ID A0A093QE92_9PASS Unreviewed; 1068 AA.
AC A0A093QE92;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Guanylate cyclase {ECO:0000256|RuleBase:RU003431};
DE EC=4.6.1.2 {ECO:0000256|RuleBase:RU003431};
GN ORFNames=N305_13950 {ECO:0000313|EMBL:KFW87268.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW87268.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW87268.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW87268.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:ARBA00036920};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13666;
CC Evidence={ECO:0000256|ARBA:ARBA00036920};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR EMBL; KL672898; KFW87268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093QE92; -.
DR STRING; 328815.ENSMVIP00005000839; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR CDD; cd14044; PK_GC-C; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR042822; GC-C_PK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR PANTHER; PTHR11920:SF347; HEAT-STABLE ENTEROTOXIN RECEPTOR; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293,
KW ECO:0000256|RuleBase:RU003431};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Receptor {ECO:0000313|EMBL:KFW87268.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053258};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1068
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001887151"
FT TRANSMEM 426..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 468..744
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 819..949
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 1068 AA; 122494 MW; 3FD2B8140D5209CF CRC64;
MKQRMLILAI WPLFSSLQLL QQVGSNRCNN KNYVINVMLM NYSDFPSSPE SLKCAVNGAL
KWVQNEFQTT GENVTVDAIF HTFASSLYVS QGCRTSTCEG VELIKTIYDS GTLGCAVIGP
ACTYATYQMV SLDTVLSLPL ISVGSFGLSC DYKENLTRLL TPARKVNGFF NYFWRDSQLP
FKTTTWESVY IYKRTETSEA CFWYMNALDA GITEFSEKLK FKDILRTPEQ LKRTVKNPNR
KSNVIIMCGS PEDVRTDLET EKVDNDIVII LIDLFNNTYF RENSSADYMQ NVLVLTLSPA
NYSNNTVIRD YTEYDFLVGY SNAILLFGHT LKKFIVSQSP VSPLSLINEF RDTTFEGLLG
PVTLDEFGDI DTNLTLLYTS PTAKHFKPLL YFNTHNNETN KATNSPDFIW KNHKLPSDTP
GTGPHVLTIA VFTLTGIVIL VLIISLVILR KYRRDNERRW KKWSHIPPEE ILPLETSETS
HVSLKIDEDK RRDTTQRLRQ GKYDKKVVIL KDLKNSDGNF SEKQKMELNK LLQVDYYNLT
KFYGTVKIDT MIFGVIEYCE RGSLRDVLND KISYPDVTFM DWEFKISVMY DIAKGMSYLH
SSKTEVHGRL KSTNCVVDNR MVVKITDFGC NSILPPRKDL WTAPEHLRHA DVSQKGDVYS
YGIIAQEIIL RRETFYTGHC RDNREKLYRV ESGKGVKPFR PDLTLETVGE RQVELYTLVK
SCWEEDPEKR PDFKKIESTL AKIFSNLHGQ TNESYMDTLI RRLQLYSRNL EHLVEERTEL
YKAERDRADR LNFMLLPRPV VKSLKETGLV EPELFEEVTI YFSDIVGFTT LCKYSTPMEV
VDMLNDIYKN FDHILDHHDV YKVETIGDAY MVASGLPKRN GNRHAVDISM MALDILSFMG
SFELRHLPGL PVWIRIGIHS GPCAAGVVGI KMPRYCLFGD TVNTASRMES TGLPLRIHVS
GSTINILKRT DCQFQYEVRG ETYLKGRGTE ITYWLTGTED KKYNLPTPPS VENQQRLQDD
LAEMITNSLQ KRENEGSKAH ELSRVASYRS GTLEYLQLVS TENFTTYV
//