ID CYAA_LEIDO Reviewed; 1380 AA.
AC Q27675;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Receptor-type adenylate cyclase A;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
GN Name=RAC-A;
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; U17042; AAA74998.1; -; Genomic_DNA.
DR PIR; T18309; T18309.
DR AlphaFoldDB; Q27675; -.
DR SMR; Q27675; -.
DR GlyCosmos; Q27675; 4 sites, No reported glycans.
DR VEuPathDB; TriTrypDB:LdBPK_170120.1; -.
DR VEuPathDB; TriTrypDB:LdCL_170007000; -.
DR VEuPathDB; TriTrypDB:LDHU3_17.0340; -.
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 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 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..1380
FT /note="Receptor-type adenylate cyclase A"
FT /id="PRO_0000195734"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..891
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 892..912
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 913..1380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 933..1087
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1270..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 938
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 981
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1380 AA; 151694 MW; 6B2D5F7D3C1107A0 CRC64;
MAMQIRPSLG GCLRHGGAGD HAARRLSRLR AAKVFVPTAV VCVLLCCAPW VMAEITNDAE
REPVYILNAM YSTEAYTNED AKALWTGMDM AFYNSHYKAA GGRPIKILHP DPDQDNLYDI
AEVILHSLAR QEKLLAVLGP YLDGRLTAAL SNADVVQSGL MLIAPFTGSS GVRTWSDSVY
FTRAEPMVEL KVVLMHIVNR LRARRVAFMR LTGMHFGGEE LTYVQDTLTS LLRDPAVLYT
VPYSESSVEV DEEAFDAMAD TNPQVIIVWA APVQQVIYFL EKVLTDPRTS SAYVISCSMI
QRVVFDVYKR LLSAGSIKPQ DGRILASATT SPVSGEGLKY MEVLKAQMSN YIENSGSFDY
YPDDDSTETL GRKARSEAPL SRKYTVDEFF QAHPSIAKLM ALGWLSGTLV QQTLEQTDWI
VNRSTYKAGL FNQNRFVIGG DYVLGDYGGP CEPLAQFLGA SCYCNQGGHS SILTVLQNAS
WDIVPDSSFK YPQSECNSSK SQIVKAVSVL ALLNQGYPKL IDAGMQLNEV LPHAFDDNLC
KGYKVSSIFL RVETAKAQQL FDAEVSNYSV DIIAGPIFQA LDVGEIFVLN PLYNHPQLRT
EKRNYVYLMP TLEQQIYVMY SKIDALRTRT DVFEDTAVVL RGYSAQEVVE ISEILFKTAG
TFNLPDPSVA TISFTDSLRG LLSPRAINVV IGMKDGDSAH FANFLAKYTD VMVVVCFDEL
TMYYEELRAT FSVQPTSVQA RLMSFSSLPL WTDASAEAKA RWPILGHFHK IFPDPINHTP
SLLRDVIIAG FIQELVSTTT VAETKLLTNA VYINGGVTTY GFTLGNFEWG CTATTSGDSC
VYKNYGASNI EILSIQRMLD PTVPQLSSPS TPTMEYRPRQ RSHALTPAQR NGLIAGCVVG
AVVLIATCTL LLYCCMDNRN NDAAPKDGDE PVTLLFTDIE SSTALWAALP QLMSDAIAAH
HRVIRQLVKK YGCYEVKTIG DSFMIACRSA HSAVSLACEI QTKLLKHDWG TEALDRAYRE
FELARVDTLD DYEPPTARLS EEEYAALWCG LRVRVGIHTG LTDIRYDEVT KGYDYYGDTS
NMAARTEAVA NGGQVVATEA AWWALSNDER AGIAHTAMGP QGLRGVPFAV EMFQLNAVPG
RRHAALRTEI EAILPDDTAT DTASSAAGAL LSSVETMSDP AAGIAFVLAS CFAPYPVAQR
VRELQPLLSK WGVGAPPRSR LVSEEDYCQG LMNRLAIRIA TVSQARLRLT REDAADGKFK
LASSEALNPL AREGDSAAGG VRPRLPGSPV TSLPAGGSSS MREWRVFTRL MNDTQHPSVT
HLSQQRPSNL TSFTEAQDAA FPLNAHCGPE SRVENSGADD EEIVIVRVSR NPHYARHAFE
//
