ID A0A0Q3T2L7_AMAAE Unreviewed; 810 AA.
AC A0A0Q3T2L7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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};
GN ORFNames=AAES_152905 {ECO:0000313|EMBL:KQK74822.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK74822.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK74822.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK74822.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQK74822.1}.
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DR EMBL; LMAW01002999; KQK74822.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3T2L7; -.
DR Proteomes; UP000051836; 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 InterPro; IPR049258; ODAD1_CC.
DR PANTHER; PTHR45655:SF2; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-1; 1.
DR PANTHER; PTHR45655; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR Pfam; PF21773; DUF6872; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07700; HNOB; 1.
DR Pfam; PF07701; HNOBA; 2.
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 Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836}.
FT DOMAIN 381..514
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 577..629
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 749..783
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 810 AA; 93792 MW; 2E95FB81844478AC CRC64;
MYGFVNHALE LLVIRNYGPA VWEDIKKEAQ LDEEGQFLVR IIYDDSKTYD LVAAASKVLN
LNAGEILQMF GKMFFVFCQE SGYDTILRVL GSNVREFLQN LDALHDHLAT IYPGMRAPSF
RCTDAXKGKG LILHYYSERE GLQDIVIGII KTVAQQIHGT EIDMKVIQQR NEECDHIQFL
IEEKESKEED YYEDLDRFEE NGTQESRISP YTFCKAFPFH IIFDRDLVVT QCGNAIYRVL
PQLTPRSIYY ESGTLNLEFY NIDFHFTVTN FKNTYKSSST EINCFSVMNL DDLTRRGLYL
SDIPLHDATR DLVLLGEQFR EEYKLTQELE ILTDRLQHTL RALEDEKKKT DTLLYSVLPP
SVANELRHKR PVPAKRYDNV TILFSGIVGF NAFCSKHASG EGAMKIVNLL NDLYTRFDIL
TDSRRNPFVY KVETVGDKYM TVSGLPEPCI HHARSICHLA LDMMEITGQV QVDGEPVQIT
IGIHTGEVVT GVIGQRMPRY CLFGNTVNLT SRTETTGEKG KINVSEYTYR CLMAPENSDP
QFHLEYRGPV SMKGKKEPMQ VWFLSRKSTE TEASVHFNTI VAKNNKLREE IESLQIRKAV
LDNFYCKLHT KLEQQKRRMN TAVEQTTQAY EQWSEAQARI AXMSXRHRKD TAQYHIEMQE
QERIFARETK LKAFMLARFT DRSELEEQAK KERDLKAAQR AKKSQGECFE TREVAYKRLL
ELAEDGNVEQ LLNSFIKKEH KSFACLFYAS ELNDDMQKMQ RKIRELQIEV ASLSKDQKHA
EAQNSHLVKE XEHIKSQPEN VFSLRYSYSD
//
