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Conserved domains on  [gi|147736423|gb|ABQ47763|]
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DsrH family protein [Thermotoga petrophila RKU-1]

Protein Classification

DsrH/TusB family sulfur relay protein( domain architecture ID 10005495)

DsrH/TusB family sulfur relay protein similar to sulfurtransferase complex subunit TusB, which is part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TusB COG2168
Sulfur transfer complex TusBCD TusB component, DsrH family [Translation, ribosomal structure ...
 16-86 1.82e-18

Sulfur transfer complex TusBCD TusB component, DsrH family [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 441771  Cd Length: 96  Bit Score: 72.56  E-value: 1.82e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 147736423 16 KLKIRSAKAEDKIVLIQNGVFWALEE-------LETPAKVYTIKDDFLARGYSEEDS-KVPLITYSEFIDLLESEEKFI 86
Cdd:COG2168  16 DSCLRLLTPGDALLLIQDGVYAALKGsralallLAAPIKVYALKEDLEARGLTAQISdGVKLIDYAGFVELTEKHDKQI 94
 
Name Accession Description Interval E-value
TusB COG2168
Sulfur transfer complex TusBCD TusB component, DsrH family [Translation, ribosomal structure ...
 16-86 1.82e-18

Sulfur transfer complex TusBCD TusB component, DsrH family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441771  Cd Length: 96  Bit Score: 72.56  E-value: 1.82e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 147736423 16 KLKIRSAKAEDKIVLIQNGVFWALEE-------LETPAKVYTIKDDFLARGYSEEDS-KVPLITYSEFIDLLESEEKFI 86
Cdd:COG2168  16 DSCLRLLTPGDALLLIQDGVYAALKGsralallLAAPIKVYALKEDLEARGLTAQISdGVKLIDYAGFVELTEKHDKQI 94
sulf_tusB_dsrH TIGR03011
sulfur relay protein TusB/DsrH; The three proteins TusB, TusC, and TusD form a heterohexamer ...
 19-84 1.02e-13

sulfur relay protein TusB/DsrH; The three proteins TusB, TusC, and TusD form a heterohexamer responsible for a sulfur relay reaction. In large numbers of proteobacterial species, this complex acts on a Cys-derived persulfide moiety, delivered by the cysteine desulfurase IscS to TusA, then to TusBCD. The activated sulfur group is then transferred to TusE (DsrC), then by MnmA (TrmU) for modification of an anticodon nucleotide in tRNAs for Glu, Lys, and Gln. The sulfur relay complex TusBCD is also found, under the designation DsrEFH, in phototrophic and chemotrophic sulfur bacteria, such as Chromatium vinosum. In these organisms, it seems the primary purpose is related to sulfur flux, such as oxidation from sulfide to molecular sulfur to sulfate. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274388 [Multi-domain]  Cd Length: 94  Bit Score: 60.33  E-value: 1.02e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147736423  19 IRSAKAEDKIVLIQNGVFWALEE-------LETPAKVYTIKDDFLARGYSEEDS-KVPLITYSEFIDLLESEEK 84
Cdd:TIGR03011 17 LRLLGPGDAILLLQDGVYAALEGnrylsalLKAGVKVYALKEDLEARGLTDRLSdGVNVIDYTGFVELTEKHDK 90
DsrH pfam04077
DsrH like protein; DsrH is involved in oxidation of intracellular sulphur in the phototrophic ...
 19-84 4.76e-11

DsrH like protein; DsrH is involved in oxidation of intracellular sulphur in the phototrophic sulphur bacterium Chromatium vinosum D.


