ID A0A090LJG0_STRRB Unreviewed; 697 AA.
AC A0A090LJG0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN ORFNames=SRAE_2000448400 {ECO:0000313|EMBL:CEF69838.1,
GN ECO:0000313|WBParaSite:SRAE_2000448400.1,
GN ECO:0000313|WormBase:SRAE_2000448400};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF69838.1};
RN [1] {ECO:0000313|EMBL:CEF69838.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000448400.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF69838.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000448400.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) 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|ARBA:ARBA00001436};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN609529; CEF69838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090LJG0; -.
DR STRING; 34506.A0A090LJG0; -.
DR EnsemblMetazoa; SRAE_2000448400.1; SRAE_2000448400.1; WBGene00264716.
DR WBParaSite; SRAE_2000448400.1; SRAE_2000448400.1; WBGene00264716.
DR WormBase; SRAE_2000448400; SRP08608; WBGene00264716; -.
DR eggNOG; KOG4171; Eukaryota.
DR OMA; EERHMHI; -.
DR OrthoDB; 2898719at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF13; SOLUBLE GUANYLATE CYCLASE GCY-35-RELATED; 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|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682}.
FT DOMAIN 444..582
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 385..412
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 697 AA; 79480 MW; 42644918131ACEA0 CRC64;
MIKINYSKIN GLLRVTGPEV MFGWIHESFR QLVYRKYGRD VWLKILEIIK FEEGSECEIS
HYYKDEDTMK IVNAMANVIG IPIEEVWEAY GGFLIQFTME TGWDELLKAL SDNLEGFLDS
LDSLHYFIDH VVYRTKLKGP SFRCEPAKNG SLILHYYSKR SGLYPIVKGV VREVARRIFN
TEVIMKVQER KQEHLDTYIT EHVIFSITMV ENENSGNNIK SLSEKSNKQK EIVIPKSGYN
LTVKDFVNAF PHHLCFDKNL ILQHVGSYLI QNLSNLKIGF TTLTDIVDLV HPELPLTFES
LIAFKNSLFV FKIKNKGLNN QDDTTTVELK GSMVHLEDQN YILYLCSLSV TTVREMIINN
LYLSDMQKHD GTRDLIMLNQ SRMSQVELNR KLEETTKNLK RMAMDLEIET QKTDELLCQL
MPSTVAESLR QGRNIEAAEF LEATCLFTDI VTFTNICALC SPYDVVNLLN DMYLRFDRLV
TLHDVYKVET IGDAYVIVGG VPKICENHAE RVLNCSIGML MESRAVISPL AHLVNNKKML
EDNSIKIRIG IHTGPVVAGV VGAKMPKYCL FGDAVNTASK MESNGVPLRI HVSDPSKNHA
LKTNPSFEFE TRGIVNLKEK GEVLTHFLIK NGRKSVWELT GKQKGKESSI DGYTELQQAY
EDYKNSLALT IKLNNLRNGN ENDVKKPKNK STFCSLM
//
