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Conserved domains on  [gi|490999963|ref|WP_004861686|]
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MULTISPECIES: nitrate reductase molybdenum cofactor assembly chaperone [Raoultella]

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
 1-231 1.97e-159

chaperone protein TorD; Validated


The actual alignment was detected with superfamily member PRK15054:

Pssm-ID: 470012  Cd Length: 231  Bit Score: 440.51  E-value: 1.97e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963   1 MRILKIIGLLLEYPDSLLWDNREEALELVRADAPALLPFVESLLAAPLLDRQAEWCEVFDRGRATSLLLFEHVHAESRDR 80
Cdd:PRK15054   1 MQILKVIGLLMEYPDELLWECKEDALALIRRDAPMLTDFTRNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963  81 GQAMVELMNQYEQAGLHIDCRELPDHLPLYLEYLSSLPPDDAREGLQNVAPILALLGGRVKQRQCQYYQLFDVLLALAGS 160
Cdd:PRK15054  81 GQAMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLAGS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999963 161 ALSSDSVTRQVAGEKRDDTRQALDAVWEEEQVKFIEDNATACDSSPMQHYQRRFSQDVAPQYVDVGAGGPK 231
Cdd:PRK15054 161 TLSSDSVTKQVNSEERDDTRQALDAVWEEEQVKFIEDNATACDSSPLNQYQRRFSQDVAPQYVDISAGGGK 231
 
Name Accession Description Interval E-value
PRK15054 PRK15054
nitrate reductase molybdenum cofactor assembly chaperone;
1-231 1.97e-159

nitrate reductase molybdenum cofactor assembly chaperone;


Pssm-ID: 185014  Cd Length: 231  Bit Score: 440.51  E-value: 1.97e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963   1 MRILKIIGLLLEYPDSLLWDNREEALELVRADAPALLPFVESLLAAPLLDRQAEWCEVFDRGRATSLLLFEHVHAESRDR 80
Cdd:PRK15054   1 MQILKVIGLLMEYPDELLWECKEDALALIRRDAPMLTDFTRNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963  81 GQAMVELMNQYEQAGLHIDCRELPDHLPLYLEYLSSLPPDDAREGLQNVAPILALLGGRVKQRQCQYYQLFDVLLALAGS 160
Cdd:PRK15054  81 GQAMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLAGS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999963 161 ALSSDSVTRQVAGEKRDDTRQALDAVWEEEQVKFIEDNATACDSSPMQHYQRRFSQDVAPQYVDVGAGGPK 231
Cdd:PRK15054 161 TLSSDSVTKQVNSEERDDTRQALDAVWEEEQVKFIEDNATACDSSPLNQYQRRFSQDVAPQYVDISAGGGK 231
NarJ COG2180
Nitrate reductase assembly protein NarJ, required for insertion of molybdenum cofactor [Energy ...
 1-174 4.77e-67

Nitrate reductase assembly protein NarJ, required for insertion of molybdenum cofactor [Energy production and conversion, Inorganic ion transport and metabolism, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441783  Cd Length: 181  Bit Score: 204.72  E-value: 4.77e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963   1 MRILKIIGLLLEYPDSLLWDNREEALELVR--ADAPALLPFVESLLAAPLLDRQAEWCEVFDRGRATSLLLFEHVHAESR 78
Cdd:COG2180    6 MKTLKALSLLLDYPDEELLAALPELRAALAeaAAREALAAFLDHLAALDLLDLQEEYVETFDRGRRTSLYLFEHVHGESR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963  79 DRGQAMVELMNQYEQAGLHIDCRELPDHLPLYLEYLSSLPPDDAREGLQNVAPILALLGGRVKQRQCQYYQLFDVLLALA 158
Cdd:COG2180   86 DRGQALVDLKELYRAAGLELDDGELPDYLPLVLEFLATLDPEEARALLGDIRHGLELLRARLEERGSPYAALFDALLALL 165

