ID A0A182VQ13_9DIPT Unreviewed; 1504 AA.
AC A0A182VQ13;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN000142-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN000142-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN000142-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 -!- 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 STRING; 112268.A0A182VQ13; -.
DR EnsemblMetazoa; AMIN000142-RA; AMIN000142-PA; AMIN000142.
DR VEuPathDB; VectorBase:AMIN000142; -.
DR OrthoDB; 3686360at2759; -.
DR Proteomes; UP000075920; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR032628; AC_N.
DR InterPro; IPR009398; Adcy_conserved_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF1; ADENYLATE CYCLASE TYPE 8; 1.
DR Pfam; PF16214; AC_N; 1.
DR Pfam; PF06327; Adcy_cons_dom; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 235..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 842..859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 865..890
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 911..931
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1027..1047
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1054..1073
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1085..1105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 472..603
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 1172..1312
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 48..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1504 AA; 168165 MW; ADC2643100EED0DE CRC64;
MELLVSPDAA RNIAAGVLDQ DQCHHGGIVN PAATIDLDQE RVENGSVISD IAKIPRVPGD
GAQAPDDNTD DRSQPTTVAP PSVPRATTTD RNNRLRSLSL AGCEPEVNGD LPKIDPSRTD
APSDNLESAD NEKPQPNGVM SPSFTIQQCG TDYQECNKGG DPLPPPPPGG GEHPALATNP
GSAHNPPHTN NTYSAFKRGN VVKGILCPSM TNSFRAPSLE RSYLTYSHRQ RQKSLILVNV
VDLVLKVVLA SVWIGFNSGM TIKPHEVTWS VCCIISNFLI CVLGSWRLFA NNYLHWAAVC
TWLLLNLQGF LGEGLGFAER EYLIWYVLFI IFVPYAMLPL PLKWCMIAGS MTAICHLVVT
SLNKFLHDKD PSCIVRQMIA NLLLYLAINF AGMYTKYLTD RGQRLAFIET HKAMEHKRES
EKEYQRTQRL LDSILPMFVN NDIRKEMYKS PEQAQVDTQF KKLYIYHMDN VSILFADIKG
FTELASKTSA QQLVKILNDL FARFDKIAED NHCLRIKLLG DCYYCVSMFD SQSWKSRPDH
AVCSVETGLH MIKAIKDVRC QTNVDLDMRI GIHSGSVMCG VLGEKKWHFD VWSNDVVIAN
HMESGGVPGR VHISEATLKC LNDTYEVEPG NGGSRDSHLK MMNIKTFLIK RTEPLRPRKR
LMDRQSTVQF EKETGARIGE SRFRKDSKTP SITSNSTNTT GTTATCSAAS ATSHATGHVA
HPHTNNNNTS NNNNNHITKR TSKSTIHEDE PTTDWIPEIP FKNLNECGVN AAESFRDKKN
CDREDPLTST EEVDELIDQS IQINSNKEIR QEYLYTWTLK FKDSSQEGTF CQLREDMFRS
NMLCVFVVWI FIVLCQAVII PRCTILIVAL SITTFLLTVG CILVMAEEFS GLPKFLQKSS
STLVHDRSRR TIFVCLTIIL MSIASSMGLM MCDLEEVEAT PDRSTVSPSY AYWQAGGELN
VNSTTVTFLR HALGEAMELN VMNRTLGGID SNATDAPIEL QSDELLEDDG QTPDQPVLHQ
SCVHPEYVVF TWVLCLISLA TALKLYYLVK TFMAIAMVAC YSFLILLVFE RVFDSYDLQY
IQASGMPLAA QMMILLGVFL TMVTYHARLV EVTSRLDFIW KEQAEKELSN MKSNRHLNDL
LIKNILPDHV ATYYLSEERT DELYAKMHEL CGVMFASIPN FKDFYSEDIE NGKACIRILN
EIISDFDSLL EEPRFEKVEK IKTVGATYMA ASNLCTTKKQ HADEQDEEAV CDLVEFALAM
RQKLQEVNKD AFNTFQLRVG ISSGPLVSGV IGARKPVYDI WGNTVNVASR MDSTGENWKV
QVPDYTAALL QTKGYTCVQR GEVNVKGKGL MLTYWVLGKN ISASQLTSPA LVPAGVPQAQ
TPSLQRQTSQ HSSLAAVVFG MMQASKRSNI NTTPTATPSP RTRFGRRGST FSSVRLNQRA
PCNNPVRRNT TRVRGRSYTM KKYPTVSSPT MGSTIPVEDF DISPHIPSFR QLHQEAPKSH
QTGL
//
