Glutamyl-prolyl-tRNA synthetase, isoform A [Drosophila melanogaster]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||||
| PLN02907 super family | cl33597 | glutamate-tRNA ligase |
1-715 | 0e+00 | |||||||||||
glutamate-tRNA ligase The actual alignment was detected with superfamily member PLN02907: Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 842.08 E-value: 0e+00
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| proS_fam_I super family | cl36641 | prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1219-1714 | 0e+00 | |||||||||||
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. [Protein synthesis, tRNA aminoacylation] The actual alignment was detected with superfamily member TIGR00408: Pssm-ID: 273062 [Multi-domain] Cd Length: 472 Bit Score: 574.37 E-value: 0e+00
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
748-797 | 8.09e-22 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. : Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 89.99 E-value: 8.09e-22
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
894-943 | 1.13e-20 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. : Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 86.52 E-value: 1.13e-20
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| WHEP-TRS | pfam00458 | WHEP-TRS domain; |
821-870 | 2.17e-20 | |||||||||||
WHEP-TRS domain; : Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 86.01 E-value: 2.17e-20
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
973-1022 | 2.63e-18 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. : Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 79.97 E-value: 2.63e-18
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
1048-1097 | 1.18e-17 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. : Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 78.05 E-value: 1.18e-17
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
1122-1169 | 1.62e-16 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. : Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 74.96 E-value: 1.62e-16
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| Name | Accession | Description | Interval | E-value | |||||||||||
| PLN02907 | PLN02907 | glutamate-tRNA ligase |
1-715 | 0e+00 | |||||||||||
glutamate-tRNA ligase Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 842.08 E-value: 0e+00
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| proS_fam_I | TIGR00408 | prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1219-1714 | 0e+00 | |||||||||||
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273062 [Multi-domain] Cd Length: 472 Bit Score: 574.37 E-value: 0e+00
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| ProRS_core_arch_euk | cd00778 | Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
1224-1486 | 5.97e-164 | |||||||||||
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria. Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 497.50 E-value: 5.97e-164
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| tRNA-synt_1c | pfam00749 | tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
203-508 | 2.59e-153 | |||||||||||
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln). Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 471.42 E-value: 2.59e-153
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| gltX_arch | TIGR00463 | glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
143-690 | 2.91e-145 | |||||||||||
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 459.29 E-value: 2.91e-145
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| GlnRS_core | cd00807 | catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
203-512 | 4.56e-130 | |||||||||||
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 405.10 E-value: 4.56e-130
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| ProS | COG0442 | Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1211-1605 | 2.25e-87 | |||||||||||
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 297.45 E-value: 2.25e-87
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| GlnS | COG0008 | Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
202-619 | 7.98e-63 | |||||||||||
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 222.75 E-value: 7.98e-63
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| ProRS-C_1 | pfam09180 | Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1630-1714 | 1.13e-23 | |||||||||||
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif. Pssm-ID: 462709 Cd Length: 67 Bit Score: 95.66 E-value: 1.13e-23
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
748-797 | 8.09e-22 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 89.99 E-value: 8.09e-22
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| WHEP-TRS | pfam00458 | WHEP-TRS domain; |
748-799 | 5.23e-21 | |||||||||||
WHEP-TRS domain; Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 87.55 E-value: 5.23e-21
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
894-943 | 1.13e-20 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 86.52 E-value: 1.13e-20
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| WHEP-TRS | pfam00458 | WHEP-TRS domain; |
821-870 | 2.17e-20 | |||||||||||
WHEP-TRS domain; Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 86.01 E-value: 2.17e-20
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| WHEP-TRS | pfam00458 | WHEP-TRS domain; |
894-945 | 2.69e-20 | |||||||||||
WHEP-TRS domain; Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 85.62 E-value: 2.69e-20
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
820-869 | 5.03e-20 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 84.98 E-value: 5.03e-20
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| ProRS-C_1 | smart00946 | Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1630-1714 | 7.84e-19 | |||||||||||
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif. Pssm-ID: 198014 Cd Length: 67 Bit Score: 81.85 E-value: 7.84e-19
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
973-1022 | 2.63e-18 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 79.97 E-value: 2.63e-18
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| WHEP-TRS | pfam00458 | WHEP-TRS domain; |
973-1025 | 1.08e-17 | |||||||||||
WHEP-TRS domain; Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 78.31 E-value: 1.08e-17
