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Database: UniProt
Entry: A0A0V0TD28_9BILA
LinkDB: A0A0V0TD28_9BILA
Original site: A0A0V0TD28_9BILA 
ID   A0A0V0TD28_9BILA        Unreviewed;      1175 AA.
AC   A0A0V0TD28;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
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:KRX36907.1};
GN   ORFNames=T05_6285 {ECO:0000313|EMBL:KRX36907.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX36907.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX36907.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX36907.1};
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:KRX36907.1}.
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DR   EMBL; JYDJ01000337; KRX36907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0TD28; -.
DR   STRING; 144512.A0A0V0TD28; -.
DR   Proteomes; UP000055048; 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:KRX36907.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        558..580
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          624..923
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          991..1121
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   1175 AA;  133457 MW;  A260479FF08A4CFB CRC64;
     MRGSVKWLLL LLLLLLLSLL LLLLLLLLLW LLLLLLLVLF SESLYKRRAL DATPRATSAS
     GGSMKADEGV GPVALLVRVV LCWGLLICDC SRAAPAQHRI QMMVAMPYEL GPPWQNPFLL
     SRSVAEPVIQ LAIDDVSRKG FLNNIAIDLH FRNTNCSDTL GPYYAVEAYC AKQLDVVLGF
     ASAYALAPVA RLSGFWSQGV PVITTIAQVD SLDDRSVYKL LTRMNGSYRE LGSTIIHLLQ
     LLNYETVAFL FHSNLRRPAF GKSECFFQMV AINNQLLKAS GWRQPPVIDF DEFFDSNYED
     LLKRASMSAN VILMCASVDT IENLMHAAAR LGMTESGKYI FFSIHIHSDM QDDFSWQLSN
     VSQAEREQDL KTFASLKIVT LRRPPQSLYR RFEEDVKALA QKKFNYTQIT GKPYKVCKLL
     YFELFIISTY GNKAQVTKFT SAFYDAIMLY AIALNETLSL GFSPRNGLEV TRRMWNRSFA
     GIGGNVTISK DGDRFSDYSV LDLNPQTGTF EEVAYYAGSQ DKLYVVGQWY WAGGSPPPDR
     PICGFDNSKC PSKNLSPWAV ILIVFSTLTV IFGVIALFVF RRYKLEAELR TMSWRIFWDE
     LSGQKKQNKC RKRNDSRAFH WLYEQRNSLI CEENYDDSFT SLTDSLCTVE GLELEKEKNA
     FTKIANYRGQ IVAVKMLNIQ RNRIELSRKL LIELKKMKDL SHEHVTRFVG ACIDSPHYCI
     VTEYCPKGSL QDILENAGIK LDKMMIYSLM HDIIKGMVFI HSTDIRSHGK LKSTNCVVDS
     RFVLKITDFG LNHIHELETV KEDFLSNSFW RAKLWTAPEL LRLDCPPMGG TQKGDVYSFA
     IILHEMLFRR GVFYTSDENS FARDIVENVR MGMQPPFRPT VLETSFDGVI ISLMVRCWSE
     NPDDRPDFRM IRKQVISLTR EFETSNIVDN LLRRMEQYAN NLESLVQERT ADYLQEKQKA
     ENLLYQLLPK SVASQLIKGE PVKAEAFDCV TIYFSDIVGF TSLCADSTPM EVVNLLNDLY
     TCFDSIIENY DVYKVETIGD AYMVVSGLPR KNGVAHAFEI ARMALALLSA VRCFTIVHRP
     KEQLKLRIGI HSGPVCAGVV GLKMPRYCLF GDTVNTASRM ESNGLPLKIH VSSATKTLLD
     SFNCFQLEYR GEVVMKGKGA QVTYWLLEPT ENHVT
//
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