5'-adenylylsulfate reductase 3, chloroplastic isoform X2 [Brassica rapa]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| APS_reduc super family | cl36649 | 5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ... |
1-468 | 0e+00 | |||||||
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism] The actual alignment was detected with superfamily member TIGR00424: Pssm-ID: 273072 [Multi-domain] Cd Length: 463 Bit Score: 902.08 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||
| APS_reduc | TIGR00424 | 5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ... |
1-468 | 0e+00 | |||||||
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism] Pssm-ID: 273072 [Multi-domain] Cd Length: 463 Bit Score: 902.08 E-value: 0e+00
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| PLN02309 | PLN02309 | 5'-adenylylsulfate reductase |
20-468 | 0e+00 | |||||||
5'-adenylylsulfate reductase Pssm-ID: 215175 [Multi-domain] Cd Length: 457 Bit Score: 896.07 E-value: 0e+00
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| CysD | COG0175 | 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
92-325 | 2.84e-85 | |||||||
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis Pssm-ID: 439945 [Multi-domain] Cd Length: 232 Bit Score: 261.32 E-value: 2.84e-85
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| PAPS_reductase | cd23945 | Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
106-294 | 1.51e-74 | |||||||
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8) is part of the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). Pssm-ID: 467510 [Multi-domain] Cd Length: 183 Bit Score: 232.10 E-value: 1.51e-74
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| PAPS_reduct | pfam01507 | Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
121-301 | 2.75e-58 | |||||||
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase). Pssm-ID: 396201 [Multi-domain] Cd Length: 173 Bit Score: 189.81 E-value: 2.75e-58
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| Name | Accession | Description | Interval | E-value | |||||||
| APS_reduc | TIGR00424 | 5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ... |
1-468 | 0e+00 | |||||||
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism] Pssm-ID: 273072 [Multi-domain] Cd Length: 463 Bit Score: 902.08 E-value: 0e+00
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| PLN02309 | PLN02309 | 5'-adenylylsulfate reductase |
20-468 | 0e+00 | |||||||
5'-adenylylsulfate reductase Pssm-ID: 215175 [Multi-domain] Cd Length: 457 Bit Score: 896.07 E-value: 0e+00
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| PRK02090 | PRK02090 | phosphoadenylyl-sulfate reductase; |
92-331 | 1.02e-97 | |||||||
phosphoadenylyl-sulfate reductase; Pssm-ID: 234997 Cd Length: 241 Bit Score: 293.67 E-value: 1.02e-97
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| APS_reductase | TIGR02055 | thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ... |
126-325 | 1.78e-85 | |||||||
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified adenosine 5'-phosphosulfate (APS) reductase activity found in sulfate-assimilatory prokaryotes, thus separating it from the traditionally described phosphoadenosine 5'-phosphosulfate (PAPS) reductases found in bacteria and fungi. Homologous to PAPS reductase in enterobacteria, cyanobacteria, and yeast, APS reductase here clusters with, and demonstrates greater homology to plant APS reductase. Additionally, the presence of two conserved C-terminal motifs (CCXXRKXXPL _ SXGCXXCT) distinguishes APS substrate specificity and serves as a FeS cluster. [Central intermediary metabolism, Sulfur metabolism] Pssm-ID: 273945 Cd Length: 191 Bit Score: 260.47 E-value: 1.78e-85
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| CysD | COG0175 | 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
92-325 | 2.84e-85 | |||||||
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis Pssm-ID: 439945 [Multi-domain] Cd Length: 232 Bit Score: 261.32 E-value: 2.84e-85
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| PAPS_reductase | cd23945 | Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
106-294 | 1.51e-74 | |||||||
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8) is part of the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). Pssm-ID: 467510 [Multi-domain] Cd Length: 183 Bit Score: 232.10 E-value: 1.51e-74
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| PDI_a_APS_reductase | cd02993 | PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ... |
356-464 | 2.51e-64 | |||||||
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -> C-terminal TRX domain -> N-terminal reductase domain -> APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly. Pssm-ID: 239291 [Multi-domain] Cd Length: 109 Bit Score: 203.07 E-value: 2.51e-64
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| PAPS_reduct | pfam01507 | Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
121-301 | 2.75e-58 | |||||||
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase). Pssm-ID: 396201 [Multi-domain] Cd Length: 173 Bit Score: 189.81 E-value: 2.75e-58
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| cysH | TIGR00434 | phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
106-326 | 1.74e-43 | |||||||
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of inorganic sulfate, is designated cysH in Bacteria and MET16 in Saccharomyces cerevisiae. Synonyms include phosphoadenosine phosphosulfate reductase, PAPS reductase, and PAPS reductase, thioredoxin-dependent. In a reaction requiring reduced thioredoxin and NADPH, it converts 3(prime)-phosphoadenylylsulfate (PAPS) to sulfite and adenosine 3(prime),5(prime) diphosphate (PAP). A related family of plant enzymes, scoring below the trusted cutoff, differs in having a thioredoxin-like C-terminal domain, not requiring thioredoxin, and in having a preference for 5(prime)-adenylylsulfate (APS) over PAPS. [Central intermediary metabolism, Sulfur metabolism] Pssm-ID: 129526 Cd Length: 212 Bit Score: 152.25 E-value: 1.74e-43
