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Conserved domains on  [gi|1134749481|ref|NP_312861|]
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Fe-Mn family superoxide dismutase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

superoxide dismutase( domain architecture ID 11485100)

superoxide dismutase [Mn] eliminates superoxide radicals by catalyzing their conversion into hydrogen peroxide and oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10925 PRK10925
superoxide dismutase [Mn];
1-206 9.93e-159

superoxide dismutase [Mn];


:

Pssm-ID: 182843  Cd Length: 206  Bit Score: 436.66  E-value: 9.93e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80
Cdd:PRK10925    1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481  81 NHSLFWKGLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGDKLAVVSTANQDSPLMGEAISGAS 160
Cdd:PRK10925   81 NHSLFWKGLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDKLAVVSTANQDSPLMGEAISGAS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1134749481 161 GFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
Cdd:PRK10925  161 GFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
 
Name Accession Description Interval E-value
PRK10925 PRK10925
superoxide dismutase [Mn];
1-206 9.93e-159

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 436.66  E-value: 9.93e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80
Cdd:PRK10925    1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481  81 NHSLFWKGLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGDKLAVVSTANQDSPLMGEAISGAS 160
Cdd:PRK10925   81 NHSLFWKGLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDKLAVVSTANQDSPLMGEAISGAS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1134749481 161 GFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
Cdd:PRK10925  161 GFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-201 6.03e-120

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 337.87  E-value: 6.03e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481   4 TLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDqlpADKKTVLRNNAGGHANHS 83
Cdd:COG0605     1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEIIKKLS---EELKRALRNNAGGHWNHT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481  84 LFWKGLKK--GTTLQGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGD-KLAVVSTANQDSPLMgeaisgAS 160
Cdd:COG0605    78 LFWENLSPngGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDgKLEIVSTPNQDNPLM------AG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1134749481 161 GFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAAR 201
Cdd:COG0605   152 GTPLLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 96-201 2.39e-62

Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one. In humans, there is a cytoplasmic Cu/Zn SOD, and a mitochondrial Mn/Fe SOD. C-terminal domain is a mixed alpha/beta fold.


Pssm-ID: 460691  Cd Length: 102  Bit Score: 188.79  E-value: 2.39e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481  96 QGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVL-KGDKLAVVSTANQDSPLMGEAIsgasgfPILGLDVWEHAY 174
Cdd:pfam02777   2 TGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYdPDGKLEIVTTPNQDNPLTDGLT------PLLGLDVWEHAY 75

                          90       100
                  ....*....|....*....|....*..
gi 1134749481 175 YLKFQNRRPDYIKEFWNVVNWDEAAAR 201
Cdd:pfam02777  76 YLDYQNRRADYVKAFWNVVNWDEVEKR 102
 
Name Accession Description Interval E-value
PRK10925 PRK10925
superoxide dismutase [Mn];
1-206 9.93e-159

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 436.66  E-value: 9.93e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80
Cdd:PRK10925    1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481  81 NHSLFWKGLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGDKLAVVSTANQDSPLMGEAISGAS 160
Cdd:PRK10925   81 NHSLFWKGLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDKLAVVSTANQDSPLMGEAISGAS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1134749481 161 GFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
Cdd:PRK10925  161 GFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-201 6.03e-120

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 337.87  E-value: 6.03e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481   4 TLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDqlpADKKTVLRNNAGGHANHS 83
Cdd:COG0605     1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEIIKKLS---EELKRALRNNAGGHWNHT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481  84 LFWKGLKK--GTTLQGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGD-KLAVVSTANQDSPLMgeaisgAS 160
Cdd:COG0605    78 LFWENLSPngGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDgKLEIVSTPNQDNPLM------AG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1134749481 161 GFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAAR 201
Cdd:COG0605   152 GTPLLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 96-201 2.39e-62

Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one. In humans, there is a cytoplasmic Cu/Zn SOD, and a mitochondrial Mn/Fe SOD. C-terminal domain is a mixed alpha/beta fold.


Pssm-ID: 460691  Cd Length: 102  Bit Score: 188.79  E-value: 2.39e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481  96 QGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVL-KGDKLAVVSTANQDSPLMGEAIsgasgfPILGLDVWEHAY 174
Cdd:pfam02777   2 TGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYdPDGKLEIVTTPNQDNPLTDGLT------PLLGLDVWEHAY 75

                          90       100
                  ....*....|....*....|....*..
gi 1134749481 175 YLKFQNRRPDYIKEFWNVVNWDEAAAR 201
Cdd:pfam02777  76 YLDYQNRRADYVKAFWNVVNWDEVEKR 102
PRK10543 PRK10543
superoxide dismutase [Fe];
1-204 1.78e-56

