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Conserved domains on  [gi|8573766|emb|CAB94731|]
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manganese superoxide dismutase [Agaricus bisporus]

Protein Classification

superoxide dismutase( domain architecture ID 11427369)

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

EC:  1.15.1.1
Gene Ontology:  GO:0046872|GO:0004784

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];
5-190 5.43e-74

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 221.16  E-value: 5.43e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766    5 LPDLPYAYDALEPYISRQIMELHHKKtssdlcecaqHcrgclrHSTAVVG---------GF-DLSLFFILTTL------- 67
Cdd:COG0605   2 LPPLPYAYDALEPHISAETMELHHDK----------H------HQAYVNNlnaaleglaELeDKSLEEIIKKLseelkra 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766   68 ------GHINHSLFWQNLAPaaGAGGQLkPGPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWLGVNPsNKRLEISTT 141
Cdd:COG0605  66 lrnnagGHWNHTLFWENLSP--NGGGEP-TGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDK-DGKLEIVST 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 8573766  142 PNQD-PLL-NLVPIIGVDIWEHAFYLQYLNVKADYLNAIWSVINFDEAQRR 190
Cdd:COG0605 142 PNQDnPLMaGGTPLLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
5-190 5.43e-74

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 221.16  E-value: 5.43e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766    5 LPDLPYAYDALEPYISRQIMELHHKKtssdlcecaqHcrgclrHSTAVVG---------GF-DLSLFFILTTL------- 67
Cdd:COG0605   2 LPPLPYAYDALEPHISAETMELHHDK----------H------HQAYVNNlnaaleglaELeDKSLEEIIKKLseelkra 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766   68 ------GHINHSLFWQNLAPaaGAGGQLkPGPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWLGVNPsNKRLEISTT 141
Cdd:COG0605  66 lrnnagGHWNHTLFWENLSP--NGGGEP-TGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDK-DGKLEIVST 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 8573766  142 PNQD-PLL-NLVPIIGVDIWEHAFYLQYLNVKADYLNAIWSVINFDEAQRR 190
Cdd:COG0605 142 PNQDnPLMaGGTPLLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PLN02471 PLN02471
superoxide dismutase [Mn]
 5-191 4.29e-59

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 185.11  E-value: 4.29e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766     5 LPDLPYAYDALEPYISRQIMELHHKKTSSDLCECAQHCRGCLRH------STAVVggfDLSLFFILTTLGHINHSLFWQN 78
Cdd:PLN02471  33 LPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQavekgdASAVV---KLQSAIKFNGGGHVNHSIFWKN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766    79 LAPAAGAGGQLKPGPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWLGVNPSNKRLEISTTPNQDPLL----NLVPII 154
Cdd:PLN02471 110 LAPVSEGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVtkgpSLVPLL 189

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 8573766   155 GVDIWEHAFYLQYLNVKADYLNAIWSVINFDEAQRRY 191
Cdd:PLN02471 190 GIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVY 226
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 92-190 8.75e-53

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: 164.14  E-value: 8.75e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766     92 GPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWLGVNPsNKRLEISTTPNQDPLL--NLVPIIGVDIWEHAFYLQYLN 169
Cdd:pfam02777   3 GALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPLtdGLTPLLGLDVWEHAYYLDYQN 81

                          90       100
                  ....*....|....*....|.
gi 8573766    170 VKADYLNAIWSVINFDEAQRR 190
Cdd:pfam02777  82 RRADYVKAFWNVVNWDEVEKR 102
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
5-190 5.43e-74

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 221.16  E-value: 5.43e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766    5 LPDLPYAYDALEPYISRQIMELHHKKtssdlcecaqHcrgclrHSTAVVG---------GF-DLSLFFILTTL------- 67
Cdd:COG0605   2 LPPLPYAYDALEPHISAETMELHHDK----------H------HQAYVNNlnaaleglaELeDKSLEEIIKKLseelkra 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766   68 ------GHINHSLFWQNLAPaaGAGGQLkPGPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWLGVNPsNKRLEISTT 141
Cdd:COG0605  66 lrnnagGHWNHTLFWENLSP--NGGGEP-TGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDK-DGKLEIVST 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 8573766  142 PNQD-PLL-NLVPIIGVDIWEHAFYLQYLNVKADYLNAIWSVINFDEAQRR 190
Cdd:COG0605 142 PNQDnPLMaGGTPLLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PLN02471 PLN02471
superoxide dismutase [Mn]
 5-191 4.29e-59

