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TPR repeat-containing thioredoxin TDX [Oryza sativa Japonica Group]
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
TRX_family | cd02947 | TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ... |
217-312 | 1.40e-29 | |||
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: 108.41 E-value: 1.40e-29
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NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
48-148 | 2.69e-20 | |||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; : Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 87.66 E-value: 2.69e-20
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Name | Accession | Description | Interval | E-value | |||
TRX_family | cd02947 | TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ... |
217-312 | 1.40e-29 | |||
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: 108.41 E-value: 1.40e-29
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CnoX | COG3118 | Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ... |
230-314 | 8.76e-24 | |||
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: 93.35 E-value: 8.76e-24
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Thioredoxin | pfam00085 | Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
210-312 | 1.53e-23 | |||
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: 92.68 E-value: 1.53e-23
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PTZ00051 | PTZ00051 | thioredoxin; Provisional |
222-308 | 1.44e-21 | |||
thioredoxin; Provisional Pssm-ID: 173347 [Multi-domain] Cd Length: 98 Bit Score: 87.24 E-value: 1.44e-21
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NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
48-148 | 2.69e-20 | |||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 87.66 E-value: 2.69e-20
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thioredoxin | TIGR01068 | thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ... |
215-314 | 2.31e-19 | |||
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: 81.57 E-value: 2.31e-19
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PLN03088 | PLN03088 | SGT1, suppressor of G2 allele of SKP1; Provisional |
56-191 | 7.92e-09 | |||
SGT1, suppressor of G2 allele of SKP1; Provisional Pssm-ID: 215568 [Multi-domain] Cd Length: 356 Bit Score: 55.95 E-value: 7.92e-09
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3a0801s09 | TIGR00990 | mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ... |
56-150 | 2.00e-07 | |||
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines] Pssm-ID: 273380 [Multi-domain] Cd Length: 615 Bit Score: 52.29 E-value: 2.00e-07
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TPR_11 | pfam13414 | TPR repeat; |
61-96 | 2.37e-04 | |||
TPR repeat; Pssm-ID: 315977 [Multi-domain] Cd Length: 42 Bit Score: 38.22 E-value: 2.37e-04
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TPR | smart00028 | Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
50-82 | 2.93e-03 | |||
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism. Pssm-ID: 197478 [Multi-domain] Cd Length: 34 Bit Score: 34.73 E-value: 2.93e-03
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Name | Accession | Description | Interval | E-value | |||
TRX_family | cd02947 | TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ... |
217-312 | 1.40e-29 | |||
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: 108.41 E-value: 1.40e-29
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CnoX | COG3118 | Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ... |
230-314 | 8.76e-24 | |||
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: 93.35 E-value: 8.76e-24
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Thioredoxin | pfam00085 | Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
210-312 | 1.53e-23 | |||
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: 92.68 E-value: 1.53e-23
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PTZ00051 | PTZ00051 | thioredoxin; Provisional |
222-308 | 1.44e-21 | |||
thioredoxin; Provisional Pssm-ID: 173347 [Multi-domain] Cd Length: 98 Bit Score: 87.24 E-value: 1.44e-21
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NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
48-148 | 2.69e-20 | |||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 87.66 E-value: 2.69e-20
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thioredoxin | TIGR01068 | thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ... |
215-314 | 2.31e-19 | |||
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: 81.57 E-value: 2.31e-19
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TRX_PICOT | cd02984 | TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ... |
227-312 | 4.50e-19 | |||
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; 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 contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. 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. Pssm-ID: 239282 [Multi-domain] Cd Length: 97 Bit Score: 80.39 E-value: 4.50e-19
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
46-187 | 9.81e-18 | |||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 80.82 E-value: 9.81e-18
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
48-150 | 1.53e-17 | |||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 80.44 E-value: 1.53e-17
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TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
219-314 | 2.19e-15 | |||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 71.64 E-value: 2.19e-15
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
48-192 | 4.89e-15 | |||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 73.50 E-value: 4.89e-15
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BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
41-151 | 5.37e-15 | |||
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 70.61 E-value: 5.37e-15
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BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
49-148 | 9.51e-15 | |||
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 70.22 E-value: 9.51e-15
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Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
48-148 | 8.39e-14 | |||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 71.95 E-value: 8.39e-14
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Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
64-148 | 7.20e-13 | |||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 68.87 E-value: 7.20e-13
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NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
