ID A0A1Z5T6G2_HORWE Unreviewed; 544 AA.
AC A0A1Z5T6G2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Quinate transporter {ECO:0000256|ARBA:ARBA00043213};
GN ORFNames=BTJ68_07271 {ECO:0000313|EMBL:OTA31615.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA31615.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA31615.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA31615.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OTA31615.1}.
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DR EMBL; MUNK01000111; OTA31615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5T6G2; -.
DR STRING; 1157616.A0A1Z5T6G2; -.
DR VEuPathDB; FungiDB:BTJ68_07271; -.
DR InParanoid; A0A1Z5T6G2; -.
DR OrthoDB; 1354898at2759; -.
DR Proteomes; UP000194280; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0019630; P:quinate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
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:SF34; 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 Quinate metabolism {ECO:0000256|ARBA:ARBA00022911};
KW Reference proteome {ECO:0000313|Proteomes:UP000194280};
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 21..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..484
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
SQ SEQUENCE 544 AA; 61175 MW; 76C73652A1FC7CA3 CRC64;
MGLLTLVEDR PTPKAVYNWR VYACACVASF ASCMIGYDSA FFGTTIALES FEEEFGFNEM
SESHLNFIKA NIVSIYQAGA FFGALFAYAS AYWLGRKSSL ILWSLLFLVG AGMMLGANGD
RGLDLIYAGR VIAGIGVGAT SNVVPIYISE LSPPAVRGRL VGIYELGWQL GGLVGFWINY
GLTEHMEPSH QQWIIPFAVQ LIPGGMLFIG AFWLRESPRW LISKNRRDQA IKNLCWIRNL
REDEIYIVEE VAFIDAAIEE QNAAIGVGFW KPFKAVGQNK KVQWRFVLGC MLFLFQNGSG
INAIPQTSIN YYSPTVFKSI GISGGNTAFL TTGIFGVVKT VLTFVWLFYL IDRLGRRNLL
MIGAGGGSVC MFIIGTWIYQ CKPNRQHRRE LIVVFWWSRR YLLLLPMDGV LHAKLECEMF
DQQVRALGQA SAAASNWFWN FIIARFTPQM FANMGPSGCG VYYFFASMMI LSIIWVYFVM
PETKGIPLES MNRLFEIMPA RKAHRTVHAE DEAREADFRQ DAEGAGLSIS KEKFDHVEKT
TEQA
//
