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Database: UniProt
Entry: C3Z8B2_BRAFL
LinkDB: C3Z8B2_BRAFL
Original site: C3Z8B2_BRAFL 
ID   C3Z8B2_BRAFL            Unreviewed;       493 AA.
AC   C3Z8B2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 97.
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};
GN   ORFNames=BRAFLDRAFT_241200 {ECO:0000313|EMBL:EEN51236.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN51236.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN51236.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN51236.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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   -!- SUBCELLULAR LOCATION: Photoreceptor outer segment membrane
CC       {ECO:0000256|ARBA:ARBA00004451}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004451}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   EMBL; GG666593; EEN51236.1; -; Genomic_DNA.
DR   RefSeq; XP_002595224.1; XM_002595178.1.
DR   AlphaFoldDB; C3Z8B2; -.
DR   STRING; 7739.C3Z8B2; -.
DR   eggNOG; KOG1023; Eukaryota.
DR   InParanoid; C3Z8B2; -.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
DR   GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR   CDD; cd07302; CHD; 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; IPR011645; HNOB_dom_associated.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR11920:SF335; GUANYLATE CYCLASE 32E; 1.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07701; HNOBA; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 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   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          1..228
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          301..431
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   493 AA;  56050 MW;  016310D0E72A102F CRC64;
     MLYEYFLSEQ MRDLHNENVN PFMGCYTEPG NQGIVNEHCS RGSLEDLIRN EEMQLDWVVK
     QSLLTDLVRG MKYLHSSPIQ VHGRLNSRNC LIDGRFVLKI SDYGLPDILA TQKESRKEHK
     EETERKLLWT APELLRDPVL RKAGTQKGDV YSFAIICQEI ILRGPPFCML SLSAEEIIAK
     VKKPPPLCRP SVTISSAPQD FINMMKQCWT ESPDMRTDFN QLYEELKIIN KGNKINIVDN
     MFKMLEQYSS NLEDMILERT KALDEEKKKT EELLSQMLPS SVADNLKRGL PVKPEAFSET
     TIYFSDIVGF TTISAMSEPM QVVDLLNDLY TTFDDVIRNY DVYKVETIGD AYMVVSGLPV
     RNGNKHAGEI ATMSLDILHA SGKFTIRHMP DVPLRIRIGL HSGPVVAGVV GITMPRYCLF
     GDTVNTASRM ESTGMPFRIH MSQTTMSILH QLGEYKFEPR GKVLLKGKGH MTSYWLTGKD
     NYDKELPDPG VDK
//
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