                        170
                 ....*....|....*.
gi 490999963 159 GSALSSDSVTRQVAGE 174
Cdd:COG2180  166 PAAAEAEAAVARLIAE 181
narJ TIGR00684
nitrate reductase molybdenum cofactor assembly chaperone; This protein is termed NarJ in most ...
 9-154 3.48e-39

nitrate reductase molybdenum cofactor assembly chaperone; This protein is termed NarJ in most species that have a single copy, and has been called the delta subunit of nitrate reductase. However, although it is required for correct assembly of active enzyme, it dissociates and is not part of the enzyme. Two hits to this model are found each in E. coli and in Mycobacterium tuberculosis, but in each case duplication to create paralogs appears to be recent. The NarX protein of Mycobacterium tuberculosis includes one of these paralogs as a domain, fused to structural domains of nitrate reductases before and after the NarJ-homologous region. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273218  Cd Length: 152  Bit Score: 132.65  E-value: 3.48e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963    9 LLLEYPDSLlWDNREEALELVRA-----DAPALLPFVESLLAAPLLDRQAEWCEVFDRGRATSLLLFEHVHAESRDRGQA 83
Cdd:TIGR00684   2 ILLSYPDED-LEELLRMREALKAlligeDAEALGLFMEFLEKLDPEAADAQYVETFDMGRKTSMYLTYLLKGEERMRGQE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999963   84 MVELMNQYEQAGLHIDCRELPDHLPLYLEYLSSLPPDDAR-EGLQNVAPILALLGGRVKQRQCQYYQLFDVL 154
Cdd:TIGR00684  81 MLELKSHYEQQGDMPVDRELPDYLPLMLEYLALVDPEAARrFAKKYLQPWVGELASRLEKNRSLYALLAKAL 152
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
 35-117 3.85e-08

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: 50.45  E-value: 3.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963   35 ALLPFVESLLAAPLLDR-QAEWCEVFDRGRATSLLLFEHVHAESRD--RGQAMVELMNQYEQAGLHI--DCRELPDHLPL 109
Cdd:pfam02613  11 ALAELAEALSREADLLElAAEYTRLFIGPGRPPASPYESVYLDERGllMGRPTLEVRAFYRAAGLEVaeELNEPPDHLAV 90


                  ....*...
gi 490999963  110 YLEYLSSL 117
Cdd:pfam02613  91 ELEFLAHL 98
 
Name Accession Description Interval E-value
PRK15054 PRK15054
nitrate reductase molybdenum cofactor assembly chaperone;
1-231 1.97e-159

nitrate reductase molybdenum cofactor assembly chaperone;


Pssm-ID: 185014  Cd Length: 231  Bit Score: 440.51  E-value: 1.97e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963   1 MRILKIIGLLLEYPDSLLWDNREEALELVRADAPALLPFVESLLAAPLLDRQAEWCEVFDRGRATSLLLFEHVHAESRDR 80
Cdd:PRK15054   1 MQILKVIGLLMEYPDELLWECKEDALALIRRDAPMLTDFTRNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963  81 GQAMVELMNQYEQAGLHIDCRELPDHLPLYLEYLSSLPPDDAREGLQNVAPILALLGGRVKQRQCQYYQLFDVLLALAGS 160
Cdd:PRK15054  81 GQAMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLAGS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490999963 161 ALSSDSVTRQVAGEKRDDTRQALDAVWEEEQVKFIEDNATACDSSPMQHYQRRFSQDVAPQYVDVGAGGPK 231
Cdd:PRK15054 161 TLSSDSVTKQVNSEERDDTRQALDAVWEEEQVKFIEDNATACDSSPLNQYQRRFSQDVAPQYVDISAGGGK 231
NarJ COG2180
Nitrate reductase assembly protein NarJ, required for insertion of molybdenum cofactor [Energy ...
 1-174 4.77e-67

