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Database: UniProt
Entry: A0A0V0USX3_9BILA
LinkDB: A0A0V0USX3_9BILA
Original site: A0A0V0USX3_9BILA 
ID   A0A0V0USX3_9BILA        Unreviewed;      1533 AA.
AC   A0A0V0USX3;
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};
DE   Flags: Fragment;
GN   ORFNames=T09_5274 {ECO:0000313|EMBL:KRX54390.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX54390.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX54390.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX54390.1};
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: 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}.
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:KRX54390.1}.
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DR   EMBL; JYDN01000173; KRX54390.1; -; Genomic_DNA.
DR   STRING; 181606.A0A0V0USX3; -.
DR   Proteomes; UP000054681; 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; cd06370; PBP1_SAP_GC-like; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
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:SF335; GUANYLATE CYCLASE 32E; 1.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        611..635
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          656..939
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1011..1141
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1482..1502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          948..983
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1485..1502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX54390.1"
SQ   SEQUENCE   1533 AA;  172460 MW;  DF063FA98E6DE0A2 CRC64;
     LVEMLLLAVR REISIAVVIF ALVLVGLVRF GFAADVGPAR QRILIGYLAG TVINRQPPIL
     LKFQIPSAPV GLGQNNNTTS RRNVSTTLDL LRSIVGASNN TGTRMANDRR RRQGSTLFDH
     SDHRLVGGGH SNLDCNFSGH VLSAHTMSLE RIAKCLQRQG LVHLSRNLQG HIISGALKYA
     IEIVNANPDI LPGYQLDFIF ADTRGLTKQS VKATMELWQK GVIAFIGPED SCQTEAMMAA
     SQNLPMISYK CFDHAVSDKS KYSTFARTVP AETEIGRAAI SLLKHYSWRK FAIVYGHNDV
     NSHLLKTVVE LSTAEGLHIL NISRFEEPYR STNFDDRQRI SEIVSETHLK TRIYLMFGSV
     SALQQMLYAM DDLELLNNGE YVIIYLEPSY TYLNPDDAMM NYFYRATLYT VEEFHNYPFV
     NRIVDLSRSV LAIIPSPVTF TDKAWQEFWE KVNQYNAQPP FNFFNPVGNS HIGKYPVVNR
     YATYLYDAVM LYATALHEEL QAGGDPRNGS SIIGRIFNRR YQSMQGFEMQ INEQGDAEGN
     FTLLTRQRLV DSRFNLTYGL IPSAYFIEKN ETLPGLLFKR GLRVDWAGGK PPQDEPECGF
     RGEYCVDQPS YAVEIVCGAI GIVMLIMAVV SFIYYRNRKY EQELAGLIWK INPKEIQFHP
     CTGYDNLGGS RATDFSSWVV DPHGLGVYRG SLVAIKEIRY AKRTREITRA TKIEMKKMRS
     LHHDNVNRFI GIIVQPNFIC VVREYCAKGS LFDVLLNENI KLENMFIASF VDDLLKGMIY
     LHDSEIRVHG NLKSTNCCIT SRWSLQVSDF GLSELREGQI YMSQESQLMG LLWTAPELLR
     ESVDHMQPCK GTQRGDSYSF GIVLHEVFSR NGPFDVYYED SLSGEEILKN IIHTPYFRPS
     LALVECDKYI SDTMLACWDE RPECRPDFRQ IRMRLKMLFK GIMKQNIMDH MMGMMEKYQS
     HLEELVEERT EELKEEKKRT ETLLHRMLPK VVAAQLMQGK DVVPETYDSV TIYFSDIVGF
     TALSAESTPV QVVAFLNDLY TLFDRIIRQY DVYKVETIGD AYMVVSGLPI RNGNQHAGEI
     ATMALELVEA VKAFQVPHKP DVACLLRIGI HTGPCAAGVV GKTMPRYCLF GDTVNTASRM
     ESNGMPLKIH CSESTKLALD KLGGYLLDER GLIPLKGKGE MRTYWLLGKQ EAVVSSRPSE
     ANVEEPLFSS SRFVRPCSVK QRSRETSMIS IRMENARSKI RRENTILENA SVSAERTAQP
     FAAGNDLKML GKYPMKCRRR ESAKQAPNRI ADDFINRKRS NSYPENIHSL TAKGGTSAPT
     LRNTTLLTNP LYCSTQPSSS AASSGQPLTL IIDSKDSSGG IIPTLADGRP GKRNSREDRS
     TCKFPVKRHS CSGPRVPRTK LNGMSISMDE FALPEHTPWR AHGNLWQVAS NRSERADMYD
     PLPNTCNGAE SISGSYPEEC GVNCPLLEPV EYFENAKVAD RQFRKDSSSQ PSNSPMASAS
     HSDSAASLWM RFLKSSMSGG SGEINAEQQP GIA
//
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