MAG: hypothetical protein A2370_00220 [Candidatus Vogelbacteria bacterium RIFOXYB1_FULL_42_16]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||||||||||
| LeuS | COG0495 | Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
14-1136 | 0e+00 | ||||||||||||||||
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases : Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 1215.66 E-value: 0e+00
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| YdeN super family | cl42716 | Predicted esterase of the alpha/beta hydrolase fold [General function prediction only]; |
253-409 | 5.24e-16 | ||||||||||||||||
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only]; The actual alignment was detected with superfamily member COG3545: Pssm-ID: 442766 [Multi-domain] Cd Length: 170 Bit Score: 76.81 E-value: 5.24e-16
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| MutT | COG0494 | 8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ... |
577-693 | 6.29e-10 | ||||||||||||||||
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX family [Defense mechanisms]; : Pssm-ID: 440260 [Multi-domain] Cd Length: 143 Bit Score: 58.51 E-value: 6.29e-10
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| Name | Accession | Description | Interval | E-value | |||||||||||||||||
| LeuS | COG0495 | Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
14-1136 | 0e+00 | |||||||||||||||||
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 1215.66 E-value: 0e+00
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| PLN02563 | PLN02563 | aminoacyl-tRNA ligase |
6-1134 | 0e+00 | |||||||||||||||||
aminoacyl-tRNA ligase Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 967.37 E-value: 0e+00
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| leuS_bact | TIGR00396 | leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases ... |
15-1134 | 0e+00 | |||||||||||||||||
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases belong to two families so broadly different that they are represented by separate models. This model includes both eubacterial and mitochondrial leucyl-tRNA synthetases. It generates higher scores for some valyl-tRNA synthetases than for any archaeal or eukaryotic cytosolic leucyl-tRNA synthetase. Note that the enzyme from Aquifex aeolicus is split into alpha and beta chains; neither chain is long enough to score above the trusted cutoff, but the alpha chain scores well above the noise cutoff. The beta chain must be found by a model and search designed for partial length matches. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273057 [Multi-domain] Cd Length: 842 Bit Score: 961.52 E-value: 0e+00
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| LeuRS_core | cd00812 | catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
44-235 | 5.02e-74 | |||||||||||||||||
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate 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. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 247.93 E-value: 5.02e-74
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| tRNA-synt_1_2 | pfam13603 | Leucyl-tRNA synthetase, Domain 2; This is a family of the conserved region of Leucine-tRNA ... |
423-582 | 1.15e-58 | |||||||||||||||||
Leucyl-tRNA synthetase, Domain 2; This is a family of the conserved region of Leucine-tRNA ligase or Leucyl-tRNA synthetase, EC:6.1.1.4. Pssm-ID: 433342 [Multi-domain] Cd Length: 185 Bit Score: 199.70 E-value: 1.15e-58
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| YdeN | COG3545 | Predicted esterase of the alpha/beta hydrolase fold [General function prediction only]; |
253-409 | 5.24e-16 | |||||||||||||||||
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only]; Pssm-ID: 442766 [Multi-domain] Cd Length: 170 Bit Score: 76.81 E-value: 5.24e-16
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| MutT | COG0494 | 8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ... |
577-693 | 6.29e-10 | |||||||||||||||||
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX family [Defense mechanisms]; Pssm-ID: 440260 [Multi-domain] Cd Length: 143 Bit Score: 58.51 E-value: 6.29e-10
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| NUDIX | pfam00293 | NUDIX domain; |
572-701 | 2.19e-09 | |||||||||||||||||
NUDIX domain; Pssm-ID: 395229 [Multi-domain] Cd Length: 132 Bit Score: 56.72 E-value: 2.19e-09
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| NUDIX_Hydrolase | cd04684 | uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase ... |
604-693 | 1.07e-08 | |||||||||||||||||
uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase from Enterococcus faecalis, which has an unknown function. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467567 [Multi-domain] Cd Length: 140 Bit Score: 54.94 E-value: 1.07e-08
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| Abhydrolase_1 | pfam00561 | alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
251-400 | 4.10e-08 | |||||||||||||||||
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 55.59 E-value: 4.10e-08
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| Name | Accession | Description | Interval | E-value | |||||||||||||||||
| LeuS | COG0495 | Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
14-1136 | 0e+00 | |||||||||||||||||
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 1215.66 E-value: 0e+00
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| PLN02563 | PLN02563 | aminoacyl-tRNA ligase |
6-1134 | 0e+00 | |||||||||||||||||
