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Conserved domains on  [gi|518684868|ref|WP_019846561|]
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Tat proofreading chaperone DmsD [Dickeya zeae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
torD super family cl00958
chaperone protein TorD; Validated
6-203 2.26e-77

chaperone protein TorD; Validated


The actual alignment was detected with superfamily member PRK11621:

Pssm-ID: 470012  Cd Length: 204  Bit Score: 230.66  E-value: 2.26e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518684868   6 VSLTGRLLGALLYYAPDDEHNVALIERLRHSAWQQTWPCGnqadiAIVARQIYSGLQPGYDERLSLAWKRWLSGDEGMPV 85
Cdd:PRK11621  10 ISVTARVLGALFYYAPESAEAAPLVAFLRQDDWETEWPLD-----AASLAPIAALFATGSEETLAQAWQRLFIGPWALPA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518684868  86 PPWGSVYLDRQNVLFGDSTLALRRWLRELGIEPRCDRHEPEDHIGLMLMLAAWCAEN-QPDNLPELLSEHLLPWAMRYLD 164
Cdd:PRK11621  85 PPWGSVWLDRESVLFGDSTLALRQWMRENGIQFEMKQNEPEDHFGLLLLLAAWLAENgRPTELEELLAWHLLPWSYRFLD 164
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 518684868 165 LLERHCCHPFYQGVARLTHITLQDWQGRFQLIQKEKALF 203
Cdd:PRK11621 165 VFIEQAGHPFYQALAQLARLTLAQWQSQLLIPVAVKPLY 203
 
Name Accession Description Interval E-value
PRK11621 PRK11621
Tat proofreading chaperone DmsD;
6-203 2.26e-77

Tat proofreading chaperone DmsD;


Pssm-ID: 236938  Cd Length: 204  Bit Score: 230.66  E-value: 2.26e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518684868   6 VSLTGRLLGALLYYAPDDEHNVALIERLRHSAWQQTWPCGnqadiAIVARQIYSGLQPGYDERLSLAWKRWLSGDEGMPV 85
Cdd:PRK11621  10 ISVTARVLGALFYYAPESAEAAPLVAFLRQDDWETEWPLD-----AASLAPIAALFATGSEETLAQAWQRLFIGPWALPA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518684868  86 PPWGSVYLDRQNVLFGDSTLALRRWLRELGIEPRCDRHEPEDHIGLMLMLAAWCAEN-QPDNLPELLSEHLLPWAMRYLD 164
Cdd:PRK11621  85 PPWGSVWLDRESVLFGDSTLALRQWMRENGIQFEMKQNEPEDHFGLLLLLAAWLAENgRPTELEELLAWHLLPWSYRFLD 164
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 518684868 165 LLERHCCHPFYQGVARLTHITLQDWQGRFQLIQKEKALF 203
Cdd:PRK11621 165 VFIEQAGHPFYQALAQLARLTLAQWQSQLLIPVAVKPLY 203
TorD COG3381
Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational ...
7-200 4.31e-51

Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442608  Cd Length: 205  Bit Score: 163.68  E-value: 4.31e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518684868   7 SLTGRLLGALLYYAPDDEhnvaLIERLRHSAWQQTWPCGNQADIAIvaRQIYSGLQPGYDERLSLAWKRWLSGDEGMPVP 86
Cdd:COG3381   12 AALYRLLARLFYREPDEE----LLEALASGELLDDLPADEELAEAL--AALASAAAEDDLEELAAEYTRLFIGPGRPPAP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518684868  87 PWGSVYLDRQNVLFGDSTLALRRWLRELGIEPRCDRHEPEDHIGLMLMLAAWCAENQPDNLP------ELLSEHLLPWAM 160
Cdd:COG3381   86 PYESVYLDEEGLLFGESTLEVRAFYRALGLELDEDFKEPEDHIALELEFMAYLAEREAEALElleaqrEFLEEHLLPWAP 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 518684868 161 RYLDLLERHCCHPFYQGVARLTHITLQDWQGRFQLIQKEK 200
Cdd:COG3381  166 RFLDDLEAHAETPFYRALAELLRAFLEADREELEELLEEA 205
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
79-159 1.10e-17

Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase enzyme, The delta subunit is not part of the nitrate reductase enzyme but is most likely needed for assembly of the multi-subunit enzyme complex. In the absence of the delta subunit the core alpha beta enzyme complex is unstable. The delta subunit is essential for enzyme activity in vivo and in vitro. The nitrate reductase enzyme, EC:1.7.99.4 catalyze the conversion of nitrite to nitrate via the reduction of an acceptor. The nitrate reductase enzyme is composed of three subunits. Nitrate is the most widely used alternative electron acceptor after oxygen. This family also now contains the family TorD, a family of cytoplasmic chaperone proteins; like many prokaryotic molybdoenzymes, the TMAO reductase (TorA) of Escherichia coli requires the insertion of a bis(molybdopterin guanine dinucleotide) molybdenum (bis(MGD)Mo) cofactor in its catalytic site to be active and translocated to the periplasm. The TorD chaperone increases apoTorA activation up to four-fold, allowing maturation of most of the apoprotein. Therefore TorD is involved in the first step of TorA maturation to make it competent to receive the cofactor.


