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Database: UniProt
Entry: A0A2Z6R8A9_9GLOM
LinkDB: A0A2Z6R8A9_9GLOM
Original site: A0A2Z6R8A9_9GLOM 
ID   A0A2Z6R8A9_9GLOM        Unreviewed;      1738 AA.
AC   A0A2Z6R8A9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=RclHR1_22770003 {ECO:0000313|EMBL:GBB94024.1};
OS   Rhizophagus clarus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=94130 {ECO:0000313|EMBL:GBB94024.1, ECO:0000313|Proteomes:UP000247702};
RN   [1] {ECO:0000313|EMBL:GBB94024.1, ECO:0000313|Proteomes:UP000247702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HR1 {ECO:0000313|EMBL:GBB94024.1,
RC   ECO:0000313|Proteomes:UP000247702};
RA   Kobayashi Y.;
RT   "The genome of Rhizophagus clarus HR1 reveals common genetic basis of
RT   auxotrophy among arbuscular mycorrhizal fungi.";
RL   Submitted (NOV-2017) 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:GBB94024.1}.
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DR   EMBL; BEXD01001421; GBB94024.1; -; Genomic_DNA.
DR   STRING; 94130.A0A2Z6R8A9; -.
DR   Proteomes; UP000247702; 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; 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; 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   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR48051; -; 1.
DR   PANTHER; PTHR48051:SF45; LEUCINE-RICH REPEAT-CONTAINING PROTEIN 10B; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF13855; LRR_8; 4.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00364; LRR_BAC; 10.
DR   SMART; SM00365; LRR_SD22; 4.
DR   SMART; SM00369; LRR_TYP; 13.
DR   SMART; SM00332; PP2Cc; 1.
DR   SMART; SM00314; RA; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF52075; Outer arm dynein light chain 1; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-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   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:UP000247702};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          365..455
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          1042..1319
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   DOMAIN          1385..1523
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1738 AA;  195769 MW;  FCC1F49BFB9194AC CRC64;
     MTPRRSSDLD ISPPSPFRTP EQYPTGGGQN RRKKSREEKD SFLSSIFGSH SRPSSPSYDP
     TLQSMNNLAA RSSKRGGLVR KLSAGNVKAG LLLPDDDEPR RKSFDSVQPN MNTRYGDFPP
     EEIAPFAYQT VIPMDNRKGS STTLSSNSDT NSYRIIHRRT KSSDSDSALD SSSVYSNNGP
     IGKEKEKRTI LKWFRKSPKD KETSTSEGIF RKNSDAETYT HSHPNLIITP YEKDEFAPIT
     PNYSRSTSLK SEKSDHHLFK IKKGSSGRRK ETTQNEFNLD IDDMDGIIRN DNREHRLSGV
     SNTLQFITCD EMLQESSNDS ILTPTSNTEM WSPPESWAVH KPQQHILESN ILDDTNNEKL
     NNGNKMYCIR VFRPDATFGT VNCLLNTTTA ELCHILGKKF YIPDISKYNI YIKRHNLERM
     LSPKERPLKL QKQLLEQTGY TENDKLDDLG REDNSYLFRF TFRETTVPRF EEEQGALSSI
     QHVDLQARNL QTIPIFLYRQ AYFIRSLNVS QNLMLDLPTD FIQSCHQLKE LHLSQNELER
     VPQSVKQSQM LSTLNLSSNR LQELDHAQLE QLKNVIELTN LQVDNNLLSS LPETFVKFRC
     LNILNVSNNS FTEFPPVICS IISLSELDMS FNNITDVPIE IGNLVNLKRL FLIGNQIMGT
     LPASFEKLTS LRKLDIRRNQ ITNIDVLSSV PNLEVLLIES NHFSLVNEGI GSSITELSLA
     HSKLNELPDR LLEDLVSLEK LDLSNNQLTK IPNSIGSLKK LAHFSCKNNT LSALPSEIGS
     LTALRVLDIH CNNLRSLPPE IWYCAGLVTL NVSSNLLEQF PMRPTSFPDV NQSINSVRPN
     SYLSKSLRAL YLGDNVLTTE IFSAVSQFIE LRILNLSFNL LDEIPTGGIV NPHLTELYLS
     GNEIPSLPDD IEKLANLRVL HVNGNKLQTL PAELSKIRKL VVLDVGNNAL KYNIANWHFE
     WNWNWNIELK YLNLSGNKRL KIKHALFNEL NPPRDRNLAD FGALTRLRVL GLMDITLLDL
     IVPDETDNRR VRTSGSEVNS MSYGMADTLG TSDNLSTWEA VIPKFRGRED ECLFGLFEGR
     AGTNRGGRVA KYLHDNFQSS FKTELERLKD FDQVESSLRR SFLSLNKELG LKMFNSNNSA
     LESEYAWESE STNSVALGID DNKSGASGIV VYISGTILYV ANVGDTKAVI GRNNGSAYEV
     ACNQSIISPS EIARIRDAGG FISHDCLVNG EVNVSRSFGH FHLTPIINAN PSIEKIKLSE
     QDEFIVLATR GLWDRMSYQT AVDVTRTERD DLMRAAQKLR DFAISYGAEE NIMVMIIGVG
     DLFDRRLRRR LDGLEGKGLL QGMAGEETTF YFGSKTKRGR REENPSDSAI ARLQKEIPPP
     TGQIALVFTD IKNSTFLWET LPDAMRSAIK QHNTIMRRQL RFIGGYEVKT EGDAFMVSFP
     TVSSALLWCF TVQLELLKVD WPSEIIESED GKIVYGGADN DLIYKGLSVR MGIHWGSPVC
     EPDIITKRMD YFGPIVNRTA RICNNADGGQ ICISSDVKTE IGLLDGMMDG GDNDSIFKKD
     GTDEEMQGTP PQSNNGVLDK NLIHLRKLGF VMRNIGERKL KGLENPEVLY LVYPEALKGR
     MEEDLVKDKD SKSLDPAIVR LCGQLCLRLE RLSSGGVINR SNTRNSRLDL FLSGLSYVKD
     NATEEELLRI MESFVTRIEN SISTLYLKDV GKLALGDMSI MDIVKALQMY AQYVGKAK
//
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