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Conserved domains on  [gi|752717907|ref|WP_041365031|]
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(2Fe-2S)-binding protein [Neorhizobium galegae]

Protein Classification

(2Fe-2S)-binding protein( domain architecture ID 10607402)

(2Fe-2S)-binding protein such as Pseudomonas aeruginosa hydrogen cyanide synthase subunit HcnA, part of a three-component membrane-bound flavoenzyme that catalyzes the formation of hydrogen cyanide, a secondary metabolite, by transfer of electrons to a cyanide-resistant branch of the aerobic respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 22-100 1.93e-23

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.


:

Pssm-ID: 433268 [Multi-domain]  Cd Length: 82  Bit Score: 85.67  E-value: 1.93e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717907   22 RPQVRFRLDGADCQALAGDTVLTAVLVCGPAVRQSEFGREKRAGFCLMGACQDCWIWQEDGGRLRACSTLVAEGMKLRT 100
Cdd:pfam13510   1 SRPVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRPRGIFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRT 79
 
Name Accession Description Interval E-value
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 22-100 1.93e-23

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.


Pssm-ID: 433268 [Multi-domain]  Cd Length: 82  Bit Score: 85.67  E-value: 1.93e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717907   22 RPQVRFRLDGADCQALAGDTVLTAVLVCGPAVRQSEFGREKRAGFCLMGACQDCWIWQEDGGRLRACSTLVAEGMKLRT 100
Cdd:pfam13510   1 SRPVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRPRGIFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRT 79
 
Name Accession Description Interval E-value
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 22-100 1.93e-23

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.


Pssm-ID: 433268 [Multi-domain]  Cd Length: 82  Bit Score: 85.67  E-value: 1.93e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752717907   22 RPQVRFRLDGADCQALAGDTVLTAVLVCGPAVRQSEFGREKRAGFCLMGACQDCWIWQEDGGRLRACSTLVAEGMKLRT 100
Cdd:pfam13510   1 SRPVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRPRGIFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRT 79
 
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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