ID A0A317X0K9_9EURO Unreviewed; 1947 AA.
AC A0A317X0K9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BO94DRAFT_583742 {ECO:0000313|EMBL:PWY91815.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY91815.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY91815.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY91815.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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:PWY91815.1}.
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DR EMBL; MSFK01000008; PWY91815.1; -; Genomic_DNA.
DR STRING; 1450535.A0A317X0K9; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000246702; 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; 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-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; PF00481; PP2C; 1.
DR SMART; SM00789; Ad_cyc_g-alpha; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 7.
DR SMART; SM00369; LRR_TYP; 9.
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; 1.
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:UP000246702};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 409..497
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1197..1475
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1533..1670
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 26..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1905..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1905..1935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1947 AA; 216867 MW; F78F62CDD98C3897 CRC64;
MTVSSQGSKS SAGALFRKKL QGFFGDEYVG NGESRHDSDN FTQSSATKPS SLDHFRARER
ANSDGSRNSG ASQAQNQARS QTPLPSSDIT PWLYQSYHDI PQYGEAPVRE APTAATDSQR
GSISQKDQSR RHFSGHRHSR SKEEKPTAAG DLAGYSSRPA TGRDDLSLEL RPSREGSLNH
VTPMTSSTTL VGRSTSPTPS VQSAYSREQG QNSPGTQTSK RSFLDKIRRP KHGHLKNITG
SKTVQDTTKA ASSKLSRREA SPARRGRQGS IESGTSSRLT ETGDSERRKD SKGLAISSTK
LRGRRGHGNE FPSAVELRKP GVPNMWALDT DLTHMEGIVN PPSPGAQSKM FDGASIRSEE
TRRPDTMPAG NWDAPESWHV KKNEPSNLLP QDTSEPGPTI SEPGGSNWYI RVFRQDATFA
TLSGGLYSTV SELVQLLSRK SFFSDPTANY ELIMQKNGLS RQVDQTEMPI LMQKRILEQV
GYTEKDRIEE VGREDHSYIL RYTYLPIRIS GSVIEGHDPP LGKTQQKFSH VDLTNRNLLT
IPIGLYKKAA EIISLNLSKN LALDVPKDFI QGCINLREIK FMGNEALRLP ASFGLASRLT
YLDVSNNCLE DLTHANLDRL HGLVSIKLAN NKLTNLPSYF GNFQYLRSLN ISSNSFHVFP
ELLCRLKNLV DLDISFNNIS GLLHIGKLTT LERLWMTNNI VRGALDDTFR DLVNLKEIDA
RFNEVTNIDI LCFLPRLELV DVGHNSISKF KGSFPKLRAL GLDHCPMTQF DIDAPVPTLR
SLNIASAKLV QFRDSLFDNL PNLQRLILDK NHFVSMSPHI GKLRKLEHFS MIKNPLAALP
ATIGCLTELK YLNLRECNLR KLPPELWHCL RLETLNVSSN VLDVFPKHGC PQPQPPSEVA
GTPAATPGIS TTPSYEELGA LEEQEARRPS QASGGALSTG NSPNGGTYRK PSVASSLGQG
RKVSAASRSL TDGSPSSRKD SNFSQHVATT FAGSLRNLYL ADNRLEDDIF RELSLIPELR
IVNLSYNELT ELPQGLLRRW PLLTELYISG NELISLPSDD LEEGSNLKVL HINANRFQVL
PAELCKVAKL AYLDAGSNSL KYNVSNWPYD WNWNWNRNLR YLNFSGNKRL EIKPPGSSLS
NHPQSSKQQP PYLTDFTSLT HLRVLGLMDV TLTITTIPEE NEDRRVRTSA SLAGALAYGM
ADFLGKSDHL SIFDMIVPRL KPDKVETVVG MFDGQSQTGG GSRIAKFLHE NFVHTFNSEL
KRIRSEQHET ALDALRRAFL TLNKNMAFAC YKSLDQDVRQ YQEDSTDQRR VRLNKDDINQ
GGVATVMYIN NMDLYVANVG DAQAILVKSD GSMRHLTQNH DPAEAHERER IRAAGGFVSR
TGKLNDVLTV SRSFGYFHMM PAIIAAPHTM HVNLTEQDEM VILASRELWD YVTPDLVVDV
TRAERRDLMI AAQKIRDLAL SFGATNKLMV MILGVGDLKR REKIRTRPSL SMVGPPEEQI
IPSVKRTKKP RDAPGDSRLA RFDYVDAPVG ELAIIFTDIK KSTSLWETCP DAMRSAIQIH
NDILRRQLGI IGGYEVKTEG DAFMVAFSTT TAALLWCFNC QTQLLEAEWP TEILEQPQCQ
VVCDSENNVI FRGLSVRMGS HWGEPVCEKD PVTNRMDYFG PMVNRASRVS AVADGGQIFV
SSDFMSDIQR NLEIFADSER AASTGSEESY AFDTLGNNIR RELQQLNSQG FVIKDQGERK
LKGLENPEPL YLIYPHALSG RLTTVDKDTS NELAPTTISK HSQLEIQTDL IWRLWEITLR
LERLCAALEY PGEALLKEPN VALFNVVKNH GGELADSTVI SLVEQQVTRI EVCITTLSVR
NMIRPFRPGD RLNDHAMPIA DVMQQLQSQL TEYRALKEQI DASAGTATSY THDPQYSNGE
SNSDSASSSY LQMGPPSDEF NPGGPRR
//
