ID A0A1B7TF63_9ASCO Unreviewed; 827 AA.
AC A0A1B7TF63;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE SubName: Full=OPT superfamily oligopeptide transporter {ECO:0000313|EMBL:OBA27377.1};
GN ORFNames=HANVADRAFT_52398 {ECO:0000313|EMBL:OBA27377.1};
OS Hanseniaspora valbyensis NRRL Y-1626.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=766949 {ECO:0000313|EMBL:OBA27377.1, ECO:0000313|Proteomes:UP000092321};
RN [1] {ECO:0000313|Proteomes:UP000092321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-1626 {ECO:0000313|Proteomes:UP000092321};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the oligopeptide OPT transporter family.
CC {ECO:0000256|ARBA:ARBA00008807}.
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:OBA27377.1}.
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DR EMBL; LXPE01000009; OBA27377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7TF63; -.
DR OrthoDB; 362380at2759; -.
DR Proteomes; UP000092321; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035673; F:oligopeptide transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR004813; OPT.
DR InterPro; IPR045035; YSL-like.
DR NCBIfam; TIGR00728; OPT_sfam; 2.
DR PANTHER; PTHR31645; OLIGOPEPTIDE TRANSPORTER YGL114W-RELATED; 1.
DR PANTHER; PTHR31645:SF0; OLIGOPEPTIDE TRANSPORTER YGL114W-RELATED; 1.
DR Pfam; PF03169; OPT; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000092321};
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|ARBA:ARBA00022448}.
FT TRANSMEM 70..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 404..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 547..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 574..592
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 719..741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 761..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 798..819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 17..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 276..303
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 17..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 91760 MW; 29345DA52D2809F8 CRC64;
MATSNRLLQS PYTNINDKRQ QVHIQSRPPT SFKFSPSPPI SQQQQNKNIE SKKKDNGIKE
FTQKAHLPQV TLRSTIVSLG IGTLVLISNM QFGLQSGWIT MMTLPSSLLA CAIFKSVYPL
LMRAIYGKDK HLTAFSDVEN VYCQSVAVAV GTSALSFGFV GIVPAIEKFL TVEEAGGLDL
SHLNYKQLVL WSSGLAFFGV FFAVPLRKQV VVKEKLPFPS GQSTAVLISV LNGNTPILQE
ISQGEMDQMR LNIENRENNN DVDEDDEEQN VFPPFGEDTN EAIKLLEQEL ESEKDDSKLY
SENINLLLIT FSVSAIYTIF SYFIPQIKSI PVFGSYLSKH YLWNVQPSPA YFGQGIIMGH
KTTAYMLFGA FLGWGFLAYI SYHFKYVKFG TNPNDWENGI SGWVLWPSLT IMLVDSIIGL
VVVTVKSFVK MVMKRHLKKN EDQDICHNFR ASFFGTRSRD ELPNLPLVYR PPNMTSSYGS
SDIELNNEDD LVFTEEEEED EHIVCEANNI SNKHVLKVKE NGHTIIYVSR EHNLDAIDPE
LLVSNTVTAI GVLLSFLLCI ATFIFVFGGN VIPIYSYIIA LLLSMFLSIL AVRALGETDL
NPVSGLGKLS QLIFSIITPK EKPGSILINL VAGAISEAGS QQAGDLMQDL KTGHLVGAAP
KSQFIGMLIG TCYSIFLSSG LYMLYNKVYV IPSEEFRIPT ALVWINSSRL FYGGGLPKGS
VNCCIAVGFI FSIISLAKNL LVEWNRFKRA AWLIDCLPSG VAVGISMIIL PAFTIQRFIG
GMFAFWYYKK EGSSRTRLII VSSGLILGEG VCSVVNMILS SCNAPHL
//
