ID A0A0R3QM93_9BILA Unreviewed; 235 AA.
AC A0A0R3QM93;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyldiphosphate specific] {ECO:0000256|ARBA:ARBA00012596};
DE EC=2.5.1.87 {ECO:0000256|ARBA:ARBA00012596};
GN ORFNames=BTMF_LOCUS6879 {ECO:0000313|EMBL:VDO22915.1};
OS Brugia timori.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0000882801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BTMF_0000882801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO22915.1, ECO:0000313|Proteomes:UP000280834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-
CC trans,poly-cis-polyprenyl diphosphate + n diphosphate;
CC Xref=Rhea:RHEA:53008, Rhea:RHEA-COMP:13431, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:136960, ChEBI:CHEBI:175763;
CC EC=2.5.1.87; Evidence={ECO:0000256|ARBA:ARBA00000976};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SIMILARITY: Belongs to the UPP synthase family.
CC {ECO:0000256|ARBA:ARBA00005432}.
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DR EMBL; UZAG01015733; VDO22915.1; -; Genomic_DNA.
DR STRING; 42155.A0A0R3QM93; -.
DR WBParaSite; BTMF_0000882801-mRNA-1; BTMF_0000882801-mRNA-1; BTMF_0000882801.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000050602; Unplaced.
DR Proteomes; UP000280834; Unassembled WGS sequence.
DR GO; GO:1904423; C:dehydrodolichyl diphosphate synthase complex; IEA:InterPro.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0045547; F:dehydrodolichyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019408; P:dolichol biosynthetic process; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1180.10; Decaprenyl diphosphate synthase-like; 1.
DR InterPro; IPR038887; Nus1/NgBR.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR21528:SF0; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE COMPLEX SUBUNIT NUS1; 1.
DR PANTHER; PTHR21528; UNCHARACTERIZED; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; Undecaprenyl diphosphate synthase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000280834};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ SEQUENCE 235 AA; 27442 MW; 23EAB1E70470036E CRC64;
MLNVVVEWLR FAYTFLEVIL NYISKPSLII KSLFYSADSN SQSHQLPNHL AVLYTDKYAI
SLEALSKLIV HSASAGITRL TLYDPWSYIF SKRELLRRLT HDIMRKACSK QLVDVEFYDS
DHFMINPNIT YTTVKILGAR DGRQSIVRAC RRLCMECAPE NITIEKISEY LAREHIWEPD
FLLQIGDLGT MADYSPWVLR ITEILQLKSL PSNFSYQQFL SYLHEYSSRD RRIGR
//
