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Conserved domains on  [gi|489485062|ref|WP_003390036|]
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MULTISPECIES: ClpX C4-type zinc finger protein [Brevibacillus]

Protein Classification

ClpX C4-type zinc finger protein( domain architecture ID 10659679)

ClpX C4-type zinc finger protein may bind zinc, similar to the N-terminal zinc finger of ATP-dependent Clp protease ATP-binding subunit ClpX

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
 95-131 4.05e-07

ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the universally conserved Hsp100 family of proteins, and possesses a putative zinc finger motif of the C4 type. This presumed zinc binding domain is found at the N-terminus of the ClpX protein. ClpX is an ATPase which functions both as a substrate specificity component of the ClpXP protease and as a molecular chaperone. The molecular function of this domain is now known.


:

Pssm-ID: 198062 [Multi-domain]  Cd Length: 39  Bit Score: 43.71  E-value: 4.05e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 489485062    95 CSFCGKSKSDVGELALGPGVSICRDCLQFGVAVIDSQ 131
Cdd:smart00994   3 CSFCGKSESEVRKLIAGPGVYICDECVELCYEILEEE 39
 
Name Accession Description Interval E-value
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
 95-131 4.05e-07

ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the universally conserved Hsp100 family of proteins, and possesses a putative zinc finger motif of the C4 type. This presumed zinc binding domain is found at the N-terminus of the ClpX protein. ClpX is an ATPase which functions both as a substrate specificity component of the ClpXP protease and as a molecular chaperone. The molecular function of this domain is now known.


Pssm-ID: 198062 [Multi-domain]  Cd Length: 39  Bit Score: 43.71  E-value: 4.05e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 489485062    95 CSFCGKSKSDVGELALGPGVSICRDCLQFGVAVIDSQ 131
Cdd:smart00994   3 CSFCGKSESEVRKLIAGPGVYICDECVELCYEILEEE 39
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 95-120 5.48e-07

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 46.96  E-value: 5.48e-07
                         10        20
                 ....*....|....*....|....*.
gi 489485062  95 CSFCGKSKSDVGELALGPGVSICRDC 120
Cdd:COG1219   11 CSFCGKSQDEVRKLIAGPGVYICDEC 36
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
95-120 2.11e-06

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 45.53  E-value: 2.11e-06
                         10        20
                 ....*....|....*....|....*.
gi 489485062  95 CSFCGKSKSDVGELALGPGVSICRDC 120
Cdd:PRK05342  12 CSFCGKSQHEVRKLIAGPGVYICDEC 37
zf-C4_ClpX pfam06689
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
 95-129 3.17e-06

ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the universally conserved Hsp100 family of proteins, and possesses a putative zinc finger motif of the C4 type. This presumed zinc binding domain is found at the N-terminus of the ClpX protein. ClpX is an ATPase which functions both as a substrate specificity component of the ClpXP protease and as a molecular chaperone. The molecular function of this domain is now known.


Pssm-ID: 461988 [Multi-domain]  Cd Length: 39  Bit Score: 41.37  E-value: 3.17e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 489485062   95 CSFCGKSKSDVGELALGP-GVSICRDCLQFGVAVID 129
Cdd:pfam06689   3 CSFCGKSEDEVKKLIAGPnGVYICDECVELCYEILE 38
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 95-122 1.10e-05

endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent proteases, ClpX has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpPX. The gene is also found to be involved in stress tolerance in Bacillus subtilis and is essential for the efficient acquisition of genes specifying type IA and IB restriction. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273047 [Multi-domain]  Cd Length: 413  Bit Score: 43.22  E-value: 1.10e-05
                          10        20
                  ....*....|....*....|....*...
gi 489485062   95 CSFCGKSKSDVGELALGPGVSICRDCLQ 122
Cdd:TIGR00382  10 CSFCGKSQDEVRKLIAGPGVYICDECIE 37
 
Name Accession Description Interval E-value
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
 95-131 4.05e-07

ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the universally conserved Hsp100 family of proteins, and possesses a putative zinc finger motif of the C4 type. This presumed zinc binding domain is found at the N-terminus of the ClpX protein. ClpX is an ATPase which functions both as a substrate specificity component of the ClpXP protease and as a molecular chaperone. The molecular function of this domain is now known.


Pssm-ID: 198062 [Multi-domain]  Cd Length: 39  Bit Score: 43.71  E-value: 4.05e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 489485062    95 CSFCGKSKSDVGELALGPGVSICRDCLQFGVAVIDSQ 131
Cdd:smart00994   3 CSFCGKSESEVRKLIAGPGVYICDECVELCYEILEEE 39
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 95-120 5.48e-07

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 46.96  E-value: 5.48e-07
                         10        20
                 ....*....|....*....|....*.
gi 489485062  95 CSFCGKSKSDVGELALGPGVSICRDC 120
Cdd:COG1219   11 CSFCGKSQDEVRKLIAGPGVYICDEC 36
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
95-120 2.11e-06

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 45.53  E-value: 2.11e-06
                         10        20
                 ....*....|....*....|....*.
gi 489485062  95 CSFCGKSKSDVGELALGPGVSICRDC 120
Cdd:PRK05342  12 CSFCGKSQHEVRKLIAGPGVYICDEC 37
zf-C4_ClpX pfam06689
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
 95-129 3.17e-06

ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the universally conserved Hsp100 family of proteins, and possesses a putative zinc finger motif of the C4 type. This presumed zinc binding domain is found at the N-terminus of the ClpX protein. ClpX is an ATPase which functions both as a substrate specificity component of the ClpXP protease and as a molecular chaperone. The molecular function of this domain is now known.


Pssm-ID: 461988 [Multi-domain]  Cd Length: 39  Bit Score: 41.37  E-value: 3.17e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 489485062   95 CSFCGKSKSDVGELALGP-GVSICRDCLQFGVAVID 129
Cdd:pfam06689   3 CSFCGKSEDEVKKLIAGPnGVYICDECVELCYEILE 38
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 95-122 1.10e-05

endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent proteases, ClpX has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpPX. The gene is also found to be involved in stress tolerance in Bacillus subtilis and is essential for the efficient acquisition of genes specifying type IA and IB restriction. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273047 [Multi-domain]  Cd Length: 413  Bit Score: 43.22  E-value: 1.10e-05
                          10        20
                  ....*....|....*....|....*...
gi 489485062   95 CSFCGKSKSDVGELALGPGVSICRDCLQ 122
Cdd:TIGR00382  10 CSFCGKSQDEVRKLIAGPGVYICDECIE 37
 
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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