NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|447002763|ref|WP_001080019|]
View 

MULTISPECIES: (2Fe-2S)-binding protein [Bacillus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 16-95 4.49e-31

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: 104.93  E-value: 4.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447002763   16 SERITFQFNGHQYEAYEHETIAAALLANEIRTLRvHEDSGTPRGIYCNIGHCSECRVTVNNQTNVRACLTVVEENMVVES 95
Cdd:pfam13510   1 SRPVTFTFDGRPVTAPEGDTIAAALLANGVRVPR-SCKYGRPRGIFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRT 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 ...
 16-95 4.49e-31

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: 104.93  E-value: 4.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447002763   16 SERITFQFNGHQYEAYEHETIAAALLANEIRTLRvHEDSGTPRGIYCNIGHCSECRVTVNNQTNVRACLTVVEENMVVES 95
Cdd:pfam13510   1 SRPVTFTFDGRPVTAPEGDTIAAALLANGVRVPR-SCKYGRPRGIFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRT 79
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 19-94 4.97e-06

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 41.23  E-value: 4.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447002763  19 ITFQFN--GHQYEAYEHETIAAALLANEIRTlrvhedsgtPRGiyCNIGHCSECRVTVN-----------------NQTN 79
Cdd:cd00207    1 VTINVPgsGVEVEVPEGETLLDAAREAGIDI---------PYS--CRAGACGTCKVEVVegevdqsdpslldeeeaEGGY 69

                         90
                 ....*....|....*
gi 447002763  80 VRACLTVVEENMVVE 94
Cdd:cd00207   70 VLACQTRVTDGLVIE 84
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 62-94 3.16e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 35.37  E-value: 3.16e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 447002763  62 CNIGHCSECRVTVNNQTnVRACLTVVEENMVVE 94
Cdd:PRK06259  54 CRAGQCGSCAVTINGEP-VLACKTEVEDGMIIE 85
 
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 ...
 16-95 4.49e-31

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: 104.93  E-value: 4.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447002763   16 SERITFQFNGHQYEAYEHETIAAALLANEIRTLRvHEDSGTPRGIYCNIGHCSECRVTVNNQTNVRACLTVVEENMVVES 95
Cdd:pfam13510   1 SRPVTFTFDGRPVTAPEGDTIAAALLANGVRVPR-SCKYGRPRGIFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRT 79
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 19-94 4.97e-06

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 41.23  E-value: 4.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447002763  19 ITFQFN--GHQYEAYEHETIAAALLANEIRTlrvhedsgtPRGiyCNIGHCSECRVTVN-----------------NQTN 79
Cdd:cd00207    1 VTINVPgsGVEVEVPEGETLLDAAREAGIDI---------PYS--CRAGACGTCKVEVVegevdqsdpslldeeeaEGGY 69

                         90
                 ....*....|....*
gi 447002763  80 VRACLTVVEENMVVE 94
Cdd:cd00207   70 VLACQTRVTDGLVIE 84
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 62-94 3.16e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 35.37  E-value: 3.16e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 447002763  62 CNIGHCSECRVTVNNQTnVRACLTVVEENMVVE 94
Cdd:PRK06259  54 CRAGQCGSCAVTINGEP-VLACKTEVEDGMIIE 85
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH