ID A0A1A9ZVI9_GLOPL Unreviewed; 1169 AA.
AC A0A1A9ZVI9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 Glossina pallidipes (Tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI026354-PA, ECO:0000313|Proteomes:UP000092445};
RN [1] {ECO:0000313|Proteomes:UP000092445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPAI026354-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI026354-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: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC 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 AlphaFoldDB; A0A1A9ZVI9; -.
DR STRING; 7398.A0A1A9ZVI9; -.
DR EnsemblMetazoa; GPAI026354-RA; GPAI026354-PA; GPAI026354.
DR VEuPathDB; VectorBase:GPAI026354; -.
DR Proteomes; UP000092445; 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; cd06352; PBP1_NPR_GC-like; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.250.780; -; 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; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR001170; ANPR/GUC.
DR InterPro; IPR011645; HNOB_dom_associated.
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:SF274; GUANYLATE CYCLASE; 1.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07701; HNOBA; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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 543..566
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 589..889
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 962..1092
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 899..930
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1169 AA; 132386 MW; 0E5139FC2EBED200 CRC64;
MQINLLLNIG YYLLVAVDIF AIGHKTKRIY FDESYWAEDV PKDSSEHLII DNSLYDLQTL
ATGENFIIIN SNDDEDISSR RKRETIEYDE IGNRVYNVGV LMASHLDSPF DLERCGPAVD
LALDVINDEF LRPHNITLRK VQASYPSCSG AKAPGLAADM HFKDDVIAFI GPACAFALEP
VARLAAYWNS PIITGMGDQP PSEGELTVTS GILGRIHKWK NESTGMFKDK TKYPTLTRMS
YCQCRLKLVF ASVFRQFNWK HVALLVDRSD LFSLTVGKNL EYGLRQEGLL SFVRELNGNE
QEPYEIYLRD ASMYARVVIL SVRGTLVRKF MLAAYSLGMT NGDWVFLDVE IFQSTYWGDH
DWEMGDDDDG RARKAYEALL RVSLLQPSSP KYQGFAENVR DMALHNYNYT FSDGEEVNFF
IGAFYDGVYL LGMALNETLS EGEDIRDGMA ITRRMWNRDF HGITGHVRID DNGDRDADYS
ILDLDPINGK FAVVAHYYGL HRNYSEVHGK KIHWPGGREE PPPDIPRCGF LGNSPECHGN
ELIIMYAMFA LAIFLGFTFL VVYLMCKQMK LNNELNNMSW RVRPDDVLLE VGRLYGSKVG
LQKLNAENFS LQQYGIHSGR ASITSCTSLP LTQVFTTIGI FRGERVAIKK IHKKKVDITS
TLLWEIKQAR DVSHENTVRF VGACIDLPRP TVLILTEYCP KGSLKDVLEN EAIQLDWNFR
MSLIHDIVKG MAYLHNSDVQ VHGKLRSCNC LIDGRFVLKI SDFGLRILTT PSEFVKDQNY
FNKFLWIAPE LLPVTVFPGN PATQKGDVYS FAIILEEIVV RGGPYETARQ FMDIQTILNR
VESHESTPFR PFIGQRDCPP DVLDLMEKCW ADNPDDRPAF ATIRSTVRLI MKGFCENLMD
DLLRRMEQYA NNLESLVEEK TEQLSIEKKR TEELLYQVLP RPVATQLLAG EMVQPEQFEC
VTIYFSDIVG FTALCAQSGP MEVVDFLNDL YSTFDRIIGF YDVYKVETIG DAYMVVSGLP
ERNGDNHARE IGLMALAILD AVKCFSIKHK PDYQLMIRIG IHSGPVCAGV VGQKMPHYCL
FGDTVNTASR MESAGLPLKI HVSSATKTIF DKFGTFEMEL RGEVELKGKG AVITYWLSGC
TEPDPRPPTP HKNNNDEIPF PILFPAIGK
//
