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Conserved domains on  [gi|493894435|ref|WP_006840378|]
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MULTISPECIES: superoxide dismutase [Corynebacterium]

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];
5-194 1.80e-97

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 280.86  E-value: 1.80e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   5 ELPDLPYAYDALEPHISAEIMELHHSKHHANYVKGANAALEALEAERGGEANP---DTLRALTKNLAFNLGGHTNHSIFW 81
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEiikKLSEELKRALRNNAGGHWNHTLFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435  82 KNMAPNAGGAPTGEVAEAINRDFGSFEKFQAHFEGIANGLQGSGWAVLGYDHiAGRLIIQQMTDQQGNISVDFTPLLMLD 161
Cdd:COG0605   81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDK-DGKLEIVSTPNQDNPLMAGGTPLLGLD 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 493894435 162 MWEHAFYLQYKNVKADYVKAFWNVVNWADVNER 194
Cdd:COG0605  160 VWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
5-194 1.80e-97

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 280.86  E-value: 1.80e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   5 ELPDLPYAYDALEPHISAEIMELHHSKHHANYVKGANAALEALEAERGGEANP---DTLRALTKNLAFNLGGHTNHSIFW 81
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEiikKLSEELKRALRNNAGGHWNHTLFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435  82 KNMAPNAGGAPTGEVAEAINRDFGSFEKFQAHFEGIANGLQGSGWAVLGYDHiAGRLIIQQMTDQQGNISVDFTPLLMLD 161
Cdd:COG0605   81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDK-DGKLEIVSTPNQDNPLMAGGTPLLGLD 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 493894435 162 MWEHAFYLQYKNVKADYVKAFWNVVNWADVNER 194
Cdd:COG0605  160 VWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 92-194 1.12e-54

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: 169.14  E-value: 1.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   92 PTGEVAEAINRDFGSFEKFQAHFEGIANGLQGSGWAVLGYDHiAGRLIIQQMTDQQGNISVDFTPLLMLDMWEHAFYLQY 171
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDY 79

                          90       100
                  ....*....|....*....|...
gi 493894435  172 KNVKADYVKAFWNVVNWADVNER 194
Cdd:pfam02777  80 QNRRADYVKAFWNVVNWDEVEKR 102
PLN02471 PLN02471
superoxide dismutase [Mn]
 4-196 6.35e-54

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 171.63  E-value: 6.35e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   4 YELPDLPYAYDALEPHISAEIMELHHSKHHANYVKGANAALEALEAERgGEANPDTLRALTKNLAFNLGGHTNHSIFWKN 83
Cdd:PLN02471  31 FTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAV-EKGDASAVVKLQSAIKFNGGGHVNHSIFWKN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435  84 MAP---NAGGAPTGEVAEAINRDFGSFEKFQAHFEGIANGLQGSGWAVLGYDHIAGRLIIQQMTDQQGNISVD--FTPLL 158
Cdd:PLN02471 110 LAPvseGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGpsLVPLL 189

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 493894435 159 MLDMWEHAFYLQYKNVKADYVKAFWNVVNWADVNERYA 196
Cdd:PLN02471 190 GIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYE 227
Superox_dis_Halo NF041312
superoxide dismutase;
5-195 2.54e-47

superoxide dismutase;


Pssm-ID: 469209  Cd Length: 196  Bit Score: 153.82  E-value: 2.54e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   5 ELPDLPYAYDALEPHISAEIMELHHSKHHANYVKGANAALEALEAERGGEANPDTLRALtKNLAFNLGGHTNHSIFWKNM 84
Cdd:NF041312   1 ELPPLPYDYDALEPHISEQVLTWHHDTHHQGYVNGLNSAEETLAENREAGDFSSTAGAM-RNVTHNGSGHYLHTLFWENM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435  85 APNAGGAPTGEVAEAINRDFGSFEKFQAHFEGIANGlqGSGWAVLGYDHIAGRLiiqqmtdqqGNISVD---------FT 155
Cdd:NF041312  80 SPNGGGEPEGDLADRIEEDFGSYEAWKGEFEAAAGA--AGGWALLVYDPVAKQL---------RNVAVDkhdqgalwgSH 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493894435 156 PLLMLDMWEHAFYLQYKNVKADYVKAFWNVVNWADVNERY 195
Cdd:NF041312 149 PILALDVWEHSYYYDYGPDRGSFVDAFFEVVDWDEVADEY 188
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
5-194 1.80e-97

