CYAA_PODAS
ID CYAA_PODAS Reviewed; 2145 AA.
AC Q01513;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Adenylate cyclase;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
OS Podospora anserina (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX NCBI_TaxID=2587412;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8621071; DOI=10.1016/0378-1119(95)00847-0;
RA Loubradou G., Begueret J., Turcq B.;
RT "An additional copy of the adenylate cyclase-encoding gene relieves
RT developmental defects produced by a mutation in a vegetative
RT incompatibility-controlling gene in Podospora anserina.";
RL Gene 170:119-123(1996).
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}.
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DR EMBL; L43413; AAB05642.1; -; Genomic_DNA.
DR PIR; JC4747; JC4747.
DR AlphaFoldDB; Q01513; -.
DR SMR; Q01513; -.
DR VEuPathDB; FungiDB:PODANS_1_3040; -.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; -; 3.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR013716; Adenylate_cyclase_G-a-bd.
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; PF08509; Ad_cyc_g-alpha; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00789; Ad_cyc_g-alpha; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00369; LRR_TYP; 12.
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; 17.
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..2145
FT /note="Adenylate cyclase"
FT /id="PRO_0000195729"
FT DOMAIN 637..727
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REPEAT 779..800
FT /note="LRR 1"
FT REPEAT 803..824
FT /note="LRR 2"
FT REPEAT 826..847
FT /note="LRR 3"
FT REPEAT 850..871
FT /note="LRR 4"
FT REPEAT 873..894
FT /note="LRR 5"
FT REPEAT 896..917
FT /note="LRR 6"
FT REPEAT 919..941
FT /note="LRR 7"
FT REPEAT 943..964
FT /note="LRR 8"
FT REPEAT 965..986
FT /note="LRR 9"
FT REPEAT 987..1006
FT /note="LRR 10"
FT REPEAT 1007..1028
FT /note="LRR 11"
FT REPEAT 1030..1051
FT /note="LRR 12"
FT REPEAT 1053..1074
FT /note="LRR 13"
FT REPEAT 1076..1097
FT /note="LRR 14"
FT REPEAT 1099..1120
FT /note="LRR 15"
FT REPEAT 1235..1255
FT /note="LRR 16"
FT REPEAT 1259..1280
FT /note="LRR 17"
FT REPEAT 1283..1304
FT /note="LRR 18"
FT REPEAT 1307..1328
FT /note="LRR 19"
FT REPEAT 1330..1352
FT /note="LRR 20"
FT REPEAT 1359..1380
FT /note="LRR 21"
FT DOMAIN 1432..1709
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT DOMAIN 1773..1910
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1718..1760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1725..1739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1741..1757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1778
