ID A0A1X0RVE4_RHIZD Unreviewed; 1860 AA.
AC A0A1X0RVE4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=BCV71DRAFT_266025 {ECO:0000313|EMBL:ORE16015.1};
OS Rhizopus microsporus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=58291 {ECO:0000313|EMBL:ORE16015.1, ECO:0000313|Proteomes:UP000242381};
RN [1] {ECO:0000313|EMBL:ORE16015.1, ECO:0000313|Proteomes:UP000242381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11559 {ECO:0000313|EMBL:ORE16015.1,
RC ECO:0000313|Proteomes:UP000242381};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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; KV921400; ORE16015.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:BCV72DRAFT_303859; -.
DR OMA; HPKSGCR; -.
DR Proteomes; UP000242381; 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; 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 InterPro; IPR029071; Ubiquitin-like_domsf.
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; 2.
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; 4.
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; SSF52075; Outer arm dynein light chain 1; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51450; LRR; 4.
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:UP000242381};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 365..462
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1124..1376
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1440..1576
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1674..1714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1681..1714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1860 AA; 207476 MW; 1107F97023C03540 CRC64;
MNIQYPRHMH SPSWDQSNNN NNNNGRKKDT QIANSLPNNQ PTDSFFNRVF GHHSSESSRA
GSPVPPPLHH QPSKQELLQK SSSRHSRNSS TGTLPISIVT PYPTSAGTEI VTAEAKMQRR
RSFDGQTTDS KSLKPKPVPV ASVSARVAAS PIPSKGVKGT TIPFPRGGRQ IGTNDDNNPS
TIRRSNSIER NQFRPEEHAP KKRHFFRLVK KKTNTGTSSS ASSTFTNASS SHTSSSITLT
NPTPTPRKRS NDIDHKPLLD GNTPYDVQRH YYQSRDEKKK STSSSAMDQN FDTLDGIINP
EYYKIASPYP QLAADNGFDF ESWAPPDSWG VQPTSIAANL ALDEDHAEFE DYQMDVQEKW
DVPKKNANIK IYRPDQTYNT LHVPLNTTTL EIFKKLASKF FMPDMTKYNL VMKRYNNERV
LGLNERPVQI QKMLQEQMGY TDDDKIDDIS YLIRFQLMPN VSQPIPPDDK DFGQHVDLQS
RSLATIPIYL YKHASSIVSL DISKNLHIEV PIDFIQMCTR LKQLWLANNE YSMLPPSTQH
ISSLEHLNIS GNRLRDLDHA KLDRLSELRT LRAINNRLES LPESFATSFV HLTSLFISNN
SFTKFPLVIC EIRSLAYLDI SFNKIQMFPD EIGQLTNLIG LFAIANRITG GLPPSFMNLT
KLQELDIRQN CITDLDVVSH LPRLEILLVD YNSTSIINFE IKNVKQLKMY KNHLTQFNLT
SATGGHCLTE LNLSNCKLSS LPEELFNNAL GLERLVLDSN TLSTLPSSIG SLQKLVKLSI
QNNYLDSLPS EIGKLSELRA LDAQKNNLKG LPREIWLCCS LQTLNCSSNL LDSFPEPFST
TTPPNSSTAM HSNSPRKDND TDAVLSMLPS QLNAGQGTIT RLDSIQKPGI MAASNVPQTP
LEASQPPNFN PPSFFASPRN HPPPLSLSLR YLYLGDNRLT DDVWSPLSLF LELRTLNLSF
NDLYEIPPEG LCHQHLYELY LSGNQLTSLP ADDIEKLQYL RILAVNGNKL QTLPAEIGKL
RKLLVLDVGN NVLKYNIANW PYDWNWNWNL GLKYLNLSGN KRLEIQKTHP DPINPKEKDL
SDFSALTRLR MLGLMDITIL GVSIPEEFHD RRVRTSPSEV NGMSYGVADW LGPSDHLSTW
DLVMPRFRSK EDECIFALFD GSKHPKSGCR LTKQLNDMLT SHLAKELACI KSEDTIVSAV
RRTFLSLEQS LGISPHIDKD SGASAAVCYI AGNKLYVANA GDALAVISRN NGQAFEITQK
HIPLNPSEVS RIRAAGGYVS NSGLLNNELN VSRSFGHFHL VPVVNCNPYV STIDLSENDE
FVIMASRGLW DKMSYQTAVD IARTEKDDLM AAAQKLRDFA ITYGANDNLM VMVIGVGDLF
DKRRKLPRKN NIGAGRGGAD GVVEEGILVK SKRRGKEEIP GDSTLARLER EVAPPVSQLA
LVFTDIKSST QFWETQPENM RAAIKIHDAI MRRTLRSVGG YEVKTEGDAF MVCFKNITAA
LLWCFTVQLQ LLEADWPAGI LDTEEGREIE KDGVVIYKGL SVRMGIHWGT PVSERNPITQ
RMDYFGPVVN KASRICNVAD GGQICVSSDV IAALRNFPSM FDEDAECDET LDADEGSFPV
SRDLLQLKKL GFHVVELGEV RLKGLETPES LSLVYSKQLL GRIEVDKSQM MAPAAQPTID
ASLSPKPSTD DTTPTIPPTP ALTSNTLSSS PDYLTARPTA RKTLRTIDPN LVCAMSNLAI
RLERLTSGHV LSQSMAGSSI LGHYTYQNSS EDNVPVVSAV HSGLGHMLDK HIREEATDEE
LMAMMENCVT RVENATSALY LQKMGRFANV LEKLGETIEV DPMHIMKALQ MYAEVVSNHS
//
