ID   A0A158QBQ2_HYMDI        Unreviewed;      1090 AA.
AC   A0A158QBQ2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, 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};
GN   ORFNames=HDID_LOCUS313 {ECO:0000313|EMBL:VDL14661.1};
OS   Hymenolepis diminuta (Rat tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX   NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000031201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HDID_0000031201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL14661.1, ECO:0000313|Proteomes:UP000274504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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|RuleBase:RU003431};
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   EMBL; UYSG01000037; VDL14661.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158QBQ2; -.
DR   STRING; 6216.A0A158QBQ2; -.
DR   WBParaSite; HDID_0000031201-mRNA-1; HDID_0000031201-mRNA-1; HDID_0000031201.
DR   Proteomes; UP000046397; Unplaced.
DR   Proteomes; UP000274504; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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   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; 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; PF00211; Guanylate_cyc; 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};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274504};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          471..744
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          819..949
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1049..1090
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1049..1063
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1090 AA;  121985 MW;  0A1F02CFC4323399 CRC64;
     MIDGCTVREQ DRGYKLLDFL SKMIDIANKS QCFTVFIGPS LGGDCLFISD WMVHTNPYIP
     MLIRPYQISY LCPTVLPTRE YVERCSVLNN SNTMLVDETI RYGEVSMGIQ QKTISATFLS
     VLRFYGWKKV LLLYEVSSLN APLYWLADII TLAFGEKSYS DSSVQIIGSR RIHSETNYYS
     LILPWENSID GSHLAILLMS SPPMAVEFLY QVQTIKKIKE GKIAIIHLDS TDSILYDVMR
     YWRLELSKRS NLGDAGQSLL LLGALPYGDG YDYQSVNLNS DTMMSLASAV ALAVKMTQHA
     LLNNSEAIPL NTDFFAPLIN NITRLPVAPN ITFTFSHLED ELTSYFDMYI FQLNTTNLYN
     KSFDVANAPF YQLFHLVSVM LAPEFSVQEL QPMKWPGGSD GPDFDVCLQS SCLEVKLRMG
     SNKLVLYPDD VTFVKSTRKC RRNSNTAVSL SQIFRSNPSC VASTVSLDSE TDAVTETPSN
     SDTETMPRSK VTAVFNGINL HIKTLELPSV TLKAKMIEHF RTLREIRHEN LNLFIGCYLD
     ADSFSVVYEE CSRGSLRSVL ATEAINLDWE FKLSLITDLI RGMSHLHKSV IAVHGYLNSE
     TCVVDNRWVL KITDYGLQKI YALYNCFPIR TPCEKLYLAP ELLRDPRAAQ AGNQPGDVFA
     AAIVMYEIFA RSPGPFGVDA DDPEAVEAML NRLLYDDQQE AGVPKYRPSF EEVDIPNAFK
     KLVQNSWSEN PKLRPTFSEL ETQLNQLSKG KKANIVDHML KVMETYSANL ESQVNQRTAE
     LQIEKQKTEM LIAKMLPPSV AQALISGSPV DPEAFEEVTI SFSDIIGFTT ISAKSTPLQI
     VALLNELYTT FDDMIQTFDV YKVETIGDAY MVASGLPIRN GNRHAGEIAT MALELISISG
     SFEIPHMPGV PLYLRLGINS GPCVAGVIGL TMPRYCLFGD TVNTASRMES TSTAFRIHVS
     PQTKAILDGL GGYHLEHRGK VLLKGKGEVD SYWLVGKDGF DKKLPDPPTD DPLEYLNEMI
     NKISPISEAN AAAQAHASKN TSEILESINR NLKRSEGSKN RNLRNKEKRH RQRKSKSPAA
     PDSMENPEED
//