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Database: UniProt
Entry: A0A166IPY2_9AGAM
LinkDB: A0A166IPY2_9AGAM
Original site: A0A166IPY2_9AGAM 
ID   A0A166IPY2_9AGAM        Unreviewed;       351 AA.
AC   A0A166IPY2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Terpene synthase {ECO:0000256|RuleBase:RU366034};
DE            EC=4.2.3.- {ECO:0000256|RuleBase:RU366034};
GN   ORFNames=PENSPDRAFT_682634 {ECO:0000313|EMBL:KZV73684.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV73684.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV73684.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV73684.1,
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; KV424487; KZV73684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166IPY2; -.
DR   STRING; 1314672.A0A166IPY2; -.
DR   InParanoid; A0A166IPY2; -.
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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU366034};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU366034};
KW   Metal-binding {ECO:0000256|RuleBase:RU366034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077086}.
SQ   SEQUENCE   351 AA;  40867 MW;  FD46291103F73A41 CRC64;
     MAVEQRQRYR LPDCLANWPW PRRLNRSYPE VKAASSAWVR SFGAFSSKAQ DAYDRCDFNL
     LTSLAYPDHN AADLRTGCDA MNQFFVYDEF SDIARPEEVQ VMANIIMDAL RDPHKPRPED
     EWVGGELTRQ FWERAIQTAS PGSQKRFLDY SAQYTQAVVQ EAEDRQNDYI RTVDEYLVVR
     RDTSGVKPCF AIIELGLSLP QEVVDHPVIK EMEILGTDMI LLFNDIASYN IEQARDDDSH
     SIATSVMHYH DTDVQGAMDW VENHHRGLEA RFLELYYHHV PKYHSCHLDA DVARYVDGLG
     NWIRANEQWS FESERYFGKR GPEIIKNRWM TLMPKERAEY IGPQLVNDVF L
//
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