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Conserved domains on  [gi|16131223|ref|NP_417803|]
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sulfurtransferase complex subunit TusC [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

sulfur relay protein TusC/DsrF( domain architecture ID 10011315)

sulfurtransferase TusC/DsrF 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; it accepts sulfur from TusA and transfers it in turn to TusE

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK00211 PRK00211
sulfurtransferase complex subunit TusC;
1-119 1.44e-69

sulfurtransferase complex subunit TusC;


:

Pssm-ID: 178930  Cd Length: 119  Bit Score: 203.94  E-value: 1.44e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131223    1 MKRIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEQCWVCA 80
Cdd:PRK00211   1 MKRIAFVFRQAPHGTASGREGLDALLATSAFTEDIGVFFIDDGVFQLLPGQQPDAILARDYIATFKLLPLYDIEQCYLCA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 16131223   81 ASLRERGLDPQTPFVVEATPLEADALRRELANYDVILRF 119
Cdd:PRK00211  81 ASLRERGLDPNTDFVLDVEPLDAAALRRKLDNYDVVLTF 119
 
Name Accession Description Interval E-value
PRK00211 PRK00211
sulfurtransferase complex subunit TusC;
1-119 1.44e-69

sulfurtransferase complex subunit TusC;


Pssm-ID: 178930  Cd Length: 119  Bit Score: 203.94  E-value: 1.44e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131223    1 MKRIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEQCWVCA 80
Cdd:PRK00211   1 MKRIAFVFRQAPHGTASGREGLDALLATSAFTEDIGVFFIDDGVFQLLPGQQPDAILARDYIATFKLLPLYDIEQCYLCA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 16131223   81 ASLRERGLDPQTPFVVEATPLEADALRRELANYDVILRF 119
Cdd:PRK00211  81 ASLRERGLDPNTDFVLDVEPLDAAALRRKLDNYDVVLTF 119
DsrF COG2923
Sulfur transfer complex TusBCD TusC component, DsrF family [Translation, ribosomal structure ...
 1-119 2.20e-60

Sulfur transfer complex TusBCD TusC component, DsrF family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442167  Cd Length: 118  Bit Score: 180.73  E-value: 2.20e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131223   1 MKRIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEQCWVCA 80
Cdd:COG2923   1 MKKLLFVFRQAPHGSAAAREGLDAALAAAAFDQDVSVLFIDDGVYQLLKGQQPEAIGQKNYIATFKALPLYDIEKVYVCA 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16131223  81 ASLRERGLDPqTPFVVEATPLEADALRRELANYDVILRF 119
Cdd:COG2923  81 ESLEERGLSE-DDLVLDVEVLSRAELRELLAEADVVLTF 118
sulf_tusC_dsrF TIGR03010
sulfur relay protein TusC/DsrF; The three proteins TusB, TusC, and TusD form a heterohexamer ...
 3-119 7.21e-60

sulfur relay protein TusC/DsrF; 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: 200229  Cd Length: 116  Bit Score: 179.27  E-value: 7.21e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131223     3 RIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEQCWVCAAS 82
Cdd:TIGR03010   1 KLAFVFRQAPHGTASGREGLDALLAASAFDEDIGVFFIDDGVLQLLKNQQPELILQKDYIATFKALPLYDIEELYVCAES 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 16131223    83 LRERGLDpQTPFVVEATPLEADALRRELANYDVILRF 119
Cdd:TIGR03010  81 LAERGLS-EDDLILDVEVLDRSALRAKLDRYDVVLTF 116
DrsE pfam02635
DsrE/DsrF-like family; DsrE is a small soluble protein involved in intracellular sulfur ...
 2-119 6.10e-31

DsrE/DsrF-like family; DsrE is a small soluble protein involved in intracellular sulfur reduction. This family also includes DsrF.


Pssm-ID: 426894  Cd Length: 117  Bit Score: 106.27  E-value: 6.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131223     2 KRIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEqCWVCAA 81
Cdd:pfam02635   1 KKVFIVVTSGPYGTEAAREALDLALAAAALGHDVAVFFHGDGVLNLLKGQEPNPIGEKNLAELLKALAEYGVK-VYVCGQ 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 16131223    82 SLRERGLDPQTPFVVEATPLEADALRRELANYDVILRF 119
Cdd:pfam02635  80 SLKARGITEDELLGVGVEVSGLGELAELQLEGDRVITF 117
 
Name Accession Description Interval E-value
PRK00211 PRK00211
sulfurtransferase complex subunit TusC;
1-119 1.44e-69

sulfurtransferase complex subunit TusC;


Pssm-ID: 178930  Cd Length: 119  Bit Score: 203.94  E-value: 1.44e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131223    1 MKRIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEQCWVCA 80
Cdd:PRK00211   1 MKRIAFVFRQAPHGTASGREGLDALLATSAFTEDIGVFFIDDGVFQLLPGQQPDAILARDYIATFKLLPLYDIEQCYLCA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 16131223   81 ASLRERGLDPQTPFVVEATPLEADALRRELANYDVILRF 119
Cdd:PRK00211  81 ASLRERGLDPNTDFVLDVEPLDAAALRRKLDNYDVVLTF 119
DsrF COG2923
Sulfur transfer complex TusBCD TusC component, DsrF family [Translation, ribosomal structure ...
 1-119 2.20e-60

Sulfur transfer complex TusBCD TusC component, DsrF family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442167  Cd Length: 118  Bit Score: 180.73  E-value: 2.20e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131223   1 MKRIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEQCWVCA 80
Cdd:COG2923   1 MKKLLFVFRQAPHGSAAAREGLDAALAAAAFDQDVSVLFIDDGVYQLLKGQQPEAIGQKNYIATFKALPLYDIEKVYVCA 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16131223  81 ASLRERGLDPqTPFVVEATPLEADALRRELANYDVILRF 119
Cdd:COG2923  81 ESLEERGLSE-DDLVLDVEVLSRAELRELLAEADVVLTF 118
sulf_tusC_dsrF TIGR03010
sulfur relay protein TusC/DsrF; The three proteins TusB, TusC, and TusD form a heterohexamer ...
 3-119 7.21e-60

sulfur relay protein TusC/DsrF; 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: 200229  Cd Length: 116  Bit Score: 179.27  E-value: 7.21e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131223     3 RIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEQCWVCAAS 82
Cdd:TIGR03010   1 KLAFVFRQAPHGTASGREGLDALLAASAFDEDIGVFFIDDGVLQLLKNQQPELILQKDYIATFKALPLYDIEELYVCAES 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 16131223    83 LRERGLDpQTPFVVEATPLEADALRRELANYDVILRF 119
Cdd:TIGR03010  81 LAERGLS-EDDLILDVEVLDRSALRAKLDRYDVVLTF 116
DrsE pfam02635
DsrE/DsrF-like family; DsrE is a small soluble protein involved in intracellular sulfur ...
 2-119 6.10e-31

DsrE/DsrF-like family; DsrE is a small soluble protein involved in intracellular sulfur reduction. This family also includes DsrF.


Pssm-ID: 426894  Cd Length: 117  Bit Score: 106.27  E-value: 6.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131223     2 KRIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEqCWVCAA 81
Cdd:pfam02635   1 KKVFIVVTSGPYGTEAAREALDLALAAAALGHDVAVFFHGDGVLNLLKGQEPNPIGEKNLAELLKALAEYGVK-VYVCGQ 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 16131223    82 SLRERGLDPQTPFVVEATPLEADALRRELANYDVILRF 119
Cdd:pfam02635  80 SLKARGITEDELLGVGVEVSGLGELAELQLEGDRVITF 117
 
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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