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Conserved domains on  [gi|1482692993|ref|WP_119757906|]
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ferritin-like domain-containing protein [Chryseolinea soli]

Protein Classification

ferritin-like domain-containing protein( domain architecture ID 10007837)

uncharacterized ferritin-like iron-binding domain containing protein similar to Escherichia coli YciF, a bacterial stress response protein

Gene Ontology:  GO:0046872
SCOP:  4001222

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YciE COG3685
Ferritin-like metal-binding protein YciE [Inorganic ion transport and metabolism];
20-154 2.08e-24

Ferritin-like metal-binding protein YciE [Inorganic ion transport and metabolism];


:

Pssm-ID: 442901  Cd Length: 165  Bit Score: 92.58  E-value: 2.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482692993  20 YQAEAKLREGLKKMTTIIQSPKLQDILKRYLESCDHKRTKVDRVFSYLNREPRSCHTHVVDEFINELYDRLKFAQEPMVQ 99
Cdd:COG3685    18 YAAEKQLLKALPKMARAATSPELKAAFEQHLEETEGQVERLEQVFERLGEKPSGKKCDAMEGLIAEGQEILEEFADDEVL 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1482692993 100 NHVLVSELLRINRYKASAYEASLHYAETLGLETAADLLQTIVHWEKNDERELLEL 154
Cdd:COG3685    98 DAALIAAAQKVEHYEIAAYGTLIALAEQLGLDEAADLLEQTLDEEKATDEKLTEL 152
 
Name Accession Description Interval E-value
YciE COG3685
Ferritin-like metal-binding protein YciE [Inorganic ion transport and metabolism];
20-154 2.08e-24

Ferritin-like metal-binding protein YciE [Inorganic ion transport and metabolism];


Pssm-ID: 442901  Cd Length: 165  Bit Score: 92.58  E-value: 2.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482692993  20 YQAEAKLREGLKKMTTIIQSPKLQDILKRYLESCDHKRTKVDRVFSYLNREPRSCHTHVVDEFINELYDRLKFAQEPMVQ 99
Cdd:COG3685    18 YAAEKQLLKALPKMARAATSPELKAAFEQHLEETEGQVERLEQVFERLGEKPSGKKCDAMEGLIAEGQEILEEFADDEVL 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1482692993 100 NHVLVSELLRINRYKASAYEASLHYAETLGLETAADLLQTIVHWEKNDERELLEL 154
Cdd:COG3685    98 DAALIAAAQKVEHYEIAAYGTLIALAEQLGLDEAADLLEQTLDEEKATDEKLTEL 152
YciF cd07909
YciF bacterial stress response protein, ferritin-like iron-binding domain; YciF is a bacterial ...
 20-154 4.82e-07

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: 46.80  E-value: 4.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482692993  20 YQAEAKLREGLKKMTTIIQSPKLQDILKRYLESCDHKRTKVDRVFSYLNREPRSCHTHVVDEFINELYDRLKFAQEPMVQ 99
Cdd:cd07909    12 YSAEKQLVKALPKMAKAATSEELKEAFESHLEETEGQVERLEQIFESLGEKPEGKKCKAMEGLIKEAEELIEETGDSAVL 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1482692993 100 NHVLVSELLRINRYKASAYEASLHYAETLGLETAADLLQTIVHWEKNDERELLEL 154
Cdd:cd07909    92 DAALIAAAQKVEHYEIAGYGTLRALAKLLGLDDAADLLQETLDEEKATDRKLTDL 146
DUF892 pfam05974
Domain of unknown function (DUF892); This family consists of several hypothetical bacterial ...
 20-140 2.17e-05

Domain of unknown function (DUF892); This family consists of several hypothetical bacterial proteins of unknown function.


Pssm-ID: 428701  Cd Length: 156  Bit Score: 42.21  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482692993  20 YQAEAKLREGLKKMTTIIQSPKLQDILKRYLESCDHKRTKVDRVFSYLNREPRSCHTHVVDEFINELYDRLK-FAQEPMV 98
Cdd:pfam05974  12 YAAEKQALKALPKMAEAAESPELKAALEQHLEETRGQIERLEQCFERLGESPSGKKCDAMEGLVAEGQALIGeFFEDEVL 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1482692993  99 QNHVLVSELLRINRYKASAYEASLHYAETLGLETAADLLQTI 140
Cdd:pfam05974  92 KDAALIAAAQAVEHYEIASYGTLIALAEQLGLAEAAALLEQT 133
 
Name Accession Description Interval E-value
YciE COG3685
Ferritin-like metal-binding protein YciE [Inorganic ion transport and metabolism];
20-154 2.08e-24

Ferritin-like metal-binding protein YciE [Inorganic ion transport and metabolism];


Pssm-ID: 442901  Cd Length: 165  Bit Score: 92.58  E-value: 2.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482692993  20 YQAEAKLREGLKKMTTIIQSPKLQDILKRYLESCDHKRTKVDRVFSYLNREPRSCHTHVVDEFINELYDRLKFAQEPMVQ 99
Cdd:COG3685    18 YAAEKQLLKALPKMARAATSPELKAAFEQHLEETEGQVERLEQVFERLGEKPSGKKCDAMEGLIAEGQEILEEFADDEVL 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1482692993 100 NHVLVSELLRINRYKASAYEASLHYAETLGLETAADLLQTIVHWEKNDERELLEL 154
Cdd:COG3685    98 DAALIAAAQKVEHYEIAAYGTLIALAEQLGLDEAADLLEQTLDEEKATDEKLTEL 152
YciF cd07909
YciF bacterial stress response protein, ferritin-like iron-binding domain; YciF is a bacterial ...
 20-154 4.82e-07

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: 46.80  E-value: 4.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482692993  20 YQAEAKLREGLKKMTTIIQSPKLQDILKRYLESCDHKRTKVDRVFSYLNREPRSCHTHVVDEFINELYDRLKFAQEPMVQ 99
Cdd:cd07909    12 YSAEKQLVKALPKMAKAATSEELKEAFESHLEETEGQVERLEQIFESLGEKPEGKKCKAMEGLIKEAEELIEETGDSAVL 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1482692993 100 NHVLVSELLRINRYKASAYEASLHYAETLGLETAADLLQTIVHWEKNDERELLEL 154
Cdd:cd07909    92 DAALIAAAQKVEHYEIAGYGTLRALAKLLGLDDAADLLQETLDEEKATDRKLTDL 146
DUF892 pfam05974
Domain of unknown function (DUF892); This family consists of several hypothetical bacterial ...
 20-140 2.17e-05

Domain of unknown function (DUF892); This family consists of several hypothetical bacterial proteins of unknown function.


Pssm-ID: 428701  Cd Length: 156  Bit Score: 42.21  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482692993  20 YQAEAKLREGLKKMTTIIQSPKLQDILKRYLESCDHKRTKVDRVFSYLNREPRSCHTHVVDEFINELYDRLK-FAQEPMV 98
Cdd:pfam05974  12 YAAEKQALKALPKMAEAAESPELKAALEQHLEETRGQIERLEQCFERLGESPSGKKCDAMEGLVAEGQALIGeFFEDEVL 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1482692993  99 QNHVLVSELLRINRYKASAYEASLHYAETLGLETAADLLQTI 140
Cdd:pfam05974  92 KDAALIAAAQAVEHYEIASYGTLIALAEQLGLAEAAALLEQT 133
 
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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