61-148 | 1.23e-12 | |||
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 63.87 E-value: 1.23e-12
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TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
64-148 | 1.41e-12 | |||
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 64.60 E-value: 1.41e-12
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NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
75-148 | 1.11e-11 | |||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 63.40 E-value: 1.11e-11
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PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
60-150 | 2.13e-11 | |||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 59.41 E-value: 2.13e-11
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
77-150 | 2.31e-11 | |||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 62.72 E-value: 2.31e-11
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
63-150 | 4.91e-11 | |||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 62.05 E-value: 4.91e-11
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
41-177 | 6.45e-11 | |||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 61.67 E-value: 6.45e-11
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PRK10996 | PRK10996 | thioredoxin 2; Provisional |
205-302 | 7.97e-11 | |||
thioredoxin 2; Provisional Pssm-ID: 182889 [Multi-domain] Cd Length: 139 Bit Score: 58.93 E-value: 7.97e-11
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
43-148 | 1.21e-10 | |||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 60.90 E-value: 1.21e-10
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Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
48-152 | 2.33e-10 | |||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 61.16 E-value: 2.33e-10
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PDI_a_family | cd02961 | Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ... |
230-295 | 2.82e-10 | |||
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: 56.46 E-value: 2.82e-10
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NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
48-144 | 1.06e-09 | |||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 57.62 E-value: 1.06e-09
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TlpA_like_ScsD_MtbDsbE | cd03011 | TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ... |
220-301 | 1.20e-09 | |||
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c. Pssm-ID: 239309 [Multi-domain] Cd Length: 123 Bit Score: 55.38 E-value: 1.20e-09
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TRX_CDSP32 | cd02985 | TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ... |
214-315 | 3.60e-09 | |||
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed of two TRX domains, a C-terminal TRX domain which contains a redox active CXXC motif and an N-terminal TRX-like domain which contains an SXXS sequence instead of the redox active motif. CDSP32 is a stress-inducible TRX, i.e., it acts as a TRX by reducing protein disulfides and is induced by environmental and oxidative stress conditions. It plays a critical role in plastid defense against oxidative damage, a role related to its function as a physiological electron donor to BAS1, a plastidic 2-cys peroxiredoxin. Plants lacking CDSP32 exhibit decreased photosystem II photochemical efficiencies and chlorophyll retention compared to WT controls, as well as an increased proportion of BAS1 in its overoxidized monomeric form. Pssm-ID: 239283 Cd Length: 103 Bit Score: 53.64 E-value: 3.60e-09
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PLN03088 | PLN03088 | SGT1, suppressor of G2 allele of SKP1; Provisional |
56-191 | 7.92e-09 | |||
SGT1, suppressor of G2 allele of SKP1; Provisional Pssm-ID: 215568 [Multi-domain] Cd Length: 356 Bit Score: 55.95 E-value: 7.92e-09
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NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
68-151 | 9.12e-09 | |||
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 53.09 E-value: 9.12e-09
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TlpA_like_family | cd02966 | TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
228-301 | 1.40e-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: 52.24 E-value: 1.40e-08
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trxA | PRK09381 | thioredoxin TrxA; |
232-306 | 3.85e-08 | |||
thioredoxin TrxA; Pssm-ID: 181812 [Multi-domain] Cd Length: 109 Bit Score: 50.83 E-value: 3.85e-08
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PTZ00102 | PTZ00102 | disulphide isomerase; Provisional |
232-307 | 6.01e-08 | |||
disulphide isomerase; Provisional Pssm-ID: 240266 [Multi-domain] Cd Length: 477 Bit Score: 53.60 E-value: 6.01e-08
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3a0801s09 | TIGR00990 | mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ... |
56-150 | 2.00e-07 | |||
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines] Pssm-ID: 273380 [Multi-domain] Cd Length: 615 Bit Score: 52.29 E-value: 2.00e-07
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
56-176 | 2.24e-07 | |||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 51.27 E-value: 2.24e-07
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
62-148 | 2.66e-07 | |||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 50.88 E-value: 2.66e-07
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3a0801s09 | TIGR00990 | mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ... |
24-173 | 3.81e-07 | |||
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines] Pssm-ID: 273380 [Multi-domain] Cd Length: 615 Bit Score: 51.52 E-value: 3.81e-07
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DsbD | COG4232 | Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ... |
212-299 | 3.99e-07 | |||
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443376 [Multi-domain] Cd Length: 416 Bit Score: 50.96 E-value: 3.99e-07
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TRX_superfamily | cd01659 | Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ... |
234-296 | 4.02e-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: 46.54 E-value: 4.02e-07
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BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
84-151 | 1.08e-06 | |||
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 47.49 E-value: 1.08e-06
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
63-150 | 1.20e-06 | |||
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator. Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 50.08 E-value: 1.20e-06
