ID A0A0C3F247_PILCF Unreviewed; 1517 AA.
AC A0A0C3F247;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=PILCRDRAFT_74961 {ECO:0000313|EMBL:KIM78865.1};
OS Piloderma croceum (strain F 1598).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Piloderma.
OX NCBI_TaxID=765440 {ECO:0000313|EMBL:KIM78865.1, ECO:0000313|Proteomes:UP000054166};
RN [1] {ECO:0000313|EMBL:KIM78865.1, ECO:0000313|Proteomes:UP000054166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F 1598 {ECO:0000313|EMBL:KIM78865.1,
RC ECO:0000313|Proteomes:UP000054166};
RG DOE Joint Genome Institute;
RA Kuo A., Tarkka M., Buscot F., Kohler A., Nagy L.G., Floudas D.,
RA Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F 1598 {ECO:0000313|Proteomes:UP000054166};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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; KN833013; KIM78865.1; -; Genomic_DNA.
DR STRING; 765440.A0A0C3F247; -.
DR HOGENOM; CLU_000430_1_1_1; -.
DR InParanoid; A0A0C3F247; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000054166; 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 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 PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 11.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00332; PP2Cc; 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:UP000054166};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 93..184
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 815..1103
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1157..1293
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1517 AA; 169221 MW; 65A707F9AAB4DB5F CRC64;
MLEKVSPKTQ APPVVLAVPP PIDGLASSAA SWEAPQSWAV EKDGEDPAEP PDYSSSEDSV
AIGHHAPKKH RSHRTSTRPK PPLKAAKPCI TNKPFKVRIY RANNTYHVAS IGLSVTVADL
APVLNTKLLL ESERETHRLY LKERGRERIL AQTERPADIV RRRLEQAGYD LADGLDLLGA
EDITFLMKFV YKTQLLGPAE EDLSFDTFEH IDLTGRSLRA IPVVLHTRAD TITTLNLSRN
PMLEIPLDFI QSCVTLRELR LSNMAMKRVP QSVRHCITLY RLDLSCNRIV ELNEAGLDQI
PKLATLNVQN NRMEKLPWYF PRLRMLRHLN ISNNKFRTLP PVVCEMASLV DLDISFNMIS
ELPDEIGQLK LLDRLIIVGN QVQKFPDECR GLVSLRDLDC RRNNILDLSV VCMLPKLEIL
RADHNTIYAL DLSLGPSLKT LDASHNDITQ ITLVPGPVGT CSPYALTSLD ISYAKLSSLD
EFALGQLSSL EILKLDHNSF RYIPESLGEL SQLRRLSCSD NALDALPSSI GRLQRLETLD
AHNNSLVELP ISLWNCASLC HINVTSNQLG IWHDPPTSTV NPADSPPTST RSILIHPERK
TSATGSIGSQ SGRTIPPLAH SLERLYLGEN NLTDDVLHPL TILKELRVLN MSFNEIQEIP
PSFFRNLIKL EEVYLSGNKL TSIPTEDLHR LTRLSVLFLN GNKLQTLPHE LGKIQSLAVL
DAGSNVLKYN INNWQFDWNW NFNPNLKYLN LSGNKRLEIK PDATGHKMQS TKDQHGRKVL
ADFSSLNQLR VLGLMDVTTT FLPNIPDDNE ERRVRTSLSE VNNMAYGIAD HLSGSDYLNM
LDLVQPHFRD NKEEAVFAMF GRAQPSTGSN RLSKYLHDKF LSVFTQQLDT LDKSKKEGVS
DALRRSFLRL NKYLHDELYN STGVNRKMSQ ASASSTGAAS ILDQAPVRSG ASGIVMYIAG
KTMYVANAGN ALAVISKQGA AELVSKKHDP FDRAETARIR AAEGWVSPKG FVNDEIDISR
SFGFYHLLPV VNARPDIYMR DLSELDEFVI IGNRGLWDYV SYQTAVDIAR SERADPMIAA
QKLRDFAISY GAKGSTMIMV ISIADLFNPG RARPSTVPSL GDYEPPSSKY KRTKQTVLDP
GLNWLDEEPP PPIGHVALVF TDIRNSTHLW EANAGMQTAM RIHHTLMRRQ LRFFGGYEVK
TEGDAFMCSF PTALSALLWC LRIQVQLLHE AWPLEILECH DGKPVYDANG TLIARGLSVR
MGVHCGTPVC EIDPVTKRMD YFGPMVNRSA RICGNAAGGE IMCSAEILRE INASIFETGP
FTEYSEFQPP SIIDAIRRMG VVVIPKGEYK LKGLELPEAL SLVYPKELAG RVDLEEFESE
PSASASRVQF SIEQTRQLGL LCLRLEALSS SRIFRPSPQR KASASKESSD GQIEDGQQLS
NIMYGDASLL LPPIHQKLSD AELMTILDSL SIRIENALVA LSQIFRPQSQ SITSTLRGVD
ERTLQEILSM LQGRSSL
//
