CYAA_LACKL
ID CYAA_LACKL Reviewed; 1839 AA.
AC P23466;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Lachancea kluyveri (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX 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 metabolism by
CC catalyzing the synthesis of a second messenger, cAMP.
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 -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X56042; CAA39513.1; -; Genomic_DNA.
DR PIR; JQ1145; OYBYK.
DR AlphaFoldDB; P23466; -.
DR SMR; P23466; -.
DR PRIDE; P23466; -.
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:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
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 CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR000159; RA_dom.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51450; LRR; 18.
DR PROSITE; PS51746; PPM_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
FT /note="Adenylate cyclase"
FT /id="PRO_0000195732"
FT DOMAIN 494..574
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REPEAT 632..655
FT /note="LRR 1"
FT REPEAT 659..679
FT /note="LRR 2"
FT REPEAT 681..702
FT /note="LRR 3"
FT REPEAT 704..726
FT /note="LRR 4"
FT REPEAT 727..748
FT /note="LRR 5"
FT REPEAT 750..771
FT /note="LRR 6"
FT REPEAT 773..794
FT /note="LRR 7"
FT REPEAT 795..816
FT /note="LRR 8"
FT REPEAT 817..834
FT /note="LRR 9"
FT REPEAT 835..856
FT /note="LRR 10"
FT REPEAT 858..879
FT /note="LRR 11"
FT REPEAT 882..903
FT /note="LRR 12"
FT REPEAT 905..926
FT /note="LRR 13"
FT REPEAT 928..950
FT /note="LRR 14"
FT REPEAT 951..971
FT /note="LRR 15"
FT REPEAT 982..1004
FT /note="LRR 16"
FT REPEAT 1006..1027
FT /note="LRR 17"
FT REPEAT 1028..1048
FT /note="LRR 18"
FT REPEAT 1051..1073
FT /note="LRR 19"
FT REPEAT 1074..1096
FT /note="LRR 20"
FT REPEAT 1103..1124
FT /note="LRR 21"
FT REPEAT 1135..1160
FT /note="LRR 22"
FT DOMAIN 1173..1439
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT DOMAIN 1483..1620
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..355
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1488
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1531
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
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
