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Conserved domains on  [gi|976214096|gb|KVB23015|]
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ferritin [Burkholderia cepacia]

Protein Classification

ferritin-like domain-containing protein( domain architecture ID 10090058)

ferritin-like domain-containing protein similar to diiron-carboxylate proteins that catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 44-162 8.58e-07

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


:

Pssm-ID: 153097  Cd Length: 130  Bit Score: 47.11  E-value: 8.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214096  44 SGSDLYTSNLSQFFndDPEVSAWLNnAWEHEELQHGRALKAYIAHVWPEFDWDTAFANFFAEysltckvEAFEKTRALEM 123
Cdd:cd00657   12 AAIIAYGQLAARAP--DPDLKDELL-EIADEERRHADALAERLRELGGTPPLPPAHLLAAYA-------LPKTSDDPAEA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 976214096 124 V-ARCVVETGTATLYRAINECSDEPVLKEITDNIRTDEVR 162
Cdd:cd00657   82 LrAALEVEARAIAAYRELIEQADDPELRRLLERILADEQR 121
 
Name Accession Description Interval E-value
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 44-162 8.58e-07

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


Pssm-ID: 153097  Cd Length: 130  Bit Score: 47.11  E-value: 8.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214096  44 SGSDLYTSNLSQFFndDPEVSAWLNnAWEHEELQHGRALKAYIAHVWPEFDWDTAFANFFAEysltckvEAFEKTRALEM 123
Cdd:cd00657   12 AAIIAYGQLAARAP--DPDLKDELL-EIADEERRHADALAERLRELGGTPPLPPAHLLAAYA-------LPKTSDDPAEA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 976214096 124 V-ARCVVETGTATLYRAINECSDEPVLKEITDNIRTDEVR 162
Cdd:cd00657   82 LrAALEVEARAIAAYRELIEQADDPELRRLLERILADEQR 121
 
Name Accession Description Interval E-value
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 44-162 8.58e-07

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


Pssm-ID: 153097  Cd Length: 130  Bit Score: 47.11  E-value: 8.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214096  44 SGSDLYTSNLSQFFndDPEVSAWLNnAWEHEELQHGRALKAYIAHVWPEFDWDTAFANFFAEysltckvEAFEKTRALEM 123
Cdd:cd00657   12 AAIIAYGQLAARAP--DPDLKDELL-EIADEERRHADALAERLRELGGTPPLPPAHLLAAYA-------LPKTSDDPAEA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 976214096 124 V-ARCVVETGTATLYRAINECSDEPVLKEITDNIRTDEVR 162
Cdd:cd00657   82 LrAALEVEARAIAAYRELIEQADDPELRRLLERILADEQR 121
 
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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