ID A0A364KT66_9EURO Unreviewed; 498 AA.
AC A0A364KT66;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Major facilitator superfamily (MFS) profile domain-containing protein {ECO:0000259|PROSITE:PS50850};
GN ORFNames=BHQ10_002703 {ECO:0000313|EMBL:RAO66691.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO66691.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO66691.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO66691.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
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 -!- 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:RAO66691.1}.
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DR EMBL; MIKG01000004; RAO66691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364KT66; -.
DR STRING; 1196081.A0A364KT66; -.
DR OrthoDB; 1332396at2759; -.
DR Proteomes; UP000249363; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd17316; MFS_SV2_like; 1.
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 PANTHER; PTHR23508; CARBOXYLIC ACID TRANSPORTER PROTEIN HOMOLOG; 1.
DR PANTHER; PTHR23508:SF10; CARBOXYLIC ACID TRANSPORTER PROTEIN HOMOLOG; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000249363};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 438..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..464
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 55140 MW; 1189A0EBA8563214 CRC64;
MADTKEYTEP SHEVSPSSFP EENMSVGRYL ATRVTSLRPP MRKAPNPFKA LMLLNKQQWL
FFLVAFWGWT WDAFDFFSVS ISLTSLAKYF DRPNSEITWG ITLVLMLRSV GAIIFGILSD
RYGRKWPFVA NNVLFIILEL GTGFCKTYKQ FLACRALFGI AMGGLYGNIA ATALEDCPPE
ARGIISGMLQ QGYAFGYLLV TAFARGLVDT TSHGWRPLFW FGACPPVLFI IFRLCLPETQ
AFQSREQVRK SLAGGVAGNF LSEGKVAVKN HWKLLIYLVL LMAGFNFMSH GSQDLYPTML
SAQFGFSANA VTVTQVIANL GAMTGGTLCG WASQIFGRRF SIIVISIVGG ALLYPYDFVS
NKSVMAAAFF EQFCVQGAWG VIPIHLMELA PGPIRTFAVG TAYQLGNLVS SASSTIESTI
GERFPLPPSK TGVKRYDYGK VICIFMGCVY AYVIIITFFG PEKLGREFDA EHDSDLNEVA
ARRMYEKDTE KGTAQHAE
//
