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Conserved domains on  [gi|1018191640|ref|NP_001309749|]
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superoxide dismutase [Mn], mitochondrial isoform E [Homo sapiens]

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];
1-170 5.78e-92

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 265.84  E-value: 5.78e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640   1 MQLHHSKHHAAYVNNLNVTEEKYQEALAK--GDVTAQI--ALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEAIK 76
Cdd:COG0605    21 MELHHDKHHQAYVNNLNAALEGLAELEDKslEEIIKKLseELKRALRNNAGGHWNHTLFWENLSPNGGGEPTGELAAAIE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640  77 RDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLqgTTGLIPLLGIDVWEHAYYLQYKNVRPDYL 155
Cdd:COG0605   101 ADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDnPL--MAGGTPLLGLDVWEHAYYLDYQNRRPDYV 177
                         170
                  ....*....|....*
gi 1018191640 156 KAIWNVINWENVTER 170
Cdd:COG0605   178 DAFWNVVNWDFVEKR 192
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
1-170 5.78e-92

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 265.84  E-value: 5.78e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640   1 MQLHHSKHHAAYVNNLNVTEEKYQEALAK--GDVTAQI--ALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEAIK 76
Cdd:COG0605    21 MELHHDKHHQAYVNNLNAALEGLAELEDKslEEIIKKLseELKRALRNNAGGHWNHTLFWENLSPNGGGEPTGELAAAIE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640  77 RDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLqgTTGLIPLLGIDVWEHAYYLQYKNVRPDYL 155
Cdd:COG0605   101 ADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDnPL--MAGGTPLLGLDVWEHAYYLDYQNRRPDYV 177
                         170
                  ....*....|....*
gi 1018191640 156 KAIWNVINWENVTER 170
Cdd:COG0605   178 DAFWNVVNWDFVEKR 192
PLN02471 PLN02471
superoxide dismutase [Mn]
1-171 2.97e-75

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 225.17  E-value: 2.97e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640   1 MQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSP--NGGGE-PKGELLEAIKR 77
Cdd:PLN02471   52 MQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFWKNLAPvsEGGGEpPHGSLGWAIDE 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640  78 DFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTG-LIPLLGIDVWEHAYYLQYKNVRPDYLK 156
Cdd:PLN02471  132 HFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGPsLVPLLGIDVWEHAYYLQYKNVRPDYLK 211
                         170
                  ....*....|....*
gi 1018191640 157 AIWNVINWENVTERY 171
Cdd:PLN02471  212 NIWKVMNWKYASEVY 226
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
67-170 4.11e-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: 181.86  E-value: 4.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640  67 PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKeRGHLQIAACPNQDPLQgTTGLIPLLGIDVWEHAYYLQ 146
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPL-TDGLTPLLGLDVWEHAYYLD 78
                          90       100
                  ....*....|....*....|....
gi 1018191640 147 YKNVRPDYLKAIWNVINWENVTER 170
Cdd:pfam02777  79 YQNRRADYVKAFWNVVNWDEVEKR 102
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
1-170 5.78e-92

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 265.84  E-value: 5.78e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640   1 MQLHHSKHHAAYVNNLNVTEEKYQEALAK--GDVTAQI--ALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEAIK 76
Cdd:COG0605    21 MELHHDKHHQAYVNNLNAALEGLAELEDKslEEIIKKLseELKRALRNNAGGHWNHTLFWENLSPNGGGEPTGELAAAIE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640  77 RDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLqgTTGLIPLLGIDVWEHAYYLQYKNVRPDYL 155
Cdd:COG0605   101 ADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDnPL--MAGGTPLLGLDVWEHAYYLDYQNRRPDYV 177
                         170
                  ....*....|....*
gi 1018191640 156 KAIWNVINWENVTER 170
Cdd:COG0605   178 DAFWNVVNWDFVEKR 192
PLN02471 PLN02471
superoxide dismutase [Mn]
1-171 2.97e-75

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 225.17  E-value: 2.97e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640   1 MQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSP--NGGGE-PKGELLEAIKR 77
Cdd:PLN02471   52 MQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFWKNLAPvsEGGGEpPHGSLGWAIDE 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640  78 DFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTG-LIPLLGIDVWEHAYYLQYKNVRPDYLK 156
Cdd:PLN02471  132 HFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGPsLVPLLGIDVWEHAYYLQYKNVRPDYLK 211
                         170
                  ....*....|....*
gi 1018191640 157 AIWNVINWENVTERY 171
Cdd:PLN02471  212 NIWKVMNWKYASEVY 226
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
67-170 4.11e-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: 181.86  E-value: 4.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640  67 PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKeRGHLQIAACPNQDPLQgTTGLIPLLGIDVWEHAYYLQ 146
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPL-TDGLTPLLGLDVWEHAYYLD 78
                          90       100
                  ....*....|....*....|....
gi 1018191640 147 YKNVRPDYLKAIWNVINWENVTER 170
Cdd:pfam02777  79 YQNRRADYVKAFWNVVNWDEVEKR 102
PRK10925 PRK10925
superoxide dismutase [Mn];
1-175 6.68e-55

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 172.41  E-value: 6.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640   1 MQLHHSKHHAAYVNNLNVTEEKYQE--ALAKGDVTAQIALQPA-----LKFNGGGHINHSIFWTNLSPngGGEPKGELLE 73
Cdd:PRK10925   24 MEIHHTKHHQTYVNNANAALESLPEfaNLPVEELITKLDQLPAdkktvLRNNAGGHANHSLFWKGLKK--GTTLQGDLKA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640  74 AIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERghLQIAACPNQD-PL-----QGTTGLiPLLGIDVWEHAYYLQY 147
Cdd:PRK10925  102 AIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDK--LAVVSTANQDsPLmgeaiSGASGF-PILGLDVWEHAYYLKF 178
                         170       180
                  ....*....|....*....|....*...
gi 1018191640 148 KNVRPDYLKAIWNVINWENVTERYMACK 175
Cdd:PRK10925  179 QNRRPDYIKEFWNVVNWDEAAARFAAKK 206
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
4-164 2.28e-45