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| PDI_a_family | cd02961 | Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ... |
367-464 | 6.56e-22 | |||||||
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29. Pssm-ID: 239259 [Multi-domain] Cd Length: 101 Bit Score: 89.98 E-value: 6.56e-22
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| PDI_a_PDI_a'_C | cd02995 | PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ... |
381-464 | 7.11e-17 | |||||||
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones. Pssm-ID: 239293 [Multi-domain] Cd Length: 104 Bit Score: 76.06 E-value: 7.11e-17
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| PDI_a_ERp38 | cd02998 | PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ... |
357-464 | 8.17e-17 | |||||||
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica. Pssm-ID: 239296 [Multi-domain] Cd Length: 105 Bit Score: 75.75 E-value: 8.17e-17
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| PDI_a_ERdj5_C | cd03004 | PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ... |
358-464 | 7.83e-16 | |||||||
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus. Pssm-ID: 239302 [Multi-domain] Cd Length: 104 Bit Score: 73.09 E-value: 7.83e-16
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| PAPS_reductase-like_YbdN | cd23947 | uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
107-300 | 1.73e-14 | |||||||
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to Escherichia coli YbdN; This subgroup contains Escherichia coli YbdN and other phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8)-like proteins. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). Pssm-ID: 467512 [Multi-domain] Cd Length: 206 Bit Score: 72.04 E-value: 1.73e-14
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| ER_PDI_fam | TIGR01130 | protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ... |
381-465 | 1.04e-11 | |||||||
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs). Pssm-ID: 273457 [Multi-domain] Cd Length: 462 Bit Score: 66.62 E-value: 1.04e-11
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| PDI_a_P5 | cd03001 | PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ... |
374-463 | 4.77e-11 | |||||||
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain. Pssm-ID: 239299 [Multi-domain] Cd Length: 103 Bit Score: 59.22 E-value: 4.77e-11
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| PTZ00102 | PTZ00102 | disulphide isomerase; Provisional |
383-465 | 2.47e-10 | |||||||
disulphide isomerase; Provisional Pssm-ID: 240266 [Multi-domain] Cd Length: 477 Bit Score: 62.46 E-value: 2.47e-10
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| CnoX | COG3118 | Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ... |
371-440 | 7.17e-10 | |||||||
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442352 [Multi-domain] Cd Length: 105 Bit Score: 55.98 E-value: 7.17e-10
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| PDI_a_ERp46 | cd03005 | PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ... |
381-464 | 1.64e-09 | |||||||
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident protein containing three redox active TRX domains. Yeast complementation studies show that ERp46 can substitute for protein disulfide isomerase (PDI) function in vivo. It has been detected in many tissues, however, transcript and protein levels do not correlate in all tissues, suggesting regulation at a posttranscriptional level. An identical protein, named endoPDI, has been identified as an endothelial PDI that is highly expressed in the endothelium of tumors and hypoxic lesions. It has a protective effect on cells exposed to hypoxia. Pssm-ID: 239303 [Multi-domain] Cd Length: 102 Bit Score: 54.98 E-value: 1.64e-09
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| PDI_a_TMX3 | cd03000 | PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ... |
372-467 | 5.94e-09 | |||||||
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase. Pssm-ID: 239298 [Multi-domain] Cd Length: 104 Bit Score: 53.61 E-value: 5.94e-09
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| Thioredoxin | pfam00085 | Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
379-465 | 3.47e-08 | |||||||
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise. Pssm-ID: 395038 [Multi-domain] Cd Length: 103 Bit Score: 51.08 E-value: 3.47e-08
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| PTZ00102 | PTZ00102 | disulphide isomerase; Provisional |
353-464 | 4.79e-08 | |||||||
disulphide isomerase; Provisional Pssm-ID: 240266 [Multi-domain] Cd Length: 477 Bit Score: 55.14 E-value: 4.79e-08
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| PTZ00443 | PTZ00443 | Thioredoxin domain-containing protein; Provisional |
379-463 | 5.07e-07 | |||||||
Thioredoxin domain-containing protein; Provisional Pssm-ID: 185622 [Multi-domain] Cd Length: 224 Bit Score: 50.39 E-value: 5.07e-07
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| TRX_superfamily | cd01659 | Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ... |
380-440 | 8.88e-07 | |||||||
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: 46.15 E-value: 8.88e-07
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| PDI_a_PDIR | cd02997 | PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ... |
357-464 | 1.03e-06 | |||||||
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity. Pssm-ID: 239295 [Multi-domain] Cd Length: 104 Bit Score: 46.93 E-value: 1.03e-06
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| TRX_family | cd02947 | TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ... |
380-440 | 1.15e-06 | |||||||
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins. Pssm-ID: 239245 [Multi-domain] Cd Length: 93 Bit Score: 46.40 E-value: 1.15e-06
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| PDI_a_MPD1_like | cd03002 | PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ... |
372-442 | 1.27e-06 | |||||||
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity. Pssm-ID: 239300 [Multi-domain] Cd Length: 109 Bit Score: 46.97 E-value: 1.27e-06
