ID A0A139II85_9PEZI Unreviewed; 2075 AA.
AC A0A139II85;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=AC579_1269 {ECO:0000313|EMBL:KXT14282.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT14282.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT14282.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT14282.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) 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:KXT14282.1}.
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DR EMBL; LFZO01000087; KXT14282.1; -; Genomic_DNA.
DR EMBL; LFZO01000087; KXT14283.1; -; Genomic_DNA.
DR STRING; 113226.A0A139II85; -.
DR Proteomes; UP000073492; 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; 4.
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; PTHR45712; AGAP008170-PA; 1.
DR PANTHER; PTHR45712:SF22; LEUCINE RICH REPEAT FAMILY PROTEIN; 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 Pfam; PF00788; RA; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 11.
DR SMART; SM00365; LRR_SD22; 8.
DR SMART; SM00369; LRR_TYP; 13.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF52058; L domain-like; 3.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51450; LRR; 6.
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:UP000073492};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 567..658
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1353..1631
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1692..1829
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2075 AA; 229698 MW; 9CEC76C149045838 CRC64;
MPLRNNTTND RHGSTGADST RSTDTVRGPF GSFTPHRPLK LHTKRQQLER QPTEDVSPGT
ILPKPTPSNA RSNSIAPWDH SPQSADTLDS HAGNIPSISR QPPTAHPSMG NWNNDRPTQM
PHSVFGTSFY INDSNENLGQ ISPGYAPGQG MNFPTDAEDR RPSVASATTV SSTGSKASVR
DRMQKKLQGF FGEHDVPLDN TSSSRQNSET SSLQNGPLPP FAPGGGNGRN RNNSMNDAIM
RSGPPSPSSS RPRTPAPQPS SEVTPWVFQD TEHVQAAPDS FFPPEPNNGR TPKNSTVSRL
HLPGHRHNRS TDEKHSYGFP LRPSTSREQS LSLMRGGNAP SAMSSALNLK TTARSTSPAP
SAHSAQSHQT NQRSPNTGAH KRSLFDRVTG RHKNDKDTLQ SQSVTSLSSA LPGMQKAATR
DRSDSKAKPK GKQETNGAAA QKKPSRIPFK SSKTAENGAG AGQQPVKDPN ATHAEDGGAL
WHLDTDMSHL EGIVDHKQGP LTPPHNEIFT GWPPEQPASQ APPDDEHKGA WDAPDSWAVN
RVADENLRRM TELDDDGNVI RDEDPGPMYF MRIFRADSTF AVISASLNTT AAELISMMAK
KTFLQDELDK YQIIMRKQDT SRQLLPGERP LVIQKRLLEM VGYQEMDHLE DLGREDHGYL
CRFTFLPSKM SGYSSLERDP GFNKMQRFNH IDLSGRNLIT IPITLYQKAT EIITLNLSRN
LTLDIPKDFI QSCSQLREIK YTSNEAWKLP PSLALASRLT TLDVSNNRLE QLSHAELNKL
QGLLSLKLSN NKLTTVPSYF GEYRSLRSLN LSSNSFTEFP DALRKLTTLV DLDISFNQVS
TLGNIATLTN LERLWATNNK LSGPFDASLS ALGSLREIDA RFNSISNIDV LSQLPKLEAL
MLGHNSVSQF EGSFHCLKVL FLNHNPVTNF DLNSPVPTLS VLNLASAKLS RLPDALFMKM
SGLTKLTISK NHFVSLSTHF GLLSKLEYLS IAKNELSRLP AEIGRLTELR YLDVRENNLS
MLPPEIWYAK RLETLNVSSN VLADFPKPGA PLPALPDNTV ALTPSAIPTN SPDFEELGKL
EDFQLRRPSQ ASGMLSTSSS PGTASRKGSV VSYTSTKGPL ARASTASSTG TITPSGGSRK
DSTLSSRLAA TFSTSLRHLF LADNRLEDDV FNELVLLPEL RILNLSYNQL YEVPPKTIRK
WTHLTELYLS GNDLTSIPSE DLEEGSSLKV LHLNNNKFQV LPAELGKVQR LAILDVGSNS
LKYNVSNWPY DWNWNWNRQL RYLNLSGNKR LEIKPSAQSL TGRDQRDLTD FSSLVNLRIL
GLMDVTLTIP SVPDQAADRR VRLAGSIIGN TMPYGMADTL GRNEHLSTLD MVVPRFRGHE
DEALIGLFDG QSLSSGGSKV AKFLHEKFKH HFIEELEKIQ PEETPADALR RTYLGLNKEL
ATAATAAMES REHSSSALVH RGSASGPELG DDDMTSGSTA TVMYLHGMEL YISNVGDAQC
LLIQSEGGHR VITRKHDPAE ATERQRIREA GGFVSRQGKL NDQLDISRAF GFIQLAPCVI
AAPHVSKLDI KESDEMILLA SRELWDYLTP DFAVDVARQE RSDLMRAAQK LRDLAIAFGA
TGKIMVMMVG VSDLRKREKA RFRTHSMSMG PSGSPDDYFT TVRKAKRGRD AVGDSKLARL
DQEVEAPTGD VTLVFTDIKN STILWETYPI AMQSAIKMHN EVMRRHLRII GGYEVKTEGD
AFMVAFPTVT SALLWCFTIQ SQLLEVQWPQ EILNSVHGEE MQDADGNVIF RGLSVRMGIH
WGRPVCEIDP VTKRMDYFGP MVNRAARIES VADGGQICVS SDFIQEVQRM LESHIESDRS
GSTGSEDTLN DDMLSQTIRR ELRSLSSQGF EVKDLGQRTL KGLENPEYIY LMYPHSLASR
LVIQQQKAEA ESRAAQASET EAKKMRNSEL TIDTDNVWDL WNVSLRLEML CSSLENSGAK
TLKPPETALL EKIKHGGGEV TDRFLVNFVE HQISRIETCI STLAVRNMIR PFQNGMLSQA
CPMSDILTEL TSQLDELKSL KAQQDEEFGF DMAPS
//
