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Database: UniProt
Entry: A0A0N4VG17_ENTVE
LinkDB: A0A0N4VG17_ENTVE
Original site: A0A0N4VG17_ENTVE 
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
//
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