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Database: UniProt
Entry: D2VVI1_NAEGR
LinkDB: D2VVI1_NAEGR
Original site: D2VVI1_NAEGR 
ID   D2VVI1_NAEGR            Unreviewed;       362 AA.
AC   D2VVI1;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=NAEGRDRAFT_81382 {ECO:0000313|EMBL:EFC39116.1};
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:EFC39116.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC39116.1,
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   -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that
CC       catalyzes the initial transfer of a defined glycan
CC       (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC       pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC       consensus motif in nascent polypeptide chains, the first step in
CC       protein N-glycosylation. N-glycosylation occurs cotranslationally and
CC       the complex associates with the Sec61 complex at the channel-forming
CC       translocon complex that mediates protein translocation across the
CC       endoplasmic reticulum (ER). All subunits are required for a maximal
CC       enzyme activity. {ECO:0000256|ARBA:ARBA00002791}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; GG738902; EFC39116.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2VVI1; -.
DR   TCDB; 1.A.76.1.12; the magnesium transporter1 (magt1) family.
DR   EnsemblProtists; EFC39116; EFC39116; NAEGRDRAFT_81382.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_81382; -.
DR   InParanoid; D2VVI1; -.
DR   OrthoDB; 5560488at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR   PANTHER; PTHR12692; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR12692:SF0; GH11935P; 1.
DR   Pfam; PF04756; OST3_OST6; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        173..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        226..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        320..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          259..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   362 AA;  42569 MW;  078C316180DA7B74 CRC64;
     MHQCLHCKLY RDLLKKYVNS FTNEMKGILI EFTPQSQELV IQKLKLTHLP SVTIQSKYTD
     QLYDCNLKEN QLWECVKDAF KQSDHDLYEN LKDFINMDDI KDLYLKYKNE YSSSSSNNQQ
     QHNQQQNNHS NESPLFDFSS LKSITKIVLI AFCIVGFVIG ISTLQNLLNG TRYMIFILCI
     LTYILCMSGT VFNMIQNPPP YQYNPRENSI SFFYPSMRMS FALEGYIATF VIVISSFYFI
     AIPYYGYYDN NNNTNNNTDN ITTITSNTNN TKNTNKKNKN KNGKKKNEEE VEEEEVVEEE
     LNEEKKKEDS HYKSVLKRLF FIWGFFITFT AAMIFFMIKT SFYLSDTPYH GWVQLLLAIF
     NH
//
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