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Conserved domains on  [gi|575523327|gb|AHG98019|]
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NifW [Cloning vector pCV_cistron14]

Protein Classification

nitrogenase-stabilizing/protective NifW family protein( domain architecture ID 8432)

nitrogenase-stabilizing/protective NifW family protein may protect the nitrogenase Fe-Mo protein from oxidative damage

Gene Symbol:  nifW
PubMed:  29724822|35432878

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NifW super family cl03935
Nitrogen fixation protein NifW; Nitrogenase is a complex metalloenzyme composed of two ...
 9-83 7.45e-11

Nitrogen fixation protein NifW; Nitrogenase is a complex metalloenzyme composed of two proteins designated the Fe-protein and the MoFe-protein. Apart from these two proteins, a number of accessory proteins are essential for the maturation and assembly of nitrogenase. Even though experimental evidence suggests that these accessory proteins are required for nitrogenase activity, the exact roles played by many of these proteins in the functions of nitrogenase are unclear. Using yeast two-hybrid screening it has been shown that NifW can interact with itself as well as NifZ.


The actual alignment was detected with superfamily member pfam03206:

Pssm-ID: 446239  Cd Length: 99  Bit Score: 53.28  E-value: 7.45e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575523327   9 GVDELRSAESFFQFFAVPYQPELLGRCSLPVLATFHRKLRAEVPLqnrLEDNDRAPWLLARRLLAESYqQQFQES 83
Cdd:pfam03206  5 ELKKLSSAEDFFDFFGVPYDPKVVNVNRLHILKRFSQYLAEADEL---EPLDEEERLARYRAALERAY-QDFVTS 75
 
Name Accession Description Interval E-value
NifW pfam03206
Nitrogen fixation protein NifW; Nitrogenase is a complex metalloenzyme composed of two ...
 9-83 7.45e-11

Nitrogen fixation protein NifW; Nitrogenase is a complex metalloenzyme composed of two proteins designated the Fe-protein and the MoFe-protein. Apart from these two proteins, a number of accessory proteins are essential for the maturation and assembly of nitrogenase. Even though experimental evidence suggests that these accessory proteins are required for nitrogenase activity, the exact roles played by many of these proteins in the functions of nitrogenase are unclear. Using yeast two-hybrid screening it has been shown that NifW can interact with itself as well as NifZ.


Pssm-ID: 427197  Cd Length: 99  Bit Score: 53.28  E-value: 7.45e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575523327   9 GVDELRSAESFFQFFAVPYQPELLGRCSLPVLATFHRKLRAEVPLqnrLEDNDRAPWLLARRLLAESYqQQFQES 83
Cdd:pfam03206  5 ELKKLSSAEDFFDFFGVPYDPKVVNVNRLHILKRFSQYLAEADEL---EPLDEEERLARYRAALERAY-QDFVTS 75
nifW PRK00810
nitrogenase stabilizing/protective protein NifW;
10-50 1.06e-04

nitrogenase stabilizing/protective protein NifW;


Pssm-ID: 234842  Cd Length: 113  Bit Score: 37.72  E-value: 1.06e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 575523327  10 VDELR---SAESFFQFFAVPYQPELLGRCSLPVLATFHRKLRAE 50
Cdd:PRK00810   9 LDQLKrlsSAEEFFQLLGVPYDPKVVNVARLHILKRMGQYLAQE 52
 
Name Accession Description Interval E-value
NifW pfam03206
Nitrogen fixation protein NifW; Nitrogenase is a complex metalloenzyme composed of two ...
 9-83 7.45e-11

Nitrogen fixation protein NifW; Nitrogenase is a complex metalloenzyme composed of two proteins designated the Fe-protein and the MoFe-protein. Apart from these two proteins, a number of accessory proteins are essential for the maturation and assembly of nitrogenase. Even though experimental evidence suggests that these accessory proteins are required for nitrogenase activity, the exact roles played by many of these proteins in the functions of nitrogenase are unclear. Using yeast two-hybrid screening it has been shown that NifW can interact with itself as well as NifZ.


Pssm-ID: 427197  Cd Length: 99  Bit Score: 53.28  E-value: 7.45e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575523327   9 GVDELRSAESFFQFFAVPYQPELLGRCSLPVLATFHRKLRAEVPLqnrLEDNDRAPWLLARRLLAESYqQQFQES 83
Cdd:pfam03206  5 ELKKLSSAEDFFDFFGVPYDPKVVNVNRLHILKRFSQYLAEADEL---EPLDEEERLARYRAALERAY-QDFVTS 75
nifW PRK00810
nitrogenase stabilizing/protective protein NifW;
10-50 1.06e-04

nitrogenase stabilizing/protective protein NifW;


Pssm-ID: 234842  Cd Length: 113  Bit Score: 37.72  E-value: 1.06e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 575523327  10 VDELR---SAESFFQFFAVPYQPELLGRCSLPVLATFHRKLRAE 50
Cdd:PRK00810   9 LDQLKrlsSAEEFFQLLGVPYDPKVVNVARLHILKRMGQYLAQE 52
 
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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