MULTISPECIES: sulfurtransferase-like selenium metabolism protein YedF [Providencia]
Protein Classification
SirA-like protein( domain architecture ID 10013705)
SirA-like protein similar to SirA, TusA, and the uncharacterized protein YedF; SirA belongs to a family of bacterial two-component response regulators that controls secondary metabolism and virulence, TusA interacts with cysteine desulfurase IscS and acts as the first member in a sulfur relay
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| PRK11018 | PRK11018 | putative sulfurtransferase YedF; |
3-79 | 7.90e-54 | ||
putative sulfurtransferase YedF; : Pssm-ID: 236822 Cd Length: 78 Bit Score: 160.98 E-value: 7.90e-54
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| Name | Accession | Description | Interval | E-value | ||
| PRK11018 | PRK11018 | putative sulfurtransferase YedF; |
3-79 | 7.90e-54 | ||
putative sulfurtransferase YedF; Pssm-ID: 236822 Cd Length: 78 Bit Score: 160.98 E-value: 7.90e-54
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| YedF | cd03422 | YedF is a bacterial SirA-like protein of unknown function. SirA (also known as UvrY, and ... |
11-79 | 8.98e-43 | ||
YedF is a bacterial SirA-like protein of unknown function. SirA (also known as UvrY, and YhhP) belongs to a family of a two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding. Pssm-ID: 239514 Cd Length: 69 Bit Score: 132.93 E-value: 8.98e-43
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| TusA | COG0425 | Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ... |
12-79 | 2.76e-21 | ||
Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ribosomal structure and biogenesis, Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440194 Cd Length: 70 Bit Score: 78.70 E-value: 2.76e-21
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| TusA | pfam01206 | Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. |
11-74 | 1.31e-17 | ||
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. Pssm-ID: 426125 Cd Length: 64 Bit Score: 69.14 E-value: 1.31e-17
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| Name | Accession | Description | Interval | E-value | ||
| PRK11018 | PRK11018 | putative sulfurtransferase YedF; |
3-79 | 7.90e-54 | ||
putative sulfurtransferase YedF; Pssm-ID: 236822 Cd Length: 78 Bit Score: 160.98 E-value: 7.90e-54
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| YedF | cd03422 | YedF is a bacterial SirA-like protein of unknown function. SirA (also known as UvrY, and ... |
11-79 | 8.98e-43 | ||
YedF is a bacterial SirA-like protein of unknown function. SirA (also known as UvrY, and YhhP) belongs to a family of a two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding. Pssm-ID: 239514 Cd Length: 69 Bit Score: 132.93 E-value: 8.98e-43
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| SirA_YedF_YeeD | cd00291 | SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and ... |
11-79 | 5.48e-23 | ||
SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and YhhP) belongs to a family of bacterial two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding. Pssm-ID: 238180 Cd Length: 69 Bit Score: 82.99 E-value: 5.48e-23
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| TusA | COG0425 | Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ... |
12-79 | 2.76e-21 | ||
Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ribosomal structure and biogenesis, Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440194 Cd Length: 70 Bit Score: 78.70 E-value: 2.76e-21
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| TusA | pfam01206 | Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. |
11-74 | 1.31e-17 | ||
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. Pssm-ID: 426125 Cd Length: 64 Bit Score: 69.14 E-value: 1.31e-17
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| SirA | cd03423 | SirA (also known as UvrY, and YhhP) belongs to a family of two-component response regulators ... |
12-79 | 1.11e-08 | ||
SirA (also known as UvrY, and YhhP) belongs to a family of two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is thought to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding. Pssm-ID: 239515 Cd Length: 69 Bit Score: 46.58 E-value: 1.11e-08
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| PRK00299 | PRK00299 | sulfurtransferase TusA; |
1-79 | 1.12e-05 | ||
sulfurtransferase TusA; Pssm-ID: 178967 Cd Length: 81 Bit Score: 39.23 E-value: 1.12e-05
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| SirA_RHOD_Pry_redox | cd03420 | SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown ... |
11-79 | 1.50e-05 | ||
SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown function. Other domains include RHOD (rhodanese homology domain), and Pry_redox (pyridine nucleotide-disulphide oxidoreductase) as well as a C-terminal domain that corresponds to COG2210. This fold is referred to as a two-layered alpha/beta sandwich, structurally similar to that of translation initiation factor 3. Pssm-ID: 239512 Cd Length: 69 Bit Score: 38.51 E-value: 1.50e-05
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| SirA_like_N | cd03421 | SirA_like_N, a protein of unknown function with an N-terminal SirA-like domain. The SirA, ... |
12-79 | 4.21e-04 | ||
SirA_like_N, a protein of unknown function with an N-terminal SirA-like domain. The SirA, YedF, YeeD protein family is present in bacteria as well as archaea. SirA (also known as UvrY, and YhhP) belongs to a family of a two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding. Pssm-ID: 239513 Cd Length: 67 Bit Score: 34.87 E-value: 4.21e-04
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