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Conserved domains on  [gi|30841303|gb|AAP34407|]
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manganese-containing superoxide dismutase, partial [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];
26-212 4.27e-106

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 303.20  E-value: 4.27e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303  26 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAK--GDVTAQI--ALQPALKFNGGGHINHSIFW 101
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKslEEIIKKLseELKRALRNNAGGHWNHTLFW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303 102 TNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLqgTTGLIPLLG 180
Cdd:COG0605  81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDnPL--MAGGTPLLG 157
                       170       180       190
                ....*....|....*....|....*....|..
gi 30841303 181 IDVWEHAYYLQYKNVRPDYLKAIWNVINWENV 212
Cdd:COG0605 158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFV 189
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
26-212 4.27e-106

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 303.20  E-value: 4.27e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303  26 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAK--GDVTAQI--ALQPALKFNGGGHINHSIFW 101
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKslEEIIKKLseELKRALRNNAGGHWNHTLFW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303 102 TNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLqgTTGLIPLLG 180
Cdd:COG0605  81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDnPL--MAGGTPLLG 157
                       170       180       190
                ....*....|....*....|....*....|..
gi 30841303 181 IDVWEHAYYLQYKNVRPDYLKAIWNVINWENV 212
Cdd:COG0605 158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFV 189
PLN02471 PLN02471
superoxide dismutase [Mn]
23-210 3.36e-88

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 259.45  E-value: 3.36e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303   23 QKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWT 102
Cdd:PLN02471  29 QTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFWK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303  103 NLSP--NGGGE-PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTG-LIPL 178
Cdd:PLN02471 109 NLAPvsEGGGEpPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGPsLVPL 188
                        170       180       190
                 ....*....|....*....|....*....|..
gi 30841303  179 LGIDVWEHAYYLQYKNVRPDYLKAIWNVINWE 210
Cdd:PLN02471 189 LGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWK 220
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
112-212 1.99e-59

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: 1.99e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303   112 PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKeRGHLQIAACPNQDPLQgTTGLIPLLGIDVWEHAYYLQ 191
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPL-TDGLTPLLGLDVWEHAYYLD 78
                          90       100
                  ....*....|....*....|.
gi 30841303   192 YKNVRPDYLKAIWNVINWENV 212
Cdd:pfam02777  79 YQNRRADYVKAFWNVVNWDEV 99
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
26-212 4.27e-106

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 303.20  E-value: 4.27e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303  26 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAK--GDVTAQI--ALQPALKFNGGGHINHSIFW 101
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKslEEIIKKLseELKRALRNNAGGHWNHTLFW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303 102 TNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLqgTTGLIPLLG 180
Cdd:COG0605  81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDnPL--MAGGTPLLG 157
                       170       180       190
                ....*....|....*....|....*....|..
gi 30841303 181 IDVWEHAYYLQYKNVRPDYLKAIWNVINWENV 212
Cdd:COG0605 158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFV 189
PLN02471 PLN02471
superoxide dismutase [Mn]
23-210 3.36e-88

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 259.45  E-value: 3.36e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303   23 QKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWT 102
Cdd:PLN02471  29 QTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFWK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303  103 NLSP--NGGGE-PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTG-LIPL 178
Cdd:PLN02471 109 NLAPvsEGGGEpPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGPsLVPL 188
                        170       180       190
                 ....*....|....*....|....*....|..
gi 30841303  179 LGIDVWEHAYYLQYKNVRPDYLKAIWNVINWE 210
Cdd:PLN02471 189 LGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWK 220
PRK10925 PRK10925
superoxide dismutase [Mn];
25-210 2.21e-64

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 198.22  E-value: 2.21e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303   25 HSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQE--ALAKGDVTAQIALQPA-----LKFNGGGHINH 97
Cdd:PRK10925   3 YTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEfaNLPVEELITKLDQLPAdkktvLRNNAGGHANH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303   98 SIFWTNLSPngGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERghLQIAACPNQD-PL-----QG 171
Cdd:PRK10925  83 SLFWKGLKK--GTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDK--LAVVSTANQDsPLmgeaiSG 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 30841303  172 TTGLiPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWE 210
Cdd:PRK10925 159 ASGF-PILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWD 196
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
112-212 1.99e-59

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: 1.99e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303   112 PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKeRGHLQIAACPNQDPLQgTTGLIPLLGIDVWEHAYYLQ 191
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPL-TDGLTPLLGLDVWEHAYYLD 78
                          90       100
                  ....*....|....*....|.
gi 30841303   192 YKNVRPDYLKAIWNVINWENV 212
Cdd:pfam02777  79 YQNRRADYVKAFWNVVNWDEV 99
PRK10543 PRK10543
superoxide dismutase [Fe];
27-212 6.85e-53