aminoacyl-tRNA ligase Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 967.37 E-value: 0e+00
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| leuS_bact | TIGR00396 | leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases ... |
15-1134 | 0e+00 | |||||||||||||||||
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases belong to two families so broadly different that they are represented by separate models. This model includes both eubacterial and mitochondrial leucyl-tRNA synthetases. It generates higher scores for some valyl-tRNA synthetases than for any archaeal or eukaryotic cytosolic leucyl-tRNA synthetase. Note that the enzyme from Aquifex aeolicus is split into alpha and beta chains; neither chain is long enough to score above the trusted cutoff, but the alpha chain scores well above the noise cutoff. The beta chain must be found by a model and search designed for partial length matches. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273057 [Multi-domain] Cd Length: 842 Bit Score: 961.52 E-value: 0e+00
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| LeuRS_core | cd00812 | catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
44-235 | 5.02e-74 | |||||||||||||||||
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate 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. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 247.93 E-value: 5.02e-74
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| tRNA-synt_1_2 | pfam13603 | Leucyl-tRNA synthetase, Domain 2; This is a family of the conserved region of Leucine-tRNA ... |
423-582 | 1.15e-58 | |||||||||||||||||
Leucyl-tRNA synthetase, Domain 2; This is a family of the conserved region of Leucine-tRNA ligase or Leucyl-tRNA synthetase, EC:6.1.1.4. Pssm-ID: 433342 [Multi-domain] Cd Length: 185 Bit Score: 199.70 E-value: 1.15e-58
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| valS | PRK13208 | valyl-tRNA synthetase; Reviewed |
12-184 | 1.94e-50 | |||||||||||||||||
valyl-tRNA synthetase; Reviewed Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 192.33 E-value: 1.94e-50
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| LeuRS_core | cd00812 | catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
746-953 | 4.18e-49 | |||||||||||||||||
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate 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. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 177.05 E-value: 4.18e-49
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| ValRS_core | cd00817 | catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
44-210 | 3.71e-39 | |||||||||||||||||
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate 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. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 150.47 E-value: 3.71e-39
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| valS | TIGR00422 | valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
11-183 | 7.20e-37 | |||||||||||||||||
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 150.59 E-value: 7.20e-37
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| tRNA-synt_1 | pfam00133 | tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
23-940 | 5.98e-33 | |||||||||||||||||
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included. Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 136.00 E-value: 5.98e-33
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| ileS | TIGR00392 | isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ... |
10-1070 | 6.12e-32 | |||||||||||||||||
isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ligase and is particularly closely related to the valyl tRNA synthetase. This model may recognize IleS from every species, including eukaryotic cytosolic and mitochondrial forms. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273054 [Multi-domain] Cd Length: 861 Bit Score: 134.81 E-value: 6.12e-32
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| IleS | COG0060 | Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
733-1070 | 1.55e-30 | |||||||||||||||||
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 130.59 E-value: 1.55e-30
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| Anticodon_Ia_Leu_BEm | cd07958 | Anticodon-binding domain of bacterial and eukaryotic mitochondrial leucyl tRNA synthetases; ... |
953-1051 | 2.07e-30 | |||||||||||||||||
Anticodon-binding domain of bacterial and eukaryotic mitochondrial leucyl tRNA synthetases; This domain is found in leucyl tRNA synthetases (LeuRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain. In contrast to other class Ia enzymes, the anticodon is not used as an identity element in LeuRS (with exceptions such as Saccharomyces cerevisiae and some other eukaryotes). No anticodon-binding site can be defined for this family, which includes bacterial and eukaryotic mitochondrial members, as well as LeuRS from the archaeal Halobacteria. LeuRS catalyzes the transfer of leucine to the 3'-end of its tRNA. Pssm-ID: 153412 [Multi-domain] Cd Length: 117 Bit Score: 116.17 E-value: 2.07e-30
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| valS | PRK13208 | valyl-tRNA synthetase; Reviewed |
752-1086 | 1.51e-29 | |||||||||||||||||
valyl-tRNA synthetase; Reviewed Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 126.85 E-value: 1.51e-29
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| IleS | COG0060 | Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
12-179 | 8.11e-28 | |||||||||||||||||
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 121.73 E-value: 8.11e-28
