ID A0A0S4J3Q2_BODSA Unreviewed; 624 AA.
AC A0A0S4J3Q2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
DE AltName: Full=ATP pyrophosphate-lyase {ECO:0000256|ARBA:ARBA00032597};
DE AltName: Full=Adenylyl cyclase {ECO:0000256|ARBA:ARBA00032637};
GN ORFNames=BSAL_84110 {ECO:0000313|EMBL:CUG73032.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG73032.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Could act as a receptor for an unknown ligand.
CC {ECO:0000256|ARBA:ARBA00002708}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001593};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; CYKH01000960; CUG73032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4J3Q2; -.
DR VEuPathDB; TriTrypDB:BSAL_84110; -.
DR OrthoDB; 5470792at2759; -.
DR Proteomes; UP000051952; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
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 Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR PANTHER; PTHR43081:SF1; PH-SENSITIVE ADENYLATE CYCLASE RV1264; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 3: Inferred from homology;
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000051952};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 225..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..408
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 624 AA; 68007 MW; 013345F719BF75CC CRC64;
MWDDERIAAT NPLLTLPRAA IQVVVRSDSS GSTSVLTNGL AALEAACSVP NPIFRESTTW
VFGSHVTLVT SAAQSSFVRT TPYALSYIVY PTAIQDGHQI ASVFDTDSQV TTTALVSSSK
LASFAVVNTT TLEVTFSTSA TFYPFVGVSY ALLDANRPRN CSEFAYIANF LLWTIKNPIP
LALADDLNYI SVPSSLSDLV TTVLQDRLSC AGNLLFPKQV EENHIAAIVA GVVVPTVLLL
VAMFVWLTFF AGKRNNSSAP KDANKPVAMA FTDIQASTTL WASVPTVMAR ALDLHNSILR
ECLARNSGYE VKTIGDAFMI AFSSVEDAVR FALDAQKELY DANWETEDID AVYEDMADDK
GLTTIPELWN GLRVRIGVHC GLLDIHLDPV TLGYDYHGTV VNTTARVEDA GHGGQVVVTQ
DVMDALPNDF LSLHRVDVKG IGATELRGLP QPVVLTQLLP EAFAARSFPP LRVEKESALL
EDDDNDVTDT GTEQSNQTAH INTMLLKVFP VAATVDVLFS AMTSGDALPI VRKISQSWGL
HVSKKATDVN VFYRRLAVRC SEVLSVRSDR MRRGSRLTAT DTNSVMSAAS KKVDKLFTKV
SAKYEFVEEI SEESDHGLHR PQKK
//