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Conserved domains on  [gi|517913675|ref|WP_019083883|]
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Tat proofreading chaperone DmsD [Yersinia enterocolitica]

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
4-201 1.10e-95

chaperone protein TorD; Validated


The actual alignment was detected with superfamily member PRK11621:

Pssm-ID: 470012  Cd Length: 204  Bit Score: 276.88  E-value: 1.10e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675   4 QQIALTGRVLGALFYCEPDSPACHDIVAQLSHGLWAAQWPYGSEQQRlAIAALLAQSvTEETREEAWQRLFIGPYALPAP 83
Cdd:PRK11621   8 DNISVTARVLGALFYYAPESAEAAPLVAFLRQDDWETEWPLDAASLA-PIAALFATG-SEETLAQAWQRLFIGPWALPAP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675  84 PWGSVYLDKENVLFGDSTLKLRHWMAQQQVEVTLDQDEPEDQFGLMLMMAAWLAEH-QPAGLPELLADHLLPWGYRYLAL 162
Cdd:PRK11621  86 PWGSVWLDRESVLFGDSTLALRQWMRENGIQFEMKQNEPEDHFGLLLLLAAWLAENgRPTELEELLAWHLLPWSYRFLDV 165
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 517913675 163 LQSDAGHPFYQGLAQLATLTLTHWQDELQVTPALVELYR 201
Cdd:PRK11621 166 FIEQAGHPFYQALAQLARLTLAQWQSQLLIPVAVKPLYR 204
 
Name Accession Description Interval E-value
PRK11621 PRK11621
Tat proofreading chaperone DmsD;
4-201 1.10e-95

Tat proofreading chaperone DmsD;


Pssm-ID: 236938  Cd Length: 204  Bit Score: 276.88  E-value: 1.10e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675   4 QQIALTGRVLGALFYCEPDSPACHDIVAQLSHGLWAAQWPYGSEQQRlAIAALLAQSvTEETREEAWQRLFIGPYALPAP 83
Cdd:PRK11621   8 DNISVTARVLGALFYYAPESAEAAPLVAFLRQDDWETEWPLDAASLA-PIAALFATG-SEETLAQAWQRLFIGPWALPAP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675  84 PWGSVYLDKENVLFGDSTLKLRHWMAQQQVEVTLDQDEPEDQFGLMLMMAAWLAEH-QPAGLPELLADHLLPWGYRYLAL 162
Cdd:PRK11621  86 PWGSVWLDRESVLFGDSTLALRQWMRENGIQFEMKQNEPEDHFGLLLLLAAWLAENgRPTELEELLAWHLLPWSYRFLDV 165
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 517913675 163 LQSDAGHPFYQGLAQLATLTLTHWQDELQVTPALVELYR 201
Cdd:PRK11621 166 FIEQAGHPFYQALAQLARLTLAQWQSQLLIPVAVKPLYR 204
TorD COG3381
Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational ...
2-195 2.68e-51

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


Pssm-ID: 442608  Cd Length: 205  Bit Score: 164.07  E-value: 2.68e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675   2 IYQQIALTGRVLGALFYCEPDSpachDIVAQLSHGLWAAQWPYGSEQQrlAIAALLAQSVTEETREE---AWQRLFIGPY 78
Cdd:COG3381    7 ELEARAALYRLLARLFYREPDE----ELLEALASGELLDDLPADEELA--EALAALASAAAEDDLEElaaEYTRLFIGPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675  79 ALPAPPWGSVYLDKENVLFGDSTLKLRHWMAQQQVEVTLDQDEPEDQFGLMLMMAAWLAEHQPAGLP------ELLADHL 152
Cdd:COG3381   81 RPPAPPYESVYLDEEGLLFGESTLEVRAFYRALGLELDEDFKEPEDHIALELEFMAYLAEREAEALElleaqrEFLEEHL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 517913675 153 LPWGYRYLALLQSDAGHPFYQGLAQLATLTLTHWQDELQVTPA 195
Cdd:COG3381  161 LPWAPRFLDDLEAHAETPFYRALAELLRAFLEADREELEELLE 203
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
40-155 1.04e-18

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: 78.19  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675   40 AQWPYGSEQQRLAIAALLAQSVTEETREEAWQRLFIGPYALPAPPWGSVYLDKENVLFGDSTLKLRHWMAQQQVEVTLDQ 119
Cdd:pfam02613   2 PALDAGLAEALAELAEALSREADLLELAAEYTRLFIGPGRPPASPYESVYLDERGLLMGRPTLEVRAFYRAAGLEVAEEL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 517913675  120 DEPEDQFGLMLMMAAWLAEHQPAGLP------------ELLADHLLPW 155
Cdd:pfam02613  82 NEPPDHLAVELEFLAHLAERAAEALEaaeaeallaaqrAFLEEHLLPW 129
 