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| Ile_Leu_Val_MetRS_core | cd00668 | catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
44-167 | 2.14e-26 | |||||||||||||||||
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate 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. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function. Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 110.97 E-value: 2.14e-26
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| MetG | COG0143 | Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
52-193 | 2.71e-25 | |||||||||||||||||
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 111.74 E-value: 2.71e-25
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| tRNA-synt_1g | pfam09334 | tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
51-246 | 5.27e-23 | |||||||||||||||||
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 102.75 E-value: 5.27e-23
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| leuS | PRK12300 | leucyl-tRNA synthetase; Reviewed |
59-186 | 3.50e-22 | |||||||||||||||||
leucyl-tRNA synthetase; Reviewed Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 103.41 E-value: 3.50e-22
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| leuS | PRK12300 | leucyl-tRNA synthetase; Reviewed |
434-1070 | 3.68e-22 | |||||||||||||||||
leucyl-tRNA synthetase; Reviewed Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 103.41 E-value: 3.68e-22
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| MetRS_core | cd00814 | catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
52-246 | 7.36e-22 | |||||||||||||||||
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. 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. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function. Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 97.99 E-value: 7.36e-22
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| ValRS_core | cd00817 | catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
749-939 | 7.68e-21 | |||||||||||||||||
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate 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. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 96.16 E-value: 7.68e-21
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| PRK11893 | PRK11893 | methionyl-tRNA synthetase; Reviewed |
52-210 | 8.58e-21 | |||||||||||||||||
methionyl-tRNA synthetase; Reviewed Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 97.65 E-value: 8.58e-21
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| valS | PRK05729 | valyl-tRNA synthetase; Reviewed |
14-183 | 2.87e-20 | |||||||||||||||||
valyl-tRNA synthetase; Reviewed Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 97.10 E-value: 2.87e-20
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| PLN02843 | PLN02843 | isoleucyl-tRNA synthetase |
21-1066 | 3.21e-20 | |||||||||||||||||
isoleucyl-tRNA synthetase Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 97.15 E-value: 3.21e-20
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| Anticodon_1 | pfam08264 | Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
981-1101 | 3.66e-20 | |||||||||||||||||
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA synthetases. The domain binds to the anticodon of the tRNA ligase. Pssm-ID: 400523 [Multi-domain] Cd Length: 141 Bit Score: 87.84 E-value: 3.66e-20
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| valS | PRK14900 | valyl-tRNA synthetase; Provisional |
15-183 | 2.85e-19 | |||||||||||||||||
valyl-tRNA synthetase; Provisional Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 94.29 E-value: 2.85e-19
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| IleRS_core | cd00818 | catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
725-940 | 1.83e-18 | |||||||||||||||||
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate 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. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. Pssm-ID: 173909 [Multi-domain] Cd Length: 338 Bit Score: 88.06 E-value: 1.83e-18
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| IleRS_core | cd00818 | catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
43-250 | 1.85e-18 | |||||||||||||||||
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate 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. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. Pssm-ID: 173909 [Multi-domain] Cd Length: 338 Bit Score: 88.06 E-value: 1.85e-18
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| ValS | COG0525 | Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
12-183 | 2.20e-18 | |||||||||||||||||
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 90.88 E-value: 2.20e-18
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| valS | PRK14900 | valyl-tRNA synthetase; Provisional |
430-1066 | 2.07e-16 | |||||||||||||||||
valyl-tRNA synthetase; Provisional Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 84.66 E-value: 2.07e-16
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| YdeN | COG3545 | Predicted esterase of the alpha/beta hydrolase fold [General function prediction only]; |
253-409 | 5.24e-16 | |||||||||||||||||
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only]; Pssm-ID: 442766 [Multi-domain] Cd Length: 170 Bit Score: 76.81 E-value: 5.24e-16
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| PTZ00419 | PTZ00419 | valyl-tRNA synthetase-like protein; Provisional |
1-183 | 5.06e-14 | |||||||||||||||||
