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Conserved domains on  [gi|553904234|gb|AGY74284|]
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manganese catalase family protein [Clostridium autoethanogenum DSM 10061]

Protein Classification

ferritin family protein( domain architecture ID 10167765)

ferritin family protein similar to rubrerythrin, a non-heme di-iron that is involved in oxidative stress defense as a peroxide scavenger in a wide range of organisms

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 16-169 1.52e-62

Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized bacterial protein family has a ferritin-like domain similar to that of the manganese catalase protein of Lactobacillus plantarum and the bll3758 protein of Bradyrhizobium japonicum. 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: 153117  Cd Length: 154  Bit Score: 189.80  E-value: 1.52e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553904234  16 PYPKPRVEKTSIGYANVLLKDYAGEVSEFTAVSLYVYQHMVSEGIFEDYAKIIGGISMAEMKHLELIGKTVKLLGIKPVY 95
Cdd:cd07908    1 PYPPIKVAGPNPRYAELLLDDYAGTNSELTAISQYIYQHLISEEKYPEIAETFLGIAIVEMHHLEILGQLIVLLGGDPRY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553904234  96 IDSACPPGQLWTPAYVNFMTFIKDMLLEDIKSEKKAIKNYKYHISIIKDRYIQELIKRIIMDEELHLKLFTELY 169
Cdd:cd07908   81 RSSSSDKFTYWTGKYVNYGESIKEMLKLDIASEKAAIAKYKRQAETIKDPYIRALLNRIILDEKLHIKILEELL 154
 
Name Accession Description Interval E-value
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 16-169 1.52e-62

Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized bacterial protein family has a ferritin-like domain similar to that of the manganese catalase protein of Lactobacillus plantarum and the bll3758 protein of Bradyrhizobium japonicum. 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: 153117  Cd Length: 154  Bit Score: 189.80  E-value: 1.52e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553904234  16 PYPKPRVEKTSIGYANVLLKDYAGEVSEFTAVSLYVYQHMVSEGIFEDYAKIIGGISMAEMKHLELIGKTVKLLGIKPVY 95
Cdd:cd07908    1 PYPPIKVAGPNPRYAELLLDDYAGTNSELTAISQYIYQHLISEEKYPEIAETFLGIAIVEMHHLEILGQLIVLLGGDPRY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553904234  96 IDSACPPGQLWTPAYVNFMTFIKDMLLEDIKSEKKAIKNYKYHISIIKDRYIQELIKRIIMDEELHLKLFTELY 169
Cdd:cd07908   81 RSSSSDKFTYWTGKYVNYGESIKEMLKLDIASEKAAIAKYKRQAETIKDPYIRALLNRIILDEKLHIKILEELL 154
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
62-172 5.96e-10

Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];


Pssm-ID: 441240  Cd Length: 141  Bit Score: 54.73  E-value: 5.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553904234  62 EDYAKIIGGISMAEMKHLELIGKTVKLLGIKPVyidsaCPPGQLWTPAYVNFMTFI------KDMLLEDIKSEKKAIKNY 135
Cdd:COG1633   30 PELKKLFEELAEEEKKHAELLEKLYEKLGGKPV-----APPEEESQPGLAELMDKLdgsvsdAEALELAIATEKDAIEFY 104

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 553904234 136 KYHISIIKDRYIQELIKRIIMDEELHLKLFTELYEKY 172
Cdd:COG1633  105 RELAAKVGDPEIKKLFEELAADEKEHAALLEGLYDRL 141
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 43-171 2.72e-05

Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as members of the DPS family and bacterioferritins.


Pssm-ID: 459712  Cd Length: 141  Bit Score: 41.89  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553904234   43 EFTAVSLYVYQHMVSEGI-FEDYAKIIGGISMAEMKHLELIGKTVKLLGIKPVYidsacPPGQLWTPAYVNFMTFIKDML 121
Cdd:pfam00210  11 ELTASYQYLQMHWYVKGPgFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNG-----TRVELLAIEAPPSFGSVLEVL 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 553904234  122 LEDIKSEKKAIKNYKYHISI---IKDRYIQELIKRIIMDEELHLKLFTELYEK 171
Cdd:pfam00210  86 EAALEHEKKVTKSLRELIELaeeEGDYATADFLQWFLDEQEEHEWFLEALLEK 138
 
Name Accession Description Interval E-value
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 16-169 1.52e-62

Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized bacterial protein family has a ferritin-like domain similar to that of the manganese catalase protein of Lactobacillus plantarum and the bll3758 protein of Bradyrhizobium japonicum. 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: 153117  Cd Length: 154  Bit Score: 189.80  E-value: 1.52e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553904234  16 PYPKPRVEKTSIGYANVLLKDYAGEVSEFTAVSLYVYQHMVSEGIFEDYAKIIGGISMAEMKHLELIGKTVKLLGIKPVY 95
Cdd:cd07908    1 PYPPIKVAGPNPRYAELLLDDYAGTNSELTAISQYIYQHLISEEKYPEIAETFLGIAIVEMHHLEILGQLIVLLGGDPRY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553904234  96 IDSACPPGQLWTPAYVNFMTFIKDMLLEDIKSEKKAIKNYKYHISIIKDRYIQELIKRIIMDEELHLKLFTELY 169
Cdd:cd07908   81 RSSSSDKFTYWTGKYVNYGESIKEMLKLDIASEKAAIAKYKRQAETIKDPYIRALLNRIILDEKLHIKILEELL 154
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 31-169 3.43e-11

