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Conserved domains on  [gi|1150940381|gb|OOO82011|]
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molecular chaperone TorD [Shigella boydii]

Protein Classification

molecular chaperone TorD( domain architecture ID 10012239)

molecular chaperone TorD is involved in the biogenesis of TorA, the terminal molybdoreductase in the reduction of trimethylamine N-oxide

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
torD PRK04976
chaperone protein TorD; Validated
1-199 2.34e-85

chaperone protein TorD; Validated


:

Pssm-ID: 235326  Cd Length: 202  Bit Score: 250.64  E-value: 2.34e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150940381   1 MTTLTAQQIACVYAWLAQLFSRELDDEQLTQIASAQMAEWFSLLKSEPPLTAAVDELENRVATLTVRDDARLELAADFCG 80
Cdd:PRK04976    3 MTTLTNEQRACVYAWLSSLFAKELDDEQLAQLQSAEFASFFALLASEPPLTASVNELQNALATLTDRDDAQLELAADFCG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150940381  81 LFLMTDKQAALPYVSAYKQDE-------QEIKRLLVEAGMETSGNFNEPADHLAIYLELLSHLHFSLGEgtvpARRIDSL 153
Cdd:PRK04976   83 LFLLTDKHSALPYASAYLQEGllfgephQEMKELLVEAGLQVNSDFNEPADHLAVYLELLSHLIFSSGE----RQQLLFI 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1150940381 154 RQktltALRQWLPEFVARCHQYDSFGFYAALSQLLLVLVEGDHQNR 199
Cdd:PRK04976  159 QT----ALLSWLPEFAAKCTQYDSFGFYAALSQLLLAFVQLDHQNL 200
 
Name Accession Description Interval E-value
torD PRK04976
chaperone protein TorD; Validated
1-199 2.34e-85

chaperone protein TorD; Validated


Pssm-ID: 235326  Cd Length: 202  Bit Score: 250.64  E-value: 2.34e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150940381   1 MTTLTAQQIACVYAWLAQLFSRELDDEQLTQIASAQMAEWFSLLKSEPPLTAAVDELENRVATLTVRDDARLELAADFCG 80
Cdd:PRK04976    3 MTTLTNEQRACVYAWLSSLFAKELDDEQLAQLQSAEFASFFALLASEPPLTASVNELQNALATLTDRDDAQLELAADFCG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150940381  81 LFLMTDKQAALPYVSAYKQDE-------QEIKRLLVEAGMETSGNFNEPADHLAIYLELLSHLHFSLGEgtvpARRIDSL 153
Cdd:PRK04976   83 LFLLTDKHSALPYASAYLQEGllfgephQEMKELLVEAGLQVNSDFNEPADHLAVYLELLSHLIFSSGE----RQQLLFI 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1150940381 154 RQktltALRQWLPEFVARCHQYDSFGFYAALSQLLLVLVEGDHQNR 199
Cdd:PRK04976  159 QT----ALLSWLPEFAAKCTQYDSFGFYAALSQLLLAFVQLDHQNL 200
TorD COG3381
Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational ...
2-197 3.22e-31

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


Pssm-ID: 442608  Cd Length: 205  Bit Score: 112.45  E-value: 3.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150940381   2 TTLTAQQIACVYAWLAQLFSRELDDEQLTQIASAqmaEWFSLLKSEPPLTAAVDELENRVatltvRDDARLELAADFCGL 81
Cdd:COG3381     4 TTAELEARAALYRLLARLFYREPDEELLEALASG---ELLDDLPADEELAEALAALASAA-----AEDDLEELAAEYTRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150940381  82 FLMTDKQAALPYVSAYKQDE--------QEIKRLLVEAGMETSGNFNEPADHLAIYLELLSHLhfsLGEGTVPARRIDSL 153
Cdd:COG3381    76 FIGPGRPPAPPYESVYLDEEgllfgestLEVRAFYRALGLELDEDFKEPEDHIALELEFMAYL---AEREAEALELLEAQ 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1150940381 154 RQKTLTALRQWLPEFVARCHQYDSFGFYAALSQLLLVLVEGDHQ 197
Cdd:COG3381   153 REFLEEHLLPWAPRFLDDLEAHAETPFYRALAELLRAFLEADRE 196
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
47-170 2.63e-23