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 280.86  E-value: 1.80e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   5 ELPDLPYAYDALEPHISAEIMELHHSKHHANYVKGANAALEALEAERGGEANP---DTLRALTKNLAFNLGGHTNHSIFW 81
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEiikKLSEELKRALRNNAGGHWNHTLFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435  82 KNMAPNAGGAPTGEVAEAINRDFGSFEKFQAHFEGIANGLQGSGWAVLGYDHiAGRLIIQQMTDQQGNISVDFTPLLMLD 161
Cdd:COG0605   81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDK-DGKLEIVSTPNQDNPLMAGGTPLLGLD 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 493894435 162 MWEHAFYLQYKNVKADYVKAFWNVVNWADVNER 194
Cdd:COG0605  160 VWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 92-194 1.12e-54

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: 169.14  E-value: 1.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   92 PTGEVAEAINRDFGSFEKFQAHFEGIANGLQGSGWAVLGYDHiAGRLIIQQMTDQQGNISVDFTPLLMLDMWEHAFYLQY 171
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDY 79

                          90       100
                  ....*....|....*....|...
gi 493894435  172 KNVKADYVKAFWNVVNWADVNER 194
Cdd:pfam02777  80 QNRRADYVKAFWNVVNWDEVEKR 102
PLN02471 PLN02471
superoxide dismutase [Mn]
 4-196 6.35e-54

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 171.63  E-value: 6.35e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   4 YELPDLPYAYDALEPHISAEIMELHHSKHHANYVKGANAALEALEAERgGEANPDTLRALTKNLAFNLGGHTNHSIFWKN 83
Cdd:PLN02471  31 FTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAV-EKGDASAVVKLQSAIKFNGGGHVNHSIFWKN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435  84 MAP---NAGGAPTGEVAEAINRDFGSFEKFQAHFEGIANGLQGSGWAVLGYDHIAGRLIIQQMTDQQGNISVD--FTPLL 158
Cdd:PLN02471 110 LAPvseGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGpsLVPLL 189

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 493894435 159 MLDMWEHAFYLQYKNVKADYVKAFWNVVNWADVNERYA 196
Cdd:PLN02471 190 GIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYE 227
PRK10925 PRK10925
superoxide dismutase [Mn];
4-198 1.01e-50

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 162.78  E-value: 1.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   4 YELPDLPYAYDALEPHISAEIMELHHSKHHANYVKGANAALEALEAERGGEAN---------PDTLRALTKNlafNLGGH 74
Cdd:PRK10925   3 YTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEelitkldqlPADKKTVLRN---NAGGH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435  75 TNHSIFWKNMapNAGGAPTGEVAEAINRDFGSFEKFQAHFEGIANGLQGSGWA--VLGYDHIAGRLIIQQMTDQQGN-IS 151
Cdd:PRK10925  80 ANHSLFWKGL--KKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAwlVLKGDKLAVVSTANQDSPLMGEaIS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 493894435 152 -VDFTPLLMLDMWEHAFYLQYKNVKADYVKAFWNVVNWADVNERYAAA 198
Cdd:PRK10925 158 gASGFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAK 205
Superox_dis_Halo NF041312
superoxide dismutase;
5-195 2.54e-47

superoxide dismutase;


Pssm-ID: 469209  Cd Length: 196  Bit Score: 153.82  E-value: 2.54e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   5 ELPDLPYAYDALEPHISAEIMELHHSKHHANYVKGANAALEALEAERGGEANPDTLRALtKNLAFNLGGHTNHSIFWKNM 84
Cdd:NF041312   1 ELPPLPYDYDALEPHISEQVLTWHHDTHHQGYVNGLNSAEETLAENREAGDFSSTAGAM-RNVTHNGSGHYLHTLFWENM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435  85 APNAGGAPTGEVAEAINRDFGSFEKFQAHFEGIANGlqGSGWAVLGYDHIAGRLiiqqmtdqqGNISVD---------FT 155
Cdd:NF041312  80 SPNGGGEPEGDLADRIEEDFGSYEAWKGEFEAAAGA--AGGWALLVYDPVAKQL---------RNVAVDkhdqgalwgSH 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493894435 156 PLLMLDMWEHAFYLQYKNVKADYVKAFWNVVNWADVNERY 195
Cdd:NF041312 149 PILALDVWEHSYYYDYGPDRGSFVDAFFEVVDWDEVADEY 188
PRK10543 PRK10543
superoxide dismutase [Fe];
4-197 8.93e-47

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 152.41  E-value: 8.93e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   4 YELPDLPYAYDALEPHISAEIMELHHSKHHANYVKGANAALEALEAErgGEANPDTLRALTKNLAFNLGGHTNHSIFWKN 83
Cdd:PRK10543   3 FELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFE--GKSLEEIVRSSEGGVFNNAAQVWNHTFYWNC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435  84 MAPNAGGAPTGEVAEAINRDFGSFEKFQAHFEGIANGLQGSGWAVLgYDHIAGRLIIQQMTDQQGNISVDFTPLLMLDMW 163
Cdd:PRK10543  81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWL-VKNADGKLAIVSTSNAGTPLTTDATPLLTVDVW 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 493894435 164 EHAFYLQYKNVKADYVKAFWNVVNWADVNERYAA 197
Cdd:PRK10543 160 EHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 7-200 6.60e-42

