ID   A0A165GKN7_EXIGL        Unreviewed;       351 AA.
AC   A0A165GKN7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Terpene synthase {ECO:0000256|RuleBase:RU366034};
DE            EC=4.2.3.- {ECO:0000256|RuleBase:RU366034};
GN   ORFNames=EXIGLDRAFT_750528 {ECO:0000313|EMBL:KZV90662.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV90662.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV90662.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV90662.1,
RC   ECO:0000313|Proteomes:UP000077266};
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; KV426044; KZV90662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165GKN7; -.
DR   STRING; 1314781.A0A165GKN7; -.
DR   InParanoid; A0A165GKN7; -.
DR   OrthoDB; 1534248at2759; -.
DR   Proteomes; UP000077266; 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:UP000077266}.
SQ   SEQUENCE   351 AA;  39838 MW;  6ED3BC379C865486 CRC64;
     MVGSTNTVES FNLPDLLAAS SRFVSRLNAH YDQAMAECRT WLIAHEVVGD KTERVFAMSD
     IERLCARAYP SAPYDKFLTV CEFVCLMFAI DEVCDVQGGA DAKRTGERFL NALRGKERDD
     YDEPNAGLMH AAREIHVRLG DWLDSDAGRR FIEVCEGYIE CVVEESALRE DGKVLSLEEY
     EPIRRENSGV RPSIAITEFA LGLSLLDTVY TNEHFLTVYW TVSDMVWWAN DIYSYAVEYQ
     KGLDGNNVLT VLMSDKTLDL QAASDYAGEH YKTLIRRHWA AREALAQLTF GSPEIDAQVA
     LFVEEMANWA IGNAVWSFET RRYLGDDGLE VKESRRAVLR TRFSDEKRMP A
//