ID E3LP94_CAERE Unreviewed; 686 AA.
AC E3LP94;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN Name=Cre-gcy-34 {ECO:0000313|EMBL:EFP05430.1};
GN ORFNames=CRE_27550 {ECO:0000313|EMBL:EFP05430.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 EMBL; DS268412; EFP05430.1; -; Genomic_DNA.
DR RefSeq; XP_003114092.1; XM_003114044.1.
DR AlphaFoldDB; E3LP94; -.
DR STRING; 31234.E3LP94; -.
DR EnsemblMetazoa; CRE27550.1; CRE27550.1; WBGene00052783.
DR eggNOG; KOG4171; Eukaryota.
DR HOGENOM; CLU_011614_4_0_1; -.
DR InParanoid; E3LP94; -.
DR OMA; YEATVMF; -.
DR OrthoDB; 2898719at2759; -.
DR Proteomes; UP000008281; 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:0007635; P:chemosensory behavior; IEA:EnsemblMetazoa.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0050913; P:sensory perception of bitter taste; IEA:EnsemblMetazoa.
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:SF12; SOLUBLE GUANYLATE CYCLASE GCY-34; 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};
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:UP000008281}.
FT DOMAIN 455..583
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 686 AA; 78216 MW; AA8B721B354B3EEF CRC64;
MFGFIHESIR QLVIRKYGED TWLQVLERSG FENGKENIVN HYYSDTDTYV LVDSVSIVIK
VTKDQVWEMY GGFLITYSME IGWDELVRSM SPNLKGFLDN LDSLHYFIDH VVYKANLRGP
SFRCEENPDG TLMLHYFTGR PGLYHIVKGV VKEVAKLVFN LDITLSVQGR TQRSVHMNNG
ERVEEHVIFL IKNVGENRRD SEASTVSLMT SAAPDFGEIV DDNLRMSLQD FSKALPYHFV
LDESCKLVQC GDELYNHIPN ELLKPGTPIL RIFEINRPQI PLDFENICNF INAVFVLQVK
TSPLKKKHMD ALTKEEQEQE VEAMEAENTS NELTQGCHLK LKGQMMMLAT KKHIIYLCSP
YVTSINELMQ FGMRLTAMPL HDATRDLILL NQQRLTDVEV NLQLEANNEQ LETMTRELEL
ERKKTDSILK DMLPRKIAKQ LLSGEHIEPC EYETTVMFCD LPAFQQIIPV CQPKNIVKLL
NEVFFKLDRI VVLRGVYKVE TVSDSYMTVS GIPDYTNEHA ETMCHVALGM MWEARSVMDP
VNNTPFLLRI GLHSGTIIAG VVGTKMPRYC LFGETVTLAS QMESLGLAGK IQCSKWTYTQ
AMETGRFEFA PRGRITVKGR GDVETYFLTR SLKKSIWEIT DHERDVNVNS IEGYEELETS
IESAQAARND NTTKANQNNS AACTIA
//