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Conserved domains on  [gi|18398564|ref|NP_564407|]
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electron carrier/iron ion-binding protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
put_zinc_LRP1 super family cl31126
putative zinc finger domain, LRP1 type; This model represents a putative zinc finger domain ...
30-62 6.05e-03

putative zinc finger domain, LRP1 type; This model represents a putative zinc finger domain found in plants. Arabidopsis thaliana has at least 10 distinct members. Proteins containing this domain, including LRP1, generally share the same size, about 300 amino acids, and architecture. This 43-residue domain, and a more C-terminal companion domain of similar size, appear as tightly conserved islands of sequence similarity. The remainder consists largely of low-complexity sequence. Several animal proteins have regions with matching patterns of Cys, Gly, and His residues. These are not included in the model but score between trusted and noise cutoffs.


The actual alignment was detected with superfamily member TIGR01623:

Pssm-ID: 130684  Cd Length: 43  Bit Score: 34.10  E-value: 6.05e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 18398564    30 KCIQCGNVARSRCPFQSCKGCCSRAENPCPIHV 62
Cdd:TIGR01623   1 VCQDCGNQAKKECLFERCRTCCKSRGFHCVTHV 33
 
Name Accession Description Interval E-value
put_zinc_LRP1 TIGR01623
putative zinc finger domain, LRP1 type; This model represents a putative zinc finger domain ...
30-62 6.05e-03

putative zinc finger domain, LRP1 type; This model represents a putative zinc finger domain found in plants. Arabidopsis thaliana has at least 10 distinct members. Proteins containing this domain, including LRP1, generally share the same size, about 300 amino acids, and architecture. This 43-residue domain, and a more C-terminal companion domain of similar size, appear as tightly conserved islands of sequence similarity. The remainder consists largely of low-complexity sequence. Several animal proteins have regions with matching patterns of Cys, Gly, and His residues. These are not included in the model but score between trusted and noise cutoffs.


Pssm-ID: 130684  Cd Length: 43  Bit Score: 34.10  E-value: 6.05e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 18398564    30 KCIQCGNVARSRCPFQSCKGCCSRAENPCPIHV 62
Cdd:TIGR01623   1 VCQDCGNQAKKECLFERCRTCCKSRGFHCVTHV 33
 
Name Accession Description Interval E-value
put_zinc_LRP1 TIGR01623
putative zinc finger domain, LRP1 type; This model represents a putative zinc finger domain ...
30-62 6.05e-03

putative zinc finger domain, LRP1 type; This model represents a putative zinc finger domain found in plants. Arabidopsis thaliana has at least 10 distinct members. Proteins containing this domain, including LRP1, generally share the same size, about 300 amino acids, and architecture. This 43-residue domain, and a more C-terminal companion domain of similar size, appear as tightly conserved islands of sequence similarity. The remainder consists largely of low-complexity sequence. Several animal proteins have regions with matching patterns of Cys, Gly, and His residues. These are not included in the model but score between trusted and noise cutoffs.


Pssm-ID: 130684  Cd Length: 43  Bit Score: 34.10  E-value: 6.05e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 18398564    30 KCIQCGNVARSRCPFQSCKGCCSRAENPCPIHV 62
Cdd:TIGR01623   1 VCQDCGNQAKKECLFERCRTCCKSRGFHCVTHV 33
 
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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