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Conserved domains on  [gi|15597381|ref|NP_250875|]
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non-heme catalase KatN [Pseudomonas aeruginosa PAO1]

Protein Classification

manganese catalase family protein( domain architecture ID 10523835)

manganese catalase family protein, similar to manganese catalase that performs a peroxide-dependent oxidation-reduction, catalyzing the conversion of hydrogen peroxide to water and molecular oxygen.; belongs to a broad superfamily of ferritin-like diiron-carboxylate proteins

CATH:  1.20.1260.10
EC:  1.11.1.6
Gene Ontology:  GO:0046872|GO:0004096
PubMed:  14745498|14871145|8749363|9444766|3304136
SCOP:  3001658

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mn_catalase pfam05067
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ...
 1-294 4.53e-131

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: 373.52  E-value: 4.53e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381     1 MFVHDKRLQYTVRVAAPDPGLANLLLEQFGGPQGELAAAMRYFTQGLGECDPGR-KDLLMDIATEELSHLEIIGSIVGML 79
Cdd:pfam05067   1 MFVHDKLLQYPVKPDHPDPVLAKKLQEQLGGQFGELSAAMRYLFQGFNTRDKGKyKDLLMDIGTEELGHVEMIATMIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381    80 NKGAKGRLAEAVEEEAeLYRSLTGGGNDSHitSLLYGGGPALVNSGGVPWSAAYIDTIGEPTADLRSNIAAEARAKIVYE 159
Cdd:pfam05067  81 LKGATFDQQEDAAEEP-VIGSVLGGMNPQH--AIVSGLGAMPMDSMGVPWTADYIVASGNLIADLRANIAAEAQARLQYM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381   160 RLINLTDDPGIKDALTFLMTRELAHQLSFEKALHSIQPNF------PQGKLQGMPEFARRYLNMSRGEGDTRGSWNEGDG 233
Cdd:pfam05067 158 RLYEMTDDPGVRDMLSFLLARETVHQNQFYKALEILEEVEtivvpvPFPRKLEKQEVARKLFNFSRGDESTIGRWAKGEA 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597381   234 WEYVEAPQPALDGGDGTASVNLseteqevlqrmadrtRSDPMTDPLTGADLGAGAAADKAP 294
Cdd:pfam05067 238 PDGGGAFEYVKEPGAGAPIPDL---------------RPAPMISHNTFLEIAKRLPPMKGF 283
 
Name Accession Description Interval E-value
Mn_catalase pfam05067
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ...
 1-294 4.53e-131

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: 373.52  E-value: 4.53e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381     1 MFVHDKRLQYTVRVAAPDPGLANLLLEQFGGPQGELAAAMRYFTQGLGECDPGR-KDLLMDIATEELSHLEIIGSIVGML 79
Cdd:pfam05067   1 MFVHDKLLQYPVKPDHPDPVLAKKLQEQLGGQFGELSAAMRYLFQGFNTRDKGKyKDLLMDIGTEELGHVEMIATMIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381    80 NKGAKGRLAEAVEEEAeLYRSLTGGGNDSHitSLLYGGGPALVNSGGVPWSAAYIDTIGEPTADLRSNIAAEARAKIVYE 159
Cdd:pfam05067  81 LKGATFDQQEDAAEEP-VIGSVLGGMNPQH--AIVSGLGAMPMDSMGVPWTADYIVASGNLIADLRANIAAEAQARLQYM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381   160 RLINLTDDPGIKDALTFLMTRELAHQLSFEKALHSIQPNF------PQGKLQGMPEFARRYLNMSRGEGDTRGSWNEGDG 233
Cdd:pfam05067 158 RLYEMTDDPGVRDMLSFLLARETVHQNQFYKALEILEEVEtivvpvPFPRKLEKQEVARKLFNFSRGDESTIGRWAKGEA 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597381   234 WEYVEAPQPALDGGDGTASVNLseteqevlqrmadrtRSDPMTDPLTGADLGAGAAADKAP 294
Cdd:pfam05067 238 PDGGGAFEYVKEPGAGAPIPDL---------------RPAPMISHNTFLEIAKRLPPMKGF 283
CotJC COG3546
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ...
 1-241 5.39e-126

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


Pssm-ID: 442767  Cd Length: 253  Bit Score: 359.15  E-value: 5.39e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381   1 MFVHDKRLQYTVRVAAPDPGLANLLLEQFGGPQGELAAAMRYFTQGLGECDPGRKDLLMDIATEELSHLEIIGSIVGMLN 80
Cdd:COG3546   1 MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMRDPKYKDLLMDIGTEELGHVEMVATTIALLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381  81 KGAKGRLAEAVEeeaeLYRSLTGGGNDSHItsLLYGGGPALVNSGGVPWSAAYIDTIGEPTADLRSNIAAEARAKIVYER 160
Cdd:COG3546  81 EGAPPELAPEDP----PLAAIKGGGNPQHF--IVHGGGALPVDSNGVPWTAAYVQASGNLVADLLSNIAAEQRARLVYER 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381 161 LINLTDDPGIKDALTFLMTRELAHQLSFEKALHSIQPNFPQGKLQGMPEFARRYLNMSRGEGDTRGSWNE----GDGWEY 236
Cdd:COG3546 155 LYEMTDDPGVKDMLGFLLAREIVHQQRFGKALEELQGKFPEKKKYEDQEFSYKYFNFSTGDYSDRGPWNGgpppGGEFEY 234