Name Accession Description Interval E-value
PRK11621 PRK11621
Tat proofreading chaperone DmsD;
4-201 1.10e-95

Tat proofreading chaperone DmsD;


Pssm-ID: 236938  Cd Length: 204  Bit Score: 276.88  E-value: 1.10e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675   4 QQIALTGRVLGALFYCEPDSPACHDIVAQLSHGLWAAQWPYGSEQQRlAIAALLAQSvTEETREEAWQRLFIGPYALPAP 83
Cdd:PRK11621   8 DNISVTARVLGALFYYAPESAEAAPLVAFLRQDDWETEWPLDAASLA-PIAALFATG-SEETLAQAWQRLFIGPWALPAP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675  84 PWGSVYLDKENVLFGDSTLKLRHWMAQQQVEVTLDQDEPEDQFGLMLMMAAWLAEH-QPAGLPELLADHLLPWGYRYLAL 162
Cdd:PRK11621  86 PWGSVWLDRESVLFGDSTLALRQWMRENGIQFEMKQNEPEDHFGLLLLLAAWLAENgRPTELEELLAWHLLPWSYRFLDV 165
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 517913675 163 LQSDAGHPFYQGLAQLATLTLTHWQDELQVTPALVELYR 201
Cdd:PRK11621 166 FIEQAGHPFYQALAQLARLTLAQWQSQLLIPVAVKPLYR 204
TorD COG3381
Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational ...
2-195 2.68e-51

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


Pssm-ID: 442608  Cd Length: 205  Bit Score: 164.07  E-value: 2.68e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675   2 IYQQIALTGRVLGALFYCEPDSpachDIVAQLSHGLWAAQWPYGSEQQrlAIAALLAQSVTEETREE---AWQRLFIGPY 78
Cdd:COG3381    7 ELEARAALYRLLARLFYREPDE----ELLEALASGELLDDLPADEELA--EALAALASAAAEDDLEElaaEYTRLFIGPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675  79 ALPAPPWGSVYLDKENVLFGDSTLKLRHWMAQQQVEVTLDQDEPEDQFGLMLMMAAWLAEHQPAGLP------ELLADHL 152
Cdd:COG3381   81 RPPAPPYESVYLDEEGLLFGESTLEVRAFYRALGLELDEDFKEPEDHIALELEFMAYLAEREAEALElleaqrEFLEEHL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 517913675 153 LPWGYRYLALLQSDAGHPFYQGLAQLATLTLTHWQDELQVTPA 195
Cdd:COG3381  161 LPWAPRFLDDLEAHAETPFYRALAELLRAFLEADREELEELLE 203
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
40-155 1.04e-18

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: 78.19  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675   40 AQWPYGSEQQRLAIAALLAQSVTEETREEAWQRLFIGPYALPAPPWGSVYLDKENVLFGDSTLKLRHWMAQQQVEVTLDQ 119
Cdd:pfam02613   2 PALDAGLAEALAELAEALSREADLLELAAEYTRLFIGPGRPPASPYESVYLDERGLLMGRPTLEVRAFYRAAGLEVAEEL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 517913675  120 DEPEDQFGLMLMMAAWLAEHQPAGLP------------ELLADHLLPW 155
Cdd:pfam02613  82 NEPPDHLAVELEFLAHLAERAAEALEaaeaeallaaqrAFLEEHLLPW 129
torD PRK04976
chaperone protein TorD; Validated
4-178 1.18e-04

chaperone protein TorD; Validated


Pssm-ID: 235326  Cd Length: 202  Bit Score: 41.48  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675   4 QQIALTGRVLGALFYCEPDspacHDIVAQLSHGLWAAQWPYGSEQQRL--AIAALLAQSVTEETREEA-------WQRLF 74
Cdd:PRK04976   9 EQRACVYAWLSSLFAKELD----DEQLAQLQSAEFASFFALLASEPPLtaSVNELQNALATLTDRDDAqlelaadFCGLF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517913675  75 IGPYALPAPPWGSVYLDKEnVLFGDSTLKLRHWMAQQQVEVTLDQDEPEDQFGLMLMMAAWLAEHQP-AGLPELLADHLL 153
Cdd:PRK04976  85 LLTDKHSALPYASAYLQEG-LLFGEPHQEMKELLVEAGLQVNSDFNEPADHLAVYLELLSHLIFSSGeRQQLLFIQTALL 163
                        170       180
                 ....*....|....*....|....*
gi 517913675 154 PWGYRYLALLQSDAGHPFYQGLAQL 178
Cdd:PRK04976 164 SWLPEFAAKCTQYDSFGFYAALSQL 188
 
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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