valyl-tRNA synthetase-like protein; Provisional Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 76.97 E-value: 5.06e-14
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| valS | PRK05729 | valyl-tRNA synthetase; Reviewed |
905-1066 | 5.11e-14 | |||||||||||||||||
valyl-tRNA synthetase; Reviewed Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 77.07 E-value: 5.11e-14
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| ValS | COG0525 | Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
905-1070 | 6.14e-14 | |||||||||||||||||
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 76.63 E-value: 6.14e-14
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| Ile_Leu_Val_MetRS_core | cd00668 | catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
750-942 | 1.04e-13 | |||||||||||||||||
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate 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. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function. Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 73.22 E-value: 1.04e-13
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| metG | PRK00133 | methionyl-tRNA synthetase; Reviewed |
52-193 | 1.07e-13 | |||||||||||||||||
methionyl-tRNA synthetase; Reviewed Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 75.57 E-value: 1.07e-13
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| PLN02882 | PLN02882 | aminoacyl-tRNA ligase |
11-179 | 1.26e-13 | |||||||||||||||||
aminoacyl-tRNA ligase Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 75.92 E-value: 1.26e-13
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| PLN02381 | PLN02381 | valyl-tRNA synthetase |
4-183 | 4.27e-13 | |||||||||||||||||
valyl-tRNA synthetase Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 74.17 E-value: 4.27e-13
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| PRK12267 | PRK12267 | methionyl-tRNA synthetase; Reviewed |
53-196 | 6.01e-12 | |||||||||||||||||
methionyl-tRNA synthetase; Reviewed Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 69.83 E-value: 6.01e-12
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| PTZ00427 | PTZ00427 | isoleucine-tRNA ligase, putative; Provisional |
21-182 | 6.71e-12 | |||||||||||||||||
isoleucine-tRNA ligase, putative; Provisional Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 70.00 E-value: 6.71e-12
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| PLN02943 | PLN02943 | aminoacyl-tRNA ligase |
409-1069 | 1.56e-11 | |||||||||||||||||
aminoacyl-tRNA ligase Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 68.81 E-value: 1.56e-11
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| PLN02943 | PLN02943 | aminoacyl-tRNA ligase |
8-183 | 2.66e-11 | |||||||||||||||||
aminoacyl-tRNA ligase Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 68.04 E-value: 2.66e-11
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| MutT | COG0494 | 8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ... |
577-693 | 6.29e-10 | |||||||||||||||||
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX family [Defense mechanisms]; Pssm-ID: 440260 [Multi-domain] Cd Length: 143 Bit Score: 58.51 E-value: 6.29e-10
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| MetG | COG0143 | Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
911-1052 | 6.91e-10 | |||||||||||||||||
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 62.82 E-value: 6.91e-10
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| PRK12267 | PRK12267 | methionyl-tRNA synthetase; Reviewed |
872-1053 | 1.43e-09 | |||||||||||||||||
methionyl-tRNA synthetase; Reviewed Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 62.13 E-value: 1.43e-09
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| NUDIX | pfam00293 | NUDIX domain; |
572-701 | 2.19e-09 | |||||||||||||||||
NUDIX domain; Pssm-ID: 395229 [Multi-domain] Cd Length: 132 Bit Score: 56.72 E-value: 2.19e-09
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| Anticodon_Ia_Ile_ABEc | cd07961 | Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA ... |
986-1077 | 4.70e-09 | |||||||||||||||||
Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA synthetases; This domain is found in isoleucyl tRNA synthetases (IleRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. This family includes bacterial, archaeal, and eukaryotic cytoplasmic members. IleRS catalyzes the transfer of isoleucine to the 3'-end of its tRNA. Pssm-ID: 153415 [Multi-domain] Cd Length: 183 Bit Score: 57.18 E-value: 4.70e-09
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| YjhB | COG1051 | ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism]; |
575-691 | 4.98e-09 | |||||||||||||||||
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism]; Pssm-ID: 440671 [Multi-domain] Cd Length: 125 Bit Score: 55.37 E-value: 4.98e-09
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| NUDIX_Hydrolase | cd04684 | uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase ... |
604-693 | 1.07e-08 | |||||||||||||||||
uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase from Enterococcus faecalis, which has an unknown function. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467567 [Multi-domain] Cd Length: 140 Bit Score: 54.94 E-value: 1.07e-08
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| PLN02882 | PLN02882 | aminoacyl-tRNA ligase |
751-1066 | 1.23e-08 | |||||||||||||||||
aminoacyl-tRNA ligase Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 59.35 E-value: 1.23e-08
