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Database: UniProt
Entry: A0A0K0E3P7_STRER
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ID   A0A0K0E3P7_STRER        Unreviewed;       685 AA.
AC   A0A0K0E3P7;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000411800.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0000411800.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) 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   AlphaFoldDB; A0A0K0E3P7; -.
DR   STRING; 6248.A0A0K0E3P7; -.
DR   WBParaSite; SSTP_0000411800.1; SSTP_0000411800.1; SSTP_0000411800.
DR   Proteomes; UP000035681; 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: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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681}.
FT   DOMAIN          457..585
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   COILED          402..429
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   685 AA;  77885 MW;  26F51897CEAFBE46 CRC64;
     MFGFIHESIR QLMFRRYGEE FWANVLLRTG FESGKENIVN HYYPDSDTYA LVDSVAALAK
     MSREQVWEMY GAFLIEYTME IGWDELLRTL SPDLKGFLDN LDSLHYFIDH VVYKANLRGP
     SFRCEQNDDG SITLHYFTGR PGLYPIVKGV LREVAKRIYL SEIAISISGR TQRSVQMSTG
     ERVEEHVIMH IRETPVKGTT ENTPAIGNGA NSDSTSSVMS SSDLKFSLEN CTLRVSHNDF
     LTSFPYHFIV DRDCKLVQAG KDLYKHILPE LLEPGTPIIR IFEITRPQIP LDFDNICNFI
     NAVFVLQVKL PPSNLQKINS KILNENDINS STEGNPNQQL KLKGQMILLE SKNHIIYLCS
     PYVTSIPELL QFGMRLSAMP LHDATRDLIL LNQQRLSDVE VNLQLEANNE QLERMAKDLE
     LEKGKTDALL KEMLPVTVAQ QLISGKSVDA KEYEEATVMF CDVPNFHNIV LYCQPKDVVH
     LLNELFTKFD RLVVYHNVYK VETVGDSYMT VGGIPEVIEN HCELVCHVAL GMLWEGRTVE
     DPVLKRPLQI RAGIHTGPIV AGVVGAKMPR YCLFGDTVNT ASRMESHSPT ARIHCSSTTF
     EAANKCGRFE FEKRGTVFIK GKGDMETYYL KKSFKKSIWE IIQRERDENI NSIDGYRELD
     DGNDINTESI INEDLKTQSK TCTIS
//
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