peroxiredoxin-5, mitochondrial isoform c precursor [Homo sapiens]
Protein Classification
thioredoxin domain-containing protein( domain architecture ID 144)
thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Thioredoxin_like super family | cl00388 | Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ... |
57-123 | 1.16e-21 | ||
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others. The actual alignment was detected with superfamily member cd03013: Pssm-ID: 469754 [Multi-domain] Cd Length: 155 Bit Score: 83.77 E-value: 1.16e-21
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| Name | Accession | Description | Interval | E-value | ||
| PRX5_like | cd03013 | Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ... |
57-123 | 1.16e-21 | ||
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs. Pssm-ID: 239311 [Multi-domain] Cd Length: 155 Bit Score: 83.77 E-value: 1.16e-21
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| AHP1 | COG0678 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
57-125 | 9.12e-14 | ||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440442 Cd Length: 160 Bit Score: 63.57 E-value: 9.12e-14
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| Redoxin | pfam08534 | Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
46-111 | 2.45e-06 | ||
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 2.45e-06
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| Name | Accession | Description | Interval | E-value | ||
| PRX5_like | cd03013 | Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ... |
57-123 | 1.16e-21 | ||
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs. Pssm-ID: 239311 [Multi-domain] Cd Length: 155 Bit Score: 83.77 E-value: 1.16e-21
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| AHP1 | COG0678 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
57-125 | 9.12e-14 | ||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440442 Cd Length: 160 Bit Score: 63.57 E-value: 9.12e-14
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| Redoxin | pfam08534 | Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
46-111 | 2.45e-06 | ||
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 2.45e-06
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