ID A0A0D7AZ15_9AGAR Unreviewed; 1842 AA.
AC A0A0D7AZ15;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Adenylate cyclase {ECO:0000256|ARBA:ARBA00021420};
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=CYLTODRAFT_493767 {ECO:0000313|EMBL:KIY63613.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY63613.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY63613.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY63613.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC -!- FUNCTION: Plays essential roles in regulation of cellular metabolism by
CC catalyzing the synthesis of a second messenger, cAMP.
CC {ECO:0000256|ARBA:ARBA00003896}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; KN880684; KIY63613.1; -; Genomic_DNA.
DR STRING; 1314674.A0A0D7AZ15; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000054007; Unassembled WGS sequence.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
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; Nucleotide cyclase; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR000159; RA_dom.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00481; PP2C; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 10.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51450; LRR; 5.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50200; RA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054007};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 435..534
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1153..1430
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1477..1613
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 74..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1842 AA; 205434 MW; AEE1C66911BA59C3 CRC64;
MSSEIELFRI YDVVDGTGQS TIMPEIDLPS AKNVDIAPWE EPPTPQAHTP KSRSFGFAHK
ASFNSFRPGS FASMGHRGRL GSDTQSTLSI PESLSSTNTD SPSEFGVQPS LRKSRSGVFN
FMRPNRSKAS LRPDGAEHPS LRPPPVPDNS AYAPFLPVAR SPSPSLRPSP PQKAEQASKR
IRKHSKRKED THPPTPPPKD EELHLDTNLS DLDGIVDPSL WRSENNAEPQ VSPATSTFPA
TSASSQRSHS RHGSSDHSSM HSHSMGIPEF RDPFKVQPLT LKSFPPRMTS LKHQGYAPTE
RKISPKTVPP APSPIPLSRP ANVSEDANQP AWIAPESWAV QADTENLSEQ EYSSGAEEAT
FATVTNDTMT VSTTARPSSS AASFSSRTPS LRNNDIDAAL PPRMNPHQRS GSSKTKGSTA
STVMQKSMSF PDRERVYTIR IYTSDNAYHV VSVGPNVTVG SLLPKLNQKL LHGEDREKHK
LYLKDRARER VLHTNERPAD IVKNRLMQAG YDLTDIASML GGESLSFLLR FIYKSEVLGT
TEKDIVFDNY EYVDLTSKGL RAIPVDLHKH ADSVVSLYLS RNPMLEIPLD FIQDCTTLRE
LRLSHMAMRK VPNSVRHSHT LHRLDLSCNK ISELDDAQLH LIPTLHHLFL QNNRLENLPL
YFPRLRSLCT LNLSNNQFLS FPVVICQLET LKDVDISFNS ITEIPEEISK MRCLERLIVV
SNQIVVISPA FSRLTNLRQF DCRRNHIEDL TVVCSLPHLE KLSADHNALL TLEVLINPYM
QSLDVSRNDL SKGKFTLIPH PPPNAPGYSL QYLELSHTSL THFDDNIFTQ LTSLRTLKFS
HNNLKALPDS LGELRWLETL ICSDNQIETL PGTIGLLQKL ETLDAHNNRL RDLPDSLWEC
ASLLKVNFTS NLLTMWKVPP SMRAGSVGDL SIRVERKGSA SSQTGRQRPP LAYSLEKLYL
GENKFSDDVL SPLLVLEGLR VLNLSFNHLQ ELSPSFFKYF PKLEELYLSG NELTALPGDH
LARMTSLSVL FLNGNKLQTL PHELGKVKSL TVLDVGSNLL RYNINNWEYD WNWNFNKNLK
YLNMSGNKRL QIKSDTREFF NKGDARQSLA GFTDLAHLRV LGLMDVTTAG IGVDIPDEND
DRRVRTSTVS GMGYGIADTM GRNEHLNMLD LVHEFPGRPG EMVFGMFGRA HPPRALSNGS
MSNRLAKHLH DRFVDVFLSH LTSLRYDEGV PDALRRAFLR LNHELHDNLY AVPVRKGSTA
SGAARPSAAE QTLQSRSGAS GLILYIAGKK LYCANAGNIL AVVSRSGKAH SLSTKHDPYD
RDEMERIRLT EGWISPPGLV NDEIDLSRSF GFFHLFSLIA RPAVQVWDLG ELDEFVIMAN
RGLWDYVSHQ TAVDIARGER DDPMIAAQKL RDFAMSYGAD GSTMIMIISV GDLFKAAQPL
PDPLQHINRR RRRADDTLDV AITRLGAEVP APTGHITMVF TDIVNSTGLW ELNPGMQSAL
AQHHKLLRRH LRLCGGYEVK TEGDAFVISF QTAVAAMWWC MTIQQELLKT EWPLELLECD
DGKPVYDNNG ILIARGMSIR MGVHCGEPIC EMDPVTRRMD YYGPMVNRVA RIEQSASGGQ
IQVSSDVLKE LQEFKAIGTD GADLDHLTDP HLAEAVEAVR RIGIVVVPVG QVKLKGLETT
LHLSTIYPEE LAGRKEVRAK PANARVQFSI EQMRQLGTLC LRLEALATSR IFKSEEDTPK
ERDGRVRDSG ILDGEQVGRQ SKFLCGNPSL LLPEMRENMS GREMMLLLDS MAGRIENAVR
SITLNVKGKQ EAMKDSLGAA LLTQGGLDME TLQKVLNVLR GI
//
