ID Q4QEI2_LEIMA Unreviewed; 1414 AA.
AC Q4QEI2;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
DE AltName: Full=ATP pyrophosphate-lyase {ECO:0000256|ARBA:ARBA00032597};
DE AltName: Full=Adenylyl cyclase {ECO:0000256|ARBA:ARBA00032637};
GN ORFNames=LMJF_17_0190 {ECO:0000313|EMBL:CAJ03426.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ03426.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAJ03426.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [2] {ECO:0000313|EMBL:CAJ03426.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
CC -!- FUNCTION: Could act as a receptor for an unknown ligand.
CC {ECO:0000256|ARBA:ARBA00002708}.
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 Evidence={ECO:0000256|ARBA:ARBA00001593};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; FR796413; CAJ03426.1; -; Genomic_DNA.
DR RefSeq; XP_001682266.1; XM_001682214.1.
DR STRING; 5664.Q4QEI2; -.
DR EnsemblProtists; CAJ03426; CAJ03426; LMJF_17_0190.
DR GeneID; 5650736; -.
DR KEGG; lma:LMJF_17_0190; -.
DR VEuPathDB; TriTrypDB:LmjF.17.0190; -.
DR VEuPathDB; TriTrypDB:LMJFC_170007800; -.
DR VEuPathDB; TriTrypDB:LMJLV39_170006500; -.
DR VEuPathDB; TriTrypDB:LMJLV39_170006600; -.
DR VEuPathDB; TriTrypDB:LMJSD75_170006400; -.
DR eggNOG; KOG0618; Eukaryota.
DR HOGENOM; CLU_007273_0_0_1; -.
DR InParanoid; Q4QEI2; -.
DR OMA; GRFTWNC; -.
DR Proteomes; UP000000542; Chromosome 17.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:RHEA.
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 3: Inferred from homology;
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Lyase {ECO:0000313|EMBL:CAJ03426.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:CAJ03426.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000542};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 912..935
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 952..1106
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 1414 AA; 154066 MW; 1862F2A9FD0D0DD3 CRC64;
MACWTVVATT CWGTGCVGVS DRVSYRGHKR TLEALRVSAW RRGLRLVAVS VLAVVAAALC
AALPVWAADG SGKDPAKNPV YLLNATYSLD PSTTKDAKAL WLGIDSALHA SGYRTASGRP
VEIVNPDPAV NKSDIIAVVQ RALEKYPTLL GVIGPFMDPL TSTVVKSDAF NGTDLMFLAP
FTGSDAVRVW NNDVYFTRGD PWTEMTILLT YMLKTIRPRR TAFMYLTGAQ FGDSEYKMVV
SLLSSFSLDL PAVYTAPYSM TNTAVKKKTF DAMADTRPQV IIVWGIPGEQ VVKFLQAVLT
DPRTSSAYIM TCFPLQQIVY RVYYDLAMAG KLTPVDGQIM SSATSLPISH TEVEHVRLFR
TEMVDYMQKT GRVDASLWAD EAKAVQKYGP GEHEASSSDS AAYMHSFYHE HPSTGQLMIA
GWLSGKLIDQ TLQEPLWTID RKTYKAGLFD QTRYVIGKDI VLGDYGGPCT SIAEYLGAVC
YCNQGGRASI LQGLFKAAWV LLPDAIFNYE QSACYLNKIV LSKPLNVVTL NFSDLPKLRK
AAEDMVKVIP RAISEERLGF SAFNPAMLNV TQLTAQGALD WEFLNYSVDL VTGPMLRSID
LSGLLVISPV FNRPNVLVAK ENYLFLMPTL EQEMYVMYSE LSSVRSLTSI GDVVNLVLHE
YRNSNVKSIT AVAMKTAATF NVPDPTVEAV SSRTSVESSL APDRINFVLG ITDQDVDGIA
SFLSKNPLAI VVISFVDLAH EYDRLTAAFA KLPDTVQARV ITFTNLPLWS DTSPSALESY
PLLKLLNAIF PNSADHTPSL LRDLLSIVFI QAVAYGDGGF AKPTSLQESI YKKGVINAYS
VTLGRFTWNC TATTNGESCV YKNFGASNIA MLSVQRMLDP TVPQLSSPGT PAMEYRPRKK
LDKLTSSERN GLIAGLVMFT VILLAAVPMI LCWCMDNRNN DAAPKDGDEP VTLLFTDIES
STALWAALPQ LMADAIAAHH RVIRQLLKKY GGYEVKTIGD SFMIACRSAH SAVSLACEIQ
TKLLKHDWGT EALDSAYREF ELARVDTLDD YVPPTARLSE EEYAALWRGL RVRVGIHTGL
TDIRYDEVTK GYDYYGDTSN MAARTEAVAN GGQVVATEAT WWALSNDERA GTAHTAMGPQ
GLRGVPFAVE MFQLNAVPGR RHAALRTEIE AMLPEGTATE TASSAAGALL SSAGTINGPA
AGIAFVLTSC FAPYPAAQRV RELQPLLSKW GVGAPPRSRL VSEEDYCQGL MNRLAVRIAT
VSQARQRMGS NEAGVSGDIQ NLISSGLLNP LLGEGSFISD GARARHSGVI AVPPTAEPSA
MRESRVLRRS TLNGLTFSRG PSSKKASLSV NTAGFLDDVV PFTAQGSRRP SEEHNSRSAS
VSCEVVVVRM PMKLGCRRRP SLLEPLAEDE AEEA
//
