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Conserved domains on  [gi|446410499|ref|WP_000488354|]
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MULTISPECIES: manganese catalase family protein [Salmonella]

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 ...
 1-239 4.00e-121

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


:

Pssm-ID: 442767  Cd Length: 253  Bit Score: 346.83  E-value: 4.00e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499   1 MFRHVKQLQYTVRVSEPNPGLANLLLEQFGGPQGELAAACRYFTQGLSDDDAGRREMLMDIATEELSHLEIIGSLVGMLN 80
Cdd:COG3546    1 MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMRDPKYKDLLMDIGTEELGHVEMVATTIALLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499  81 KGAKGELAEgtesEAELYRSLTQNGNDSHItsLLYGGGPALTNSGGVPWTAAYIDTIGEVTADLRSNIAAEARAKIIYER 160
Cdd:COG3546   81 EGAPPELAP----EDPPLAAIKGGGNPQHF--IVHGGGALPVDSNGVPWTAAYVQASGNLVADLLSNIAAEQRARLVYER 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499 161 LINLTDDPGVKDTLSFLMTREVAHQLSFEKALYSIRNNFPPGKLPPVEQYTDVYYNMSQGDD-PRGSWNSD----ENFNY 235
Cdd:COG3546  155 LYEMTDDPGVKDMLGFLLAREIVHQQRFGKALEELQGKFPEKKKYEDQEFSYKYFNFSTGDYsDRGPWNGGpppgGEFEY 234


                 ....
gi 446410499 236 VAEP 239
Cdd:COG3546  235 VDGP 238
 
Name Accession Description Interval E-value
CotJC COG3546
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ...
 1-239 4.00e-121

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


Pssm-ID: 442767  Cd Length: 253  Bit Score: 346.83  E-value: 4.00e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499   1 MFRHVKQLQYTVRVSEPNPGLANLLLEQFGGPQGELAAACRYFTQGLSDDDAGRREMLMDIATEELSHLEIIGSLVGMLN 80
Cdd:COG3546    1 MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMRDPKYKDLLMDIGTEELGHVEMVATTIALLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499  81 KGAKGELAEgtesEAELYRSLTQNGNDSHItsLLYGGGPALTNSGGVPWTAAYIDTIGEVTADLRSNIAAEARAKIIYER 160
Cdd:COG3546   81 EGAPPELAP----EDPPLAAIKGGGNPQHF--IVHGGGALPVDSNGVPWTAAYVQASGNLVADLLSNIAAEQRARLVYER 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499 161 LINLTDDPGVKDTLSFLMTREVAHQLSFEKALYSIRNNFPPGKLPPVEQYTDVYYNMSQGDD-PRGSWNSD----ENFNY 235
Cdd:COG3546  155 LYEMTDDPGVKDMLGFLLAREIVHQQRFGKALEELQGKFPEKKKYEDQEFSYKYFNFSTGDYsDRGPWNGGpppgGEFEY 234


                 ....
gi 446410499 236 VAEP 239
Cdd:COG3546  235 VDGP 238
Mn_catalase pfam05067
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ...
 1-289 6.44e-104

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: 304.56  E-value: 6.44e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499    1 MFRHVKQLQYTVRVSEPNPGLANLLLEQFGGPQGELAAACRYFTQGLSDDDAGR-REMLMDIATEELSHLEIIGSLVGML 79
Cdd:pfam05067   1 MFVHDKLLQYPVKPDHPDPVLAKKLQEQLGGQFGELSAAMRYLFQGFNTRDKGKyKDLLMDIGTEELGHVEMIATMIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499   80 NKGAKGELAEGTESEAeLYRSLTQNGNDSHitSLLYGGGPALTNSGGVPWTAAYIDTIGEVTADLRSNIAAEARAKIIYE 159
Cdd:pfam05067  81 LKGATFDQQEDAAEEP-VIGSVLGGMNPQH--AIVSGLGAMPMDSMGVPWTADYIVASGNLIADLRANIAAEAQARLQYM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499  160 RLINLTDDPGVKDTLSFLMTREVAHQLSFEKALYSIRNNF------PPGKLPPVEQYTDVYYNMSQGD-DPRGSWNSDEN 232
Cdd:pfam05067 158 RLYEMTDDPGVRDMLSFLLARETVHQNQFYKALEILEEVEtivvpvPFPRKLEKQEVARKLFNFSRGDeSTIGRWAKGEA 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446410499  233 FNYVAEPMPAVDGGDGLATVKLpreqmallkamaertKSDPTVDPLTGAELGCGEPK 289
Cdd:pfam05067 238 PDGGGAFEYVKEPGAGAPIPDL---------------RPAPMISHNTFLEIAKRLPP 279
Mn_catalase cd01051
Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member ...
 1-196 7.51e-82

