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Database: UniProt
Entry: A0A183A534_9TREM
LinkDB: A0A183A534_9TREM
Original site: A0A183A534_9TREM 
ID   A0A183A534_9TREM        Unreviewed;       689 AA.
AC   A0A183A534;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN   ORFNames=ECPE_LOCUS2069 {ECO:0000313|EMBL:VDP65326.1};
OS   Echinostoma caproni.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC   Echinostoma.
OX   NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0000206901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ECPE_0000206901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP65326.1, ECO:0000313|Proteomes:UP000272942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Egypt {ECO:0000313|EMBL:VDP65326.1,
RC   ECO:0000313|Proteomes:UP000272942};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   EMBL; UZAN01039400; VDP65326.1; -; Genomic_DNA.
DR   WBParaSite; ECPE_0000206901-mRNA-1; ECPE_0000206901-mRNA-1; ECPE_0000206901.
DR   Proteomes; UP000050740; Unplaced.
DR   Proteomes; UP000272942; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 6.10.250.780; -; 1.
DR   Gene3D; 3.90.1520.10; H-NOX domain; 1.
DR   Gene3D; 3.30.450.260; Haem NO binding associated domain; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR038158; H-NOX_domain_sf.
DR   InterPro; IPR011644; Heme_NO-bd.
DR   InterPro; IPR011645; HNOB_dom_associated.
DR   InterPro; IPR042463; HNOB_dom_associated_sf.
DR   InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR45655; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR   PANTHER; PTHR45655:SF10; SOLUBLE GUANYLATE CYCLASE 88E; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07700; HNOB; 1.
DR   Pfam; PF07701; HNOBA; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000272942}.
FT   DOMAIN          411..541
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          270..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          347..381
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   689 AA;  78076 MW;  90E2C4C8520DC63C CRC64;
     MYGLFLEGFK AYILSTFSEA VWRQVIVEAQ CETFDFEVRR DYDEDLLGRL FKATSKVTNL
     SDYKIKYGMG KSFKDFFGFK EYQAVLRVLG RELRDFLNGL DNLHEFIRAT YPQIRPPSFF
     CVNESRSGIT LKYQSKRDGM VPFFVGWMEN VSQMYFNIQM KITIIHSEKK ETSNITILRL
     HFVNEAFPEV IEELSVPAHL FFEAFPFNFV FNRGMILINV GSSMIHALPD IVRRNLNEVF
     VLERPHIELK WDDIMLHTNN IFQMVSNRAK PLDDDEENPT NDSNNPRKGC LRMRGQMKYM
     VEWDAIVFLG TPIMEDVDAM WEVGLFLNDL SMHDSSRDMV LAGEQQSAEL KMALEQESEK
     GKRLEESLRR LDEEVRRTDE LLYRMIPKAV AERLRSGASA IDTCETFENM TLLLSDVVGF
     TTICSGLAPL EVVDLLNRLY SCFDGLTEKH KVYKVETIGD AYMIASGVPV RTKYHAPFIA
     EMALDMVSGV QEVKDESKDP PESLRIRVGL HSGTVVAGVV GVKMPRYCLF GNTVTTAELM
     EATSSPQRVQ ISKATFEKLS EYGVYDMTEK GTVQTKDGNT IYTYWLNGRP NEADCPKTAK
     LCAHLAKERE LLADSNMAAN HSQTGEGWES VSASRGSSAR ALASKRSSLA AGGRASMGRL
     SMIMDDKFAN KRKSLARVAQ MSRKISGAV
//
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