ID   CYAA_TRYCO              Reviewed;         745 AA.
AC   Q26896;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Receptor-type adenylate cyclase;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase;
DE   AltName: Full=Adenylyl cyclase;
DE   Flags: Fragment;
OS   Trypanosoma congolense.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX   NCBI_TaxID=5692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8813663; DOI=10.1016/0166-6851(96)02591-1;
RA   Alexandre S., Paindavoine P., Hanocq-Quertier J., Paturiaux-Hanocq F.,
RA   Tebabi P., Pays E.;
RT   "Families of adenylate cyclase genes in Trypanosoma brucei.";
RL   Mol. Biochem. Parasitol. 77:173-182(1996).
CC   -!- FUNCTION: Could act as a receptor for an unknown ligand.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC       {ECO:0000305}.
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DR   EMBL; Z67964; CAA91903.1; -; mRNA.
DR   AlphaFoldDB; Q26896; -.
DR   SMR; Q26896; -.
DR   PRIDE; Q26896; -.
DR   VEuPathDB; TriTrypDB:TcIL3000.11.16970; -.
DR   VEuPathDB; TriTrypDB:TcIL3000.A.H_000860400; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma 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; 1.
DR   Gene3D; 3.30.70.1230; -; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; SSF55073; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; cAMP biosynthesis; Cell membrane; Glycoprotein; Lyase;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Receptor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           <1..745
FT                   /note="Receptor-type adenylate cyclase"
FT                   /id="PRO_0000195740"
FT   TOPO_DOM        <1..341
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..745
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          384..538
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         389
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         432
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        15
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   745 AA;  81653 MW;  160FA017769A147E CRC64;
     GELGQTDRFF VRIINTTVSE AAHTLTSEKE ERIVTAVFGI VSEDMLDTPN TTFIDPLRLS
     PRLNKFRRNV IHLSPTLEQQ LFVLASHLQS IGSSKALAVI CSEESNDIGD AVRRTLAEFD
     VPLESVRTRM DGEALDGYLP AGGDVFVIGL SVADVEVIAK KLEKHSALRV IVLFSDVALL
     YDVFSVAFNG TTGCERLVFA TNLPHWSDAT PSSVTVQRFH TALSDPKMWT PLSLLAFATG
     RLMQSILPRM EKVGSDTLAN FFYADSSVVV DGMRYGVFDD IECKPAGSDL EVCASNYGAT
     QISVRSMSRT FNASIALLAE PMTPSMRFRD PNEGALTRAQ LIGVVVGTIF AVLLLLALGI
     VLCVALRNTR DNDSAPKEFT DPVTLIFTDI ESSTALWAAH PGMMADAVAT HHRLIRSLIA
     LYGAYEVKTV GDSFMIACRS AFAAVELARD LQLTLVHHDW GTVAIDESYR KFEEERAVED
     SDYAPPTARL DSAVYCKLWN GLRVRAGIHT GLCDIAHDEV TKGYDYYGRT PNLAARTESA
     ANGGQVLVTG ATYYSLSVAE RARLDATPIG PVPLRGVPEP VEMYQLNAVS GRTFAALRLD
     RKVDLINDES DATDGVYSEC GSTHGELSHS AQTIMMVLCA LIGTFTAPQR EKLLIPFCER
     WRVSLPRKTG TAWDENYSRE VVRCIALKVG HVINFDSSAY DFDDLPVSMR RQSSFIVLSH
     QLMESIQETT QQGPSGSDEV ARTCV