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Conserved domains on  [gi|447089093|ref|WP_001166349|]
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MULTISPECIES: nitrate reductase molybdenum cofactor assembly chaperone [Enterobacteriaceae]

Protein Classification

nitrate reductase molybdenum cofactor assembly chaperone( domain architecture ID 10014953)

nitrate reductase molybdenum cofactor assembly chaperone similar to Escherichia coli Redox enzyme maturation protein NarW that is required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15054 PRK15054
nitrate reductase molybdenum cofactor assembly chaperone;
1-231 3.18e-170

nitrate reductase molybdenum cofactor assembly chaperone;


:

Pssm-ID: 185014  Cd Length: 231  Bit Score: 467.86  E-value: 3.18e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093   1 MQILKVIGLLMEYPDELLWECKEDALALIRRDAPMLTDFTHNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDR 80
Cdd:PRK15054   1 MQILKVIGLLMEYPDELLWECKEDALALIRRDAPMLTDFTRNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093  81 GQAMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLAGS 160
Cdd:PRK15054  81 GQAMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLAGS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447089093 161 ILSSDSVTKQVNSEERDDTRQALDAVWEEEQVKFIEDNATACDSSPLNQYQRRFSQDVAPQYVDISAGGGK 231
Cdd:PRK15054 161 TLSSDSVTKQVNSEERDDTRQALDAVWEEEQVKFIEDNATACDSSPLNQYQRRFSQDVAPQYVDISAGGGK 231
 
Name Accession Description Interval E-value
PRK15054 PRK15054
nitrate reductase molybdenum cofactor assembly chaperone;
1-231 3.18e-170

nitrate reductase molybdenum cofactor assembly chaperone;


Pssm-ID: 185014  Cd Length: 231  Bit Score: 467.86  E-value: 3.18e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093   1 MQILKVIGLLMEYPDELLWECKEDALALIRRDAPMLTDFTHNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDR 80
Cdd:PRK15054   1 MQILKVIGLLMEYPDELLWECKEDALALIRRDAPMLTDFTRNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093  81 GQAMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLAGS 160
Cdd:PRK15054  81 GQAMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLAGS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447089093 161 ILSSDSVTKQVNSEERDDTRQALDAVWEEEQVKFIEDNATACDSSPLNQYQRRFSQDVAPQYVDISAGGGK 231
Cdd:PRK15054 161 TLSSDSVTKQVNSEERDDTRQALDAVWEEEQVKFIEDNATACDSSPLNQYQRRFSQDVAPQYVDISAGGGK 231
NarJ COG2180
Nitrate reductase assembly protein NarJ, required for insertion of molybdenum cofactor [Energy ...
 1-167 1.69e-64

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: 198.17  E-value: 1.69e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093   1 MQILKVIGLLMEYPDELLWECKEDALALIRRD--APMLTDFTHNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESR 78
Cdd:COG2180    6 MKTLKALSLLLDYPDEELLAALPELRAALAEAaaREALAAFLDHLAALDLLDLQEEYVETFDRGRRTSLYLFEHVHGESR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093  79 DRGQAMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLA 158
Cdd:COG2180   86 DRGQALVDLKELYRAAGLELDDGELPDYLPLVLEFLATLDPEEARALLGDIRHGLELLRARLEERGSPYAALFDALLALL 165


                 ....*....
gi 447089093 159 GSILSSDSV 167
Cdd:COG2180  166 PAAAEAEAA 174
narJ TIGR00684
nitrate reductase molybdenum cofactor assembly chaperone; This protein is termed NarJ in most ...
 9-154 5.31e-37

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: 126.88  E-value: 5.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093    9 LLMEYPDELLWECKEDALALIR----RDAPMLTDFTHNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDRGQAM 84
Cdd:TIGR00684   2 ILLSYPDEDLEELLRMREALKAlligEDAEALGLFMEFLEKLDPEAADAQYVETFDMGRKTSMYLTYLLKGEERMRGQEM 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447089093   85 VDLLAEYEKVGLQLDCRELPDYLPLYLEYLS-VLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDAL 154
Cdd:TIGR00684  82 LELKSHYEQQGDMPVDRELPDYLPLMLEYLAlVDPEAARRFAKKYLQPWVGELASRLEKNRSLYALLAKAL 152
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
 45-153 3.11e-09

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: 53.54  E-value: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093   45 NAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRD--RGQAMVDLLAEYEKVGLQL--DCRELPDYLPLYLEYLSVLPDD 120
Cdd:pfam02613  22 EADLLELAAEYTRLFIGPGRPPASPYESVYLDERGllMGRPTLEVRAFYRAAGLEVaeELNEPPDHLAVELEFLAHLAER 101

