ID A0A1I8GF39_9PLAT Unreviewed; 1071 AA.
AC A0A1I8GF39;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0001745-snap-gene-0.5-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0001745-snap-gene-0.5-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-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 -!- 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}.
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DR AlphaFoldDB; A0A1I8GF39; -.
DR WBParaSite; maker-uti_cns_0001745-snap-gene-0.5-mRNA-1; maker-uti_cns_0001745-snap-gene-0.5-mRNA-1; maker-uti_cns_0001745-snap-gene-0.5.
DR Proteomes; UP000095280; Unplaced.
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 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; 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; 2.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 429..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 560..826
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 899..1029
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 482..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 836..863
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 482..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 122538 MW; C8BA86A30BA3D9F0 CRC64;
MSLEQVLPVV DIAIETVTTL DLLHGHSVSL IANDSKCDYS VAPVLGVLLL QQKIDLMLGP
YCSFALAAVA RYNRMPHYRR PILTTGGVAS ALRDKAEYFN LIRVGPSFDG VEKMLYLVFQ
RFNWKPRDVQ TILFIELPDE DVKEKRTRDE IGVTQSRILC HGIEKHFVQE KYIVRRLQYE
MHNAQFKSEI FRVMRDEIRL VVLCADPDTV REIMIKAQEL GFINGEYVFF NIDLFSSEKL
TLQPWRREND THERNEKAAR AYRALMTITL RKPSSPEYRN FSQQVKSIAK SKYNFTYPEE
EVNSFVGAFH DAVILYALAI NDTVYEHGFE GIANGSLITE KMKNRTFEGI TGTVSINANG
DRDADYSLLD MDKNTRNFVV VAHYYGNRQK YELVPGKEID WYNEDNLPPR DIPKCGFDYS
MCKQDLSKVA TYAVVVLLVL ICVLSVVIAV IYRKLRLESE LHAMNWRIPW SELEPMERIA
AGRRTSESGK DLQQQDEEPE QSQPHRHHQH RGQSHQKRTD SVRILFGNSH NEGSTSKKNR
DEKKHQNDQH SGAAAEEMSL VSVDTIAGVP LSQIPVTQLF TKTAYYKGAL VALKPLSLRN
KRIEVTNKLL MEVKRVKDLT SDNVIRFIGA CLDAPNECLV SEYCPKGSLQ DVLENDNLNL
DWMFKFSLML DICRGMIYLH HNFGSHGNLK SSNCLVDSRF SLKIADFGLQ SLRGTKDYKD
KEDAEYSSYR RTKEGDVYSF AIICQEIIYR RGVFFISDYD FPEPQEIVEK VKEISNQMYR
PTLDAETNDP DQERSEALIN TVRNCWQEDP AARPSFNSIK SRISRFNKDA ESGNILDNLL
KRMEQYSNNL ESLVAKRTDL YLEEKKKAEN LLYCMLPKSV ATTLLRGESV TAEWFDSVTI
YFSDICGFTA LSSESTPLEV VTLLNDLYTL FDRIIEQYDC YKVETIGDAY MVVSGLPMRN
GILHAREISR MALSFLQNIY SFKIRHKPDV QLKLRIGIHS GPVCAGVVGL KMPRYCLFGD
TVNTASRMES NGLPLKIHIS SFTHEILEEI GGFVTTARGE VEMKMGHNAL F
//
