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Conserved domains on  [gi|675091871|gb|AIL35839|]
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Superoxide dismutase [Fe] [Shigella flexneri 2003036]

Protein Classification

superoxide dismutase( domain architecture ID 11484781)

superoxide dismutase [Fe] 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
PRK10543 PRK10543
superoxide dismutase [Fe];
1-193 5.26e-142

superoxide dismutase [Fe];


:

Pssm-ID: 182534  Cd Length: 193  Bit Score: 393.16  E-value: 5.26e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871   1 MSFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGGVFNNAAQVWNHTFYWNC 80
Cdd:PRK10543   1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSSEGGVFNNAAQVWNHTFYWNC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871  81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWE 160
Cdd:PRK10543  81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDATPLLTVDVWE 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 675091871 161 HAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
Cdd:PRK10543 161 HAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
 
Name Accession Description Interval E-value
PRK10543 PRK10543
superoxide dismutase [Fe];
1-193 5.26e-142

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 393.16  E-value: 5.26e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871   1 MSFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGGVFNNAAQVWNHTFYWNC 80
Cdd:PRK10543   1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSSEGGVFNNAAQVWNHTFYWNC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871  81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWE 160
Cdd:PRK10543  81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDATPLLTVDVWE 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 675091871 161 HAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
Cdd:PRK10543 161 HAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-190 4.40e-122

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 342.49  E-value: 4.40e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871   4 ELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTA-FEGKSLEEIIRSS----EGGVFNNAAQVWNHTFYW 78
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAeLEDKSLEEIIKKLseelKRALRNNAGGHWNHTLFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871  79 NCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDV 158
Cdd:COG0605   81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLGLDV 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 675091871 159 WEHAYYIDYRNARPGYLEHFWALVNWEFVAKN 190
Cdd:COG0605  161 WEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 89-190 2.21e-60

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: 183.40  E-value: 2.21e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871   89 PTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWEHAYYIDYR 168
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQ 80

                          90       100
                  ....*....|....*....|..
gi 675091871  169 NARPGYLEHFWALVNWEFVAKN 190
Cdd:pfam02777  81 NRRADYVKAFWNVVNWDEVEKR 102
 
Name Accession Description Interval E-value
PRK10543 PRK10543
superoxide dismutase [Fe];
1-193 5.26e-142

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 393.16  E-value: 5.26e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871   1 MSFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGGVFNNAAQVWNHTFYWNC 80
Cdd:PRK10543   1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSSEGGVFNNAAQVWNHTFYWNC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871  81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWE 160
Cdd:PRK10543  81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDATPLLTVDVWE 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 675091871 161 HAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
Cdd:PRK10543 161 HAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-190 4.40e-122

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 342.49  E-value: 4.40e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871   4 ELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTA-FEGKSLEEIIRSS----EGGVFNNAAQVWNHTFYW 78
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAeLEDKSLEEIIKKLseelKRALRNNAGGHWNHTLFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871  79 NCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDV 158
Cdd:COG0605   81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLGLDV 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 675091871 159 WEHAYYIDYRNARPGYLEHFWALVNWEFVAKN 190
Cdd:COG0605  161 WEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 6-193 9.18e-93

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 268.58  E-value: 9.18e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871   6 PALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGGVFNNAAQVWNHTFYWNCLAPNA 85
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLENKTLEELIKEYSGAVFNNAAQIWNHNFYWLSMGPNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871  86 GGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTD-ATPLLTVDVWEHAYY 164
Cdd:PTZ00078  81 GGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPIKDNtGKPLLTCDIWEHAYY 160

                        170       180
                 ....*....|....*....|....*....
gi 675091871 165 IDYRNARPGYLEHFWALVNWEFVAKNLAA 193
Cdd:PTZ00078 161 IDYRNDRASYVNSWWNKVNWDFANKNLKK 189
PLN02685 PLN02685
iron superoxide dismutase
 3-193 4.06e-75

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 227.58  E-value: 4.06e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871   3 FELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEII-----RSSEGGVFNNAAQVWNHTFY 77
Cdd:PLN02685  47 FELKPPPYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQIVGTELDGMSLEDVVlitynKGDMLPAFNNAAQAWNHEFF 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871  78 WNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLV----------------KNSDGKLAIVSTSN 141
Cdd:PLN02685 127 WESMKPGGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAykanrldvgnavnpcpSEEDKKLVVVKSPN 206

