ID Q4QEI3_LEIMA Unreviewed; 1377 AA.
AC Q4QEI3;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
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 Name=RAC-A {ECO:0000313|EMBL:CAJ03424.1};
GN ORFNames=LMJF_17_0200 {ECO:0000313|EMBL:CAJ03424.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ03424.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAJ03424.1, 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:CAJ03424.1, 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; CAJ03424.1; -; Genomic_DNA.
DR RefSeq; XP_001682265.1; XM_001682213.1.
DR SMR; Q4QEI3; -.
DR STRING; 5664.Q4QEI3; -.
DR EnsemblProtists; CAJ03424; CAJ03424; LMJF_17_0200.
DR GeneID; 5650735; -.
DR KEGG; lma:LMJF_17_0200; -.
DR VEuPathDB; TriTrypDB:LmjF.17.0200; -.
DR VEuPathDB; TriTrypDB:LMJFC_170007600; -.
DR VEuPathDB; TriTrypDB:LMJLV39_170006100; -.
DR VEuPathDB; TriTrypDB:LMJSD75_170006400; -.
DR eggNOG; KOG0618; Eukaryota.
DR HOGENOM; CLU_007273_0_0_1; -.
DR InParanoid; Q4QEI3; -.
DR OMA; ILNAMYS; -.
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; cd07302; CHD; 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:CAJ03424.1};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:CAJ03424.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000542}.
FT DOMAIN 930..1084
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 1377 AA; 151166 MW; BC22736E9EFE2E5C CRC64;
MQIRPSLGGC LRHGGAGDHA ARQMSRLRAT KLLVSTAVAC VLLCSAPWVL AEITNNAEQE
PVYILNAMYS TEAYTDDDAK ALWTGMDMAF YSSQYKAAGG RPIKILHPDP DQDNLYDIAE
VILHSLARQE KLLAVLGPYL DGRLTAALGN AEVVQSGLVL IAPFTGSSGV RTWSDSVYFT
RAEPMVELKV VVKHIINKLR FRRIAFMRLT GMHFGREEMM YVQDTLASLL RDPAVIYSVP
YSEISVAVDE AAFDAMADTH PQVIILWAAP VPQVIHFLEK VMTDPRTSSA YIMSCSMIQR
VVFDVYKRLL SAGSIKPQDG RILASATTSP VSSSMKYMEA FKTQMADYIE HSGSFDYYPV
DDNAEALGQK ARPEAPRSRK YTIDEFFQEH PSIAKLMALG WLSGTLVQQT LQQTDWIVNR
STYKAGLFNQ NRFVIGGDYV LGDYGGPCEP LAQFLGASCY CNQGGHSAML TALRNASWYT
VFDSSFQYPQ SECNSSKSQI VVAVNVLTLL HEGYPKLIDA GMQLNEVLPH AFDSTLCKGY
QVGSTFLRVE TAKAQLLFDT EVSNYSVDIV AGPILQGLDV GEMFVLNPLQ NLPQLRTERR
NYVYLMPTLE QQLYVMYATI DALRNTMHVL EDTAVVLRGY SAEEVVGISE ILFKTAGTFN
LPDPSIAAIS LTDSLHDLLS PTAINIVMGM QDGDSVHFAN FLAKHIDAMV VVCFDELTMY
YEELRATFSV QQASVQGRLM SFSSLPLWTD TSTEAEDRWP ILQRFHNIFP DPINHTPSLL
RDVVIAGFIQ ALVSTTTVVE TKLLTNAVYI NGGVTTYGFT LGTFEWGCTT TTKGESCVYK
NFGASSIEIL SIQRMLDPTV PQLSPPITPA MEYRPRQRLH ALTPAQRNGL IAGCVVGVVV
LITTCTLILY CCMDSRNNDA APKDGDEPVT LLFTDIESST ALWAALPQLM ADAIAAHHRV
IRQLLKKYGG YEVKTIGDSF MIACRSAHSA VSLACEIQTK LLKHDWGTEA LDSAYHKFEL
ARVDTLDDYV PPTARLSEEE YAALWRGLRV RMGIHTGLTD IRYDEVTKGY DYYGDTPNMA
ARTEAVANGG QVLATEATWW ALSNDERAGT AHTVMGPQGL RGVPFAVEMF QLNAVPGRRH
AALRTEIEAM LPEDTATETA SSAAGALLSS VGTMSDPAAG IAFVLTSCFA PYPAAQRVRE
LQPLLSKWGV GAPPRSRLVS EEDYCQGLMN RLAVRIATVS QARLQLTRED AADGGLKRAS
SEALNPLARE GDCAAGGVRP RVTGSSAASL PVGIGSAMRE WHVRSRLMND TGRPSVTHVS
QQRASQLTSH TEAQDAVFRL SALSVPESTV ESSGADDEEI VIVRVSRNPH YARHAFE
//
