O-phosphoseryl-tRNA(Sec) selenium transferase isoform X1 [Rattus norvegicus]
Protein Classification
O-phosphoseryl-tRNA(Sec) selenium transferase( domain architecture ID 10022574)
O-phosphoseryl-tRNA(Sec) selenium transferase converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| selenium_SpcS | TIGR03531 | O-phosphoseryl-tRNA(Sec) selenium transferase; In the archaea and eukaryotes, the conversion ... |
13-403 | 0e+00 | ||||||
O-phosphoseryl-tRNA(Sec) selenium transferase; In the archaea and eukaryotes, the conversion of the mischarged serine to selenocysteine (Sec) on its tRNA is accomplished in two steps. This enzyme, O-phosphoseryl-tRNA(Sec) selenium transferase, acts second, after a phosphophorylation step catalyzed by a homolog of the bacterial SelA protein. [Protein synthesis, tRNA aminoacylation] : Pssm-ID: 211833 Cd Length: 444 Bit Score: 722.99 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| selenium_SpcS | TIGR03531 | O-phosphoseryl-tRNA(Sec) selenium transferase; In the archaea and eukaryotes, the conversion ... |
13-403 | 0e+00 | ||||||
O-phosphoseryl-tRNA(Sec) selenium transferase; In the archaea and eukaryotes, the conversion of the mischarged serine to selenocysteine (Sec) on its tRNA is accomplished in two steps. This enzyme, O-phosphoseryl-tRNA(Sec) selenium transferase, acts second, after a phosphophorylation step catalyzed by a homolog of the bacterial SelA protein. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 211833 Cd Length: 444 Bit Score: 722.99 E-value: 0e+00
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| SepSecS | pfam05889 | O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, ... |
61-403 | 0e+00 | ||||||
O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, SepSecS, of several eukaryotic and archaeal proteins, was involved in antigen-antibodies responses in the liver and pancreas. Structural studies show that the family is O-phosphoseryl-tRNA(Sec) selenium transferase, an enzyme involved in the synthesis of the amino acid selenocysteine (Sec). Sec is the only amino acid whose biosynthesis occurs on its cognate transfer RNA (tRNA). SepSecS catalyzes the final step in the formation of the amino acid. The early observation that autoantibodies isolated from patients with type I autoimmune hepatitis targeted a ribonucleoprotein complex containing tRNASec led to the identification and characterization of the archaeal and the human SepSecS. SepSecS forms its own branch in the family of fold-type I pyridoxal phosphate (PLP) enzymes that goes back to the last universal common ancestor which explains why the archaeal sequences Swiss:Q8TXK0 and Swiss:Q8TYR3 are annotated as being pyridoxal phosphate-dependent enzymes. Pssm-ID: 399111 Cd Length: 389 Bit Score: 552.20 E-value: 0e+00
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| AAT_I | cd01494 | Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
180-295 | 2.51e-05 | ||||||
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V). Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 44.30 E-value: 2.51e-05
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| Name | Accession | Description | Interval | E-value | ||||||
| selenium_SpcS | TIGR03531 | O-phosphoseryl-tRNA(Sec) selenium transferase; In the archaea and eukaryotes, the conversion ... |
13-403 | 0e+00 | ||||||
O-phosphoseryl-tRNA(Sec) selenium transferase; In the archaea and eukaryotes, the conversion of the mischarged serine to selenocysteine (Sec) on its tRNA is accomplished in two steps. This enzyme, O-phosphoseryl-tRNA(Sec) selenium transferase, acts second, after a phosphophorylation step catalyzed by a homolog of the bacterial SelA protein. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 211833 Cd Length: 444 Bit Score: 722.99 E-value: 0e+00
|
||||||||||
| SepSecS | pfam05889 | O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, ... |
61-403 | 0e+00 | ||||||
O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, SepSecS, of several eukaryotic and archaeal proteins, was involved in antigen-antibodies responses in the liver and pancreas. Structural studies show that the family is O-phosphoseryl-tRNA(Sec) selenium transferase, an enzyme involved in the synthesis of the amino acid selenocysteine (Sec). Sec is the only amino acid whose biosynthesis occurs on its cognate transfer RNA (tRNA). SepSecS catalyzes the final step in the formation of the amino acid. The early observation that autoantibodies isolated from patients with type I autoimmune hepatitis targeted a ribonucleoprotein complex containing tRNASec led to the identification and characterization of the archaeal and the human SepSecS. SepSecS forms its own branch in the family of fold-type I pyridoxal phosphate (PLP) enzymes that goes back to the last universal common ancestor which explains why the archaeal sequences Swiss:Q8TXK0 and Swiss:Q8TYR3 are annotated as being pyridoxal phosphate-dependent enzymes. Pssm-ID: 399111 Cd Length: 389 Bit Score: 552.20 E-value: 0e+00
|
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| AAT_I | cd01494 | Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
180-295 | 2.51e-05 | ||||||
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V). Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 44.30 E-value: 2.51e-05
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| AAT_like | cd00609 | Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
174-355 | 3.77e-05 | ||||||
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein. Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 45.41 E-value: 3.77e-05
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