ID   G0NL65_CAEBE            Unreviewed;      1061 AA.
AC   G0NL65;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Guanylate cyclase {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
GN   ORFNames=CAEBREN_24032 {ECO:0000313|EMBL:EGT33280.1};
OS   Caenorhabditis brenneri (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN   [1] {ECO:0000313|Proteomes:UP000008068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG   Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA   Wilson R.K.;
RL   Submitted (JUL-2011) 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         ECO:0000256|RuleBase:RU003431};
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   EMBL; GL379904; EGT33280.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0NL65; -.
DR   STRING; 135651.G0NL65; -.
DR   EnsemblMetazoa; CBN24032.1; CBN24032.1; WBGene00162757.
DR   eggNOG; KOG1023; Eukaryota.
DR   HOGENOM; CLU_001072_1_2_1; -.
DR   InParanoid; G0NL65; -.
DR   OMA; YERKLHS; -.
DR   Proteomes; UP000008068; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   PANTHER; PTHR11920:SF436; RECEPTOR-TYPE GUANYLATE CYCLASE GCY-15-RELATED; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293,
KW   ECO:0000256|RuleBase:RU003431};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        386..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          478..780
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          851..981
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   1061 AA;  118872 MW;  405308177B0F1C33 CRC64;
     MGLSRSCYIQ STILNINGKI GLSDVCEMDL SSVKGFDQTT VLMNSQTNSL AKSVIYFLNK
     YSWTKVALVS PSTTLSAFDS RVRSDLLDAL TTSKIDVLVD TRVDPMTDFS DKVKEDAQKA
     RIFIICDWSS NANLLQNYLF RLGEMNKMQS GEYFVLGYVA YGTNYQWLEA TTGDQRLLHL
     GASDCRLNDY NLTENDLHEV YKNVVILSDG PPPAEPNSTW KDIQNQILTK KAKKMCPPFC
     NTTVSDKISP RWDRIKLLFD GIQYLADATN DALKIGANIY LSSIFYEYLL SRQIESVSGV
     TEYVDGYGAI VGSMQIYYHF TSTVHNAYSL YPCARLGQAS LLTTQWTLTD YSEGLSIDFV
     NKSAPKDTPE CGFYGEKCAP PGSNTFIIVI SVGMAVLIGL AIAAAFLYKR YRYERKLHSL
     FFMIDRNQII LKKHTNLMSQ QSLRSMASIH GSVVAASQTL RDSHFFIEDF NNVGASNSQM
     SSIFHTGSTA RVTGSFGPIP GFGGVTGTSE DDKWHQIADF GVGLFEGRTV ALKRIYRTDV
     ELTRSIRMEI AKFQEASNSN LIEFVGLVIH SPDVFVVTEL AQRGSLKDIL DNDDMPLDDV
     FRAQMTKDIL AGLEYLHSSP IGCHGRLKST NCLIDGRWMI RLSSFGLREM RAEEMTEREE
     DVQAGKDDLW TAPELLRWST GLNECGHLLV QKADVYSLAI VLYELFGRLG PWGDEPMEPT
     EIVSLVKRGT ASGKKAFRPD LAVIKEAPTI VQHTVAAAWT EDPLDRPSLF QIKRKLRPLT
     VGLKRTIMDN MVSIIEKFTV KLEKDIAERN EELEAEKQKS EMLLKMMLPE VVADSLKLGS
     NVSAESFECC TVFFSDCPGF VEMSATSKPI DIVQFLNDLY TVFDRVIDQF DVYKVETIAD
     AYMVASGLPI PNGNHHVGEI ASLGLALLKA VEAFKIRHLP NEKVRLRIGM NSGPCVAGVV
     GLKMPRYCLF GDTVNTASRM ESNGIPLRIN CSESSKQILD QLGGYQMEER GIVEMKGKGK
     QMTYFVRGED EEMRRERIIR DRVKFVSLKK AKIQEKTFEF V
//