ID A0A5N7AAN8_9EURO Unreviewed; 2151 AA.
AC A0A5N7AAN8;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=BDV27DRAFT_124670 {ECO:0000313|EMBL:KAE8366961.1};
OS Aspergillus caelatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=61420 {ECO:0000313|EMBL:KAE8366961.1, ECO:0000313|Proteomes:UP000326268};
RN [1] {ECO:0000313|EMBL:KAE8366961.1, ECO:0000313|Proteomes:UP000326268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 763.97 {ECO:0000313|EMBL:KAE8366961.1,
RC ECO:0000313|Proteomes:UP000326268};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics studyof 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) 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; ML737605; KAE8366961.1; -; Genomic_DNA.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000326268; 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; 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; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00789; Ad_cyc_g-alpha; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 9.
DR SMART; SM00365; LRR_SD22; 5.
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:UP000326268};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 618..709
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1404..1682
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1742..1879
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2151 AA; 238768 MW; 40D154F1C420AB6E CRC64;
MSFQGGDLPE GRRSSESSGG NSWLSQETVK DNQTNRYQRN HAMLNGRLIS PFSGFAKVDR
SNSQGRKQPP TLGAHDLSTS NFTWPSPDVS PTDKRKDSGF TGHRKSSAAI GPDEPGPPPT
FSSSPRLSCP NSDEVDYFQQ DPNASYSSSP KMAPGDGNGT LFQDLSEHEA SPASTSFRPG
TSRTYASEPL ELDYNGDHRR PSVASATTIS SQGSKSSTGG RFRKKLKGFF GEEYMPGDSK
LESDNGIQHP TKKSSLSEHH IFRERANSDG ARSPPQRLIG ESSPQRPRPR APLPSSEITP
WVFQSFNDIP QYGEAPVREA PIGADGRRAA AQMARGPQRN QTGRQFSGHR HSRSKEEKST
TTDDMAEYPS RPTTGRDDFG IGLRANSLNN SAMNSTSTLV RSTSPTPSMQ SAHSREQGQS
SPGTQLPNKR SILDKIRRPK AHGPLKHFPG AKGVQEATKS TSKLARRDVS PARRGRQGSL
EGTSTPKTGD ESDRKKDGRG LAISSAKLRG RRVLGTDTPL RDTKPAEEQE GMYELDTDLS
HMEGIVRKRS PQPAADRTQP VDGNSKLHEE GKSRDGQPTG HWDAPDSWHV RRHGEDSSAA
FPSGDAEAAR TIPEPEGAPY FIRVFRIDST FATLSTGLNA TVADILVILG RKSFLTDHLN
NYEIVMRKND LTRQLDPTEK PILMQKQMLE QIGYTTKDRL EEIGREDHSY VLRFTFLPTK
LSGLTSLQGG EPGFNRNQKF SHVDLSGKGL VTIPITLYGK AAEIISLNLS KNMSLDVPKD
FIQGCINLRE LKFIGNEAPR LPASFGLASR LTYLDVSNNY LEQLDHAGLD KLQGLVSIKL
SNNKLTGLPS YFGNFAYLRS LNLSSNNFRV FPDFLCNLKS LVDLDISFNN IAELPSIGNL
STLERLWMTN NVLRGALDES FKDLVNVKEI DARFNEITNI DNLSYVPRLE QLHVGHNAIS
KFKGSFPKLR TLLLDHCPIT QFDIDAPMPT LTLLNIASAK LVQLRDTLFE NVPNLTKLIL
DKNHFVSMSS HIGKLRKLEH FSMIKNPLDA LPPTFGCLTE LRYLNLRECN LSRLPPELWN
CNKLETLNVS SNVLDSFPKH GTPMPQLPGE PVPGTPGTST PTNYEDLAAD DQEGRRPSQT
SGSILSTGGS PNGSGGYRKP SVASSLSQGG RKVSTASRSL NEGSPASRKD SSFSNLSNQT
FGGSLRNLYL ADNRLEDDVF RELSLLTELR VVNLSYNELT ELPQGLLKRW SNLTELYLSG
NELTSLPSDD LEEGSQLKIL NINANRFQVL PAELCKVSKL SILDVGSNSL KYNVSNWPYD
WNWNWNRNLK YLNFSGNKRL EIKPHGSPLQ GPPNTNETDL TDFNSLTYLR VLGLMDVTLT
TSTIPEENED RRVRTSASLA GFLAYGMADF LGKSDHLSIF DMIVPRLKPD NVETVVGMFD
GTSQSTGGSK VAKFMHENFL RTFSTELRRL RRDMQETPLD ALRRAFLALN KNMAGYCYKS
LNDKNVQRYD DAPDQKGLRL TKDDIETGGV ATVLYLHNMD LFVANVGDAQ AILVKSDGSL
RHLTRTHDPA EPHERARIRA AGGYVSRQGK LNDVLPVSRS FGHFHLMPAV IAAPHTMHVN
LTEQDEMIIL ASRELWDYVT PDLVVDVTRA ERRDLMVAAQ KIRDLAISFG ANNKLMVMIL
GVGDLKKRDR QSKLRNASVS TGMLEEQQIL PTSKRTKKPR DMPGDSRLAR FEFVDAPVGE
LAIIFTDIKG STSLWETCPD AMRSAIQIHN DILRRQLGII GGYEVKTEGD AFMVAFSTTT
AALLWCFNCQ MQLLEAEWPT EILEQSQCQV EYDMDNNIIF RGLSVRMGIH WGEPVCEKDP
VTNRMDYFGP MVNRASRISA VADGGQIFVS SDFMSDIQRN LEVFADSERA ASTGSEEGYA
VDNLGYNIRR ELQQLNSLGF VIKDQGERKL KGLENPEPLY LIYPHTLSGR LSIMQKDATS
DKNVPTTISK HSQLEIQTDL IWRLWEITLR LERLCGALEY PGEARLKEPN VSLFNVVKNH
GGELADSTVV SLVEQQVTRI EMTVNTLAIR NMLRPFRPHD RLNDHAMPIR DVLQELQTQL
AEYRALKEQI AVSAAGITGR SPSYTASLED SNSSASSSFV RMSISADDAN N
//
