ID A0A165DES2_9APHY Unreviewed; 335 AA.
AC A0A165DES2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Terpene synthase {ECO:0000256|RuleBase:RU366034};
DE EC=4.2.3.- {ECO:0000256|RuleBase:RU366034};
GN ORFNames=LAESUDRAFT_657286 {ECO:0000313|EMBL:KZT04728.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT04728.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT04728.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT04728.1,
RC ECO:0000313|Proteomes:UP000076871};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV427634; KZT04728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165DES2; -.
DR STRING; 1314785.A0A165DES2; -.
DR InParanoid; A0A165DES2; -.
DR OrthoDB; 1534248at2759; -.
DR Proteomes; UP000076871; 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:UP000076871}.
SQ SEQUENCE 335 AA; 38056 MW; C74A62A36B638305 CRC64;
MSYCTKIIRL PDIMDAIPFP IRMNPYTRFL SAASDTFILA STNFTEKQRS RFLGLKAGLL
CGMSYVESGP EKLRVCMDFT SFLFCLDDWS DEFNTTQTET LEAVVMNTLR YPEIFYSNTV
AARITKSWWK RMLKNIGPRC KERFISSMDL YFKAITQQAA DRASKHVSEL DAYISLRRDT
SGCKAGFVLI EYATYIDLPD EVYENLVVQD LMDAANDSVS WGNDIFSYSR ERSRGDPHNL
VAVIAHAFGI GQQAAVDHAA AMCNETVERF LACKAALPSW GRVVDAQVET FVRGLEDWMI
ANAEWSFVTE RYFGKNAPQV RKSLRVHLLP VVNPL
//