                ....*
gi 15597381 237 VEAPQ 241
Cdd:COG3546 235 VDGPE 239
Mn_catalase cd01051
Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member ...
 1-196 5.68e-80

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: 239.01  E-value: 5.68e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381   1 MFVHDKRLQYTVRVAAPDPGLANLLLEQFGGPQGELAAAMRYFTQGLG-ECDPGRKDLLMDIATEELSHLEIIGSIVGML 79
Cdd:cd01051   1 MFYHVKKLQYPVRVDKPDPRFAKLLQEQLGGAFGELSAAMQYLFQSFNfREDPKYRDLLLDIGTEELSHLEMVATLIAML 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381  80 NKgakgrlaeaveeeaelyrsltgggndshitsllygggpalvNSGGVPWSAAYIDTIGEPTADLRSNIAAEARAKIVYE 159
Cdd:cd01051  81 LK-----------------------------------------DSQGVPWTAAYIQSSGNLVADLRSNIAAESRARLTYE 119

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15597381 160 RLINLTDDPGIKDALTFLMTRELAHQLSFEKALHSIQ 196
Cdd:cd01051 120 RLYEMTDDPGVKDTLSFLLVREIVHQNAFGKALESLG 156
 
Name Accession Description Interval E-value
Mn_catalase pfam05067
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ...
 1-294 4.53e-131

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: 373.52  E-value: 4.53e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381     1 MFVHDKRLQYTVRVAAPDPGLANLLLEQFGGPQGELAAAMRYFTQGLGECDPGR-KDLLMDIATEELSHLEIIGSIVGML 79
Cdd:pfam05067   1 MFVHDKLLQYPVKPDHPDPVLAKKLQEQLGGQFGELSAAMRYLFQGFNTRDKGKyKDLLMDIGTEELGHVEMIATMIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381    80 NKGAKGRLAEAVEEEAeLYRSLTGGGNDSHitSLLYGGGPALVNSGGVPWSAAYIDTIGEPTADLRSNIAAEARAKIVYE 159
Cdd:pfam05067  81 LKGATFDQQEDAAEEP-VIGSVLGGMNPQH--AIVSGLGAMPMDSMGVPWTADYIVASGNLIADLRANIAAEAQARLQYM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381   160 RLINLTDDPGIKDALTFLMTRELAHQLSFEKALHSIQPNF------PQGKLQGMPEFARRYLNMSRGEGDTRGSWNEGDG 233
Cdd:pfam05067 158 RLYEMTDDPGVRDMLSFLLARETVHQNQFYKALEILEEVEtivvpvPFPRKLEKQEVARKLFNFSRGDESTIGRWAKGEA 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597381   234 WEYVEAPQPALDGGDGTASVNLseteqevlqrmadrtRSDPMTDPLTGADLGAGAAADKAP 294
Cdd:pfam05067 238 PDGGGAFEYVKEPGAGAPIPDL---------------RPAPMISHNTFLEIAKRLPPMKGF 283
CotJC COG3546
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ...
 1-241 5.39e-126

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


Pssm-ID: 442767  Cd Length: 253  Bit Score: 359.15  E-value: 5.39e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381   1 MFVHDKRLQYTVRVAAPDPGLANLLLEQFGGPQGELAAAMRYFTQGLGECDPGRKDLLMDIATEELSHLEIIGSIVGMLN 80
Cdd:COG3546   1 MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMRDPKYKDLLMDIGTEELGHVEMVATTIALLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381  81 KGAKGRLAEAVEeeaeLYRSLTGGGNDSHItsLLYGGGPALVNSGGVPWSAAYIDTIGEPTADLRSNIAAEARAKIVYER 160
Cdd:COG3546  81 EGAPPELAPEDP----PLAAIKGGGNPQHF--IVHGGGALPVDSNGVPWTAAYVQASGNLVADLLSNIAAEQRARLVYER 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381 161 LINLTDDPGIKDALTFLMTRELAHQLSFEKALHSIQPNFPQGKLQGMPEFARRYLNMSRGEGDTRGSWNE----GDGWEY 236
Cdd:COG3546 155 LYEMTDDPGVKDMLGFLLAREIVHQQRFGKALEELQGKFPEKKKYEDQEFSYKYFNFSTGDYSDRGPWNGgpppGGEFEY 234


                ....*
gi 15597381 237 VEAPQ 241
Cdd:COG3546 235 VDGPE 239
Mn_catalase cd01051
Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member ...
 1-196 5.68e-80

