ID A0A0V0X0V4_9BILA Unreviewed; 1191 AA.
AC A0A0V0X0V4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, 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};
GN Name=Npr1 {ECO:0000313|EMBL:KRX81549.1};
GN ORFNames=T06_1263 {ECO:0000313|EMBL:KRX81549.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX81549.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX81549.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX81549.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX81549.1}.
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DR EMBL; JYDK01000030; KRX81549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0X0V4; -.
DR STRING; 92179.A0A0V0X0V4; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
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; cd06373; PBP1_NPR-like; 1.
DR CDD; cd14042; PK_GC-A_B; 1.
DR Gene3D; 3.40.50.2300; -; 3.
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:SF494; GUANYLATE CYCLASE; 1.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 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};
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, ECO:0000313|EMBL:KRX81549.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 559..581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 625..939
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1007..1137
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 1191 AA; 135338 MW; B9CBFF6F26F11800 CRC64;
MVSENCNQFY ANYGTSRPAG RRGVENLNFP RTNGGREYRF DSESLYKQRA LDATPRATSA
SGGSMKADEG VGPVALLVRV VLCWGLLICD CSRAAPAQHR IQMMVAMPYE LGPPWQNPFL
LSRSVAEPVI QLAIDDVSRK GFLNNIAIDL HFRNTNCSDT LGPYYAVEAY CAKQLDVVLG
FASAYALAPV ARLSGFWSQG VPVITTIAQV DSLDDRSVYK LLTRMNGSYR ELGSTIIHLL
QLLNYETVAF LFHSNLRRPA FGKSECFFQM VAINNQLLKA SGWRQPPVID FDEFFDSNYE
DLLKRASMSA NVILMCASVD TIENLMHAAA RLGMTESGKY IFFSIHIHSD MQDDFSWQLS
NVSQAEREQD LKTFASLKIV TLRRPPQSLY RRFEEDVKAL AQKKFNYTQI TGKPYKVCKL
LYFELCIIST YGNKAQVTKF TSAFYDAIML YAIALNETLS LGFSPRNGLE VTRRMWNRSF
AGIGGNVTIS KDGDRFSDYS VLDLNPQTGT FEEVAYYAGS QDKLYVVGQW YWAGGSPPPD
RPICGFDNSK CPSKNLSPWA VILIVFSTLT VIFGVIALFV FRRYKLEAEL RTMSWRIFWD
ELSGQKKQNK CRKRNDSRAF HWLYEQRNSL ICEENYDDSF TSLTDSLCTV EGLELEKEKN
AFTKIANYRG QIVAVKMLNI QRNRIELSRK LLIELKKHVD NFRLFIFCFA FQMKDLSHEH
VTRFVGACID SPHYCIVTEY CPKGSLQDIL ENAGIKLDKM MIYSLMHDII KGMVFIHSTD
IRSHGKLKST NCVVDSRFVL KITDFGLNHI HELETVKEDF LSNSFWRAKL WTAPELLRLD
CPPMGGTQKG DVYSFAVILH EMLFRRGVFY TSDENSFARD IVENVRMGMQ PPFRPTVLET
SFDGVIISLM VRCWSENPDD RPDFRMIRKQ VISLTREFET SNIVDNLLRR MEQYANNLES
LVQERTADYL QEKQKAENLL YQLLPKSVAS QLIKGEPVKA EAFDCVTIYF SDIVGFTSLC
ADSTPMEVVN LLNDLYTCFD SIIENYDVYK VETIGDAYMV VSGLPRKNGV AHAFEIARMA
LALLSAVRCF TIVHRPKEQL KLRIGIHSGP VCAGVVGLKM PRYCLFGDTV NTASRMESNG
LPLKIHVSSA TKTLLDSFNC FQLEYRGEVV MKGKGAQVTY WLLEPTENHV T
//
