ID A0A183QT23_9TREM Unreviewed; 536 AA.
AC A0A183QT23;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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};
OS Schistosoma rodhaini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6188 {ECO:0000313|WBParaSite:SROB_0000682201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SROB_0000682201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
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 AlphaFoldDB; A0A183QT23; -.
DR STRING; 6188.A0A183QT23; -.
DR WBParaSite; SROB_0000682201-mRNA-1; SROB_0000682201-mRNA-1; SROB_0000682201.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR11920:SF506; GUANYLATE CYCLASE; 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; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1..253
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 326..456
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 536 AA; 61366 MW; DCAE582A8986E152 CRC64;
MLFNFFSDCV PVAMKQIYVE FTDLTSDMQK QLWEVKKMKH NNLVKLIGVT FISPVLSFYT
EFCDRGSLCY VLRRDSIPLS WSLRIGFLTG LANGLAYLHN YQIVHGRLNS SNCVVSDKWT
CKITDYGLDS LIWSNNFEKH KTFLDKPENL PYIPPEYRGK YYKETLFVPA VDIYSFGTIM
WETASRSDPS QDDEFVAEPM YNHPELPTKR RFETDVKYEV TSVPPFEEYN NLMESCWSEV
TLRPNLNTII EWLTKINPRN IGVDTGTILV SKYARCLESI IEDRTQALRS EQKMADTLLN
SMLPKQVVEM LRHGENVPPE AFEQCTIYFS DIVGFTTISS SSTPFEVVEF LNKLYTQFDD
IIDRYDVYKV ETIGDAYMVA SGVPRRNGER HAIAIADMSL DLVNVSHSFV IPHKPDEPLK
IRVGLHSGPV CAGVVGLKMP RYCLFGDTVN TASRMESTGE AYKIHCSETT HAILDRLGGF
TFEKRGTITV KGKGDMQTWW ITGRTRADLA KDCCPLPLNW KKRLKKPENP NPNEDH
//
