ID A8XXN9_CAEBR Unreviewed; 273 AA.
AC A8XXN9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Protein CBG20392 {ECO:0000313|EMBL:CAP37408.2};
GN ORFNames=CBG20392 {ECO:0000313|EMBL:CAP37408.2}, CBG_20392
GN {ECO:0000313|EMBL:CAP37408.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP37408.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP37408.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP37408.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR EMBL; HE601396; CAP37408.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XXN9; -.
DR STRING; 6238.A8XXN9; -.
DR eggNOG; KOG4171; Eukaryota.
DR HOGENOM; CLU_1112175_0_0_1; -.
DR InParanoid; A8XXN9; -.
DR OMA; FFLERND; -.
DR OrthoDB; 1356373at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016849; F:phosphorus-oxygen lyase activity; IEA:InterPro.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 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; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR11920:SF335; GUANYLATE CYCLASE 32E; 1.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 19..138
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 224..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 273 AA; 30467 MW; 8D9F57B1282E7FA4 CRC64;
MYLYGLSHVR WREEFADCTL LFTDIVTFTN ICALCTPYDV VTLLNDLYLR FDRLVGLHDA
YKVETIGDAY MIVGVSQSTV AFLGMLMESK LVLSPITHKP IKIRLGVHCG PVVAGVVGIK
MPRYCLFGDT VNVANKMESN GIQCKIHVSE SAKLNGLKAN PSYVFIDRGN TEIRGKGMMY
TFFLERNDRK SVWELCARPR SGEQTIDGYM ELHDQAIYQE EGTVESQNAE NGTTHTTNAS
NNNNTHHSGR KMMNGSSVDP GSHHVRSPTC TIC
//