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: 243.64  E-value: 7.51e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499   1 MFRHVKQLQYTVRVSEPNPGLANLLLEQFGGPQGELAAACRYFTQGLSDD-DAGRREMLMDIATEELSHLEIIGSLVGML 79
Cdd:cd01051    1 MFYHVKKLQYPVRVDKPDPRFAKLLQEQLGGAFGELSAAMQYLFQSFNFReDPKYRDLLLDIGTEELSHLEMVATLIAML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499  80 nkgakgelaegteseaelyrsltqngndshitsllygggpaLTNSGGVPWTAAYIDTIGEVTADLRSNIAAEARAKIIYE 159
Cdd:cd01051   81 -----------------------------------------LKDSQGVPWTAAYIQSSGNLVADLRSNIAAESRARLTYE 119

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446410499 160 RLINLTDDPGVKDTLSFLMTREVAHQLSFEKALYSIR 196
Cdd:cd01051  120 RLYEMTDDPGVKDTLSFLLVREIVHQNAFGKALESLG 156
 
Name Accession Description Interval E-value
CotJC COG3546
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ...
 1-239 4.00e-121

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


Pssm-ID: 442767  Cd Length: 253  Bit Score: 346.83  E-value: 4.00e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499   1 MFRHVKQLQYTVRVSEPNPGLANLLLEQFGGPQGELAAACRYFTQGLSDDDAGRREMLMDIATEELSHLEIIGSLVGMLN 80
Cdd:COG3546    1 MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMRDPKYKDLLMDIGTEELGHVEMVATTIALLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499  81 KGAKGELAEgtesEAELYRSLTQNGNDSHItsLLYGGGPALTNSGGVPWTAAYIDTIGEVTADLRSNIAAEARAKIIYER 160
Cdd:COG3546   81 EGAPPELAP----EDPPLAAIKGGGNPQHF--IVHGGGALPVDSNGVPWTAAYVQASGNLVADLLSNIAAEQRARLVYER 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499 161 LINLTDDPGVKDTLSFLMTREVAHQLSFEKALYSIRNNFPPGKLPPVEQYTDVYYNMSQGDD-PRGSWNSD----ENFNY 235
Cdd:COG3546  155 LYEMTDDPGVKDMLGFLLAREIVHQQRFGKALEELQGKFPEKKKYEDQEFSYKYFNFSTGDYsDRGPWNGGpppgGEFEY 234


                 ....
gi 446410499 236 VAEP 239
Cdd:COG3546  235 VDGP 238
Mn_catalase pfam05067
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ...
 1-289 6.44e-104

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: 304.56  E-value: 6.44e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499    1 MFRHVKQLQYTVRVSEPNPGLANLLLEQFGGPQGELAAACRYFTQGLSDDDAGR-REMLMDIATEELSHLEIIGSLVGML 79
Cdd:pfam05067   1 MFVHDKLLQYPVKPDHPDPVLAKKLQEQLGGQFGELSAAMRYLFQGFNTRDKGKyKDLLMDIGTEELGHVEMIATMIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499   80 NKGAKGELAEGTESEAeLYRSLTQNGNDSHitSLLYGGGPALTNSGGVPWTAAYIDTIGEVTADLRSNIAAEARAKIIYE 159
Cdd:pfam05067  81 LKGATFDQQEDAAEEP-VIGSVLGGMNPQH--AIVSGLGAMPMDSMGVPWTADYIVASGNLIADLRANIAAEAQARLQYM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499  160 RLINLTDDPGVKDTLSFLMTREVAHQLSFEKALYSIRNNF------PPGKLPPVEQYTDVYYNMSQGD-DPRGSWNSDEN 232
Cdd:pfam05067 158 RLYEMTDDPGVRDMLSFLLARETVHQNQFYKALEILEEVEtivvpvPFPRKLEKQEVARKLFNFSRGDeSTIGRWAKGEA 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446410499  233 FNYVAEPMPAVDGGDGLATVKLpreqmallkamaertKSDPTVDPLTGAELGCGEPK 289
Cdd:pfam05067 238 PDGGGAFEYVKEPGAGAPIPDL---------------RPAPMISHNTFLEIAKRLPP 279
Mn_catalase cd01051
Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member ...
 1-196 7.51e-82

