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Database: UniProt
Entry: F2TX50_SALR5
LinkDB: F2TX50_SALR5
Original site: F2TX50_SALR5 
ID   F2TX50_SALR5            Unreviewed;       873 AA.
AC   F2TX50;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN   ORFNames=PTSG_00667 {ECO:0000313|EMBL:EGD75959.1};
OS   Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX   NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN   [1] {ECO:0000313|Proteomes:UP000007799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Salpingoeca rosetta.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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; GL832956; EGD75959.1; -; Genomic_DNA.
DR   RefSeq; XP_004998135.1; XM_004998078.1.
DR   AlphaFoldDB; F2TX50; -.
DR   STRING; 946362.F2TX50; -.
DR   EnsemblProtists; EGD75959; EGD75959; PTSG_00667.
DR   GeneID; 16078731; -.
DR   KEGG; sre:PTSG_00667; -.
DR   eggNOG; KOG4171; Eukaryota.
DR   InParanoid; F2TX50; -.
DR   OrthoDB; 2898719at2759; -.
DR   Proteomes; UP000007799; 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: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|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Lyase {ECO:0000256|RuleBase:RU000405};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007799}.
FT   DOMAIN          506..634
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          286..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          707..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          451..481
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        305..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..752
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   873 AA;  95131 MW;  C02201FDB8B68EBD CRC64;
     MYGFVEEALN AYVLSLPDGK EKLDLIRREA NVTHTAVNFH HAYSDEHTLN MVVSAAKVLG
     IDAEECLSQI GFFQVGVLVE KGYLPLVQSL GDNFYELLLH LDSMHLNIVN AYPSMKGPSF
     KPHRQKDGSL LLHYYSSRMG IYPYAIALLK DIAKKVYSLD IELKHVKKKG QDHDHDVFHI
     FMGPEGYGEK EYFDSEKAHA ISGQLTFGPS MVDSVFPWHI SFDRTFTITS VGPRLKERLP
     AGGVGQPFFR LMRVVRPDIR GLGFDSLLES FDHSPLLVQA CAVPPGSDAS TAPPSGCPFA
     AAAARTTGSA TTPKPNQTRR RRGNSVSQST SAGSSSTSSS SSNSDTAEAN KNKSAQGSGV
     NDDTALPGVF PDDGGKDPIS GITILKDGLF LKGELVFSPE HDAMLFLCIP TISSLEEMEK
     LDICLEDIPI HSNGRELVIS TAHQSATVLM AQTLQNTTAS LDKAMEDLDK EKERVDGLLH
     SILPTQVAQA LKAGEIPEPE HYEAVSILFS DIVSFTKISS SVPVREVMDM LNELFSKFDA
     LCTKHGVYKV ETIGDAYMVA SGLPKADPRH ADVIAAFAVE MVAAAETVIS PMDGEPINIR
     VGMHSGRIMA GVVGRERPRY CLFGDTVNVA SRMESTGVGG AVQVSYAFIK ALPNKDDWNI
     LKRGTVPVKG KGEMKTFFVL GRAGSSMQLA PPDASDYESE AQTPRIAFGH AGSDPRSPAS
     YGFMPQPQHQ QQPVPASPAP QARQLPPPPK PDTMFEVVVH GSDIDIKLPY VPSSMTLGEL
     MLEIHPEGTR DNADSDYRFY LDDMHEGMLL PRLTVEQLYA SLVTNKVIES GSRQLSLYAE
     TRTCLKHPFA TPRIQTRAPS IPNIAVAPSN EFI
//
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