ID A0A099ZEG9_TINGU Unreviewed; 588 AA.
AC A0A099ZEG9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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};
DE Flags: Fragment;
GN ORFNames=N309_12653 {ECO:0000313|EMBL:KGL79245.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL79245.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL79245.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL79245.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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}.
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DR EMBL; KL891846; KGL79245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099ZEG9; -.
DR STRING; 94827.A0A099ZEG9; -.
DR Proteomes; UP000053641; 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: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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053641}.
FT DOMAIN 397..530
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL79245.1"
FT NON_TER 588
FT /evidence="ECO:0000313|EMBL:KGL79245.1"
SQ SEQUENCE 588 AA; 67113 MW; ADE1190AE81F4158 CRC64;
FRKEAQLDEE GQFLVRIIYD DSKTYDLVAA ASKVLNLNAG EILQMFGKMF FVFCQESGYD
TILRVLGSNV REFLQNLDAL HDHLATIYPG MRAPSFRCTD AEKGKGLILH YYSEREGLQD
IVIGIIKTVA QQIHGTEIDM KVIQQRNEEC DHIQFLIEEK ESKEEDYYED LDRFEENGTQ
ESRISPYTFC KAFPFHIIFD RDLVVTQCGN AIYRVLPQLQ PGNCSLLSVF SLVRPHIDIS
FHGILSHINT VFVLRTKEGL LDVEKLECED ELTGTEISCL RLKGQMIYLP EADSILFLCS
PSVMNLDDLT RRGLYLSDIP LHDATRDLVL LGEQFREEYK LTQELEILTD RLQHTLRALE
DEKKKTDTLL YSVLPPSVAN ELRHKRPVPA KRYDNVTILF SGIVGFNTFC SKHASGEGAM
KIVNLLNDLY TRFDILTDSR RNPFVYKVET VGDKYMTVSG LPEPCIHHAR SICHLALDMM
EIAGQVQVDG EPVQITIGIH TGEVVTGVIG QRMPRYCLFG NTVNLTSRTE TTGEKGKINV
SEFTYRCLMT PENSDPQFHL EYRGPVSMKG KKEPMQVWFL SRKSTETE
//
