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Conserved domains on  [gi|1900639061|emb|CAB5080957|]
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hypothetical protein IST4134_02971 [Burkholderia cenocepacia]

Protein Classification

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

ferritin-like domain-containing protein belongs to a broad superfamily of ferritin-like diiron-carboxylate proteins that catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers

CATH:  1.20.1260.10
Gene Ontology:  GO:0046872
PubMed:  8749363|9444766|3304136
SCOP:  3001658

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, ...
 35-162 1.89e-06

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: 46.34  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900639061  35 LLCASSFIESGSDLYTSNLSEFFNDDPEVSAWLnnAWEHEELQHGRALKAYIAHVWPEFDWDTAFANFFAEysktcsvEA 114
Cdd:cd00657     2 LLNDALAGEYAAIIAYGQLAARAPDPDLKDELL--EIADEERRHADALAERLRELGGTPPLPPAHLLAAYA-------LP 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1900639061 115 FEKTRALEMV-ARCVVETGTATLYRAINECSDEPVLKEITDNIRTDEVR 162
Cdd:cd00657    73 KTSDDPAEALrAALEVEARAIAAYRELIEQADDPELRRLLERILADEQR 121
 
Name Accession Description Interval E-value
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 35-162 1.89e-06

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: 46.34  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900639061  35 LLCASSFIESGSDLYTSNLSEFFNDDPEVSAWLnnAWEHEELQHGRALKAYIAHVWPEFDWDTAFANFFAEysktcsvEA 114
Cdd:cd00657     2 LLNDALAGEYAAIIAYGQLAARAPDPDLKDELL--EIADEERRHADALAERLRELGGTPPLPPAHLLAAYA-------LP 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1900639061 115 FEKTRALEMV-ARCVVETGTATLYRAINECSDEPVLKEITDNIRTDEVR 162
Cdd:cd00657    73 KTSDDPAEALrAALEVEARAIAAYRELIEQADDPELRRLLERILADEQR 121
 
Name Accession Description Interval E-value
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 35-162 1.89e-06

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: 46.34  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900639061  35 LLCASSFIESGSDLYTSNLSEFFNDDPEVSAWLnnAWEHEELQHGRALKAYIAHVWPEFDWDTAFANFFAEysktcsvEA 114
Cdd:cd00657     2 LLNDALAGEYAAIIAYGQLAARAPDPDLKDELL--EIADEERRHADALAERLRELGGTPPLPPAHLLAAYA-------LP 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1900639061 115 FEKTRALEMV-ARCVVETGTATLYRAINECSDEPVLKEITDNIRTDEVR 162
Cdd:cd00657    73 KTSDDPAEALrAALEVEARAIAAYRELIEQADDPELRRLLERILADEQR 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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