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Database: UniProt
Entry: A0A1L9U779_ASPBC
LinkDB: A0A1L9U779_ASPBC
Original site: A0A1L9U779_ASPBC 
ID   A0A1L9U779_ASPBC        Unreviewed;       730 AA.
AC   A0A1L9U779;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Geranylgeranyl pyrophosphate synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASPBRDRAFT_135175 {ECO:0000313|EMBL:OJJ67547.1};
OS   Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ67547.1, ECO:0000313|Proteomes:UP000184499};
RN   [1] {ECO:0000313|Proteomes:UP000184499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC   {ECO:0000313|Proteomes:UP000184499};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
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DR   EMBL; KV878693; OJJ67547.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9U779; -.
DR   STRING; 767769.A0A1L9U779; -.
DR   VEuPathDB; FungiDB:ASPBRDRAFT_135175; -.
DR   OMA; IDNEHEF; -.
DR   OrthoDB; 5770at2759; -.
DR   Proteomes; UP000184499; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046165; P:alcohol biosynthetic process; IEA:UniProt.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:UniProt.
DR   CDD; cd00867; Trans_IPPS; 1.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 2.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   PANTHER; PTHR12001; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR12001:SF72; THIJ_PFPI FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G01210)-RELATED; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   Pfam; PF19086; Terpene_syn_C_2; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000184499};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..390
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   730 AA;  81778 MW;  2B6F27174869D57F CRC64;
     MFKQYSHILS HKRRRSRGST INQVLSGAQS EPASEAATVT EQPVEVWTHS QVLPEDDEHR
     KDCFTTLTPR IHKYDHVAQR GSDRFVQDLT AALNLDEPQT SYLSSPVGNY ASFLYPECLP
     ERLETVAYLT ELGNLHDGKQ QGKKTDESAE SPRVAARKEL LEKAMSELSD KDKDGHEIID
     CYRSNWLVTP EVPTAENCAN LDDYVARRRL NAGIDVYWTL MGFAHGTRLG KEDQAVVRDA
     LDAAERTMFF TNDYYSWPKE KRVSKKRPVA NVILFLMEHQ NMSEEDAVAK AKQLIIDNEH
     EFVRRREALY QANADLAPQL RKWMEVLGAS LAGIHYWCKN APRYAVPETA EESEEDEEES
     SSEEDGSEEE SSSEEDTEDD DEEEEEGEEK AAPVEVVPEP EESEEPVEVA VWTPLVTEEE
     TPDVHLDTSA LLAPSSYARS ISRSTLHSDL LTSLNAWLQV PARPLAFIRQ VVTELQDSTG
     MLADVQDQAA LRDQRTPAHL VYGPAQCMNS AAYLFVRAAR IVTSLNCPGM LDALLQELEA
     HFVGQSWELN WRFSTHCPGE TEYLAMVDQK AGASFRLLTR LMQAASMGGA TLDLDPFTKV
     LGRLSQIRHE YLGLLESATN ERSFGEDLDQ AKVTYPIVRA CNLDPAGRAV IFGIFRQKPA
     GTVLPIESKR QIVSLVQQTG ALQATYDLIR QLGREAMNTL SELETAAEEL NPSLRAVVKS
     LVEVPAPEHL
//
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