Pssm-ID: 460619 [Multi-domain]  Cd Length: 135  Bit Score: 75.49  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518684868   79 GDEGMPVPPWGSVYLDRQNVLFGDSTLALRRWLRELGIEPRCDRHEPEDHIGLMLMLAA---------WCAENQPDNLP- 148
Cdd:pfam02613  38 GPGRPPASPYESVYLDERGLLMGRPTLEVRAFYRAAGLEVAEELNEPPDHLAVELEFLAhlaeraaeaLEAAEAEALLAa 117
                          90
                  ....*....|...
gi 518684868  149 --ELLSEHLLPWA 159
Cdd:pfam02613 118 qrAFLEEHLLPWV 130
 
Name Accession Description Interval E-value
PRK11621 PRK11621
Tat proofreading chaperone DmsD;
6-203 2.26e-77

Tat proofreading chaperone DmsD;


Pssm-ID: 236938  Cd Length: 204  Bit Score: 230.66  E-value: 2.26e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518684868   6 VSLTGRLLGALLYYAPDDEHNVALIERLRHSAWQQTWPCGnqadiAIVARQIYSGLQPGYDERLSLAWKRWLSGDEGMPV 85
Cdd:PRK11621  10 ISVTARVLGALFYYAPESAEAAPLVAFLRQDDWETEWPLD-----AASLAPIAALFATGSEETLAQAWQRLFIGPWALPA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518684868  86 PPWGSVYLDRQNVLFGDSTLALRRWLRELGIEPRCDRHEPEDHIGLMLMLAAWCAEN-QPDNLPELLSEHLLPWAMRYLD 164
Cdd:PRK11621  85 PPWGSVWLDRESVLFGDSTLALRQWMRENGIQFEMKQNEPEDHFGLLLLLAAWLAENgRPTELEELLAWHLLPWSYRFLD 164
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 518684868 165 LLERHCCHPFYQGVARLTHITLQDWQGRFQLIQKEKALF 203
Cdd:PRK11621 165 VFIEQAGHPFYQALAQLARLTLAQWQSQLLIPVAVKPLY 203
TorD COG3381
Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational ...
7-200 4.31e-51

Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442608  Cd Length: 205  Bit Score: 163.68  E-value: 4.31e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518684868   7 SLTGRLLGALLYYAPDDEhnvaLIERLRHSAWQQTWPCGNQADIAIvaRQIYSGLQPGYDERLSLAWKRWLSGDEGMPVP 86
Cdd:COG3381   12 AALYRLLARLFYREPDEE----LLEALASGELLDDLPADEELAEAL--AALASAAAEDDLEELAAEYTRLFIGPGRPPAP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518684868  87 PWGSVYLDRQNVLFGDSTLALRRWLRELGIEPRCDRHEPEDHIGLMLMLAAWCAENQPDNLP------ELLSEHLLPWAM 160
Cdd:COG3381   86 PYESVYLDEEGLLFGESTLEVRAFYRALGLELDEDFKEPEDHIALELEFMAYLAEREAEALElleaqrEFLEEHLLPWAP 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 518684868 161 RYLDLLERHCCHPFYQGVARLTHITLQDWQGRFQLIQKEK 200
Cdd:COG3381  166 RFLDDLEAHAETPFYRALAELLRAFLEADREELEELLEEA 205
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
79-159 1.10e-17

Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase enzyme, The delta subunit is not part of the nitrate reductase enzyme but is most likely needed for assembly of the multi-subunit enzyme complex. In the absence of the delta subunit the core alpha beta enzyme complex is unstable. The delta subunit is essential for enzyme activity in vivo and in vitro. The nitrate reductase enzyme, EC:1.7.99.4 catalyze the conversion of nitrite to nitrate via the reduction of an acceptor. The nitrate reductase enzyme is composed of three subunits. Nitrate is the most widely used alternative electron acceptor after oxygen. This family also now contains the family TorD, a family of cytoplasmic chaperone proteins; like many prokaryotic molybdoenzymes, the TMAO reductase (TorA) of Escherichia coli requires the insertion of a bis(molybdopterin guanine dinucleotide) molybdenum (bis(MGD)Mo) cofactor in its catalytic site to be active and translocated to the periplasm. The TorD chaperone increases apoTorA activation up to four-fold, allowing maturation of most of the apoprotein. Therefore TorD is involved in the first step of TorA maturation to make it competent to receive the cofactor.


Pssm-ID: 460619 [Multi-domain]  Cd Length: 135  Bit Score: 75.49  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518684868   79 GDEGMPVPPWGSVYLDRQNVLFGDSTLALRRWLRELGIEPRCDRHEPEDHIGLMLMLAA---------WCAENQPDNLP- 148
Cdd:pfam02613  38 GPGRPPASPYESVYLDERGLLMGRPTLEVRAFYRAAGLEVAEELNEPPDHLAVELEFLAhlaeraaeaLEAAEAEALLAa 117
                          90
                  ....*....|...
gi 518684868  149 --ELLSEHLLPWA 159
Cdd:pfam02613 118 qrAFLEEHLLPWV 130
torD PRK04976
chaperone protein TorD; Validated
87-187 7.77e-07

chaperone protein TorD; Validated


Pssm-ID: 235326  Cd Length: 202  Bit Score: 47.64  E-value: 7.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518684868  87 PWGSVYLDrQNVLFGDSTLALRRWLRELGIEPRCDRHEPEDHIGLMLMLAAWCAENQPDNLP-ELLSEHLLPWAMRYLDL 165
Cdd:PRK04976  94 PYASAYLQ-EGLLFGEPHQEMKELLVEAGLQVNSDFNEPADHLAVYLELLSHLIFSSGERQQlLFIQTALLSWLPEFAAK 172
                         90       100
                 ....*....|....*....|..
gi 518684868 166 LERHCCHPFYQGVARLTHITLQ 187
Cdd:PRK04976 173 CTQYDSFGFYAALSQLLLAFVQ 194
 
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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