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Database: UniProt
Entry: A0A1B0FJD2_GLOMM
LinkDB: A0A1B0FJD2_GLOMM
Original site: A0A1B0FJD2_GLOMM 
ID   A0A1B0FJD2_GLOMM        Unreviewed;       642 AA.
AC   A0A1B0FJD2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Guanylate cyclase soluble subunit beta-1 {ECO:0000256|ARBA:ARBA00039698};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
DE   AltName: Full=Guanylate cyclase soluble subunit beta-3 {ECO:0000256|ARBA:ARBA00041698};
DE   AltName: Full=Soluble guanylate cyclase small subunit {ECO:0000256|ARBA:ARBA00043208};
OS   Glossina morsitans morsitans (Savannah tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=37546 {ECO:0000313|EnsemblMetazoa:GMOY003931-PA, ECO:0000313|Proteomes:UP000092444};
RN   [1] {ECO:0000313|Proteomes:UP000092444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RA   Lawson D.;
RT   "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT   Trypanosomiasis.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RG   International Glossina Genome Initiative W.H.O.;
RA   Lawson D.;
RT   "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT   Trypanosomiasis.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:GMOY003931-PA}
RP   IDENTIFICATION.
RC   STRAIN=Yale {ECO:0000313|EnsemblMetazoa:GMOY003931-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- FUNCTION: Mediates responses to nitric oxide (NO) by catalyzing the
CC       biosynthesis of the signaling molecule cGMP.
CC       {ECO:0000256|ARBA:ARBA00037442}.
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}.
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DR   EMBL; CCAG010015277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A1B0FJD2; -.
DR   STRING; 37546.A0A1B0FJD2; -.
DR   EnsemblMetazoa; GMOY003931-RA; GMOY003931-PA; GMOY003931.
DR   VEuPathDB; VectorBase:GMOY003931; -.
DR   PhylomeDB; A0A1B0FJD2; -.
DR   Proteomes; UP000092444; 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:0003676; F:nucleic acid 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   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR45655:SF2; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-1; 1.
DR   PANTHER; PTHR45655; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 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.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
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}.
FT   DOMAIN          493..626
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          598..642
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          166..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  72719 MW;  B0AC0F41BF6A15A6 CRC64;
     MVNMDGQFLV RQIYDDEITY NLIGAAVEIL NIPADDILEI FGKTFFEFCQ DSGYDKILQV
     LGATPRDFLQ NLDALHDHLG TLYPGMRAPS FRCTEKDGSL LLHYYSERPG LEHIVIGIVK
     AVASKLHGVE VEIDIIKRKG DPVEEHEKDD VFSQQLQQQQ HVTSNTFAGE ENNNHNRNLN
     NNNEDTVENF SNTDGVNKNE EQCVFTKPKS SSISSTTATK ADSFDADEDK EQKCLRLLKN
     KSDDIERYDH VQFLIREITS DAKADSKETA TKDEASKEPP DEIDFLCEAP LISPASFCKI
     FPFHLMFDRQ MKIVQAGKSV SRVIPRVADE NCSLLEVLEA IRPHLQLTFE NVLAHINTIY
     VLQTRQGAMG KHERYLRLKG QMMYLPETER ILFQCYPSVM NLDDLAKKGL YISDVPLHDA
     TRDLVLLSEK FEAEYKLTKN LEMLTDKLQQ TFRDLESEKQ KTDRLLYSVL PKSVANELRH
     QRPVAPKRYD SVTLMFSGIV GFGQYCAENT DPEGAMKIVK MLNELYTVFD ALTDSKRNPN
     IYKVETVGDK YMAVSGLPDH CEDHAKCIAR LALDMMEMAK NVKMGPNPMQ ITIGIHSGEV
     VTGVIGNRVP RYCLFGNTVN LTSRTETTGI PGRINVSEVT YK
//
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