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Database: UniProt
Entry: A0A1J4JEP0_9EUKA
LinkDB: A0A1J4JEP0_9EUKA
Original site: A0A1J4JEP0_9EUKA 
ID   A0A1J4JEP0_9EUKA        Unreviewed;       986 AA.
AC   A0A1J4JEP0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN   ORFNames=TRFO_36745 {ECO:0000313|EMBL:OHS97129.1};
OS   Tritrichomonas foetus.
OC   Eukaryota; Metamonada; Parabasalia; Tritrichomonadida; Tritrichomonadidae;
OC   Tritrichomonas.
OX   NCBI_TaxID=1144522 {ECO:0000313|EMBL:OHS97129.1, ECO:0000313|Proteomes:UP000179807};
RN   [1] {ECO:0000313|Proteomes:UP000179807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K {ECO:0000313|Proteomes:UP000179807};
RA   Benchimol M., Almeida L.G., Vasconcelos A.T., Perreira-Neves A., Rosa I.A.,
RA   Tasca T., Bogo M.R., de Souza W.;
RL   Submitted (OCT-2016) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OHS97129.1}.
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DR   EMBL; MLAK01001136; OHS97129.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4JEP0; -.
DR   VEuPathDB; TrichDB:TRFO_36745; -.
DR   OrthoDB; 2898719at2759; -.
DR   Proteomes; UP000179807; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR   PANTHER; PTHR45627:SF12; ADENYLATE CYCLASE TYPE 3; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000179807};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        372..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        580..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          659..714
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          802..933
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   986 AA;  113044 MW;  22AF9A838DA97F90 CRC64;
     MINLFPNYLK KRILDFNGKT LINRRRERGR SASDSLHSTN DILDIDENED IGARILRKPK
     LKMTLRRAVD NMKCKGKTIL IISSLIRFVF VIACCSAMIN TSTHYFRSRE GVFNIIQHVG
     SLRVLIDNTL LRYCRLWVIK FGITPKRGKI LRKLDVDEMC PHYINLSEST TDYLISSALE
     SFYTSEQLDE ALSSLPVKKT ANLFEQPFPF RFCFGEHNEF TEDVNFTIHH VPVYFTSLAL
     KYAANQDKIP PDEWHDEFEA CEIVSNFNSI VNYLDSLSTM LLDIESKASE KFQRQAFFVY
     VILAPLVFVF LLVFHYIGYY DLLKGFHQIF DALIFLPTEV YKEISKPVFL LNQEEFLDGS
     QIVESQDYKR RLYLAVTIIS ILLTSATIVI FSYILCVYDK KFVYLNFWLD ASSHRGPLIL
     ESVINTYFYV IYSNTKNGNS SNHADFLDHV YLAQSRLASI HHDLIWGYDN VISCNGFDPR
     LDSIHFDPMC KIEDNGTGLH KGYECLSADQ LILTFSKVSV DLKKKMLDKD IKERDLLRTK
     EFIHYQHVSM THLYARLMEA QEILYDGLNV QMKRLKNISL ILSVIIIIIQ CILFLIETFI
     GFQLNESFQI IRILISRIPT QFILKSPTLL ELITGVEDSL KSDLLSPSKT ALKRSNKIIF
     SINENLNLVT ANTTALRVFN FTEEQFYGQS IQKFVTEESY QKMKTIIGQM FRGEIDHIQR
     LSFVGLSDEL KEIYNEAFLE YIESDKIVVL CSSDTTQIQH NLDEIENVQQ GIDVLMKKSI
     PLPILDQYKK DVNISFSLKT AAVLSMNIHN FVEYIASMSK TQVVHDLSIV FSTFDAIIAD
     HYPNLIKYKI YGTCFYVAAG LFTSDLKAAT TDIINFALEC IQSLEDINQM IDSSLYASIG
     INAGGSLTAG VMGKESLLFE IVGETLTATH MLMNVTGDNK VSISQEAYSI VKYDPHFVFQ
     EAGKIKLCCK SDTLQSYYDV TLSEEK
//
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