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stem-specific protein TSJT1 [Oryza sativa Japonica Group]
Wali7 domain-containing protein( domain architecture ID 10575738)
Wali7 domain-containing protein
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
DUF3700 | pfam12481 | Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
2-226 | 1.77e-134 | ||||
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains. : Pssm-ID: 403619 [Multi-domain] Cd Length: 228 Bit Score: 377.48 E-value: 1.77e-134
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Name | Accession | Description | Interval | E-value | ||||
DUF3700 | pfam12481 | Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
2-226 | 1.77e-134 | ||||
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains. Pssm-ID: 403619 [Multi-domain] Cd Length: 228 Bit Score: 377.48 E-value: 1.77e-134
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Wali7 | cd01910 | This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
2-226 | 1.29e-132 | ||||
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced by aluminum. Wali7 has a single domain similar to the glutamine amidotransferase domain of glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The Wali7 domain is also somewhat similar to the Ntn hydrolase fold of the proteasomal alph and beta subunits. Pssm-ID: 238891 [Multi-domain] Cd Length: 224 Bit Score: 372.41 E-value: 1.29e-132
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asnB | PRK09431 | asparagine synthetase B; Provisional |
124-219 | 3.88e-15 | ||||
asparagine synthetase B; Provisional Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 73.79 E-value: 3.88e-15
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asn_synth_AEB | TIGR01536 | asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
123-197 | 6.84e-07 | ||||
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family] Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 49.25 E-value: 6.84e-07
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AsnB | COG0367 | Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
124-187 | 2.44e-05 | ||||
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 44.83 E-value: 2.44e-05
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Name | Accession | Description | Interval | E-value | ||||
DUF3700 | pfam12481 | Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
2-226 | 1.77e-134 | ||||
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains. Pssm-ID: 403619 [Multi-domain] Cd Length: 228 Bit Score: 377.48 E-value: 1.77e-134
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Wali7 | cd01910 | This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
2-226 | 1.29e-132 | ||||
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced by aluminum. Wali7 has a single domain similar to the glutamine amidotransferase domain of glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The Wali7 domain is also somewhat similar to the Ntn hydrolase fold of the proteasomal alph and beta subunits. Pssm-ID: 238891 [Multi-domain] Cd Length: 224 Bit Score: 372.41 E-value: 1.29e-132
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Gn_AT_II | cd00352 | Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
53-192 | 9.73e-19 | ||||
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer. Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 81.34 E-value: 9.73e-19
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asnB | PRK09431 | asparagine synthetase B; Provisional |
124-219 | 3.88e-15 | ||||
asparagine synthetase B; Provisional Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 73.79 E-value: 3.88e-15
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PLN02549 | PLN02549 | asparagine synthase (glutamine-hydrolyzing) |
124-206 | 9.95e-14 | ||||
asparagine synthase (glutamine-hydrolyzing) Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 69.79 E-value: 9.95e-14
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PTZ00077 | PTZ00077 | asparagine synthetase-like protein; Provisional |
110-205 | 2.00e-12 | ||||
asparagine synthetase-like protein; Provisional Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 65.89 E-value: 2.00e-12
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GATase_7 | pfam13537 | Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
124-169 | 3.46e-08 | ||||
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase. Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 50.59 E-value: 3.46e-08
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AsnB | cd00712 | Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
124-188 | 1.45e-07 | ||||
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia. Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 50.25 E-value: 1.45e-07
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asn_synth_AEB | TIGR01536 | asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
123-197 | 6.84e-07 | ||||
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family] Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 49.25 E-value: 6.84e-07
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AsnB | COG0367 | Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
124-187 | 2.44e-05 | ||||
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 44.83 E-value: 2.44e-05
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GATase_6 | pfam13522 | Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
80-169 | 9.13e-05 | ||||
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase. Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 41.14 E-value: 9.13e-05
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Blast search parameters | ||||
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