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 139.92  E-value: 6.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   7 PDLPYAYDALEPHISAEIMELHHSKHHANYVKGANAALEALEAERggEANPDTLRALTKNLAFNLGGHTNHSIFWKNMAP 86
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLEN--KTLEELIKEYSGAVFNNAAQIWNHNFYWLSMGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435  87 NAGGAPTGEVAEAINRDFGSFEKFQAHFEGIANGLQGSGWA--VLGYDhiaGRLIIQQMTDQQGNISVDF-TPLLMLDMW 163
Cdd:PTZ00078  79 NGGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGwlVLKND---GKLEIVQTHDAGNPIKDNTgKPLLTCDIW 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 493894435 164 EHAFYLQYKNVKADYVKAFWNVVNWADVNERYAAAAK 200
Cdd:PTZ00078 156 EHAYYIDYRNDRASYVNSWWNKVNWDFANKNLKKLMQ 192
PLN02685 PLN02685
iron superoxide dismutase
 2-198 3.43e-41

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 141.29  E-value: 3.43e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   2 AVYELPDLPYAYDALEPHISAEIMELHHSKHHANYVKGANAALEaleaerGGEANPDTLR---ALTKNL-----AFNLGG 73
Cdd:PLN02685  45 AKFELKPPPYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQIV------GTELDGMSLEdvvLITYNKgdmlpAFNNAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435  74 HT-NHSIFWKNMAPNAGGAPTGEVAEAINRDFGSFEKFQAHFEGIANGLQGSGWAVLGYDhiAGR--------------- 137
Cdd:PLN02685 119 QAwNHEFFWESMKPGGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAYK--ANRldvgnavnpcpseed 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493894435 138 --LIIQQMTDQQGNISVDFTPLLMLDMWEHAFYLQYKNVKADYVKAFW-NVVNWADVNERYAAA 198
Cdd:PLN02685 197 kkLVVVKSPNAVNPLVWDYSPLLTIDVWEHAYYLDFQNRRPDYISTFMeKLVSWEAVSARLESA 260
PLN02622 PLN02622
iron superoxide dismutase
 1-198 1.22e-36

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 128.21  E-value: 1.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   1 MAVYELPDLPYAYDALEPHISAEIMELHHSKHHANYVKGANAALEALEAERGgeANPDTLRALTKNLA-----FNLGGHT 75
Cdd:PLN02622  45 VAYYGLKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAKDDILYG--YTMDELVKVTYNNGnplpeFNNAAQV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435  76 -NHSIFWKNMAPNAGGAPTGEVAEAINRDFGSFEKFQAHFEGIANGLQGSGWAVLGYDHIAGRLIIQQMTDQQGNISVDF 154
Cdd:PLN02622 123 wNHDFFWESMQPGGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREERRLEVVKTSNAINPLVWDD 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 493894435 155 TPLLMLDMWEHAFYLQYKNVKADYVKAFWN-VVNWADVNERYAAA 198
Cdd:PLN02622 203 IPIICLDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAMARMARA 247
PLN02184 PLN02184
superoxide dismutase [Fe]
 2-198 3.14e-34

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 120.62  E-value: 3.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435   2 AVYELPDLPYAYDALEPHISAEIMELHHSKHHANYVK------------GANAALEALEAERGGEANPdtlraltknlAF 69
Cdd:PLN02184   9 ANYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDnlkkqvlgteleGKPLEHIIHSTYNNGDLLP----------AF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435  70 NLGGHT-NHSIFWKNMAPNAGGAPTGEVAEAINRDFGSFEKFQAHFEGIANGLQGSGWAVLGYDHiaGRLIIQQMTDQQG 148
Cdd:PLN02184  79 NNAAQAwNHEFFWESMKPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSN--EKLKVVKTPNAVN 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 493894435 149 NISVDFTPLLMLDMWEHAFYLQYKNVKADYVKAFW-NVVNWADVNERYAAA 198
Cdd:PLN02184 157 PLVLGSFPLLTIDVWEHAYYLDFQNRRPDYIKTFMtNLVSWEAVSARLEAA 207
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 4-85 5.15e-28

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: 100.46  E-value: 5.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493894435    4 YELPDLPYAYDALEPHISAEIMELHHSKHHANYVKGANAALEALEAERgGEANPDTLRALTKNLAFNLGGHTNHSIFWKN 83
Cdd:pfam00081   2 YELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEAR-KPLEELIIKALLGGLFNNGGGHWNHSLFWKN 80


                  ..
gi 493894435   84 MA 85
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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