sulfurtransferase [Serratia marcescens WW4]
Protein Classification
sulfurtransferase( domain architecture ID 10011363)
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 | ||
| PRK00299 | PRK00299 | sulfurtransferase TusA; |
1-80 | 4.67e-57 | ||
sulfurtransferase TusA; : Pssm-ID: 178967 Cd Length: 81 Bit Score: 169.43 E-value: 4.67e-57
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| Name | Accession | Description | Interval | E-value | ||
| PRK00299 | PRK00299 | sulfurtransferase TusA; |
1-80 | 4.67e-57 | ||
sulfurtransferase TusA; Pssm-ID: 178967 Cd Length: 81 Bit Score: 169.43 E-value: 4.67e-57
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| SirA | cd03423 | SirA (also known as UvrY, and YhhP) belongs to a family of two-component response regulators ... |
11-79 | 3.64e-43 | ||
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: 134.02 E-value: 3.64e-43
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| TusA | COG0425 | Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ... |
12-80 | 2.10e-29 | ||
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: 99.11 E-value: 2.10e-29
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| TusA | pfam01206 | Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. |
11-74 | 1.16e-19 | ||
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. Pssm-ID: 426125 Cd Length: 64 Bit Score: 74.53 E-value: 1.16e-19
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| selenium_YedF | TIGR03527 | selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in ... |
12-80 | 4.78e-05 | ||
selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in size, and include the uncharacterized YedF protein of Escherichia coli. This family shares an N-terminal domain, modeled by pfam01206, with the sulfurtransferase TusA (also called SirA). The C-terminal domain includes a typical redox-active disulfide motif, CGXC. This protein family found only among those genomes that also carry the selenium donor protein SelD, and its connection to selenium metabolism is indicated by the method of partial phylogenetic profiling vs. SelD. Its gene typically is found next to selD. Members of this family are found even when selenocysteine and selenouridine biosynthesis pathways are, except for SelD, completely absent, as in Enterococcus faecalis. Its role in selenium metabolism is unclear, but may include either detoxification or a role in labile selenoprotein biosynthesis. Pssm-ID: 274630 [Multi-domain] Cd Length: 194 Bit Score: 39.14 E-value: 4.78e-05
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| Name | Accession | Description | Interval | E-value | ||
| PRK00299 | PRK00299 | sulfurtransferase TusA; |
1-80 | 4.67e-57 | ||
sulfurtransferase TusA; Pssm-ID: 178967 Cd Length: 81 Bit Score: 169.43 E-value: 4.67e-57
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| SirA | cd03423 | SirA (also known as UvrY, and YhhP) belongs to a family of two-component response regulators ... |
11-79 | 3.64e-43 | ||
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: 134.02 E-value: 3.64e-43
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| TusA | COG0425 | Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ... |
12-80 | 2.10e-29 | ||
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: 99.11 E-value: 2.10e-29
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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 | 2.12e-25 | ||
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: 89.15 E-value: 2.12e-25
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| TusA | pfam01206 | Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. |
11-74 | 1.16e-19 | ||
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. Pssm-ID: 426125 Cd Length: 64 Bit Score: 74.53 E-value: 1.16e-19
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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 | 1.37e-12 | ||
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: 56.62 E-value: 1.37e-12
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| PRK11018 | PRK11018 | putative sulfurtransferase YedF; |
7-79 | 1.80e-06 | ||
putative sulfurtransferase YedF; Pssm-ID: 236822 Cd Length: 78 Bit Score: 41.18 E-value: 1.80e-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, ... |
11-79 | 3.13e-06 | ||
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: 40.26 E-value: 3.13e-06
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| selenium_YedF | TIGR03527 | selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in ... |
12-80 | 4.78e-05 | ||
selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in size, and include the uncharacterized YedF protein of Escherichia coli. This family shares an N-terminal domain, modeled by pfam01206, with the sulfurtransferase TusA (also called SirA). The C-terminal domain includes a typical redox-active disulfide motif, CGXC. This protein family found only among those genomes that also carry the selenium donor protein SelD, and its connection to selenium metabolism is indicated by the method of partial phylogenetic profiling vs. SelD. Its gene typically is found next to selD. Members of this family are found even when selenocysteine and selenouridine biosynthesis pathways are, except for SelD, completely absent, as in Enterococcus faecalis. Its role in selenium metabolism is unclear, but may include either detoxification or a role in labile selenoprotein biosynthesis. Pssm-ID: 274630 [Multi-domain] Cd Length: 194 Bit Score: 39.14 E-value: 4.78e-05
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| YedF | cd03422 | YedF is a bacterial SirA-like protein of unknown function. SirA (also known as UvrY, and ... |
12-79 | 7.30e-04 | ||
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: 34.32 E-value: 7.30e-04
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| Blast search parameters | ||||
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