MULTISPECIES: hypothetical protein [Citrobacter]
Protein Classification
thioredoxin domain-containing protein( domain architecture ID 144)
thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or 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_like super family | cl00388 | Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ... |
11-63 | 3.85e-04 | ||
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is 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 the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others. The actual alignment was detected with superfamily member pfam13192: Pssm-ID: 469754 [Multi-domain] Cd Length: 71 Bit Score: 35.27 E-value: 3.85e-04
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| Name | Accession | Description | Interval | E-value | ||
| Thioredoxin_3 | pfam13192 | Thioredoxin domain; |
11-63 | 3.85e-04 | ||
Thioredoxin domain; Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 35.27 E-value: 3.85e-04
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| redox_disulf_2 | TIGR00412 | small redox-active disulfide protein 2; This small protein is found in three archaeal species ... |
8-65 | 3.37e-03 | ||
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: 32.95 E-value: 3.37e-03
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| Name | Accession | Description | Interval | E-value | ||
| Thioredoxin_3 | pfam13192 | Thioredoxin domain; |
11-63 | 3.85e-04 | ||
Thioredoxin domain; Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 35.27 E-value: 3.85e-04
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| redox_disulf_2 | TIGR00412 | small redox-active disulfide protein 2; This small protein is found in three archaeal species ... |
8-65 | 3.37e-03 | ||
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: 32.95 E-value: 3.37e-03
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