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| NUDIX_Ap4A_Nudt2 | cd03428 | diadenosine tetraphosphate; Diadenosine tetraphosphate (Ap4A; EC 3.6.1.17), also called NUDIX ... |
587-698 | 1.51e-08 | |||||||||||||||||
diadenosine tetraphosphate; Diadenosine tetraphosphate (Ap4A; EC 3.6.1.17), also called NUDIX (nucleoside diphosphate-linked moiety X)) motif 2/Nudt2, is a member of the NUDIX hydrolase superfamily. Ap4A hydrolases are well represented in a variety of prokaryotic and eukaryotic organisms. Phylogenetic analysis reveals two distinct subgroups where plant enzymes fall into one subfamily and fungi/animals/archaea enzymes, represented by this subfamily, fall into another. Bacterial enzymes are found in both subfamilies. Ap4A is a potential by-product of aminoacyl tRNA synthesis, and accumulation of Ap4A has been implicated in a range of biological events, such as DNA replication, cellular differentiation, heat shock, metabolic stress, and apoptosis. Ap4A hydrolase cleaves Ap4A asymmetrically into ATP and AMP. It is important in the invasive properties of bacteria and thus presents a potential target for inhibition of such invasive bacteria. Besides the signature NUDIX motif (G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val) that functions as a metal binding and catalytic site, and a required divalent cation, Ap4A hydrolase is structurally similar to the other members of the NUDIX hydrolase superfamily with some degree of variation. Several regions in the sequences are poorly defined and substrate and metal binding sites are only predicted based on kinetic studies. Pssm-ID: 467534 [Multi-domain] Cd Length: 132 Bit Score: 54.48 E-value: 1.51e-08
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| PRK11893 | PRK11893 | methionyl-tRNA synthetase; Reviewed |
911-1076 | 1.78e-08 | |||||||||||||||||
methionyl-tRNA synthetase; Reviewed Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 58.35 E-value: 1.78e-08
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| NUDIX_Hydrolase | cd02883 | NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ... |
575-685 | 1.98e-08 | |||||||||||||||||
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467528 [Multi-domain] Cd Length: 106 Bit Score: 53.18 E-value: 1.98e-08
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| NUDIX_Hydrolase | cd18875 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
585-710 | 2.11e-08 | |||||||||||||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467587 [Multi-domain] Cd Length: 144 Bit Score: 54.11 E-value: 2.11e-08
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| Abhydrolase_1 | pfam00561 | alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
251-400 | 4.10e-08 | |||||||||||||||||
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 55.59 E-value: 4.10e-08
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| NUDIX_Ap6A_hydrolase | cd03673 | diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a ... |
604-688 | 4.22e-08 | |||||||||||||||||
diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a member of the NUDIX hydrolase superfamily. Ap6A hydrolase specifically hydrolyzes diadenosine polyphosphates, but not ATP or diadenosine triphosphate, and it generates ATP as the product. Ap6A, the most preferred substrate, hydrolyzes to produce two ATP molecules, which is a novel hydrolysis mode for Ap6A. These results indicate that Ap6A hydrolase is a diadenosine polyphosphate hydrolase. It requires the presence of a divalent cation, such as Mn2+, Mg2+, Zn2+, and Co2+, for activity. Members of the NUDIX hydrolase superfamily are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Pssm-ID: 467541 [Multi-domain] Cd Length: 131 Bit Score: 52.94 E-value: 4.22e-08
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| EstA | COG1075 | Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
247-342 | 8.62e-08 | |||||||||||||||||
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism]; Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 51.37 E-value: 8.62e-08
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| PldB | COG2267 | Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
249-347 | 1.58e-07 | |||||||||||||||||
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 53.47 E-value: 1.58e-07
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| NUDIX_Hydrolase | cd04688 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
578-691 | 1.65e-07 | |||||||||||||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467570 [Multi-domain] Cd Length: 130 Bit Score: 51.40 E-value: 1.65e-07
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| PTZ00427 | PTZ00427 | isoleucine-tRNA ligase, putative; Provisional |
751-940 | 2.18e-07 | |||||||||||||||||
isoleucine-tRNA ligase, putative; Provisional Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 55.36 E-value: 2.18e-07
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| NUDIX_Nudt17 | cd04694 | nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) ... |
604-697 | 1.03e-06 | |||||||||||||||||
nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) motif 17 (EC 3.6.1.-) encoded by the NUDT17 gene on chromosome 1q21.1 and encodes an enzyme thought to hydrolyse some nucleoside diphosphate derivatives. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. Pssm-ID: 467576 [Multi-domain] Cd Length: 135 Bit Score: 49.21 E-value: 1.03e-06
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| NUDIX_ASFGF2_Nudt6 | cd04670 | Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC ... |
604-698 | 1.04e-06 | |||||||||||||||||
Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC 3.6.1.-), also known as nucleoside diphosphate-linked moiety X)) motif 6/Nudt6, and similar proteins including peroxisomal coenzyme A diphosphatase/Nudt7 and mitochondrial coenzyme A diphosphatase/Nudt8. The Nudt6 gene overlaps and lies on the opposite strand from FGF2 gene, and is thought to be the FGF2 antisense gene. The two genes are independently transcribed, and their expression shows an inverse relationship, suggesting that this antisense transcript may regulate FGF2 expression. This gene has also been shown to have hormone-regulatory and antiproliferative actions in the pituitary that are independent of FGF2 expression. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. Pssm-ID: 467554 [Multi-domain] Cd Length: 131 Bit Score: 49.07 E-value: 1.04e-06
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| Anticodon_Ia_Ile_BEm | cd07960 | Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; ... |
986-1066 | 1.09e-06 | |||||||||||||||||
Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; This domain is found in isoleucyl tRNA synthetases (IleRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. This family includes bacterial and eukaryotic mitochondrial members. IleRS catalyzes the transfer of isoleucine to the 3'-end of its tRNA. Pssm-ID: 153414 [Multi-domain] Cd Length: 180 Bit Score: 50.22 E-value: 1.09e-06
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| Anticodon_Ia_Leu_AEc | cd07959 | Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
953-1048 | 1.75e-06 | |||||||||||||||||
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This domain is found in leucyl tRNA synthetases (LeuRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain. In contrast to other class Ia enzymes, the anticodon is not used as an identity element in LeuRS (with exceptions such as Saccharomyces cerevisiae and some other eukaryotes). No anticodon-binding site can be defined for this family, which includes archaeal and eukaryotic cytoplasmic members. LeuRS catalyzes the transfer of leucine to the 3'-end of its tRNA. Pssm-ID: 153413 [Multi-domain] Cd Length: 117 Bit Score: 47.97 E-value: 1.75e-06
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| NUDIX_DHNTPase_like | cd04664 | dihydroneopterin hydrolase; DHNTP pyrophosphatase (DHNTPase) catalyzes the hydrolysis of ... |
577-693 | 2.03e-06 | |||||||||||||||||
dihydroneopterin hydrolase; DHNTP pyrophosphatase (DHNTPase) catalyzes the hydrolysis of dihydroneopterin triphosphate (DHNTP) to dihydroneopterin monophosphate (DHNMP) and pyrophosphate,the second step in the pterin branch of the folate synthesis pathway in bacteria. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. Pssm-ID: 467549 [Multi-domain] Cd Length: 132 Bit Score: 48.01 E-value: 2.03e-06
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| PLN02959 | PLN02959 | aminoacyl-tRNA ligase |
18-96 | 2.68e-06 | |||||||||||||||||
aminoacyl-tRNA ligase Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 51.99 E-value: 2.68e-06
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| NUDIX_ADPRase_Nudt5_UGPPase_Nudt14 | cd03424 | ADP-ribose pyrophosphatase, UDP-glucose pyrophosphatase, and similar proteins; ADP-ribose ... |
572-638 | 3.44e-06 | |||||||||||||||||
ADP-ribose pyrophosphatase, UDP-glucose pyrophosphatase, and similar proteins; ADP-ribose pyrophosphatase (ADPRase) ( NUDIX (Nucleoside diphosphate-linked moiety X)) motif 5; Nudt5) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as nucleoside diphosphate-linked moiety X)) motif 14; Nudt14) hydrolyzes the pyrophosphate of the nucleoside diphosphate sugar to generate glucose-1-P and UMP. In mammals, UDP-glucose is the glucosyl donor for the synthesis of the storage polysaccharide glycogen. UGPPase, as a regulator of UDP-glucose, could play a regulatory role, but it has been shown to prefer ADP-ribose over UDP-glucose. Like other members of the NUDIX hydrolase superfamily, it requires a divalent cation, such as Mg2+, for its activity. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. Pssm-ID: 467530 [Multi-domain] Cd Length: 134 Bit Score: 47.50 E-value: 3.44e-06
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| Anticodon_Ia_Val | cd07962 | Anticodon-binding domain of valyl tRNA synthetases; This domain is found in valyl tRNA ... |
986-1051 | 1.63e-05 | |||||||||||||||||
Anticodon-binding domain of valyl tRNA synthetases; This domain is found in valyl tRNA synthetases (ValRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. ValRS catalyzes the transfer of valine to the 3'-end of its tRNA. Pssm-ID: 153416 [Multi-domain] Cd Length: 135 Bit Score: 45.63 E-value: 1.63e-05
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| PTZ00419 | PTZ00419 | valyl-tRNA synthetase-like protein; Provisional |
422-547 | 2.32e-05 | |||||||||||||||||
valyl-tRNA synthetase-like protein; Provisional Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 48.85 E-value: 2.32e-05
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| MetRS_core | cd00814 | catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
881-948 | 2.44e-05 | |||||||||||||||||
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. 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. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function. Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 47.53 E-value: 2.44e-05
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| PLN02610 | PLN02610 | probable methionyl-tRNA synthetase |
