NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1131031844|ref|WP_075791401|]
View 

manganese catalase family protein [Massilia putida]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CotJC COG3546
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ...
 1-245 2.68e-125

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


:

Pssm-ID: 442767  Cd Length: 253  Bit Score: 358.38  E-value: 2.68e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844   1 MFAHNKRLQYTVRVSEPNPGLANLMLEQFGGPQGELAAAMRYFTQAVGEDDAGRKDMLFDIATEELSHLEVIGHIVAMLN 80
Cdd:COG3546     1 MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMRDPKYKDLLMDIGTEELGHVEMVATTIALLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844  81 KGAKGELAEavdsEAELYRKIQGAGNDSHvtQVLYGGGPALVNSAGVPWTAAYIDTIGEPTADLRSNIAAEARAKIVYER 160
Cdd:COG3546    81 EGAPPELAP----EDPPLAAIKGGGNPQH--FIVHGGGALPVDSNGVPWTAAYVQASGNLVADLLSNIAAEQRARLVYER 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844 161 LIALTDDPGVKEALGFLMTREIAHQKSFEKALYTIAPNFPPGKMPGDPRFANTYFNMSQGAGEVRGPWNQ----GENWDF 236
Cdd:COG3546   155 LYEMTDDPGVKDMLGFLLAREIVHQQRFGKALEELQGKFPEKKKYEDQEFSYKYFNFSTGDYSDRGPWNGgpppGGEFEY 234


                  ....*....
gi 1131031844 237 ISDREKQMA 245
Cdd:COG3546   235 VDGPEGGPP 243
 
Name Accession Description Interval E-value
CotJC COG3546
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ...
 1-245 2.68e-125

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


Pssm-ID: 442767  Cd Length: 253  Bit Score: 358.38  E-value: 2.68e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844   1 MFAHNKRLQYTVRVSEPNPGLANLMLEQFGGPQGELAAAMRYFTQAVGEDDAGRKDMLFDIATEELSHLEVIGHIVAMLN 80
Cdd:COG3546     1 MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMRDPKYKDLLMDIGTEELGHVEMVATTIALLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844  81 KGAKGELAEavdsEAELYRKIQGAGNDSHvtQVLYGGGPALVNSAGVPWTAAYIDTIGEPTADLRSNIAAEARAKIVYER 160
Cdd:COG3546    81 EGAPPELAP----EDPPLAAIKGGGNPQH--FIVHGGGALPVDSNGVPWTAAYVQASGNLVADLLSNIAAEQRARLVYER 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844 161 LIALTDDPGVKEALGFLMTREIAHQKSFEKALYTIAPNFPPGKMPGDPRFANTYFNMSQGAGEVRGPWNQ----GENWDF 236
Cdd:COG3546   155 LYEMTDDPGVKDMLGFLLAREIVHQQRFGKALEELQGKFPEKKKYEDQEFSYKYFNFSTGDYSDRGPWNGgpppGGEFEY 234


                  ....*....
gi 1131031844 237 ISDREKQMA 245
Cdd:COG3546   235 VDGPEGGPP 243
Mn_catalase pfam05067
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ...
 1-289 4.90e-101

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: 298.02  E-value: 4.90e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844   1 MFAHNKRLQYTVRVSEPNPGLANLMLEQFGGPQGELAAAMRYFTQAVGEDDAGR-KDMLFDIATEELSHLEVIGHIVAML 79
Cdd:pfam05067   1 MFVHDKLLQYPVKPDHPDPVLAKKLQEQLGGQFGELSAAMRYLFQGFNTRDKGKyKDLLMDIGTEELGHVEMIATMIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844  80 NKGAKGELAEAVdSEAELYRKIQGAGNDSHVtqVLYGGGPALVNSAGVPWTAAYIDTIGEPTADLRSNIAAEARAKIVYE 159
Cdd:pfam05067  81 LKGATFDQQEDA-AEEPVIGSVLGGMNPQHA--IVSGLGAMPMDSMGVPWTADYIVASGNLIADLRANIAAEAQARLQYM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844 160 RLIALTDDPGVKEALGFLMTREIAHQKSFEKALYTIAPNF------PPGKMPGDPRFANTYFNMSQGAGEVRGPWNQGEN 233
Cdd:pfam05067 158 RLYEMTDDPGVRDMLSFLLARETVHQNQFYKALEILEEVEtivvpvPFPRKLEKQEVARKLFNFSRGDESTIGRWAKGEA 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1131031844 234 WDFISdrEKQMAVDGGSGEAEVKLAakdidllkqmadrtmSDPSIDPPTGAELGMG 289
Cdd:pfam05067 238 PDGGG--AFEYVKEPGAGAPIPDLR---------------PAPMISHNTFLEIAKR 276
Mn_catalase cd01051
Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member ...
 1-195 6.14e-78

