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Conserved domains on  [gi|504410038|ref|WP_014597140|]
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MULTISPECIES: DUF6306 domain-containing protein [Stutzerimonas]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF6306 super family cl45217
Domain of unknown function (DUF6306); This family of proteins is functionally uncharacterized. ...
 18-136 6.70e-34

Domain of unknown function (DUF6306); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 137 and 172 amino acids in length. Protein in this family belong to the ferritin clan.


The actual alignment was detected with superfamily member pfam19825:

Pssm-ID: 437657  Cd Length: 129  Bit Score: 114.95  E-value: 6.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410038   18 LQDLLSAERAGAKVAGESLQQATDPEQRQLLEQIRQGEIESCKLLLNCLQHLGVEPNKDTGAFYGKAMAIESLDDRLPFV 97
Cdd:pfam19825   7 LNELLEAERAGARVALKSAKAAAEPAYAELMQDVRKDEARWCAMLSRAIRRLDGAPSRRTGAFHGKAMAIAEPWERLAFL 86

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 504410038   98 DKGQQWVIRKLREYLPGCQDPLLRSELQRMLDIHEENSA 136
Cdd:pfam19825  87 NRGQAWVVRKLETLTPRVRDDELHADLEAMLAAHRHNIA 125
 
Name Accession Description Interval E-value
DUF6306 pfam19825
Domain of unknown function (DUF6306); This family of proteins is functionally uncharacterized. ...
 18-136 6.70e-34

Domain of unknown function (DUF6306); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 137 and 172 amino acids in length. Protein in this family belong to the ferritin clan.


Pssm-ID: 437657  Cd Length: 129  Bit Score: 114.95  E-value: 6.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410038   18 LQDLLSAERAGAKVAGESLQQATDPEQRQLLEQIRQGEIESCKLLLNCLQHLGVEPNKDTGAFYGKAMAIESLDDRLPFV 97
Cdd:pfam19825   7 LNELLEAERAGARVALKSAKAAAEPAYAELMQDVRKDEARWCAMLSRAIRRLDGAPSRRTGAFHGKAMAIAEPWERLAFL 86

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 504410038   98 DKGQQWVIRKLREYLPGCQDPLLRSELQRMLDIHEENSA 136
Cdd:pfam19825  87 NRGQAWVVRKLETLTPRVRDDELHADLEAMLAAHRHNIA 125
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 17-129 1.52e-04

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: 39.02  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410038  17 LLQDLLSAERAGAKVAGESLQQATDPEQRQLLEQIRQGEIESCKLLLNCLQHLGVEP---NKDTGAFYGKAMAIESLDDR 93
Cdd:cd00657    2 LLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRELGGTPplpPAHLLAAYALPKTSDDPAEA 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 504410038  94 LPFVDKGQQWVIRKLREYLPGCQDPLLRSELQRMLD 129
Cdd:cd00657   82 LRAALEVEARAIAAYRELIEQADDPELRRLLERILA 117
 
Name Accession Description Interval E-value
DUF6306 pfam19825
Domain of unknown function (DUF6306); This family of proteins is functionally uncharacterized. ...
 18-136 6.70e-34

Domain of unknown function (DUF6306); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 137 and 172 amino acids in length. Protein in this family belong to the ferritin clan.


Pssm-ID: 437657  Cd Length: 129  Bit Score: 114.95  E-value: 6.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410038   18 LQDLLSAERAGAKVAGESLQQATDPEQRQLLEQIRQGEIESCKLLLNCLQHLGVEPNKDTGAFYGKAMAIESLDDRLPFV 97
Cdd:pfam19825   7 LNELLEAERAGARVALKSAKAAAEPAYAELMQDVRKDEARWCAMLSRAIRRLDGAPSRRTGAFHGKAMAIAEPWERLAFL 86

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 504410038   98 DKGQQWVIRKLREYLPGCQDPLLRSELQRMLDIHEENSA 136
Cdd:pfam19825  87 NRGQAWVVRKLETLTPRVRDDELHADLEAMLAAHRHNIA 125
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 17-129 1.52e-04

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: 39.02  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410038  17 LLQDLLSAERAGAKVAGESLQQATDPEQRQLLEQIRQGEIESCKLLLNCLQHLGVEP---NKDTGAFYGKAMAIESLDDR 93
Cdd:cd00657    2 LLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRELGGTPplpPAHLLAAYALPKTSDDPAEA 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 504410038  94 LPFVDKGQQWVIRKLREYLPGCQDPLLRSELQRMLD 129
Cdd:cd00657   82 LRAALEVEARAIAAYRELIEQADDPELRRLLERILA 117
YciF cd07909
YciF bacterial stress response protein, ferritin-like iron-binding domain; YciF is a bacterial ...
 18-77 7.25e-03

YciF bacterial stress response protein, ferritin-like iron-binding domain; YciF is a bacterial protein of unknown function that is up-regulated when bacteria experience stress conditions, and is highly conserved in a broad range of bacterial species. YciF has a ferritin-like domain. 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: 153118  Cd Length: 147  Bit Score: 34.47  E-value: 7.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410038  18 LQDLLSAERAGAKVAGESLQQATDPEQRQLLEQIRQGEIESCKLLLNCLQHLGVEPNKDT 77
Cdd:cd07909    8 LRDLYSAEKQLVKALPKMAKAATSEELKEAFESHLEETEGQVERLEQIFESLGEKPEGKK 67
 
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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