Pssm-ID: 461159  Cd Length: 87  Bit Score: 53.33  E-value: 4.76e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147736423  19 IRSAKAEDKIVLIQNGVFWALEE-------LETPAKVYTIKDDFLARGYSEE-DSKVPLITYSEFIDLLESEEK 84
Cdd:pfam04077 13 LRLLTPGDAVLLIQDGVYAALKGnrflaalQAAGVKLYALKEDLEARGLSDQiSPGVKVIDYDGFVDLTVKHDK 86
PRK13510 PRK13510
sulfurtransferase complex subunit TusB;
19-78 2.66e-10

sulfurtransferase complex subunit TusB;


Pssm-ID: 184101  Cd Length: 95  Bit Score: 51.90  E-value: 2.66e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 147736423 19 IRSAKAEDKIVLIQNGVFWALEE-------LETPAKVYTIKDDFLARGYSEEDS-KVPLITYSEFIDL 78
Cdd:PRK13510 18 LRLLKEGDDLLLLQDGVTAALKGnrfleslRNAPIKLYALKEDLIARGLTGQISdSIILISYTDFVRL 85
 
Name Accession Description Interval E-value
TusB COG2168
Sulfur transfer complex TusBCD TusB component, DsrH family [Translation, ribosomal structure ...
 16-86 1.82e-18

Sulfur transfer complex TusBCD TusB component, DsrH family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441771  Cd Length: 96  Bit Score: 72.56  E-value: 1.82e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 147736423 16 KLKIRSAKAEDKIVLIQNGVFWALEE-------LETPAKVYTIKDDFLARGYSEEDS-KVPLITYSEFIDLLESEEKFI 86
Cdd:COG2168  16 DSCLRLLTPGDALLLIQDGVYAALKGsralallLAAPIKVYALKEDLEARGLTAQISdGVKLIDYAGFVELTEKHDKQI 94
sulf_tusB_dsrH TIGR03011
sulfur relay protein TusB/DsrH; The three proteins TusB, TusC, and TusD form a heterohexamer ...
 19-84 1.02e-13

sulfur relay protein TusB/DsrH; The three proteins TusB, TusC, and TusD form a heterohexamer responsible for a sulfur relay reaction. In large numbers of proteobacterial species, this complex acts on a Cys-derived persulfide moiety, delivered by the cysteine desulfurase IscS to TusA, then to TusBCD. The activated sulfur group is then transferred to TusE (DsrC), then by MnmA (TrmU) for modification of an anticodon nucleotide in tRNAs for Glu, Lys, and Gln. The sulfur relay complex TusBCD is also found, under the designation DsrEFH, in phototrophic and chemotrophic sulfur bacteria, such as Chromatium vinosum. In these organisms, it seems the primary purpose is related to sulfur flux, such as oxidation from sulfide to molecular sulfur to sulfate. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274388 [Multi-domain]  Cd Length: 94  Bit Score: 60.33  E-value: 1.02e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147736423  19 IRSAKAEDKIVLIQNGVFWALEE-------LETPAKVYTIKDDFLARGYSEEDS-KVPLITYSEFIDLLESEEK 84
Cdd:TIGR03011 17 LRLLGPGDAILLLQDGVYAALEGnrylsalLKAGVKVYALKEDLEARGLTDRLSdGVNVIDYTGFVELTEKHDK 90
DsrH pfam04077
DsrH like protein; DsrH is involved in oxidation of intracellular sulphur in the phototrophic ...
 19-84 4.76e-11

DsrH like protein; DsrH is involved in oxidation of intracellular sulphur in the phototrophic sulphur bacterium Chromatium vinosum D.


Pssm-ID: 461159  Cd Length: 87  Bit Score: 53.33  E-value: 4.76e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147736423  19 IRSAKAEDKIVLIQNGVFWALEE-------LETPAKVYTIKDDFLARGYSEE-DSKVPLITYSEFIDLLESEEK 84
Cdd:pfam04077 13 LRLLTPGDAVLLIQDGVYAALKGnrflaalQAAGVKLYALKEDLEARGLSDQiSPGVKVIDYDGFVDLTVKHDK 86
PRK13510 PRK13510
sulfurtransferase complex subunit TusB;
19-78 2.66e-10

sulfurtransferase complex subunit TusB;


Pssm-ID: 184101  Cd Length: 95  Bit Score: 51.90  E-value: 2.66e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 147736423 19 IRSAKAEDKIVLIQNGVFWALEE-------LETPAKVYTIKDDFLARGYSEEDS-KVPLITYSEFIDL 78
Cdd:PRK13510 18 LRLLKEGDDLLLLQDGVTAALKGnrfleslRNAPIKLYALKEDLIARGLTGQISdSIILISYTDFVRL 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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