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Conserved domains on  [gi|664518152|ref|WP_031034895|]
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MULTISPECIES: superoxide dismutase [Streptomyces]

Protein Classification

superoxide dismutase( domain architecture ID 11427369)

Mn/Fe superoxide dismutase eliminates superoxide radicals by catalyzing their conversion into hydrogen peroxide and oxygen

CATH:  1.10.287.990
EC:  1.15.1.1
Gene Ontology:  GO:0046872|GO:0004784|GO:0006801
PubMed:  3345848|3315461

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
5-198 6.50e-91

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 264.68  E-value: 6.50e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152   5 SLPELPYDYSELEPVINPQIIELHHDKHHAAYVKGANDTLEQLAEARDKE----QWGSINGLEKNLAFHLSGHILHSIYW 80
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSleeiIKKLSEELKRALRNNAGGHWNHTLFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152  81 HNMTGDGGGEPlaadgVGDLADAIAESFGSFAGFKAQLTKAAATTQGSGWGVLAYEPlSGRLIVEQVYDHQGNVGQGATP 160
Cdd:COG0605   81 ENLSPNGGGEP-----TGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDK-DGKLEIVSTPNQDNPLMAGGTP 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 664518152 161 ILVFDAWEHAFYLQYKNQKVDFIDAMWAVVNWQDVAKR 198
Cdd:COG0605  155 LLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
5-198 6.50e-91

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 264.68  E-value: 6.50e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152   5 SLPELPYDYSELEPVINPQIIELHHDKHHAAYVKGANDTLEQLAEARDKE----QWGSINGLEKNLAFHLSGHILHSIYW 80
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSleeiIKKLSEELKRALRNNAGGHWNHTLFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152  81 HNMTGDGGGEPlaadgVGDLADAIAESFGSFAGFKAQLTKAAATTQGSGWGVLAYEPlSGRLIVEQVYDHQGNVGQGATP 160
Cdd:COG0605   81 ENLSPNGGGEP-----TGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDK-DGKLEIVSTPNQDNPLMAGGTP 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 664518152 161 ILVFDAWEHAFYLQYKNQKVDFIDAMWAVVNWQDVAKR 198
Cdd:COG0605  155 LLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PLN02471 PLN02471
superoxide dismutase [Mn]
 4-200 2.34e-52

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 168.16  E-value: 2.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152   4 YSLPELPYDYSELEPVINPQIIELHHDKHHAAYVKGANDTLEQLAEARDKEQWGSINGLEKNLAFHLSGHILHSIYWHNM 83
Cdd:PLN02471  31 FTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFWKNL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152  84 T--GDGGGEPLAadgvGDLADAIAESFGSFAGFKAQLTKAAATTQGSGWGVLAYEPLSGRLIVEQVYDHQGNVGQGAT-- 159
Cdd:PLN02471 111 ApvSEGGGEPPH----GSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGPSlv 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 664518152 160 PILVFDAWEHAFYLQYKNQKVDFIDAMWAVVNWQDVAKRYE 200
Cdd:PLN02471 187 PLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYE 227
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 98-198 9.12e-47

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: 149.50  E-value: 9.12e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152   98 GDLADAIAESFGSFAGFKAQLTKAAATTQGSGWGVLAYEPlSGRLIVEQVYDHQGNVGQGATPILVFDAWEHAFYLQYKN 177
Cdd:pfam02777   3 GALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQN 81

                          90       100
                  ....*....|....*....|.
gi 664518152  178 QKVDFIDAMWAVVNWQDVAKR 198
Cdd:pfam02777  82 RRADYVKAFWNVVNWDEVEKR 102
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
5-198 6.50e-91

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 264.68  E-value: 6.50e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152   5 SLPELPYDYSELEPVINPQIIELHHDKHHAAYVKGANDTLEQLAEARDKE----QWGSINGLEKNLAFHLSGHILHSIYW 80
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSleeiIKKLSEELKRALRNNAGGHWNHTLFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152  81 HNMTGDGGGEPlaadgVGDLADAIAESFGSFAGFKAQLTKAAATTQGSGWGVLAYEPlSGRLIVEQVYDHQGNVGQGATP 160
Cdd:COG0605   81 ENLSPNGGGEP-----TGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDK-DGKLEIVSTPNQDNPLMAGGTP 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 664518152 161 ILVFDAWEHAFYLQYKNQKVDFIDAMWAVVNWQDVAKR 198
Cdd:COG0605  155 LLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PLN02471 PLN02471
superoxide dismutase [Mn]
 4-200 2.34e-52

