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Conserved domains on  [gi|496059565|ref|WP_008784072|]
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MULTISPECIES: molecular chaperone [Citrobacter]

Protein Classification

molecular chaperone( domain architecture ID 10007290)

molecular chaperone such as redox enzyme maturation protein (REMP) which is system-specific chaperones required for the maturation of complex iron sulfur molybdoenzymes.

Gene Ontology:  GO:0061077
PubMed:  23746257

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TorD COG3381
Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational ...
 30-178 3.90e-26

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


:

Pssm-ID: 442608  Cd Length: 205  Bit Score: 98.97  E-value: 3.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059565  30 LKAAYSALDTNASTLTEQEwLEAEYdfNALFVGPQTLKAPPFASVYLEEDALVMGKSTLSIREFMANIGLSINHVNNIPD 109
Cdd:COG3381   49 LAEALAALASAAAEDDLEE-LAAEY--TRLFIGPGRPPAPPYESVYLDEEGLLFGESTLEVRAFYRALGLELDEDFKEPE 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059565 110 DHISCVLELAVLLSANARISAEYQIVMTRYVIEYIAMWMPAYIEKIHINAQTVTLKNVAERLSFWLDEL 178
Cdd:COG3381  126 DHIALELEFMAYLAEREAEALELLEAQREFLEEHLLPWAPRFLDDLEAHAETPFYRALAELLRAFLEAD 194
 
Name Accession Description Interval E-value
TorD COG3381
Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational ...
 30-178 3.90e-26

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


Pssm-ID: 442608  Cd Length: 205  Bit Score: 98.97  E-value: 3.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059565  30 LKAAYSALDTNASTLTEQEwLEAEYdfNALFVGPQTLKAPPFASVYLEEDALVMGKSTLSIREFMANIGLSINHVNNIPD 109
Cdd:COG3381   49 LAEALAALASAAAEDDLEE-LAAEY--TRLFIGPGRPPAPPYESVYLDEEGLLFGESTLEVRAFYRALGLELDEDFKEPE 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059565 110 DHISCVLELAVLLSANARISAEYQIVMTRYVIEYIAMWMPAYIEKIHINAQTVTLKNVAERLSFWLDEL 178
Cdd:COG3381  126 DHIALELEFMAYLAEREAEALELLEAQREFLEEHLLPWAPRFLDDLEAHAETPFYRALAELLRAFLEAD 194
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
 30-153 7.25e-20

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: 80.89  E-value: 7.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059565   30 LKAAYSALDTNASTLTEQEWLEAEYdfNALFVGPQTLKAPPFASVYLEEDALVMGKSTLSIREFMANIGLSINHVNNIPD 109
Cdd:pfam02613   8 LAEALAELAEALSREADLLELAAEY--TRLFIGPGRPPASPYESVYLDERGLLMGRPTLEVRAFYRAAGLEVAEELNEPP 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 496059565  110 DHISCVLELAVLLS---ANARISAEYQIVMTRYVI---EYIAMWMPAYIE 153
Cdd:pfam02613  86 DHLAVELEFLAHLAeraAEALEAAEAEALLAAQRAfleEHLLPWVPRFAA 135
PRK11621 PRK11621
Tat proofreading chaperone DmsD;
59-127 8.02e-14

Tat proofreading chaperone DmsD;


Pssm-ID: 236938  Cd Length: 204  Bit Score: 66.56  E-value: 8.02e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059565  59 LFVGPQTLKAPPFASVYLEEDALVMGKSTLSIREFMANIGLSINHVNNIPDDHISCVLELAVLLSANAR 127
Cdd:PRK11621  75 LFIGPWALPAPPWGSVWLDRESVLFGDSTLALRQWMRENGIQFEMKQNEPEDHFGLLLLLAAWLAENGR 143
 
Name Accession Description Interval E-value
TorD COG3381
Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational ...
 30-178 3.90e-26

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


Pssm-ID: 442608  Cd Length: 205  Bit Score: 98.97  E-value: 3.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059565  30 LKAAYSALDTNASTLTEQEwLEAEYdfNALFVGPQTLKAPPFASVYLEEDALVMGKSTLSIREFMANIGLSINHVNNIPD 109
Cdd:COG3381   49 LAEALAALASAAAEDDLEE-LAAEY--TRLFIGPGRPPAPPYESVYLDEEGLLFGESTLEVRAFYRALGLELDEDFKEPE 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059565 110 DHISCVLELAVLLSANARISAEYQIVMTRYVIEYIAMWMPAYIEKIHINAQTVTLKNVAERLSFWLDEL 178
Cdd:COG3381  126 DHIALELEFMAYLAEREAEALELLEAQREFLEEHLLPWAPRFLDDLEAHAETPFYRALAELLRAFLEAD 194
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
 30-153 7.25e-20

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: 80.89  E-value: 7.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059565   30 LKAAYSALDTNASTLTEQEWLEAEYdfNALFVGPQTLKAPPFASVYLEEDALVMGKSTLSIREFMANIGLSINHVNNIPD 109
Cdd:pfam02613   8 LAEALAELAEALSREADLLELAAEY--TRLFIGPGRPPASPYESVYLDERGLLMGRPTLEVRAFYRAAGLEVAEELNEPP 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 496059565  110 DHISCVLELAVLLS---ANARISAEYQIVMTRYVI---EYIAMWMPAYIE 153
Cdd:pfam02613  86 DHLAVELEFLAHLAeraAEALEAAEAEALLAAQRAfleEHLLPWVPRFAA 135
PRK11621 PRK11621
Tat proofreading chaperone DmsD;
59-127 8.02e-14

Tat proofreading chaperone DmsD;


Pssm-ID: 236938  Cd Length: 204  Bit Score: 66.56  E-value: 8.02e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059565  59 LFVGPQTLKAPPFASVYLEEDALVMGKSTLSIREFMANIGLSINHVNNIPDDHISCVLELAVLLSANAR 127
Cdd:PRK11621  75 LFIGPWALPAPPWGSVWLDRESVLFGDSTLALRQWMRENGIQFEMKQNEPEDHFGLLLLLAAWLAENGR 143
torD PRK04976
chaperone protein TorD; Validated
 30-156 9.54e-06

chaperone protein TorD; Validated


Pssm-ID: 235326  Cd Length: 202  Bit Score: 44.18  E-value: 9.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059565  30 LKAAYSALDTNASTLTEQE--WLEAEYDFNALFVGPQTLKAPPFASVYLEEDALvMGKSTLSIREFMANIGLSINHVNNI 107
Cdd:PRK04976  52 LTASVNELQNALATLTDRDdaQLELAADFCGLFLLTDKHSALPYASAYLQEGLL-FGEPHQEMKELLVEAGLQVNSDFNE 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 496059565 108 PDDHISCVLELAvllsANARISAEyQIVMTRYVIEYIAMWMPAYIEKIH 156
Cdd:PRK04976 131 PADHLAVYLELL----SHLIFSSG-ERQQLLFIQTALLSWLPEFAAKCT 174
 
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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