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hypothetical protein HMPREF9695_01357 [Afipia broomeae ATCC 49717]
peroxiredoxin-like family protein( domain architecture ID 10121943)
peroxiredoxin (PRX)-like family protein containing a CXXC motif, with the second cysteine in the motif corresponding to the peroxidatic cysteine of PRX, however, it does not contain the other two residues of the catalytic triad of PRXs; similar to vertebrate peroxiredoxin-like 2A, 2B (prostamide/prostaglandin F synthase) and 2C
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
PRX_like2 | cd02970 | Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ... |
68-214 | 1.47e-28 | |||
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins. : Pssm-ID: 239268 [Multi-domain] Cd Length: 149 Bit Score: 105.13 E-value: 1.47e-28
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Name | Accession | Description | Interval | E-value | ||||
PRX_like2 | cd02970 | Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ... |
68-214 | 1.47e-28 | ||||
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins. Pssm-ID: 239268 [Multi-domain] Cd Length: 149 Bit Score: 105.13 E-value: 1.47e-28
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Bcp | COG1225 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
69-228 | 4.67e-20 | ||||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 82.61 E-value: 4.67e-20
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AhpC-TSA | pfam00578 | AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
65-210 | 5.49e-19 | ||||
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA). Pssm-ID: 425763 [Multi-domain] Cd Length: 124 Bit Score: 79.58 E-value: 5.49e-19
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SelL_rel_redox | NF040769 | SelL-related redox protein; Members of this family are related to the C-terminal region of ... |
67-228 | 4.61e-11 | ||||
SelL-related redox protein; Members of this family are related to the C-terminal region of selenoprotein L (SelL), found in many non-mammalian animals. But while SelL itself has a pair of selenocysteine (U) residues (e.g. XP_029705782.1), typically in the motif ULPU, this family is defined more broadly. Most members of the seed alignment for this HMM are bacterial proteins that have one or zero selenocysteine residues, and are shorter than SelU, although SelU members are also included. Pssm-ID: 468728 Cd Length: 172 Bit Score: 59.63 E-value: 4.61e-11
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bcp | PRK09437 | thioredoxin-dependent thiol peroxidase; Reviewed |
65-157 | 1.95e-03 | ||||
thioredoxin-dependent thiol peroxidase; Reviewed Pssm-ID: 181857 Cd Length: 154 Bit Score: 37.61 E-value: 1.95e-03
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Name | Accession | Description | Interval | E-value | ||||
PRX_like2 | cd02970 | Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ... |
68-214 | 1.47e-28 | ||||
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins. Pssm-ID: 239268 [Multi-domain] Cd Length: 149 Bit Score: 105.13 E-value: 1.47e-28
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Bcp | COG1225 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
69-228 | 4.67e-20 | ||||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 82.61 E-value: 4.67e-20
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AhpC-TSA | pfam00578 | AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
65-210 | 5.49e-19 | ||||
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA). Pssm-ID: 425763 [Multi-domain] Cd Length: 124 Bit Score: 79.58 E-value: 5.49e-19
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Redoxin | pfam08534 | Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
65-215 | 4.64e-12 | ||||
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 61.62 E-value: 4.64e-12
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PRX_AhpE_like | cd03018 | Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ... |
63-228 | 6.73e-12 | ||||
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers. Pssm-ID: 239316 [Multi-domain] Cd Length: 149 Bit Score: 61.14 E-value: 6.73e-12
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SelL_rel_redox | NF040769 | SelL-related redox protein; Members of this family are related to the C-terminal region of ... |
67-228 | 4.61e-11 | ||||
SelL-related redox protein; Members of this family are related to the C-terminal region of selenoprotein L (SelL), found in many non-mammalian animals. But while SelL itself has a pair of selenocysteine (U) residues (e.g. XP_029705782.1), typically in the motif ULPU, this family is defined more broadly. Most members of the seed alignment for this HMM are bacterial proteins that have one or zero selenocysteine residues, and are shorter than SelU, although SelU members are also included. Pssm-ID: 468728 Cd Length: 172 Bit Score: 59.63 E-value: 4.61e-11
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PRX_like1 | cd02969 | Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ... |
66-161 | 1.93e-08 | ||||
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. Pssm-ID: 239267 [Multi-domain] Cd Length: 171 Bit Score: 52.24 E-value: 1.93e-08
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TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
65-231 | 5.37e-08 | ||||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 50.46 E-value: 5.37e-08
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TlpA_like_family | cd02966 | TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
71-212 | 9.02e-08 | ||||
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases. Pssm-ID: 239264 [Multi-domain] Cd Length: 116 Bit Score: 49.16 E-value: 9.02e-08
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SCO | cd02968 | SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ... |
68-148 | 2.99e-05 | ||||
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II. Pssm-ID: 239266 Cd Length: 142 Bit Score: 42.59 E-value: 2.99e-05
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bcp | PRK09437 | thioredoxin-dependent thiol peroxidase; Reviewed |
65-157 | 1.95e-03 | ||||
thioredoxin-dependent thiol peroxidase; Reviewed Pssm-ID: 181857 Cd Length: 154 Bit Score: 37.61 E-value: 1.95e-03
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Blast search parameters | ||||
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