ID A8X487_CAEBR Unreviewed; 759 AA.
AC A8X487;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN Name=gcy-36 {ECO:0000313|WormBase:CBG07710a};
GN Synonyms=Cbr-gcy-36 {ECO:0000313|EMBL:CAP27447.2};
GN ORFNames=CBG07710 {ECO:0000313|WormBase:CBG07710a}, CBG_07710
GN {ECO:0000313|EMBL:CAP27447.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP27447.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP27447.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP27447.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE601041; CAP27447.2; -; Genomic_DNA.
DR RefSeq; XP_002645943.1; XM_002645897.1.
DR AlphaFoldDB; A8X487; -.
DR STRING; 6238.A8X487; -.
DR GeneID; 8587942; -.
DR WormBase; CBG07710a; CBP45995; WBGene00029673; Cbr-gcy-36.
DR eggNOG; KOG4171; Eukaryota.
DR HOGENOM; CLU_011614_4_0_1; -.
DR InParanoid; A8X487; -.
DR OMA; YPKRLWI; -.
DR OrthoDB; 2898719at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0070482; P:response to oxygen levels; IBA:GO_Central.
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:UP000008549}.
FT DOMAIN 534..662
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 479..506
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 759 AA; 85950 MW; 51C76398BBF7EF42 CRC64;
MSQTLPQSTA EFSELYSAFV KKELSFSKKG SNVRKEIVQQ TIEGRLAAFL VIRKCRKRAA
AINAKKATDN MEEKTTKRPT KCCVFGFIHE SVRQLMIRTY GESFWAKVLE RAGFEAGKEN
IINHYYSDQD TYTLIDAVSV ILKVTREQVW EMYGCFLIQY TMETGWDDLI RSMSPNLKGF
LDNLDSLHYF IDHVVYKANL RGPSFRCEDN PDGTITLHYY TGRPGLYPIV KGVLREAAKR
VFKLDVSMSI TGRTQRSVQM ATGERIEEHV IFLIKTQNTD QSNEDALGTA VVQHSNNYKI
RLTHMDFVTT FPYHMVVDQD CKIVQVGREL YNHIPKDLLA VGTPLMRIFE VTRPQIPLDF
DSICNFINAV FVLQVKTTPM EFQRNANKRA GQITDGFDNA PEDGNSAVAT LSQSQHLKLK
GQMMLMTSGG HIMYLCSPYV TSIPELLQYG LRLTAMPLHD ATRDLILLNQ QRLSDVEMNL
QLEANNEQLE NMAKDLEVEK GKTDALLREM LPPSVAQQLK QGLSVDAREY EEATVMFTDV
PTFQQIVPLC QPKDIVHLLN ELFTKFDRLI GIQKAYKVET VGDSYMSVGG IPDTVDDHCE
VICHLALGMV MEARTVCDPI TSTPLHIRAG IHSGPVVAGV VGAKMPRYCL FGDTVNTASR
MESHSPIGRI HCSENAKKCA ESTGRFEFEP RGKVQIKGKG EMNTYFLLRS FKRSIWEIID
RRRDENCNSI DGYNELREGY VDDVINKTTQ KNSKTCSIS
//
