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Conserved domains on  [gi|498057793|ref|WP_010371949|]
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MULTISPECIES: 2Fe-2S iron-sulfur cluster-binding protein [Pseudoalteromonas]

Protein Classification

2Fe-2S iron-sulfur cluster-binding family protein( domain architecture ID 1376)

2Fe-2S iron-sulfur cluster-binding family protein such as ferredoxin, an iron-sulfur protein transfering electrons in a wide variety of metabolic reactions

Gene Ontology:  GO:0051536

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
fer2 super family cl00159
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 19-97 6.20e-13

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.


The actual alignment was detected with superfamily member pfam13510:

Pssm-ID: 444718 [Multi-domain]  Cd Length: 82  Bit Score: 58.70  E-value: 6.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498057793   19 QIQIDDIAVNACDGETVLSVLLAANYKqIMES-DREAVSGAYCGMGVCHCCQVTINKQHKQKACQTLVQPNMQVETkQNR 97
Cdd:pfam13510   5 TFTFDGRPVTAPEGDTIAAALLANGVR-VPRScKYGRPRGIFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRT-QNG 82
 
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 ...
 19-97 6.20e-13

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: 58.70  E-value: 6.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498057793   19 QIQIDDIAVNACDGETVLSVLLAANYKqIMES-DREAVSGAYCGMGVCHCCQVTINKQHKQKACQTLVQPNMQVETkQNR 97
Cdd:pfam13510   5 TFTFDGRPVTAPEGDTIAAALLANGVR-VPRScKYGRPRGIFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRT-QNG 82
 
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 ...
 19-97 6.20e-13

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: 58.70  E-value: 6.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498057793   19 QIQIDDIAVNACDGETVLSVLLAANYKqIMES-DREAVSGAYCGMGVCHCCQVTINKQHKQKACQTLVQPNMQVETkQNR 97
Cdd:pfam13510   5 TFTFDGRPVTAPEGDTIAAALLANGVR-VPRScKYGRPRGIFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRT-QNG 82
 
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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