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| PRK13794 | PRK13794 | hypothetical protein; Provisional |
91-298 | 1.93e-06 | |||||||
hypothetical protein; Provisional Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 50.05 E-value: 1.93e-06
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| PDI_a_TMX | cd02994 | PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ... |
379-414 | 2.39e-06 | |||||||
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC. Pssm-ID: 239292 [Multi-domain] Cd Length: 101 Bit Score: 45.83 E-value: 2.39e-06
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| ER_PDI_fam | TIGR01130 | protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ... |
356-465 | 5.58e-06 | |||||||
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs). Pssm-ID: 273457 [Multi-domain] Cd Length: 462 Bit Score: 48.52 E-value: 5.58e-06
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| thioredoxin | TIGR01068 | thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ... |
380-442 | 6.67e-06 | |||||||
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport] Pssm-ID: 200072 [Multi-domain] Cd Length: 101 Bit Score: 44.59 E-value: 6.67e-06
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| TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
373-443 | 1.24e-05 | |||||||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 45.07 E-value: 1.24e-05
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| FAD_synthase | cd23948 | FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
107-294 | 1.45e-05 | |||||||
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases. Pssm-ID: 467513 [Multi-domain] Cd Length: 179 Bit Score: 45.59 E-value: 1.45e-05
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| PRK13795 | PRK13795 | hypothetical protein; Provisional |
115-298 | 2.29e-05 | |||||||
hypothetical protein; Provisional Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 46.91 E-value: 2.29e-05
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| Thioredoxin_2 | pfam13098 | Thioredoxin-like domain; |
380-443 | 6.90e-05 | |||||||
Thioredoxin-like domain; Pssm-ID: 379034 [Multi-domain] Cd Length: 103 Bit Score: 42.03 E-value: 6.90e-05
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| Sulfate_adenylyltransferase_2 | cd23946 | Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
99-288 | 9.91e-05 | |||||||
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in the sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN, coupled to ATP hydrolysis by CysD. CysD belongs to the ATP pyrophosphatase (ATP PPase) family of proteins, members of which include PAPS reductase, GMP synthetase, asparagine synthetase, and NAD(+) synthetase. This subunit is responsible for directly forming APS under control of the G protein. A modified version of the P loop (PP-loop), the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Pssm-ID: 467511 Cd Length: 214 Bit Score: 43.64 E-value: 9.91e-05
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| PDI_a_ERp44 | cd02996 | PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ... |
357-464 | 1.19e-04 | |||||||
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol. Pssm-ID: 239294 [Multi-domain] Cd Length: 108 Bit Score: 41.22 E-value: 1.19e-04
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| PDI_a_ERp44_like | cd02999 | PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ... |
370-463 | 1.64e-04 | |||||||
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER. Pssm-ID: 239297 [Multi-domain] Cd Length: 100 Bit Score: 40.80 E-value: 1.64e-04
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| PDI_a_ERdj5_N | cd03003 | PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ... |
358-463 | 2.14e-04 | |||||||
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Pssm-ID: 239301 [Multi-domain] Cd Length: 101 Bit Score: 40.59 E-value: 2.14e-04
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| TMX2 | cd02962 | TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ... |
354-468 | 8.60e-04 | |||||||
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related transmembrane protein, identified and characterized through the cloning of its cDNA from a human fetal library. It contains a TRX domain but the redox active CXXC motif is replaced with SXXC. Sequence analysis predicts that TMX2 may be a Type I membrane protein, with its C-terminal half protruding on the luminal side of the endoplasmic reticulum (ER). In addition to the TRX domain, transmembrane region and ER-retention signal, TMX2 also contains a Myb DNA-binding domain repeat signature and a dileucine motif in the tail. Pssm-ID: 239260 [Multi-domain] Cd Length: 152 Bit Score: 39.67 E-value: 8.60e-04
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| PRK08557 | PRK08557 | hypothetical protein; Provisional |
91-302 | 2.35e-03 | |||||||
hypothetical protein; Provisional Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 40.12 E-value: 2.35e-03
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| Bcp | COG1225 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
380-412 | 2.67e-03 | |||||||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 37.92 E-value: 2.67e-03
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| Phd_like | cd02957 | Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ... |
376-440 | 5.71e-03 | |||||||
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as cytosolic regulators of G protein functions. Phd and PhLPs specifically bind G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane and impeding G protein-mediated signal transduction by inhibiting the formation of a functional G protein trimer (G protein alphabetagamma). Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain. Also included in this family is a PhLP characterized as a viral inhibitor of apoptosis (IAP)-associated factor, named VIAF, that functions in caspase activation during apoptosis. Pssm-ID: 239255 [Multi-domain] Cd Length: 113 Bit Score: 36.76 E-value: 5.71e-03
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