ID A0A2T3ABF0_9PEZI Unreviewed; 2048 AA.
AC A0A2T3ABF0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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=BD289DRAFT_214656 {ECO:0000313|EMBL:PSR90442.1};
OS Coniella lustricola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Schizoparmaceae; Coniella.
OX NCBI_TaxID=2025994 {ECO:0000313|EMBL:PSR90442.1, ECO:0000313|Proteomes:UP000241462};
RN [1] {ECO:0000313|EMBL:PSR90442.1, ECO:0000313|Proteomes:UP000241462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B22-T-1 {ECO:0000313|EMBL:PSR90442.1,
RC ECO:0000313|Proteomes:UP000241462};
RA Raudabaugh D.B., Iturriaga T., Carver A., Mondo S., Pangilinan J.,
RA Lipzen A., He G., Amirebrahimi M., Grigoriev I.V., Miller A.N.;
RT "Coniella lustricola, a new species from submerged detritus.";
RL Mycol. Prog. 17:191-203(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}.
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DR EMBL; KZ678419; PSR90442.1; -; Genomic_DNA.
DR STRING; 2025994.A0A2T3ABF0; -.
DR InParanoid; A0A2T3ABF0; -.
DR Proteomes; UP000241462; 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; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; ZGC:77287; 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; 10.
DR SMART; SM00369; LRR_TYP; 12.
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:UP000241462};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 522..613
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1320..1596
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1661..1798
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1625..1649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1625..1642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2048 AA; 226596 MW; F5EEDE18B6E326CD CRC64;
MQQVAPWMVG GGAGSIQGSS GPSTAAGGGG GATAATTSTA LGGSNGNNSY FNHHNHSQTP
ISANAGTMAT SFYNDSSDNL SSASPSQMSP SFRSASVSAL MRPTQNPPGS DSPDAAYFDD
ERRPSAASVT TTASSQASKS SGQRVGGMRK LQGFFGEEFP GRDSSDTSLP PSYAGKEARS
HSYSHTPRPH RDRNYSNATD HTRDASPSSS RPRTPVPAPE VVPFLYQEAE DIARYGEAPV
REELTGPDRE RYVTENGSQN PPKTSSSNRS GPSIAHGQSH SHRHNKSNED PRILRPSISR
EDSQASILNP SKIAPNPVYG SRSRAQSPTP SGHSTLVMKN GGFDGPASPN YTHHHKKGLF
NRFRGKKEKE EIGPPLSKKL STSTQSVASS WAPKAARHEF IRDDVSIAPS RSNKGFDDTE
ELIGPTERSG GAGTYYRLDT DLEDMSGIVI RHDPLTPVAP GNIIIPQENE RAPAPPRNTG
GINGVWNAPD SWAVRKTENE VTTQALEPED IGGPPRPDEK LTPYCIRVFR SDGTFATLQM
ALDSSVQDLI GQIIKKSYVT ESLDNYHIVL KKHDLVRVLN HAERPLYIQK RLLQQVGYEE
RDRIEDLGRE DNSYICRFLF LSAKESDFHA STHDLGFGRM QKFNHIDLSG RNLVTIPISL
YSRANDIISL NLSRNLSLDL PRDFIHSCVN LRDIKFNNNE ARKLPLSFSR ANKLTYLDVS
NNRLEMLDHA ELGNLSGLLK LNLANNRLKT LPPYFGVYRS LRTLNISSNF LEFFPSFLCD
LESLVDLDMS FNLITDFHDN IGGLKSLERL VITNNRLQGT LPASFKNLQS LRELDIKYNQ
IQVIDVISEL PKLEIMTADH NAISQFTGSF ERLRSLKLNA NPITKFGVTA PVPTLKLLNL
SHAQLASIDD TFHNILNLER LVLDRNYFVS LPAQIGSLRR LEHFSIANNA LGELPPEIGC
LTELRVLDIR SNNLRKLPMD LWWANKLETL NASTNILDSF PKPASRAPQP PPDLSTPGSS
NTLKPGSVAG LSPSPSSDDL MPDGSRRPSQ ASSTLLSVGP SPVPAGPDRK SSVVSVYGKG
GRKTSVLSRT TTSQSVASIQ TPTPGPRKDS GLSSRLTNTF AGSLRNLYLA DNQLDDEVFD
HIILLGELRV LNLSYNELSD MPQRSIKNWP QLVELYLSGN ELTSLPADDL EEYNSLQVIH
INSNKFTNLP ADISKAKKLA VLDCGSNYLK YNISNVPYDW NWNLNPNLRF LNLSGNRRLE
IKQTVFGAAN ANREQYTDFN RLLNLRVLGL MDVTLISTSI PDQSEDRRIR TSGSLAGFLP
YGMADTLGRN EHLSTIDLVV PRFNASDTET LLGLFDGQAL SSGGSKIAKY LHENFGHIFA
MELKALKPRL QETPVDAMRR AFLALNKDLV TIATQYAEER SIVSHRGSAA SVVLSKEDLN
SGAVATVAYL QGQELYVANV GDVQAILIES DSTQKPLTKK HDPAEPEERS RIREAGGWVS
RNGRLNDVLE VSRAFGYADL MPAVQAAPHV YHVTIKEQHE VIVIATRELW EYLTPTLVTD
VVKAERPDLM RASQKVRDLA MAYGASGKIM VMMISVADLK KRNERSRLHR GQSMSLVPSG
LDSDLIPRET RKNKRAAKND ALDSNLRKAG TEVPAPTGMI AIVFTDIKNS TNLWETYPTA
MRSAIKVHNE LMRRQLRRIG GYEVKTEGDA FMVSFPTATS ALLWCFAVQI ALLDVDWPQE
ILNSVNCQEV FDKDKNLIFR GLSVRMGTHW GEPLCEVDPI THRMDYYGPI VNKASRVSAC
ADGGQITVSS DFISEIQRCL ETYQDNNATL EDTFEEDTFA QAVRKELRNL SSQGFEVKEM
GEKKLKGLEN PEVVYSLYPH SLAGRIEQHL FHERQQSGEA DKQLSAPSAP PGELNFDPEV
IWALWRVSLR LEMLCSTLEE NSGRGLQPPE TELLERMKQK SGEVTERFLV NFMEHQVSRI
ETCVSTLSMR HLASGNGQIT TLDDLRAPMT DVLSSLAEQL MELQRYKARF GEIQGNPRIE
ELQGGDLY
//