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 177.07  E-value: 1.78e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESlPEFANLPVEELITKLDqlpadkkTVLRNNAGGHA 80
Cdd:PRK10543    1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKG-TAFEGKSLEEIVRSSE-------GGVFNNAAQVW 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481  81 NHSLFWKGL--KKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGD-KLAVVSTANQDSPLMGEAIs 157
Cdd:PRK10543   73 NHTFYWNCLapNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADgKLAIVSTSNAGTPLTTDAT- 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1134749481 158 gasgfPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAA 204
Cdd:PRK10543  152 -----PLLTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
PLN02471 PLN02471
superoxide dismutase [Mn]
 2-199 3.67e-56

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 177.79  E-value: 3.67e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481   2 SYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLdqlpadkKTVLRNNAGGHAN 81
Cdd:PLN02471   30 TFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKL-------QSAIKFNGGGHVN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481  82 HSLFWKGLKK-----GTTLQGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGD--KLAVVSTANQDsPLMGE 154
Cdd:PLN02471  103 HSIFWKNLAPvseggGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKElkKLVVETTANQD-PLVTK 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1134749481 155 aisGASGFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAA 199
Cdd:PLN02471  182 ---GPSLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYAS 223
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 6-198 2.21e-55

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 174.59  E-value: 2.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481   6 PSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPeFANLPVEELITKLDqlpadkkTVLRNNAGGHANHSLF 85
Cdd:PTZ00078    1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTP-LENKTLEELIKEYS-------GAVFNNAAQIWNHNFY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481  86 WKGLKK--GTTLQGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGD-KLAVVSTANQDSPlmgeaISGASGF 162
Cdd:PTZ00078   73 WLSMGPngGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDgKLEIVQTHDAGNP-----IKDNTGK 147

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1134749481 163 PILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEA 198
Cdd:PTZ00078  148 PLLTCDIWEHAYYIDYRNDRASYVNSWWNKVNWDFA 183
PLN02685 PLN02685
iron superoxide dismutase
 3-206 1.02e-54

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 176.35  E-value: 1.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481   3 YTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESlPEFANLPVEELIT----KLDQLPAdkktvlRNNAGG 78
Cdd:PLN02685   47 FELKPPPYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQIVG-TELDGMSLEDVVLitynKGDMLPA------FNNAAQ 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481  79 HANHSLFWKGLKKGTTLQ--GDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGD-----------------KL 139
Cdd:PLN02685  120 AWNHEFFWESMKPGGGGKpsGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAYKANrldvgnavnpcpseedkKL 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749481 140 AVVSTANQDSPLMGEAisgasgFPILGLDVWEHAYYLKFQNRRPDYIKEFW-NVVNWDEAAARFAAKK 206
Cdd:PLN02685  200 VVVKSPNAVNPLVWDY------SPLLTIDVWEHAYYLDFQNRRPDYISTFMeKLVSWEAVSARLESAK 261
PLN02184 PLN02184
superoxide dismutase [Fe]
 2-206 3.01e-51

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 164.54  E-value: 3.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481   2 SYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESlPEFANLPVEELITKL----DQLPAdkktvlRNNAG 77
Cdd:PLN02184   10 NYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLG-TELEGKPLEHIIHSTynngDLLPA------FNNAA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481  78 GHANHSLFWKGLKKGT--TLQGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGDKLAVVSTANQDSPLMgea 155
Cdd:PLN02184   83 QAWNHEFFWESMKPGGggKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEKLKVVKTPNAVNPLV--- 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134749481 156 isgASGFPILGLDVWEHAYYLKFQNRRPDYIKEFW-NVVNWDEAAARFAAKK 206
Cdd:PLN02184  160 ---LGSFPLLTIDVWEHAYYLDFQNRRPDYIKTFMtNLVSWEAVSARLEAAK 208
PLN02622 PLN02622
iron superoxide dismutase
 3-203 9.65e-49

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 159.79  E-value: 9.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481   3 YTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKL----DQLPAdkktvlRNNAGG 78
Cdd:PLN02622   48 YGLKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAKDDILYGYTMDELVKVTynngNPLPE------FNNAAQ 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481  79 HANHSLFWKGLKK--GTTLQGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGD--KLAVVSTANQDSPLMGE 154
Cdd:PLN02622  122 VWNHDFFWESMQPggGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREerRLEVVKTSNAINPLVWD 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1134749481 155 AIsgasgfPILGLDVWEHAYYLKFQNRRPDYIKEFWN-VVNWDEAAARFA 203
Cdd:PLN02622  202 DI------PIICLDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAMARMA 245
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 2-90 1.97e-40

Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one. In humans, there is a cytoplasmic Cu/Zn SOD, and a mitochondrial Mn/Fe SOD. N-terminal domain is a long alpha antiparallel hairpin. A small fragment of YTRE_LEPBI matches well - sequencing error?


Pssm-ID: 425457  Cd Length: 82  Bit Score: 132.43  E-value: 1.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749481   2 SYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLpEFANLPVEELITKldqlpaDKKTVLRNNAGGHAN 81
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGL-EEARKPLEELIIK------ALLGGLFNNGGGHWN 73


                  ....*....
gi 1134749481  82 HSLFWKGLK 90
Cdd:pfam00081  74 HSLFWKNLS 82
 
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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