ID   A0A0N5A634_PARTI        Unreviewed;       690 AA.
AC   A0A0N5A634;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001737100.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001737100.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   STRING; 131310.A0A0N5A634; -.
DR   WBParaSite; PTRK_0001737100.1; PTRK_0001737100.1; PTRK_0001737100.
DR   Proteomes; UP000038045; Unplaced.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR018297; A/G_cyclase_CS.
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; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   3: Inferred from homology;
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, ECO:0000256|RuleBase:RU000405};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134}.
FT   DOMAIN          462..590
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          315..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          407..434
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   690 AA;  77715 MW;  80590039FF7C8501 CRC64;
     MFGFIHESIR QLMFRRYGEE FWTNVLLRAG FESGKENIVN HYYPDSDTYA LVDSVSALAK
     MSREQVWEMY GAFLIEYTME IGWDELLRTL SPDLKGFLDN LDSLHYFIDH VVYKANLRGP
     SFRCEQNDDG SITLHYFTGR PGLYPIVKGV LREVARRIYL SEISISISGR TQRSVQMSTG
     ERVEEHVIMV IKETPSSTGE TNGSLTNGIN SASTGSIISS ADQKYNLENS VLRVSHSDFL
     GAFPYHFIVD RDCKIVQAGK DLYKHIVPEL LEPGTPLIRV FEITRPQIPL DFDNICNFIN
     AVFVLQVKLP PSNLQRXXXX TQHHGSRAQS DADITSSENS ANQQLKLKGQ MILLESKNHI
     IYLCSPYVTS IPELLQFGMR LSAMPLHDAT RDLILLNQQR LSDVEVNLQL EANNEQLEQM
     AKDLETEKGK TDALLKEMLP ASVASQLISG KSVDAKEYEE ATVMFCDVPN FHNIVPHCQP
     KDVVHLLNEL FTKFDRLVGL HNVYKVETVG DSYMTVGGVP ETCENHCELI CHVALGMLWE
     ARTVEDPVLK KPLQIRAGIH SGPIVAGVVG AKMPRYCLFG DTVNTSSRME SHSPTARIHC
     SSSAFQAANK CGRFEFQKRG TVFIKGKGDM ETYYLKKSLK KSIWEIIQRD RDENVNSIDG
     YQELDEGTDL DSEIVINEGL KAQSKTCSIS
//