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
1048-1097 | 1.18e-17 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 78.05 E-value: 1.18e-17
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| WHEP-TRS | pfam00458 | WHEP-TRS domain; |
1050-1100 | 1.50e-17 | |||||||||||
WHEP-TRS domain; Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 77.92 E-value: 1.50e-17
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| WHEP-TRS | smart00991 | A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
821-871 | 1.81e-17 | |||||||||||
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes. Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 77.77 E-value: 1.81e-17
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| WHEP-TRS | smart00991 | A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
750-798 | 4.07e-17 | |||||||||||
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes. Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 76.61 E-value: 4.07e-17
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
1122-1169 | 1.62e-16 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 74.96 E-value: 1.62e-16
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| WHEP-TRS | smart00991 | A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
896-944 | 2.07e-16 | |||||||||||
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes. Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 74.69 E-value: 2.07e-16
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| WHEP-TRS | pfam00458 | WHEP-TRS domain; |
1122-1169 | 3.11e-16 | |||||||||||
WHEP-TRS domain; Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 74.07 E-value: 3.11e-16
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| WHEP-TRS | smart00991 | A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
975-1028 | 4.22e-15 | |||||||||||
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes. Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 70.83 E-value: 4.22e-15
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| WHEP-TRS | smart00991 | A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
1050-1100 | 9.04e-15 | |||||||||||
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes. Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 70.06 E-value: 9.04e-15
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| PRK09194 | PRK09194 | prolyl-tRNA synthetase; Provisional |
1445-1601 | 7.10e-13 | |||||||||||
prolyl-tRNA synthetase; Provisional Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 73.58 E-value: 7.10e-13
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| WHEP-TRS | smart00991 | A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
1124-1168 | 7.60e-13 | |||||||||||
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes. Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 64.67 E-value: 7.60e-13
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| PLN02734 | PLN02734 | glycyl-tRNA synthetase |
889-938 | 8.68e-06 | |||||||||||
glycyl-tRNA synthetase Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 50.51 E-value: 8.68e-06
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| PLN02734 | PLN02734 | glycyl-tRNA synthetase |
821-855 | 2.95e-05 | |||||||||||
glycyl-tRNA synthetase Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 48.97 E-value: 2.95e-05
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| PLN02734 | PLN02734 | glycyl-tRNA synthetase |
746-793 | 5.22e-05 | |||||||||||
glycyl-tRNA synthetase Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 48.20 E-value: 5.22e-05
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| PLN02734 | PLN02734 | glycyl-tRNA synthetase |
1120-1157 | 9.23e-04 | |||||||||||
glycyl-tRNA synthetase Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 43.97 E-value: 9.23e-04
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| Name | Accession | Description | Interval | E-value | |||||||||||
| PLN02907 | PLN02907 | glutamate-tRNA ligase |
1-715 | 0e+00 | |||||||||||
glutamate-tRNA ligase Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 842.08 E-value: 0e+00
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| PLN03233 | PLN03233 | putative glutamate-tRNA ligase; Provisional |
196-722 | 0e+00 | |||||||||||
putative glutamate-tRNA ligase; Provisional Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 576.96 E-value: 0e+00
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| proS_fam_I | TIGR00408 | prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1219-1714 | 0e+00 | |||||||||||
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273062 [Multi-domain] Cd Length: 472 Bit Score: 574.37 E-value: 0e+00
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| PTZ00402 | PTZ00402 | glutamyl-tRNA synthetase; Provisional |
155-789 | 8.86e-180 | |||||||||||
glutamyl-tRNA synthetase; Provisional Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 553.80 E-value: 8.86e-180
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| ProRS_core_arch_euk | cd00778 | Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
1224-1486 | 5.97e-164 | |||||||||||
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria. Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 497.50 E-value: 5.97e-164
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| tRNA-synt_1c | pfam00749 | tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
203-508 | 2.59e-153 | |||||||||||
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln). Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 471.42 E-value: 2.59e-153
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| gltX_arch | TIGR00463 | glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
143-690 | 2.91e-145 | |||||||||||
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 459.29 E-value: 2.91e-145
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| GlnRS_core | cd00807 | catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
203-512 | 4.56e-130 | |||||||||||
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 405.10 E-value: 4.56e-130
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| PRK05347 | PRK05347 | glutaminyl-tRNA synthetase; Provisional |
202-693 | 1.58e-125 | |||||||||||
glutaminyl-tRNA synthetase; Provisional Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 405.26 E-value: 1.58e-125
