ID A0A0J9U4J4_FUSO4 Unreviewed; 1800 AA.
AC A0A0J9U4J4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=FOXG_00154 {ECO:0000313|EMBL:KNA93782.1};
OS Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS / NRRL 34936) (Fusarium vascular wilt of tomato).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=426428 {ECO:0000313|EMBL:KNA93782.1, ECO:0000313|Proteomes:UP000009097};
RN [1] {ECO:0000313|EMBL:KNA93782.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4287 {ECO:0000313|EMBL:KNA93782.1};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA Brockman W., MacCallum I.A., Young S., LaButti K., DeCaprio D.,
RA Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA Larson L., White J., O'Leary S., Kodira C., Zeng Q., Yandava C.,
RA Alvarado L., Kistler C., Shim W.-B., Kang S., Woloshuk C.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KNA93782.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4287 {ECO:0000313|EMBL:KNA93782.1};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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; DS231696; KNA93782.1; -; Genomic_DNA.
DR RefSeq; XP_018231828.1; XM_018376285.1.
DR GeneID; 28942475; -.
DR KEGG; fox:FOXG_00154; -.
DR VEuPathDB; FungiDB:FOXG_00154; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000009097; 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:UP000009097};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 258..349
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1054..1330
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1394..1531
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1766..1800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1776..1800
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1800 AA; 200217 MW; 93D4613A1C00C1E1 CRC64;
MSRDDTAIGT QMSRDRGGSS AVYSTKSRGQ SPTPSTRSAG MTWSTKSSQV DGQTSPGHHH
GKRGIFGRLR RHHKDKDDIA KLRDLPQSTR SLQPKTSKPD LHRPSDVSTT TLPFSGTFVP
GETSDVPDMR PVPGQRGATF NNKFPFAKKG RTHRPQDYVD DAIGPTDRND PNNIYHLDTN
LNDMEGILTK PPPLTPMDTS FVNNVEPERH DSIISTAPKG RWDAPDSWAV RRNTEDNSYH
GPEPDEIGSP PRPEEKASPY CIRIFRSDGT FSTHSMPLDS NVTDVISQVI KKTYVVDGLE
NYHIIMKKHD LIRVLTPPER PLLMQKRLLQ QVGYEEKDRI EDLGREDNSY LCRFMFLSAR
ESDFHAKTTD MGLARAQKLN YVDLSGRNLV TIPISLYSKA MEIISLNLSR NLSLDVPRDF
IQSCKHLRDI KFNNNEARKL PPSLSRANRL TFLDVANNRL EQLEHAELNS LTGMLKMNLA
NNRLKHLPSY FGAYQSLRSL NISSNFLDKF PTFLCNLPSL VDLDLSFNAI ATIPHEIGGL
KNLEKLLITN NRLTHAVPAS FGQLVSLREL DIKYNGISSI DIISELPKLE ILSADHNCVS
AFVGQFESLR QLKLNSNPLN KFEIVAPVPT LKILNLSNAQ LASIDSSFVN MVNLEHLILD
KNYFVSLPQE IGTLSRLEHF SIANNSVGEL PAQIGCLTEL RVLNVRGNNI SKLPMELWWA
NRLETFNASS NVLEHFPKPA SRAPRIPGEE SQPAPPPVNG RAAPLGTLSA TASSEELSDD
RRPSQNSSTL LSVGPSPLNA GDRKSSVVSV YGKGGRKTSV VSRSATPSAP TQTVNTRKDS
GMSSRLNSTF AGSLRNLHLA DNRLDDDVFD QITLLAELRV LNLSYNDEIS DMPQRSIKNW
PQLVELYLSG NALTTLPADD LEESSLLQAL YINGNRFTNL PADISRAKNL AVLDCGSNYL
KYNISNVPYD WNWNLNPNLR YLNLSGNKRL EIKQTNTGPL GPGAVNREEY TDFSRLLNLR
ILGLMDVTLT QPSIPDQSED RRVRTSGSLA GHLPYGMADT LGKHEHLSTV DLVVPRFNSS
ETEMLLGLFD GQALSSGGSK IAKYLHENFG HIFAGELKQL KTRSNETPVD ALRRSFLQLN
KDLVTIAIQQ SEERPLKTHR GSGQPVILTK EDLNSGGVAT VVYLQSTELY VANVGDAQAM
VIQTDGTHKM LTRKHDPAEP NERSRIREAG GWVSRNGRLN DLLQVSRAFG YVDLMPAVQA
APYVSNMTIR EQDDIILIAT GELWEYLSPG LVTDIARAER QDLMRAAQKL RDLAIAYGAS
GKIMVMMISV ADLKRRVERS RLHRGASMSL YPSGIPDDAQ VLNTRRGRRT KGDVLDSSLN
RLEAEIPAPT GNVSIVFTDI KNSTTLWEMY PSAMRSAIKL HNEVMRRQLR RIGGYEVKTE
GDAFMVSFPT ATSALLWTFA VQMQLLDVNW PSEVLNSVSC QPVYDKDNSL IFKGLSVRMG
IHFGDCVSET DPVTRRMDYF GPMVNKAARI SAVADGGQIT VSTDFISEIQ RCLENYQDTD
RGNASGSEDT FDDETYASAI RKDLRSLTSQ GFEVKEMGEK KLKGLENPEV VYSLYPHALA
GRIEFHLQHE RKEEGGGGGG DKPAVLAPGA ELSIDPDAIW TLWRISLRLE MLCSSLEGNE
APGLQPPETE LLERIKQRGG EVTDRFLLNF LEHQVSRIET CISTLAMRHL ATGGGPIKEL
EDLQGPMTAI LDMFMAQRKE LERYRRKYGA LPSSSSSEDE DDDDDDDPDT EEGSDTEQEL
//