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TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
59-184 | 1.40e-06 | |||
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 47.26 E-value: 1.40e-06
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
43-148 | 1.48e-06 | |||
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator. Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 49.70 E-value: 1.48e-06
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
48-184 | 2.41e-06 | |||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 48.08 E-value: 2.41e-06
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Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
66-150 | 3.65e-06 | |||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 48.45 E-value: 3.65e-06
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TryX_like_family | cd02964 | Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ... |
225-271 | 3.85e-06 | |||
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX. Pssm-ID: 239262 [Multi-domain] Cd Length: 132 Bit Score: 45.68 E-value: 3.85e-06
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TRX_NDPK | cd02948 | TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ... |
232-314 | 3.90e-06 | |||
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are fusion proteins which contain one redox active TRX domain containing a CXXC motif and three NDPK domains, and are characterized as intermediate chains (ICs) of axonemal outer arm dynein. Dyneins are molecular motors that generate force against microtubules to produce cellular movement, and are divided into two classes: axonemal and cytoplasmic. They are supramolecular complexes consisting of three protein groups classified according to size: dynein heavy, intermediate and light chains. Axonemal dyneins form two structures, the inner and outer arms, which are attached to doublet microtubules throughout the cilia and flagella. The human homolog is the sperm-specific Sptrx-2, presumed to be a component of the human sperm axoneme architecture. Included in this group is another human protein, TRX-like protein 2, a smaller fusion protein containing one TRX and one NDPK domain, which is also associated with microtubular structures. The other members of this group are hypothetical insect proteins containing a TRX domain and outer arm dynein light chains (14 and 16kDa) of Chlamydomonas reinhardtii. Using standard assays, the fusion proteins have shown no TRX enzymatic activity. Pssm-ID: 239246 [Multi-domain] Cd Length: 102 Bit Score: 44.63 E-value: 3.90e-06
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DsbDgamma | cd02953 | DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ... |
222-300 | 6.10e-06 | |||
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes. Pssm-ID: 239251 [Multi-domain] Cd Length: 104 Bit Score: 44.13 E-value: 6.10e-06
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SoxW | COG2143 | Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ... |
219-304 | 6.80e-06 | |||
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441746 [Multi-domain] Cd Length: 146 Bit Score: 45.28 E-value: 6.80e-06
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TryX_like_TryX_NRX | cd03009 | Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ... |
227-271 | 1.08e-05 | |||
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors. Pssm-ID: 239307 [Multi-domain] Cd Length: 131 Bit Score: 44.20 E-value: 1.08e-05
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PDI_a_ERp46 | cd03005 | PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ... |
237-302 | 1.28e-05 | |||
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: 43.43 E-value: 1.28e-05
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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' ... |
233-294 | 1.62e-05 | |||
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: 42.93 E-value: 1.62e-05
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Bcp | COG1225 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
228-302 | 1.89e-05 | |||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 43.70 E-value: 1.89e-05
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ybbN | cd02956 | ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ... |
228-302 | 1.90e-05 | |||
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria. Pssm-ID: 239254 [Multi-domain] Cd Length: 96 Bit Score: 42.64 E-value: 1.90e-05
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TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
55-115 | 2.30e-05 | |||
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 43.80 E-value: 2.30e-05
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PDI_a_ERp38 | cd02998 | PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ... |
237-295 | 4.15e-05 | |||
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: 41.85 E-value: 4.15e-05
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PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
93-179 | 4.52e-05 | |||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 41.69 E-value: 4.52e-05
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TRX_NTR | cd02949 | TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ... |
231-301 | 4.66e-05 | |||
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found only in oxygenic photosynthetic organisms containing both TRX and NTR domains. The TRX domain functions as a protein disulfide reductase via the reversible oxidation of an active center dithiol present in a CXXC motif, while the NTR domain functions as a reductant to oxidized TRX. The fusion protein is bifunctional, showing both TRX and NTR activities, but it is not an independent NTR/TRX system. In plants, the protein is found exclusively in shoots and mature leaves and is localized in the chloroplast. It is involved in plant protection against oxidative stress. Pssm-ID: 239247 [Multi-domain] Cd Length: 97 Bit Score: 41.72 E-value: 4.66e-05
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CpoB | COG1729 | Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
58-146 | 7.28e-05 | |||
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 441335 [Multi-domain] Cd Length: 113 Bit Score: 41.52 E-value: 7.28e-05
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PDI_a_ERp44 | cd02996 | PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ... |
208-293 | 7.67e-05 | |||
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: 7.67e-05
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Thioredoxin_8 | pfam13905 | Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
231-296 | 1.02e-04 | |||
