PHQF_PENFE
ID PHQF_PENFE Reviewed; 411 AA.
AC L0E4G6;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=MFS-type transporter phqF {ECO:0000303|PubMed:23213353};
DE AltName: Full=Paraherquamide biosynthesis cluster protein F {ECO:0000303|PubMed:23213353};
GN Name=phqF {ECO:0000303|PubMed:23213353};
OS Penicillium fellutanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=70095;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 20841 / MF5123;
RX PubMed=23213353; DOI=10.1039/c2md20029e;
RA Li S., Anand K., Tran H., Yu F., Finefield J.M., Sunderhaus J.D.,
RA McAfoos T.J., Tsukamoto S., Williams R.M., Sherman D.H.;
RT "Comparative analysis of the biosynthetic systems for fungal
RT bicyclo[2.2.2]diazaoctane indole alkaloids: the (+)/(-)-notoamide,
RT paraherquamide and malbrancheamide pathways.";
RL Med. Chem. Commun. 3:987-996(2012).
CC -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC biosynthesis of paraherquamide, a dichlorinated fungal indole alkaloid
CC that belongs to a family of natural products containing a
CC characteristic bicyclo[2.2.2]diazaoctane core.
CC {ECO:0000305|PubMed:23213353}.
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; JQ708195; AGA37273.1; -; Genomic_DNA.
DR AlphaFoldDB; L0E4G6; -.
DR SMR; L0E4G6; -.
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; -; 1.
DR InterPro; IPR010573; MFS_Str1/Tri12-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF06609; TRI12; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..411
FT /note="MFS-type transporter phqF"
FT /id="PRO_0000448870"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 411 AA; 45211 MW; D5AA6F6F4C46B154 CRC64;
MHNTQSDTKC ENASDTPESP TGEEESVGLA RWKLGLLMFG NTLAVFCVAL DNTIMSNAIP
RVTQTFDSLE DIGWGSPARR HFDRQRERTT SPKTAVYGCF GGIGGAFAEN STWRWCFYIN
LPLGAVTTVL ILCFFFDSRT GTSDVSMSSW NRFRGLDIPG LLLFLPTVFC LLLALQWGGA
KYPWNNVRVI VLFVIFILAG GCWIFIQHSM KDQASVPPRL IRNRNVWSSA VYMGCIVGSF
IIILYYFPIW FQAVKGGSPI QSGTMILPII IGLIVWLGFG FQLPFIAVQT ALPRSDIPVA
TAIVTFAQNL SEAVLVALAQ TIFQNRLFAH VKQLSTLVDP NALVHAGAAN LDQHFSADVL
PEIVRAYSAA VTETFYAATG IAALSFIGLI RLQWLSVKKT KTNGNAAQTH L
