ID A0A1I7T809_9PELO Unreviewed; 680 AA.
AC A0A1I7T809;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold536.g3311.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold536.g3311.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 -!- 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 -!- 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-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR AlphaFoldDB; A0A1I7T809; -.
DR STRING; 1561998.A0A1I7T809; -.
DR WBParaSite; Csp11.Scaffold536.g3311.t1; Csp11.Scaffold536.g3311.t1; Csp11.Scaffold536.g3311.
DR Proteomes; UP000095282; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016849; F:phosphorus-oxygen lyase activity; IEA:InterPro.
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; 2.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627:SF16; ADENYLATE CYCLASE; 1.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 324..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 376..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..172
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 487..624
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 680 AA; 77898 MW; 73B1CDCE05333A0B CRC64;
MHRQEKILLA VLPKNIAFEV KKDMQDTHEE RMFHKIYIRK YEDISILFAD ICGFTNLASE
YNPKDLVLML NELFARFDKV ASIHQCMRIK ILGDCYYCVC GVPEYQKNHA INTVEMGRDM
IEAIRLVREM TLVNVNMRVG IHTGKAHCGV LGLKKWQFDV WSNDVTLANQ MESGGLPGRV
HITDATRRYL NGAYILEEGN GASRSKFLEK EKIKTWLVVD RSPDYDIVSQ ETANHPMTIP
WKSTRGISKQ ERLTGMSTRT RGASTRNGLS EEEVLVENVD SHLRQGIQAI HQENWKSMYC
QNWSLKYKQV RVENKFVRMK YKDIPFQVTL YVAIVAICIG IKFGLMNLMV FSFIPQAFIL
LTSIMIFILT RLLMSLIYFS SFIVLITVKL VAIDKYDTLF SVYANFCVLS CLTLLLVVFS
TRRSELISRY DFIWKLQALD EQLQMKRKHE QNRSVLENIL PSHVAKHFVE DATSVSKLYH
ESRDNACIMF ATLTAFDKFY IECDGNNEGV ECLRLLNEII SDFDQILDRD EFRKIEKIKT
ISTTYMVASG LAGEECADNS HVEAIALFAR ELLLKLESIN MHSFNDFNLR IGINVGPVVA
GVIGSDKPHY DIWGNSVNVA SRMDSGGVAG RIQVTEEVKS ILEPLGYQFE CRGQINVKGK
GMMTTFFLLP PDDCQCELYK
//