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 185.11  E-value: 4.29e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766     5 LPDLPYAYDALEPYISRQIMELHHKKTSSDLCECAQHCRGCLRH------STAVVggfDLSLFFILTTLGHINHSLFWQN 78
Cdd:PLN02471  33 LPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQavekgdASAVV---KLQSAIKFNGGGHVNHSIFWKN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766    79 LAPAAGAGGQLKPGPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWLGVNPSNKRLEISTTPNQDPLL----NLVPII 154
Cdd:PLN02471 110 LAPVSEGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVtkgpSLVPLL 189

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 8573766   155 GVDIWEHAFYLQYLNVKADYLNAIWSVINFDEAQRRY 191
Cdd:PLN02471 190 GIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVY 226
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 92-190 8.75e-53

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: 164.14  E-value: 8.75e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766     92 GPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWLGVNPsNKRLEISTTPNQDPLL--NLVPIIGVDIWEHAFYLQYLN 169
Cdd:pfam02777   3 GALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPLtdGLTPLLGLDVWEHAYYLDYQN 81

                          90       100
                  ....*....|....*....|.
gi 8573766    170 VKADYLNAIWSVINFDEAQRR 190
Cdd:pfam02777  82 RRADYVKAFWNVVNWDEVEKR 102
PRK10925 PRK10925
superoxide dismutase [Mn];
1-194 3.64e-47

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 153.54  E-value: 3.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766     1 MAHVLPDLPYAYDALEPYISRQIMELHHKKtssdlcecaqHCRGCLRHSTAVVGGF----DLSLFFILTTL--------- 67
Cdd:PRK10925   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTK----------HHQTYVNNANAALESLpefaNLPVEELITKLdqlpadkkt 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766    68 -------GHINHSLFWQNLApaagAGGQLKpGPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWLGVNpsNKRLEIST 140
Cdd:PRK10925  71 vlrnnagGHANHSLFWKGLK----KGTTLQ-GDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLK--GDKLAVVS 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8573766   141 TPNQD-PLLNLV-------PIIGVDIWEHAFYLQYLNVKADYLNAIWSVINFDEAQRRYVEA 194
Cdd:PRK10925 144 TANQDsPLMGEAisgasgfPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAK 205
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 6-196 3.22e-31

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 112.19  E-value: 3.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766     6 PDLPYAYDALEPYISRQIMELHHKKtssdlcecaqHCRGCLRHSTAVVGG---FDLSLF-FILTTLGHI--------NHS 73
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSK----------HHAGYVNKLNGLIKGtplENKTLEeLIKEYSGAVfnnaaqiwNHN 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766    74 LFWQNLAPAAGAggqlKP-GPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWLGVNPSNKrLEISTTPNQD-PLL--N 149
Cdd:PTZ00078  71 FYWLSMGPNGGG----EPtGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGK-LEIVQTHDAGnPIKdnT 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 8573766   150 LVPIIGVDIWEHAFYLQYLNVKADYLNAIWSVINFDEAQRRYVEATQ 196
Cdd:PTZ00078 146 GKPLLTCDIWEHAYYIDYRNDRASYVNSWWNKVNWDFANKNLKKLMQ 192
PRK10543 PRK10543
superoxide dismutase [Fe];
1-185 3.17e-29

