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Database: UniProt
Entry: A0A093QE92_9PASS
LinkDB: A0A093QE92_9PASS
Original site: A0A093QE92_9PASS 
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
//
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