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: 90.13  E-value: 2.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150940381  47 EPPLTAAVDELENRVATLTVRDDARLELAADFCGLFLMTDKQAALPYVSAYKQDE--------QEIKRLLVEAGMETSGN 118
Cdd:pfam02613   1 EPALDAGLAEALAELAEALSREADLLELAAEYTRLFIGPGRPPASPYESVYLDERgllmgrptLEVRAFYRAAGLEVAEE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1150940381 119 FNEPADHLAIYLELLSHLHFSLGEGTVPAR---RIDSLRQKTLTALRQWLPEFVA 170
Cdd:pfam02613  81 LNEPPDHLAVELEFLAHLAERAAEALEAAEaeaLLAAQRAFLEEHLLPWVPRFAA 135
 
Name Accession Description Interval E-value
torD PRK04976
chaperone protein TorD; Validated
1-199 2.34e-85

chaperone protein TorD; Validated


Pssm-ID: 235326  Cd Length: 202  Bit Score: 250.64  E-value: 2.34e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150940381   1 MTTLTAQQIACVYAWLAQLFSRELDDEQLTQIASAQMAEWFSLLKSEPPLTAAVDELENRVATLTVRDDARLELAADFCG 80
Cdd:PRK04976    3 MTTLTNEQRACVYAWLSSLFAKELDDEQLAQLQSAEFASFFALLASEPPLTASVNELQNALATLTDRDDAQLELAADFCG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150940381  81 LFLMTDKQAALPYVSAYKQDE-------QEIKRLLVEAGMETSGNFNEPADHLAIYLELLSHLHFSLGEgtvpARRIDSL 153
Cdd:PRK04976   83 LFLLTDKHSALPYASAYLQEGllfgephQEMKELLVEAGLQVNSDFNEPADHLAVYLELLSHLIFSSGE----RQQLLFI 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1150940381 154 RQktltALRQWLPEFVARCHQYDSFGFYAALSQLLLVLVEGDHQNR 199
Cdd:PRK04976  159 QT----ALLSWLPEFAAKCTQYDSFGFYAALSQLLLAFVQLDHQNL 200
TorD COG3381
Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational ...
2-197 3.22e-31

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


Pssm-ID: 442608  Cd Length: 205  Bit Score: 112.45  E-value: 3.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150940381   2 TTLTAQQIACVYAWLAQLFSRELDDEQLTQIASAqmaEWFSLLKSEPPLTAAVDELENRVatltvRDDARLELAADFCGL 81
Cdd:COG3381     4 TTAELEARAALYRLLARLFYREPDEELLEALASG---ELLDDLPADEELAEALAALASAA-----AEDDLEELAAEYTRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150940381  82 FLMTDKQAALPYVSAYKQDE--------QEIKRLLVEAGMETSGNFNEPADHLAIYLELLSHLhfsLGEGTVPARRIDSL 153
Cdd:COG3381    76 FIGPGRPPAPPYESVYLDEEgllfgestLEVRAFYRALGLELDEDFKEPEDHIALELEFMAYL---AEREAEALELLEAQ 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1150940381 154 RQKTLTALRQWLPEFVARCHQYDSFGFYAALSQLLLVLVEGDHQ 197
Cdd:COG3381   153 REFLEEHLLPWAPRFLDDLEAHAETPFYRALAELLRAFLEADRE 196
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
47-170 2.63e-23

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: 90.13  E-value: 2.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150940381  47 EPPLTAAVDELENRVATLTVRDDARLELAADFCGLFLMTDKQAALPYVSAYKQDE--------QEIKRLLVEAGMETSGN 118
Cdd:pfam02613   1 EPALDAGLAEALAELAEALSREADLLELAAEYTRLFIGPGRPPASPYESVYLDERgllmgrptLEVRAFYRAAGLEVAEE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1150940381 119 FNEPADHLAIYLELLSHLHFSLGEGTVPAR---RIDSLRQKTLTALRQWLPEFVA 170
Cdd:pfam02613  81 LNEPPDHLAVELEFLAHLAERAAEALEAAEaeaLLAAQRAFLEEHLLPWVPRFAA 135
 
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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