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Database: UniProt
Entry: A0A319DJM7_9EURO
LinkDB: A0A319DJM7_9EURO
Original site: A0A319DJM7_9EURO 
ID   A0A319DJM7_9EURO        Unreviewed;       326 AA.
AC   A0A319DJM7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Oligosaccharyl transferase subunit {ECO:0000313|EMBL:PYH97735.1};
GN   ORFNames=BO71DRAFT_317890 {ECO:0000313|EMBL:PYH97735.1};
OS   Aspergillus ellipticus CBS 707.79.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH97735.1, ECO:0000313|Proteomes:UP000247810};
RN   [1] {ECO:0000313|EMBL:PYH97735.1, ECO:0000313|Proteomes:UP000247810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH97735.1,
RC   ECO:0000313|Proteomes:UP000247810};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SIMILARITY: Belongs to the OST3/OST6 family.
CC       {ECO:0000256|ARBA:ARBA00009561}.
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DR   EMBL; KZ825820; PYH97735.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319DJM7; -.
DR   STRING; 1448320.A0A319DJM7; -.
DR   Proteomes; UP000247810; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12692; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR12692:SF0; GH11935P; 1.
DR   Pfam; PF04756; OST3_OST6; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247810};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:PYH97735.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..326
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016345640"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        209..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        262..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   326 AA;  36399 MW;  92E4998FE6572397 CRC64;
     MKLLSLFVSI LCIIPIAFCS VPDKDKFERY HSLSRFAPIE LNDSSYEDIT SKPRDYHVAV
     ILTATEARYG CILCREFQPE WELIARSWNK GSKPDELKML FATLDFSNGK GTFQKLMLQT
     APVLLVFPPT VGPFAKVDDT PLRFDFSGPI SADQLYTWIV RHLPEGSKPS LVRPVNYMRL
     VSGVIILMGA VTLFTVLSPY ILPIIRNRNL WAAFSLIAIL LFTSGHMFNH IRKVPYVAGD
     GKGGISYFAG GFSNQFGMET QIIAAIYAVL SFSTIALAMK VPRIADAKAQ QVAVIIWSSV
     LLGMYSFLIN VFKAKNGGYP FFLPPF
//
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