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 147.63  E-value: 2.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640   4 HHSKHHAAYVNNLNvteekyqeALAKGDVTAQIALQPALK------FNGGGHI-NHSIFWTNLSPNGGGEPKGELLEAIK 76
Cdd:PTZ00078   22 HYSKHHAGYVNKLN--------GLIKGTPLENKTLEELIKeysgavFNNAAQIwNHNFYWLSMGPNGGGEPTGEIKEKID 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640  77 RDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLQGTTGlIPLLGIDVWEHAYYLQYKNVRPDYL 155
Cdd:PTZ00078   94 EKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKND-GKLEIVQTHDAGnPIKDNTG-KPLLTCDIWEHAYYIDYRNDRASYV 171

                  ....*....
gi 1018191640 156 KAIWNVINW 164
Cdd:PTZ00078  172 NSWWNKVNW 180
PRK10543 PRK10543
superoxide dismutase [Fe];
1-173 1.15e-43

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 143.55  E-value: 1.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640   1 MQLHHSKHHAAYVNNLNvteekyqeALAKGDVTAQIALQPALK------FNGGGHI-NHSIFWTNLSPNGGGEPKGELLE 73
Cdd:PRK10543   24 LEYHYGKHHQTYVTNLN--------NLIKGTAFEGKSLEEIVRsseggvFNNAAQVwNHTFYWNCLAPNAGGEPTGKVAE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640  74 AIKRDFGSFDKFKEKLTAASVGVQGSGWGWLgFNKERGHLQIAACPNQ-DPLqgTTGLIPLLGIDVWEHAYYLQYKNVRP 152
Cdd:PRK10543   96 AIAASFGSFADFKAQFTDAAIKNFGSGWTWL-VKNADGKLAIVSTSNAgTPL--TTDATPLLTVDVWEHAYYIDYRNARP 172
                         170       180
                  ....*....|....*....|.
gi 1018191640 153 DYLKAIWNVINWENVTERYMA 173
Cdd:PRK10543  173 GYLEHFWALVNWEFVAKNLAA 193
PLN02685 PLN02685
iron superoxide dismutase
1-175 5.84e-42

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 142.06  E-value: 5.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640   1 MQLHHSKHHAAYVNNLN-----------VTEEKYQEALAKGDvtaqiaLQPAlkFNGGGHI-NHSIFWTNLSPNGGGEPK 68
Cdd:PLN02685   68 LEYHWGKHHRAYVDNLNkqivgteldgmSLEDVVLITYNKGD------MLPA--FNNAAQAwNHEFFWESMKPGGGGKPS 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640  69 GELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERghLQIAACPNQDPLQGTTGLI----------------P 132
Cdd:PLN02685  140 GELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAYKANR--LDVGNAVNPCPSEEDKKLVvvkspnavnplvwdysP 217
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1018191640 133 LLGIDVWEHAYYLQYKNVRPDYLKA-IWNVINWENVTERYMACK 175
Cdd:PLN02685  218 LLTIDVWEHAYYLDFQNRRPDYISTfMEKLVSWEAVSARLESAK 261
PLN02184 PLN02184
superoxide dismutase [Fe]
1-175 1.94e-37

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 127.94  E-value: 1.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640   1 MQLHHSKHHAAYVNNLNVT------EEKYQEALAKGDVTAQiALQPALKfNGGGHINHSIFWTNLSPNGGGEPKGELLEA 74
Cdd:PLN02184   32 LEFHWGKHHRAYVDNLKKQvlgtelEGKPLEHIIHSTYNNG-DLLPAFN-NAAQAWNHEFFWESMKPGGGGKPSGELLAL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640  75 IKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERghLQIAACPNQ-DPLqgTTGLIPLLGIDVWEHAYYLQYKNVRPD 153
Cdd:PLN02184  110 LERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEK--LKVVKTPNAvNPL--VLGSFPLLTIDVWEHAYYLDFQNRRPD 185
                         170       180
                  ....*....|....*....|...
gi 1018191640 154 YLKA-IWNVINWENVTERYMACK 175
Cdd:PLN02184  186 YIKTfMTNLVSWEAVSARLEAAK 208
PLN02622 PLN02622
iron superoxide dismutase
1-173 5.34e-37

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 128.21  E-value: 5.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640   1 MQLHHSKHHAAYVNNLNvteekyqEALAKGDVTAQIALQ-----------PALKFNGGGHI-NHSIFWTNLSPNGGGEPK 68
Cdd:PLN02622   69 LEVHWGEHHRGYVEGLN-------KQLAKDDILYGYTMDelvkvtynngnPLPEFNNAAQVwNHDFFWESMQPGGGDMPE 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640  69 GELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQ-DPLqgTTGLIPLLGIDVWEHAYYLQY 147
Cdd:PLN02622  142 LGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREERRLEVVKTSNAiNPL--VWDDIPIICLDVWEHAYYLDY 219
                         170       180
                  ....*....|....*....|....*..
gi 1018191640 148 KNVRPDYLKAIWN-VINWENVTERyMA 173
Cdd:PLN02622  220 KNDRGKYVNAFMNhLVSWNAAMAR-MA 245
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
1-60 1.60e-26

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: 95.84  E-value: 1.60e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191640   1 MQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLS 60
Cdd:pfam00081  23 MEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIKALLGGLFNNGGGHWNHSLFWKNLS 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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