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: 239.01  E-value: 5.68e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381   1 MFVHDKRLQYTVRVAAPDPGLANLLLEQFGGPQGELAAAMRYFTQGLG-ECDPGRKDLLMDIATEELSHLEIIGSIVGML 79
Cdd:cd01051   1 MFYHVKKLQYPVRVDKPDPRFAKLLQEQLGGAFGELSAAMQYLFQSFNfREDPKYRDLLLDIGTEELSHLEMVATLIAML 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381  80 NKgakgrlaeaveeeaelyrsltgggndshitsllygggpalvNSGGVPWSAAYIDTIGEPTADLRSNIAAEARAKIVYE 159
Cdd:cd01051  81 LK-----------------------------------------DSQGVPWTAAYIQSSGNLVADLRSNIAAESRARLTYE 119

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15597381 160 RLINLTDDPGIKDALTFLMTRELAHQLSFEKALHSIQ 196
Cdd:cd01051 120 RLYEMTDDPGVKDTLSFLLVREIVHQNAFGKALESLG 156
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 12-192 3.47e-13

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: 65.76  E-value: 3.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381  12 VRVAAPDPGLANLLLEQFGGPQGELAAAMRYFTQGL--GECDPGRKDLLMDIATEELSHLEIIGSIVGMLnkgakgrlae 89
Cdd:cd07908   5 IKVAGPNPRYAELLLDDYAGTNSELTAISQYIYQHLisEEKYPEIAETFLGIAIVEMHHLEILGQLIVLL---------- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381  90 aveeeaelyrsltgGGNDSHITSLlygggpalvNSGGVPWSAAYIDTIGEPTADLRSNIAAEARAKIVYERLINLTDDPG 169
Cdd:cd07908  75 --------------GGDPRYRSSS---------SDKFTYWTGKYVNYGESIKEMLKLDIASEKAAIAKYKRQAETIKDPY 131

                       170       180
                ....*....|....*....|...
gi 15597381 170 IKDALTFLMTRELAHQLSFEKAL 192
Cdd:cd07908 132 IRALLNRIILDEKLHIKILEELL 154
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 34-192 1.25e-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: 46.72  E-value: 1.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381  34 GELAAAMRYFTQGLGECDPGRKDLLMDIATEELSHLEIIGSIVGMLnkgakgrlaeaveeeaelyrsltgggndshitsl 113
Cdd:cd00657   9 GEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADALAERLREL---------------------------------- 54

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597381 114 lygGGPALVNSGGVPWSAAYIDTIGEPTADLRSNIAAEARAKIVYERLINLTDDPGIKDALTFLMTRELAHQLSFEKAL 192
Cdd:cd00657  55 ---GGTPPLPPAHLLAAYALPKTSDDPAEALRAALEVEARAIAAYRELIEQADDPELRRLLERILADEQRHAAWFRKLL 130
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
33-195 3.73e-06

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 45.87  E-value: 3.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381  33 QGELAAAMRYFTQGLGECDPGRKDLLMDIATEELSHLEIIGSivgmlnkgakgrlaeaveeeaeLYRSLTGGgndsHITS 112
Cdd:COG1633  11 AMEEEAIEFYLELAEKAKDPELKKLFEELAEEEKKHAELLEK----------------------LYEKLGGK----PVAP 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597381 113 LLYGGGPALvnsggvpwsAAYIDTIGEPTAD---LRSNIAAEARAKIVYERLINLTDDPGIKDALTFLMTRELAHQLSFE 189
Cdd:COG1633  65 PEEESQPGL---------AELMDKLDGSVSDaeaLELAIATEKDAIEFYRELAAKVGDPEIKKLFEELAADEKEHAALLE 135


                ....*.
gi 15597381 190 KALHSI 195
Cdd:COG1633 136 GLYDRL 141
Ferritin_like_AB2 cd01048
Uncharacterized family of ferritin-like proteins found in archaea and bacteria; Ferritin-like ...
 119-192 3.66e-04

Uncharacterized family of ferritin-like proteins found in archaea and bacteria; Ferritin-like domain found in archaea and bacteria, subgroup 2 (Ferritin_like_AB2). This uncharacterized domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins whose function is unknown. The conserved residues of a diiron center are present within the putative active site.


Pssm-ID: 153107  Cd Length: 135  Bit Score: 39.96  E-value: 3.66e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597381 119 PALVNSGGVPWSAAYIDTIGEPTADLRSNIAAEARAKIV----YERLINLTDDPGIKDALTFLMTRELAHQLSFEKAL 192
Cdd:cd01048  58 PVDPFSGGVFTNPQYNQLVEQGPKSLQDALEVGVLIEELdiadYDRLLERTQNPDIRDVFENLQAASRNHHLPFFRRL 135
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
144-211 1.92e-03

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 37.78  E-value: 1.92e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597381 144 LRSNIAAEARAKIVYERLINLTDDPGIKDALTFLMTRELAHQLSFEKALHSIQPN-FPQGKLQGMPEFA 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.
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