ID E3LUJ7_CAERE Unreviewed; 1111 AA.
AC E3LUJ7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN Name=Cre-acy-2 {ECO:0000313|EMBL:EFP11117.1};
GN ORFNames=CRE_30837 {ECO:0000313|EMBL:EFP11117.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) 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 -!- 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 EMBL; DS268415; EFP11117.1; -; Genomic_DNA.
DR RefSeq; XP_003112596.1; XM_003112548.1.
DR AlphaFoldDB; E3LUJ7; -.
DR STRING; 31234.E3LUJ7; -.
DR EnsemblMetazoa; CRE30837.1; CRE30837.1; WBGene00058838.
DR eggNOG; KOG3619; Eukaryota.
DR HOGENOM; CLU_001072_4_0_1; -.
DR InParanoid; E3LUJ7; -.
DR OMA; SKMVEFW; -.
DR OrthoDB; 3686360at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
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:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0002119; P:nematode larval development; IEA:EnsemblMetazoa.
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; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF23; AT30656P-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..643
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 650..667
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 673..696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 708..731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 737..757
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 769..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 318..445
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 872..1034
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1083..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1111 AA; 125629 MW; 817D6FECA7080F08 CRC64;
MSTVMEMSTT RAEIRSVLVK HWRSLDKARL HTIHLWLLLY AAAQIFIEYY FSEVYAVLML
EADDRPQSKE NHESVKKWSP FCFYASIFFI AYLILTCFAI RIRQPVSQLF LDPHKEGMGL
VLVSLSLCVL LPAFSWILHL PVVIFVSRER IHTNEHDHSA LYTSLCIASV IQFFILPRHR
RIFFIVAVSW IVANFLLIVA INWDALNVNS LFMCSCLSLF LHQGVIAIVG VIADSNEAGN
RAEIAKKLTE AVYRRTELET LKDRQEQLLL SVIPAYLADQ VSKSIIQSSS TGTGTGKANS
KNHKLFHDLH VQVHDNVSIL FADIVNFTVL AAQLTARDLV RTLNELYSKF DRDAQRLQCM
RIKFLGDCYY CVSGMPVNRP NHADMCVVMG LEMINTIKQV RLATGVDVNM RIGVHTGSVL
CGIMGLRKWQ FDIWSDDVTL ANHMESAGVP GAVHITKSTK DRLLGEYCFV DTIADDPHVM
SYGQQTYHIL PDKTSAIERT ASIYRSSRLS TSPALQSRVS MKAKVSKMVE FWGAETPFAN
FTKKKFSTSH DPALITDEIA RRPTYINTIP SMTLIENNLT NFSFNNINSM FNCELPTIPA
SPKLLWPFSR KSITCNLSDC VLLMIVCIPS ALANMLLCSL YCPSDVLQQI SLQQFFTIIG
LAMLALLGKV CSYAGPLITM VAFILSSCIP IGPHIIIKKS KLDGVMAFNS LIFLPSCVSH
LVSVFILYRL PYSHRCFLFF ADFVIFQVLL SIFPAYGAEV YVGYMGYHLS IVSISLSLLV
VLLFFIDWIV SFHNCFKIHL YYPQTNYERK RESACHVSFQ NEERDVETMQ DINKILIENI
LPSSVAAKFL SPDRAVNNIL QELYARQHDN VCVMFASIPN FKDFWSEWDT NRKLECLRLL
NEIVCEFDKL LSKPKFSSVE KIKTVGSTYM AAAGLNESET DCEDDELIYL EKQNHGKFNN
NLRRGNLAFR NANLMIEFAL AMSQILDALN RDSFQNFELR IGMSVGPLVA GVIGAQKPQY
DIWGNTVNLA SRMDTHGEPR KIHATTDMGL ILQAGGYRVQ SRGKIRVKGV KEPMETFLIE
VDSKRNSSVS GEPQQNHNNN NNKDNTCHST L
//
