ID J4GWM7_9APHY Unreviewed; 1771 AA.
AC J4GWM7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=FIBRA_08354 {ECO:0000313|EMBL:CCM06105.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM06105.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM06105.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM06105.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
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; HE797224; CCM06105.1; -; Genomic_DNA.
DR RefSeq; XP_012185388.1; XM_012329998.1.
DR STRING; 599839.J4GWM7; -.
DR GeneID; 24101016; -.
DR HOGENOM; CLU_000430_1_1_1; -.
DR InParanoid; J4GWM7; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000006352; 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 CDD; cd17214; RA_CYR1_like; 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; 2.
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; 3.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 10.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF52058; L domain-like; 3.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51450; LRR; 3.
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:UP000006352};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 377..480
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1145..1383
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1426..1562
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 76..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1771 AA; 195649 MW; 6996BF687923B27B CRC64;
MSTTTTHSRP AAVGLAPQYP YLAMSPAPHY TPSSSVISLG VSELSAVPQD VPVLHPQDLL
PHAPPNDADN VVIAPWLASP DDEPPTPPPK PQRYGFPHKS SFASFSLPRQ LSASNLSLAT
TRSSESHVLH SSSLGHDTHH SREPRRAKSS ISSILTHPLS NFVKKQRSRS RLRSDVALSE
EPVPPLPIFD HLSTYSAAST APSLLKHRKH KIPSISSESP PPVGDAEFKL DVDLDRMEGI
IDPHILSAPD SGSPRSGGFD NSSSEVSSTH HSLGASSSNI FSHPHPFGPP TVRVQRYHYD
GRRISPTSRP ADFPDDDTRS WAPPQSWEVD QEGGATTIAE ESSSDENEPG PPRKPGRLRP
ESKIRPRPPI KSASSSALYK IRIYRANGTY HVVSISLAVT VDELMPELNK KLSLNPDREP
HSLYLKERGR ERVLAPTERP ANIVRRRLDQ AGYEEADSLE QLGAEDLTFL MRFVYKSNVL
GLSNADDHNI DTFDMIDLTG RGVRTVPILL YPHADAIVSL NLSRNPMLEI PLDFIQACTT
LRELRLSQMA MKKVPQSVRY RDTLHRLDLS CNRIGDLDDA GLDWIPELRS LKVQNNRMES
LPWWFPRLGA LKDLNISNNK FGALPSVVVE ITGLVDLDIS FNMIDKLPDD FGRLQSLERL
IIVGNQVTEF PSSCSGLVNL RMLDCRRNNI SDLSVVCRLP KVQQIFADHN SVHALDVSFG
PCLKQLDASH NDFTQLLLLP GPVGQPYALT SLDISHSKLS ALDELALAHL TALETLHLDH
NSLRYIPESL GALTRLVHLS CSNNQLRALP ASISRLYNLE TLEVHNNSLA ELPSTLWNCE
NLHLINATSN LLGSWSLPSG SDVGRRAGVN GTTQNGPVPV RSDSSSVRKA SSANSIMCIE
KKWPPIVNSL HRLYLGENQF TDHAVHPLAL LAELRVLNLS FNELQEIPPS FFEKLTSLNE
LYLSGNKLST IPTEDLHRLT KLEVLFLNGN KLQTLPKEIG KLTNLIVLDV GSNILKYNIF
NWEFDWNWNF NTSLQYLNLS GNKRLEIRTD IAPVKHDEKR KILADFSSLT QLRVLGLMDV
TATNGAIIPD ENEDRRVRIS LSEINGVGYG IADTLGATEH LTMLDLVQPK FRANNDEAIF
AMFGRATHTG NNYWLNHYLQ SNFLDVYSGE LAHLRPEKGE GIPDALRRAF LQLNKHLHDF
LYSNSSARKM SQVSTSTGNA VIRDMNKRCG ASGIVLHLVG KTLYVANAGR SLAVMSRQGN
AMLLSRLHDP FARPEITRIR NAEGWVSPKG YVNDEVDVAR SFGFYSLLPV VNARPHICTW
DITAQDEFVI VGNSGLWDNV PYQTAVDIAR SNCGNAMIAA QKLRDLAISH GAEGSAMIMV
IAVGDLYPAN DAGSILSAKP TKRPEIINRD ISRLGDEVPA PTGHVALVFT DIRNSTHLWE
VNAGMPTAMI LHNNLLRRQL RFCGGYEVKT EGDAFMCSFP NTMSALWWCL SVQVQLLYVD
WPLEILECED GKEVYDVEGN LVARGLSVRV GIHCGKPVCE PDPITGRMDY FGPMVNRSAR
IEGSAAGGQI MCSADVVREI NARIFETEPP TPYSHLEPPQ VVDAIRRIGL IVVQVGEVKL
KGLEVPEMLS IVYPQALAGR RGLSLVQTTS NPPGRVQFSI EQMGELALLC IRLEMLSAGK
TFRASSNAPN QGNEESDSAV FSHRELKALL PAMDKATDAD LMLLLGSLTT RIDNALTKLA
ATRLRACRDK VPLADGLDGR YLNQLLEILC P
//
