ID A0A0L0BWC8_LUCCU Unreviewed; 1083 AA.
AC A0A0L0BWC8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN ORFNames=FF38_04625 {ECO:0000313|EMBL:KNC24332.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC24332.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC24332.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC24332.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC24332.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
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:KNC24332.1}.
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DR EMBL; JRES01001243; KNC24332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0BWC8; -.
DR STRING; 7375.A0A0L0BWC8; -.
DR EnsemblMetazoa; KNC24332; KNC24332; FF38_04625.
DR OMA; VCPMRSK; -.
DR Proteomes; UP000037069; 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; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR PANTHER; PTHR45655:SF10; SOLUBLE GUANYLATE CYCLASE 88E; 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 Coiled coil {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:UP000037069}.
FT DOMAIN 422..550
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 702..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..392
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 792..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 121783 MW; 92BF4B52BF4DC997 CRC64;
MYGLLLENLS EYIKSVYGEE KWEDIRRQAG VDSPSFSVHQ VYPENLLNKL AKKAQQVLGV
SEREFMDQMG VYFVGFVGQY GYDRVLSVLG RHMRDFLNGL DNLHEYLKFS YPRMRAPSFI
CENETKQGLT LHYRSKRRGF VYYTMGQIRE VARYFYHKEM HIELVREEIL FDTVHVTFQL
TFDNRAFTLA SLAMTREEKH LPISAHVLFE IFPFCIVFGA DMVVRSIGNS LMVILPELLG
KKITAWFDLV RPLIAFKFQT ILNRTNNIFE LVTVDPVTDK DDEQKSNELI LHEDGSESEK
SLRLKGQMVY MENWRMIMFL GTPVMPDLNS LITTGLYIND LSMHDFSRDL MLAGTQQSVE
LKLALDQEQQ KSKKLEESMR KLDEEMRRTD ELLYQMIPKQ VADRLRRGEN PIDTCEMFDC
VSILFSDVVT FTEICSRITP MEVVSMLNAM YSIFDTLTER NSVYKVETIG DAYMVVAGAP
EKDPNHAEKV CDMALDMVDA ITDLKDPSTG QHLRIRVGVH SGAVVAGIVG LKMPRYCLFG
DSVNTASRME STSMAMKVHV SESTKEFLGP NYRLTERGEI DVKGKGTMKT YWLDEREHRK
PLQLSMAQVH PLSAYPPATS SASTALIGAT KSVPKAIMPA PSPVVAKEIP PVSKAVAVQN
PTEVIVDNSM NASSLTEDRS RIYSPVTFKD VARRSIANSP VRSLYGGSTV SQEKGRESRS
NSTGHVFMRS PSDVFGSLIL DTEEFLEDLQ ISRSSLANNS QCPCSPIPPF RIGSAPSKPR
PNNPDQFTPE ELAAMDQTTP PSTAPARDNY NMKSSSSTSS LTVEKVKKTR KITFSPRITN
VTTPQEKLEK TRPAMVTTAP TPVAVCPQKK VQQQMKQKHL QQQKQLQQTC EKKLAFTDSR
STSKESISMH SPPPIRSMSA PLPMSKAARK AFLAAKQTKA IEKLDKMIEE VTECEQQMKT
SHSMRIHDVF GDRIQGQGHG EDDMDMEGGC PLFLPPPPRH MANSISDSNI CSHGHSHGHA
PTMHHAPCHH VHEPSSSTKI STSQSFSHAR HTASIHPCCS GYTPHSSNGR HSHRMHSNAC
EIL
//