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 675091871 142 AGTPLTTDATPLLTVDVWEHAYYIDYRNARPGYLEHFWA-LVNWEFVAKNLAA 193
Cdd:PLN02685 207 AVNPLVWDYSPLLTIDVWEHAYYLDFQNRRPDYISTFMEkLVSWEAVSARLES 259
PLN02622 PLN02622
iron superoxide dismutase
 3-192 4.90e-61

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 190.61  E-value: 4.90e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871   3 FELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNN-LIKGTAFEGKSLEEIIRSSEGG-----VFNNAAQVWNHTF 76
Cdd:PLN02622  48 YGLKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKqLAKDDILYGYTMDELVKVTYNNgnplpEFNNAAQVWNHDF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871  77 YWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLV-KNSDGKLAIVSTSNAGTPLTTDATPLLT 155
Cdd:PLN02622 128 FWESMQPGGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVlKREERRLEVVKTSNAINPLVWDDIPIIC 207

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 675091871 156 VDVWEHAYYIDYRNARPGYLEHFWA-LVNWEFVAKNLA 192
Cdd:PLN02622 208 LDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAMARMA 245
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 89-190 2.21e-60

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: 183.40  E-value: 2.21e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871   89 PTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWEHAYYIDYR 168
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQ 80

                          90       100
                  ....*....|....*....|..
gi 675091871  169 NARPGYLEHFWALVNWEFVAKN 190
Cdd:pfam02777  81 NRRADYVKAFWNVVNWDEVEKR 102
PLN02184 PLN02184
superoxide dismutase [Fe]
 2-193 4.70e-58

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 181.48  E-value: 4.70e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871   2 SFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGG-----VFNNAAQVWNHTF 76
Cdd:PLN02184  10 NYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTELEGKPLEHIIHSTYNNgdllpAFNNAAQAWNHEF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871  77 YWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDgKLAIVSTSNAGTPLTTDATPLLTV 156
Cdd:PLN02184  90 FWESMKPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNE-KLKVVKTPNAVNPLVLGSFPLLTI 168

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 675091871 157 DVWEHAYYIDYRNARPGYLEHFWA-LVNWEFVAKNLAA 193
Cdd:PLN02184 169 DVWEHAYYLDFQNRRPDYIKTFMTnLVSWEAVSARLEA 206
PRK10925 PRK10925
superoxide dismutase [Mn];
1-193 2.95e-55

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 173.95  E-value: 2.95e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871   1 MSFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKG-TAFEGKSLEEIIRS-------SEGGVFNNAAQVW 72
Cdd:PRK10925   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESlPEFANLPVEELITKldqlpadKKTVLRNNAGGHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871  73 NHTFYWNCLapNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDgKLAIVSTSNAGTPLTTDAT- 151
Cdd:PRK10925  81 NHSLFWKGL--KKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGD-KLAVVSTANQDSPLMGEAIs 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 675091871 152 -----PLLTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
Cdd:PRK10925 158 gasgfPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAA 204
PLN02471 PLN02471
superoxide dismutase [Mn]
 2-186 2.24e-43

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 144.67  E-value: 2.24e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871   2 SFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIK--GTAFEGKSLEEIIRSSEGGVFNNAAQVwNHTFYWN 79
Cdd:PLN02471  30 TFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEqlDQAVEKGDASAVVKLQSAIKFNGGGHV-NHSIFWK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871  80 CLAP--NAGGE-PTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDA---TPL 153
Cdd:PLN02471 109 NLAPvsEGGGEpPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGpslVPL 188

                        170       180       190
                 ....*....|....*....|....*....|...
gi 675091871 154 LTVDVWEHAYYIDYRNARPGYLEHFWALVNWEF 186
Cdd:PLN02471 189 LGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKY 221
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 2-82 2.12e-41

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: 134.36  E-value: 2.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675091871    2 SFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEII-RSSEGGVFNNAAQVWNHTFYWNC 80
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIiKALLGGLFNNGGGHWNHSLFWKN 80


                  ..
gi 675091871   81 LA 82
Cdd:pfam00081  81 LS 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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