PHM3_PYRSX
ID PHM3_PYRSX Reviewed; 485 AA.
AC A0A2Z5XAK5;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 23-FEB-2022, entry version 13.
DE RecName: Full=MFS-type transporter phm3 {ECO:0000303|PubMed:29972614};
DE AltName: Full=Phomasetin biosynthesis cluster protein 3 {ECO:0000303|PubMed:29972614};
GN Name=phm3 {ECO:0000303|PubMed:29972614};
OS Pyrenochaetopsis sp.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pyrenochaetopsidaceae;
OC Pyrenochaetopsis; unclassified Pyrenochaetopsis.
OX NCBI_TaxID=1756125;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=RK10-F058;
RX PubMed=29972614; DOI=10.1002/anie.201805050;
RA Kato N., Nogawa T., Takita R., Kinugasa K., Kanai M., Uchiyama M.,
RA Osada H., Takahashi S.;
RT "Control of the stereochemical course of [4+2] cycloaddition during trans-
RT decalin formation by Fsa2-family enzymes.";
RL Angew. Chem. Int. Ed. 57:9754-9758(2018).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of the trans-fused decalin-containing tetramic acid
CC phomasetin. {ECO:0000269|PubMed:29972614}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; LC361337; BBC43186.1; -; Genomic_DNA.
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; 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; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..485
FT /note="MFS-type transporter phm3"
FT /id="PRO_0000453356"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 52729 MW; 72B7FD4D8192AC80 CRC64;
MSLQDPTKEH NNTSPSPKDE KTDYVVDWDG AEDAANPRNW TTRTKTAHVL CVSGFTLYSN
LAAVMFAPGA PLLVADFHIT STIVASLTVS IYILGFVFGP FLLASLSELY GRLWLYHICN
LIYLAFTVGC ALSTNTAMFL AFRFICGCAA SGPMTIGGGT IADLYEAEER GKAMALFGLG
PLLGPVIGPV VGGFVTEHLN WRWTFYLVLI LAAIIAIAGA VIMRETFEPV LLERKAADER
VRTGNRQLRA RTSDGTRTAN QLLLRAIIRP LKMLCVSPIV LSLSVYCAFL FGLTYLLFTT
FPAVFGLTYQ FSTEQEGLAF LGLGVGMIFG IALFAILSDK LLHQPRGGTL ARPELRLVLM
VWSSPLVPIG FFWYGWSAQS TTHWIVPIIG TAVIGIGAFL ILMPAQLYLV DAFGTEGAAS
ALAVNTGLRS LFGAVLPLAG PPLYSKLDLG WGNSVLAFIG LAFVPVPFVL YKYGETLRKR
FPIDR
