ID X0C4I3_FUSOX Unreviewed; 2140 AA.
AC X0C4I3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=FOQG_07951 {ECO:0000313|EMBL:EXK89310.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK89310.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK89310.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK89310.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) 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}.
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DR EMBL; JH658378; EXK89310.1; -; Genomic_DNA.
DR Proteomes; UP000030663; 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:UP000030663};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 597..688
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1393..1669
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1733..1870
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 21..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2105..2140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2115..2140
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2140 AA; 237375 MW; 96C6A8468624B15B CRC64;
MPSPVSRSPA AISRPVAVHL ASHHPAKRFP ASHRSSFKDE PQLSPTATNF APRAGANAHP
KDRRMSDLTN YRRELAVLET SRVPQIHQIP PTGGASPQIA PWMNQPGSPT TSSNMPTSFF
NDSSDNLSLA SQLSPGHQIS NRQPPQHQYP SHPSQHDAPE ASYFDGRRPS AASILTASSQ
GSKTSITRGG FRKLQGFFGE EFPGRDSSDG SLPTSLAGKD QRGRSYSHSR PTHRDRNYSN
ATDHTRDASP SSSRPRTPVP APEVVPFLYQ DNSDIARYGE APVRDIMTGP DRERYVGDGS
SQIPPKTSSS SRSGHSIVHL PGHHRHHKSN DDPRTLRPTM SRDDTAIGTQ MSRDRGGSSA
VYSTKSRGQS PTPSTRSAGM TWSTKSSQVD GQTSPGHHHG KRGIFGRLRR HHKDKDDIAK
LRDLPQSTRS LQPKTSKPDL HRPSDVSTTT LPFSGTFVPG EMSDVPDMRP VPGQRGATFN
NKFPFAKKGR THRPHDYVDD AIGPTDRNDP NNIYHLDTNL NDMEGILTKP PPLTPMDTSF
VNNVEPERHD SIISTAPKGR WDAPDSWAVR RNTEDNSYHG PEPDEIGSPP RPEEKASPYC
IRIFRSDGTF STHSMPLDSN VTDVISQVIK KTYVVDGLEN YHIIMKKHDL IRVLTPPERP
LLMQKRLLQQ VGYEEKDRIE DLGREDNSYL CRFMFLSARE SDFHAKTTDM GLARAQKLNY
VDLSGRNLVT IPISLYSKAM EIISLNLSRN LSLDVPRDFI QSCKHLRDIK FNNNEARKLP
PSLSRANRLT FLDVANNRLE QLEHAELNSL TGMLKMNLAN NRLKHLPSYF GAYQSLRSLN
ISSNFLDKFP TFLCNLPSLV DLDLSFNAIA TIPHEIGGLK NLEKLLITNN RLTHAVPASF
GQLVSLRELD IKYNGISSID IISELPKLEI LSADHNCVSA FVGQFESLRQ LKLNSNPLNK
FEIVAPVPTL KILNLSNAQL ASIDSSFVNM VNLEHLILDK NYFVSLPQEI GTLSRLEHFS
IANNSVGELP AQIGCLTELR VLNVRGNNIS KLPMELWWAN RLETFNASSN VLEHFPKPAS
RAPRIPGEES QPAPPPVNGR AAPLGTLSAT ASSEELSDDR RPSQNSSTLL SVGPSPLNAG
DRKSSVVSVY GKGGRKTSVV SRSATPSAPT QTVNTRKDSG MSSRLNNTFA GSLRNLHLAD
NRLDDDVFDQ ITLLAELRVL NLSYNDEISD MPQRSIKNWP QLVELYLSGN ALTTLPADDL
EESSLLQALY INGNRFTNLP ADISRAKNLA VLDCGSNYLK YNISNVPYDW NWNLNPNLRY
LNLSGNKRLE IKQTNTGPLG PGAVNREEYT DFSRLLNLRI LGLMDVTLTQ PSIPDQSEDR
RVRTSGSLAG HLPYGMADTL GKHEHLSTVD LVVPRFNSSE TEMLLGLFDG QALSSGGSKI
AKYLHENFGH IFAGELKQLK TRSNETPVDA LRRSFLQLNK DLVTIAIQQS EERPLKTHRG
SGQPVILTKE DLNSGGVATV VYLQSTELYV ANVGDAQAMV IQTDGTHKML TRKHDPAEPN
ERSRIREAGG WVSRNGRLND LLQVSRAFGY VDLMPAVQAA PYVSNMTIRE QDDIILIATG
ELWEYLSPGL VTDIARAERQ DLMRAAQKLR DLAIAYGASG KIMVMMISVA DLKRRVERSR
LHRGASMSLY PSGIPDDAQV LNTRRGRRTK GDVLDSSLNR LEAEIPAPTG NVSIVFTDIK
NSTTLWEMYP SAMRSAIKLH NEVMRRQLRR IGGYEVKTEG DAFMVSFPTA TSALLWTFAV
QMQLLDVNWP SEVLNSVSCQ PVYDKDNSLI FKGLSVRMGI HFGDCVSETD PVTRRMDYFG
PMVNKAARIS AVADGGQITV STDFISEIQR CLENYQDTDR GNASGSEDTF DDETYASAIR
KDLRSLTSQG FEVKEMGEKK LKGLENPEVV YSLYPHALAG RIEFHLQHER KEEGGGGGGD
KPAVLAPGAE LSIDPDAIWT LWRISLRLEM LCSSLEGNEA PGLQPPETEL LERIKQRGGE
VTDRFLLNFL EHQVSRIETC ISTLAMRHLA TGGGPIKELE DLQGPMTAIL DMFMAQRKEL
ERYRRKYGAL PSSSSSEDED DDDDDDDPDT EEGSDTEQEL
//
