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Database: UniProt
Entry: G0NLP8_CAEBE
LinkDB: G0NLP8_CAEBE
Original site: G0NLP8_CAEBE 
ID   G0NLP8_CAEBE            Unreviewed;       817 AA.
AC   G0NLP8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
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_08948 {ECO:0000313|EMBL:EGT33839.1};
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; GL379906; EGT33839.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0NLP8; -.
DR   STRING; 135651.G0NLP8; -.
DR   eggNOG; KOG1023; Eukaryota.
DR   HOGENOM; CLU_001072_1_3_1; -.
DR   InParanoid; G0NLP8; -.
DR   OMA; TVANERW; -.
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; 6.10.250.780; -; 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; IPR001828; ANF_lig-bd_rcpt.
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:SF265; RECEPTOR-TYPE GUANYLATE CYCLASE GCY-1-RELATED; 1.
DR   Pfam; PF01094; ANF_receptor; 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   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..817
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003405076"
FT   TRANSMEM        242..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          291..589
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          627..689
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   817 AA;  92952 MW;  0B6B951EBB7E600E CRC64;
     MDVIWKVLSL FILFYEVDGQ LISTYNGTAN STAGSRRTIK VGIAAAQQIQ TGSIGWSVCG
     GAVPLAIEKL KQAGYAKNFD FELGFAAAKM LQQYRWGRIA MLYYQSDLDY CSKVMDDVEA
     TFNDQDTPVN IVIKAEMYLN DDETTDIVLQ SVKSRARSMT GEVVISTNLT RMSIFQLYGL
     NAQYDQAAYI NFTFINDKMS VSVFYKDEAT TVWHFYGYSR PLDTPICGFL GKSCPVSFWE
     QYRILIVVAI ILILLLMVLI LVGCCCMISS RRAEQERINS EWQIPFLKLL EPEKRQRAHG
     ASKRSLQSAP STATGDSRLT AISDFCENYT IMVYEKDMVL TAKHQYTHLT KADMERFVKL
     RTLEHENLNK FIGLSIDSSH FIAVSKLCSR GSLQDILSRG NFSMDYFFMF CIIRDVAKGM
     DYLHKSFLRL HGNLRSATCL VNDSWQVKLA EYGLDNLDEE QTPPKKRLLW VAPEVLRGSL
     SVSQMDSSAD VYSFAIIASE ILTRKEAWDF LDRKEDCEEI VYMVKKGGPF PIRPEIVTDI
     PDVNPTLISL VKDCWAENPE DRPTANSICT QLKSMMPKSK SNLMDHVFNM LEEYTATLEV
     EIEDRTKELT LEKKKADLLL SRMLPQQIVD MSLRFMEYCS HFKIPHLPRE KVELRIGINS
     GPCVAGVVGL SMPRYCLFGD TVNTASRMES NGKPSMIHMT ADAYSLLITH YPHQYETSSR
     GEVIIKGKGV METYWVLGKV EDYMDNFGRR ETLPVHELVE FKPEPILKQS ANKKEEVSEE
     CSLKGKEIRS VSSHSSRSSS VFNPLKDHRE FKMEMCV
//
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