ID A0A0V0RUQ3_9BILA Unreviewed; 2131 AA.
AC A0A0V0RUQ3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN Name=adcy9 {ECO:0000313|EMBL:KRX18222.1};
GN ORFNames=T07_14915 {ECO:0000313|EMBL:KRX18222.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX18222.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX18222.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX18222.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX18222.1}.
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DR EMBL; JYDL01000076; KRX18222.1; -; Genomic_DNA.
DR Proteomes; UP000054630; 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:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 2.
DR CDD; cd17113; RA_ARAPs; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF8; ADENYLATE CYCLASE TYPE 9; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00044; CYCc; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
DR PROSITE; PS50238; RHOGAP; 1.
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:UP000054630};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 895..918
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1026..1044
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1050..1072
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1079..1101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1121..1145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1656..1678
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1684..1707
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1728..1752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1764..1783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 356..549
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 1254..1381
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 1893..2033
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2090..2131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2131 AA; 240364 MW; B2AB775B25CAAC5E CRC64;
MDLDTPPKPT PRLSKLKKPD TAHAVQKSNQ DLDNAGLARV DTADQVDEVV QKTEMDNALN
ELCTSIDALD SNETSYRDAQ SVGSDNSLWN SVSWSSGGES EPIEDRLNSI GNNNAESVGN
GDTASNQPHS PLLTLNANVC FVGWIGGKKG RATTMTKMWA VLKNKKLSFF VDDTCEKLID
CLPCNKILLV SKQHSSESAV EPVLILHYMH PRRKKIKFRR FVVEDENDLT AWITLLGKSI
IGDVMGGMDG VFDTVGKVYI KHGTTRIWTC ADLVKRNYSL YYATEGIDCF FEVDFRKVYS
IRDMAEKHEC CADVKEKGPC FALLMENDTL WIQADSKAIT SAWRAVVQSM INKQSNVLSE
QRLSSDNVPM IVEKCINFIS VYGLETEGIH RMCGTVSKID DLYSKLIVDP FSTHLLPHEH
SVHTVTSVLR KFFASVDEPL VPKNITINLL NHINDTVEWK CRLRYYDEAI RQLGRINYST
LRKLVGHLKE VTQFSETNKM NVQNLACIFS PTIFRMNQID DDKDKISFQY SVKLFTVMAD
LIENYEILFN ISEEENRRDS LVQKAKKKLI SPTETPKKVS SGILHCLHVL EKDRISFNIK
VGVDLTAENV CEYVRSRGVA SLPSQIALFE VICDGQLERL VPSDESVFDI VMRWISWPLG
DRVGNYLIVK GDSISSKLND YATKFTSSSP WSTAYVSVTK SFAKRYLALF PNELMLFRNQ
KDDNAEQVWR ISDFLWFIGA EAKRHPPAKF NVTFIRNCEF LTRSKTLPFM GVALSFKQES
DQLRLLSAVY SENPLISVSN CYLVEHLLEI FQIRAERLLY KLRLSVIEVK ICVFQAVAGC
GNRRMYARRW SVGRSIRQFL ACFFSIGAER RRFARPTSSS KQLITQQLRF CKRRFAVFVV
HVVDVVVELV VGTATAVMRA RQKKLPFSAS SRSAVAVAVK LMMQREQSTG VTYDASMPMI
SDKLTCPFET PEVLEPREEQ AGRRRWWAWL GNATSKCWRP EFSSRVLESQ YWQCVFPQFQ
RRFRAGLLYT IIYALMWLVY FASLHPLGEI YPYVLFSVVY LVTFSLIFAF TFTKSLYNGL
YVSTSVLCVC LLAVASAFVF IADKPSLGPL AKFALSVELV LLIYTVIPVP MYLCLLMAVV
FSVMYEELCA GAYKPVTIVL HGLAHLLGAH IYTLTQVRDR KTFIKLGQSL LARHDLEIEK
EFKDRMIRSV MPQTVAEELL KESSELKRPS NTPSSDRCTN LFRPFTMNLM RDVSILFADI
VGFTTMSSNK SADELVNMLN DLFGRFDALC GQSGCEKIST LGDCYYCVSG CPEPRADHAQ
CCVKMGLAMI EAIHQFDIDR NQEVNMRVGI HTGTVLCGIV GRRRFKFDVF SNDVDLANAM
ESTGMSGRVH VSEATAAFLD DQYTLEPAPD YKDRLRSSEL RHIDSSDMAI SDAAVNSKKY
LNKTLSVSNL TSSERCKSDS IFPPGVALNQ RTKWASASLV EPSKTASVTT GGEQVPLEKL
SENTEPEPRR SSRVVTFDSD RNAEFVSGVD GVESSIDHVL STHTASISRF EADHVDFDHR
LADAIRGSSL ARGDYLVRRK ALTRTLNFID PAVEQQYRAH FELGARRSVG EQEAQTDNPE
HQEPATTAAT AAATDPLAVK VARLDDWRVD PPKFSVVMDL VVSTIVFWTL LLICMLAVND
QWWYNAAFVT YATLSGSFVL ALAAWTLRCV LSRATLPSIW VRWWPKHALS LTMINLPLGA
LLASVHCPAA GFSFAQPRYW QSESLLLLFC LLVLMVMFGH VNYSQIRSWP KSLFCCLIGI
GLVTMVHLCA SNCQPSHTAA VGLVNSTVVF YNATFEASFR MSFYGDLQAC ETIRRMKEMK
DQADWLLSNI IPHHVVEHLA KTSKYSENHA MVAVLFASVV NWNDMYEETY EGGREFLRVL
NELVSDFDEL LDRPEFTQVE KIKTIGPTYM AASGLNPARR RLSMHPYSHL YELMEFALAL
QETLDNFNKD LLSFEFRMKI GFNIGPVTAG VIGTTKLYYD IWGDTVNIGS RMYSTGVVGR
IQVSRQAKER LDTVYEFEFR DHISVKGVDG GMDVYLLKSR KQKPPSLLLA DAAAGAASSE
DGDDGHHHHQ QQQQQQQHHH QASITCDGHI H
//
