ID A0A0V1LQP0_9BILA Unreviewed; 2259 AA.
AC A0A0V1LQP0;
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:KRZ61676.1};
GN ORFNames=T02_2246 {ECO:0000313|EMBL:KRZ61676.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ61676.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ61676.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ61676.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ61676.1}.
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DR EMBL; JYDW01000016; KRZ61676.1; -; Genomic_DNA.
DR Proteomes; UP000054721; 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:UP000054721};
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 1703..1725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1731..1754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1775..1799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1811..1830
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1839..1855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1947..1963
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 2023..2163
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..33
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 1422..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1905..1926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2216..2259
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 1424..1452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2259 AA; 254661 MW; C883C004FF72AD16 CRC64;
MDLDTPPKPT PRLSKLKKPD TAHAVQKSNQ GLDNAGLARV DTADQVDEVV QKAEMDNALN
ELCTSIDALD SNETSYRDAQ SVGSDNSLWN SVSWSSGGES EPIEDRLNSI GNNNAESVGN
GDTASNQPHS PLLTLNANVC FVGWIGGKKG RATTMTKMWA VLKNKKLSFF VDDTCEKLID
CLPCNKILLV SKQHSLESAV EPVLILHYMH PRRKKIKFRR FVVEDENDLT AWITLLGKSI
IGDVMGGMDG VFDTVGKVYI KHGTTRIWTC ADLVKRNYSL YYATEGIDCF FEVDFRKVYS
IRDMAEKHEC CADVKEKGPC FALLMENDTL WIQADSKAIT SAWRAVVQSM INKQSNVLSE
QRLSSDNVPM IVEKCINFIS VYGLETEGIH RMCGTVSKID DLYSKLIVDP FSTHLLPHEH
SVHTVTSVLR KFLASVDEPL 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 CYLVEHLLEN FQIRAERLLY KLRLSVIEVK ICVFQAVAGC
GSRRMYARRW SVGRSIRQFL ACYFSIGAER RRFARPTSSS KQLITQQLRF CKRRFAVFVV
HVVDVVVELV VGTATAVMRA RKKKLPFSAS SRTVVAVAVK LMMQREQSTG VTYDASMPMI
SDKLTCPFET PEVLEPREEQ AGRRRWWAWL GNATSKCWRP EFSSRVLESQ YWQCVFPQFQ
RRFRAGLLYT IIYALMWLVY FASLHPLGEI YPYVLFSVVY LVTFSLIFAF TFTKSLYNGL
YVSTSVLCVC LLAVASAFVF IADKPSLGPL AKFALSVELV LLIYTVIPLP 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 VSEATADFLD DQYTLEPAPD YKGIKTYFIV NNVDQEPPPP PPPAAADAPA
SQDVPSPPPP SSISNTHIHD RLRSSELRHI DSSDMAISDA AVNSKKHLNK TLSVSNLTSS
ERCKSDSIFP PGVALNQRTK WASASLVEPS KTASVTTGGE QVPLEKLSEN TEPEPRRSSR
VVTFDSDRNA EFVSGVDGVE SSIDHVLSTH TASISRFEAD HVDFDHRLAD AIRGSSLARG
DYLVRRKALT RTLNFIDPAV EQQYRAHFEL GARRSVGEQE TQTDNLDHQE PATTAATAAA
TDPLAVKVAR LDDWRVDPPK FSVVMDLVVS TIVFWTLLLI CILAVNDQWW YNAAFVTYAT
LSGSFVLALA AWTLRCVLSR ATLPSIWVRW WPKHALSLTM INLPLGALLA SVHCPAAGFS
FAQPRYWQSE SLLLLFCLLV LMVMFGHVNY SQIRSWPKSL FCCLIGIGLV TMVHLCASNC
QPSHTAAVGL VNSTVVFYNA TVNGQDDGSG GGGVVPLIPD HHHKQNDVQQ QHHHHQQQQQ
QLEHEHEKEK LFVQSDHQQY SCCRNEIYMV VLLACLLVIY LNYQFEASFR MSFYGDLQAC
ETIRRMKEMK DQADWLLSNI IPHHVVEHLA RTSKYSENHA MVAVLFASVV NWNDMYEETY
EGGREFLRVL NELVSDFDEL LDRPEFTQVE KIKTIGPTYM AASGLNPARR RLSMHPYSHL
YELMEFALAL QETLDNFNKD LLSFEFRMKI GFNIGPVTAG VIGTTKLYYD IWGDTVNIGS
RMYSTGVVGR IQVSRQAKER LDTVYEFEFR DHISVKGVDG GMDVYLLKSR KQKPPSLQLA
DAAVGAPSSE DGDDGHHHQQ QQQQQQHHLA SITCDGHIH
//
