ID A0A0F4GYS9_9PEZI Unreviewed; 2081 AA.
AC A0A0F4GYS9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=TI39_contig293g00009 {ECO:0000313|EMBL:KJY01371.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY01371.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJY01371.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJY01371.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJY01371.1}.
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DR EMBL; LAFY01000285; KJY01371.1; -; Genomic_DNA.
DR STRING; 1047168.A0A0F4GYS9; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000033647; 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; PF13855; LRR_8; 3.
DR Pfam; PF00481; PP2C; 1.
DR Pfam; PF00788; RA; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 9.
DR SMART; SM00365; LRR_SD22; 8.
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; 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:UP000033647};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 574..665
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1364..1642
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1703..1840
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2081 AA; 230438 MW; BA34B93C34862D6B CRC64;
MTLRNSTADG KRHGSTGAES SRSVDTVRGP FASFSTVKGL GKLHTKRQLE RQDSEVSPST
LVPKPTPTNA RGDIAPWENT PPRDEQMSKQ PHMSTPPAKD RNRRRQPPAM LPMPAWATDK
TAQVPSVFQG SFFGNDSNDN LGQISPGYNP PGGAMGFPGD GEDRRPSIAS LTTVSSAGSK
SSAGGGRVHK KLQGFFGDDV TLPGVISEAS RQNSEASSIR NGASSALASG GRPGLRNNSF
NDAMMRSGPP SPSFSRPRTP NPQPVSEVTP WVVQDPENAP DSFFPTGASN GKSSKNSTAS
RLHLPGHRHN RSNDERQSGG FPLRPATSRE QSFSGMRKEP APTSRSAALN LKHTRSISPA
PSERSVRSHQ TAQRSPTNSQ APKRSLLDRV TRRHKPPERQ GPVTMQQSSS VTSLPCLTQA
STKGRSERAD SKAVSKPVTK SKTDLASMGA TPRKEHRLPF KSKKTDTFPT EANRPVKDPN
ESHAVAGEAL WHLDTDMSHM EGIVDHKQPL MTPPTGEIYA GWPPEQEPVE LTTEATGAWD
APDSWAVNKV ADENLRRLTE LDDDGNVPTD DSGPMYFMRI FRADSTFAVI SASLNTTAAE
LISMMAKKTF LQDELDKYQI IMRKQDTSRQ LAPGERPLVI QKRLLEMAGY QEQDHLEDLG
REDHGYLCRF TFLPSKMSGY SSLERDPGFN KMQRFNHIDL SGRNLITIPI TLYQKATEII
TLNLSRNLTL DIPKDFIQSC SQLREIKYTS NEAWRVPPSL SLATRLTTLD ISNNRLEQLE
HADLHKLQGL LSLKLSNNKL ANVPPYFQQY RALRSLNLSS NSLTEFPDAL RKLTTLIDLD
ISFNSISNMG DVSTLVNLER LWATNNKLSG PFHKSFSSLV SLREIDARFN AISNIDVVSQ
LPKLEALMLG HNSISQFEGS FHCLKVLFLN HNPVTNFDLN SPVPSLSVLN LASAKLAQLP
DALFMKMSGL TKLTISKNHF VSLSPNFGLL QKLEYLSIAK NELSRIPPEI GRLTELRYLD
VRENNLGMLP PEIWYAKRLE TLNVSSNVLQ DFPKPGSPLP PLPDAPVTLT PSTLVPNSGG
SPDFEELGKL EDFQLRRPSQ VAGMMSTSSS PGSNSRKGSV VSYHSGKSNA LARGSTASSV
GTVTPGGPPR KDSTLSSRLA ATFSSSLRHL FLADNRLEDD VFNELVLLPE LRILNLSYNR
LYDVPTRTIR KWTHLTELYL SGNDLTSIPS EDLEEGSSLK VLHINNNKFQ VLPAELGKVQ
RLAILDVGSN MLKYNVSNWP YDWNWNWNRQ LRYLNLSGNK RLEIKPASQA STERGQRDLT
DFSSLINLRI LGLMDVTLTI PSVPDQAPDR RVRLAGSVIG TTMPYGMADT LGRNEHLSTL
DMVVPRFRGH EDEALIGLFD GQSLSSGGSK IAKFLHEKFK HYFIEELEKT KPEENPIDAL
RRTYLALNKE LATAATQAID AKGHPSSALV HRGSVVGPEL GEDDLTSGST ATVMYLHGME
LYMSNVGDAQ ALLIQSEGGH RQITRKHDPA EASERQRIRE AGGFVSRQGK LNDQLDVSRA
FGYVQLTPCV IAEPYVSKVD IKESDEMILL ASRELWDYLT PDFAVDVARS ERADLMRAAQ
KLRDLAIAFG ATGKIMVMMI GVSDLRKREK ARFRTHSMSM GPSGSPDDYF TTVRKAKRGR
DAVGDSRLAR LDQEVDAPTG EVTLVFTDIK NSTILWETYP IAMQSAIKMH NEVMRRHLRI
IGGYEVKTEG DAFMVAFPTV TSALLWCFTI QSQLLEVQWP QEILNSVHGE EMRDGDGNPI
FRGLSVRMGI HWGRPVCEID PVTKRMDYFG PMVNRAARIE SVADGGQICV SSDFIQEVQR
MLESHIESDR STSTGSEDTL NDDIMSQTIR RELRSLSSQG FEVKDLGQRT LKGLENPEYI
YLMYPHSLAS RLVVQQQKAE AESRAHIASE KEAKKTRNSQ LTIDTDNVWD LWNVSLRLEM
LCSTLESPGV KSLRAPETAL LERMKHGQGA GEITDRFLVN FVEHQISRIE TCISTLAIRN
MIRPFAKGML SQACPMEDVL GDLTAQLSEL KTLKAAAAAD Q
//
