ID   A0A0N5AUR7_9BILA        Unreviewed;      1000 AA.
AC   A0A0N5AUR7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
DT   27-MAR-2024, entry version 42.
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   Syphacia muris.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX   NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000860901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0000860901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-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: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   AlphaFoldDB; A0A0N5AUR7; -.
DR   STRING; 451379.A0A0N5AUR7; -.
DR   WBParaSite; SMUV_0000860901-mRNA-1; SMUV_0000860901-mRNA-1; SMUV_0000860901.
DR   Proteomes; UP000046393; Unplaced.
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   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; IPR001170; ANPR/GUC.
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:SF493; RECEPTOR-TYPE GUANYLATE CYCLASE GCY-22; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00255; NATPEPTIDER.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          451..740
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          811..941
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   COILED          752..779
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1000 AA;  112956 MW;  499A705774F1A269 CRC64;
     MGLSIMSEEI VQGIRFETTA PAIDIAIEEM HEQGLLTDVN FTVFYGGKYC TLLDLTTEAL
     RLVTQQNISI LFGPVSTAAA AVVSPILLHY DVPNILWGPA PKSEFGDKGA FPTTTFLIPT
     AYSFGMGLLA VCKEFQWNDI AFVYSTSPKD IVCIHIANEF ELAMTSHEHR VTVNLKMMLN
     LNNDEYMNKV LSRIRDSVRV VFACLQNSED MRKFMSVIHE HGMTNNEYVY ISPNTYNYSG
     GKWNDGLDDV VEIAEKYFFF LGNIQNVNTN EIKVFNEKVL ERSKLPPFNC QNCTSVSNYA
     YYLHDAVKFY LLRLNDILSD GSMDIDTEKL MNCSKTTFEG LTGTVEITEN CDRIQQLYLL
     AVNPSRKLES YMTIKSGTTF YVESQTEEQA KAVWEYRGGE RPLNKPICGF KNDECFHSEL
     VWAPVKKRER AALMKLWQVS TQNLQRPKKL TESHRSLQSN ALSESSVITD VDTFASGYEV
     YMYEGEKVFV KAHTKRIGEL TKAQNLLMIG MKQLVSENLN PFVGLCLDNP LNVLSVWKYN
     DRGSLKDVFA LKVPTNDVFF RYCLMKDLIE GIVAIHQSSF LKYHGRLTSE CCLVSDRWQI
     RISDYGLEHM NFQEEQTNLG YKSLKVNLKI EVAELLWTAP ELLRSKTTPT KASDIYSFGI
     ICSEILTQQS AYNSLADEGD AEEIIYKIKR GRTPLTRPSL ENNLIDCGQI FVRIISDCWS
     EDPDDRPSAG TVKALLHSVK LSNKRNLMDH MLAVLEEYAA ELEDVVDQKN EEALQEKKKV
     DLLLYKILPK QIAEKLKFGE TVEPEYYTEV TIFYSDIVSF TVLASKCTPM QVITVLNDLY
     TMFDSIIEEH DVYKVETIGD AYLCASGVPR RNEHNHGREI ACMALAVVAQ IKEFKVAHLN
     DEVVNVRIGI HTGPVTAGVV GLTMPRYCLF GDSVTIATKM ESSGKPGKIQ LSPKANDLLT
     KVLTGFKTEP RGEVLIQGRG VMETFWLLEA DSRTTATTSG
//