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Database: UniProt
Entry: A0A3Q0J9Y7_DIACI
LinkDB: A0A3Q0J9Y7_DIACI
Original site: A0A3Q0J9Y7_DIACI 
ID   A0A3Q0J9Y7_DIACI        Unreviewed;       493 AA.
AC   A0A3Q0J9Y7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN   Name=LOC103514898 {ECO:0000313|RefSeq:XP_026683540.1};
OS   Diaphorina citri (Asian citrus psyllid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae;
OC   Diaphorininae; Diaphorina.
OX   NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_026683540.1};
RN   [1] {ECO:0000313|RefSeq:XP_026683540.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_026683540.1; XM_026827739.1.
DR   AlphaFoldDB; A0A3Q0J9Y7; -.
DR   STRING; 121845.A0A3Q0J9Y7; -.
DR   PaxDb; 121845-A0A3Q0J9Y7; -.
DR   KEGG; dci:103514898; -.
DR   OrthoDB; 3087296at2759; -.
DR   Proteomes; UP000079169; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009975; F:cyclase activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016849; F:phosphorus-oxygen lyase activity; IEA:InterPro.
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; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR   PANTHER; PTHR45627:SF12; ADENYLATE CYCLASE TYPE 3; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
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:UP000079169};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..493
FT                   /note="adenylate cyclase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017975621"
FT   TRANSMEM        73..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          223..370
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   493 AA;  54929 MW;  9EBF0C6AF60FF9BC CRC64;
     MGASVSLLIF LVNIIYMLMC ESSPAETANF NSTSTDDAAA TATTVAAAST VAPLHNCTLS
     ETSSTQLCVF PSYYSMFCIL VLIGIILHGQ NTFLQKVILL AAMVAFQIGS NYFFIRESMQ
     CERYFSGVFP GGNPQFGLLG PSTLLLFVAL SLTFLAFYME KASKVLFIWK KEVESQKETA
     SDIRRRNEAL VYNILPPHVA SHFLGNRKRQ HEELYSQSYA EVGVLFASMP NFSEFYCEDD
     VNKQGLECLR FLNEVISDFD ALLELPKFKE VIKIKTIGST YMAASGLDPN FVATIKPSDP
     IEVRWKHLDV LIEFAMEMKK ALTGINEQSF NHFVLKMGVN HGPITAGVIG ARKPHYDIWG
     NTVNVASRME STGRAGFIQV TEETTHILQH FGYIFEQRGL VSVKGKGQLM TYYLLGKSTT
     GANYPSGLPP FENSVMEPLK EVDEEKEEEI HEGQVNLDMD ETNETEGLLK KEDVQNGVIV
     NPTVPSEEQE NLL
//
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