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Database: UniProt
Entry: A0A094K6A2_9PEZI
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ID   A0A094K6A2_9PEZI        Unreviewed;      1230 AA.
AC   A0A094K6A2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   10-MAY-2017, entry version 14.
DE   RecName: Full=Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific) {ECO:0000256|RuleBase:RU363018};
DE            EC=2.5.1.87 {ECO:0000256|RuleBase:RU363018};
GN   ORFNames=V501_01945 {ECO:0000313|EMBL:KFZ17003.1};
OS   Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ17003.1, ECO:0000313|Proteomes:UP000029315};
RN   [1] {ECO:0000313|EMBL:KFZ17003.1, ECO:0000313|Proteomes:UP000029315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A.,
RA   Gerasimov E.S., Kochkina G.A., Ivanushkina N.E., Vasilenko O.V.,
RA   Kondrashov A.S., Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence
RT   of horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adds multiple copies of isopentenyl pyrophosphate (IPP)
CC       to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl
CC       diphosphate (Dedol-PP), a precursor of dolichol which is utilized
CC       as a sugar carrier in protein glycosylation in the endoplasmic
CC       reticulum (ER). {ECO:0000256|RuleBase:RU363018}.
CC   -!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + n isopentenyl
CC       diphosphate = n diphosphate + ditrans,polycis-polyprenyl
CC       diphosphate (n = 10-55). {ECO:0000256|RuleBase:RU363018}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|RuleBase:RU363018}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family.
CC       {ECO:0000256|RuleBase:RU363018}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|RuleBase:RU363018}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KFZ17003.1}.
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DR   EMBL; JPKD01000693; KFZ17003.1; -; Genomic_DNA.
DR   EnsemblFungi; KFZ17003; KFZ17003; V501_01945.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000029315; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00475; Cis_IPPS; 1.
DR   Gene3D; 3.40.1180.10; -; 1.
DR   HAMAP; MF_01139; ISPT; 1.
DR   InterPro; IPR001441; UPP_synth-like.
DR   InterPro; IPR018520; UPP_synth-like_CS.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   PANTHER; PTHR11629; PTHR11629; 1.
DR   Pfam; PF01255; Prenyltransf; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
DR   SUPFAM; SSF64005; SSF64005; 2.
DR   TIGRFAMs; TIGR00055; uppS; 1.
DR   PROSITE; PS01066; UPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029315};
KW   Membrane {ECO:0000256|RuleBase:RU363018};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029315};
KW   Transferase {ECO:0000256|RuleBase:RU363018};
KW   Transmembrane {ECO:0000256|RuleBase:RU363018};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU363018}.
FT   TRANSMEM    784    809       Helical. {ECO:0000256|RuleBase:RU363018}.
FT   TRANSMEM    829    848       Helical. {ECO:0000256|RuleBase:RU363018}.
FT   TRANSMEM    908    926       Helical. {ECO:0000256|RuleBase:RU363018}.
FT   TRANSMEM    938    961       Helical. {ECO:0000256|RuleBase:RU363018}.
FT   TRANSMEM   1017   1036       Helical. {ECO:0000256|RuleBase:RU363018}.
FT   TRANSMEM   1130   1149       Helical. {ECO:0000256|RuleBase:RU363018}.
FT   TRANSMEM   1161   1182       Helical. {ECO:0000256|RuleBase:RU363018}.
FT   COILED      461    488       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1230 AA;  140012 MW;  0090EC387CBAC4C5 CRC64;
     MTSMHLNQLR KWVYSSPPVE WGMNQLRELL IGAVSQGPVP QHIAFVMDGN RRFARSHKIE
     TAEGHNLGFE SLAKILEVCY KLGVKVITVY AFSIENFKRS KYEVDALMDL FKVKLAQISQ
     HGELLDQYGA SIRILGQRDL IRPDILEACN NAVEVTRGNG DAILNICFPY TSRDEITTAI
     RSTVDELSTP LPTPKRPFSE RRIAQKLRSR NLTSTSSSPP RQASPTRVEV PGAGVELDDS
     ISSSATLHPD SVSSSDLPNP EEPTYPDPES ITAATVEAHL FTAGNPPLDL LIRTSGVNRL
     SDFMLWQCHE DTQLRFLDCY WPEFSLRHFL PVLIEWQWQR KYGDDKEGGA VKTRPKFFAI
     MAPAKDTMFR SVDMSMVQLY VANEIGREVI NALGEIGQIQ FRDLNSETSA FQRTFTQEIR
     RLDNVERQLR YFHSQMEKAG IPLRKLDLDI ESLAAPSTSE IDELSDRSQS LEQRVASLND
     SYETLKKREV ELIEWRWVLK EAGGFFDRAH GNVDELRTSI DQDDDAPLLQ DVEQHPQNGD
     AGERSLSIMN IGFVSGVIPR ERVAAFERIL WRTLRGNLYM NQSEIPETLI DPTNNESVDK
     NVFVIFAHGK EIIAKIRKIS ESLGADLYAV DENSDLRRDQ IHEVNTRLSD LGSVLRNTKQ
     TLDAELTQIA RSLAAWIVII KKEKAVYETL NLLSYDHARK TLIAEAWCPS NSLPQIKAAL
     QDVNNRAGLA VPSIINEIRT NKTPPTLQKT NRFTEGFQTI INAYGTSKYH EVNPGLPTIV
     TFPFLFAVMF GDLGHGFIMF CAAAAMIYWE KPLKKVRDEL FTMAYYGRYI MLMMGIFSMY
     TGLIYNDIFS RSMSLFSSAW EWPTDFKKGD TVVAHLNRDG HRYPFGLDWM WHGAENELLF
     ANSYKMKLSI LMGWCHMTYS LCLSYINARR FKSPIDIWGN FIPGMIFFQS IFGYLVFTIV
     YKWSTDWYPL APDDWPAGVQ APNHRNPPGL LNMLIYMFLQ PDKIDVPLYG DGTYQKIIQN
     FLVVIAIIQV PILLFLKPFY LRWEHNQARA KGYRGIGETS RISALDGDDD DRRASIASET
     EGVDMITQGI DNDGEGHEEF EFGEVMIHQV IHTIEFCLNC VSHTASYLRL WALSLAHQQL
     SLVLWSMTLN NGLTSTGISG VITLVITFYM WFFLSVCVLV VMEGTSAMLH SLRLHWVEAM
     SKHFMGDGIA FEPFSFRQML EEDEEVKEFS
//
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