ID D2VY17_NAEGR Unreviewed; 561 AA.
AC D2VY17;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC38246.1};
GN ORFNames=NAEGRDRAFT_73938 {ECO:0000313|EMBL:EFC38246.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC38246.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC38246.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=riboflavin(in) = riboflavin(out); Xref=Rhea:RHEA:35015,
CC ChEBI:CHEBI:57986; Evidence={ECO:0000256|ARBA:ARBA00000215};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC {ECO:0000256|ARBA:ARBA00006366}.
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DR EMBL; GG738909; EFC38246.1; -; Genomic_DNA.
DR RefSeq; XP_002670990.1; XM_002670944.1.
DR AlphaFoldDB; D2VY17; -.
DR STRING; 5762.D2VY17; -.
DR TCDB; 2.A.125.1.5; the eukaryotic riboflavin transporter (e-rft) family.
DR EnsemblProtists; EFC38246; EFC38246; NAEGRDRAFT_73938.
DR GeneID; 8857800; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_73938; -.
DR eggNOG; KOG4255; Eukaryota.
DR InParanoid; D2VY17; -.
DR OrthoDB; 5477759at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR009357; Riboflavin_transptr.
DR PANTHER; PTHR12929:SF10; RIBOFLAVIN TRANSPORTER; 1.
DR PANTHER; PTHR12929; SOLUTE CARRIER FAMILY 52; 1.
DR Pfam; PF06237; SLC52_ribofla_tr; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 93..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 423..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 561 AA; 63286 MW; AF15FA970C400BF9 CRC64;
MTETSGRVVA SADLKEVVDD QVQQHADVVD NHHQQQYQAS AEKAIANGQS DVVVNDAQVL
DKMGEITKNE MNQTERFYLR KIVAKTCSDP PNLIIYSLII LFGLSSWIAV NGIYSEIPLL
GYVMPEGYAI AVDMNLSLQL ANIVPFMYFV FMIFKKMIQR KLKPTTTRKS TFDIVDTVSI
LSLFVIGIGA LIGMSFLWNI PINGRSWPFL IMMFLVGVSD CTSTLLFYPF VLHFKHAYSS
ALLIGESLTG LIASIISIIQ NSTPTPLFPF WVFCIIIAGI TAISLVSYCL LRFLPYSKKE
LRRDVDALDE ETRELIVKKR PLMTWSTVRL IFFQFLISCS ENGVVVSIMP YVFAHYKHHA
TLLQYAITIG MIISPIASGV AYLVPFYNFF IAMFCHLIWI VGACFLTVIA FNNPNPPLKY
STAFGGFLVV VAILTKGFMS FCKTKEFLHS HQVIEKQDEM IYKKLLLESR KKTEQTQHVE
EKLEQIEPIS TEQQEATIVP NGEEIIDLPI NQKKLTFGER LRDALTQMDL NPFRCAGFGI
QIGALVATVT VKLFSDAHYF S
//
