hypothetical protein AMS58_00385 [Pseudoalteromonas porphyrae]
Protein Classification
glutaredoxin family protein( domain architecture ID 10002164)
glutaredoxin (GRX) family protein similar to GRX, a glutathione dependent reductase that catalyzes the reduction of disulfides in target proteins using an active site dithiol, present in a CXXC motif
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| GrxC | COG0695 | Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
6-77 | 6.26e-21 | ||
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; : Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 77.93 E-value: 6.26e-21
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| Name | Accession | Description | Interval | E-value | ||
| GrxC | COG0695 | Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
6-77 | 6.26e-21 | ||
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 77.93 E-value: 6.26e-21
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| NrdH | cd02976 | NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
6-77 | 3.19e-19 | ||
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein. Pssm-ID: 239274 [Multi-domain] Cd Length: 73 Bit Score: 73.80 E-value: 3.19e-19
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| GlrX_YruB | TIGR02196 | Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ... |
6-68 | 1.30e-14 | ||
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system. Pssm-ID: 274027 [Multi-domain] Cd Length: 74 Bit Score: 62.01 E-value: 1.30e-14
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| Glutaredoxin | pfam00462 | Glutaredoxin; |
7-60 | 2.99e-12 | ||
Glutaredoxin; Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 55.59 E-value: 2.99e-12
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| Uxx_star | NF041212 | Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ... |
7-52 | 3.90e-10 | ||
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature. Pssm-ID: 469116 [Multi-domain] Cd Length: 70 Bit Score: 50.54 E-value: 3.90e-10
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| spxA | PRK13344 | transcriptional regulator Spx; Reviewed |
7-41 | 8.50e-05 | ||
transcriptional regulator Spx; Reviewed Pssm-ID: 183988 Cd Length: 132 Bit Score: 38.02 E-value: 8.50e-05
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| Name | Accession | Description | Interval | E-value | ||
| GrxC | COG0695 | Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
6-77 | 6.26e-21 | ||
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 77.93 E-value: 6.26e-21
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| NrdH | cd02976 | NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
6-77 | 3.19e-19 | ||
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein. Pssm-ID: 239274 [Multi-domain] Cd Length: 73 Bit Score: 73.80 E-value: 3.19e-19
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| GlrX_YruB | TIGR02196 | Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ... |
6-68 | 1.30e-14 | ||
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system. Pssm-ID: 274027 [Multi-domain] Cd Length: 74 Bit Score: 62.01 E-value: 1.30e-14
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| Glutaredoxin | pfam00462 | Glutaredoxin; |
7-60 | 2.99e-12 | ||
Glutaredoxin; Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 55.59 E-value: 2.99e-12
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| GRX_family | cd02066 | Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ... |
6-68 | 1.30e-10 | ||
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family. Pssm-ID: 239017 [Multi-domain] Cd Length: 72 Bit Score: 51.70 E-value: 1.30e-10
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| Uxx_star | NF041212 | Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ... |
7-52 | 3.90e-10 | ||
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature. Pssm-ID: 469116 [Multi-domain] Cd Length: 70 Bit Score: 50.54 E-value: 3.90e-10
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| GRX_GRXb_1_3_like | cd03418 | Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ... |
6-52 | 5.15e-10 | ||
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3, which are members of this subfamily. Pssm-ID: 239510 [Multi-domain] Cd Length: 75 Bit Score: 50.28 E-value: 5.15e-10
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| ArsC_Spx | cd03032 | Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ... |
6-59 | 8.32e-08 | ||
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding protein present in bacilli and some mollicutes. It inhibits transcription by binding to the C-terminal domain of the alpha subunit of RNAP, disrupting complex formation between RNAP and certain transcriptional activator proteins like ResD and ComA. In response to oxidative stress, Spx can also activate transcription, making it a general regulator that exerts both positive and negative control over transcription initiation. Spx has been shown to exert redox-sensitive transcriptional control over genes like trxA (TRX) and trxB (TRX reductase), genes that function in thiol homeostasis. This redox-sensitive activity is dependent on the presence of a CXXC motif, present in some members of the Spx subfamily, that acts as a thiol/disulfide switch. Spx has also been shown to repress genes in a sulfate-dependent manner independent of the presence of the CXXC motif. Pssm-ID: 239330 Cd Length: 115 Bit Score: 45.70 E-value: 8.32e-08
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| GRX_DEP | cd03027 | Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ... |
6-67 | 1.55e-07 | ||
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of uncharacterized proteins containing a GRX domain and additional domains DEP and DUF547, both of which have unknown functions. GRX is a glutathione (GSH) dependent reductase containing a redox active CXXC motif in a TRX fold. It has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. By altering the redox state of target proteins, GRX is involved in many cellular functions. Pssm-ID: 239325 [Multi-domain] Cd Length: 73 Bit Score: 43.94 E-value: 1.55e-07
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| GlrX_actino | TIGR02200 | Glutaredoxin-like protein; This family of glutaredoxin-like proteins is limited to the ... |
6-43 | 2.55e-07 | ||
Glutaredoxin-like protein; This family of glutaredoxin-like proteins is limited to the Actinobacteria and contains the conserved CxxC motif. Pssm-ID: 131255 [Multi-domain] Cd Length: 77 Bit Score: 43.68 E-value: 2.55e-07