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 168.16  E-value: 2.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152   4 YSLPELPYDYSELEPVINPQIIELHHDKHHAAYVKGANDTLEQLAEARDKEQWGSINGLEKNLAFHLSGHILHSIYWHNM 83
Cdd:PLN02471  31 FTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFWKNL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152  84 T--GDGGGEPLAadgvGDLADAIAESFGSFAGFKAQLTKAAATTQGSGWGVLAYEPLSGRLIVEQVYDHQGNVGQGAT-- 159
Cdd:PLN02471 111 ApvSEGGGEPPH----GSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGPSlv 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 664518152 160 PILVFDAWEHAFYLQYKNQKVDFIDAMWAVVNWQDVAKRYE 200
Cdd:PLN02471 187 PLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYE 227
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 98-198 9.12e-47

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: 149.50  E-value: 9.12e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152   98 GDLADAIAESFGSFAGFKAQLTKAAATTQGSGWGVLAYEPlSGRLIVEQVYDHQGNVGQGATPILVFDAWEHAFYLQYKN 177
Cdd:pfam02777   3 GALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQN 81

                          90       100
                  ....*....|....*....|.
gi 664518152  178 QKVDFIDAMWAVVNWQDVAKR 198
Cdd:pfam02777  82 RRADYVKAFWNVVNWDEVEKR 102
PRK10925 PRK10925
superoxide dismutase [Mn];
4-203 6.35e-43

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 143.14  E-value: 6.35e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152   4 YSLPELPYDYSELEPVINPQIIELHHDKHHAAYVKGANDTLEQLAEARDKEQWGSINGLEKNLAFHLS-------GHILH 76
Cdd:PRK10925   3 YTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPADKKTvlrnnagGHANH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152  77 SIYWHnmtgdggGEPLAADGVGDLADAIAESFGSFAGFKAQLTKAAATTQGSGWG--VLAYEPLSGRLIVEQVYDHQGNV 154
Cdd:PRK10925  83 SLFWK-------GLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAwlVLKGDKLAVVSTANQDSPLMGEA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 664518152 155 GQGAT--PILVFDAWEHAFYLQYKNQKVDFIDAMWAVVNWQDVAKRYEAAK 203
Cdd:PRK10925 156 ISGASgfPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
PRK10543 PRK10543
superoxide dismutase [Fe];
4-201 3.11e-40

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 135.85  E-value: 3.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152   4 YSLPELPYDYSELEPVINPQIIELHHDKHHAAYVKGANDTLE--QLAEARDKEQWGSINGLEKNLAFHLSGHilhSIYWH 81
Cdd:PRK10543   3 FELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKgtAFEGKSLEEIVRSSEGGVFNNAAQVWNH---TFYWN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152  82 NMTGDGGGEPlaadgVGDLADAIAESFGSFAGFKAQLTKAAATTQGSGWGVLAYEPlSGRLIVEQVYDHQGNVGQGATPI 161
Cdd:PRK10543  80 CLAPNAGGEP-----TGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNA-DGKLAIVSTSNAGTPLTTDATPL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 664518152 162 LVFDAWEHAFYLQYKNQKVDFIDAMWAVVNWQDVAKRYEA 201
Cdd:PRK10543 154 LTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 7-202 5.65e-36

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 124.90  E-value: 5.65e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152   7 PELPYDYSELEPVINPQIIELHHDKHHAAYVKGANDTLEQ--LAEARDKEQWGSINGLEKNLAFHLSGHilhSIYWHNMT 84
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGtpLENKTLEELIKEYSGAVFNNAAQIWNH---NFYWLSMG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152  85 GDGGGEPlaadgVGDLADAIAESFGSFAGFKAQLTKAAATTQGSGWGVLAYEPlSGRLIVEQVYDH----QGNVGqgaTP 160
Cdd:PTZ00078  78 PNGGGEP-----TGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKN-DGKLEIVQTHDAgnpiKDNTG---KP 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 664518152 161 ILVFDAWEHAFYLQYKNQKVDFIDAMWAVVNWQDVAKRYEAA 202
Cdd:PTZ00078 149 LLTCDIWEHAYYIDYRNDRASYVNSWWNKVNWDFANKNLKKL 190
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 4-84 9.03e-33

