EUPT_PHOSX
ID EUPT_PHOSX Reviewed; 1430 AA.
AC A0A4P8GG95;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=ABC transporter eupT {ECO:0000303|PubMed:30980906};
DE AltName: Full=Eupenifeldin biosynthesis cluster protein T {ECO:0000303|PubMed:30980906};
GN Name=eupT {ECO:0000303|PubMed:30980906}; ORFNames=gme12638;
OS Phoma sp.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Phoma.
OX NCBI_TaxID=1707701;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=XZ068 / CGMCC No. 10481;
RX PubMed=30980906; DOI=10.1016/j.fgb.2019.04.004;
RA Zhai Y., Li Y., Zhang J., Zhang Y., Ren F., Zhang X., Liu G., Liu X.,
RA Che Y.;
RT "Identification of the gene cluster for bistropolone-humulene meroterpenoid
RT biosynthesis in Phoma sp.";
RL Fungal Genet. Biol. 129:7-15(2019).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=8360103; DOI=10.7164/antibiotics.46.1082;
RA Mayerl F., Gao Q., Huang S., Klohr S.E., Matson J.A., Gustavson D.R.,
RA Pirnik D.M., Berry R.L., Fairchild C., Rose W.C.;
RT "Eupenifeldin, a novel cytotoxic bistropolone from Eupenicillium
RT brefeldianum.";
RL J. Antibiot. 46:1082-1088(1993).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=18095654; DOI=10.1021/np070513k;
RA Ayers S., Zink D.L., Powell J.S., Brown C.M., Grund A., Bills G.F.,
RA Platas G., Thompson D., Singh S.B.;
RT "Noreupenifeldin, a tropolone from an unidentified ascomycete.";
RL J. Nat. Prod. 71:457-459(2008).
RN [4]
RP BIOTECHNOLOGY.
RX DOI=10.1016/j.phytol.2008.09.008;
RA Bunyapaiboonsri T., Veeranondha S., Boonruangprapa T., Somrithipol S.;
RT "Ramiferin, a bisphenol-sesquiterpene from the fungus Kionochaeta ramifera
RT BCC 7585.";
RL Phytochem. Lett. 1:204-206(2008).
CC -!- FUNCTION: ABC transporter; part of the gene cluster that mediates the
CC biosynthesis of eupenifeldin, a bistropolone meroterpenoid that acts as
CC an antitumor agent. {ECO:0000305|PubMed:30980906}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of eupenifeldin.
CC {ECO:0000269|PubMed:30980906}.
CC -!- BIOTECHNOLOGY: Eupenifeldin is a bistropolone-humulene meroterpenoid
CC first discovered as an antitumor and anti-leukemia agent
CC (PubMed:8360103). This metabolite shows also anthelmintic activity
CC against the parasitic worm Hemonchus contortus, anti-malarial activity
CC as well as antifungal activity (PubMed:18095654, Ref.4).
CC {ECO:0000269|PubMed:18095654, ECO:0000269|PubMed:8360103,
CC ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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; MK400120; QCO93116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P8GG95; -.
DR SMR; A0A4P8GG95; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1430
FT /note="ABC transporter eupT"
FT /id="PRO_0000449159"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1133..1153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1213..1233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1249..1269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1278..1298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1305..1325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1400..1420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 112..368
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 789..1032
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 825..832
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1019
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1430 AA; 159610 MW; ED9426603F22E5DB CRC64;
MAPAIDSTVN DLQPNTPNPE KALSSQAQAF VRAYSEDGDS GGQSVLGAED PLSPLNPRGE
RFNARAWAKN LAAVTRERGE GFRQVGISFQ NVNVFGYGTP TDFQKNVGNV WLALPAMIRQ
LFAPKGGQTR IDILNHFNGL VRPGEMCVVL GPPGSGCSTF LKTISGHTSG LHVNPDAHFN
YQGLSAKEMI TAHRGDCIYT AEVDVHFPML TVGETLTFAA RARSQQHLPE GISRNNYCDQ
LRDVIMAMYG IRHTIHTKVG DDFVRGVSGG ERKRVSVAEA TLANAPFQCW DNSTRGLDSA
NAIEFCRTLR LQSEIFGQTC VVSMYQAPQT AYDLFDKVLL IYEGRQIYFG STSKAKDYFV
NLGFECPARQ TTPDFLTSIT FPAERIPRPD CQPPRTPDEF SQVWKNSLEC KALQDEINEY
NMEHPINGPD ADTFRQLKQA SQAQGQKVTS PFTLTYSQQV KLCMWRGWAR FKADPWPAVW
VMVGNTIMAL IMSSLFYNMG QDTNSFYGRS VVLFMAILFN AFSSILEVMT LYAQRPIVEK
QSRYAFYHPS AEAYASVLVD MPMKITSTIS FNLVFYFMTN LNRAPGNFFF YLLVVFLIVL
AMSGVFRFIG SLSRTEQQAM VPASVLMLAL LIFTGFVVPV DYMLPWCRWI NYVNPVAYGY
EALMVNEFHG REFTCSTYIP EYANATSGTG ACSVVGATPG NLFWRNVGII IAMVIFNYLM
YFIASEYVTA KKSRGEILVF RRGHTPSIPA KGSGDLEKLE SGHATTVLER SDPSMVHKGE
GFQGSVSVFH WNNVCYDLEI KGKPRRILDN VDGWIKPGTL TALMGVSGAG KTTLLDCLAN
RRVGVGIVTG EMLVDGKVCD QSFQRKTGYA QQQDLHLETS TVREALTFSA FLRQPHSIPK
ADKLTYVEEV IKLLAMQDYA DAVVGVIGEG LNVEQRKRLT LGVELVAKPP LLLFVDEPTS
GLDSQTSWAV LDLLEKLSKA GQSILCTIHQ PSAMLFQRFD RLLFLAEGGK PVYFGEIGND
SSTLIDYFER NGAKPCLPGS NPAEWMLEAV GAAPSISSEG DWPEIWRSSP EYQSVHHELA
RLKAVDIDQL SADKPDPTSY NEFAAPLWQQ LVVVTQRAFL QSWRSPSYIY SKITLCIATS
LFIGLVFFNA PLSIQGLQNQ MFAIFEVMSI VGQLVDQQMP NFLTQRSLYE VRERPAKTYS
WMVFMLSQIV TELPWSTLAS VFMWALFYYP IGFHKNAQAA GQGTERGALM WLLFWQFLVW
VSTFTHMCIS FVDSADDGGN IANFLFVLAF FFCGVLASPS QMPRFWIFLY RASPLSYWVS
AVLSTGFANV QVTCTDKEYT AFDPPKGSTC GEYMAEYISR AGGYVKDPQA TESCGYCTIK
DTNVFLAAVS SDYDTRWRNF GILWVYIGFN IAAALALYWI ARMPKGKKRL
