ID A0A158NMG5_ATTCE Unreviewed; 1342 AA.
AC A0A158NMG5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN Name=105621896 {ECO:0000313|EnsemblMetazoa:XP_012058723.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012058723.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012058723.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) 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|PIRSR:PIRSR039050-51};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR039050-51};
CC Note=Binds 2 magnesium ions per subunit. Is also active with manganese
CC (in vitro). {ECO:0000256|PIRSR:PIRSR039050-51};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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; ADTU01020473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01020474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012058723.1; XM_012203333.1.
DR STRING; 12957.A0A158NMG5; -.
DR EnsemblMetazoa; XM_012203333.1; XP_012058723.1; LOC105621896.
DR GeneID; 105621896; -.
DR KEGG; acep:105621896; -.
DR eggNOG; KOG3619; Eukaryota.
DR InParanoid; A0A158NMG5; -.
DR OMA; TTEWIPE; -.
DR OrthoDB; 3686360at2759; -.
DR Proteomes; UP000005205; 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; IPR030672; Adcy.
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 PIRSF; PIRSF039050; Ade_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, ECO:0000256|PIRSR:PIRSR039050-
KW 50}; cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR039050-
KW 51}; Manganese {ECO:0000256|PIRSR:PIRSR039050-51};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR039050-51};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR039050-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 707..728
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 734..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 780..799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 998..1018
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1030..1047
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 389..516
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 1115..1254
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 45..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 394..399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 394
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-51"
FT BINDING 394
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-51"
FT BINDING 395
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-51"
FT BINDING 436..438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-51"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-51"
FT BINDING 482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 1165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 1241..1243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 1248..1252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
FT BINDING 1288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039050-50"
SQ SEQUENCE 1342 AA; 151875 MW; C9295527B47C71B6 CRC64;
MITEQTWSMM LDSDVTSINE SSISPRKQLW IKAVKKLTSE RLGREGLAAW EDRKSNTDPE
VAAEAKDDGE APINDDETSK AEPEAADGAE QSVADEEAQT QRDVFKKGML YKGIFLPSLT
NSFHSKQLET SYLLYSNRQR QKSLIMLNIV DLSLKITLTA IWLWQRDSNG GGLIEGLSWA
ACCMAANLVI CVLGWWRCFS NNYLYWASIF TWLLINSQGF IGAGLNFTTQ QRLMWYILFV
VYAPYAMLPL PLRWCVLAGY GTALTHMMMA GISLLRDSTY LQDAACIIRM LTTNVLLYLA
VNLAGMYTKY LTDRGQRQAF LETHRSTETR QRTQNENNRQ EKLLLSVLPD FVAKEMIRDI
ARETARGGTI SFTPNQFHRI YIHRYENVSI LFADIKGFTA LASQCSAQEL VKVLNDLFAR
FDKLSAENHC LRIKLLGDCY YCISGLPIAR SDHAHCCVEM GLHMIKAIRD VRFTTKVDLN
MRIGIHSGSV LCGVLGLRKW QFDVWSYDVT LANHLESGGI PGRVHISADT LKCLNDVYEV
EPGYGCERDN YLKDRNVETY LIKQLEPLKS RRRQSSKPKV WTEEELAANK NKKSFKVNPH
ATVNSNAPAP GSLDDDIGVD WTPEIPFENL NTATSVSNLE SEYLEEENGQ PAKPSNKAAS
TTAVEKKGAI ETASNKRMRS ANINTWTLRY NDESLESKFD QLREDMFKSN MICCFVIWLF
IAVCQAIILS DCMILLISLL VTTVILVASS ILVMAEEFKG MPTYLQHTSS MLVHNKKHRT
IFICGVITLM TLTSIIGVLT CPITVRPYQE VMVLEQQQIP TTIVAAPLPV QEKLTATTER
SGLDHFVLTF LEAALSDEST EGGKTIPSTE NNTLETGSSN IELKLTRVVN DREPGKSRRE
FFRFYRYEQH YGKPEIGSRH YRRVARKRDI EVGSQRKILS VVGEENQKAR SKRLALMSSD
ELEETDCIRP EYMVFTWILC LIALASALKL YYLVKTALAA AIVVVYAVLI LVVCKDMFTE
RERNVSAISL PAQMLTFLTV FLVMVTYHGR LVEVTSRLDF LWKQQAEREL NDMIESRHNN
MQLLKNILPD HVAHHFLTTD RAPEELYSQS RDKVGVMFAS VPNFTEFYSE DVNKGMECIR
LLNEIIADFD ELLDETPFHC IEKIKTVGAT YMAASGLNPS QIDNNGDDME HLCRLVDYAV
AMRHRLEDVN VHSFNNFDLR VGISCGPLVG GVIGARKPVF DIWGNTVNEA SRMDSTGVMG
KIQVPHDIAR FLESRGYQTQ KRGLIEVKGK GTMETYFVLG KATLQQEGTP RHRSTCRSLA
AVVYGVVQAR RKQIRKQAMR RT
//
