protein deglycase YajL [Escherichia albertii]
Protein Classification
DJ-1/PfpI family protein( domain architecture ID 10793591)
DJ-1/PfpI family protein, similar to Escherichia coli YajL, a covalent chaperone that protects cells against protein sulfenylation
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| PRK11574 | PRK11574 | protein deglycase YajL; |
1-196 | 1.98e-148 | ||||
protein deglycase YajL; : Pssm-ID: 183210 [Multi-domain] Cd Length: 196 Bit Score: 409.55 E-value: 1.98e-148
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| Name | Accession | Description | Interval | E-value | ||||
| PRK11574 | PRK11574 | protein deglycase YajL; |
1-196 | 1.98e-148 | ||||
protein deglycase YajL; Pssm-ID: 183210 [Multi-domain] Cd Length: 196 Bit Score: 409.55 E-value: 1.98e-148
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| not_thiJ | TIGR01383 | DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ... |
4-183 | 9.99e-82 | ||||
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of proteins. PfpI, represented by a distinct model, is a putative intracellular cysteine protease. DJ-1 is described as an oncogene that acts cooperatively with H-Ras. Many members of the DJ-1 clade are annotated (apparently incorrectly) as ThiJ, a protein of thiamine biosynthesis. However, published reports of ThiJ activity and identification of a ThiJ/ThiD bifunctional protein describe an unrelated locus mapping near ThiM, rather than the DJ-1 homolog of E. coli. The ThiJ designation for this family may be spurious; the cited paper refers to a locus near thiD and thiM in E. coli, unlike the gene represented here. Current public annotation reflects ThiJ/ThiD bifunctional activity, apparently a property of ThiD and not of this locus. [Unknown function, General] Pssm-ID: 213612 [Multi-domain] Cd Length: 179 Bit Score: 240.30 E-value: 9.99e-82
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| GATase1_DJ-1 | cd03135 | Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ... |
5-172 | 1.44e-58 | ||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme. Pssm-ID: 153229 [Multi-domain] Cd Length: 163 Bit Score: 180.83 E-value: 1.44e-58
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| DJ-1_PfpI | pfam01965 | DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ... |
3-171 | 2.94e-57 | ||||
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators. Pssm-ID: 396514 [Multi-domain] Cd Length: 165 Bit Score: 177.83 E-value: 2.94e-57
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| YajL | COG0693 | Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ... |
1-172 | 4.66e-51 | ||||
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms]; Pssm-ID: 440457 [Multi-domain] Cd Length: 170 Bit Score: 162.20 E-value: 4.66e-51
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| Name | Accession | Description | Interval | E-value | ||||
| PRK11574 | PRK11574 | protein deglycase YajL; |
1-196 | 1.98e-148 | ||||
protein deglycase YajL; Pssm-ID: 183210 [Multi-domain] Cd Length: 196 Bit Score: 409.55 E-value: 1.98e-148
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| not_thiJ | TIGR01383 | DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ... |
4-183 | 9.99e-82 | ||||
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of proteins. PfpI, represented by a distinct model, is a putative intracellular cysteine protease. DJ-1 is described as an oncogene that acts cooperatively with H-Ras. Many members of the DJ-1 clade are annotated (apparently incorrectly) as ThiJ, a protein of thiamine biosynthesis. However, published reports of ThiJ activity and identification of a ThiJ/ThiD bifunctional protein describe an unrelated locus mapping near ThiM, rather than the DJ-1 homolog of E. coli. The ThiJ designation for this family may be spurious; the cited paper refers to a locus near thiD and thiM in E. coli, unlike the gene represented here. Current public annotation reflects ThiJ/ThiD bifunctional activity, apparently a property of ThiD and not of this locus. [Unknown function, General] Pssm-ID: 213612 [Multi-domain] Cd Length: 179 Bit Score: 240.30 E-value: 9.99e-82
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| GATase1_DJ-1 | cd03135 | Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ... |
5-172 | 1.44e-58 | ||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme. Pssm-ID: 153229 [Multi-domain] Cd Length: 163 Bit Score: 180.83 E-value: 1.44e-58
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| DJ-1_PfpI | pfam01965 | DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ... |
3-171 | 2.94e-57 | ||||
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators. Pssm-ID: 396514 [Multi-domain] Cd Length: 165 Bit Score: 177.83 E-value: 2.94e-57
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| YajL | COG0693 | Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ... |
1-172 | 4.66e-51 | ||||
