ID Q0TX81_PHANO Unreviewed; 1717 AA.
AC Q0TX81;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 102.
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=SNOG_15891 {ECO:0000313|EMBL:EAT76729.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT76729.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445365; EAT76729.2; -; Genomic_DNA.
DR RefSeq; XP_001806026.1; XM_001805974.1.
DR STRING; 321614.Q0TX81; -.
DR EnsemblFungi; SNOT_15891; SNOT_15891; SNOG_15891.
DR GeneID; 5982956; -.
DR KEGG; pno:SNOG_15891; -.
DR VEuPathDB; FungiDB:JI435_158910; -.
DR eggNOG; KOG0618; Eukaryota.
DR HOGENOM; CLU_000430_4_0_1; -.
DR InParanoid; Q0TX81; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; 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 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; 4.
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-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; PF08509; Ad_cyc_g-alpha; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00560; LRR_1; 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; 11.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00314; RA; 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:UP000001055};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 302..393
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1099..1376
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1411..1549
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1717 AA; 191289 MW; EA53BE84B3DE7036 CRC64;
MMRLPGHNHR HKNSKEDNVT AESRTDISQP YPLRPATSRE DSSFSVRQGS QYTSAISSAL
NSKTNLSARP SSPTPSALSD MARDTGASQR SPSTTKSHGL FARLRGRDKD KDKKDRSGPP
DNLKNLGVTG NISVTSLNPS INSAKFTRAE PSPQSQMSRA NVQNGASDKI SMKDARRGHH
ARLPTFRKEK RVPTNELPPV GRDPNQATEN VNSDAVFYLD RDLNNMEGIV NTQHPPMTPP
IGELQKQPTF PGDELPNPAA PEDEAAWDAP DSWAVKRTRE DGSLYGEVDE HGDPVQEQTD
TKTYCLRIFR VDSTFATLSA TLNTTVQEII QILGKKTVLQ DELDNYHIVM RKHDTSRQLE
SNERPLFIQK RLLEQAGYTD LDRLEDVGRE DNSYLCRFTF LPAKMSGYSS LERDPGFSKM
QKFSHIDLQG RNLITIPITL YQKATEIISL NLSRNLSLDV PKDFIQACTN LREIKYTSND
ARRLPPSLSL ASRLTMLDIS NNRLQSLDRS ELHKLQSLQG LRLSNNGLTR LPSYFGQYRA
LRSLNLSSNA LHEFPDFLCE VRTLVDLDIS FNSITSLPKI GQLTCLERLW ATNNKLTGSF
PSALSNLVNL REIDVRFNAL DSMDVMSQLP RLEYLMIGHN NISSFEGYFP KIRVLHMNHN
PVTRFGLSAA VPSLTALNLA SAKLAQLPED LFGKLTGLTK LILDKNHFTS LSNNIGRLFR
LEHLSVARNS LDVLPAEIGR LIELRYLDVR ENNLSHLPME IWYARRLETL NVSSNVLDSF
PKPGAAPPAA VTNGEVANLD GAMPMPAPSL TTTPSYEELG KLEDFQNRRP SQASGGQLSL
GTSSGSSQRK GSMASYSTTG TARKPSVASR APTEGTLTPM SRKDSSLSSR LVTTFAGSLR
HVFLADNRLT DDVFDELCLL PELRIVNLAY NLIYDVPSRT IRRWQHLAEL YLSGNDLTSL
PSEDLEEVGS LKVLHINNNK FQVLPAELGK VAQLAVLDVA SNSLKYNVSN WPYDWNWNWN
HKLRYLNLSG NKRLEIKPSG SYSGSGVNMR EGRDLTDFSS LTNLRVLGLM DVTMMVPSVP
EQSEDRRVRT AGSAVGSMAY GMADSLGRNE HISTMDMVVP RFRSHDDEQV LGLFDAQPLA
GGGSKIAKYL YDHFKNRFAD ELDRLRPQES PSDALRRTYL GLNKELATVA SQTLEKNGYT
APQGQGHRAS VPELGDDDLT SGSVATVLYL KEMELYISNV GDAQALLIRS EGGHKILTRK
HDPAEPSERA RIREAGGFVS RQGKLNDQLE VSRAFGYVQM SPSVIASPHL MNVTLGDTDE
MILVASRELW EYLSPDFAVD VARSERGDLM RAAQKLRDLA IAFGATNKIM VMLLGVSDLK
SKQRARNRIW VGDSKLARLD NEVDAPTGEV SLVFTDIKNS TLLWETYPIA MRSAIKMHNE
LMRRQLRIIG GYEVKTEGDA FMVAFRTVTS ALLWCFTIQS QLLEVQWPQE ILNSVNGQEV
VDPDGNVIFR GLSVRMGIHW GTPVCEVDPV TRPRVSKSKT LVSGASRVLR IPEYIYLMYP
HSLASRLAVQ RQTAEQKPAP ANEAQVGQKM ANSQLTIDTE DVWDLWNISL RLEMLCSSLE
SPGCSELKPP ETALLERMKS RGGEITDRFL LNFVEHQISR IESCANTLAL RNMVRPFGAA
PLLDQACHMG DIFAELEAKL QRLALFEKGV LEDMAPS
//
