ID A0A150UVR7_9PEZI Unreviewed; 527 AA.
AC A0A150UVR7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Major facilitator superfamily (MFS) profile domain-containing protein {ECO:0000259|PROSITE:PS50850};
GN ORFNames=M433DRAFT_417097 {ECO:0000313|EMBL:KYG42369.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG42369.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG42369.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG42369.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000256|ARBA:ARBA00010992,
CC ECO:0000256|RuleBase:RU003346}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYG42369.1}.
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DR EMBL; JPDO01000471; KYG42369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150UVR7; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR NCBIfam; TIGR00879; SP; 1.
DR PANTHER; PTHR48022:SF38; MAJOR FACILITATOR SUPERFAMILY (MFS) PROFILE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR48022; PLASTIDIC GLUCOSE TRANSPORTER 4; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU003346}.
FT TRANSMEM 63..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 419..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..472
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
SQ SEQUENCE 527 AA; 58718 MW; D7127CEFB42A6B15 CRC64;
MARYGSQTSR YNRLVTVFVA LGSLTYGYCA SIIGSTIGQP GWYRFFNLPR EGQPGYATTT
THAIATANGL FSAGGAVGAL FIMWSADYFG RKRNIQFGSL LAVVGGAFQG GAAALAMFQV
GRFISGLGIG ILVTVCPMYL SEMASPFVRG WLVGHHAIFL VFGYMLSSWL GYACYWATPV
NESFAWRFPL CMQCLSPTLL LFGSPWVPRS PRWLISKGRV EEARVVLRRL RESPDDPDDL
IAREEFYQIS EQLKMDEQKL KSTGYSNIWV AVWKKKSYRW RMIMGFLIQW GAEFGGPLII
NNYAVILYTN LGQTGGMPLL LSAIWLTTAG LIYNPGGAWL HDKVNSRRKM FITGLAGCLV
TTSCLAAMIA KYAGTTNQVG NAFGIFFIFL YLAFQGTGCD TTMYLWVSEI FPTEIRSIGM
GFSLFGQFAA TIILLQTAPI GFAQVGWKYF LIVICWCAVF IPIVYFYFPE TARLTLEEIA
QKFGDDVAVH ITDATQEEQE RLERAIRNKG DDAPIELEET PDIEKMV
//
