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Database: UniProt
Entry: A0A016UT92_9BILA
LinkDB: A0A016UT92_9BILA
Original site: A0A016UT92_9BILA 
ID   A0A016UT92_9BILA        Unreviewed;       552 AA.
AC   A0A016UT92;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN   Name=Acey_s0027.g1630 {ECO:0000313|EMBL:EYC18639.1};
GN   ORFNames=Y032_0027g1630 {ECO:0000313|EMBL:EYC18639.1};
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:EYC18639.1, 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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EYC18639.1}.
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DR   EMBL; JARK01001363; EYC18639.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016UT92; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 6.10.250.780; -; 1.
DR   Gene3D; 3.90.1520.10; H-NOX domain; 1.
DR   Gene3D; 3.30.450.260; Haem NO binding associated domain; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR038158; H-NOX_domain_sf.
DR   InterPro; IPR011644; Heme_NO-bd.
DR   InterPro; IPR011645; HNOB_dom_associated.
DR   InterPro; IPR042463; HNOB_dom_associated_sf.
DR   InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR45655; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR   PANTHER; PTHR45655:SF13; SOLUBLE GUANYLATE CYCLASE GCY-35-RELATED; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07700; HNOB; 1.
DR   Pfam; PF07701; HNOBA; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT   DOMAIN          322..450
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   COILED          267..294
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   552 AA;  62760 MW;  F702DD19C3D4FDF3 CRC64;
     MTREQVWEMY GCFLIEYTME IGWDELVRSM SPNLKGFLDN LDSLHYFIDH VVYKANLRGP
     SFRCEENPDG SLTLHYFTGR PGLYPIVKEN FGQALRLNAA DFCNALPYHV IMDEHCHLIQ
     TGRELANHIP KELLAVGTPI MRIFEVNRPQ IPFDFDNICN FINAVFVLQV KTSPTDMRKQ
     REQAERLEDG NGSIASTAFH QGHHLKLKGQ MMLLSDSKSL IYLCSPYVTS IPELMQYGMR
     LTAMPLHDAT RDLILLNQQR LTDVEVNLQL EANNEQLEIL AKDLDAEKRK TERILRDMLP
     SSVASQLMSG EHIEAREYEH ATVMFSDVPN FQSVLSNSQP KDIVQMLNDL FHRFDRLVLM
     HKVFKVETVG DSYLTVGGIP EQLAEHAEII CHVAIGMLWE ARAVFEPVTK KSINVRIGIH
     SGPLVAGVVA LCMPRYCLFG ETVSMASSIE MNGLPGKIHC SEKTYKYAMQ TGRFDFTSRG
     RILIKGKGEM ETYLLVRSTK KSVWEIVDRE RDVQKNSIDG YEELETGMSF AAQQHTIVRP
     LATQTSKTCS IS
//
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