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Conserved domains on  [gi|15599068|ref|NP_252562|]
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respiratory nitrate reductase subunit delta [Pseudomonas aeruginosa PAO1]

Protein Classification

nitrate reductase molybdenum cofactor assembly chaperone( domain architecture ID 10005502)

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
torD super family cl00958
chaperone protein TorD; Validated
 16-215 3.53e-58

chaperone protein TorD; Validated


The actual alignment was detected with superfamily member PRK15054:

Pssm-ID: 470012  Cd Length: 231  Bit Score: 184.35  E-value: 3.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068   16 DYPRAEL---REESLglhALIRTcELPEalrdgLAALLNELCQGDLLDVQARYDGLFERGRSVSLLLFEHVHGESRDRGQ 92
Cdd:PRK15054  12 EYPDELLwecKEDAL---ALIRR-DAPM-----LTDFTRNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDRGQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068   93 AMVDLLDRYTGAGLQIDVPELPDYLPLYLEYLSLLPFAAASEGLAEVAHILGLLALRLEERGSAYAAIFEALLELGGERP 172
Cdd:PRK15054  83 AMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLAGSTL 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15599068  173 DLGALRRDQAQEQRDDSLEAIDRAWEETPVSFT-DPAGGCPSSS 215
Cdd:PRK15054 163 SSDSVTKQVNSEERDDTRQALDAVWEEEQVKFIeDNATACDSSP 206
 
Name Accession Description Interval E-value
PRK15054 PRK15054
nitrate reductase molybdenum cofactor assembly chaperone;
16-215 3.53e-58

nitrate reductase molybdenum cofactor assembly chaperone;


Pssm-ID: 185014  Cd Length: 231  Bit Score: 184.35  E-value: 3.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068   16 DYPRAEL---REESLglhALIRTcELPEalrdgLAALLNELCQGDLLDVQARYDGLFERGRSVSLLLFEHVHGESRDRGQ 92
Cdd:PRK15054  12 EYPDELLwecKEDAL---ALIRR-DAPM-----LTDFTRNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDRGQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068   93 AMVDLLDRYTGAGLQIDVPELPDYLPLYLEYLSLLPFAAASEGLAEVAHILGLLALRLEERGSAYAAIFEALLELGGERP 172
Cdd:PRK15054  83 AMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLAGSTL 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15599068  173 DLGALRRDQAQEQRDDSLEAIDRAWEETPVSFT-DPAGGCPSSS 215
Cdd:PRK15054 163 SSDSVTKQVNSEERDDTRQALDAVWEEEQVKFIeDNATACDSSP 206
NarJ COG2180
Nitrate reductase assembly protein NarJ, required for insertion of molybdenum cofactor [Energy ...
 16-184 4.78e-57

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: 179.69  E-value: 4.78e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068  16 DYPRAELREESLGLHALIRtcelPEALRDGLAALLNELCQGDLLDVQARYDGLFERGRSVSLLLFEHVHGESRDRGQAMV 95
Cdd:COG2180  17 DYPDEELLAALPELRAALA----EAAAREALAAFLDHLAALDLLDLQEEYVETFDRGRRTSLYLFEHVHGESRDRGQALV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068  96 DLLDRYTGAGLQIDVPELPDYLPLYLEYLSLLPFAAASEGLAEVAHILGLLALRLEERGSAYAAIFEALLELGGERPDLG 175
Cdd:COG2180  93 DLKELYRAAGLELDDGELPDYLPLVLEFLATLDPEEARALLGDIRHGLELLRARLEERGSPYAALFDALLALLPAAAEAE 172


                ....*....
gi 15599068 176 ALRRDQAQE 184
Cdd:COG2180 173 AAVARLIAE 181
narJ TIGR00684
nitrate reductase molybdenum cofactor assembly chaperone; This protein is termed NarJ in most ...
 17-164 5.78e-31

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: 111.85  E-value: 5.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068    17 YPRAELREESLGLHALIRTCELPEAlrDGLAALLNELCQGDLLDVQARYDGLFERGRSVSLLLFEHVHGESRDRGQAMVD 96
Cdd:TIGR00684   6 YPDEDLEELLRMREALKALLIGEDA--EALGLFMEFLEKLDPEAADAQYVETFDMGRKTSMYLTYLLKGEERMRGQEMLE 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599068    97 LLDRYTGAGLQIDVPELPDYLPLYLEYLSLL-PFAAASEGLAEVAHILGLLALRLEERGSAYAAIFEAL 164
Cdd:TIGR00684  84 LKSHYEQQGDMPVDRELPDYLPLMLEYLALVdPEAARRFAKKYLQPWVGELASRLEKNRSLYALLAKAL 152
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
 37-161 1.71e-10

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: 57.39  E-value: 1.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068    37 ELPEALRDGLAALLNELCQG-DLLDVQARYDGLFE--RGRSVSLLLFEHVHGESRDRGQAMVDLLDRYTGAGLQI--DVP 111
Cdd:pfam02613   3 ALDAGLAEALAELAEALSREaDLLELAAEYTRLFIgpGRPPASPYESVYLDERGLLMGRPTLEVRAFYRAAGLEVaeELN 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15599068   112 ELPDYLPLYLEYLSLLPFAAASEGLAEVA-HILGLLALRLEERGSAYAAIF 161
Cdd:pfam02613  83 EPPDHLAVELEFLAHLAERAAEALEAAEAeALLAAQRAFLEEHLLPWVPRF 133
 