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: 243.64  E-value: 7.51e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499   1 MFRHVKQLQYTVRVSEPNPGLANLLLEQFGGPQGELAAACRYFTQGLSDD-DAGRREMLMDIATEELSHLEIIGSLVGML 79
Cdd:cd01051    1 MFYHVKKLQYPVRVDKPDPRFAKLLQEQLGGAFGELSAAMQYLFQSFNFReDPKYRDLLLDIGTEELSHLEMVATLIAML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499  80 nkgakgelaegteseaelyrsltqngndshitsllygggpaLTNSGGVPWTAAYIDTIGEVTADLRSNIAAEARAKIIYE 159
Cdd:cd01051   81 -----------------------------------------LKDSQGVPWTAAYIQSSGNLVADLRSNIAAESRARLTYE 119

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446410499 160 RLINLTDDPGVKDTLSFLMTREVAHQLSFEKALYSIR 196
Cdd:cd01051  120 RLYEMTDDPGVKDTLSFLLVREIVHQNAFGKALESLG 156
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 12-192 3.83e-16

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: 73.85  E-value: 3.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499  12 VRVSEPNPGLANLLLEQFGGPQGELAAACRYFTQGLSDDDAGR--REMLMDIATEELSHLEIIGSLVGMLnkgakgelae 89
Cdd:cd07908    5 IKVAGPNPRYAELLLDDYAGTNSELTAISQYIYQHLISEEKYPeiAETFLGIAIVEMHHLEILGQLIVLL---------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499  90 gteseaelyrsltqngndshitsllyGGGPAL---TNSGGVPWTAAYIDTIGEVTADLRSNIAAEARAKIIYERLINLTD 166
Cdd:cd07908   75 --------------------------GGDPRYrssSSDKFTYWTGKYVNYGESIKEMLKLDIASEKAAIAKYKRQAETIK 128

                        170       180
                 ....*....|....*....|....*.
gi 446410499 167 DPGVKDTLSFLMTREVAHQLSFEKAL 192
Cdd:cd07908  129 DPYIRALLNRIILDEKLHIKILEELL 154
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 34-192 1.50e-04

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: 40.94  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410499  34 GELAAACRYFTQGLSDDDAGRREMLMDIATEELSHLEIIgslvgmlnkgakgelaegteseAELYRSLtqngndshitsl 113
Cdd:cd00657    9 GEYAAIIAYGQLAARAPDPDLKDELLEIADEERRHADAL----------------------AERLREL------------ 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410499 114 lyGGGPALTNSGGVPWTAAYiDTIGEVTADLRSNIAAEARAKIIYERLINLTDDPGVKDTLSFLMTREVAHQLSFEKAL 192
Cdd:cd00657   55 --GGTPPLPPAHLLAAYALP-KTSDDPAEALRAALEVEARAIAAYRELIEQADDPELRRLLERILADEQRHAAWFRKLL 130
Ferritin_like_AB2 cd01048
Uncharacterized family of ferritin-like proteins found in archaea and bacteria; Ferritin-like ...
 119-192 5.17e-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: 39.19  E-value: 5.17e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410499 119 PALTNSGGVPWTAAYIDTIGEVTADLRSNIAAEARAKII----YERLINLTDDPGVKDTLSFLMTREVAHQLSFEKAL 192
Cdd:cd01048   58 PVDPFSGGVFTNPQYNQLVEQGPKSLQDALEVGVLIEELdiadYDRLLERTQNPDIRDVFENLQAASRNHHLPFFRRL 135
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
144-195 9.91e-03

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


Pssm-ID: 441240  Cd Length: 141  Bit Score: 35.85  E-value: 9.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446410499 144 LRSNIAAEARAKIIYERLINLTDDPGVKDTLSFLMTREVAHQLSFEKALYSI 195
Cdd:COG1633    6 LKEAIAMEEEAIEFYLELAEKAKDPELKKLFEELAEEEKKHAELLEKLYEKL 57
 
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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