ID A0A0N4VG17_ENTVE Unreviewed; 456 AA.
AC A0A0N4VG17;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN ORFNames=EVEC_LOCUS9109 {ECO:0000313|EMBL:VDD94358.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000969901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000969901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD94358.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; UXUI01009814; VDD94358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4VG17; -.
DR STRING; 51028.A0A0N4VG17; -.
DR WBParaSite; EVEC_0000969901-mRNA-1; EVEC_0000969901-mRNA-1; EVEC_0000969901.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF29; ADENYLYL CYCLASE; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000274131}.
FT DOMAIN 1..101
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 348..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 51621 MW; F685F2E96CECDC92 CRC64;
MSILLQHEGV EKIRNANRTY IAAVGILPEV CKNVHDTPSV IGDLLAELTQ FALDVSAFAA
DHSITLNIGI DCGPVLSVVT SAEQPNYEIY GNTCLRAYEL MRRADCYGIM VSEEIFLALR
PRDFSFDPRP LKISQDLTAY VFDDCYPEEN NENETRAATL PVEQTTDTQN EMMASMNSSF
SSEVYSVDVG GIETDSEMEW ITPEMLHYER KDQPSTSAMY SSEVIYIPTE DSECDRSTTP
EWSSRKRRLK RSRYPGWLSR SVTSDTSRSR IERAERLAAA ANRVDRMLEE LNAVADLDTG
LECHPFPTSA LSASSRSIRS VFSKRELSSA CHTEYDNAES EGVFSDSEML DNRIRHPNKK
PLKNSENRKK RRRLWSNVDN GNEADIDSVC SSLNFSSIFS NLRWNSVHSI GYDNEYEIAS
SEDLRELARS QMEALSRDIR SNFGDYQLAT FSDNDF
//