CY43_TRYBB
ID CY43_TRYBB Reviewed; 1229 AA.
AC Q99280;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Receptor-type adenylate cyclase GRESAG 4.3;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
GN Name=GRESAG 4.3;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=EATRO 1125;
RX PubMed=1982555; DOI=10.1016/0166-6851(90)90152-c;
RA Alexandre S., Paindavione P., Tebabi P., Pays A., Halleux S., Steinert M.,
RA Pays E.;
RT "Differential expression of a family of putative adenylate/guanylate
RT cyclase genes in Trypanosoma brucei.";
RL Mol. Biochem. Parasitol. 43:279-288(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=11157750; DOI=10.1093/emboj/20.3.433;
RA Bieger B., Essen L.-O.;
RT "Structural analysis of adenylate cyclases from Trypanosoma brucei in their
RT monomeric state.";
RL EMBO J. 20:433-445(2001).
RN [3]
RP ERRATUM OF PUBMED:11157750.
RA Bieger B., Essen L.-O.;
RL EMBO J. 20:5302-5302(2001).
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;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000305}.
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DR EMBL; X52121; CAA36366.1; -; mRNA.
DR PIR; S14199; S14199.
DR PDB; 1FX4; X-ray; 1.90 A; A=876-1106.
DR PDBsum; 1FX4; -.
DR AlphaFoldDB; Q99280; -.
DR SMR; Q99280; -.
DR EvolutionaryTrace; Q99280; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; cAMP biosynthesis; Glycoprotein; Lyase;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Receptor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1229
FT /note="Receptor-type adenylate cyclase GRESAG 4.3"
FT /id="PRO_0000195739"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..845
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 846..866
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 867..1229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 889..1043
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 894
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 937
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 768
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 888..895
FT /evidence="ECO:0007829|PDB:1FX4"
FT HELIX 898..904
FT /evidence="ECO:0007829|PDB:1FX4"
FT TURN 906..908
FT /evidence="ECO:0007829|PDB:1FX4"
FT HELIX 909..926
FT /evidence="ECO:0007829|PDB:1FX4"
FT STRAND 930..935
FT /evidence="ECO:0007829|PDB:1FX4"
FT STRAND 938..944
FT /evidence="ECO:0007829|PDB:1FX4"
FT HELIX 946..962
FT /evidence="ECO:0007829|PDB:1FX4"
FT HELIX 969..984
FT /evidence="ECO:0007829|PDB:1FX4"
FT STRAND 985..987
FT /evidence="ECO:0007829|PDB:1FX4"
FT HELIX 997..1003
FT /evidence="ECO:0007829|PDB:1FX4"
FT STRAND 1009..1016
FT /evidence="ECO:0007829|PDB:1FX4"
FT STRAND 1019..1022
FT /evidence="ECO:0007829|PDB:1FX4"
FT TURN 1024..1026
FT /evidence="ECO:0007829|PDB:1FX4"
FT STRAND 1029..1033
FT /evidence="ECO:0007829|PDB:1FX4"
FT HELIX 1034..1045
FT /evidence="ECO:0007829|PDB:1FX4"
FT STRAND 1051..1054
FT /evidence="ECO:0007829|PDB:1FX4"
FT HELIX 1055..1060
FT /evidence="ECO:0007829|PDB:1FX4"
FT HELIX 1063..1067
FT /evidence="ECO:0007829|PDB:1FX4"
FT STRAND 1071..1077
FT /evidence="ECO:0007829|PDB:1FX4"
FT STRAND 1086..1091
FT /evidence="ECO:0007829|PDB:1FX4"
SQ SEQUENCE 1229 AA; 136142 MW; 2B2AA575C62AC288 CRC64;
MIARVCRLTK HSKPPHLPIT LTTPTLFLVV LVLLQLHPIC VLVNVDDGGG VTVKAISLLY
SRKWNVKVIN AVNAGLNASL AARNWTVAPG VNVEVVRPPS YDIDPAQFLD VYLKVLNDDK
SLLVVLGPMG NDDAEKLYDT LEENRLVGFG PMTVSTRHEG YMPHLYFLRP EATGESYCPS
TLCGESLRVL RQGFMYLDGL LGGSEAYDHA VDFISRMGYS FCCVFTVEDK AGGQGGSSEE
FDAVWDEFAG GNPQAVIMFA TMKPDAKKFL VRLVSDPRTE DTFVLTPIFL QKSIVSIWKE
TLEEANVPLH PHRVIQTGSN PLAKEDYIDA IKRFQTEMRN YLTEYKEWSG FNDADHFLKN
DADGELMVNG WIAGEVLRRA LRSHGWMNTA TAFLESLYEQ RRYVIDDIVV GDFGGECDSF
TSANGATCRC NRGGKNVYMR EIAEDYRLQP LVGGHIMTTP LQCHIDPSIL RPPLTGLTVD
MEDHEELLRG STQFETGVST TTSSGKAGEM NSFFLQKVVT DTQKVSNELN TLRQERIVTA
VFGIVTKAVL GLPGLTFIDP ITPTPHLNSF SRNVIHLSPT LEQQLYVLVN YLSSIRADFP
NCVIRGGEAP AIIDALRKTL VTFGLNLSST VVLTPGDTVG EHLPKSGITF IIGLAVDDIV
VIEEHLRIHT KARVLVQFSD IALLYNEFVQ AFNNSDGAKH LLFATSLPHW ADVDTTSETV
RRFHEAVREV EKWTPLSLLG FTTGRLIQEN LQNMERVTSD LLVDLFFNQT VITIDDMHYG
PYKHYDCIIN GVVTADDCMA NFGATDISVW SMARALRSDE PLLQNPMSPS LVYTVPNGNA
LTPAQLAGVV GGSLFVVALA ICLSVLACFT LRGTRDNDSA PKEPTGPVTL IFTDIESSTA
LWAAHPDLMP DAVATHHRLI RSLITRYECY EVKTVGDSFM IASKSPFAAV QLAQELQLRF
LRLDWETNAL DESYREFEEQ RAEGECEYTP PTAHMDPEVY SRLWNGLRVR VGIHTGLCDI
RYDEVTKGYD YYGRTSNMAA RTESVANGGQ VLMTHAAYMS LSGEDRNQLD VTTLGATVLR
GVPEPVRMYQ LNAVPGRNFA ALRLDRELFN DGEDETTTSC SDHSSLRAEL SIAAQTIAAS
LQSLLGTFTP AQRQKALTPF CERCGVTLPR KMGHVWDNDS CQEVIRRIAA KVGHVVDRHA
AETRERSVCT LSSGSVIIIS NDLSDMIRV
