thioredoxin family protein [Thermosipho africanus]
Protein Classification
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; |
8-78 | 6.19e-28 | ||
Thioredoxin domain; : Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 95.36 E-value: 6.19e-28
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| Name | Accession | Description | Interval | E-value | ||
| Thioredoxin_3 | pfam13192 | Thioredoxin domain; |
8-78 | 6.19e-28 | ||
Thioredoxin domain; Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 95.36 E-value: 6.19e-28
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| redox_disulf_2 | TIGR00412 | small redox-active disulfide protein 2; This small protein is found in three archaeal species ... |
4-78 | 1.94e-22 | ||
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: 81.88 E-value: 1.94e-22
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| GrxC | COG0695 | Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
4-78 | 5.07e-04 | ||
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 34.79 E-value: 5.07e-04
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| GRX_GRXh_1_2_like | cd03419 | Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ... |
10-60 | 3.66e-03 | ||
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3. Pssm-ID: 239511 [Multi-domain] Cd Length: 82 Bit Score: 32.90 E-value: 3.66e-03
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| Name | Accession | Description | Interval | E-value | ||
| Thioredoxin_3 | pfam13192 | Thioredoxin domain; |
8-78 | 6.19e-28 | ||
Thioredoxin domain; Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 95.36 E-value: 6.19e-28
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| redox_disulf_2 | TIGR00412 | small redox-active disulfide protein 2; This small protein is found in three archaeal species ... |
4-78 | 1.94e-22 | ||
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: 81.88 E-value: 1.94e-22
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| GrxC | COG0695 | Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
4-78 | 5.07e-04 | ||
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 34.79 E-value: 5.07e-04
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| GRX_GRXh_1_2_like | cd03419 | Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ... |
10-60 | 3.66e-03 | ||
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3. Pssm-ID: 239511 [Multi-domain] Cd Length: 82 Bit Score: 32.90 E-value: 3.66e-03
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| Blast search parameters | ||||
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