TP_NEOBT
ID TP_NEOBT Reviewed; 564 AA.
AC Q6F5E3;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Aspyridones efflux protein {ECO:0000303|PubMed:14745177};
GN Name=TP;
OS Neocamarosporium betae (Beet black rot fungus) (Pleospora betae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Neocamarosporium.
OX NCBI_TaxID=1979465;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION OF GENE CLUSTER.
RC STRAIN=PS-16;
RX PubMed=14745177; DOI=10.1271/bbb.68.146;
RA Toyomasu T., Nakaminami K., Toshima H., Mie T., Watanabe K., Ito H.,
RA Matsui H., Mitsuhashi W., Sassa T., Oikawa H.;
RT "Cloning of a gene cluster responsible for the biosynthesis of diterpene
RT aphidicolin, a specific inhibitor of DNA polymerase alpha.";
RL Biosci. Biotechnol. Biochem. 68:146-152(2004).
CC -!- FUNCTION: Efflux pump that may be involved in the secretion of leporins
CC (PubMed:14745177). {ECO:0000305|PubMed:14745177}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR EMBL; AB114137; BAD29973.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6F5E3; -.
DR SMR; Q6F5E3; -.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 2.
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 Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..564
FT /note="Aspyridones efflux protein"
FT /id="PRO_0000438564"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 564 AA; 60191 MW; 203CE6B6DD79F3F5 CRC64;
MHPDQADTAA MQQQTTTECS DRSRPEKAEE GHAREHTVTR TCSREPEQTA TATKPTGLKL
ICLTTAICLT IFLISVDFSI LATAIPAITA EFKSVADIGW YGSSYLLTTA SSQLLLGKCY
TVFDLKWTFL LALLTFEVGS IICATAPSSV VLIIGRAIAG CGNAGLLSGA LLILTHSVPL
EKRPLFMAMT GGTYGVAAIA GPPLGGVFTD KLSWRWCFWI NLPIGALTFL VIVFLFKSPP
RSGFDGSRSW LAKVMRFDPV GTLMFMPAII CVLLALQWGG TTHAWNSGIV VALLVVGGVL
VIAFGIVQWL MHDDATIPLR IIKKRTIWAC AAYQFALGAA FFVFIYFLPI WFQGVQGASA
IQSGVRTLPM LVGNIVATAV SGVLVTIIGY YAPFMILGTI LASVGAGLLL LFTPNVTAAS
WIGYQAIVGL GIGFGWQQPF VAVQTVLDIK DVPIATATLS FAQTLGGTLF VSVAQTAFST
KLTQELVSQV PQLDPASILH EGGAAELDKL VPEQYLPDVV LSYNNSLLSA FFVATIMAIM
SLVGCTFVEW NSVKGKKADA VPAA