nitrogen fixation protein NifQ is required for the biosynthesis of iron-molybdenum cofactor (FeMo-co) of nitrogenase and may be involved in molybdenum processing
NifQ; NifQ is involved in early stages of the biosynthesis of the iron-molybdenum cofactor ...
31-191
1.23e-84
NifQ; NifQ is involved in early stages of the biosynthesis of the iron-molybdenum cofactor (FeMo-co), which is an integral part of the active site of dinitrogenase. The conserved C-terminal cysteine residues may be involved in metal binding.
:
Pssm-ID: 428177 Cd Length: 159 Bit Score: 246.74 E-value: 1.23e-84
NifQ; NifQ is involved in early stages of the biosynthesis of the iron-molybdenum cofactor ...
31-191
1.23e-84
NifQ; NifQ is involved in early stages of the biosynthesis of the iron-molybdenum cofactor (FeMo-co), which is an integral part of the active site of dinitrogenase. The conserved C-terminal cysteine residues may be involved in metal binding.
Pssm-ID: 428177 Cd Length: 159 Bit Score: 246.74 E-value: 1.23e-84
NifQ; NifQ is involved in early stages of the biosynthesis of the iron-molybdenum cofactor ...
31-191
1.23e-84
NifQ; NifQ is involved in early stages of the biosynthesis of the iron-molybdenum cofactor (FeMo-co), which is an integral part of the active site of dinitrogenase. The conserved C-terminal cysteine residues may be involved in metal binding.
Pssm-ID: 428177 Cd Length: 159 Bit Score: 246.74 E-value: 1.23e-84
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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