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| ArsC_family | cd02977 | Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins ... |
7-55 | 2.71e-06 | ||
Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins including the transcriptional regulator, Spx. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione (GSH) via glutaredoxin (GRX), through a single catalytic cysteine. This family of predominantly bacterial enzymes is unrelated to two other families of arsenate reductases which show similarity to low-molecular-weight acid phosphatases and phosphotyrosyl phosphatases. Spx is a general regulator that exerts negative and positive control over transcription initiation by binding to the C-terminal domain of the alpha subunit of RNA polymerase. Pssm-ID: 239275 Cd Length: 105 Bit Score: 41.71 E-value: 2.71e-06
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| ArsC | pfam03960 | ArsC family; This family is related to glutaredoxins pfam00462. |
15-59 | 3.10e-06 | ||
ArsC family; This family is related to glutaredoxins pfam00462. Pssm-ID: 427617 Cd Length: 109 Bit Score: 41.43 E-value: 3.10e-06
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| COG4545 | COG4545 | Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones]; |
5-47 | 3.99e-06 | ||
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443610 Cd Length: 87 Bit Score: 40.67 E-value: 3.99e-06
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| spxA | PRK13344 | transcriptional regulator Spx; Reviewed |
7-41 | 8.50e-05 | ||
transcriptional regulator Spx; Reviewed Pssm-ID: 183988 Cd Length: 132 Bit Score: 38.02 E-value: 8.50e-05
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| PRK10638 | PRK10638 | glutaredoxin 3; Provisional |
6-61 | 1.45e-04 | ||
glutaredoxin 3; Provisional Pssm-ID: 182607 [Multi-domain] Cd Length: 83 Bit Score: 36.72 E-value: 1.45e-04
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| GRX_hybridPRX5 | cd03029 | Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ... |
7-39 | 2.98e-04 | ||
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing peroxiredoxin (PRX) and GRX domains, which is found in some pathogenic bacteria and cyanobacteria. PRXs are thiol-specific antioxidant (TSA) proteins that 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. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins. PRX-GRX hybrid proteins from Haemophilus influenza and Neisseria meningitis exhibit GSH-dependent peroxidase activity. The flow of reducing equivalents in the catalytic cycle of the hybrid protein goes from NADPH -> GSH reductase -> GSH -> GRX domain of hybrid -> PRX domain of hybrid -> peroxide substrate. Pssm-ID: 239327 [Multi-domain] Cd Length: 72 Bit Score: 35.57 E-value: 2.98e-04
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| GRX_PICOT_like | cd03028 | Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ... |
15-47 | 1.57e-03 | ||
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum. Pssm-ID: 239326 Cd Length: 90 Bit Score: 34.01 E-value: 1.57e-03
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| arsC_related | TIGR01617 | transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins ... |
7-59 | 1.77e-03 | ||
transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins within the larger set covered by pfam03960. That larger family includes a glutaredoxin-dependent arsenate reductase (TIGR00014). Characterized members of this family include Spx and MgsR from Bacillus subtili. Spx is a global regulator for response to thiol-specific oxidative stress. It interacts with RNA polymerase. MgsR (modulator of the general stress response, also called YqgZ) provides a second level of regulation for more than a third of the proteins in the B. subtilis general stress regulon controlled by Sigma-B. [Regulatory functions, DNA interactions] Pssm-ID: 273720 Cd Length: 117 Bit Score: 34.33 E-value: 1.77e-03
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| TRX_superfamily | cd01659 | Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ... |
7-69 | 2.21e-03 | ||
Thioredoxin (TRX) superfamily; 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 TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others. Pssm-ID: 238829 [Multi-domain] Cd Length: 69 Bit Score: 33.44 E-value: 2.21e-03
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| spxA | PRK01655 | transcriptional regulator Spx; Reviewed |
7-59 | 2.31e-03 | ||
transcriptional regulator Spx; Reviewed Pssm-ID: 179316 Cd Length: 131 Bit Score: 34.28 E-value: 2.31e-03
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| ArsC | COG1393 | Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ... |
6-54 | 3.72e-03 | ||
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and metabolism]; Pssm-ID: 441003 Cd Length: 115 Bit Score: 33.53 E-value: 3.72e-03
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| ArsC_like | cd03036 | Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a ... |
7-48 | 4.55e-03 | ||
Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a CXXC motif with similarity to thioredoxin (TRX)-fold arsenic reductases, ArsC. Proteins containing a redox active CXXC motif like TRX and glutaredoxin (GRX) function as protein disulfide oxidoreductases, altering the redox state of target proteins via the reversible oxidation of the active site dithiol. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione via GRX, through a single catalytic cysteine. Pssm-ID: 239334 Cd Length: 111 Bit Score: 33.37 E-value: 4.55e-03
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| GST_N_mPGES2 | cd03040 | GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a ... |
6-83 | 4.76e-03 | ||
GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a membrane-anchored dimeric protein containing a CXXC motif which catalyzes the isomerization of PGH2 to PGE2. Unlike cytosolic PGE synthase (cPGES) and microsomal PGES Type 1 (mPGES1), mPGES2 does not require glutathione (GSH) for its activity, although its catalytic rate is increased two- to four-fold in the presence of DTT, GSH or other thiol compounds. PGE2 is widely distributed in various tissues and is implicated in the sleep/wake cycle, relaxation/contraction of smooth muscle, excretion of sodium ions, maintenance of body temperature and mediation of inflammation. mPGES2 contains an N-terminal hydrophobic domain which is membrane associated, and a C-terminal soluble domain with a GST-like structure. Pssm-ID: 239338 Cd Length: 77 Bit Score: 32.77 E-value: 4.76e-03
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