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Database: UniProt
Entry: A0A1Y3N0L9_PIRSE
LinkDB: A0A1Y3N0L9_PIRSE
Original site: A0A1Y3N0L9_PIRSE 
ID   A0A1Y3N0L9_PIRSE        Unreviewed;      2225 AA.
AC   A0A1Y3N0L9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=PIROE2DRAFT_13090 {ECO:0000313|EMBL:OUM61017.1};
OS   Piromyces sp. (strain E2).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Piromyces.
OX   NCBI_TaxID=73868 {ECO:0000313|EMBL:OUM61017.1, ECO:0000313|Proteomes:UP000195826};
RN   [1] {ECO:0000313|EMBL:OUM61017.1, ECO:0000313|Proteomes:UP000195826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2 {ECO:0000313|EMBL:OUM61017.1,
RC   ECO:0000313|Proteomes:UP000195826};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-2016) 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; KZ151003; OUM61017.1; -; Genomic_DNA.
DR   STRING; 73868.A0A1Y3N0L9; -.
DR   OMA; HPKSGCR; -.
DR   Proteomes; UP000195826; Unassembled WGS sequence.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
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; 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; 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; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF00481; PP2C; 2.
DR   Pfam; PF00788; RA; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00364; LRR_BAC; 8.
DR   SMART; SM00365; LRR_SD22; 5.
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; 5.
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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000195826};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          355..445
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          1257..1635
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   DOMAIN          1769..1958
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1312..1339
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2185..2212
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        15..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2225 AA;  251174 MW;  5806E40E7C089AEE CRC64;
     MDPLGIGDTH LSKKKANNPI FSHTTGQSNP NTPPPRKQYY DGTGASSSNK YTMTMGNPNS
     NANIQNGYDY NSGDMNQNYL PYGNMPISSN NPNNPNAYKS SGILGKNFLK PRHNGSPPTQ
     IQSTSNHYPK KSVSSSKSSL NSSASNINSS ASSLYALMSV NTPNIQNQHF YASSPNLTSN
     TVNSGSSSGI QQSKSIHDYG IFKKKERPKL PQEQETSGTT DVVDFSDFMS DPNHVPLECV
     SLPALANQSS SQNLNRGDGL QQIYNPNMNQ TIMTSSWEPP DSWDVKIDEP LPMKDILQES
     LGTQGHNDIN KFSNTNQELS VIHSGSIKDT ESFQTPEDIY YDNHYSNVKI EEDQKYNYIR
     VFKTDLTFTT VMCYLNSNAD YVCKKVAAKF FINDYNKYNL VVIRNKLERI IKPNEYPLLM
     QKRWLERLGY TSQDKLDLQG REDNSYCYRF IFKEIQIGRE ISPNHWKKPE VKDNPHINLA
     GFGLTILPVY LFQNASEIIS LDLSRNLNIQ ELHSDLTPSL TSLKSLSLSH NRIHNFPRNV
     HCITTLTHLN LSFNRIRTLE HTGIEHLRNL LVLELQCNLI EDIPESIAKG CQRLQYISLS
     NNRIKSIPIS LFHNLRRVLR HIDISFNRLI GKLPPEIGEL EVLEILRLNG NRMDGDIPKR
     LSECLQLREL DLRGNRFGSI VTYDQDGTEI LTETENYAQT MEVLSECKKL EILLLDGNPI
     RWIGKMSAVE DVQHEMSTNI DPSKFIDFPV LKRFSMSYRI SIGNQKPMIF RITNLTGTLS
     ELNISFCGLE ILPNNFFTKL TGIERLILDG NHLSELPNFS SSVRVHQKEI RQIGPFRMRH
     LSIYYNRLMA LPDDIGELVE LEYLDVRSNN LKTLPDSIWQ CGKLRSINAT SNQLEQFPIP
     INDENDTVSV NTAITDATLV ARRQRRMTTN ISIQAFPPLS FSLLALFLAD NRLTEDLCLA
     LYFMPNLVVL NASYNDIADI TSWLDCAPPT PLVEQPYKSS RAQTPANWFS HLQELYLSGN
     NIVTLPGEIE KLHNLSWLFL DNNKLSTIPG EVAKLKKLCA FDVGGQGGGR GEGSGLRYNI
     NNWPYDWNWS WNLELKYLNL SGNKRLEITP NAHNQKLIPF DKDNKRLMGS MNKIDLPSRH
     QAAGYNPYGN DLDQNQAMNI SISQRKSLSN FTTLTNLSML GLMDVTCLMV QIPDENDQRR
     IRTTSSEIPQ TGIPGGIIKY GISDTLCRFA SEAARRESLY ISRDHSNNVR DSTYITNTAI
     GVIPKEKYFL GIWDVVIPQF RNMDNESLFG IFDGRGTEDG TKLAEYLFRL FAGDFQAELK
     KVEESLIKER NQMKGHSRNK EPIVLDSNSI KSAIRRTFLG LNKELGEKFR TSVSNKNHSD
     YKNYNEDDDD ELFGCSAVIV YMVGDRKKEN CSLYVANVGD GTCILSKAGG NAQVISRSFK
     VGNVMDWASS RVYDQNKVNS SSLSTYSMES HRTVQHSLNS SQGSLTGNVY TSSNSDSPKF
     ISGLGDEMER IQNAGGWITS DGLVNGKTDV TRAFGYFNCL GSLNANPWIV KMELDFGDNN
     QSGNVVHLTP ESDKHDDEAA DIKLKLGQNH SDEFLVLVNG AVLDAIRCGA DANNNETPGF
     SLSTLDDTAQ VIVDIARSAL GNESSKRSKG TYQYQGIGKN TRSTTGWGSA ATKIRDVALS
     HGAYGARTTI NANQKVKSSK GMMVMVLGLR DLVETAQRWM GARRGSTETG SDSLELMNLK
     RRGSDVALKM KKGDMSIPPS IEPPTGQLAL VFTDIKNSTA LWETHAIAMR NSIKLHNLRM
     RALLKQYGGY EVKTDGDSFM VSFVDLMSAI QWCLDVQTEL LKIDWPKEIL ESEDGEEVWW
     DTINSEPVFN DEYLDDEDTD NDMDDDINED DEDIYQEKEE LPLETRIAMR KKNDIVLLFR
     GLCVRMGIHY GTPLCEKDPT TGRMDYFGPM VNRASRICSA AQGGQIFISS EVIKEVTKRK
     GGDLSQLRMS DTLDEKITDS MNIKTWIIGE KKLKGLETPE VLHVMYPKQY YLRHEYFTLM
     QNRKQESGNN TGNLMDIRMN PIDINPMKEH RSSEPTTIDR NYVQTLGNLC LRLEFLAVNA
     QNICFNNQNF DERIPVYPYL INSSSISIPL EATEKELTAA LEGIAIRIEN AVSILYLIQS
     SPLNRILKTL GSYIDVNPNQ ILSALQEYVL AMKERDERLE RIRNERRERE RRIKNRASKA
     ANTSI
//
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