ID   A0A166DAF6_9AGAM        Unreviewed;       347 AA.
AC   A0A166DAF6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Terpene synthase {ECO:0000256|RuleBase:RU366034};
DE            EC=4.2.3.- {ECO:0000256|RuleBase:RU366034};
GN   ORFNames=PENSPDRAFT_755041 {ECO:0000313|EMBL:KZV67273.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV67273.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV67273.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV67273.1,
RC   ECO:0000313|Proteomes:UP000077086};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|RuleBase:RU366034};
CC   -!- SIMILARITY: Belongs to the terpene synthase family.
CC       {ECO:0000256|ARBA:ARBA00006333, ECO:0000256|RuleBase:RU366034}.
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DR   EMBL; KV424580; KZV67273.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166DAF6; -.
DR   STRING; 1314672.A0A166DAF6; -.
DR   InParanoid; A0A166DAF6; -.
DR   OrthoDB; 1534248at2759; -.
DR   Proteomes; UP000077086; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR034686; Terpene_cyclase-like_2.
DR   PANTHER; PTHR35201; TERPENE SYNTHASE; 1.
DR   PANTHER; PTHR35201:SF4; TERPENE SYNTHASE; 1.
DR   Pfam; PF19086; Terpene_syn_C_2; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|RuleBase:RU366034};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU366034};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU366034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077086}.
SQ   SEQUENCE   347 AA;  40104 MW;  641EB3F9165DC1CC CRC64;
     MILNASSEHE MSFRLPDLLT LCHPFTGATS PHHAQAAAES SAWIAHFTPS LFNGDDHTSF
     VLESKESELL ISHTYPHAPY DRFRTLCDYM NILFVLDEVC EKQDGTGARE TGYRYLKSMR
     DVDWDDGSVI ARMIKQFRAR LLRSCGPQSF ARLLQLSTDY VAAQAREAEL RETRTVLDPE
     SFRTVRRENS AIRLCLGLIE FSLGIDLPDE VFKDEEFMTL YWAVVDMVDL ANDLYSYERE
     QYLGAADHNN ITVVMRAYGM SLQDASMYLG EQYADMMRIY MDAKNRLKAR SFGDEQLDAD
     VMHYVEAMEF WPIGNINWSL ETVRYFSRPD EVKRTRLVVL RQRKVEG
//