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: 234.39  E-value: 6.14e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844   1 MFAHNKRLQYTVRVSEPNPGLANLMLEQFGGPQGELAAAMRYFTQAVG-EDDAGRKDMLFDIATEELSHLEVIGHIVAML 79
Cdd:cd01051     1 MFYHVKKLQYPVRVDKPDPRFAKLLQEQLGGAFGELSAAMQYLFQSFNfREDPKYRDLLLDIGTEELSHLEMVATLIAML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844  80 NKgakgelaeavdseaelyrkiqgagndshvtqvlygggpalvNSAGVPWTAAYIDTIGEPTADLRSNIAAEARAKIVYE 159
Cdd:cd01051    81 LK-----------------------------------------DSQGVPWTAAYIQSSGNLVADLRSNIAAESRARLTYE 119

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1131031844 160 RLIALTDDPGVKEALGFLMTREIAHQKSFEKALYTI 195
Cdd:cd01051   120 RLYEMTDDPGVKDTLSFLLVREIVHQNAFGKALESL 155
 
Name Accession Description Interval E-value
CotJC COG3546
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ...
 1-245 2.68e-125

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


Pssm-ID: 442767  Cd Length: 253  Bit Score: 358.38  E-value: 2.68e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844   1 MFAHNKRLQYTVRVSEPNPGLANLMLEQFGGPQGELAAAMRYFTQAVGEDDAGRKDMLFDIATEELSHLEVIGHIVAMLN 80
Cdd:COG3546     1 MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMRDPKYKDLLMDIGTEELGHVEMVATTIALLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844  81 KGAKGELAEavdsEAELYRKIQGAGNDSHvtQVLYGGGPALVNSAGVPWTAAYIDTIGEPTADLRSNIAAEARAKIVYER 160
Cdd:COG3546    81 EGAPPELAP----EDPPLAAIKGGGNPQH--FIVHGGGALPVDSNGVPWTAAYVQASGNLVADLLSNIAAEQRARLVYER 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844 161 LIALTDDPGVKEALGFLMTREIAHQKSFEKALYTIAPNFPPGKMPGDPRFANTYFNMSQGAGEVRGPWNQ----GENWDF 236
Cdd:COG3546   155 LYEMTDDPGVKDMLGFLLAREIVHQQRFGKALEELQGKFPEKKKYEDQEFSYKYFNFSTGDYSDRGPWNGgpppGGEFEY 234


                  ....*....
gi 1131031844 237 ISDREKQMA 245
Cdd:COG3546   235 VDGPEGGPP 243
Mn_catalase pfam05067
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ...
 1-289 4.90e-101

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: 298.02  E-value: 4.90e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844   1 MFAHNKRLQYTVRVSEPNPGLANLMLEQFGGPQGELAAAMRYFTQAVGEDDAGR-KDMLFDIATEELSHLEVIGHIVAML 79
Cdd:pfam05067   1 MFVHDKLLQYPVKPDHPDPVLAKKLQEQLGGQFGELSAAMRYLFQGFNTRDKGKyKDLLMDIGTEELGHVEMIATMIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844  80 NKGAKGELAEAVdSEAELYRKIQGAGNDSHVtqVLYGGGPALVNSAGVPWTAAYIDTIGEPTADLRSNIAAEARAKIVYE 159
Cdd:pfam05067  81 LKGATFDQQEDA-AEEPVIGSVLGGMNPQHA--IVSGLGAMPMDSMGVPWTADYIVASGNLIADLRANIAAEAQARLQYM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844 160 RLIALTDDPGVKEALGFLMTREIAHQKSFEKALYTIAPNF------PPGKMPGDPRFANTYFNMSQGAGEVRGPWNQGEN 233
Cdd:pfam05067 158 RLYEMTDDPGVRDMLSFLLARETVHQNQFYKALEILEEVEtivvpvPFPRKLEKQEVARKLFNFSRGDESTIGRWAKGEA 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1131031844 234 WDFISdrEKQMAVDGGSGEAEVKLAakdidllkqmadrtmSDPSIDPPTGAELGMG 289
Cdd:pfam05067 238 PDGGG--AFEYVKEPGAGAPIPDLR---------------PAPMISHNTFLEIAKR 276
Mn_catalase cd01051
Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member ...
 1-195 6.14e-78