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| glnS | TIGR00440 | glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
204-695 | 2.30e-101 | |||||||||||
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 336.12 E-value: 2.30e-101
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| gltX | PRK04156 | glutamyl-tRNA synthetase; Provisional |
154-688 | 1.98e-95 | |||||||||||
glutamyl-tRNA synthetase; Provisional Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 320.65 E-value: 1.98e-95
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| PRK14703 | PRK14703 | glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
195-738 | 3.13e-93 | |||||||||||
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 320.90 E-value: 3.13e-93
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| ProRS_anticodon_zinc | cd00862 | ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
1492-1714 | 1.16e-89 | |||||||||||
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs. Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 289.97 E-value: 1.16e-89
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| PTZ00437 | PTZ00437 | glutaminyl-tRNA synthetase; Provisional |
202-688 | 4.85e-89 | |||||||||||
glutaminyl-tRNA synthetase; Provisional Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 302.67 E-value: 4.85e-89
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| ProS | COG0442 | Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1211-1605 | 2.25e-87 | |||||||||||
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 297.45 E-value: 2.25e-87
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| PLN02859 | PLN02859 | glutamine-tRNA ligase |
202-688 | 4.75e-86 | |||||||||||
glutamine-tRNA ligase Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 300.14 E-value: 4.75e-86
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| ProRS_core | cd00772 | Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
1228-1485 | 7.40e-70 | |||||||||||
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 235.73 E-value: 7.40e-70
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| GlnS | COG0008 | Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
202-619 | 7.98e-63 | |||||||||||
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 222.75 E-value: 7.98e-63
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| GluRS_non_core | cd09287 | catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
203-512 | 2.51e-57 | |||||||||||
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 198.73 E-value: 2.51e-57
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| tRNA-synt_1c_C | pfam03950 | tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
510-688 | 6.68e-35 | |||||||||||
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln). Pssm-ID: 427609 [Multi-domain] Cd Length: 175 Bit Score: 132.01 E-value: 6.68e-35
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| GST_C_GluProRS_N | cd10309 | Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ... |
76-153 | 5.02e-34 | |||||||||||
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional Glutamyl-Prolyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, bifunctional GluRS-Prolyl-tRNA synthetase (GluProRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluProRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluProRS may be involved in protein-protein interactions, mediating the formation of the multi-aaRS complex in higher eukaryotes. The multi-aaRS complex acts as a molecular hub for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain. Pssm-ID: 198342 [Multi-domain] Cd Length: 81 Bit Score: 125.89 E-value: 5.02e-34
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| GlxRS_core | cd00418 | catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
203-513 | 3.18e-32 | |||||||||||
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains. Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 126.05 E-value: 3.18e-32
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| Gly_His_Pro_Ser_Thr_tRS_core | cd00670 | Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
1256-1484 | 1.14e-30 | |||||||||||
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 121.73 E-value: 1.14e-30
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| ProRS-C_1 | pfam09180 | Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1630-1714 | 1.13e-23 | |||||||||||
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif. Pssm-ID: 462709 Cd Length: 67 Bit Score: 95.66 E-value: 1.13e-23
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
748-797 | 8.09e-22 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 89.99 E-value: 8.09e-22
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| WHEP-TRS | pfam00458 | WHEP-TRS domain; |
748-799 | 5.23e-21 | |||||||||||
WHEP-TRS domain; Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 87.55 E-value: 5.23e-21
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
894-943 | 1.13e-20 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 86.52 E-value: 1.13e-20
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| WHEP-TRS | pfam00458 | WHEP-TRS domain; |
821-870 | 2.17e-20 | |||||||||||
WHEP-TRS domain; Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 86.01 E-value: 2.17e-20
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| WHEP-TRS | pfam00458 | WHEP-TRS domain; |
894-945 | 2.69e-20 | |||||||||||
WHEP-TRS domain; Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 85.62 E-value: 2.69e-20
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
820-869 | 5.03e-20 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 84.98 E-value: 5.03e-20
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| HGTP_anticodon | pfam03129 | Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
1503-1604 | 5.59e-20 | |||||||||||
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain. Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 86.10 E-value: 5.59e-20
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| ProRS-C_1 | smart00946 | Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
1630-1714 | 7.84e-19 | |||||||||||
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif. Pssm-ID: 198014 Cd Length: 67 Bit Score: 81.85 E-value: 7.84e-19
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
973-1022 | 2.63e-18 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 79.97 E-value: 2.63e-18
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| WHEP-TRS | pfam00458 | WHEP-TRS domain; |
973-1025 | 1.08e-17 | |||||||||||
WHEP-TRS domain; Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 78.31 E-value: 1.08e-17
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
1048-1097 | 1.18e-17 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 78.05 E-value: 1.18e-17
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| WHEP-TRS | pfam00458 | WHEP-TRS domain; |
1050-1100 | 1.50e-17 | |||||||||||
WHEP-TRS domain; Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 77.92 E-value: 1.50e-17
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| WHEP-TRS | smart00991 | A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
821-871 | 1.81e-17 | |||||||||||
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes. Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 77.77 E-value: 1.81e-17
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| WHEP-TRS | smart00991 | A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
750-798 | 4.07e-17 | |||||||||||
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes. Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 76.61 E-value: 4.07e-17
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| WEPRS_RNA | cd00936 | WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
1122-1169 | 1.62e-16 | |||||||||||
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 74.96 E-value: 1.62e-16
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| WHEP-TRS | smart00991 | A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
896-944 | 2.07e-16 | |||||||||||
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes. Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 74.69 E-value: 2.07e-16
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| WHEP-TRS | pfam00458 | WHEP-TRS domain; |
1122-1169 | 3.11e-16 | |||||||||||
WHEP-TRS domain; Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 74.07 E-value: 3.11e-16
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| class_II_aaRS-like_core | cd00768 | Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
1273-1475 | 1.42e-15 | |||||||||||
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ. Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 77.54 E-value: 1.42e-15
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| WHEP-TRS | smart00991 | A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
975-1028 | 4.22e-15 | |||||||||||
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes. Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 70.83 E-value: 4.22e-15
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| WHEP-TRS | smart00991 | A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
1050-1100 | 9.04e-15 | |||||||||||
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes. Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 70.06 E-value: 9.04e-15
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| WHEPGMRS_RNA | cd01200 | EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
751-790 | 2.16e-14 | |||||||||||
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 68.72 E-value: 2.16e-14
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| tRNA-synt_2b | pfam00587 | tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
1310-1487 | 8.52e-14 | |||||||||||
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members. Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 71.29 E-value: 8.52e-14
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| WHEPGMRS_RNA | cd01200 | EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
895-936 | 9.06e-14 | |||||||||||
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 66.79 E-value: 9.06e-14
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| WHEPGMRS_RNA | cd01200 | EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
821-862 | 1.57e-13 | |||||||||||
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 66.02 E-value: 1.57e-13
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| PRK09194 | PRK09194 | prolyl-tRNA synthetase; Provisional |
1445-1601 | 7.10e-13 | |||||||||||
prolyl-tRNA synthetase; Provisional Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 73.58 E-value: 7.10e-13
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| WHEP-TRS | smart00991 | A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
1124-1168 | 7.60e-13 | |||||||||||
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes. Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 64.67 E-value: 7.60e-13
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| WHEPGMRS_RNA | cd01200 | EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
1049-1090 | 1.25e-12 | |||||||||||
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 63.71 E-value: 1.25e-12
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| WHEPGMRS_RNA | cd01200 | EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
1124-1164 | 1.87e-12 | |||||||||||
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 62.94 E-value: 1.87e-12
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| HGTP_anticodon | cd00738 | HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
1518-1602 | 7.55e-12 | |||||||||||
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b). Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 63.19 E-value: 7.55e-12
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| WHEPGMRS_RNA | cd01200 | EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
974-1015 | 3.40e-11 | |||||||||||
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 59.48 E-value: 3.40e-11
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| PLN02627 | PLN02627 | glutamyl-tRNA synthetase |
202-405 | 7.92e-11 | |||||||||||
glutamyl-tRNA synthetase Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 66.69 E-value: 7.92e-11
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| PLN02837 | PLN02837 | threonine-tRNA ligase |
1283-1607 | 4.93e-10 | |||||||||||
threonine-tRNA ligase Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 64.53 E-value: 4.93e-10
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| MetRS_RNA | cd00939 | MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
1051-1092 | 2.02e-09 | |||||||||||
