ID   A0A0V1P3W4_9BILA        Unreviewed;      1084 AA.
AC   A0A0V1P3W4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Farnesyl pyrophosphate synthase {ECO:0000256|ARBA:ARBA00034546};
GN   Name=FPS1 {ECO:0000313|EMBL:KRZ90779.1};
GN   ORFNames=T08_8752 {ECO:0000313|EMBL:KRZ90779.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ90779.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ90779.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ90779.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Pheromone biosynthesis. {ECO:0000256|ARBA:ARBA00033740}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ90779.1}.
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DR   EMBL; JYDM01000052; KRZ90779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1P3W4; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0042811; P:pheromone biosynthetic process; IEA:UniProt.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 6.10.280.150; -; 2.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR   InterPro; IPR039702; FPS1-like.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   InterPro; IPR003124; WH2_dom.
DR   PANTHER; PTHR11525:SF0; FARNESYL PYROPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR11525; FARNESYL-PYROPHOSPHATE SYNTHETASE; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   Pfam; PF02205; WH2; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SMART; SM00246; WH2; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS51082; WH2; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        45..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          665..682
FT                   /note="WH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51082"
FT   REGION          395..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..628
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1084 AA;  121210 MW;  8E3C2BA30B7ECB5B CRC64;
     MIDGSMPQCV EKLTDTSEFI TKKFFMLFFT ADDARFENDP LNIKAVVYLS AIFAPYILIS
     AVIYVLLLMP CCKREFLLRI CGIALRVGVM FVRMRLFRGK FLLFFLSIDE SLAMEMNLNK
     QNRKYRAKLM RTGQRANNSV ATVVVQYGWI VVVEMPLTKR EVSPVLLCRH RLPSGVRDKE
     LQCIANGTLA NLIRQLGSLS SHAEDLFAEL SKDLIKIEHR TNLLQTRLDS LGQKVNDLDS
     GIDETSIRSF YLRKPFKSKP LIDQQSLSRH TMPTAMGLRY QRCCPPPRLD KLDCFRDDGK
     SAMKFYTDPD YFFELWRCEM LGNGDNAKRA TKANAKLKDV HDGRKRTEQL ENRQQAAPYL
     ATSRKNLANA DSDLYIPARV VDVAALDAGA QKVIHSTVDS RTSSTRMPAD YNFPASTTTT
     TTRDRQQSTT GLTKMPTSRV GTGQSSSAYP YGQSGRWCPP TNDNNNGAAS NDQYSSCKSP
     LRPSQPPPLP PGQPLSTNQL DVQSSSIHGR PCYYGDQELT VRMENWHLGE DDQRRQFHET
     TVDEPMGQQF QNGHRPTAVK SVSPELPPPP PPLSTAHVGE VALRPDQSPI GNPASSDALP
     PPPPPPPPPP PPPPPPPPPP PPPPSSQQQS LPANGQAVGA GGDAARPAKA PLPFSAGVPV
     EVIDTRSDLL KAIRQGIQLK KVDRQEEQKR ESNAAKEGHD VAAILKRRME YLFVASFILA
     MTFFSIAQYD IIDEKDEILN PNNTSSSTPP RQCSSRCSLL QFSGGEMNQP LLTALRRFTN
     NQQLLANLLE QTAGGKGIRG RLLTGALEAN VLFDDRTSLA QKAHTIASAV EMLHAGFLIQ
     DDIMDNASTR RGKPCWYRQV GLSGINDGVL LQSAASWLPS VVLDDHPQKH AIVSSFVEAT
     VITSLGQKLD MEKARPDTCS WDRYRELVTN KTAHYSFWFP LKVGLLLADV QLEEVEIELK
     NICYEFGFYF QAKDDYLNCF GDEWVTKKHS SDIACGKLTW LLLTAVDMSK LDGDRLKIIW
     QNYAQSEQRM IQEVRSLYEQ LDLRGKFQLF EQAVVEKLST LVCRLKMPQL CPVLFEMLHL
     IKNQ
//