ID A0A074WT54_9PEZI Unreviewed; 1871 AA.
AC A0A074WT54;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=M436DRAFT_42339 {ECO:0000313|EMBL:KEQ74734.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ74734.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ74734.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ74734.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584706; KEQ74734.1; -; Genomic_DNA.
DR RefSeq; XP_013428935.1; XM_013573481.1.
DR STRING; 1043004.A0A074WT54; -.
DR GeneID; 25409736; -.
DR HOGENOM; CLU_000430_4_0_1; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000027730; 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; 3.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR013716; Adenylate_cyclase_G-a-bd.
DR InterPro; IPR048580; CYAA_C.
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; PF21187; CYAA_C; 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; 9.
DR SMART; SM00369; LRR_TYP; 11.
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; 3.
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:UP000027730};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 354..445
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1143..1423
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1484..1621
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1871 AA; 207318 MW; 60BD3845736EBF9A CRC64;
MSPGFVPQNI NNLSLEWNGE DRRPSVASTT TMSSTGSSKR SITGKFHKKL QGFFGDDFDP
NAPPPKDQPD QLDKRGRNPS NATQVTQTTR PGSPSASRPR TPNTSSEVTP WDFEPAPANV
GFQQTRKDKG SVSGRHHRLH LPGHRHKTSL EDIDDGASVM SGRAGTIRKD STLPASLNGA
RARATSPSPS MKSMMSAQQS QSSDAQGQRS PGTSHSAKRS LFDRPMALAL AKKEHTRIPF
KPRRAEPSAE FNKKDPNAPR PEAVRNASAL WHLDTDMSQM EGIVNRSQPM TPPVTSEIFT
GFPGIEPPKP AEEEAGTWEV PDSWAVKRVP DQNVAALREV DDEGQVPRDE DPGSMYFMRI
FRADSTFAVI SAGLNTTASE LIQMMAKKTF LQDELDTYQI VMRKTGSSRI LAAGERPLAI
QKHMLEMAGY NDKDRPEDLG REDHGYLVRF TFLPGKLSGY SSLERDPGFK GQQKFNHIDL
SGRDLVTIPI TLYQKATEII TLNLSRNLSL DIPKDFIQSC SNLREIKYTS NEAWKLPASI
CLASRLTMLD VSNNRLEQMQ HADLHKLHNL VSLKLSNNKL TSLPAYFGCY QALRSLNLAS
NNLDVFPDFL CELRTVVDLD ISFNGISALP KVGKLINLER LFATNNKLSG AFPETFKQLV
KLTQIDIRFN ALDNIDVMAE LPLLEHLLVG HNSIAAYEAS FHRIKVLSLD HNPVTRFGLT
TPVPTLSVLN LASAKLTQLP DDLFAKISNI TKLVLDKNHF TALSPLIGKL TRLEHLSVAK
NMLNNLPSDI GRLQDLKYLD IRENNLSRLP QEIWYARRLE SLNIASNVLN EFPKPGAPPP
TLISEVPTPT TTTGGPQTPD FDELGKLEAF QMRRPSQVGH GMMPGGSPAG RKGSVASTYG
VQSSRHPSLA PRGSTESGLS SGAATPGPRK DSTMSNRLAS TFASTLRHLI LADNRLSDDV
FDEIVLLPEL RVLNLSYNEL YDIPPRTIRR WPHLTELYLS GNDLSALPAE DFEEGSGLRV
LHLNSNRFNV LPAELGKIQK LQTLDVGSNA LKYNVSNWPY DWNWNWNHQL RYLNMSGNKR
LEIKPNVNVV PGRETRDLTD FSTLQHLRIL GLMDVTLTIP SVPDQGPDRR VRTAGSIIGT
HIPYGMADTL GRHEHLSTLD MVIPSFGGHE DRLLFGMFDG ATLTTGGSKV AKFLYEKFRH
HFADELAKLQ EDSDDSPLDA LRRAYLSLNK DLATAATQAI EARAHPSAAI LHRASVTGLE
LGEDDMTSGA VATIMYLQNM ELYVSNVGDA QALLIDSEGG HRVITRKHAP AEADERIRIR
EAGGYVSRQG KLNDALEVSR AFGFVPHMPG VVACPHTARI SLKESDEIIV IASRELWDYL
TMDFAVDVAR SERGDLMRAA QKLRDLAIAF GATGKIMVMM LGVSDLRKRE RARFRTHSMS
MGPSGAPDEL MTISRRNKRG RDNVGDSKLA RLDQEIDPPQ GEVTLVFTDI KNSTMLWESY
PIAMRSAIKL HNELMRRHLR IIGGYEVKTE GDAFMVAFQT VTSALLWTFT IQSQLLEVPW
PQEILNSIHG QEVLDTDGNR IFRGLSVRMG IHFGRPVCEQ DPVTGRMDYF GPMVNRSARI
QSVADGGQIT VSSDFIAEIQ RLLETHIETD RNGSTGSDDA MGDEMIGNAI RRELRSLSSQ
GFEVKDLGQR NLKGLENPEY IYLMYPHSLA ARLVVQQQQQ AQAELVKAQA AAAPSNNNVG
IESPTGTAAT KSADSQLSID TDHVWDLWNV SLRLEMLCSS LETTGLTALK APETALLERM
KQRGGEITDR FVINFVEHQI SRIETCVTTL ALRHMVQPFR PGILAASKPM HEILGEVTAA
MQELKRLKGE A
//
