ID A0A168IYL2_CORDF Unreviewed; 878 AA.
AC A0A168IYL2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE SubName: Full=Oligopeptide transporter {ECO:0000313|EMBL:OAA79811.1};
GN ORFNames=LEL_03297 {ECO:0000313|EMBL:OAA79811.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA79811.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA79811.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA79811.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(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:OAA79811.1}.
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DR EMBL; AZHF01000002; OAA79811.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168IYL2; -.
DR OrthoDB; 2782392at2759; -.
DR Proteomes; UP000076881; 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; TIGR00727; ISP4_OPT; 1.
DR NCBIfam; TIGR00728; OPT_sfam; 1.
DR PANTHER; PTHR22601; ISP4 LIKE PROTEIN; 1.
DR PANTHER; PTHR22601:SF9; OLIGOPEPTIDE TRANSPORTER 2; 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:UP000076881};
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 146..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 708..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 750..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 784..802
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 814..837
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 98875 MW; 082C977787FF061E CRC64;
MAKAASVHEA VEPAASPDAE KHGIYTTTSA DNVPYADQIP HEMMETLAPN GEADFIRAKI
NAMSEDEALA IIQESLEFHS DDWNFPADMR ERMRRCLDGP KVYGEWYERD LRVDAVMMKY
SSPYPGVRAV ASPLDDEKVP VETIRAYFLG IGWAIIGTFM ATFFNSRFPG IGLGSAVIQI
LLFPCAKVLE AILPDWGFTA FGTRHSLNPG PWTFKEQMFS TITYNIAIYS TNAYTMILVQ
RSPVFYGLDF VDFGYQLLLT LFIQLMGMGF AGYLRRFSVY PVKALWPTLL PIIAMNRALT
KPEPRENING WTISRYRFFF VCAVGMFLYY WIPGYLFQAL STFNWMTWIA PENLTLAILT
GSRLGLGLFN PITTFDWNVA TSSYAALSQP FFATCTMYIS AIFGGLVILG IYYTNMYNTA
YLPINSAAAF ANDGTIFDVK KVVVDNKLDN AKLQAYSLPF YSAGYVLTVG ANFAFYPVYF
FYIMVNQWKT MSKAYVDFYR GLRHGKGNYE DAMDVHNREM RKYKEVPDWW FLAILVITIA
LSIVWIEIYP LGIPVWLIFL LIAINLVFAV PLSFLSATTG TNLGLGALIQ IITGYLLPNN
PNAFLFSQAL GSWALAGYGD NYVQDQKMAH YCKIAPRAVF RSQIGTIIIT CFVAVGTQNF
ILTSVPGLCT EKQPSQFTCM GDGHPMYASS LMWGLLGSER MFGSLYPLFK WCFLMGFGIA
MIFLVAQGLG PKYLPPVRES LRRKLRPNTY AMLDRTLFPF VASLLWLNPV LIIQGIQHWA
PSNLSYKTPG FILSYIFMYW LPRHRLAWWA KYNYVLSAAL TAGLAVSALI MFFAIGYHPH
ALKWWGNTVS GAGVDGSNKG IYPIPSRGYF GPERGTFP
//