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1821
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2145 AA; 237517 MW; 88E7EF6E4AC0687D CRC64;
MPRNDASSRF SSMTGSSTDS ARSNITVKPL PSLPPSASSS SPFAASSNQT SNASRSASHG
SRRAAPSRLK TDENGQLSRS FKDSDAQVSP TSTSPCVSPS SITSSNSIRE HRMSDLADYR
RDLAILDPAG GRASRTQQNN PSSGSLSQIA PWMAAAPTPA SSGPLPTSFF NDSTDNLSLS
SQTSPGLRNA TARPSQTTTG STESPETLYF TDERRPSIAS ITTTASSQGS RASGARGGIR
KLQGFFGEEF PGRDSSEISL SHPIVGKEHR SHSYSHARPH RDRNYSNATD HGRDASPASR
PRTPVPKPEV VPFLYQEADD IARYGEAPVR DILSGPDRER FVNDSSQQNN PPKTSGSGRS
GHSIGVHLTG HHHRHNKSNE DPRSLRPTVS REDSTISVPK DRNGSSTMYG TRSRAQSPAP
STTGSYWGHK SGSTDGQTSP GQPKKSFLGR LGRRLKEKDD APDLKKLGPA SQSSLHSRPS
RQELSKADGQ FARGADGKYQ PDVRDGIRPD LARPANGPQT FNKFSLSKKA PRSKTQDDLD
EAIGPTDRQD VGTVFHLDTN LNNMDGILSK PAPLTPMNAH EIFDEVGSGK GSISYPSSNG
AWNAPDSWAV LRDDDAGAQL PDTEDIGSPP RPEEKQHNYC IRVFRADGTF ATLQMPLLTS
VSELINQIVK KSYLQDPDKF KLVLKKHDLY KVLQSTDRPL LLQKRLLEQV GFEERDRIED
IGREDNSYLC RFLFYPFTDN SYEVMDQMEF LRSQKNNHID LSGRSLSAIP VQLYPRANEI
ISLNLSRNLS LQVPRDFISV CPNLRDIKFN NNEARALPKS FGYASRLTML DASNNRLESL
ESAALHNLTG LLKLNLANNK LKQLPREFEA FAVLRTLNIS SNLLNNFPPF LAKLENLVDL
DLSFNTIQSL PDNVGQMTSL ERLVITNNEL SGSLPPSFKN LRSLRELDIK YNAISNIDVI
SQLPKLEILS ATRNNISQFS GTFERVRSIK LNWNPITKFE IKAPVPTLKA LNLSNAQLAS
IDESFHNMSN LERLELDKNY FVSLPAHIGN LRRLEYFSIA HNSVGELPPE IGCLTELKRL
DVRGNNIRKL PMELWWANKL DYLNASSNVL ENFPKPASRA PHPPGETNGN TSFPTGRIGP
PTGALSQTPS AEELNDPSRR PSQASSSLLS VGPSPVPGGA DRKSSMVSVY GKGGRKTSVI
SRSTTQSSTA LATPTASSRK DSSHTQRLTN TFAGSLRYLY MADNQLDDDC FDQLCMLENL
RVLNLSYNDL SDMPQRSIKS WPQLVELYLS GNELASLPAD DLEEYSMLQT LHINGNKFTN
LPADISRAKK LTVFDCGSNS LKYNIANVPY DWNWNLNPNL RYLNLSGNRR LEIKQSSVPT
AAQNREQYTD FGRLTNLRVL GLMDVTVLNS TLPDQSEDRR VRTSGSLAGY MPYGMADTLG
SKNEHLSTID LVVPRFNSND SETLLGLFDG QALSSGGSKI AKYLQENFGH IFSQELRDLK
NTENPADALR RSFLSLNKDL IAAGNTHTED RSLMVHRGST APLVLSREDM NSGGVATIVY
IQNQDLYVAN VGDVQAMIIK SDSTHVMLTK KHDPADPNER TRIREAGGWV SRNGRLNDLL
EVSRAFGYLD LMPAVQSAPN IEKHTIGEHD EMILIATREV WEYLPKDVLV DVTRSVRQDP
DPMRAAQKVR DLAMAYGCSN KMTVQMLGVS NLKARRERSR QHKGQSMPVY ASLQDDGGSS
TGMRRARKAR DGPLDSTLGR LDAEVPAPTG LIAIVFTDIK NSTQLWETYP EAMRTAIKNH
NELMRRQLRT IGGFEVKTEG DAFMVSFPTA TSALLWCFAV QCKLLHLDWP AELYNSVNCQ
PVYDRDNNLI FKGLSVRMGI HWGEPLSEPD PVTRRMDYYG PMVNKASRIS ACADGGQIAV
SSDFIAEIQR CLEHYQEPTS TAVDLNEDSF ATAIRSELRS LSGQGFEVKD MGEKKLKGLE
NPEFIYSLYP HALSGRIETH SKHEKEQAQD LREIRPAILS PGSELSVEPD DIWSLWRVAL
RLEMLCSMLE DNSKALQPPE TGLLDRMRQR GGEVSEDFLV NFLDHQVSRI ETCINTIYMR
HLVSQSSIGS NFGALRGPMD EVLKVVAEQF QLVAEYKARY GDLRA
