CY41_TRYBB
ID CY41_TRYBB Reviewed; 1242 AA.
AC Q99279;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Receptor-type adenylate cyclase GRESAG 4.1;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
GN Name=GRESAG 4.1;
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).
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; X52119; CAA36364.1; -; mRNA.
DR PIR; S14201; S14201.
DR PDB; 1FX2; X-ray; 1.46 A; A=888-1122.
DR PDBsum; 1FX2; -.
DR AlphaFoldDB; Q99279; -.
DR SMR; Q99279; -.
DR EvolutionaryTrace; Q99279; -.
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 InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF53822; SSF53822; 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..1242
FT /note="Receptor-type adenylate cyclase GRESAG 4.1"
FT /id="PRO_0000195737"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..862
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 863..883
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 884..1242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 901..1056
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 906
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 949
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 889..891
FT /evidence="ECO:0007829|PDB:1FX2"
FT STRAND 900..907
FT /evidence="ECO:0007829|PDB:1FX2"
FT HELIX 910..916
FT /evidence="ECO:0007829|PDB:1FX2"
FT TURN 918..920
FT /evidence="ECO:0007829|PDB:1FX2"
FT HELIX 921..938
FT /evidence="ECO:0007829|PDB:1FX2"
FT STRAND 942..947
FT /evidence="ECO:0007829|PDB:1FX2"
FT STRAND 950..956
FT /evidence="ECO:0007829|PDB:1FX2"
FT HELIX 958..974
FT /evidence="ECO:0007829|PDB:1FX2"
FT HELIX 981..996
FT /evidence="ECO:0007829|PDB:1FX2"
FT HELIX 1009..1015
FT /evidence="ECO:0007829|PDB:1FX2"
FT STRAND 1021..1028
FT /evidence="ECO:0007829|PDB:1FX2"
FT STRAND 1039..1046
FT /evidence="ECO:0007829|PDB:1FX2"
FT HELIX 1047..1057
FT /evidence="ECO:0007829|PDB:1FX2"
FT STRAND 1064..1067
FT /evidence="ECO:0007829|PDB:1FX2"
FT HELIX 1068..1072
FT /evidence="ECO:0007829|PDB:1FX2"
FT HELIX 1076..1080
FT /evidence="ECO:0007829|PDB:1FX2"
FT STRAND 1084..1090
FT /evidence="ECO:0007829|PDB:1FX2"
FT STRAND 1099..1104
FT /evidence="ECO:0007829|PDB:1FX2"
SQ SEQUENCE 1242 AA; 138158 MW; 452F8B22FFC0A2E3 CRC64;
MHWQEGGGRG CVYTHGNCRR NLTARALQAL QHVEALTCHY CVSLLHLLPL LLMWMPPVCA
DDSAVTVNVL SMMYNPEYYV EKVNAINAGF DASLSAHGWK TGSGATISVI RPPSYNTTAE
DIFQLGVKQS EGKLLVVFGP LGTDPVVWVR DKLKENDLVA IAPIAYSSEV RGWNPHLYSI
SVEPNAELLA LIRYAVVYLG LPRVGLMYAK GNGFDKESYE FTMRIMEIMG RKPCGVFAVE
SSGGRDVLEG QLNTKWGQFV ATRPQAVLLF SSLEEETTGW FVKKIAQDNR TVDMYLLAPS
SFQHFLIKTW SDALVSLNRT FTPGQLITTG TVPLASDNRS SMVRHFQRDM DNYLDTNSDW
KGFAKPEHYL KDDKLGEMMV FGWLAGEVLF EALNNAPQLT NRTSFMESLY KQRRYVIDDF
VVGDFGGECD EALHYRVPCV IAIKAAAWTH MRVVDDSLSL KPMKKGSVTW SVSECSSANV
QVSAPLIGLY VVLTDDKVAQ RASMRWSLGA RSIEEADDVD KRIFFHSLKV NLKNLTQSLE
QVRDTKAVAA VLGVTADILS VPNMTFIGPI PLFPRLNKFW RNVIHLQPLL AHELYVLAVY
LSNTSSTGVK ALVRGGEASE VVDTLDKSLV TFGVSLDSSK TLGDGDPMSS YLSGNGDVFC
IGLTPPDVAA VARHLQTHLR ARVFVPFNDI LLFYQEFVAG FNASKESIAS SEGLLFATSF
PHWGKKNRKS DMVARFHRHV NESHWDPLTF LGFATTRLLQ VVISNMRKVN AEPLADRIYT
ESNIRVDDVG FGPFSDAECV SGTSVSANEC ASNFGATNIS VWSMGACAEF KLAQDTGWDD
TVYGLCYSAR GSTHTVTDSW NNFWVCIRLV IIYCPWCVPT HLPAERRNNN RAPKEPTDPV
TLIFTDIESS TALWAAHPDL MPDAVAAHHR MVRSLIGRYK CYEVKTVGDS FMIASKSPFA
AVQLAQELQL CFLHHDWGTN ALDDSYREFE EQRAEGECEY TPPTAHMDPE VYSRLWNGLR
VRVGIHTGLC DIIRHDEVTK GYDYYGRTPN MAARTESVAN GGQVLMTHAA YMSLSAEDRK
QIDVTALGDV ALRGVSDPVK MYQLNTVPSR NFAALRLDRE YFFDEGEDGT TTSTSDHSSS
RADVSESGQI IATALQSLLS TFKTAHREKL LLPYCERWRV PLPRKAASEW DDAYCEEVVR
RIAVKVGRVA DHGADSGSES SSTQGSSSII IVPFYDMHLQ EY
