ID A0A0N5APX3_9BILA Unreviewed; 684 AA.
AC A0A0N5APX3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
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_0000671601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000671601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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; A0A0N5APX3; -.
DR STRING; 451379.A0A0N5APX3; -.
DR WBParaSite; SMUV_0000671601-mRNA-1; SMUV_0000671601-mRNA-1; SMUV_0000671601.
DR Proteomes; UP000046393; 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; cd12087; TM_EGFR-like; 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; 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:SF493; RECEPTOR-TYPE GUANYLATE CYCLASE GCY-22; 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}; 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, 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 84..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 178..443
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 516..646
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 457..484
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 684 AA; 77557 MW; 27EE7B7DB12C45C4 CRC64;
MDFVGYQYTA AAVTVAARRL HEENYLTDYN FTYIWYFDEC DQSASVGYAT KLIFDDDVDV
IIGPTCAESA KIVGLLGRFY NFPVIIWVVL IYLVKINFFH LQMWYPKDSM KKAWAHWGGQ
KPLVRPVCGF DGLSCPATTT VARYIIIAGA MLIIIGIVIV ALIVFIIIRY MLYIAITYCV
EHSLSSSSSL TSCPQQQKLP KAVEDCEYYI HNGKPVLVVK HTVRPKITRN DADVLRFMRE
QYHDNLNAFL GLCIDGTEYL SVWRHCSRGS LQRKAVKIDS FFTMSIMRDI CAGICFIHNS
ILEYHGRLTS ACCFLNERWQ VKISEYGPQF VNNLEQRPKR TLLWTAPEHL RSGDSKGSKK
GDIYSFAIIS SEIITAEPAF NISPDQEDDV LEGGRGYRPE LVADGSRLYS LNPTILQLIK
QCWDENPESR PNAKALRKVK PEINFDKVFS TLMDHMFQLL EENALNLENE VKQRTRELNE
ERERSDQLLY RMLPKQVAEK LKCGQTVVPE SYEAATIFFS DVVKFTDLAR KCSPVQVIEL
LNNLYVMLDS IIEQYDVSKV ETVCDGYLCA SGLPHRNGDE HASKVADMAF SFLSSVKSFK
ISHLPGVQIQ ICIGIHTGAV VAGIIGQTMP HYCLFGDTVN TASRMESNSE ANRIHISSET
NRYLTEIIGG YRTICRGEIQ IKVS
//
