ID A0A0F4YRC3_TALEM Unreviewed; 966 AA.
AC A0A0F4YRC3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Oligopeptide transporter protein {ECO:0000313|EMBL:KKA20630.1};
GN ORFNames=T310_5359 {ECO:0000313|EMBL:KKA20630.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA20630.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA20630.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA20630.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000256|ARBA:ARBA00008066}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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:KKA20630.1}.
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DR EMBL; LASV01000244; KKA20630.1; -; Genomic_DNA.
DR RefSeq; XP_013327242.1; XM_013471788.1.
DR AlphaFoldDB; A0A0F4YRC3; -.
DR STRING; 1408163.A0A0F4YRC3; -.
DR GeneID; 25317704; -.
DR OrthoDB; 774342at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05346; SDR_c5; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013057; AA_transpt_TM.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR42901; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR42901:SF1; ALCOHOL DEHYDROGENASE; 1.
DR Pfam; PF01490; Aa_trans; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 493..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 570..588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 600..618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 739..756
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 776..801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 821..841
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 847..871
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 912..937
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 489..869
FT /note="Amino acid transporter transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01490"
FT REGION 372..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 106048 MW; 7C409806349C3C33 CRC64;
MYPLRAAARS IRHLSRASTS KSFPAFHSAF AYRSALEPSV QHAVLRRAMA SAVAKRLEGK
TIVITGASSG IGYSTAKEFA RSSPKNLKLI VTARRVDRLE QLAKEIKEEV GDGVKVLPVK
LDVSNPEEVK NFVPSLPAEF QDIHVLVNNA GLVKGVAQAP DINPDDINVM ISTNVTGLIN
MTQAILPIFK KRDEGGRGDI INVGSIAGRE AYPGGSIYCA TKAFVRSFTD ALRKELISTR
IRVIEIDPGQ VETEFSIVRY YGDKAKADAV YAGCEPLTPD DIAEVIVFAA SRRENVVIAD
TLIFPSHQGS PTHLHHRYPY KIPHRSNNFV AVQFSPTGSL ISIDTVLLAA NTSDSQAWKV
LSKTFIMLLQ GQQSAMDPEE QPRGDASPPR AVIKPQHRRL HDPDVTFEEY HYYALKTREE
EKAAAASDGP TTTLWKTLFR GRSASQPTQD ESQNSPPPPT GDQTKEATAN RLEISDEEWT
NASRMMRTAT AGACFYLITT DILGPYGVGF AMGTLGWGPG IALYTVFGFM AGYSGYLLWK
AFLGLDSHEF PVRNYGDLVF RIYGPYARHF VNVLQALLLL LILGQVIILE GQGISQVSKF
RLCYSVCCVL FVIVGYFIGQ VRTLRNYGWL ANTAVWINLL VIFITMGVMA HSPPNYEISV
LGSAGGAVDP ATITPDPRTG IYPAIIHYNG NPNPHSLIGS INGLLQGVFA YGGAQLFIEF
MAEMKRPHDF IKAMWGAQFF IYTVYLVYGC YVYYFQGQYA YQISYQGVSL YGFQVVGDML
ACVSGLIAAG LYGNIGIKVF YNNVLMDILK APPLTHRRGK ILWAIIVPLW WSIAYVVAAA
IPDYFGFVSV ISATTVIQFT YSFPPILALG YNIKLYALKT SAGDEFDPTT GTVTRQDTGV
RRWVRGLIKG PWHWNILHVL YAIGALATAG LGLYAAIEGM IVAFEIPQVN AFTCVSPLDL
SAQGSS
//