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Pssm-ID: 464033 [Multi-domain] Cd Length: 95 Bit Score: 40.75 E-value: 1.02e-04
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TxlA | cd02950 | TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ... |
234-301 | 1.12e-04 | |||
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport. Pssm-ID: 239248 [Multi-domain] Cd Length: 142 Bit Score: 41.55 E-value: 1.12e-04
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NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
60-148 | 1.59e-04 | |||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 42.21 E-value: 1.59e-04
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Phd_like_TxnDC9 | cd02989 | Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ... |
255-306 | 2.05e-04 | |||
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; composed of predominantly uncharacterized eukaryotic proteins, containing a TRX-like domain without the redox active CXXC motif. The gene name for the human protein is TxnDC9. The two characterized members are described as Phd-like proteins, PLP1 of Saccharomyces cerevisiae and PhLP3 of Dictyostelium discoideum. Gene disruption experiments show that both PLP1 and PhLP3 are non-essential proteins. Unlike Phd and most Phd-like proteins, members of this group do not contain the Phd N-terminal helical domain which is implicated in binding to the G protein betagamma subunit. Pssm-ID: 239287 Cd Length: 113 Bit Score: 40.25 E-value: 2.05e-04
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TPR_11 | pfam13414 | TPR repeat; |
61-96 | 2.37e-04 | |||
TPR repeat; Pssm-ID: 315977 [Multi-domain] Cd Length: 42 Bit Score: 38.22 E-value: 2.37e-04
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TlpA_like_DsbE | cd03010 | TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ... |
231-302 | 3.91e-04 | |||
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c. Pssm-ID: 239308 [Multi-domain] Cd Length: 127 Bit Score: 39.48 E-value: 3.91e-04
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PDI_a_TMX | cd02994 | PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ... |
237-293 | 4.18e-04 | |||
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: 38.90 E-value: 4.18e-04
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
56-148 | 4.54e-04 | |||
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator. Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 41.99 E-value: 4.54e-04
|
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
57-148 | 4.66e-04 | |||
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator. Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 41.99 E-value: 4.66e-04
|
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TPR_1 | pfam00515 | Tetratricopeptide repeat; |
50-82 | 6.17e-04 | |||
Tetratricopeptide repeat; Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 36.63 E-value: 6.17e-04
|
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NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
64-118 | 1.19e-03 | |||
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 38.45 E-value: 1.19e-03
|
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ER_PDI_fam | TIGR01130 | protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ... |
232-294 | 1.44e-03 | |||
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: 40.04 E-value: 1.44e-03
|
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
56-150 | 1.48e-03 | |||
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator. Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 40.45 E-value: 1.48e-03
|
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
48-155 | 2.11e-03 | |||
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator. Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 39.68 E-value: 2.11e-03
|
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Phd_like | cd02957 | Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ... |
253-306 | 2.17e-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: 37.15 E-value: 2.17e-03
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TMX2 | cd02962 | TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ... |
237-298 | 2.42e-03 | |||
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: 37.75 E-value: 2.42e-03
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TPR_9 | pfam13371 | Tetratricopeptide repeat; |
93-141 | 2.65e-03 | |||
Tetratricopeptide repeat; Pssm-ID: 463860 [Multi-domain] Cd Length: 73 Bit Score: 36.04 E-value: 2.65e-03
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TPR | smart00028 | Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
50-82 | 2.93e-03 | |||
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism. Pssm-ID: 197478 [Multi-domain] Cd Length: 34 Bit Score: 34.73 E-value: 2.93e-03
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
40-147 | 3.66e-03 | |||
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator. Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 38.91 E-value: 3.66e-03
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
55-152 | 4.03e-03 | |||
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator. Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 38.91 E-value: 4.03e-03
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
111-151 | 4.12e-03 | |||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 38.06 E-value: 4.12e-03
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
95-192 | 4.48e-03 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 4.48e-03
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Thioredoxin_2 | pfam13098 | Thioredoxin-like domain; |
231-302 | 5.83e-03 | |||
Thioredoxin-like domain; Pssm-ID: 379034 [Multi-domain] Cd Length: 103 Bit Score: 35.86 E-value: 5.83e-03
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ER_PDI_fam | TIGR01130 | protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ... |
233-294 | 8.19e-03 | |||
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: 37.73 E-value: 8.19e-03
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SirB1 | COG2912 | Regulator of sirC expression, contains transglutaminase-like and TPR domains [Signal ... |
93-142 | 8.67e-03 | |||
Regulator of sirC expression, contains transglutaminase-like and TPR domains [Signal transduction mechanisms]; Pssm-ID: 442156 [Multi-domain] Cd Length: 264 Bit Score: 37.11 E-value: 8.67e-03
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TPR_2 | pfam07719 | Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ... |
50-82 | 8.71e-03 | |||
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515. Pssm-ID: 429619 [Multi-domain] Cd Length: 33 Bit Score: 33.27 E-value: 8.71e-03
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