ID R9AMX4_WALI9 Unreviewed; 316 AA.
AC R9AMX4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Magnesium transporter protein 1 {ECO:0000313|EMBL:EOR03582.1};
GN ORFNames=J056_003039 {ECO:0000313|EMBL:EOR03582.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR03582.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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; KE007226; EOR03582.1; -; Genomic_DNA.
DR RefSeq; XP_009266618.1; XM_009268343.1.
DR AlphaFoldDB; R9AMX4; -.
DR STRING; 1299270.R9AMX4; -.
DR GeneID; 20375991; -.
DR KEGG; wic:J056_003039; -.
DR eggNOG; KOG2603; Eukaryota.
DR HOGENOM; CLU_052855_1_2_1; -.
DR OMA; VLFGMYS; -.
DR OrthoDB; 4604288at2759; -.
DR Proteomes; UP000014064; 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:UP000014064};
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 168..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 316 AA; 35818 MW; CC31EFA296B77DD3 CRC64;
MKIPEIISIL IIASIALAKS ALLSKYDSLA QNQAGVVKLD DLSYNELIRT PERDFGVAVV
LTAMDERMKC TPCHKFAPEF HLLAKQAKGR RSTNKNSIVF ASLDFMDGQR TFNDLGLNTA
PSLFYHPPHQ LNGHLYDFNR NGFLAERLVA FLNTHSPTKF AFKRPVDHTS TVIALVLLTI
LAVFAKKNWN TLTKPFIFSK WSWCMLTLII ILTMTSGYMW NQIRKPPQMV MTKNGAQYFA
NGVTNQYRAE TVIIGTIYAL LASTIVILTI SVPKIQNTGR QRAAAYLWTL ILIVTFSVLV
YIFKMKQPIY PFRLFV
//
