGMECLR
     LLNEIIADFD ELLGEDRFSP IDKIKTVGST YMAAVGLIPD KKMTDDPSTR KHMATLVEFV
     FAMRDKLKDI NDNSYNNFML RVGINVGPVV AGVIGARKPQ YDIWGNTVNV ASRMDSTGLP
     NHTQVTEEVY QVLKDMPYQF VCRGKVKVKG KGEMTTYFLT DRTLDNGGGQ NNSNGQPQNP
     PSAYGGVATP LAMLQNSARR AAAQPSRLPP LRESTGSGEN EPLLPPNGQQ NGNNHKGTKG
     RRNKDQDDNP PPPPPHGISA NPRWPPPRAL VPPWPRPQEP RPPVVHKRRP PTRLPRPRSS
     ESLPLARSPR VHSSADELSS LTRSPSLSSS DESYSRTTDA SPSPPRPAAW LPPARPSRND
     ITSAYDYPVL RTNKPTANVI NELYAKHKLS NKPVLEDKIL DDIGYQKEEE KLHRSILNML
     QTSAKRDSCS QTDKKDVSSR LAPRTNSFSS SGSRPTNLKH LNHDSREVFS KRSPSDVACV
     PPFEREIQRL LDDKNIIMNN PPKNERKDLN LELRSQNSSL EVGRSANNNS SPLHAVGLAA
     IAQLARREPS PAPTHPPPPA PTHAHAHAHT DFPGVLPTDV VVCLPSRDNT PGGTFDRKID
     SSTKEKHEND AHERLHNRVT TSNHREMNLY GESQSEWSSS CSDGEGDGEG EGECGQPEST
     GYTTDDPALE NVSMLNEAGL TDAEAALSDV NSCYFDRDDD VSSRASSRLL DSEALVSLES
     LSAIYDSDEP AHRYLANIRT VSESITRNFG QPAHVTDGES DV
//
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