ID   A0A0C2G493_9BILA        Unreviewed;       478 AA.
AC   A0A0C2G493;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN   ORFNames=ANCDUO_14036 {ECO:0000313|EMBL:KIH55800.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH55800.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH55800.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH55800.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- 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};
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; KN736719; KIH55800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2G493; -.
DR   Proteomes; UP000054047; 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:SF16; ADENYLATE CYCLASE; 1.
DR   PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR   Pfam; PF06327; Adcy_cons_dom; 1.
DR   Pfam; PF00211; Guanylate_cyc; 3.
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:UP000054047};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        209..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..43
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          263..399
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   478 AA;  53312 MW;  A72E3E225346BF6A CRC64;
     MTRVNVNMRV GIHSGRAHCG VLGLKKWQFD VWSDDVTLAN HMESGGLPGR VHITRATLDS
     LNGEYIVEEG HGGERSKYLA EHHVDTFLVV EAKNKQASAH PQARLNANKE LRLTGHASKL
     QRGQSLRQAV KPTKPLKDDV ENHLKQGIQA INKENWRQTH CKRITLRFEK DHVEKKDQSI
     TVAKNRCIFQ LRNAKRGAKK LKCSRSVRIF FIFAIVLLAH SAIISALDSD QCSFECTTAG
     PILTNSSCQE IPSGQAEARD YACIIFITIT DFSKFYMELD ANNEGVECLR LLNEIISDFD
     DLLDRDEFKC IEKIKTISTT YMAASGLYGK TEDNSHVVAV ARFAQALLVK IQAINEHSFN
     NFDLRIGINV GPVVAGVIGL MKPHYDIWGN SVNVASRMDS SGVPGKIQVN APLILERTPG
     PATKSVVKVT EETKSILEKE GFQFECRGEI NVKGKGLMTT YFLVSGPYDL QDQVEQFV
//