ID A0A0M9WFK3_9EURO Unreviewed; 339 AA.
AC A0A0M9WFK3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACN38_g6237 {ECO:0000313|EMBL:KOS42902.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS42902.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS42902.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS42902.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-2015) 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}.
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:KOS42902.1}.
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DR EMBL; LHQQ01000094; KOS42902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9WFK3; -.
DR STRING; 229535.A0A0M9WFK3; -.
DR OrthoDB; 4604288at2759; -.
DR Proteomes; UP000037696; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:UP000037696};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..339
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005839768"
FT TRANSMEM 190..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 339 AA; 37520 MW; 7B6D1F1EDF3A5AC6 CRC64;
MPPITCPAPW NVKMKLWTAL FLLFSVVSGV LSASSTPDKF ASYQSLSRSG PVDLDSASYE
DLTSARRDYY AMVILTATDP RFGCILCRDF ESEWDLIARS WTKGTKPDDL KVVFGTLDFD
NGKAVFQKLM LQTAPVLLVF PPTIGPFAKV EGNPLRFDFT GPISADQLYS WIGRHLPEGP
KPQLVRPINY MRIVSAITLL MAVVTAIAVL SPYLLPVIQN RNLWAAISLI AILLFTSGQM
FNHIRKVPYV ATDGKGGISY FAGGFQNQFG METQIVAIIY AVLSFATIAL ALKVPRMEDV
KGQQLAVLVW ATVLFATYSF LLSVFKTKNG GYPFYLPPF
//
