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Database: UniProt
Entry: A0A182QJY0_9DIPT
LinkDB: A0A182QJY0_9DIPT
Original site: A0A182QJY0_9DIPT 
ID   A0A182QJY0_9DIPT        Unreviewed;       992 AA.
AC   A0A182QJY0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Guanylate cyclase {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
OS   Anopheles farauti.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF011771-PA, ECO:0000313|Proteomes:UP000075886};
RN   [1] {ECO:0000313|Proteomes:UP000075886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AFAF011771-PA}
RP   IDENTIFICATION.
RC   STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF011771-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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:ARBA00001436,
CC         ECO:0000256|RuleBase:RU003431};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {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; AXCN02000174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182QJY0; -.
DR   STRING; 69004.A0A182QJY0; -.
DR   EnsemblMetazoa; AFAF011771-RA; AFAF011771-PA; AFAF011771.
DR   VEuPathDB; VectorBase:AFAF011771; -.
DR   OrthoDB; 3683909at2759; -.
DR   Proteomes; UP000075886; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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; cd14042; PK_GC-A_B; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
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; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR001170; ANPR/GUC.
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:SF494; GUANYLATE CYCLASE; 1.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00255; NATPEPTIDER.
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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        249..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          303..586
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          662..792
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          872..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          951..992
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..889
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        899..937
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        951..966
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   992 AA;  110704 MW;  46E7A0F0FBF8468E CRC64;
     MVRRFETTDV TGVVVMCASP STIREIMLAA AELNMVNSGE YVFFNIEIFG SMTATKQPPW
     YAKNDTDERN QKAKEAFTAL LQVVAREPED EEYRQFSEEV KELTRTKHNY TYAEDEPVST
     FVTAFYDAVL LYAYALNDSI AKLGEERALR QPINGTHLAQ LMWGRSFKGI TGNVTIDSNG
     DRISNYSLLD LNPETGLFEV VANYYYGGGL QFVEGKAIHW AGDRTKAPPD RPTCGFDGSL
     CPDNSLPGYA ILSLVLGVCV VCMGIASIVG YRHYKLEAEI NSMTWKVNPN DVLSCNPSRG
     HRGSFHSMVK RGSQATIYSE DLNSLPGDRQ IYIHFGFYKG CKVAIKKINV QNLSLTRSLM
     LEFKRMKDIQ HDHLVRFYGA CLELQPDPFI LTEYCPKGSL QDILENETIK LDWMFKISLM
     HDIVKGMAFL HSTDLHSHGS LKSSNCVVDS RFVLKITDFG LHQLRRNTDD GDIESYAYWQ
     KLLWTAPELL RDPQCPPAGS QKGDVYSFGI IIQEIVSRQG PFYLGTEEKS PKEIITLVRD
     RVGPMDVPFR PKVDESSYED VNNIMVKCWA EDPADRPDFG GLKTIIRKIN KENESGNILD
     NLLQRMEQYA NNLEALVDER TQDYFEEKRK CEELLYQLLP KSVAAQLIMG KSVIAETYDQ
     VTIYFSDIVG FTSISAQSTP MQVVDLLNDL YTCFDSIVEN FDVYKVETIG DAYMVVSGLP
     VRNGNLHARE ISRMALRLLA AVYKFTIRHR PNEQLRLRIG LHSGPCVAGV VGLKMPRYCL
     FGDTVNTASR MESNGEALKI HVSHTTKTLL DTFGTFDLTE RGLVPMKGKG EMLTYWLEGE
     RTDQLQLPPP TTLPNGLKGQ QALLLGPVSV TEGQQLPTPN QQQLNGSVHS PPPAGILVNH
     HHNNNNNNNN SPCSLNNNNN NNNNNSPNSC HNVPPPTKKL NSVSYSFMKA SGSAASNSNG
     GSAKASTHSA KPAKLPDVEA LRGASVTKPL LT
//
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