L-seryl-tRNA(Sec) selenium transferase catalyzes the formation of selenocysteinyl-tRNA(Sec) from seryl-tRNA(Sec) and L-selenophosphate in selenoprotein biosynthesis
L-seryl-tRNA(Sec) selenium transferase; In bacteria, the incorporation of selenocysteine as ...
9-462
0e+00
L-seryl-tRNA(Sec) selenium transferase; In bacteria, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelA. This model excludes homologs that appear to differ in function from Frankia alni, Helicobacter pylori, Methanococcus jannaschii and other archaea, and so on. [Protein synthesis, tRNA aminoacylation]
:
Pssm-ID: 273099 [Multi-domain] Cd Length: 454 Bit Score: 631.14 E-value: 0e+00
L-seryl-tRNA(Sec) selenium transferase; In bacteria, the incorporation of selenocysteine as ...
9-462
0e+00
L-seryl-tRNA(Sec) selenium transferase; In bacteria, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelA. This model excludes homologs that appear to differ in function from Frankia alni, Helicobacter pylori, Methanococcus jannaschii and other archaea, and so on. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273099 [Multi-domain] Cd Length: 454 Bit Score: 631.14 E-value: 0e+00
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
166-308
4.73e-03
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: 37.75 E-value: 4.73e-03
L-seryl-tRNA(Sec) selenium transferase; In bacteria, the incorporation of selenocysteine as ...
9-462
0e+00
L-seryl-tRNA(Sec) selenium transferase; In bacteria, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelA. This model excludes homologs that appear to differ in function from Frankia alni, Helicobacter pylori, Methanococcus jannaschii and other archaea, and so on. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273099 [Multi-domain] Cd Length: 454 Bit Score: 631.14 E-value: 0e+00
Selenocysteine synthase N terminal; This domain family is found in bacteria, and is ...
9-48
3.16e-07
Selenocysteine synthase N terminal; This domain family is found in bacteria, and is approximately 40 amino acids in length. The family is found in association with pfam03841. There is a single completely conserved residue P that may be functionally important. This family is the N terminal region of selenocysteine synthase which catalyzes the conversion of seryl-tRNA(Sec) into selenocysteyl-tRNA(Sec).
Pssm-ID: 432519 Cd Length: 40 Bit Score: 46.62 E-value: 3.16e-07
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
166-308
4.73e-03
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: 37.75 E-value: 4.73e-03
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
166-318
5.90e-03
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 38.72 E-value: 5.90e-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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