ID A0A0V1I100_9BILA Unreviewed; 871 AA.
AC A0A0V1I100;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 {ECO:0000256|ARBA:ARBA00017612};
DE EC=3.1.1.96 {ECO:0000256|ARBA:ARBA00013056};
DE AltName: Full=Ribophorin II {ECO:0000256|ARBA:ARBA00032139};
DE AltName: Full=Ribophorin-2 {ECO:0000256|ARBA:ARBA00030078};
GN Name=RPN2 {ECO:0000313|EMBL:KRZ15653.1};
GN ORFNames=T11_267 {ECO:0000313|EMBL:KRZ15653.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ15653.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ15653.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ15653.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96;
CC Evidence={ECO:0000256|ARBA:ARBA00033671};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96;
CC Evidence={ECO:0000256|ARBA:ARBA00000741};
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 SWP1 family.
CC {ECO:0000256|ARBA:ARBA00009038}.
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:KRZ15653.1}.
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DR EMBL; JYDP01000016; KRZ15653.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1I100; -.
DR STRING; 268475.A0A0V1I100; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:InterPro.
DR GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:InterPro.
DR Gene3D; 3.50.80.10; D-tyrosyl-tRNA(Tyr) deacylase; 1.
DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR InterPro; IPR023509; DTD-like_sf.
DR InterPro; IPR008814; Swp1.
DR PANTHER; PTHR12640:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT 2; 1.
DR PANTHER; PTHR12640; RIBOPHORIN II; 1.
DR Pfam; PF05817; Ribophorin_II; 1.
DR Pfam; PF02580; Tyr_Deacylase; 1.
DR SUPFAM; SSF69500; DTD-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:KRZ15653.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 572..591
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 598..619
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 631..649
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..818
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 871 AA; 98201 MW; C8600AA8567C4B9F CRC64;
MMISNFCFKC ILRAVIICCI VNVGNSMILT EVMTESDVAA AHQFFLDSIS KQSSIESLAW
VANGLKTMNK KIPDDKAKLI CESAKEAVKN TSEIQPIYWA AFAVHALENC QLPSFPSNYF
DKYLFDKSNA KTVAHAVSSI GYLKVKCMNY VLAYDMEKMR SVVSALVKTS TSPNDRSMLL
NTAPFLSGDL KFLTDCVNDL VSQVDESDER YLRFDGGIGT TASIVHGIYQ LSVKTGNPVA
LKKEQILKFA NYLISRRRIY HPRVTSLIFS ALHDMTDDKV ANLPKNSVPL AILLEHNGSL
DQVKSSIQFM VTDIFGHIVP TDRVIADKIV HISSKEVVMN SKPFSRISAK GNDVYELKFV
DQKRKAGFYE CFVSVGATNS KYMPIVQEGI VIKVSREIFI SGLNLAIHES ERFPLDDKTE
SMKINEKKLM QLSADDHQKL AVIFVIKDKL TKESILVDQA YLQFEKQNTK TIITVPVAND
NANVYKADID FKQMAKDYEF TSGMYEISLI VGDDVIMNSV ILKFALLNLQ LPAVVEHARK
SVLEATDYKM KPEIVHSFRP PEKRPPKFIS DIFSVAVVIP FFILLCIWFY LGANIWGIPF
SPVVIVFHAG LGGIFWLYYQ FWIHLNMFET LKYLGILGTI TFLSGISVLR KRADRIKKSG
LKRVRKIASE RRFFFVIGCS SYSVNTLNES CFAKVNGEVV SSIQRGICAL IGLSRDDDAN
DIEYIVRKLL NLRIFSGDAE KRWDKSVNDL QLEILCVSQF TLNALLKGNK LDFHLSMNPS
EAAQFYCTFV DKLRQNYRED LVKGFVSCGI LILLFLIYTD YGKFGAHMQL SIENDGPVCS
QFTEDKSKSS CPLLLKSVCH LSVIQGKRNI H
//