Name Accession Description Interval E-value
PRK15054 PRK15054
nitrate reductase molybdenum cofactor assembly chaperone;
16-215 3.53e-58

nitrate reductase molybdenum cofactor assembly chaperone;


Pssm-ID: 185014  Cd Length: 231  Bit Score: 184.35  E-value: 3.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068   16 DYPRAEL---REESLglhALIRTcELPEalrdgLAALLNELCQGDLLDVQARYDGLFERGRSVSLLLFEHVHGESRDRGQ 92
Cdd:PRK15054  12 EYPDELLwecKEDAL---ALIRR-DAPM-----LTDFTRNLLNAPLLDKQAEWCEVFDRGRTTSLLLFEHVHAESRDRGQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068   93 AMVDLLDRYTGAGLQIDVPELPDYLPLYLEYLSLLPFAAASEGLAEVAHILGLLALRLEERGSAYAAIFEALLELGGERP 172
Cdd:PRK15054  83 AMVDLLAEYEKVGLQLDCRELPDYLPLYLEYLSVLPDDQAKEGLLNVAPILALLGGRLKQREAPWYALFDALLQLAGSTL 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15599068  173 DLGALRRDQAQEQRDDSLEAIDRAWEETPVSFT-DPAGGCPSSS 215
Cdd:PRK15054 163 SSDSVTKQVNSEERDDTRQALDAVWEEEQVKFIeDNATACDSSP 206
NarJ COG2180
Nitrate reductase assembly protein NarJ, required for insertion of molybdenum cofactor [Energy ...
 16-184 4.78e-57

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: 179.69  E-value: 4.78e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068  16 DYPRAELREESLGLHALIRtcelPEALRDGLAALLNELCQGDLLDVQARYDGLFERGRSVSLLLFEHVHGESRDRGQAMV 95
Cdd:COG2180  17 DYPDEELLAALPELRAALA----EAAAREALAAFLDHLAALDLLDLQEEYVETFDRGRRTSLYLFEHVHGESRDRGQALV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068  96 DLLDRYTGAGLQIDVPELPDYLPLYLEYLSLLPFAAASEGLAEVAHILGLLALRLEERGSAYAAIFEALLELGGERPDLG 175
Cdd:COG2180  93 DLKELYRAAGLELDDGELPDYLPLVLEFLATLDPEEARALLGDIRHGLELLRARLEERGSPYAALFDALLALLPAAAEAE 172


                ....*....
gi 15599068 176 ALRRDQAQE 184
Cdd:COG2180 173 AAVARLIAE 181
narJ TIGR00684
nitrate reductase molybdenum cofactor assembly chaperone; This protein is termed NarJ in most ...
 17-164 5.78e-31

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: 111.85  E-value: 5.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068    17 YPRAELREESLGLHALIRTCELPEAlrDGLAALLNELCQGDLLDVQARYDGLFERGRSVSLLLFEHVHGESRDRGQAMVD 96
Cdd:TIGR00684   6 YPDEDLEELLRMREALKALLIGEDA--EALGLFMEFLEKLDPEAADAQYVETFDMGRKTSMYLTYLLKGEERMRGQEMLE 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599068    97 LLDRYTGAGLQIDVPELPDYLPLYLEYLSLL-PFAAASEGLAEVAHILGLLALRLEERGSAYAAIFEAL 164
Cdd:TIGR00684  84 LKSHYEQQGDMPVDRELPDYLPLMLEYLALVdPEAARRFAKKYLQPWVGELASRLEKNRSLYALLAKAL 152
Nitrate_red_del pfam02613
Nitrate reductase delta subunit; This family is the delta subunit of the nitrate reductase ...
 37-161 1.71e-10

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: 57.39  E-value: 1.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068    37 ELPEALRDGLAALLNELCQG-DLLDVQARYDGLFE--RGRSVSLLLFEHVHGESRDRGQAMVDLLDRYTGAGLQI--DVP 111
Cdd:pfam02613   3 ALDAGLAEALAELAEALSREaDLLELAAEYTRLFIgpGRPPASPYESVYLDERGLLMGRPTLEVRAFYRAAGLEVaeELN 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15599068   112 ELPDYLPLYLEYLSLLPFAAASEGLAEVA-HILGLLALRLEERGSAYAAIF 161
Cdd:pfam02613  83 EPPDHLAVELEFLAHLAERAAEALEAAEAeALLAAQRAFLEEHLLPWVPRF 133
TorD COG3381
Cytoplasmic chaperone TorD involved in molybdoenzyme TorA maturation [Posttranslational ...
 40-127 7.25e-06

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


Pssm-ID: 442608  Cd Length: 205  Bit Score: 45.43  E-value: 7.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599068  40 EALRDGLAALLNELCQGDLLDVQARYDGLFERGRSVSLLLFE--HVHGESRDRGQAMVDLLDRYTGAGLQI--DVPELPD 115
Cdd:COG3381  47 EELAEALAALASAAAEDDLEELAAEYTRLFIGPGRPPAPPYEsvYLDEEGLLFGESTLEVRAFYRALGLELdeDFKEPED 126

                        90
                ....*....|..
gi 15599068 116 YLPLYLEYLSLL 127
Cdd:COG3381 127 HIALELEFMAYL 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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