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Conserved domains on  [gi|1265088494|gb|PGQ17081|]
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spore coat protein CotJC [Bacillus cereus]

Protein Classification

manganese catalase family protein( domain architecture ID 11466390)

manganese catalase family protein similar to manganese catalase, which catalyzes the conversion of hydrogen peroxide to water and molecular oxygen, and to Bacillus paralicheniformis spore coat peptide assembly protein CotJC

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CotJC COG3546
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ...
 1-189 2.74e-102

Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and metabolism];


:

Pssm-ID: 442767  Cd Length: 253  Bit Score: 294.83  E-value: 2.74e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494   1 MWIYEKKLQYPVKVGTCNPALAKLLIEQYGGADGELAAALRYLNQRYTIPD-KVIGLLTDIGTEEFAHLEMIATMVYKLT 79
Cdd:COG3546     1 MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMRDpKYKDLLMDIGTEELGHVEMVATTIALLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494  80 KDATPEQ---------MKAAGLDPHYADHDSALHYHNAAGVPFTATYIQAKGDPIADLYEDIAAEEKARATYQWLINLSD 150
Cdd:COG3546    81 EGAPPELapedpplaaIKGGGNPQHFIVHGGGALPVDSNGVPWTAAYVQASGNLVADLLSNIAAEQRARLVYERLYEMTD 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1265088494 151 DPDINDSLRFLREREIVHSQRFREAVEILKEERDRKIYF 189
Cdd:COG3546   161 DPGVKDMLGFLLAREIVHQQRFGKALEELQGKFPEKKKY 199
 
Name Accession Description Interval E-value
CotJC COG3546
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ...
 1-189 2.74e-102

Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and metabolism];


Pssm-ID: 442767  Cd Length: 253  Bit Score: 294.83  E-value: 2.74e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494   1 MWIYEKKLQYPVKVGTCNPALAKLLIEQYGGADGELAAALRYLNQRYTIPD-KVIGLLTDIGTEEFAHLEMIATMVYKLT 79
Cdd:COG3546     1 MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMRDpKYKDLLMDIGTEELGHVEMVATTIALLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494  80 KDATPEQ---------MKAAGLDPHYADHDSALHYHNAAGVPFTATYIQAKGDPIADLYEDIAAEEKARATYQWLINLSD 150
Cdd:COG3546    81 EGAPPELapedpplaaIKGGGNPQHFIVHGGGALPVDSNGVPWTAAYVQASGNLVADLLSNIAAEQRARLVYERLYEMTD 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1265088494 151 DPDINDSLRFLREREIVHSQRFREAVEILKEERDRKIYF 189
Cdd:COG3546   161 DPGVKDMLGFLLAREIVHQQRFGKALEELQGKFPEKKKY 199
Mn_catalase pfam05067
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ...
 1-184 7.00e-97

Manganese containing catalase; Catalases are important antioxidant metalloenzymes that catalyze disproportionation of hydrogen peroxide, forming dioxygen and water. Two families of catalases are known, one having a heme cofactor, and this family that is a structurally distinct family containing non-heme manganese.


Pssm-ID: 252986 [Multi-domain]  Cd Length: 283  Bit Score: 282.22  E-value: 7.00e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494   1 MWIYEKKLQYPVKVGTCNPALAKLLIEQYGGADGELAAALRYLNQRYTIPDKVI--GLLTDIGTEEFAHLEMIATMVYKL 78
Cdd:pfam05067   1 MFVHDKLLQYPVKPDHPDPVLAKKLQEQLGGQFGELSAAMRYLFQGFNTRDKGKykDLLMDIGTEELGHVEMIATMIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494  79 TKDATPEQMKAAGLDP------------HYADHDSALHYHNAAGVPFTATYIQAKGDPIADLYEDIAAEEKARATYQWLI 146
Cdd:pfam05067  81 LKGATFDQQEDAAEEPvigsvlggmnpqHAIVSGLGAMPMDSMGVPWTADYIVASGNLIADLRANIAAEAQARLQYMRLY 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1265088494 147 NLSDDPDINDSLRFLREREIVHSQRFREAVEILKEERD 184
Cdd:pfam05067 161 EMTDDPGVRDMLSFLLARETVHQNQFYKALEILEEVET 198
Mn_catalase cd01051
Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member ...
 1-180 1.71e-77

Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member of a broad superfamily of ferritin-like diiron enzymes. While many diiron enzymes catalyze dioxygen-dependent reactions, manganese catalase performs peroxide-dependent oxidation-reduction. Catalases are important antioxidant metalloenzymes that catalyze disproportionation of hydrogen peroxide, forming dioxygen and water. Manganese catalase, a nonheme type II catalase, contains a binuclear manganese cluster that catalyzes the redox dismutation of hydrogen peroxide, interconverting between dimanganese(II) [(2,2)] and dimanganese(III) [(3,3)] oxidation states during turnover. Mn catalases are found in a broad range of microorganisms in microaerophilic environments, including the mesophilic lactic acid bacteria (e.g., Lactobacillus plantarum) and bacterial and archaeal thermophiles (e.g., Thermus thermophilus and Pyrobaculum caldifontis). L. plantarum and T. thermophilus holoenzymes are homohexameric structures; each subunit contains a dimanganese active site. The manganese ions are linked by a mu 1,3-bridging glutamate carboxylate and two mu-bridging solvent oxygens that electronically couple the metal centers. Several members of this CD lack the C-terminal strands that pack against the neighboring catalytic domains as seen in L. plantarum. One such sequence, Bacillus subtilis CotJC, is known to be a component of the inner spore coat that interacts with spore coat protein, CotJA. It has been suggested that CotJC could modulate the degree of Mn SodA-dependent cross-linking of an outer coat component, or the two enzymes could serve to protect specific cellular structures during the developmental process.


Pssm-ID: 153110  Cd Length: 156  Bit Score: 228.61  E-value: 1.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494   1 MWIYEKKLQYPVKVGTCNPALAKLLIEQYGGADGELAAALRYLNQRYT--IPDKVIGLLTDIGTEEFAHLEMIATMVYKL 78
Cdd:cd01051     1 MFYHVKKLQYPVRVDKPDPRFAKLLQEQLGGAFGELSAAMQYLFQSFNfrEDPKYRDLLLDIGTEELSHLEMVATLIAML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494  79 TKDAtpeqmkaagldphyadhdsalhyhnaAGVPFTATYIQAKGDPIADLYEDIAAEEKARATYQWLINLSDDPDINDSL 158
Cdd:cd01051    81 LKDS--------------------------QGVPWTAAYIQSSGNLVADLRSNIAAESRARLTYERLYEMTDDPGVKDTL 134

                         170       180
                  ....*....|....*....|..
gi 1265088494 159 RFLREREIVHSQRFREAVEILK 180
Cdd:cd01051   135 SFLLVREIVHQNAFGKALESLG 156
 
Name Accession Description Interval E-value
CotJC COG3546
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ...
 1-189 2.74e-102

Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and metabolism];


Pssm-ID: 442767  Cd Length: 253  Bit Score: 294.83  E-value: 2.74e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494   1 MWIYEKKLQYPVKVGTCNPALAKLLIEQYGGADGELAAALRYLNQRYTIPD-KVIGLLTDIGTEEFAHLEMIATMVYKLT 79
Cdd:COG3546     1 MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMRDpKYKDLLMDIGTEELGHVEMVATTIALLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494  80 KDATPEQ---------MKAAGLDPHYADHDSALHYHNAAGVPFTATYIQAKGDPIADLYEDIAAEEKARATYQWLINLSD 150
Cdd:COG3546    81 EGAPPELapedpplaaIKGGGNPQHFIVHGGGALPVDSNGVPWTAAYVQASGNLVADLLSNIAAEQRARLVYERLYEMTD 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1265088494 151 DPDINDSLRFLREREIVHSQRFREAVEILKEERDRKIYF 189
Cdd:COG3546   161 DPGVKDMLGFLLAREIVHQQRFGKALEELQGKFPEKKKY 199
Mn_catalase pfam05067
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ...
 1-184 7.00e-97

Manganese containing catalase; Catalases are important antioxidant metalloenzymes that catalyze disproportionation of hydrogen peroxide, forming dioxygen and water. Two families of catalases are known, one having a heme cofactor, and this family that is a structurally distinct family containing non-heme manganese.


Pssm-ID: 252986 [Multi-domain]  Cd Length: 283  Bit Score: 282.22  E-value: 7.00e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494   1 MWIYEKKLQYPVKVGTCNPALAKLLIEQYGGADGELAAALRYLNQRYTIPDKVI--GLLTDIGTEEFAHLEMIATMVYKL 78
Cdd:pfam05067   1 MFVHDKLLQYPVKPDHPDPVLAKKLQEQLGGQFGELSAAMRYLFQGFNTRDKGKykDLLMDIGTEELGHVEMIATMIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494  79 TKDATPEQMKAAGLDP------------HYADHDSALHYHNAAGVPFTATYIQAKGDPIADLYEDIAAEEKARATYQWLI 146
Cdd:pfam05067  81 LKGATFDQQEDAAEEPvigsvlggmnpqHAIVSGLGAMPMDSMGVPWTADYIVASGNLIADLRANIAAEAQARLQYMRLY 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1265088494 147 NLSDDPDINDSLRFLREREIVHSQRFREAVEILKEERD 184
Cdd:pfam05067 161 EMTDDPGVRDMLSFLLARETVHQNQFYKALEILEEVET 198
Mn_catalase cd01051
Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member ...
 1-180 1.71e-77

Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member of a broad superfamily of ferritin-like diiron enzymes. While many diiron enzymes catalyze dioxygen-dependent reactions, manganese catalase performs peroxide-dependent oxidation-reduction. Catalases are important antioxidant metalloenzymes that catalyze disproportionation of hydrogen peroxide, forming dioxygen and water. Manganese catalase, a nonheme type II catalase, contains a binuclear manganese cluster that catalyzes the redox dismutation of hydrogen peroxide, interconverting between dimanganese(II) [(2,2)] and dimanganese(III) [(3,3)] oxidation states during turnover. Mn catalases are found in a broad range of microorganisms in microaerophilic environments, including the mesophilic lactic acid bacteria (e.g., Lactobacillus plantarum) and bacterial and archaeal thermophiles (e.g., Thermus thermophilus and Pyrobaculum caldifontis). L. plantarum and T. thermophilus holoenzymes are homohexameric structures; each subunit contains a dimanganese active site. The manganese ions are linked by a mu 1,3-bridging glutamate carboxylate and two mu-bridging solvent oxygens that electronically couple the metal centers. Several members of this CD lack the C-terminal strands that pack against the neighboring catalytic domains as seen in L. plantarum. One such sequence, Bacillus subtilis CotJC, is known to be a component of the inner spore coat that interacts with spore coat protein, CotJA. It has been suggested that CotJC could modulate the degree of Mn SodA-dependent cross-linking of an outer coat component, or the two enzymes could serve to protect specific cellular structures during the developmental process.


Pssm-ID: 153110  Cd Length: 156  Bit Score: 228.61  E-value: 1.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494   1 MWIYEKKLQYPVKVGTCNPALAKLLIEQYGGADGELAAALRYLNQRYT--IPDKVIGLLTDIGTEEFAHLEMIATMVYKL 78
Cdd:cd01051     1 MFYHVKKLQYPVRVDKPDPRFAKLLQEQLGGAFGELSAAMQYLFQSFNfrEDPKYRDLLLDIGTEELSHLEMVATLIAML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494  79 TKDAtpeqmkaagldphyadhdsalhyhnaAGVPFTATYIQAKGDPIADLYEDIAAEEKARATYQWLINLSDDPDINDSL 158
Cdd:cd01051    81 LKDS--------------------------QGVPWTAAYIQSSGNLVADLRSNIAAESRARLTYERLYEMTDDPGVKDTL 134

                         170       180
                  ....*....|....*....|..
gi 1265088494 159 RFLREREIVHSQRFREAVEILK 180
Cdd:cd01051   135 SFLLVREIVHQNAFGKALESLG 156
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 11-175 3.66e-14

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: 66.53  E-value: 3.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494  11 PVKVGTCNPALAKLLIEQYGGADGELAAALRYLNQRYTIPDKV--IG-LLTDIGTEEFAHLEMIATMVYKLtkdatpeqm 87
Cdd:cd07908     4 PIKVAGPNPRYAELLLDDYAGTNSELTAISQYIYQHLISEEKYpeIAeTFLGIAIVEMHHLEILGQLIVLL--------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494  88 kaaGLDPHYA-DHDSALHYHNAAGVPFTATYIQAkgdpiadLYEDIAAEEKARATYQWLINLSDDPDINDSLRFLREREI 166
Cdd:cd07908    75 ---GGDPRYRsSSSDKFTYWTGKYVNYGESIKEM-------LKLDIASEKAAIAKYKRQAETIKDPYIRALLNRIILDEK 144


                  ....*....
gi 1265088494 167 VHSQRFREA 175
Cdd:cd07908   145 LHIKILEEL 153
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 34-175 8.07e-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: 43.64  E-value: 8.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265088494  34 GELAAALRYLNQRYTIPDKVIG-LLTDIGTEEFAHLEMIATMVYKLTKDATPEqmkaagldphyadhdsALHYHNAAGVP 112
Cdd:cd00657     9 GEYAAIIAYGQLAARAPDPDLKdELLEIADEERRHADALAERLRELGGTPPLP----------------PAHLLAAYALP 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265088494 113 FTATyiqakgDPIADLYEDIAAEEKARATYQWLINLSDDPDINDSLRFLREREIVHSQRFREA 175
Cdd:cd00657    73 KTSD------DPAEALRAALEVEARAIAAYRELIEQADDPELRRLLERILADEQRHAAWFRKL 129
 
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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