ID   A0A3B3RN57_9TELE        Unreviewed;      1074 AA.
AC   A0A3B3RN57;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Guanylate cyclase {ECO:0000256|RuleBase:RU003431};
DE            EC=4.6.1.2 {ECO:0000256|RuleBase:RU003431};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000019161.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000019161.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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|RuleBase:RU003431};
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   AlphaFoldDB; A0A3B3RN57; -.
DR   Ensembl; ENSPKIT00000036003.1; ENSPKIP00000019161.1; ENSPKIG00000004268.1.
DR   GeneTree; ENSGT00940000164853; -.
DR   Proteomes; UP000261540; Unplaced.
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; cd06371; PBP1_sensory_GC_DEF-like; 1.
DR   CDD; cd14043; PK_GC-2D; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
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; 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:SF228; RETINAL GUANYLYL CYCLASE 1; 1.
DR   Pfam; PF01094; ANF_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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          531..803
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          875..1005
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   COILED          812..839
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1074 AA;  120334 MW;  4D33802C7BCFAF30 CRC64;
     MPSRTDSCFL ISLSNHPRWQ LGAIATRRRK KDGTRVSPTD DDPFATMFSP SLHTRSWCSS
     WMFILLLMAA YVPCAWSTTY KIAIVGPWRC DPFFSKALPD LAAQLAMSRI NKDPHLSRGY
     WYDYILVNED CQSSRALARF TELQAYASAF LGPANPGYCS SAALLAKNWN KGLMSWSCLK
     PNMEGGSYPS FLRSLPLSSH VLFAVLRFFR WAHVAVVTSG EELWVATGQE LASSLRALGL
     PVGIVVTIKA DAEGPRKALQ KIRNTDQVKV VIMCMHSVLI GADTQHALLT TALDMRMVDR
     GYIFIPYDTL LYALPYKDVS YPALANDSKL RQAYDAVLTV TMDSGDRNFY EAFGDAQESM
     EIRSSLAPQE VSPFFGTIYS MLYFLAMSVE QTRMAAGRWV SGELLAQSPG GFEIPGFNQP
     LFAGAEGEGM LAHYVVLDTD GEGTSLAATH ALDAAHTHGK FGGLKYLGRP IHFAGRTPSS
     DAHCWFSPYI ACGGGRWYTP TKLILTLDDL VFINTHVSKK KLNEDTAARS TLDVRTPQHS
     VSGRSYIAST PETSNIGILE GDWVWLKKFP NGDSVVEVKE STQAVFIKLR DMRHENLNLL
     LGLFFDGGVF GVVMEHCTRG SLEDLLNNED MRLDWMFKSS LLTDLIRGMK YLHHRNIVHG
     RLKSRNCVVD GRFVLKVGEY GFNEITRAQG LVTPESRPEE LLWTAPELLR NPALEKKGTY
     KGDIYSFAII MQEVISRNSP FCMLDVPVKE IIEKVRSPPP LCRPAVSMDE APLECIQIMK
     KSWSEEPERR PTFEEVFIEF KSINKGKKTN IIDSMLRMLE QYSSNLEDLI RERTEELEVE
     RTKTENLVAQ MLPRSVALAL KTGKPVKPEY FKEVTLYFSD IVGFTTISAL SEPIEVVDLL
     NDLYTLFDAI IGQHDVYKVE TIGDAYMVAS GVPNRNGSQH AAEVSNMSLD ILHCIGAFKM
     RHMPNVKVKI RIGLHSGSVV AGVVGLTMPR YCLFGDTVNT ASRMESTGLP YRIHVNQTTV
     EILHSLQLGY RLEIRGKTEL KGKGIEDTYW LVGRADSIPA DRRQRFLDRQ KTMK
//