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: 57.51  E-value: 3.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553904234  31 NVLLKDYAGEvseFTAVslYVYQHMVSEGIFEDYAKIIGGISMAEMKHLELIGKTVKLLGIKPVYIDSACPPGQLWTPAY 110
Cdd:cd00657    1 RLLNDALAGE---YAAI--IAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAHLLAAYALPKTS 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 553904234 111 VNfmtfIKDMLLEDIKSEKKAIKNYKYHISIIKDRYIQELIKRIIMDEELHLKLFTELY 169
Cdd:cd00657   76 DD----PAEALRAALEVEARAIAAYRELIEQADDPELRRLLERILADEQRHAAWFRKLL 130
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
62-172 5.96e-10

Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];


Pssm-ID: 441240  Cd Length: 141  Bit Score: 54.73  E-value: 5.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553904234  62 EDYAKIIGGISMAEMKHLELIGKTVKLLGIKPVyidsaCPPGQLWTPAYVNFMTFI------KDMLLEDIKSEKKAIKNY 135
Cdd:COG1633   30 PELKKLFEELAEEEKKHAELLEKLYEKLGGKPV-----APPEEESQPGLAELMDKLdgsvsdAEALELAIATEKDAIEFY 104

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 553904234 136 KYHISIIKDRYIQELIKRIIMDEELHLKLFTELYEKY 172
Cdd:COG1633  105 RELAAKVGDPEIKKLFEELAADEKEHAALLEGLYDRL 141
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
117-172 2.26e-07

Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];


Pssm-ID: 441240  Cd Length: 141  Bit Score: 47.80  E-value: 2.26e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 553904234 117 IKDMLLEDIKSEKKAIKNYKYHISIIKDRYIQELIKRIIMDEELHLKLFTELYEKY 172
Cdd:COG1633    2 LLEILKEAIAMEEEAIEFYLELAEKAKDPELKKLFEELAEEEKKHAELLEKLYEKL 57
Ferritin pfam00210
Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as ...
 43-171 2.72e-05

Ferritin-like domain; This family contains ferritins and other ferritin-like proteins such as members of the DPS family and bacterioferritins.


Pssm-ID: 459712  Cd Length: 141  Bit Score: 41.89  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553904234   43 EFTAVSLYVYQHMVSEGI-FEDYAKIIGGISMAEMKHLELIGKTVKLLGIKPVYidsacPPGQLWTPAYVNFMTFIKDML 121
Cdd:pfam00210  11 ELTASYQYLQMHWYVKGPgFEGLHEFFDEQAEEEREHADKLAERILDLGGTPNG-----TRVELLAIEAPPSFGSVLEVL 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 553904234  122 LEDIKSEKKAIKNYKYHISI---IKDRYIQELIKRIIMDEELHLKLFTELYEK 171
Cdd:pfam00210  86 EAALEHEKKVTKSLRELIELaeeEGDYATADFLQWFLDEQEEHEWFLEALLEK 138
DPSL cd01052
DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a ...
 33-168 1.04e-04

DPS-like protein, ferritin-like diiron-binding domain; DPSL (DPS-like). DPSL is a phylogenetically distinct class within the ferritin-like superfamily, and similar in many ways to the DPS (DNA Protecting protein under Starved conditions) proteins. Like DPS, these proteins are expressed in response to oxidative stress, form dodecameric cage-like particles, preferentially utilize hydrogen peroxide in the controlled oxidation of iron, and possess a short N-terminal extension implicated in stabilizing cellular DNA. This domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. These proteins are distantly related to bacterial ferritins which assemble 24 monomers, each of which have a four-helix bundle with a fifth shorter helix at the C terminus and a diiron (ferroxidase) center. Ferritins contain a center where oxidation of ferrous iron by molecular oxygen occurs, facilitating the detoxification of iron, protection against dioxygen and radical products, and storage of iron in the ferric form. Many of the conserved residues of a diiron center are present in this domain.


Pssm-ID: 153111  Cd Length: 148  Bit Score: 40.35  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553904234  33 LLKDYAgevSEFTAVSLYVYQHMVSEGIFEDYAKIIGGISMAE-MKHLELIGKTVKLLGIKPV------YIDSACPPGQL 105
Cdd:cd01052   11 LNKAFA---DEWLAYYYYTILAKHVKGPEGEGIKEELEEAAEEeLNHAELLAERIYELGGTPPrdpkdwYEISGCKCGYL 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553904234 106 wtpayVNFMTFIKDMLLEDIKSEKKAIKNYKYHISII--KDRYIQELIKRIIMDEELHLKLFTEL 168
Cdd:cd01052   88 -----PPDPPDVKGILKVNLKAERCAIKVYKELCDMThgKDPVTYDLALAILNEEIEHEEDLEEL 147
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 119-171 1.65e-03

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: 36.71  E-value: 1.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 553904234 119 DMLLEDIKSEKKAIKNYKYHISIIKDRYIQELIKRIIMDEELHLKLFTELYEK 171
Cdd:cd00657    1 RLLNDALAGEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLRE 53
 
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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