ID CYAA_SACKL Reviewed; 1839 AA. AC P23466; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 16-JUN-2009, entry version 63. DE RecName: Full=Adenylate cyclase; DE EC=4.6.1.1; DE AltName: Full=ATP pyrophosphate-lyase; DE AltName: Full=Adenylyl cyclase; GN Name=CYR1; OS Saccharomyces kluyveri (Yeast) (Saccharomyces silvestris). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea. OX NCBI_TaxID=4934; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91323718; PubMed=1864503; DOI=10.1016/0378-1119(91)90551-L; RA Young D., O'Neill K., Broek D., Wigler M.; RT "The adenylyl cyclase-encoding gene from Saccharomyces kluyveri."; RL Gene 102:129-132(1991). CC -!- FUNCTION: Plays essential roles in regulation of cellular CC metabolism by catalyzing the synthesis of a second messenger, CC cAMP. CC -!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family. CC -!- SIMILARITY: Contains 1 guanylate cyclase domain. CC -!- SIMILARITY: Contains 21 LRR (leucine-rich) repeats. CC -!- SIMILARITY: Contains 1 PP2C-like domain. CC -!- SIMILARITY: Contains 1 Ras-associating domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X56042; CAA39513.1; -; Genomic_DNA. DR PIR; JQ1145; OYBYK. DR HSSP; Q99280; 1FX4. DR BRENDA; 4.6.1.1; 274780. DR GO; GO:0004016; F:adenylate cyclase activity; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IEA:InterPro. DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0007242; P:intracellular signaling cascade; IEA:InterPro. DR InterPro; IPR001054; A/G_cyclase. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR001932; PP2C-related. DR InterPro; IPR014045; PP2C_N. DR InterPro; IPR000159; Ras-assoc. DR Gene3D; G3DSA:3.30.70.1230; A/G_cyclase; 1. DR Gene3D; G3DSA:3.60.40.10; PP2C-related; 1. DR Pfam; PF00211; Guanylate_cyc; 1. DR Pfam; PF00560; LRR_1; 10. DR Pfam; PF00481; PP2C; 1. DR Pfam; PF00788; RA; 1. DR SMART; SM00044; CYCc; 1. DR SMART; SM00369; LRR_TYP; 2. DR SMART; SM00332; PP2Cc; 1. DR SMART; SM00314; RA; 1. DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1. DR PROSITE; PS50200; RA; 1. PE 3: Inferred from homology; KW ATP-binding; cAMP biosynthesis; Leucine-rich repeat; Lyase; Magnesium; KW Metal-binding; Nucleotide-binding; Repeat. FT CHAIN 1 1839 Adenylate cyclase. FT /FTId=PRO_0000195732. FT DOMAIN 494 574 Ras-associating. FT REPEAT 632 655 LRR 1. FT REPEAT 659 679 LRR 2. FT REPEAT 680 702 LRR 3. FT REPEAT 703 724 LRR 4. FT REPEAT 726 748 LRR 5. FT REPEAT 749 771 LRR 6. FT REPEAT 773 793 LRR 7. FT REPEAT 794 818 LRR 8. FT REPEAT 820 833 LRR 9. FT REPEAT 834 857 