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 54.40 E-value: 2.02e-09
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| GST_C_AIMP3 | cd10305 | Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
74-164 | 2.51e-09 | |||||||||||
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 3; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 3 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP3, also called p18 or eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1), contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It specifically interacts with methionyl-tRNA synthetase (MetRS) and is translocated to the nucleus during DNA synthesis or in response to DNA damage and oncogenic stress. In the nucleus, it interacts with ATM and ATR, which are upstream kinase regulators of p53. It appears to work against DNA damage in cooperation with AIMP2, and similar to AIMP2, AIMP3 is also a haploinsufficient tumor suppressor. AIMP3 transgenic mice have shorter lifespans than wild-type mice and they show characteristics of progeria, suggesting that AIMP3 may also be involved in cellular and organismal aging. Pssm-ID: 198338 [Multi-domain] Cd Length: 101 Bit Score: 56.14 E-value: 2.51e-09
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| GST_C_AaRS_like | cd10289 | Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ... |
78-153 | 2.82e-09 | |||||||||||
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA synthetases and similar domains; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl-tRNA synthetase (AaRS)-like subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of some eukaryotic AaRSs, as well as similar domains found in proteins involved in protein synthesis including Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2 (AIMP2), AIMP3, and eukaryotic translation Elongation Factor 1 beta (eEF1b). AaRSs comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. AaRSs in this subfamily include GluRS from lower eukaryotes, as well as GluProRS, MetRS, and CysRS from higher eukaryotes. AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex found in higher eukaryotes. The GST_C-like domain is involved in protein-protein interactions, mediating the formation of aaRS complexes such as the MetRS-Arc1p-GluRS ternary complex in lower eukaryotes and the multi-aaRS complex in higher eukaryotes, that act as molecular hubs for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain. Pssm-ID: 198322 [Multi-domain] Cd Length: 82 Bit Score: 55.40 E-value: 2.82e-09
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| MetRS_RNA | cd00939 | MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
1122-1166 | 1.25e-08 | |||||||||||
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 52.47 E-value: 1.25e-08
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| MetRS_RNA | cd00939 | MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
973-1016 | 4.82e-08 | |||||||||||
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 50.55 E-value: 4.82e-08
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| PRK12325 | PRK12325 | prolyl-tRNA synthetase; Provisional |
1444-1601 | 9.37e-08 | |||||||||||
prolyl-tRNA synthetase; Provisional Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 56.41 E-value: 9.37e-08
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| MetRS_RNA | cd00939 | MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
898-937 | 9.86e-08 | |||||||||||
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 49.78 E-value: 9.86e-08
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| HisRS_RNA | cd00938 | HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
746-784 | 3.53e-07 | |||||||||||
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 48.23 E-value: 3.53e-07
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| GST_C_EF1Bgamma_like | cd03181 | Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ... |
76-160 | 1.89e-06 | |||||||||||
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds to membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF. Pssm-ID: 198290 [Multi-domain] Cd Length: 123 Bit Score: 48.71 E-value: 1.89e-06
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| GstA | COG0625 | Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
24-160 | 1.98e-06 | |||||||||||
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 50.28 E-value: 1.98e-06
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| HisRS_RNA | cd00938 | HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
1121-1158 | 2.10e-06 | |||||||||||
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 45.92 E-value: 2.10e-06
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| MetRS_RNA | cd00939 | MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
748-792 | 8.63e-06 | |||||||||||
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 44.39 E-value: 8.63e-06
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| PLN02734 | PLN02734 | glycyl-tRNA synthetase |
889-938 | 8.68e-06 | |||||||||||
glycyl-tRNA synthetase Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 50.51 E-value: 8.68e-06
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| HisRS_RNA | cd00938 | HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
821-857 | 8.91e-06 | |||||||||||
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 44.38 E-value: 8.91e-06
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| MetRS_RNA | cd00939 | MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
824-863 | 2.13e-05 | |||||||||||
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 43.23 E-value: 2.13e-05
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| PLN02734 | PLN02734 | glycyl-tRNA synthetase |
821-855 | 2.95e-05 | |||||||||||
glycyl-tRNA synthetase Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 48.97 E-value: 2.95e-05
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| PLN02734 | PLN02734 | glycyl-tRNA synthetase |
746-793 | 5.22e-05 | |||||||||||
glycyl-tRNA synthetase Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 48.20 E-value: 5.22e-05
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| HisRS_RNA | cd00938 | HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
892-930 | 6.74e-05 | |||||||||||
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 41.69 E-value: 6.74e-05
