ID A0A428Q935_9HYPO Unreviewed; 2222 AA.
AC A0A428Q935;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CEP53_004978 {ECO:0000313|EMBL:RSL61801.1};
OS Fusarium sp. AF-6.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL61801.1, ECO:0000313|Proteomes:UP000287544};
RN [1] {ECO:0000313|EMBL:RSL61801.1, ECO:0000313|Proteomes:UP000287544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL61801.1,
RC ECO:0000313|Proteomes:UP000287544};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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:RSL61801.1}.
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DR EMBL; NKCJ01000086; RSL61801.1; -; Genomic_DNA.
DR STRING; 1325737.A0A428Q935; -.
DR Proteomes; UP000287544; 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; PTHR45752; LEUCINE-RICH REPEAT-CONTAINING; 1.
DR PANTHER; PTHR45752:SF149; LEUCINE-RICH REPEAT-CONTAINING PROTEIN 39; 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 SMART; SM00789; Ad_cyc_g-alpha; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 8.
DR SMART; SM00369; LRR_TYP; 10.
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:UP000287544};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 682..773
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1475..1751
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1816..1953
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2051..2070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2191..2222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2202..2222
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2222 AA; 244971 MW; 4DC9D3CF71C2D4A8 CRC64;
MTRNEAGNRI SSITSSSTGT DDSTHSAVTV KPSSSLSSSS TTATATAASS TAPASATSTP
IPTHSPTPNP DHTATATPTP APSSAAAAPA VPGASSASTS TWALPSTSRW HSHPARSSAD
DNASLMNQWS SSKDDHQVSP TATSFAARGI ANVASKDRRM SDLTNYRREL AVLETRIPQI
QHNPPTASPN PHIAPWMNHN GSSTPSSTMP TSFYNDSSDN LSLASQLSPG HPPPNHRQVA
ASHDPPDASY FDGRRPSAAS ILTASSQGSK TSVSRGGFRK LQGFFGEEFP GRDSSESSLP
TSLVGRDQRS RSYSHSRPTH RDRNYSNATD HTRDGSPSSS RPRTPVPAPE VVPFLYQDNT
DIARYGEAPV RDILTGPDRD RYVNDGSSQV PPKTSSSSRS GHSIVHMPGH HRHHKSNDDP
RTLRPTVSRD DTAIGTQLQR DRGGGSVAMY STRSRGQSPT PSTRSGGMTW GSKSGQLDGQ
TSPGHHGKRG LLGRFRRHHK EKEDTARLRD LPQSTRSLQP KTSKPDLHRP ELSPSVLPLS
GTFGPGDQSD VPDSRPGTRG AATFNNKFPF SKKGRSHRPH DYVDESIGPT DRNDPDKIYH
LDTNLNDMEG ILTKPPPLTP MDISFVNNVE ADRTDSVVSI APKGRWDAPD SWAVRRNTED
NSYHGPDLDE IGSPPRPEEK TAPYCIRIFR SDGTFSTHSM SLDSSVTDVI SQVIKKTYVV
DGLENYHIIL KKHDLIRVLT PPERPLLMQK RLLQQVGYEE KDRIEDLGRE DNSYLCRFMF
LSARESDFHA KTTDMGLARA QKLNYVDLSG RNLITIPISL YSKAGEIISL NLSRNLSLDV
PRDFIQSCKH LRDIKFNNNE ARKLPPSLSR ANRLTFLDVA NNRLEQLEHA ELNILTGILK
MNLANNRLKH IPSYFGAYLS LRSLNISSNF LDKFPLFLCN LPSLVDLDLS FNGIATLPPE
ISGLQNLEKL LITNNRLTHA MPASFRQLVS LRELDIKYNG ITSIDIISEL PKLEILSADH
NCVSSFVGQF ESIRQLKLNS NPLNKFEIVA PVPTLKTLNL SNAQLASIDS SFANMINLEH
LILDKNYFVS LPQEIGTLSR LEHFSIANNS VGELPAQIGC LNELRVLNVR GNNISKLPME
LWWANRLETF NASSNVLEHF PAPASRAPRI PGEESQPAPP PVNGRAAPLG TLSATPSSEE
LSDERRPSQN SSTLLSVGPS PLAGDRKSSV VSVYGKGGRK TSVVSRTTAP SVTTSSANPR
KDSSSRFTNT FAGTLRNLYL ADNRLDDDIF EQISLLPELK VLNLSYNEDI SDMPQRSMKR
WPQLVELYLS GNGLTTLPAD DLEESSLLQA LYINGNKFTN LPADISRAKN LAVLDCGNNF
LKYNISNVPY DWNWNLNPNL RYLNLSGNKR LEIKQTTYGP SGPGVVDREE YTDFSRLLNL
RILGLMDVTL TQPSIPDQSE DRRVRTSGSL AGHLPYGMAD TLGKHEHLST VDLVVPRFNA
SETEMLLGLF DGQALSSGGS KIAKYLHENF GHIFALELKS LKAQSKETPI DALRRAFLAL
NKDLVTIAIQ HSEERPLKVH RGSGQPVILT KEDLNSGGVA TVVYLQSTEL YVANVGDAQA
MVIQTDGTHK MLTRKHDPAE PSERSRIREA GGWVSRNGRL NDLLSVSRAF GYVDLMPAVQ
AAPYVSNMTL KETDDIILIA TRELWEYLSP GLVTDIARAE RGDLMRAAQK LRDLAIAYGA
SGKIMVMMIS VADLKRRMER SRNHRGTTSM SLYPSGIPDG AQVLSTRRPR RGKADVLDSS
LNRLEAEIPA PTGNVSIVFT DIKNSTTLWE MYPSAMRSAI KLHNEFMRRQ LRKIGGYEVK
TEGDAFMVSF PTATSALLWT FSVQTGLLDL PWPSEVLNSV SCQPAYDKDN SLIFKGLSVR
MGIHFGDCVS ETDPVTRRMD YFGPMVNKAS RISAVADGGQ ITVSTDFISE IQRCLENFQD
TDRSNASEAE DSFEDETYAT AIRKDLKHLT SQGFEVKELG EKKLKGLENP EVVYSLYPHA
LAGRIEFHQQ HERREEGGGG GGGDKPAILA PGAELTFDPD MIWTLWRVSL RLEMLCSSLE
LPRDEAPGGL QSPETELLER IKQRGGEVTD RFLINFMEHQ VSRIETCIST LAMRHLAIGG
GVIKELDELR GPMSDILDEL TAQRKELERY KKRYGKLPSP DSSDDDEDDY DTDEGSDTEQ
ES
//