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: 113.17  E-value: 9.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152    4 YSLPELPYDYSELEPVINPQIIELHHDKHHAAYVKGANDTLEQLAEARDKEQWGSINGLEKNLAFHLSGHILHSIYWHNM 83
Cdd:pfam00081   2 YELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIKALLGGLFNNGGGHWNHSLFWKNL 81


                  .
gi 664518152   84 T 84
Cdd:pfam00081  82 S 82
PLN02685 PLN02685
iron superoxide dismutase
 2-206 8.24e-29

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 109.32  E-value: 8.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152   2 AVYSLPELPYDYSELEPVINPQIIELHHDKHHAAYVKGANDTLEQLA-EARDKEQWGSINGLEKNL--AFHLSGHIL-HS 77
Cdd:PLN02685  45 AKFELKPPPYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQIVGTElDGMSLEDVVLITYNKGDMlpAFNNAAQAWnHE 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152  78 IYWHNMTGDGGGEPlaadgVGDLADAIAESFGSFAGFKAQLTKAAATTQGSGWGVLAYE-----------PLSG----RL 142
Cdd:PLN02685 125 FFWESMKPGGGGKP-----SGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAYKanrldvgnavnPCPSeedkKL 199

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664518152 143 IVEQVYDHQGNVGQGATPILVFDAWEHAFYLQYKNQKVDFIDA-MWAVVNWQDVAKRYEAAKSRA 206
Cdd:PLN02685 200 VVVKSPNAVNPLVWDYSPLLTIDVWEHAYYLDFQNRRPDYISTfMEKLVSWEAVSARLESAKARA 264
PLN02622 PLN02622
iron superoxide dismutase
 1-208 5.89e-27

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 103.55  E-value: 5.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152   1 MAVYSLPELPYDYSELEPVINPQIIELHHDKHHAAYVKGANDTLeqlaeARDKEQWG---------SINGLEKNLAFHLS 71
Cdd:PLN02622  45 VAYYGLKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQL-----AKDDILYGytmdelvkvTYNNGNPLPEFNNA 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152  72 GHIL-HSIYWHNMTGDGGGEPLAAdgvgdLADAIAESFGSFAGFKAQLTKAAATTQGSGWGVLAYEPLSGRLIVEQVYDH 150
Cdd:PLN02622 120 AQVWnHDFFWESMQPGGGDMPELG-----VLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREERRLEVVKTSNA 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 664518152 151 QGNVGQGATPILVFDAWEHAFYLQYKNQKVDFIDA-MWAVVNWQDVAKRYEAAKSRANV 208
Cdd:PLN02622 195 INPLVWDDIPIICLDVWEHAYYLDYKNDRGKYVNAfMNHLVSWNAAMARMARAEAFVNL 253
PLN02184 PLN02184
superoxide dismutase [Fe]
 2-207 2.19e-25

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 98.28  E-value: 2.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152   2 AVYSLPELPYDYSELEPVINPQIIELHHDKHHAAYVKG-ANDTLEQLAEARDKEQ--WGSINGLEKNLAFHLSGHIL-HS 77
Cdd:PLN02184   9 ANYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNlKKQVLGTELEGKPLEHiiHSTYNNGDLLPAFNNAAQAWnHE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664518152  78 IYWHNMTGDGGGEPlaadgVGDLADAIAESFGSFAGFKAQLTKAAATTQGSGWGVLAYEplSGRLIVEQVYDHQGNVGQG 157
Cdd:PLN02184  89 FFWESMKPGGGGKP-----SGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYS--NEKLKVVKTPNAVNPLVLG 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 664518152 158 ATPILVFDAWEHAFYLQYKNQKVDFIDA-MWAVVNWQDVAKRYEAAKSRAN 207
Cdd:PLN02184 162 SFPLLTIDVWEHAYYLDFQNRRPDYIKTfMTNLVSWEAVSARLEAAKAASA 212
 
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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