dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3 is a catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation
Oligosaccharyl transferase STT3 subunit; This family consists of the oligosaccharyl ...
2162-2648
2.48e-169
Oligosaccharyl transferase STT3 subunit; This family consists of the oligosaccharyl transferase STT3 subunit and related proteins. The STT3 subunit is part of the oligosaccharyl transferase (OTase) complex of proteins and is required for its activity. In eukaryotes, OTase transfers a lipid-linked core-oligosaccharide to selected asparagine residues in the ER. In the archaea STT3 occurs alone, rather than in an OTase complex, and is required for N-glycosylation of asparagines.
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Pssm-ID: 396873 Cd Length: 478 Bit Score: 531.19 E-value: 2.48e-169
Oligosaccharyl transferase STT3 subunit; This family consists of the oligosaccharyl ...
2162-2648
2.48e-169
Oligosaccharyl transferase STT3 subunit; This family consists of the oligosaccharyl transferase STT3 subunit and related proteins. The STT3 subunit is part of the oligosaccharyl transferase (OTase) complex of proteins and is required for its activity. In eukaryotes, OTase transfers a lipid-linked core-oligosaccharide to selected asparagine residues in the ER. In the archaea STT3 occurs alone, rather than in an OTase complex, and is required for N-glycosylation of asparagines.
Pssm-ID: 396873 Cd Length: 478 Bit Score: 531.19 E-value: 2.48e-169
oligosaccharyl transferase, archaeosortase A system-associated; Members of this protein family ...
2167-2703
3.21e-35
oligosaccharyl transferase, archaeosortase A system-associated; Members of this protein family occur, one to three members per genome, in the same species of Euryarchaeota as contain the predicted protein-sorting enzyme archaeosortase (TIGR04125) and its cognate protein-sorting signal PGF-CTERM (TIGR04126).
Pssm-ID: 275016 [Multi-domain] Cd Length: 817 Bit Score: 147.07 E-value: 3.21e-35
Solute carrier 5 family, sodium/glucose transporters and related proteins; solute-binding ...
2228-2465
2.78e-05
Solute carrier 5 family, sodium/glucose transporters and related proteins; solute-binding domain; This family represents the solute-binding domain of SLC5 proteins (also called the sodium/glucose cotransporter family or solute sodium symporter family) that co-transport Na+ with sugars, amino acids, inorganic ions or vitamins. Family members include: the human glucose (SGLT1, 2, 4, 5), chiro-inositol (SGLT5), myo-inositol (SMIT), choline (CHT), iodide (NIS), multivitamin (SMVT), and monocarboxylate (SMCT) cotransporters, as well as Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. Vibrio parahaemolyticus Na(+)/galactose cotransporter (vSGLT) has 13 transmembrane helices (TMs): TM-1, an inverted topology repeat: TMs1-5 and TMs6-10, and TMs 11-12 (TMs numbered to conform to the solute carrier 6 family Aquifex aeolicus LeuT). One member of this family, human SGLT3, has been characterized as a glucose sensor and not a transporter. Members of this family are important in human physiology and disease.
Pssm-ID: 271357 [Multi-domain] Cd Length: 454 Bit Score: 49.48 E-value: 2.78e-05
Oligosaccharyl transferase STT3 subunit; This family consists of the oligosaccharyl ...
2162-2648
2.48e-169
Oligosaccharyl transferase STT3 subunit; This family consists of the oligosaccharyl transferase STT3 subunit and related proteins. The STT3 subunit is part of the oligosaccharyl transferase (OTase) complex of proteins and is required for its activity. In eukaryotes, OTase transfers a lipid-linked core-oligosaccharide to selected asparagine residues in the ER. In the archaea STT3 occurs alone, rather than in an OTase complex, and is required for N-glycosylation of asparagines.
Pssm-ID: 396873 Cd Length: 478 Bit Score: 531.19 E-value: 2.48e-169
oligosaccharyl transferase, archaeosortase A system-associated; Members of this protein family ...
2167-2703
3.21e-35
oligosaccharyl transferase, archaeosortase A system-associated; Members of this protein family occur, one to three members per genome, in the same species of Euryarchaeota as contain the predicted protein-sorting enzyme archaeosortase (TIGR04125) and its cognate protein-sorting signal PGF-CTERM (TIGR04126).
Pssm-ID: 275016 [Multi-domain] Cd Length: 817 Bit Score: 147.07 E-value: 3.21e-35
Solute carrier 5 family, sodium/glucose transporters and related proteins; solute-binding ...
2228-2465
2.78e-05
Solute carrier 5 family, sodium/glucose transporters and related proteins; solute-binding domain; This family represents the solute-binding domain of SLC5 proteins (also called the sodium/glucose cotransporter family or solute sodium symporter family) that co-transport Na+ with sugars, amino acids, inorganic ions or vitamins. Family members include: the human glucose (SGLT1, 2, 4, 5), chiro-inositol (SGLT5), myo-inositol (SMIT), choline (CHT), iodide (NIS), multivitamin (SMVT), and monocarboxylate (SMCT) cotransporters, as well as Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. Vibrio parahaemolyticus Na(+)/galactose cotransporter (vSGLT) has 13 transmembrane helices (TMs): TM-1, an inverted topology repeat: TMs1-5 and TMs6-10, and TMs 11-12 (TMs numbered to conform to the solute carrier 6 family Aquifex aeolicus LeuT). One member of this family, human SGLT3, has been characterized as a glucose sensor and not a transporter. Members of this family are important in human physiology and disease.
Pssm-ID: 271357 [Multi-domain] Cd Length: 454 Bit Score: 49.48 E-value: 2.78e-05
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
2266-2406
4.87e-04
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.
Pssm-ID: 396786 [Multi-domain] Cd Length: 245 Bit Score: 44.61 E-value: 4.87e-04
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
2260-2568
4.77e-03
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.
Pssm-ID: 349949 [Multi-domain] Cd Length: 378 Bit Score: 42.03 E-value: 4.77e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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