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 107.35  E-value: 3.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766     1 MAHVLPDLPYAYDALEPYISRQIMELHHKKtssdlcecaqhcrgclRHSTAVVGGFDL---------SLFFIL-TTLGHI 70
Cdd:PRK10543   1 MSFELPALPYAKDALAPHISAETLEYHYGK----------------HHQTYVTNLNNLikgtafegkSLEEIVrSSEGGV 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766    71 --------NHSLFWQNLAPAAGAggqlKP-GPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWLgVNPSNKRLEISTT 141
Cdd:PRK10543  65 fnnaaqvwNHTFYWNCLAPNAGG----EPtGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWL-VKNADGKLAIVST 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 8573766   142 PNQDPLL--NLVPIIGVDIWEHAFYLQYLNVKADYLNAIWSVINFD 185
Cdd:PRK10543 140 SNAGTPLttDATPLLTVDVWEHAYYIDYRNARPGYLEHFWALVNWE 185
PLN02622 PLN02622
iron superoxide dismutase
 9-194 9.87e-29

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 107.79  E-value: 9.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766     9 PYAYDALEPYISRQIMELHHKKtssdlcecaqHCRGCLRHSTAVVGGFDLSLFFILTTLGHI------------------ 70
Cdd:PLN02622  54 PYPLDALEPYMSRRTLEVHWGE----------HHRGYVEGLNKQLAKDDILYGYTMDELVKVtynngnplpefnnaaqvw 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766    71 NHSLFWQNLAPAagaGGQLKPGPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWLGVNPSNKRLEISTTPNQ-DPLL- 148
Cdd:PLN02622 124 NHDFFWESMQPG---GGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREERRLEVVKTSNAiNPLVw 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 8573766   149 NLVPIIGVDIWEHAFYLQYLNVKADYLNAIWS-VINFDEAQRRYVEA 194
Cdd:PLN02622 201 DDIPIICLDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAMARMARA 247
PLN02685 PLN02685
iron superoxide dismutase
 9-176 1.01e-24

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 98.15  E-value: 1.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766     9 PYAYDALEPYISRQIMELHHKKtssdlcecaqHCRGCLRHSTAVVGGFDL------SLFFILTTLGHI-----------N 71
Cdd:PLN02685  53 PYPLDALEPHMSRETLEYHWGK----------HHRAYVDNLNKQIVGTELdgmsleDVVLITYNKGDMlpafnnaaqawN 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766    72 HSLFWQNLAPaaGAGGqlKP-GPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWL-----------GVNP----SNKR 135
Cdd:PLN02685 123 HEFFWESMKP--GGGG--KPsGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLaykanrldvgnAVNPcpseEDKK 198

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 8573766   136 LEISTTPNQ-DPLL-NLVPIIGVDIWEHAFYLQYLNVKADYLN 176
Cdd:PLN02685 199 LVVVKSPNAvNPLVwDYSPLLTIDVWEHAYYLDFQNRRPDYIS 241
PLN02184 PLN02184
superoxide dismutase [Fe]
 3-198 3.50e-23

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 92.12  E-value: 3.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766     3 HVLPDLPYAYDALEPYISRQIMELHHKKtssdlcecaqHCRGCLRHSTAVVGGFDLSlffiLTTLGHI------------ 70
Cdd:PLN02184  11 YVLKPPPFALDALEPHMSKQTLEFHWGK----------HHRAYVDNLKKQVLGTELE----GKPLEHIihstynngdllp 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766    71 ---------NHSLFWQNLAPaaGAGGqlKP-GPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWLGVnpSNKRLEIST 140
Cdd:PLN02184  77 afnnaaqawNHEFFWESMKP--GGGG--KPsGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAY--SNEKLKVVK 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766   141 TPNQ-DPL-LNLVPIIGVDIWEHAFYLQYLNVKADYLNAIWSVINFDEAQRRYVEATQGS 198
Cdd:PLN02184 151 TPNAvNPLvLGSFPLLTIDVWEHAYYLDFQNRRPDYIKTFMTNLVSWEAVSARLEAAKAA 210
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 2-80 1.42e-15

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: 68.49  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8573766      2 AHVLPDLPYAYDALEPYISRQIMELHHKKtssdlcecaqHCRGCLRHSTAVVGGFD--------LSLFFILTTL-----G 68
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTK----------HHQTYVNNLNAALEGLEearkpleeLIIKALLGGLfnnggG 70

                          90
                  ....*....|..
gi 8573766     69 HINHSLFWQNLA 80
Cdd:pfam00081  71 HWNHSLFWKNLS 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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