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: 234.39  E-value: 6.14e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844   1 MFAHNKRLQYTVRVSEPNPGLANLMLEQFGGPQGELAAAMRYFTQAVG-EDDAGRKDMLFDIATEELSHLEVIGHIVAML 79
Cdd:cd01051     1 MFYHVKKLQYPVRVDKPDPRFAKLLQEQLGGAFGELSAAMQYLFQSFNfREDPKYRDLLLDIGTEELSHLEMVATLIAML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844  80 NKgakgelaeavdseaelyrkiqgagndshvtqvlygggpalvNSAGVPWTAAYIDTIGEPTADLRSNIAAEARAKIVYE 159
Cdd:cd01051    81 LK-----------------------------------------DSQGVPWTAAYIQSSGNLVADLRSNIAAESRARLTYE 119

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1131031844 160 RLIALTDDPGVKEALGFLMTREIAHQKSFEKALYTI 195
Cdd:cd01051   120 RLYEMTDDPGVKDTLSFLLVREIVHQNAFGKALESL 155
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 12-192 2.63e-12

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: 63.45  E-value: 2.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844  12 VRVSEPNPGLANLMLEQFGGPQGELAAAMRYFTQA--VGEDDAGRKDMLFDIATEELSHLEVIGHIVAMLnkgakgelae 89
Cdd:cd07908     5 IKVAGPNPRYAELLLDDYAGTNSELTAISQYIYQHliSEEKYPEIAETFLGIAIVEMHHLEILGQLIVLL---------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844  90 avdseaelyrkiqgagndshvtqvlyGGGPALVNS---AGVPWTAAYIDTIGEPTADLRSNIAAEARAKIVYERLIALTD 166
Cdd:cd07908    75 --------------------------GGDPRYRSSssdKFTYWTGKYVNYGESIKEMLKLDIASEKAAIAKYKRQAETIK 128

                         170       180
                  ....*....|....*....|....*.
gi 1131031844 167 DPGVKEALGFLMTREIAHQKSFEKAL 192
Cdd:cd07908   129 DPYIRALLNRIILDEKLHIKILEELL 154
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 34-192 6.43e-07

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: 47.88  E-value: 6.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844  34 GELAAAMRYFTQAVGEDDAGRKDMLFDIATEELSHLEVIghivamlnkgakgelaeavdseAELYRKIqgagndshvtqv 113
Cdd:cd00657     9 GEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADAL----------------------AERLREL------------ 54

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131031844 114 lygGGPALVNSAGVPWTAAYIDTIGEPTADLRSNIAAEARAKIVYERLIALTDDPGVKEALGFLMTREIAHQKSFEKAL 192
Cdd:cd00657    55 ---GGTPPLPPAHLLAAYALPKTSDDPAEALRAALEVEARAIAAYRELIEQADDPELRRLLERILADEQRHAAWFRKLL 130
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
33-192 8.99e-07

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 47.41  E-value: 8.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844  33 QGELAAAMRYFTQAVGEDDAGRKDMLFDIATEELSHLEVIGHIVAMLnkGAKGELAEAVDSEAELyrkiqgagndshvtq 112
Cdd:COG1633    11 AMEEEAIEFYLELAEKAKDPELKKLFEELAEEEKKHAELLEKLYEKL--GGKPVAPPEEESQPGL--------------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131031844 113 vlygggpalvnsagvpwtAAYIDTIGEPTAD---LRSNIAAEARAKIVYERLIALTDDPGVKEALGFLMTREIAHQKSFE 189
Cdd:COG1633    74 ------------------AELMDKLDGSVSDaeaLELAIATEKDAIEFYRELAAKVGDPEIKKLFEELAADEKEHAALLE 135


                  ...
gi 1131031844 190 KAL 192
Cdd:COG1633   136 GLY 138
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
144-211 1.69e-03

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 38.17  E-value: 1.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131031844 144 LRSNIAAEARAKIVYERLIALTDDPGVKEALGFLMTREIAHQKSFEKALYTIAPN-FPPGKMPGDPRFA 211
Cdd:COG1633     6 LKEAIAMEEEAIEFYLELAEKAKDPELKKLFEELAEEEKKHAELLEKLYEKLGGKpVAPPEEESQPGLA 74
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH