ID A0A165NP71_9APHY Unreviewed; 794 AA.
AC A0A165NP71;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE SubName: Full=Peptide transporter MTD1 {ECO:0000313|EMBL:KZT67204.1};
GN ORFNames=DAEQUDRAFT_673820 {ECO:0000313|EMBL:KZT67204.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT67204.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT67204.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT67204.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(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}.
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DR EMBL; KV429079; KZT67204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165NP71; -.
DR OrthoDB; 1327484at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035673; F:oligopeptide transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR004648; Oligpept_transpt.
DR InterPro; IPR004813; OPT.
DR NCBIfam; TIGR00728; OPT_sfam; 1.
DR PANTHER; PTHR22601; ISP4 LIKE PROTEIN; 1.
DR PANTHER; PTHR22601:SF25; OLIGOPEPTIDE TRANSPORTER; 1.
DR Pfam; PF03169; OPT; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Peptide transport {ECO:0000256|ARBA:ARBA00022856};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
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 116..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 485..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 511..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 595..612
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 662..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 712..728
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 42..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 88381 MW; 148208A047CA8224 CRC64;
MRVELDGNPP IYSLDTVEVI GGDGPHHRHA YPTPDTPAVE RFQDGSVPTV YPPDSDHSSD
LEKSNGNWKE HPNADVEEVL YDDNADGREK VLETAEDFAQ RLISLDDDPT MPIHTFRMWF
TGLGLAVFAS VLGMLFQFRP QVLTVSPLFL QLIAYMIGRV FEFTIPGPGS KYHTGSAFWN
WLNPGPFNLK EHVAVQIMSN TASVAATACF VFASDDLFYN ITINPGNAIF TLLASQLIGY
GFAGMFRSFL VYPTVMLYPQ NLIYVNLFDV LHRSKGEMLQ GKRLRFFWYV TAAVFVYEWF
PEYIAPLLGS FNIVCLAARN SDWVSYIFGG AEANEGMGLL GFGVDWANIT SRPFYYPLST
QISNYVGWAI NYALLPAIFA ANVWKSKNFP FISQNLFFEN GTIYNQNLIL NADLSLNKTA
LEIYGQPWQS GSTVIYNLGI NLSIGATIVH IALWHGRDIY DAIKREPIDD VHYKMMGVYK
EVPTWWYAAI TLGAFVTAMV CCYTEKSGLP WWALIVALVF AILILPFYGA MYAISAVQLV
VTNLFQILGA ALVPGSSQAN MYFELYSSQA VLQASSMLSD LKLGQYTKLP PRSTFSVQMA
GTVVGALLNY VIMQQVISNQ REILLSNEGT RVWSGQQVQS YNANAVLWGA LGKEIYGPKG
PYFIVPLGLV IGLALPVIPW LLYKKYRWSW LPLVNTAVLA YNIGDLAGGT NGYINTWMAI
GLTSHFYIRR YRAGWFRKYN YLLGAAVDGG SQIFVFIFSF ALGGAGGSGV LFPFWALNPD
GNADYCKVTG QEAS
//