thioredoxin family protein [Arcanobacterium haemolyticum]
thioredoxin family protein( domain architecture ID 10590097)
thioredoxin family protein may function as a thiol disulfide reductase that catalyzes the reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif
List of domain hits
Name | Accession | Description | Interval | E-value | ||
Thioredoxin_3 | pfam13192 | Thioredoxin domain; |
6-76 | 3.75e-32 | ||
Thioredoxin domain; : Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 106.14 E-value: 3.75e-32
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Name | Accession | Description | Interval | E-value | ||
Thioredoxin_3 | pfam13192 | Thioredoxin domain; |
6-76 | 3.75e-32 | ||
Thioredoxin domain; Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 106.14 E-value: 3.75e-32
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redox_disulf_2 | TIGR00412 | small redox-active disulfide protein 2; This small protein is found in three archaeal species ... |
1-75 | 1.75e-20 | ||
small redox-active disulfide protein 2; This small protein is found in three archaeal species so far (Methanococcus jannaschii, Archeoglobus fulgidus, and Methanobacterium thermoautotrophicum) as well as in Anabaena PCC7120. It is homologous to thioredoxins, glutaredoxins, and protein disulfide isomerases, and shares with them a redox-active disulfide. The redox active disulfide region CXXC motif resembles neither thioredoxin nor glutaredoxin. A closely related protein found in the same three Archaea, described by redox_disulf_1, has a glutaredoxin-like CP[YH]C sequence; it has been characterized in functional assays as redox-active but unlikely to be a thioredoxin or glutaredoxin. [Unknown function, General] Pssm-ID: 129506 Cd Length: 76 Bit Score: 76.87 E-value: 1.75e-20
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AhpF | COG3634 | Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]; |
42-76 | 1.70e-04 | ||
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]; Pssm-ID: 442851 [Multi-domain] Cd Length: 200 Bit Score: 37.42 E-value: 1.70e-04
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AhpF_NTD_C | cd03026 | TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ... |
10-64 | 6.15e-04 | ||
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) subfamily, C-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which then reduces hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD containing two contiguous TRX-fold subdomains similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -> catalytic core of AhpF -> NTD of AhpF -> AhpC -> peroxide substrates. The catalytic CXXC motif of the NTD of AhpF is contained in its C-terminal TRX subdomain. Pssm-ID: 239324 [Multi-domain] Cd Length: 89 Bit Score: 34.96 E-value: 6.15e-04
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Name | Accession | Description | Interval | E-value | ||
Thioredoxin_3 | pfam13192 | Thioredoxin domain; |
6-76 | 3.75e-32 | ||
Thioredoxin domain; Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 106.14 E-value: 3.75e-32
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redox_disulf_2 | TIGR00412 | small redox-active disulfide protein 2; This small protein is found in three archaeal species ... |
1-75 | 1.75e-20 | ||
small redox-active disulfide protein 2; This small protein is found in three archaeal species so far (Methanococcus jannaschii, Archeoglobus fulgidus, and Methanobacterium thermoautotrophicum) as well as in Anabaena PCC7120. It is homologous to thioredoxins, glutaredoxins, and protein disulfide isomerases, and shares with them a redox-active disulfide. The redox active disulfide region CXXC motif resembles neither thioredoxin nor glutaredoxin. A closely related protein found in the same three Archaea, described by redox_disulf_1, has a glutaredoxin-like CP[YH]C sequence; it has been characterized in functional assays as redox-active but unlikely to be a thioredoxin or glutaredoxin. [Unknown function, General] Pssm-ID: 129506 Cd Length: 76 Bit Score: 76.87 E-value: 1.75e-20
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AhpF | COG3634 | Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]; |
42-76 | 1.70e-04 | ||
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]; Pssm-ID: 442851 [Multi-domain] Cd Length: 200 Bit Score: 37.42 E-value: 1.70e-04
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AhpF_NTD_C | cd03026 | TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ... |
10-64 | 6.15e-04 | ||
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) subfamily, C-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which then reduces hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD containing two contiguous TRX-fold subdomains similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -> catalytic core of AhpF -> NTD of AhpF -> AhpC -> peroxide substrates. The catalytic CXXC motif of the NTD of AhpF is contained in its C-terminal TRX subdomain. Pssm-ID: 239324 [Multi-domain] Cd Length: 89 Bit Score: 34.96 E-value: 6.15e-04
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DsbG | COG1651 | Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ... |
17-75 | 7.46e-04 | ||
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441257 [Multi-domain] Cd Length: 152 Bit Score: 35.74 E-value: 7.46e-04
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FrnE | COG2761 | Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ... |
22-75 | 1.54e-03 | ||
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442047 [Multi-domain] Cd Length: 205 Bit Score: 34.86 E-value: 1.54e-03
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TRX_GRX_like | cd02973 | Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ... |
42-64 | 1.76e-03 | ||
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins that show similarity to both TRX and GRX, including the C-terminal TRX-fold subdomain of Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). All members contain a redox-active CXXC motif and may function as PDOs. The archaeal proteins Mj0307 and Mt807 show structures more similar to GRX, but activities more similar to TRX. Some members of the family are similar to PfPDO in that they contain a second CXXC motif located in a second TRX-fold subdomain at the N-terminus; the superimposable N- and C-terminal TRX subdomains form a compact structure. PfPDO is postulated to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI). The C-terminal CXXC motif of PfPDO is required for its oxidase, reductase and isomerase activities. Also included in the family is the C-terminal TRX-fold subdomain of the N-terminal domain (NTD) of bacterial AhpF, which has a similar fold as PfPDO with two TRX-fold subdomains but without the second CXXC motif. Pssm-ID: 239271 [Multi-domain] Cd Length: 67 Bit Score: 33.31 E-value: 1.76e-03
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NrdH | cd02976 | NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
7-75 | 3.76e-03 | ||
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein. Pssm-ID: 239274 [Multi-domain] Cd Length: 73 Bit Score: 32.58 E-value: 3.76e-03
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Blast search parameters | ||||
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