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Conserved domains on  [gi|15241373|ref|NP_199923|]
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Fe superoxide dismutase 2 [Arabidopsis thaliana]

Protein Classification

PLN02685 family protein( domain architecture ID 11477059)

PLN02685 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02685 PLN02685
iron superoxide dismutase
 5-305 0e+00

iron superoxide dismutase


:

Pssm-ID: 215369  Cd Length: 299  Bit Score: 588.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373    5 AVTATPSSLLYSPLLLPSQGPNRRMQWKrnGKRRLGTKVAVSGVITAGFELKPPPYPLDALEPHMSRETLDYHWGKHHKT 84
Cdd:PLN02685   1 AVTATPASLSLSPALLPSQGPSRRMQWK--GKRRTCTRKAVSGVITAKFELKPPPYPLDALEPHMSRETLEYHWGKHHRA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373   85 YVENLNKQILGTDLDALSLEEVVLLSYNKGNMLPAFNNAAQAWNHEFFWESIQPGGGGKPTGELLRLIERDFGSFEEFLE 164
Cdd:PLN02685  79 YVDNLNKQIVGTELDGMSLEDVVLITYNKGDMLPAFNNAAQAWNHEFFWESMKPGGGGKPSGELLQLIERDFGSFERFVE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373  165 RFKSAAASNFGSGWTWLAYKANRLDVANAVNPLPKEEDKKLVIVKTPNAVNPLVWDYSPLLTIDTWEHAYYLDFENRRAE 244
Cdd:PLN02685 159 EFKSAAATQFGSGWAWLAYKANRLDVGNAVNPCPSEEDKKLVVVKSPNAVNPLVWDYSPLLTIDVWEHAYYLDFQNRRPD 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241373  245 YINTFMEKLVSWETVSTRLESAIARAVQREQEGTETEDEENPDDEVPEVYLDSDIDVSEVD 305
Cdd:PLN02685 239 YISTFMEKLVSWEAVSARLESAKARAAQREQEETRTEDEEEPDSEAVEMYLDSDIDVSEVD 299
 
Name Accession Description Interval E-value
PLN02685 PLN02685
iron superoxide dismutase
 5-305 0e+00

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 588.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373    5 AVTATPSSLLYSPLLLPSQGPNRRMQWKrnGKRRLGTKVAVSGVITAGFELKPPPYPLDALEPHMSRETLDYHWGKHHKT 84
Cdd:PLN02685   1 AVTATPASLSLSPALLPSQGPSRRMQWK--GKRRTCTRKAVSGVITAKFELKPPPYPLDALEPHMSRETLEYHWGKHHRA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373   85 YVENLNKQILGTDLDALSLEEVVLLSYNKGNMLPAFNNAAQAWNHEFFWESIQPGGGGKPTGELLRLIERDFGSFEEFLE 164
Cdd:PLN02685  79 YVDNLNKQIVGTELDGMSLEDVVLITYNKGDMLPAFNNAAQAWNHEFFWESMKPGGGGKPSGELLQLIERDFGSFERFVE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373  165 RFKSAAASNFGSGWTWLAYKANRLDVANAVNPLPKEEDKKLVIVKTPNAVNPLVWDYSPLLTIDTWEHAYYLDFENRRAE 244
Cdd:PLN02685 159 EFKSAAATQFGSGWAWLAYKANRLDVGNAVNPCPSEEDKKLVVVKSPNAVNPLVWDYSPLLTIDVWEHAYYLDFQNRRPD 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241373  245 YINTFMEKLVSWETVSTRLESAIARAVQREQEGTETEDEENPDDEVPEVYLDSDIDVSEVD 305
Cdd:PLN02685 239 YISTFMEKLVSWEAVSARLESAKARAAQREQEETRTEDEEEPDSEAVEMYLDSDIDVSEVD 299
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
54-262 5.71e-98