Nitrate reductase assembly protein NarJ, required for insertion of molybdenum cofactor [Energy production and conversion, Inorganic ion transport and metabolism, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441783  Cd Length: 181  Bit Score: 204.72  E-value: 4.77e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963   1 MRILKIIGLLLEYPDSLLWDNREEALELVR--ADAPALLPFVESLLAAPLLDRQAEWCEVFDRGRATSLLLFEHVHAESR 78
Cdd:COG2180    6 MKTLKALSLLLDYPDEELLAALPELRAALAeaAAREALAAFLDHLAALDLLDLQEEYVETFDRGRRTSLYLFEHVHGESR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963  79 DRGQAMVELMNQYEQAGLHIDCRELPDHLPLYLEYLSSLPPDDAREGLQNVAPILALLGGRVKQRQCQYYQLFDVLLALA 158
Cdd:COG2180   86 DRGQALVDLKELYRAAGLELDDGELPDYLPLVLEFLATLDPEEARALLGDIRHGLELLRARLEERGSPYAALFDALLALL 165

                        170
                 ....*....|....*.
gi 490999963 159 GSALSSDSVTRQVAGE 174
Cdd:COG2180  166 PAAAEAEAAVARLIAE 181
narJ TIGR00684
nitrate reductase molybdenum cofactor assembly chaperone; This protein is termed NarJ in most ...
 9-154 3.48e-39

nitrate reductase molybdenum cofactor assembly chaperone; This protein is termed NarJ in most species that have a single copy, and has been called the delta subunit of nitrate reductase. However, although it is required for correct assembly of active enzyme, it dissociates and is not part of the enzyme. Two hits to this model are found each in E. coli and in Mycobacterium tuberculosis, but in each case duplication to create paralogs appears to be recent. The NarX protein of Mycobacterium tuberculosis includes one of these paralogs as a domain, fused to structural domains of nitrate reductases before and after the NarJ-homologous region. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273218  Cd Length: 152  Bit Score: 132.65  E-value: 3.48e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963    9 LLLEYPDSLlWDNREEALELVRA-----DAPALLPFVESLLAAPLLDRQAEWCEVFDRGRATSLLLFEHVHAESRDRGQA 83
Cdd:TIGR00684   2 ILLSYPDED-LEELLRMREALKAlligeDAEALGLFMEFLEKLDPEAADAQYVETFDMGRKTSMYLTYLLKGEERMRGQE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490999963   84 MVELMNQYEQAGLHIDCRELPDHLPLYLEYLSSLPPDDAR-EGLQNVAPILALLGGRVKQRQCQYYQLFDVL 154
Cdd:TIGR00684  81 MLELKSHYEQQGDMPVDRELPDYLPLMLEYLALVDPEAARrFAKKYLQPWVGELASRLEKNRSLYALLAKAL 152
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
 35-117 3.85e-08

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: 50.45  E-value: 3.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963   35 ALLPFVESLLAAPLLDR-QAEWCEVFDRGRATSLLLFEHVHAESRD--RGQAMVELMNQYEQAGLHI--DCRELPDHLPL 109
Cdd:pfam02613  11 ALAELAEALSREADLLElAAEYTRLFIGPGRPPASPYESVYLDERGllMGRPTLEVRAFYRAAGLEVaeELNEPPDHLAV 90


                  ....*...
gi 490999963  110 YLEYLSSL 117
Cdd:pfam02613  91 ELEFLAHL 98
TorD COG3381
Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational ...
 9-117 5.21e-05

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


Pssm-ID: 442608  Cd Length: 205  Bit Score: 42.73  E-value: 5.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999963   9 LLLEYPDSLLWDN-----REEALELVRADAPALLPFVESLLAAPLLDRQAEWCEVFDRGRATSLLLFE--HVHAESRDRG 81
Cdd:COG3381   21 LFYREPDEELLEAlasgeLLDDLPADEELAEALAALASAAAEDDLEELAAEYTRLFIGPGRPPAPPYEsvYLDEEGLLFG 100

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490999963  82 QAMVELMNQYEQAGLHI--DCRELPDHLPLYLEYLSSL 117
Cdd:COG3381  101 ESTLEVRAFYRALGLELdeDFKEPEDHIALELEFMAYL 138
 
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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