low molecular weight phosphatase (LMWP) family protein similar to arsenate reductase that plays an important role in the reduction of intracellular arsenate to arsenite, an important step in arsenic detoxification
Low molecular weight phosphatase family; Low molecular weight phosphatases (LMWPs) are a group ...
1-131
3.41e-95
Low molecular weight phosphatase family; Low molecular weight phosphatases (LMWPs) are a group of small soluble enzymes that are characterized by a highly conserved active site motif (V/I)CXGNXCRS and share no sequence similarity with other types of protein tyrosine phosphatases (PTPs). This family includes protein tyrosine phosphatases, arginine phosphatases and arsenate reductases.
The actual alignment was detected with superfamily member PRK13530:
Pssm-ID: 469616 Cd Length: 133 Bit Score: 269.69 E-value: 3.41e-95
arsenate reductase (thioredoxin); This family describes the well-studied thioredoxin-dependent ...
6-128
3.75e-79
arsenate reductase (thioredoxin); This family describes the well-studied thioredoxin-dependent arsenate reductase of Staphylococcus aureaus plasmid pI258 and other mechanistically similar arsenate reductases. The mechanism involves an intramolecular disulfide bond cascade, and aligned members of this family have four absolutely conserved Cys residues. This group of arsenate reductases belongs to the low-molecular weight protein-tyrosine phosphatase family (pfam01451), as does a group of glutathione/glutaredoxin type arsenate reductases (TIGR02689). At least two other, non-homologous groups of arsenate reductases involved in arsenical resistance are also known. This enzyme reduces arsenate to arsenite, which may be more toxic but which is more easily exported. [Cellular processes, Detoxification]
Pssm-ID: 131738 Cd Length: 129 Bit Score: 229.28 E-value: 3.75e-79
Arsenate reductase of the LMWP family; Arsenate reductase plays an important role in the ...
6-128
4.13e-69
Arsenate reductase of the LMWP family; Arsenate reductase plays an important role in the reduction of intracellular arsenate to arsenite, an important step in arsenic detoxification. The reduction involves three different thiolate nucleophiles. In arsenate reductases of the LMWP family, reduction can be coupled with thioredoxin (Trx)/thioredoxin reductase (TrxR) or glutathione (GSH)/glutaredoxin (Grx).
Pssm-ID: 319973 Cd Length: 132 Bit Score: 203.83 E-value: 4.13e-69
arsenate reductase (thioredoxin); This family describes the well-studied thioredoxin-dependent ...
6-128
3.75e-79
arsenate reductase (thioredoxin); This family describes the well-studied thioredoxin-dependent arsenate reductase of Staphylococcus aureaus plasmid pI258 and other mechanistically similar arsenate reductases. The mechanism involves an intramolecular disulfide bond cascade, and aligned members of this family have four absolutely conserved Cys residues. This group of arsenate reductases belongs to the low-molecular weight protein-tyrosine phosphatase family (pfam01451), as does a group of glutathione/glutaredoxin type arsenate reductases (TIGR02689). At least two other, non-homologous groups of arsenate reductases involved in arsenical resistance are also known. This enzyme reduces arsenate to arsenite, which may be more toxic but which is more easily exported. [Cellular processes, Detoxification]
Pssm-ID: 131738 Cd Length: 129 Bit Score: 229.28 E-value: 3.75e-79
Arsenate reductase of the LMWP family; Arsenate reductase plays an important role in the ...
6-128
4.13e-69
Arsenate reductase of the LMWP family; Arsenate reductase plays an important role in the reduction of intracellular arsenate to arsenite, an important step in arsenic detoxification. The reduction involves three different thiolate nucleophiles. In arsenate reductases of the LMWP family, reduction can be coupled with thioredoxin (Trx)/thioredoxin reductase (TrxR) or glutathione (GSH)/glutaredoxin (Grx).
Pssm-ID: 319973 Cd Length: 132 Bit Score: 203.83 E-value: 4.13e-69
Low molecular weight phosphatase family; Low molecular weight phosphatases (LMWPs) are a group ...
6-129
3.71e-43
Low molecular weight phosphatase family; Low molecular weight phosphatases (LMWPs) are a group of small soluble enzymes that are characterized by a highly conserved active site motif (V/I)CXGNXCRS and share no sequence similarity with other types of protein tyrosine phosphatases (PTPs). This family includes protein tyrosine phosphatases, arginine phosphatases and arsenate reductases.
Pssm-ID: 319970 Cd Length: 137 Bit Score: 138.39 E-value: 3.71e-43
low molecular weight protein arginine phosphatase; Low molecular weight protein arginine ...
4-126
9.11e-27
low molecular weight protein arginine phosphatase; Low molecular weight protein arginine phosphatases are part of the low molecular weight phosphatase (LMWP) family. They share a highly conserved active site motif (V/I)CXGNTCRS. It has been shown that the conserved threonine, which in many LMWPTPs is an isoleucine, confers specificity to phosphoarginine over phosphotyrosine.
Pssm-ID: 319972 Cd Length: 142 Bit Score: 96.73 E-value: 9.11e-27
Low molecular weight protein tyrosine phosphatase; Low molecular weight protein tyrosine ...
4-129
7.51e-14
Low molecular weight protein tyrosine phosphatase; Low molecular weight protein tyrosine phosphatases (LMW-PTP) are a family of small soluble single-domain enzymes that are characterized by a highly conserved active site motif (V/I)CXGNXCRS and share no sequence similarity with other types of protein tyrosine phosphatases (PTPs). LMW-PTPs play important roles in many biological processes and are widely distributed in prokaryotes and eukaryotes.
Pssm-ID: 319971 Cd Length: 147 Bit Score: 63.61 E-value: 7.51e-14
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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