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Conserved domains on  [gi|1101217992|gb|OIP66740|]
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hypothetical protein AUK29_00155 [Nitrospirae bacterium CG2_30_53_67]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DsrH super family cl46469
DsrH like protein; DsrH is involved in oxidation of intracellular sulphur in the phototrophic ...
 4-87 3.12e-09

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


The actual alignment was detected with superfamily member COG2168:

Pssm-ID: 480809  Cd Length: 96  Bit Score: 49.06  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101217992  4 LHIIKKT-NDTYAWEAALRQREKKDGqvlVLLLHDAVLA--SGPVDADG-------VFACRDDVAARGVK----TKAQLV 69
Cdd:COG2168    2 LHTVSKSpFETNDLDSCLRLLTPGDA---LLLIQDGVYAalKGSRALALllaapikVYALKEDLEARGLTaqisDGVKLI 78

                         90
                 ....*....|....*...
gi 1101217992 70 GYEEIVKMLLEADSVVCW 87
Cdd:COG2168   79 DYAGFVELTEKHDKQISW 96
 
Name Accession Description Interval E-value
TusB COG2168
Sulfur transfer complex TusBCD TusB component, DsrH family [Translation, ribosomal structure ...
 4-87 3.12e-09

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


Pssm-ID: 441771  Cd Length: 96  Bit Score: 49.06  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101217992  4 LHIIKKT-NDTYAWEAALRQREKKDGqvlVLLLHDAVLA--SGPVDADG-------VFACRDDVAARGVK----TKAQLV 69
Cdd:COG2168    2 LHTVSKSpFETNDLDSCLRLLTPGDA---LLLIQDGVYAalKGSRALALllaapikVYALKEDLEARGLTaqisDGVKLI 78

                         90
                 ....*....|....*...
gi 1101217992 70 GYEEIVKMLLEADSVVCW 87
Cdd:COG2168   79 DYAGFVELTEKHDKQISW 96
sulf_tusB_dsrH TIGR03011
sulfur relay protein TusB/DsrH; The three proteins TusB, TusC, and TusD form a heterohexamer ...
 5-87 2.47e-04

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: 36.45  E-value: 2.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101217992  5 HIIKKT-NDTYAWEAALRQREKKDGqvlVLLLHDAVLA--SGPVDADG-------VFACRDDVAARG----VKTKAQLVG 70
Cdd:TIGR03011  1 HTVKKSpFEDNDLELCLRLLGPGDA---ILLLQDGVYAalEGNRYLSAllkagvkVYALKEDLEARGltdrLSDGVNVID 77

                         90
                 ....*....|....*..
gi 1101217992 71 YEEIVKMLLEADSVVCW 87
Cdd:TIGR03011 78 YTGFVELTEKHDKVITW 94
 
Name Accession Description Interval E-value
TusB COG2168
Sulfur transfer complex TusBCD TusB component, DsrH family [Translation, ribosomal structure ...
 4-87 3.12e-09

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


Pssm-ID: 441771  Cd Length: 96  Bit Score: 49.06  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101217992  4 LHIIKKT-NDTYAWEAALRQREKKDGqvlVLLLHDAVLA--SGPVDADG-------VFACRDDVAARGVK----TKAQLV 69
Cdd:COG2168    2 LHTVSKSpFETNDLDSCLRLLTPGDA---LLLIQDGVYAalKGSRALALllaapikVYALKEDLEARGLTaqisDGVKLI 78

                         90
                 ....*....|....*...
gi 1101217992 70 GYEEIVKMLLEADSVVCW 87
Cdd:COG2168   79 DYAGFVELTEKHDKQISW 96
sulf_tusB_dsrH TIGR03011
sulfur relay protein TusB/DsrH; The three proteins TusB, TusC, and TusD form a heterohexamer ...
 5-87 2.47e-04

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: 36.45  E-value: 2.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101217992  5 HIIKKT-NDTYAWEAALRQREKKDGqvlVLLLHDAVLA--SGPVDADG-------VFACRDDVAARG----VKTKAQLVG 70
Cdd:TIGR03011  1 HTVKKSpFEDNDLELCLRLLGPGDA---ILLLQDGVYAalEGNRYLSAllkagvkVYALKEDLEARGltdrLSDGVNVID 77

                         90
                 ....*....|....*..
gi 1101217992 71 YEEIVKMLLEADSVVCW 87
Cdd:TIGR03011 78 YTGFVELTEKHDKVITW 94
 
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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