ID A0A0K0DWC3_STRER Unreviewed; 1513 AA.
AC A0A0K0DWC3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000154000.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000154000.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR AlphaFoldDB; A0A0K0DWC3; -.
DR STRING; 6248.A0A0K0DWC3; -.
DR WBParaSite; SSTP_0000154000.1; SSTP_0000154000.1; SSTP_0000154000.
DR Proteomes; UP000035681; 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:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF26; ADENYLATE CYCLASE TYPE 1; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
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:UP000035681};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 597..615
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 627..649
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 661..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 702..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 755..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 304..439
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 857..967
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1368..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1457..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1513 AA; 173691 MW; 903E7204DEA4E4EE CRC64;
MPLSSFFISP FGDVNLEQAY QNQLLKKHGD LLIYFLLIIT ISSILFSINH LPQPDGGMIL
ATITAILSVI LIAILTIKNN EDKKDSNNGS TIKIKYYTNV AKRSYTISLI ISFWLTFVIL
LLMITGEHYV IIITITLYIS FYMLFPFELS SNIIIGAILS FFEITFYILW EYFDKTRLDK
VFFNIIWRRI MENNLSNNDN VYEIQETSMV NEIDKDRVMA SIIAHIWCNF IGIYLYIIRS
RLTRATFLNA RGALRGTICV ESQNIRIDKL LSRPLPPHVL KNVKKSIKEG IVPQIHVETF
NDAVVVYGKI HNLENILSQI SVQDSGRLLN ELEKRIDMIV EKNNCIKIVS DCIIICSGIP
SLHIPNNCPS FFSKSPARWG FQAGIELALM IKSFVDVTQA DISFQIGISQ GIVNGGIMGL
DKWHYDIIGE AIDRAKELCN LAIPGNIFLD KDIGEKLCNE FAMELINDGK EYRIKINEVF
NKMLEKQNYH SSVVFPSQKR LSMTTVPQSI NRLLETVNSV LIVDNIHKRT AKTINNRGSK
RQIINGEIRE KSILEQDERN EYYKNYKSQN YNIMNTFTLR FQDHYFEKYY HKLIDRWLIP
ALITSIIFII ISTFYQQLIV SNFTTILVFS IFGIGILSIM FAFLFLDYFQ FMCQFITQTC
IGHSTVITTL LFSIMSCTMY SFYSCDNSKK CSNPNLNTTN LVMWMIIVPL YVKLSNIASL
LTFILSIIIY SGYVFEKQAE IFVNASSIAG WRVDFDLLII LITLSFILYI RIRRNEKLQR
CDHLSAMRIV EEKKIYENYE KVIENIMLQF LPKHIANSYD IKSEPYCHLF HTAGIGYIQI
MPGYTDKDKW NNQEDFKYLN EIIINIDQML GNFNGLVKVR NSNDIYVVAA GVLPESSHLV
QEAPSTIGDL LSSLTDFAIN VREYVKQFGI WVKIGIDCGP VISYALGDDK PTFNITGKTY
INAMNLSLHS HNFDGLMVSE EIYLALRPRQ YKFADEHVAE VKVRSFIKTL QNEEEIYYSI
PPECSKKNEY VKSIEYIIKG YVFENDLKTK IENDMFVDEL KIQENYKSKN YSSTGKNKTI
FKDANAILKD HCINPIEFLS SMNTSYSSDV YSIDIDIESD SDIEWCSPQY TTIYPDNINK
KIDNDKIIET TSLIETPSSP PIPAPNEEKL LRKASIVSEN KQCLNSFNKR YMSNRALVYS
DFSESEALLS NYSPRIGGNK RVSLTRNGPK IPHWLTSSKN SINVSEISIN RKTSRSHSKI
GSLSALDRLN ATALKVDRML KELACVDDFE MGSCKFDDPE YSKFPLHYAS SIGGESNKSS
LHRFGRGVSS TCHTDYDNMD SEANSDQEVD CQVYSKLEEL KKALKGTDID QSRYSNNSTK
PGNRRNKKSR KSLFDSFKRR KYTIPDTGDE ADGEESNCSS LAASQFFDNI RWKSVHSIGY
ENEYEFTDDN NMNTSFGFID DDVESQHNDS NNENENRKKD EKNIDAKEEM SKLARDIQQN
FGDYKLASFE KLN
//
