ID A0A395SSL0_9HYPO Unreviewed; 2260 AA.
AC A0A395SSL0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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=FLONG3_5711 {ECO:0000313|EMBL:RGP75458.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP75458.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP75458.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP75458.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP75458.1}.
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DR EMBL; PXOG01000122; RGP75458.1; -; Genomic_DNA.
DR STRING; 694270.A0A395SSL0; -.
DR Proteomes; UP000266234; 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:SF43; LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47-LIKE PROTEIN; 1.
DR Pfam; PF08509; Ad_cyc_g-alpha; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13855; LRR_8; 4.
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; 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; 2.
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:UP000266234};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 716..807
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1512..1788
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1852..1989
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2221..2260
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 41..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2236..2260
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2260 AA; 249881 MW; 52853A8CABC4CD5D CRC64;
MTRNEHVNRI SSVMGSSNID TYSAVTVRSQ TEPEPEPEPL PQYQSTSFLT ASTTPAPASA
TSTISTPTPI PAHHSPTPNP APNPIPKPDP NADTDALTPT PSSSATTASS DNSYVFSSTP
RRHPHPPANP LTRLSTDGTA SLSNQWSSFK DEPQLSPTAT ATSTTFAPRA GANAQFNDRR
MSDLANYRRE LAVLETSRVP QIQQIPPTGG ASPQIAPWAN QPGSPTNTST MPTTFFNDST
DNLSLASQLS PGHQISNRQQ HQQQYPSHPS QHDAPDASYF DGRRPSAASI LTASSQGSKT
SIRGGFRKLQ GFFGEEFPGR DSSEGSLPTS LAGKDQRGRS YSHSRPTHRD RNYSNATDHT
RDASPSSSRP RTPVPAPEVV PFLYQDNSDI ARYGEAPVRD IMTGPDRERY AGDGSSQVPP
KTSSSSRSGH SIAHLPGHHR HNKSNEDPRT LRPTISRDDT AIGTQIPRDR GAGSNAMYPT
RSRGQSPTPS TRSAGMTWSS SKSTQVDGQT SPGHHNHGKR GFLRRLRGHH KEKDDAAARL
RDLPQSTRSL QTKSSKTDLH RPSDVSSTTL PYAGSVGPGE MTDLNDMRPA TAQRGATFNN
KFPFAKKGRT HRPQDYTEDT IGPTDRNDPN NMYHLDTNLN DMEGILTKPP PLTPMDTTFV
NNVEPERHDS IISTAPKGRW DAPDSWAVRR NTEDNSYNGP ELDEIGSPPR PEEKASPYCI
RIFRSDGTFS THSMSLDSSV TDVISQVIKK TYVMDGLENY HIIMKKHDLI RVLTPPERPL
LMQKRLLQQV GYEEKDRIED LGREDNSYLC RFMFLSARES DFHAKTTDMG LARAQKLNYV
DLSGRNLVTI PISLYSKAME IISLNLSRNL SLDVPRDFIQ SCKHLRDIKF NNNEARKLPP
SLSRANKLTF LDVANNRLEQ LEHAELNALT GMLKMNLANN RLKHLPSYFG AYQSLRSLNI
SSNFLDKFPT FLCGLPSLVD LDLSFNAIAT IPHEIGSLRN LEKLLITNNR LTHAVPASFG
QLVSLRELDI KYNGISSIDI ISELPRLEIL SADHNCVSAF VGQFESLRQL KLNSNPLNKF
EIVAPVPTLK TLNLSNAQLA SIDSSFVNMV NLEHLILDKN YFVSLPQEIG TLSRLEHFSI
ANNSVGELPA QIGCLTELRV LNVRGNNISK LPMELWWANR LETFNASSNV LEHFPKPASR
APRVPGEESQ PAPPPVNGRA APLGTLSATA SSEELSDDRR PSQNSSTLLS VGPSPLNAGD
RKSSVVSVYG KGGRKTSVVS RSATPSAPTQ SVNPRKDSGL SSRLNNTFAG SLRNLHLADN
RLDDDVFDQI TLLNELRVLN LSYNDEISDM PQRSIKSWPQ LVELYLSGNA LTTLPADDLE
ESSLLQALYI NGNRFTNLPA DISRAKNLAV LDCGSNYLKY NISNVPYDWN WNLNPNLRYL
NLSGNKRLEI KQTATGPLGP GAVNREEYTD FSRLLNLRIL GLMDVTLTQP SIPDQSEDRR
VRTSGSLAGH LPYGMADTLG KHEHLSTVDL VVPRFNASET EMLLGLFDGQ ALSSGGSKIA
KYLHENFGHI FALELKALKT RLNETPVDAL RRAFLALNKD LVTIAIQQSE ERPLQTHRNS
GQPIILTKED LNSGGVATVV YLQSTELYVA NVGDAQAMVI QTDGTHKMLT RKHDPAEPNE
RSRIREAGGW VSRNGRLNDL LQVSRAFGYV DLMPAVQAAP YVSNMTIREQ DDIILIATGE
LWEYLSPGLV TDVARAERQD LMRAAQKLRD LAIAYGASGK IMVMMISVAD LKRRVERSRL
HRGASMSLYP SGIPDDAQVL NTRRGRRTKG DVLDSSLNRL EAEIPAPTGN VSIVFTDIKN
STTLWEMYPS AMRSAIKLHN EVMRRQLRRI GGYEVKTEGD AFMVSFPTAT SALLWTFAVQ
MQLLDVNWPS EVLNSVSCQP IYDKDNSLIF KGLSVRMGIH FGDCVSETDP VTRRMDYFGP
MVNKAARISA VADGGQITVS TDFISEIQRC LENYQDTDRG NTSGSEDTFG EEETYASAIR
KDLRSLTSQG FEVKEMGEKK LKGLENPEVV YSLYPHALAG RIEFHTQHER KEEGGGDKPV
VLAPGAELCI DPDSVWTLWR ISLRLEMLCS SLEGNEPPGL QPPETELLER IKQRGGEVTD
RFLLNFLEHQ VARIETCIST LAMRHIAIGG GTIKELDDLH GPMSAILDQF MAQNRELKRY
RRKYGALPNP VSSSSSSEEE EDDDDDDPDT EEGSDTEQEL
//