LRR 10. FT REPEAT 859 879 LRR 11. FT REPEAT 880 903 LRR 12. FT REPEAT 905 926 LRR 13. FT REPEAT 927 949 LRR 14. FT REPEAT 951 974 LRR 15. FT REPEAT 1004 1025 LRR 16. FT REPEAT 1026 1048 LRR 17. FT REPEAT 1050 1072 LRR 18. FT REPEAT 1074 1096 LRR 19. FT REPEAT 1101 1124 LRR 20. FT REPEAT 1135 1160 LRR 21. FT DOMAIN 1185 1440 PP2C-like. FT DOMAIN 1483 1620 Guanylate cyclase. FT METAL 1488 1488 Magnesium (By similarity). FT METAL 1531 1531 Magnesium (By similarity). SQ SEQUENCE 1839 AA; 206896 MW; 86A69BCB1F2733CB CRC64; MSSPTDAERV NMRREKHPQI EETFEEHVHN AMPKFKKHYA LGITTHTNDE DDDPRDHRQR GIHNPNFIHS PNDPRPPLSQ PIKPRFSVHG TASNASVFSH GDIAPVRKTS RAGSLFKRLA GKKSTTSLLG TEHQQRQQQQ SSNSLVPAAG LRRKMSTFIH GGSGSQSNES RGTRSSIFFP STSNSRRGSA TSTMTSGSRS SHPPDTPPIT SQQQEQQYDQ QRQQRPETRE QEQKPPTLSD MPIVSRSPSF FMLDTDLNNL SDITNIISAT PKNTESDEVR STGANKTLKY PKPPLSSHKS TSASDLSHHK AQWTAPESWD IEEDANKLLA TKRKAKHHHH YHHPQHPRPP HRKHYSNFSK PIEDKAVVEK EQEPPEKCPQ PISTDSNDAQ GLEIAKPIDE SSGIQHSAST QSVSSFSSGA TGASGATGKQ IGGDQETEST ISTVGEDEEV TNLRSIDSEQ TDDTSFSKFD EEYDKAEYQL EKYYNDFSDV DLNRRYAIRI FNIDDTFTTL SCTPNTTLQD MMPQLKRKFN VGQGSYQVSL KVGKLSKILR PTAKPILIQR RLLLLNGYLK SDPLHIMGIE DLSFIFSFVF HPVATSHLNY EQEQRLSRGD FVHVDLRNMD LTTPPIILYQ HTSDIESLDV SNNANIFLPL DFIESAIKLS SLRMVNIRAS KFPANVTDAY KLVSLDLERN FIKKVPDSIF KLNNLTIVNL QCNNLERLPP GFSKLKNLQL LDISSNKFVN YPEVINSCTN LLQIDLSYNK IHSLPVSINQ LVKLAKMNLF NNRLTSVGDL SQMKNLRTLN LRCNRVTSIE CHAPNLQNLF LTDNRISTFD DDLTRLRTLE LQQNPITSMV CGGNYMANMT SLSLNKAKLS SFSAELLSKL PRLEKLELNE NNLTQLPPEI NKLTRLIYLS VARNKLESIP DEISDLRSLK SLDLHSNNLR MLMNNLEDLE LTSLNVSSNL LTGFHGSPAK FFASPSPKLA KSLLFLSVAD NNLTDSIWPL VNTFQNLKTL NLSYNNFVEI SDLKLQNLTE LYLSGNNFTS LPGEAVQHLR SLKVLMLNGN KLLSLPAELS QLSRLSVLDV GSNQLKYNIS NYHYDWNWRN NKDLKYLNFS GNKRFEIKSA LDPEGKNDLS DLGILKQLRV LGLMDVTLKT SKVPDESVSI RLRTTASMIN GMRYGVADTL GQSDSVCSRD VTFERFRGRE DECLICLYDG KNENASSGHK ISKIIRDIYD KILIRLLEKY GEESDGIKRA LRYSFLQLNK EINGMLVSVE DGNTDSGLTS ADLLSGSSAT VVYLKGKKIY TANIGDTMAV LSKNNGDFVT LTKLHVPAER EEYERIRTSG GYVNNQKLDG VSEVSRAVGF FDLLPHIHAS PDISETVLSY SDEMLIIATH KLWEYLDYET VCDISRENKS QPMSAAEKMK DYAISYGCSD NITILCVSLD KSVNQQSQFT LNREDLISRK NTFEDTVLRR LQPEIAPPTG NVAIVFTDIK NSTFLWELFP DAMRAAIKTH NDIMRRQLRI YGGYEVKTEG DAFMVAFPTP TSALVWCLSV QLKLLEAEWP EEITSIQDGC LITDNSGTKV YLGLSVRMGV HWGCPVPEID LVTQRMDYLG PVVNKAARVS GVADGGQITL SSDFCSEFKK IMKFHKRVVE NQEPLKEVYG EDFIGEVLER EIHMLENVGW VFKDLGEQKL KGLETKEFIT IAYPKTLASR HDLATKNQNS SVLNDDLLFQ LRTISNKLEN ILSSINGGLI ESETPGNSSI YMTFDKNTKD AVITKSTESD WISFLDHLVT RVESTVAILQ LRQKLQGGLE LYTSSDSTMH KSVFELLDEI LKIQTDQKQ //