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms]; Pssm-ID: 440457 [Multi-domain] Cd Length: 170 Bit Score: 162.20 E-value: 4.66e-51
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| GATase1_PfpI_like | cd03134 | A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ... |
5-171 | 1.51e-13 | ||||
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704. Pssm-ID: 153228 [Multi-domain] Cd Length: 165 Bit Score: 65.26 E-value: 1.51e-13
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| PfpI | TIGR01382 | intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ... |
6-172 | 5.26e-11 | ||||
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 273591 [Multi-domain] Cd Length: 166 Bit Score: 58.58 E-value: 5.26e-11
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| GATase1_PfpI_2 | cd03139 | Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ... |
27-185 | 2.10e-08 | ||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Pssm-ID: 153233 [Multi-domain] Cd Length: 183 Bit Score: 51.77 E-value: 2.10e-08
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| GATase1 | cd01653 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
6-107 | 2.45e-08 | ||||
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 50.29 E-value: 2.45e-08
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| GATase1_PfpI_1 | cd03169 | Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ... |
27-157 | 4.30e-08 | ||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Pssm-ID: 153243 [Multi-domain] Cd Length: 180 Bit Score: 50.72 E-value: 4.30e-08
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| GAT_1 | cd03128 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
6-107 | 1.60e-07 | ||||
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain. Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 47.58 E-value: 1.60e-07
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| GATase1_PfpI_3 | cd03140 | Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ... |
5-172 | 2.31e-07 | ||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Pssm-ID: 153234 [Multi-domain] Cd Length: 170 Bit Score: 48.37 E-value: 2.31e-07
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| GATase1_Hsp31_like | cd03141 | Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ... |
57-172 | 2.22e-06 | ||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein (EcHsp31). This group includes EcHsp31 and Saccharomyces cerevisiae Ydr533c protein. EcHsp31 has chaperone activity. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. EcHsp31 coordinates a metal ion using a 2-His-1-carboxylate motif present in various ions that use iron as a cofactor such as Carboxypeptidase A. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1 domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For EcHsp31, this Cys together with a different His and, an Asp (rather than a Glu) residue form a different catalytic triad from the typical GATase1 domain. For Ydr533c a catalytic triad forms from the conserved Cys together with a different His and Glu from that of the typical GATase1domain. Ydr533c protein and EcHsp31 are homodimers. Pssm-ID: 153235 [Multi-domain] Cd Length: 221 Bit Score: 46.40 E-value: 2.22e-06
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| GATase1_AraC_ArgR_like | cd03136 | AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ... |
36-186 | 3.82e-05 | ||||
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to the Pseudomonas aeruginosa ArgR regulator. ArgR functions in the control of expression of certain genes of arginine biosynthesis and catabolism. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in some sequences in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Pssm-ID: 153230 [Multi-domain] Cd Length: 185 Bit Score: 42.57 E-value: 3.82e-05
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| GATase1_AraC_2 | cd03138 | AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ... |
45-182 | 2.27e-04 | ||||
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Pssm-ID: 153232 [Multi-domain] Cd Length: 195 Bit Score: 40.32 E-value: 2.27e-04
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| GATase1_AraC_1 | cd03137 | AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ... |
44-188 | 3.19e-04 | ||||
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Pssm-ID: 153231 [Multi-domain] Cd Length: 187 Bit Score: 39.79 E-value: 3.19e-04
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| PRK11780 | PRK11780 | isoprenoid biosynthesis glyoxalase ElbB; |
58-110 | 8.67e-04 | ||||
isoprenoid biosynthesis glyoxalase ElbB; Pssm-ID: 236980 Cd Length: 217 Bit Score: 38.61 E-value: 8.67e-04
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| GATase1_CobQ | cd01750 | Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
65-107 | 4.61e-03 | ||||
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ. Pssm-ID: 153221 [Multi-domain] Cd Length: 194 Bit Score: 36.45 E-value: 4.61e-03
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