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Database: UniProt
Entry: A0A194RK59_PAPMA
LinkDB: A0A194RK59_PAPMA
Original site: A0A194RK59_PAPMA 
ID   A0A194RK59_PAPMA        Unreviewed;      1356 AA.
AC   A0A194RK59;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   28-JUN-2023, entry version 26.
DE   RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN   ORFNames=RR48_06620 {ECO:0000313|EMBL:KPJ17814.1};
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:KPJ17814.1, ECO:0000313|Proteomes:UP000053240};
RN   [1] {ECO:0000313|EMBL:KPJ17814.1, ECO:0000313|Proteomes:UP000053240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ17814.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPJ17814.1};
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; KQ460106; KPJ17814.1; -; Genomic_DNA.
DR   STRING; 76193.A0A194RK59; -.
DR   InParanoid; A0A194RK59; -.
DR   Proteomes; UP000053240; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
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; IPR032628; AC_N.
DR   InterPro; IPR009398; Adcy_conserved_dom.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR   PANTHER; PTHR45627:SF1; ADENYLATE CYCLASE TYPE 8; 1.
DR   Pfam; PF16214; AC_N; 1.
DR   Pfam; PF06327; Adcy_cons_dom; 1.
DR   Pfam; PF00211; Guanylate_cyc; 2.
DR   SMART; SM00044; CYCc; 2.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
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:UP000053240};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        147..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        180..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        208..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        700..718
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        724..744
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        822..842
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        847..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        880..899
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          391..518
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          965..1101
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          55..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1186..1213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1232..1356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1249..1263
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1284..1299
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1300..1327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1328..1356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1356 AA;  153890 MW;  6F86428F9AC04698 CRC64;
     MHNTIHIAEK GTEWKNTLRE MLSYPQEFGN DVQRKRARDI YGLCCEVVRE GDCEAAPDSE
     RLPGDGASCS APDDQHRISD EDGSSNSPRN SIDPFRTESD PVSSESILRT GRYYKGIYWP
     SITNSFKDET VELSYQRYSR RQRQKSLIMV NVVDLALKIC LSLIYTLTNR HDIESVADGY
     QIAWTVAFAC LNVAVCLLGC WRCFANNYLH WAAAATWILL IAQGLSGQGI GFQAPENQVW
     YMLFIIFAPY AMLPLSLGWC IVIGLLSSVS HVLATAVVIK DIMNNSAEVA QSCAIRLLVA
     NALLYNAVNF AGMYAKYLTD WGQRKAFLET HRSMVTRQRT KRESDRQWKL FQSVIPDFLA
     KEIYSHVSRV KGEFQEQQFN NLYIQRHENV SILFADIKGF TELSSKCNAQ ELVKILNELF
     ARFDRLATEN HCLRIKLLGD CYFCVSGLPE RRSNHAYCCV NMGLHMIRVI RDVRYNAQVD
     LDMRIGVHSG AVLCGVLGLL KWQFDLWSLD VTIANHMESG GLPGRVHISS ATLECLNGTF
     EVEAGEGETR DPCLRELGLT TYLIKSSEQP RRTRHRSRPN CIQAVPQAPC DTPRRTSSSI
     DDENTTDWTP EMPFQSYFSS SSAIVTRLPC LIKREDAEQG QDVEITSMSD EDDIINHSIE
     VSSNRRMRLD NMRSWSLRFR RASLEQRFAS QDERTFKSNV MCCLVLWLFI LAVQYVIHFN
     CWKLVAILGV MTVPLALSFC LVMAEEFPGV APRVARVSAA LGRSRLRRNL HICGFVTIMS
     ISSTTKLYIC PSSFRNATSS LERPNGTDTE HERAGECYRP EYIVFTWILC LVALTSILKL
     YYLIKTLLAV LNVAMFSVLL LLYYNEYDFN SLNRSTQLPF YVQMLILMVM FLVMVVYHAR
     LVEVTSRLDL LWRLQAQTDL AEMRDTQRTN RHLLKHILPD HVVAHFLAKD RCPDELYSQW
     RDEVGVMFAG IPNFHEFYSE QKAIDCMRLL NEIIFDFDKL LMQPRFKSIE KIKTIGATYM
     AASGLNPNHK SGQDECEHLC ALVDYAFALR EALDDINKHS FNKFRLRVGI SCGPLVGGVI
     GARKPVYDIW GNTVNEASRM ESTGAMDRIQ VTKYTKQVLE RRGYGLEARG LVEVKGKGRM
     ETWWVRRRRA RGAGPLPAPA PPRSLAALVY TMLQARKRIY THPLDTPAIS SSRAGSVRAE
     RRAPKRHTHT NGQKMEMGIR PHASSMVVRR PDMAPPIMGS ASAPHTPTAP HAPQAPQPAA
     PQPHMSEPRL GIGARLKAAS FSYRTRPARE RDRSPRLRDQ TEGSTGSVAN GTPGSFRFRS
     VTTASFFRSR NRDRRNKEQV DEDAKENGDT HVTTRM
//
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