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Database: UniProt
Entry: A0A016V8S9_9BILA
LinkDB: A0A016V8S9_9BILA
Original site: A0A016V8S9_9BILA 
ID   A0A016V8S9_9BILA        Unreviewed;       263 AA.
AC   A0A016V8S9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Guanylate cyclase domain-containing protein {ECO:0000259|PROSITE:PS50125};
GN   Name=Acey_s0014.g2276 {ECO:0000313|EMBL:EYC24029.1};
GN   ORFNames=Y032_0014g2276 {ECO:0000313|EMBL:EYC24029.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC24029.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(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};
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYC24029.1}.
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DR   EMBL; JARK01001350; EYC24029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016V8S9; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
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   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR011645; HNOB_dom_associated.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   PANTHER; PTHR11920:SF503; RECEPTOR-TYPE GUANYLATE CYCLASE GCY-9; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07701; HNOBA; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          78..208
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   COILED          15..42
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   263 AA;  29160 MW;  28F9EA6E8C96E236 CRC64;
     MVNANLRSTG KGSLVDQMMK MMEEYTSNLE NMVRDRTALL EEAQKQADRL LNSMLPKSVA
     EDLKVGKPVL PQLYQCATVL FSDIRGFTRI SSTSTPLQVV TFLNDMFSGF DAIIAKHDAY
     KVETIGDAYM IVSGVPNENG NNHVQHIADI ALKMRSFVSN FKLAHRPDEV MMVRIGFHSG
     SVAAGVVGLA APRYCLFGDT VNMASRMEST GVANKIQISE QAHNLLHCFF QQFVVVERGK
     IEVKGKGECT TFYLEGKTVP KNR
//
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