60-191 | 2.94e-05 | |||||||||||||||||
probable methionyl-tRNA synthetase Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 48.24 E-value: 2.94e-05
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| NUDIX_ADPRase_Nudt5 | cd18888 | ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) (also known as NUDIX ... |
566-626 | 3.83e-05 | |||||||||||||||||
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) (also known as NUDIX (Nucleoside diphosphate-linked moiety X)) motif 5; Nudt5) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. Pssm-ID: 467598 [Multi-domain] Cd Length: 149 Bit Score: 44.78 E-value: 3.83e-05
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| NUDIX_Dcp2p_Nudt20 | cd03672 | mRNA decapping enzyme 2; mRNA decapping enzyme 2 (Dcp2p; EC 3.6.1.62), nucleoside diphosphate ... |
577-634 | 4.10e-05 | |||||||||||||||||
mRNA decapping enzyme 2; mRNA decapping enzyme 2 (Dcp2p; EC 3.6.1.62), nucleoside diphosphate linked moiety X))-type motif 20/Nudt20, is required for degradation of mRNAs, both in normal mRNA turnover, and in nonsense-mediated mRNA decay (NMD). Its catalytic subunit, and Dcp1p are the two components of the decapping enzyme complex. Decapping is a key step in both general and nonsense-mediated 5'->3' mRNA-decay pathways. Dcp2p contains an all-alpha helical N-terminal domain and a C-terminal domain which has the NUDIX fold. While decapping is not dependent on the N-terminus of Dcp2p, it does affect its efficiency. Dcp1p binds the N-terminal domain of Dcp2p stimulating the decapping activity of Dcp2p. Decapping permits the degradation of the transcript and is a site of numerous control inputs. It is responsible for nonsense-mediated decay as well as AU-rich element (ARE)-mediated decay. In addition, it may also play a role in the levels of mRNA. Enzymes belonging to the NUDIX hydrolase superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V). Pssm-ID: 467540 Cd Length: 144 Bit Score: 44.85 E-value: 4.10e-05
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| NUDIX_Hydrolase | cd04667 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
604-691 | 6.91e-05 | |||||||||||||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467552 [Multi-domain] Cd Length: 117 Bit Score: 43.43 E-value: 6.91e-05
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| NUDIX_Hydrolase | cd04693 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
576-694 | 6.94e-05 | |||||||||||||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467575 [Multi-domain] Cd Length: 157 Bit Score: 44.44 E-value: 6.94e-05
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| NUDIX_Hydrolase | cd04663 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
604-656 | 1.25e-04 | |||||||||||||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467548 [Multi-domain] Cd Length: 132 Bit Score: 43.05 E-value: 1.25e-04
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| MenH | COG0596 | 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
253-408 | 1.30e-04 | |||||||||||||||||
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 44.61 E-value: 1.30e-04
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| PLN02224 | PLN02224 | methionine-tRNA ligase |
30-187 | 1.45e-04 | |||||||||||||||||
methionine-tRNA ligase Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 45.86 E-value: 1.45e-04
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| NUDIX_Hydrolase | cd04685 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
604-627 | 1.57e-04 | |||||||||||||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467568 [Multi-domain] Cd Length: 138 Bit Score: 42.95 E-value: 1.57e-04
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| NUDIX_Hydrolase | cd03674 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
604-691 | 2.92e-04 | |||||||||||||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467542 [Multi-domain] Cd Length: 130 Bit Score: 41.86 E-value: 2.92e-04
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| NUDIX_Hydrolase | cd18882 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
598-631 | 3.04e-04 | |||||||||||||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467593 [Multi-domain] Cd Length: 130 Bit Score: 41.86 E-value: 3.04e-04
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| NUDIX_Hydrolase | cd04692 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
571-686 | 3.05e-04 | |||||||||||||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467574 [Multi-domain] Cd Length: 142 Bit Score: 42.16 E-value: 3.05e-04
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| NUDIX_MutT_Nudt1 | cd18886 | MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ... |
585-631 | 3.10e-04 | |||||||||||||||||
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 1/Nudt1, is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases. Pssm-ID: 467596 [Multi-domain] Cd Length: 147 Bit Score: 42.22 E-value: 3.10e-04
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| NUDIX_Ap4A_hydrolase_plant_like | cd03671 | plant diadenosine tetraphosphate (Ap4A) hydrolase and similar proteins; Diadenosine ... |
601-625 | 4.45e-04 | |||||||||||||||||
