ID A0A1I7V4E1_9PELO Unreviewed; 1038 AA.
AC A0A1I7V4E1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
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};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold630.g22277.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold630.g22277.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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 ECO:0000256|RuleBase:RU003431};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR AlphaFoldDB; A0A1I7V4E1; -.
DR STRING; 1561998.A0A1I7V4E1; -.
DR WBParaSite; Csp11.Scaffold630.g22277.t1; Csp11.Scaffold630.g22277.t1; Csp11.Scaffold630.g22277.
DR eggNOG; KOG1023; Eukaryota.
DR Proteomes; UP000095282; Unplaced.
DR GO; GO:0005886; C:plasma 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 CDD; cd06352; PBP1_NPR_GC-like; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; IPR011645; HNOB_dom_associated.
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:SF495; RECEPTOR-TYPE GUANYLATE CYCLASE GCY-7; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07701; HNOBA; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 417..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 429..768
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 826..956
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1008..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 116498 MW; AD83371BFD52B08F CRC64;
MPRVTIPLSS FTIVWDDCIE SEAAGKTVEL IEKHNVDVII GPTMNQPTLA SFIVSNYYNR
PVIAWGLVNA AQLDDFERFP NAGIMSAGQR SLGVAIRAVL SEYGWNQFVF AYFTEEDAEK
CVTMRNDLQQ VVSYFGDIIL AYSIQVTDIS NDGMIAALRK IESRGRIIVT CMKDGIGLRR
KWVLAAEEAG MIGDEYVYIF SDIKSKGYYV PLLGGGERPA WIPSTGADEN TTRALKAFKK
SIFVCDMMGQ GSIATNYTIF GQEVIARMKE APYFCTDDCE GKNYSVAATY SGQLHDAVYA
YGVALDKMQK AGQMANYRNA SAFMRFFPQQ FVGMSGNVNI NDKGTRNPTL FLLSLDENGN
SSLRATIYVE NMSATFSPLY TDEGVMWSSR KGNVRPNDVP TCGFTGTGCP KSFVEEYLVW
VIVAVVVLFL ALCAAGSGIY FSIKARRDEV ERLNMLWQIP FVHLHQINSK QKGKTEHSVR
SLQSGTSTMS SRTTVSFKTE TRNFLFYSLQ RESDYEPVVA KKHAYRPRLD DEKCAFMRSL
RTLDHDNLNR FIGLCLDGPQ MLSVWRFCSR GSMADVILKA TIQMDNFFIY SLIKDIVHGL
VFLHGSIVGC HGMLTSKCCL IDDRWQVKIS NYGLKDLRSI EMYEKKDLLW SAPELLREEN
IKGTKEGDVY SLGIICAELI TRKGVFNMED RKEDPEEIIY LLKKGGMKSP RPDLDYDHTI
EINPALLHLI RDCFTERPSE RPPIETVRSQ LRGMNSSRND NLMDHVFNML ESYASSLEEE
VSERTKELVE EKKKSDVLLY RMLPKTVADK LKLGQTVEPE TFEQVTIFFS DVVQFTTLAS
KCTPLQVVNL LNDLYTIFDG IIERHDVYKV ETIGDGYLCV SGLPHRNGNE HVRQIALMSL
AFLSSLEFFR VPHLPSERIN LRIGMNCGSV VAGVVGLTMP RFCLFGDAVN TASRMESNGK
PGKIHLSAEA NRLLTEVVGG FATESRGEVI IKGKGVMETF WLLGPSSGAV PARKPAKPKK
IESLQRQETL KSDEILSD
//
