ID F4X775_ACREC Unreviewed; 1061 AA.
AC F4X775;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN ORFNames=G5I_14213 {ECO:0000313|EMBL:EGI57687.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI57687.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) 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 -!- 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 EMBL; GL888828; EGI57687.1; -; Genomic_DNA.
DR AlphaFoldDB; F4X775; -.
DR STRING; 103372.F4X775; -.
DR eggNOG; KOG3619; Eukaryota.
DR InParanoid; F4X775; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 3.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR032628; AC_N.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF23; AT30656P-RELATED; 1.
DR Pfam; PF16214; AC_N; 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 Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 593..616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 659..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 730..749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 769..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 267..367
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 854..997
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 1061 AA; 122132 MW; EFAC24AEBE4E01E2 CRC64;
MDDPKSANEV RMDMELVTRA SVSSLEKDFD EWTWSGLRVG MKECLLEIVV YCIVGALMCP
MIALSFRSRH IAKNTYLPIM LSWMIIVLLV VCDLTIPLFY VFTYAEDIPP IRPAYATHSL
LACYVFLPIT KNSHALVLGL TASMCYLATL SIITYNNTSD YITKIISDAI YFMCVNALGL
YFRFMNEVVI RRSFLDRRKC VESTLRLNYE KDQEEQLTRS ILPQHIVAKI KKDFRDIFKF
IEEHKKSPPP KGRPYSDLCV ETHDNVSILY ADVVNFSGLT VTLPIRKLVE TLNDLFGSFD
EASERHNVLR IKFLGDCYYC VSGVPTPNSQ HAKSCVDLGN IISGILGTNK WQYDVWSRDV
VIANKMEQTG KPGKVHVTQQ TLDLVNASDY NYIPVERLDD EVLRKYEIRS YLITPSLPET
SILSPTRRTL LQNSENSLNT ISPDTPTLSY SVSNKHYVKF NNGRTNTIIS TNSRTRLMVN
NQADVFASTY RRRTHFMDSC LRDYHLMLKA ADAEMENAIN QMPLSKWEQW SNWKHINPLF
LTFRQWSWEI PFLREPDPVF KFYIGCSAFV LIFMGFMYLV PTFMLPQWHL RTLVGYFSVL
MFLFALMPLT WMHFVWNRCK DPHDEHEGHV PHPRNKLLYF FYQTSVKVVW SALLRTILYL
VITIMLAACA MLDMIFECKN HHEDNLLDAN VTSSVSEVSS KFDCIATPWQ MTETCSLAIL
TSFLFLRVHY ILKFVISICV VAFYAWNVWV HRSNIFQLSD TWNPNMEPRL AHILSVLFLT
FSLHLIDRQA EYLSRLDYQW KRQLTKEQDE AFHTRNANKL LLRNILPEHV AEFYLNMNRT
EENEPYHEAH NNVAVMFASL TELSIVESNI LSDLNEIICE FDKLLFEPSF MCRIEKIKVA
GTTYMAACGL DAYRRGSMHS TESDENCNDN VVKVMAQFAV HMMSVLDKMN ARSFTTSKPH
KLRIGISHGE VTAGVVGAQK PLYDIWGDAV NMASRMDTTG LPGKIQVTAD TAAVLEQQGV
KCHLRGETYV KPKGEVTTYF VGIDEKGILE RVDAREESTS L
//
