ID   UCSM_ACRSP              Reviewed;         599 AA.
AC   A0A411KUQ2;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=MFS-type transporter ucsM {ECO:0000303|PubMed:29373009};
DE   AltName: Full=UCS1025A pyrrolizidinone biosynthesis cluster protein M {ECO:0000303|PubMed:29373009};
GN   Name=ucsM {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. Proton-
CC       dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC       {ECO:0000305}.
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DR   EMBL; MH375776; QBC88157.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A411KUQ2; -.
DR   SMR; A0A411KUQ2; -.
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; IPR036259; MFS_trans_sf.
DR   InterPro; IPR000109; POT_fam.
DR   PANTHER; PTHR11654; PTHR11654; 1.
DR   Pfam; PF00854; PTR2; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..599
FT                   /note="MFS-type transporter ucsM"
FT                   /id="PRO_0000450534"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        424..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        454..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        539..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        563..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          23..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   599 AA;  65669 MW;  A9426FF5F2946D36 CRC64;
     MKHADPLRAD TLGTAPLSQA IEAHHHGKER EAHRQSLSSV PGDTVVEAPE KVVDLEINSV
     DNDKEHHRAP TRDEIQTLRK VPGSIPATAY LLCFVDFAER ASWFGARSVS SNFMQFPLPE
     GGNGAGAPPS GSELPAGALG HGQRFSVALG LVFSFLSYVI PIFGAWLAEA KVGRYRTILI
     GVLIGGVAHI IMIAGAVPSI LQAGKGTAPF LVSLFLLALG AGLFRPNVSP TVLDQHRHYQ
     PFVKELPSGE NVIIDPEATM QRIMLIFYAL INVGAFYSLA TVYSEKLVGY WLAFLLPGII
     YLLLPLMLWY LNDKLIKVPP DGGALTKFWK ILTVSLVENK GMVWKKGFFD RVQPGALLQK
     YPSSGPVKWT SKDVEDVKRT LVACEIFLYF PIYHLNDGGV GTILPSQGAA MLKKGVPNDL
     LGNFNPITIM ITVPVLTYIV YPALRKSNIK FGRISRITLG FWLAVISGLV SSLVQWRIYK
     TSPCGYHATT CPEVAPVSIW WQLPSYVLGA LSECFSNVTG YELAYARSPP GMRSLVVSLF
     LFSTALSSAL GLILTPAIVD PHLVWVWAGP TIALAVQTVI FWVRHRKYND DEFMIEGDE