ID CYAB_LEIDO Reviewed; 1331 AA.
AC Q25263;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Receptor-type adenylate cyclase B;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
GN Name=RAC-B;
OS Leishmania donovani.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5661;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MHOM/SD/62/1S;
RX PubMed=7615561; DOI=10.1074/jbc.270.29.17551;
RA Sanchez M.A., Zeoli D., Klamo E.M., Kavanaugh M.P., Landfear S.M.;
RT "A family of putative receptor-adenylate cyclases from Leishmania
RT donovani.";
RL J. Biol. Chem. 270:17551-17558(1995).
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: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the insect stage (promastigote) but
CC not in the mammalian host stage of the parasite life cycle.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000305}.
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DR EMBL; U17043; AAA74999.1; -; Genomic_DNA.
DR PIR; T18310; T18310.
DR AlphaFoldDB; Q25263; -.
DR SMR; Q25263; -.
DR GlyCosmos; Q25263; 5 sites, No reported glycans.
DR VEuPathDB; TriTrypDB:LdBPK_170140.1; -.
DR VEuPathDB; TriTrypDB:LdBPK_363330.1; -.
DR VEuPathDB; TriTrypDB:LdCL_170007400; -.
DR VEuPathDB; TriTrypDB:LDHU3_17.0400; -.
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; cd07556; Nucleotidyl_cyc_III; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR PANTHER; PTHR43081:SF1; PH-SENSITIVE ADENYLATE CYCLASE RV1264; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; cAMP biosynthesis; Glycoprotein; Lyase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Receptor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1331
FT /note="Receptor-type adenylate cyclase B"
FT /id="PRO_0000195735"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..898
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 899..919
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 920..1331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 940..1094
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 945
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 988
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1331 AA; 144163 MW; 5FC3AA22DC1E5072 CRC64;
MYADATHPRR ACWCGAGGVS GCVRQRHAYR CSRLLAGVLL IVGALTLTLA VSTVPAAWAA
GAVASSDEPV YLLNAMYSLS DYNAKHAKAL WLGIDSALHA VGYTAARGRP IKIIEPDPTD
DLSDIVAVVL KALKDYPTLL GVIGPYSDTR LGAVLISPEI QNSGLMFLGP FTGSSSMRAW
NENLYFMRAE PRLEIMAMVK HIANTFRARR TAFMYLTGEQ YGSFEHKSLV ELMTSLSLDP
PAVYSASYST STAVNMTAFD AMADTRPQVI IIWGIPAGQV EELLKVVLTD PRTSSAYIMP
SFALQQMTFQ VYYDLAMAGK LTPVDGQIIS SATSFPLTEP ASVHLRVFRA QMGEYMVKTG
RVDASLWADE AKAVQQYGPW EHEASSSDSA AYVNNFFNEH PCVTQLMIAG WISGSLIAQT
LAEENRIANR TAYRQYMFSQ QRYIVGEDFV LGDYGGPCNG VAEFLGAVCY CNQGGHSAVL
SRLDRAVWTV ITESGVSFTQ KNCYSDGTTL PRPLNFLTLI FAEHPLLAQV GLTFKTSIST
LVAYLQYNAS PVNAATVNVT DTTPQALHDA VTTNYTTDVV VGVTVKGMNV DGYLVPSPIH
PRPHLVELLR NYVYLMPTLE QQMFVLYAKL SAVRGVTSID SAVHMILHGY ASDEVANITA
VLRKSAATFN YDNPTVTAVP STKTVGSALA HGQINFVLAV TAADVADIVD FLVEEKTSIV
VIVFDDLVIQ YPTLVTALKS KPASVQARVI TFTNLPLWSD TSESAHAASK LLTVFHDALP
DPSQHTPGFL SAVLTGSFCA SMRRLADSVH STSLTDMVYR EGSVTTFAEP FGRFQWGCTT
TPTDRFCVYH NYGAQGIVML SVQRMLDPTV PQLSSPMTPT MDYRPRQRSH ALTPAQRGGA
IAGIALLTVI LLAVAGLALY CCMDNRNNDA APKDGDEPVT LLFTDIESST ALWAALPQLM
SDAIAAHHRV IRQLVKKYGC YEVKTIGDSF MIACRSAHSA VSLACEIQTK LLKHDWGTEA
LDRAYREFEL ARVDTLDDYE PPTARLSEEE YAALWCGLRV RVGIHTGLTD IRYDEVTRGY
DYYGDTSNMA ARTEAVANGG QVVATEAAWW ALSNDERAGI AHTAMGPQGL RGVPFAVEMF
QLNAVPGRRH AALRTEIEAI LPDDTATDTA SSAAGALLSS VGTINGPAAG IAFVLASCFA
PYPVAQRVRE LQPLLSKWGV GAPPRSRLVS EEDYCQGLMN RLAIRIATVS QARCPVGNNG
AAVDLDVQHA GTAEVMNPLL GEGSFISDGA RARHSGLTAV PPSAEPSAMR MRRVGRKVPE
RPTVCNVRGA H
//