plant diadenosine tetraphosphate (Ap4A) hydrolase and similar proteins; Diadenosine tetraphosphate (Ap4A) hydrolase is a member of the NUDIX hydrolase superfamily. Members of this family are well represented in a variety of prokaryotic and eukaryotic organisms. Phylogenetic analysis reveals two distinct subgroups where plant enzymes fall into one group (represented by this subfamily) and fungi/animals/archaea enzymes fall into another. Bacterial enzymes are found in both subfamilies. Ap4A is a potential by-product of aminoacyl tRNA synthesis, and accumulation of Ap4A has been implicated in a range of biological events, such as DNA replication, cellular differentiation, heat shock, metabolic stress, and apoptosis. Ap4A hydrolase cleaves Ap4A asymmetrically into ATP and AMP. It is important in the invasive properties of bacteria and thus presents a potential target for the inhibition of such invasive bacteria. Besides the signature NUDIX motif (G[X5]E[X7]REUXEEXGU where U is Ile, Leu, or Val), Ap4A hydrolase is structurally similar to the other members of the NUDIX hydrolase superfamily with some degree of variations. Several regions in the sequences are poorly defined and substrate and metal binding sites are only predicted based on kinetic studies. Pssm-ID: 467539 [Multi-domain] Cd Length: 147 Bit Score: 41.78 E-value: 4.45e-04
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| Idi | COG1443 | Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ... |
604-694 | 6.00e-04 | |||||||||||||||||
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis Pssm-ID: 441052 [Multi-domain] Cd Length: 162 Bit Score: 41.72 E-value: 6.00e-04
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| LIDHydrolase | pfam10230 | Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. ... |
293-350 | 6.49e-04 | |||||||||||||||||
Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. The function is as a lipid-droplet hydrolase. Human LDAH plays a role in cholesterol homeostasis. Pssm-ID: 370901 Cd Length: 261 Bit Score: 43.05 E-value: 6.49e-04
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| Anticodon_Ia_like | cd07375 | Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ... |
956-1040 | 6.53e-04 | |||||||||||||||||
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This domain is found in a variety of class Ia aminoacyl tRNA synthetases, C-terminal to the catalytic core domain. It recognizes and specifically binds to the anticodon of the tRNA. Aminoacyl tRNA synthetases catalyze the transfer of cognate amino acids to the 3'-end of their tRNAs by specifically recognizing cognate from non-cognate amino acids. Members include valyl-, leucyl-, isoleucyl-, cysteinyl-, arginyl-, and methionyl-tRNA synthethases. This superfamily also includes a domain from MshC, an enzyme in the mycothiol biosynthetic pathway. Pssm-ID: 153408 [Multi-domain] Cd Length: 117 Bit Score: 40.57 E-value: 6.53e-04
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| NUDIX_ADPRase_NudE | cd24156 | NUDIX domain family NudE found in Escherichia coli, and similar proteins; The adenosine ... |
600-626 | 1.99e-03 | |||||||||||||||||
NUDIX domain family NudE found in Escherichia coli, and similar proteins; The adenosine nucleotide hydrolase NudE protein in Escherichia coli is a NUDIX hydrolase family member active against ADP ribose, NADH, AP2A and AP3A33, and is classified as a hydrolase (E.C. 3.6.1.-) based on gene annotations. It is an ADPRase (EC 3.6.1.13) catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. Pssm-ID: 467604 [Multi-domain] Cd Length: 134 Bit Score: 39.54 E-value: 1.99e-03
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| NUDIX_Hydrolase | cd18874 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
598-692 | 2.70e-03 | |||||||||||||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467586 [Multi-domain] Cd Length: 125 Bit Score: 39.19 E-value: 2.70e-03
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| Abhydrolase_6 | pfam12697 | Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
252-347 | 5.10e-03 | |||||||||||||||||
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity. Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 39.76 E-value: 5.10e-03
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| metG | PRK00133 | methionyl-tRNA synthetase; Reviewed |
911-1054 | 5.25e-03 | |||||||||||||||||
methionyl-tRNA synthetase; Reviewed Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 40.91 E-value: 5.25e-03
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| tRNA-synt_1g | pfam09334 | tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
911-948 | 5.53e-03 | |||||||||||||||||
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 40.35 E-value: 5.53e-03
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| nudE | PRK11762 | adenosine nucleotide hydrolase NudE; Provisional |
600-626 | 6.66e-03 | |||||||||||||||||
adenosine nucleotide hydrolase NudE; Provisional Pssm-ID: 183303 Cd Length: 185 Bit Score: 39.02 E-value: 6.66e-03
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| NUDIX_Hydrolase | cd03675 | uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase ... |
578-627 | 7.63e-03 | |||||||||||||||||
uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase from Nitrosomonas europaea, which has an unknown function. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467543 [Multi-domain] Cd Length: 138 Bit Score: 37.89 E-value: 7.63e-03
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| COG4119 | COG4119 | Predicted NTP pyrophosphohydrolase, NUDIX family [Nucleotide transport and metabolism, General ... |
604-629 | 9.85e-03 | |||||||||||||||||
Predicted NTP pyrophosphohydrolase, NUDIX family [Nucleotide transport and metabolism, General function prediction only]; Pssm-ID: 443295 [Multi-domain] Cd Length: 153 Bit Score: 37.88 E-value: 9.85e-03
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