ID   UCSD_ACRSP              Reviewed;         586 AA.
AC   A0A411KUX1;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=MFS-type transporter ucsD {ECO:0000303|PubMed:29373009};
DE   AltName: Full=UCS1025A pyrrolizidinone biosynthesis cluster protein D {ECO:0000303|PubMed:29373009};
GN   Name=ucsD {ECO:0000303|PubMed:29373009};
OS   Acremonium sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium;
OC   unclassified Acremonium.
OX   NCBI_TaxID=2046025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=KY4917;
RX   PubMed=29373009; DOI=10.1021/jacs.8b00056;
RA   Li L., Tang M.C., Tang S., Gao S., Soliman S., Hang L., Xu W., Ye T.,
RA   Watanabe K., Tang Y.;
RT   "Genome mining and assembly-line biosynthesis of the UCS1025A
RT   pyrrolizidinone family of fungal alkaloids.";
RL   J. Am. Chem. Soc. 140:2067-2071(2018).
CC   -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC       the biosynthesis of UCS1025A, a member of the pyrrolizidinone family
CC       that acts as a strong telomerase inhibitor and displays potent
CC       antibacterial and antitumor properties (PubMed:29373009). These
CC       compounds share a hemiaminal-containing pyrrolizidinone core fused with
CC       a gamma-lactone, giving a furopyrrolizidine that is connected to a
CC       decalin fragment (PubMed:29373009). {ECO:0000269|PubMed:29373009}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {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; MH375767; QBC88148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A411KUX1; -.
DR   SMR; A0A411KUX1; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..586
FT                   /note="MFS-type transporter ucsD"
FT                   /id="PRO_0000450533"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        458..478
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        532..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   586 AA;  62810 MW;  5D30A6047237D107 CRC64;
     MSRNSGTTLE DGPLHADPTT EAPNNATVTT NVTANDENTE KEVDADAAAA APAEAPKPNQ
     GFRFWAIVAA LAFTALLSSL EGTIITSALP KITADLGGGN SFIWVPNGYF LATIVMLPLM
     AQASNLFGRR WLTLISVATF TLGSGICGGA NSQAMLIGGR VVQGFGGGGI ALMINIILTD
     LVPLRERGKY MGIVQMVSAV GAALGPFLGG LLTSKSTWRW VFYINLPIGG TSLVALFFFL
     RVAKPPPTTL AEKISRIDFS GNAIFIASTV SVLIGVTWGG AVYPWSSFRV IVPLVLGFFG
     LGLFVVYEWT VAKNPSLPKD IILNRTAATV LGVTFLHTVA TYWSFYFMPI YFQAVKGETS
     FWSGVDTLPL FAGIFPFAIL GGMLLAKFGR YKPMHLIGMA IITLSFGLFS LLDQGSSKAA
     WACFQLLFAV GAGLMIAILL PAMQAPLPES LVALSTGVWT FVRGFGTVWG VTIPSAIFNN
     QCRLKAADLS DQGVASHLNS GKAYQYATKD FLDSIHDDAT RRQVVELFTS SLRTVWYVGV
     ALAGFGWLLI WLEKEVTLRS KLNTKFGLEE KKKAAKADED VESASA