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| GST_C_YghU_like | cd10292 | C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and ... |
98-158 | 8.98e-05 | |||||||||||
C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YghU-like subfamily; composed of the Escherichia coli YghU and related proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YghU is one of nine GST homologs in the genome of Escherichia coli. It is similar to Escherichia coli YfcG in that it has poor GSH transferase activity towards typical substrates. It shows modest reductase activity towards some organic hydroperoxides. Like YfcG, YghU also shows good disulfide bond oxidoreductase activity comparable to the activities of glutaredoxins and thioredoxins. YghU does not contain a redox active cysteine residue, and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YghU reveals two GSH molecules bound in its active site. Pssm-ID: 198325 [Multi-domain] Cd Length: 118 Bit Score: 43.60 E-value: 8.98e-05
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| HisRS_RNA | cd00938 | HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
1049-1093 | 1.25e-04 | |||||||||||
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 40.92 E-value: 1.25e-04
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| GST_C_Ure2p_like | cd03178 | C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; ... |
97-158 | 1.39e-04 | |||||||||||
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p, YfcG and YghU from Escherichia coli, and related GST-like proteins. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. YfcG and YghU are two of the nine GST homologs in the genome of Escherichia coli. They display very low or no GSH transferase, but show very good disulfide bond oxidoreductase activity. YghU also shows modest organic hydroperoxide reductase activity. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of GSH with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Pssm-ID: 198288 [Multi-domain] Cd Length: 110 Bit Score: 43.01 E-value: 1.39e-04
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| GST_C_YfcG_like | cd10291 | C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ... |
101-158 | 3.61e-04 | |||||||||||
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG and related proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG does not contain a redox active cysteine residue and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified. Pssm-ID: 198324 [Multi-domain] Cd Length: 110 Bit Score: 41.87 E-value: 3.61e-04
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| HisRS_RNA | cd00938 | HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
972-1008 | 4.12e-04 | |||||||||||
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 39.76 E-value: 4.12e-04
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| ProRS_core_prok | cd00779 | Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
1321-1484 | 4.46e-04 | |||||||||||
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes. Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 44.10 E-value: 4.46e-04
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| ThrS | COG0441 | Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
1478-1601 | 6.27e-04 | |||||||||||
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 44.64 E-value: 6.27e-04
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| PRK13808 | PRK13808 | adenylate kinase; Provisional |
1120-1221 | 7.05e-04 | |||||||||||
adenylate kinase; Provisional Pssm-ID: 172341 [Multi-domain] Cd Length: 333 Bit Score: 43.72 E-value: 7.05e-04
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| GlyRS_RNA | cd00935 | GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
822-861 | 7.36e-04 | |||||||||||
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix-turn-helix structure , which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes. Pssm-ID: 238472 [Multi-domain] Cd Length: 51 Bit Score: 39.01 E-value: 7.36e-04
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| PLN02734 | PLN02734 | glycyl-tRNA synthetase |
1120-1157 | 9.23e-04 | |||||||||||
glycyl-tRNA synthetase Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 43.97 E-value: 9.23e-04
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| PRK11752 | PRK11752 | putative S-transferase; Provisional |
98-158 | 1.85e-03 | |||||||||||
putative S-transferase; Provisional Pssm-ID: 183298 [Multi-domain] Cd Length: 264 Bit Score: 42.22 E-value: 1.85e-03
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| GST_C_AIMP2 | cd03200 | Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
57-146 | 1.96e-03 | |||||||||||
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 2 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP2, also called p38 or JTV-1, contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It plays an important role in the control of cell fate via antiproliferative (by enhancing the TGF-beta signal) and proapoptotic (activation of p53 and TNF-alpha) activities. Its roles in the control of cell proliferation and death suggest that it is a potent tumor suppressor. AIMP2 heterozygous mice with lower than normal expression of AIMP2 show high susceptibility to tumorigenesis. AIMP2 is also a substrate of Parkin, an E3 ubiquitin ligase that is involved in the ubiquitylation and proteasomal degradation of its substrates. Mutations in the Parkin gene is found in 50% of patients with autosomal-recessive early-onset parkinsonism. The accumulation of AIMP2, due to impaired Parkin function, may play a role in the pathogenesis of Parkinson's disease. Pssm-ID: 198309 [Multi-domain] Cd Length: 96 Bit Score: 39.42 E-value: 1.96e-03
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| GST_C | pfam00043 | Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ... |
97-154 | 5.31e-03 | |||||||||||
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes. Pssm-ID: 459647 [Multi-domain] Cd Length: 93 Bit Score: 38.04 E-value: 5.31e-03
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| GST_C_3 | pfam14497 | Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. |
98-162 | 8.26e-03 | |||||||||||
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. Pssm-ID: 464190 [Multi-domain] Cd Length: 104 Bit Score: 37.54 E-value: 8.26e-03
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