TWMF_TALWO
ID TWMF_TALWO Reviewed; 549 AA.
AC A0A2L0P0L8;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=MFS-type transporter TwmF {ECO:0000303|PubMed:29343058};
DE AltName: Full=Wortmanamides biosynthesis cluster protein F {ECO:0000303|PubMed:29343058};
GN Name=TwmF {ECO:0000303|PubMed:29343058};
GN Synonyms=TwnF {ECO:0000303|PubMed:29343058};
OS Talaromyces wortmannii (Penicillium wortmannii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28567;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 26942 / CBS 387.67 / CCM F-175 / VKM F-2091;
RX PubMed=29343058; DOI=10.1021/jacs.7b13350;
RA Hai Y., Tang Y.;
RT "Biosynthesis of long-chain N-acyl amide by a truncated polyketide
RT synthase-nonribosomal peptide synthetase hybrid megasynthase in fungi.";
RL J. Am. Chem. Soc. 140:1271-1274(2018).
CC -!- FUNCTION: MFS efflux transporter; part of the gene cluster that
CC mediates the biosynthesis of wortmanamides A and B, reduced long-chain
CC polyketides amidated with a specific omega-amino acid, 5-aminopentanoic
CC acid (5PA). {ECO:0000269|PubMed:29343058}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; MG837523; AUY61974.1; -; Genomic_DNA.
DR EMBL; MH399766; QBC19708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L0P0L8; -.
DR SMR; A0A2L0P0L8; -.
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..549
FT /note="MFS-type transporter TwmF"
FT /id="PRO_0000452492"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 549 AA; 59380 MW; 0EF73E3B384C2966 CRC64;
MKSPSSSAEM QSSSPEPAPW KPDFQVYAIV IGLGITNLLA ALENTVLTIA APVVLTDLEL
GENFIWVTNA FFLSSTAILP LFGQFSNIFG RRYVMLTAVA IFVLGSGLCG GASTGAMLIA
GRAIQGVGSG GIIMLSSIII SDLVPLRQRG NFSAILMSIL GIGSALGPLI GGAIVSSISW
RWVFYLNLPI GGVSFVFLFI FLRVKYNKEM TFWQKIKRID LVGNAIVIAS TVAILYALSY
AGTRYPWRSW HTLVPLLVGF LGLFIFAGLQ TTAFSAEPLM PTRFFRAPTS IILAINTFVS
AALLYWCLFF LPVFLQSVKL YSPRRAGVAL LPISLLGIPG SMVGAIALVR WGRYKPVHIF
AFALQTLGLG LFTLFREDTS VAEWAVFQCI VAFGGGMIFT TMLPAFQAFI HERDIAACTA
AWYFIRLFGH IWGVAIPAAI FNQRIDTLLG QGAISDPSVS KTIAAGGAYQ AASAAFVKQF
PGSLQLEIRS VYSQAIQRVF QVSIAFAGVA FLLTLLEKDV GLRKTLETDF GLEKEGAGQQ
ADVEGRSHE