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 168.21  E-value: 6.85e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303   27 LPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNvteekyqeALAKGDVTAQIALQPALK------FNGGGHI-NHSI 99
Cdd:PRK10543   5 LPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLN--------NLIKGTAFEGKSLEEIVRsseggvFNNAAQVwNHTF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303  100 FWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLgFNKERGHLQIAACPNQ-DPLqgTTGLIPL 178
Cdd:PRK10543  77 YWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWL-VKNADGKLAIVSTSNAgTPL--TTDATPL 153
                        170       180       190
                 ....*....|....*....|....*....|....
gi 30841303  179 LGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENV 212
Cdd:PRK10543 154 LTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFV 187
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
28-209 2.66e-51

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 164.19  E-value: 2.66e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303   28 PDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNvteekyqeALAKGDVTAQIALQPALK------FNGGGHI-NHSIF 100
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLN--------GLIKGTPLENKTLEELIKeysgavFNNAAQIwNHNFY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303  101 WTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLQGTTGlIPLL 179
Cdd:PTZ00078  73 WLSMGPNGGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKND-GKLEIVQTHDAGnPIKDNTG-KPLL 150
                        170       180       190
                 ....*....|....*....|....*....|
gi 30841303  180 GIDVWEHAYYLQYKNVRPDYLKAIWNVINW 209
Cdd:PTZ00078 151 TCDIWEHAYYIDYRNDRASYVNSWWNKVNW 180
PLN02685 PLN02685
iron superoxide dismutase
31-213 2.36e-47

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 157.47  E-value: 2.36e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303   31 PYDYGALEPHINAQIMQLHHSKHHAAYVNNLN-----------VTEEKYQEALAKGDvtaqiaLQPAlkFNGGGHI-NHS 98
Cdd:PLN02685  53 PYPLDALEPHMSRETLEYHWGKHHRAYVDNLNkqivgteldgmSLEDVVLITYNKGD------MLPA--FNNAAQAwNHE 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303   99 IFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERghLQIAACPNQDPLQGTTGLI-- 176
Cdd:PLN02685 125 FFWESMKPGGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAYKANR--LDVGNAVNPCPSEEDKKLVvv 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30841303  177 --------------PLLGIDVWEHAYYLQYKNVRPDYLKA-IWNVINWENVT 213
Cdd:PLN02685 203 kspnavnplvwdysPLLTIDVWEHAYYLDFQNRRPDYISTfMEKLVSWEAVS 254
PLN02184 PLN02184
superoxide dismutase [Fe]
31-213 2.68e-42

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 141.81  E-value: 2.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303   31 PYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVT------EEKYQEALAKGDVTAQiALQPALKfNGGGHINHSIFWTNL 104
Cdd:PLN02184  17 PFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQvlgtelEGKPLEHIIHSTYNNG-DLLPAFN-NAAQAWNHEFFWESM 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303  105 SPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERghLQIAACPNQ-DPLqgTTGLIPLLGIDV 183
Cdd:PLN02184  95 KPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEK--LKVVKTPNAvNPL--VLGSFPLLTIDV 170
                        170       180       190
                 ....*....|....*....|....*....|.
gi 30841303  184 WEHAYYLQYKNVRPDYLKA-IWNVINWENVT 213
Cdd:PLN02184 171 WEHAYYLDFQNRRPDYIKTfMTNLVSWEAVS 201
PLN02622 PLN02622
iron superoxide dismutase
31-209 3.02e-42

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 143.23  E-value: 3.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303   31 PYDYGALEPHINAQIMQLHHSKHHAAYVNNLNvteekyqEALAKGDVTAQIALQ-----------PALKFNGGGHI-NHS 98
Cdd:PLN02622  54 PYPLDALEPYMSRRTLEVHWGEHHRGYVEGLN-------KQLAKDDILYGYTMDelvkvtynngnPLPEFNNAAQVwNHD 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303   99 IFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQ-DPLqgTTGLIP 177
Cdd:PLN02622 127 FFWESMQPGGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREERRLEVVKTSNAiNPL--VWDDIP 204
                        170       180       190
                 ....*....|....*....|....*....|...
gi 30841303  178 LLGIDVWEHAYYLQYKNVRPDYLKAIWN-VINW 209
Cdd:PLN02622 205 IICLDVWEHAYYLDYKNDRGKYVNAFMNhLVSW 237
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
24-105 1.85e-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: 135.51  E-value: 1.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30841303    24 KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTN 103
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIKALLGGLFNNGGGHWNHSLFWKN 80

                  ..
gi 30841303   104 LS 105
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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