Chain A, HYPOTHETICAL 8.6 KDA PROTEIN IN AMYA-FLIE INTERGENIC REGION
Protein Classification
sulfurtransferase TusA family protein( domain architecture ID 2263)
sulfurtransferase TusA family protein similar to sulfurtransferase TusA, which interacts with cysteine desulfurase IscS and acts as the first member in a sulfur relay mechanism, transfering sulfur to the TusBCD complex
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| PRK11018 | PRK11018 | putative sulfurtransferase YedF; |
20-97 | 1.84e-57 | ||
putative sulfurtransferase YedF; : Pssm-ID: 236822 Cd Length: 78 Bit Score: 171.00 E-value: 1.84e-57
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| Name | Accession | Description | Interval | E-value | ||
| PRK11018 | PRK11018 | putative sulfurtransferase YedF; |
20-97 | 1.84e-57 | ||
putative sulfurtransferase YedF; Pssm-ID: 236822 Cd Length: 78 Bit Score: 171.00 E-value: 1.84e-57
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| YedF | cd03422 | YedF is a bacterial SirA-like protein of unknown function. SirA (also known as UvrY, and ... |
29-97 | 1.33e-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: 136.02 E-value: 1.33e-43
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| TusA | COG0425 | Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ... |
30-97 | 4.15e-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: 81.40 E-value: 4.15e-22
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| TusA | pfam01206 | Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. |
29-92 | 1.78e-17 | ||
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. Pssm-ID: 426125 Cd Length: 64 Bit Score: 69.52 E-value: 1.78e-17
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| Name | Accession | Description | Interval | E-value | ||
| PRK11018 | PRK11018 | putative sulfurtransferase YedF; |
20-97 | 1.84e-57 | ||
putative sulfurtransferase YedF; Pssm-ID: 236822 Cd Length: 78 Bit Score: 171.00 E-value: 1.84e-57
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| YedF | cd03422 | YedF is a bacterial SirA-like protein of unknown function. SirA (also known as UvrY, and ... |
29-97 | 1.33e-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: 136.02 E-value: 1.33e-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 ... |
29-97 | 3.04e-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: 84.14 E-value: 3.04e-23
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| TusA | COG0425 | Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ... |
30-97 | 4.15e-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: 81.40 E-value: 4.15e-22
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| TusA | pfam01206 | Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. |
29-92 | 1.78e-17 | ||
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. Pssm-ID: 426125 Cd Length: 64 Bit Score: 69.52 E-value: 1.78e-17
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| SirA | cd03423 | SirA (also known as UvrY, and YhhP) belongs to a family of two-component response regulators ... |
30-97 | 1.36e-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: 46.97 E-value: 1.36e-08
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| PRK00299 | PRK00299 | sulfurtransferase TusA; |
26-97 | 4.37e-06 | ||
sulfurtransferase TusA; Pssm-ID: 178967 Cd Length: 81 Bit Score: 40.78 E-value: 4.37e-06
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| SirA_RHOD_Pry_redox | cd03420 | SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown ... |
29-97 | 6.68e-06 | ||
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: 40.05 E-value: 6.68e-06
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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, ... |
30-97 | 5.11e-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: 37.95 E-value: 5.11e-05
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| Blast search parameters | ||||
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