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 286.25  E-value: 5.71e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373  54 ELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGT-DLDALSLEEVVLLSYNKGNMlPAFNNAAQAWNHEFF 132
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLaELEDKSLEEIIKKLSEELKR-ALRNNAGGHWNHTLF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373 133 WESIQPGGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKAnrldvanavnplpkeeDKKLVIVKTPN 212
Cdd:COG0605  80 WENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDK----------------DGKLEIVSTPN 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15241373 213 AVNPLVWDYSPLLTIDTWEHAYYLDFENRRAEYINTFMeKLVSWETVSTR 262
Cdd:COG0605 144 QDNPLMAGGTPLLGLDVWEHAYYLDYQNRRPDYVDAFW-NVVNWDFVEKR 192
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 144-262 3.13e-49

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: 159.13  E-value: 3.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373   144 PTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKAnrldvanavnplpkeeDKKLVIVKTPNAVNPLVWDYSP 223
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP----------------DGKLEIVTTPNQDNPLTDGLTP 64

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 15241373   224 LLTIDTWEHAYYLDFENRRAEYINTFMeKLVSWETVSTR 262
Cdd:pfam02777  65 LLGLDVWEHAYYLDYQNRRADYVKAFW-NVVNWDEVEKR 102
 
Name Accession Description Interval E-value
PLN02685 PLN02685
iron superoxide dismutase
 5-305 0e+00

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 588.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373    5 AVTATPSSLLYSPLLLPSQGPNRRMQWKrnGKRRLGTKVAVSGVITAGFELKPPPYPLDALEPHMSRETLDYHWGKHHKT 84
Cdd:PLN02685   1 AVTATPASLSLSPALLPSQGPSRRMQWK--GKRRTCTRKAVSGVITAKFELKPPPYPLDALEPHMSRETLEYHWGKHHRA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373   85 YVENLNKQILGTDLDALSLEEVVLLSYNKGNMLPAFNNAAQAWNHEFFWESIQPGGGGKPTGELLRLIERDFGSFEEFLE 164
Cdd:PLN02685  79 YVDNLNKQIVGTELDGMSLEDVVLITYNKGDMLPAFNNAAQAWNHEFFWESMKPGGGGKPSGELLQLIERDFGSFERFVE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373  165 RFKSAAASNFGSGWTWLAYKANRLDVANAVNPLPKEEDKKLVIVKTPNAVNPLVWDYSPLLTIDTWEHAYYLDFENRRAE 244
Cdd:PLN02685 159 EFKSAAATQFGSGWAWLAYKANRLDVGNAVNPCPSEEDKKLVVVKSPNAVNPLVWDYSPLLTIDVWEHAYYLDFQNRRPD 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241373  245 YINTFMEKLVSWETVSTRLESAIARAVQREQEGTETEDEENPDDEVPEVYLDSDIDVSEVD 305
Cdd:PLN02685 239 YISTFMEKLVSWEAVSARLESAKARAAQREQEETRTEDEEEPDSEAVEMYLDSDIDVSEVD 299
PLN02184 PLN02184
superoxide dismutase [Fe]
 43-268 1.36e-103

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 301.67  E-value: 1.36e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373   43 VAVSGVITAGFELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGTDLDALSLEEVVLLSYNKGNMLPAFNN 122
Cdd:PLN02184   1 MAASSAVTANYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTELEGKPLEHIIHSTYNNGDLLPAFNN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373  123 AAQAWNHEFFWESIQPGGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKanrldvanavnplpkeeD 202
Cdd:PLN02184  81 AAQAWNHEFFWESMKPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYS-----------------N 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15241373  203 KKLVIVKTPNAVNPLVWDYSPLLTIDTWEHAYYLDFENRRAEYINTFMEKLVSWETVSTRLESAIA 268
Cdd:PLN02184 144 EKLKVVKTPNAVNPLVLGSFPLLTIDVWEHAYYLDFQNRRPDYIKTFMTNLVSWEAVSARLEAAKA 209
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
54-262 5.71e-98

