ID A0A162VBL6_DIDRA Unreviewed; 2120 AA.
AC A0A162VBL6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=EKO05_0000332 {ECO:0000313|EMBL:UPX09647.1}, EKO05_000333
GN {ECO:0000313|EMBL:KAF9712603.1}, ST47_g10463
GN {ECO:0000313|EMBL:KZM18346.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM18346.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM18346.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM18346.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
RN [2] {ECO:0000313|EMBL:KAF9712603.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9712603.1};
RA Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF9712603.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9712603.1};
RX PubMed=32345704; DOI=10.1534/g3.120.401265;
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RT "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT ArME14.";
RL G3 (Bethesda) 10:2131-2140(2020).
RN [4] {ECO:0000313|EMBL:KAF9712603.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9712603.1};
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:UPX09647.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:UPX09647.1};
RA Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL Submitted (MAR-2022) 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; RYYQ01000002; KAF9712603.1; -; Genomic_DNA.
DR EMBL; JYNV01000333; KZM18346.1; -; Genomic_DNA.
DR EMBL; CP095288; UPX09647.1; -; Genomic_DNA.
DR STRING; 5454.A0A162VBL6; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR Proteomes; UP000617380; Chromosome 1.
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; 2.
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; 10.
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; 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:UP000076837};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 609..700
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1405..1680
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1741..1878
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2120 AA; 235128 MW; 4B25B169E7EDC4B6 CRC64;
MTRPDTSLNR HGSIESSWSS RSGDTVRPYG RQGSLRGTPV TVKTTKDPNA PVEKEPDISP
TTIPPAPPPK DPQHQPRKPP VWEGPISHDF RDYRKDLAVL QTSGGRVPSI SRNPPTASSA
NSNPPWASSA PNGGTNMANN VWSSFFNDSD NDDVAQLSPG FAPSGGNARE DAMGFPRDDR
RPSVASAMTV SSTGSKSSFS RGFHKKLQNV FGEDFPGEGR QNSDTSLNNA RSNITETQSL
HAPRNRGNSL NNTFGSGAYS SRPTSPTSSR PRTPQPSSEV TPWEFQDSQD AASSTENGRR
RSSEQTLTKP GHRAHKITSR LPGHRHHRSK EENKTAPDSR GDISATYPLR PATSREDSTY
SVRRVQQQQP SALSSAFASK TSLAPRPPSP TPSTYSEMTQ HSVAQQSQSP STSKGPGRFF
ARLRGKEKTE NHPAVDHLKN MPAASSQISL APSMNGPPST RVDPNQPSFI SRKKSTFDQL
KGPSHTVKDG KKEHRRLPFK SSDKRAMSHA EPKGKDPNDA KADAVGNEAM WFLDTKLDDM
SGIVNPQQPP MTPPTGDVQH VALAGDDEPG PKDDTWDAPD SWAVKRLDEL REQSLDEPEV
AAREQNDTKT YCLRIFRADS TFATLSATLN TTVAEIIQIL GKKTVLQDEL DNYHIVMRKH
DTSRQLESNE RPLLIQKRLL EQAGYSDADR LEDVGREDNS YLCRFTFLPA KMSGFSSLEK
DPGFKQMQKF SHIDLQGKNL ITIPITLYQK ATEIISLNLS RNLSLDVPKD FIQACTNLRE
IKYTSNDARR LPPSLSMASR LTMLDISNNC LQTLDRAELH KLQSLQGLRL SNNGLTSLPS
YFGQYRALRS LNLSSNSLTE FPDFLCEVRT LVDLDISFNS ISSLPKIGQL TCLERLWATN
NKLSGSFPPT LSNLVNLREV DVRFNALDSM DVMSQLPRLE FLMIGHNSIS AFEGCFPKIR
VLHMNHNPVT RFGLSGPVPS LTVLNLASAK LAQLPEDLFQ KLTGLTKLIL DKNHFTSLSN
NIGRLYRLEH LSVARNSLDE LPAEIGRLVE LRYLDVRENN LGRLPPELWY ARRLETLNVS
SNVLYAFPKP SAAPPQEANS GIQLDGSHSL STPGPAASPS YEELGKLEDF QHRRPSQASG
GYLSSGTSPA SSTRKGSMAS FNTASTARKP SAVTRVPTEG TVTSTMTRKD SSLSSRLVTT
FAGSLRHLFL ADNRLEDNVF DELCLLPELR IVNLAYNLIY DIPPRTIRRW QHLAELYLSG
NDLTSLPSED LEEVGSLKVL HINNNKFQVL PAELGKVAQL AVLDVASNSL KYNVSNWPYD
WNWNWNHKLR YLNLSGNKRL EIKPSGSYSG SGAAMREGRD LTDFTALVSL RVLGLMDVTM
MIPSVPEQTE DRRVRTAGSA VGTMAYGMAD SLGRTEHIST MDMVVPRFRS HDDEQVLGLF
DAQPLAGGGS KIAKFLYDNF KNRFADELDR LRPNENPVDA LRRTYLGLNK ELATSASQSL
DKNAYTPPTQ PRGAVPELGD DDLTSGCVAT VMYLKEMELY ISNVGDAQAL LIRSEGGHKI
LTRKHDPAEP SERARIREAG GFVSRQGKLN DVLEVSRAFG YVQMSPSVIA SPHILNLTLG
DTDEMILVAS RELWEYLTPD FAVDVARSER NDLMRAAQKL RDLAIAFGAT NKIHVMLLGV
SDLKSKQRAR FRTHSMSMGP SGSPDDFLVG RRPGKRARNM VGDSKLARLD QEVDAPTGEV
SLVFTDIKSS TLLWETYPIA MRSAIKMHNE LMRRQLRIIG GYEVKTEGDA FMVAFRTVTS
ALLWCFTIQS QLLEVQWPQE ILNSVNGQEV VDPDGNVIFR GLSVRMGIHW GRPVCEVDPV
TKRMDYFGPM VNRASRISSV ADGGQITVSS DFIAEIQRLL ETHIEGDRSN STGSEEAFGD
DVHSQLIRQE LRSLSSQGFE VKDLGERRLK GLENPEYIYL MYPHSLASRL VVQRQLEQQA
ASSTQESSMG QKMPGSQLTI DTEDVWDLWN ISLRLEMLCS ALENPGSSEL KAPETALLER
MKNRGGEITD RFLINFVEHQ ISRIESCATT LALRHMMRPM GSAPLLQQAC HMGDIFSELE
AKLKRLEQFE QEAMADMAPS
//
