sulfurtransferase-like selenium metabolism protein YedF [Escherichia coli]
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; |
1-77 | 5.22e-54 | ||
putative sulfurtransferase YedF; : Pssm-ID: 236822 Cd Length: 78 Bit Score: 161.37 E-value: 5.22e-54
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Name | Accession | Description | Interval | E-value | ||
PRK11018 | PRK11018 | putative sulfurtransferase YedF; |
1-77 | 5.22e-54 | ||
putative sulfurtransferase YedF; Pssm-ID: 236822 Cd Length: 78 Bit Score: 161.37 E-value: 5.22e-54
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YedF | cd03422 | YedF is a bacterial SirA-like protein of unknown function. SirA (also known as UvrY, and ... |
9-77 | 2.10e-42 | ||
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: 131.78 E-value: 2.10e-42
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TusA | COG0425 | Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ... |
10-77 | 5.39e-22 | ||
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: 80.24 E-value: 5.39e-22
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TusA | pfam01206 | Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. |
9-72 | 6.95e-18 | ||
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. Pssm-ID: 426125 Cd Length: 64 Bit Score: 69.91 E-value: 6.95e-18
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Name | Accession | Description | Interval | E-value | ||
PRK11018 | PRK11018 | putative sulfurtransferase YedF; |
1-77 | 5.22e-54 | ||
putative sulfurtransferase YedF; Pssm-ID: 236822 Cd Length: 78 Bit Score: 161.37 E-value: 5.22e-54
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YedF | cd03422 | YedF is a bacterial SirA-like protein of unknown function. SirA (also known as UvrY, and ... |
9-77 | 2.10e-42 | ||
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: 131.78 E-value: 2.10e-42
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SirA_YedF_YeeD | cd00291 | SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and ... |
9-77 | 6.17e-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: 82.60 E-value: 6.17e-23
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TusA | COG0425 | Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ... |
10-77 | 5.39e-22 | ||
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: 80.24 E-value: 5.39e-22
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TusA | pfam01206 | Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. |
9-72 | 6.95e-18 | ||
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. Pssm-ID: 426125 Cd Length: 64 Bit Score: 69.91 E-value: 6.95e-18
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SirA | cd03423 | SirA (also known as UvrY, and YhhP) belongs to a family of two-component response regulators ... |
10-77 | 9.70e-09 | ||
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: 9.70e-09
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PRK00299 | PRK00299 | sulfurtransferase TusA; |
6-77 | 2.93e-06 | ||
sulfurtransferase TusA; Pssm-ID: 178967 Cd Length: 81 Bit Score: 40.78 E-value: 2.93e-06
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SirA_RHOD_Pry_redox | cd03420 | SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown ... |
9-77 | 1.04e-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: 38.90 E-value: 1.04e-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, ... |
10-77 | 5.07e-05 | ||
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: 37.18 E-value: 5.07e-05
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Blast search parameters | ||||
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