ID A0A1A9UTM4_GLOAU Unreviewed; 1469 AA.
AC A0A1A9UTM4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-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 Glossina austeni (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7395 {ECO:0000313|EnsemblMetazoa:GAUT014912-PA, ECO:0000313|Proteomes:UP000078200};
RN [1] {ECO:0000313|Proteomes:UP000078200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTRI {ECO:0000313|Proteomes:UP000078200};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GAUT014912-PA}
RP IDENTIFICATION.
RC STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT014912-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 STRING; 7395.A0A1A9UTM4; -.
DR EnsemblMetazoa; GAUT014912-RA; GAUT014912-PA; GAUT014912.
DR VEuPathDB; VectorBase:GAUT014912; -.
DR OrthoDB; 3683909at2759; -.
DR Proteomes; UP000078200; 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; cd06373; PBP1_NPR-like; 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}; 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 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 519..541
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 557..867
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 943..1073
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1292..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 880..911
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1292..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1469 AA; 167050 MW; C367EE159D6A30D4 CRC64;
MKLFNNEKFA NVLMLLFVVV IVVVVNTNSI MCVALSNDCL QKTESLDPMA ASESEQYFPA
NPERYNSDPS YMMSHYKNLS FVALLPSHEQ QNKNDCIMPK VLPVLELAIK HIQNLGFVHG
SRIDVTLISR DTNCSSIHGP IGFFEIYMKF SELNAVFGLP CEYVLAPISR YAGVWQIPVL
TSGGNAADFS NKATSYPTLT RLKGAQANNL GNAIRAIIAN FNWTRTALIY QNEHTKIKGN
SVCFFCIVVV HDKLNEHKAS VYQQAFDTDQ WKKSDIVRML VTVSKHTRIV IMCADPQSIR
KIMLTAEELN MIDSGEYVFI NIELFSRAPQ LTSQPWYDKE DTKENNERAR KAYTAMLTVT
PKQPNDDEYI RVSNEIKSIA ASRYNYTFHN NEPISAFVTS FYDGVLLYAS ALNDSIRDDP
TILNRPINGT EMVRRMWNRS FKGITGNVTI DANGDRISAY SLLDMNPETG RFEIVAHFQQ
NLLEFVNKIH WAGNRTKAPD DSPVCGYDGA LCPETLPGYA ILSLILGVVV IIISVCFFVS
YRHYKSEAEI NSMAWKINID EVICHNSAGR CLRGSLYCLV KHSSQMTLMS DDMNSLSGGD
RQIFIPVGFY RGCKVAIKTI NNNISLTRSL MLELKRMKDL QHDHLVKFYG ACLDPTKSFI
LTEYCPKGSL QDILENEQFQ LDWMFKLSLM HDIVRGMQFL HSSDIKSHGN LKSSNCVVDS
RFVLKICDFG LHTMRTRRNE DQCSDVENCN SHAYWSKLLW TAPELLKMGD QRPAEGTQKG
DVYSFGIIIH EITTRQGPFY LGKLTDEKSP EEIIHLIKGY PHLTQCPFRP QLVDISPDFK
EINSVMQKCW SEEPNERPDF NALKTIIRNI NKDNETGNIV DNLLKRMEQY ANNLEELVEE
RTQDYIEEKK KCEKLLYQLL PQSVAAQLIS GQPVVAEFFD QVTIYFSDIV GFTAISASST
PMQVVQFLND LYTCFDSIVE NFDVYKVETI GDAYMVVSGL PIRNGNKHAP EIARMALALL
EAVHNFKIHH RPNDRLKLRI GLHTGACVAG VVGLKMPRYC LFGDTVNTAS RMESNGEALK
IHISEKTKLA LDEFESFVTT RRGYVPMKGK GEMLTYWLEG EIAKVESPLL TDKLMISRRC
SLKQNPRYGL TSKQYNEKIA NFSYHNSPNL RVKRKISSSS PKLNDTEFKT EDFYYNFGTN
PNGKIPTSHL RPLANDIHSS RSFREDSVRD TNWEMANFRL PLSGTLKTHA NAKLQGYSQL
SSTQSNFNLS NSQPISAKLK IKNSSTIASA MNNNNDSITS MNSTNRIIPN GTKGSEEGQN
LLPRETHEER EEEQIEEAIS PLVQNYEKFK ESKSVNNSTI PLDFPHETPL ALNTNVINNS
DDRHYENVNN LNNVKKFITI PNKKSNTQMP LNNRGESEEF LSPEEKEITE NFIHNNDRSH
HLNHLHSHHH KLRKLFIDVD LIKINNNYI
//