                          90       100       110
                  ....*....|....*....|....*....|....
gi 447089093  121 QAKEGLLNVAP-ILALLGGRLKQREAPWYALFDA 153
Cdd:pfam02613 102 AAEALEAAEAEaLLAAQRAFLEEHLLPWVPRFAA 135
 
Name Accession Description Interval E-value
PRK15054 PRK15054
nitrate reductase molybdenum cofactor assembly chaperone;
1-231 3.18e-170

nitrate reductase molybdenum cofactor assembly chaperone;


Pssm-ID: 185014  Cd Length: 231  Bit Score: 467.86  E-value: 3.18e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093   1 MQILKVIGLLMEYPDELLWECKEDALALIRRDAPMLTDFTHNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDR 80
Cdd:PRK15054   1 MQILKVIGLLMEYPDELLWECKEDALALIRRDAPMLTDFTRNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093  81 GQAMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLAGS 160
Cdd:PRK15054  81 GQAMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLAGS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447089093 161 ILSSDSVTKQVNSEERDDTRQALDAVWEEEQVKFIEDNATACDSSPLNQYQRRFSQDVAPQYVDISAGGGK 231
Cdd:PRK15054 161 TLSSDSVTKQVNSEERDDTRQALDAVWEEEQVKFIEDNATACDSSPLNQYQRRFSQDVAPQYVDISAGGGK 231
NarJ COG2180
Nitrate reductase assembly protein NarJ, required for insertion of molybdenum cofactor [Energy ...
 1-167 1.69e-64

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: 198.17  E-value: 1.69e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093   1 MQILKVIGLLMEYPDELLWECKEDALALIRRD--APMLTDFTHNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESR 78
Cdd:COG2180    6 MKTLKALSLLLDYPDEELLAALPELRAALAEAaaREALAAFLDHLAALDLLDLQEEYVETFDRGRRTSLYLFEHVHGESR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093  79 DRGQAMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLA 158
Cdd:COG2180   86 DRGQALVDLKELYRAAGLELDDGELPDYLPLVLEFLATLDPEEARALLGDIRHGLELLRARLEERGSPYAALFDALLALL 165


                 ....*....
gi 447089093 159 GSILSSDSV 167
Cdd:COG2180  166 PAAAEAEAA 174
narJ TIGR00684
nitrate reductase molybdenum cofactor assembly chaperone; This protein is termed NarJ in most ...
 9-154 5.31e-37

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: 126.88  E-value: 5.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093    9 LLMEYPDELLWECKEDALALIR----RDAPMLTDFTHNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDRGQAM 84
Cdd:TIGR00684   2 ILLSYPDEDLEELLRMREALKAlligEDAEALGLFMEFLEKLDPEAADAQYVETFDMGRKTSMYLTYLLKGEERMRGQEM 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447089093   85 VDLLAEYEKVGLQLDCRELPDYLPLYLEYLS-VLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDAL 154
Cdd:TIGR00684  82 LELKSHYEQQGDMPVDRELPDYLPLMLEYLAlVDPEAARRFAKKYLQPWVGELASRLEKNRSLYALLAKAL 152
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
 45-153 3.11e-09

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: 53.54  E-value: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093   45 NAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRD--RGQAMVDLLAEYEKVGLQL--DCRELPDYLPLYLEYLSVLPDD 120
Cdd:pfam02613  22 EADLLELAAEYTRLFIGPGRPPASPYESVYLDERGllMGRPTLEVRAFYRAAGLEVaeELNEPPDHLAVELEFLAHLAER 101

                          90       100       110
                  ....*....|....*....|....*....|....
gi 447089093  121 QAKEGLLNVAP-ILALLGGRLKQREAPWYALFDA 153
Cdd:pfam02613 102 AAEALEAAEAEaLLAAQRAFLEEHLLPWVPRFAA 135
TorD COG3381
Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational ...
 9-117 2.66e-03

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


Pssm-ID: 442608  Cd Length: 205  Bit Score: 37.72  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447089093   9 LLMEYPDELLWE--CKEDALALIRRDAPM---LTDFTHNLLNAPLLDKQAEWCEVFDRGRTTSLLLFE--HVHAESRDRG 81
Cdd:COG3381   21 LFYREPDEELLEalASGELLDDLPADEELaeaLAALASAAAEDDLEELAAEYTRLFIGPGRPPAPPYEsvYLDEEGLLFG 100

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 447089093  82 QAMVDLLAEYEKVGLQL--DCRELPDYLPLYLEYLSVL 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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