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 286.25  E-value: 5.71e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373  54 ELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGT-DLDALSLEEVVLLSYNKGNMlPAFNNAAQAWNHEFF 132
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLaELEDKSLEEIIKKLSEELKR-ALRNNAGGHWNHTLF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373 133 WESIQPGGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKAnrldvanavnplpkeeDKKLVIVKTPN 212
Cdd:COG0605  80 WENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDK----------------DGKLEIVSTPN 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15241373 213 AVNPLVWDYSPLLTIDTWEHAYYLDFENRRAEYINTFMeKLVSWETVSTR 262
Cdd:COG0605 144 QDNPLMAGGTPLLGLDVWEHAYYLDYQNRRPDYVDAFW-NVVNWDFVEKR 192
PLN02622 PLN02622
iron superoxide dismutase
 26-268 1.59e-94

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 280.36  E-value: 1.59e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373   26 NRRMQWKRNGKRRLGTKVAVSGvitagfeLKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGTD-LDALSLE 104
Cdd:PLN02622  28 NLRNKQRRRSLQRASKVVAYYG-------LKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAKDDiLYGYTMD 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373  105 EVVLLSYNKGNMLPAFNNAAQAWNHEFFWESIQPGGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYk 184
Cdd:PLN02622 101 ELVKVTYNNGNPLPEFNNAAQVWNHDFFWESMQPGGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVL- 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373  185 anrldvanavnplpKEEDKKLVIVKTPNAVNPLVWDYSPLLTIDTWEHAYYLDFENRRAEYINTFMEKLVSWETVSTRLE 264
Cdd:PLN02622 180 --------------KREERRLEVVKTSNAINPLVWDDIPIICLDVWEHAYYLDYKNDRGKYVNAFMNHLVSWNAAMARMA 245


                 ....
gi 15241373  265 SAIA 268
Cdd:PLN02622 246 RAEA 249
PRK10543 PRK10543
superoxide dismutase [Fe];
53-265 4.36e-71

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 218.28  E-value: 4.36e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373   53 FELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGTDLDALSLEEVVLLSynKGNMlpaFNNAAQAWNHEFF 132
Cdd:PRK10543   3 FELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSS--EGGV---FNNAAQVWNHTFY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373  133 WESIQPGGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAykanrldvanavnplpKEEDKKLVIVKTPN 212
Cdd:PRK10543  78 WNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLV----------------KNADGKLAIVSTSN 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15241373  213 AVNPLVWDYSPLLTIDTWEHAYYLDFENRRAEYINTFMeKLVSWETVSTRLES 265
Cdd:PRK10543 142 AGTPLTTDATPLLTVDVWEHAYYIDYRNARPGYLEHFW-ALVNWEFVAKNLAA 193
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 59-266 1.42e-65

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 204.25  E-value: 1.42e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373   59 PYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGTDLDALSLEEVVllsynKGNMLPAFNNAAQAWNHEFFWESIQP 138
Cdd:PTZ00078   4 PYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLENKTLEELI-----KEYSGAVFNNAAQIWNHNFYWLSMGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373  139 GGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKanrldvanavnplpkeEDKKLVIVKTPNAVNPLV 218
Cdd:PTZ00078  79 NGGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLK----------------NDGKLEIVQTHDAGNPIK 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15241373  219 WDY-SPLLTIDTWEHAYYLDFENRRAEYINTFMEKlVSWETVSTRLESA 266
Cdd:PTZ00078 143 DNTgKPLLTCDIWEHAYYIDYRNDRASYVNSWWNK-VNWDFANKNLKKL 190
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 144-262 3.13e-49

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: 159.13  E-value: 3.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373   144 PTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKAnrldvanavnplpkeeDKKLVIVKTPNAVNPLVWDYSP 223
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP----------------DGKLEIVTTPNQDNPLTDGLTP 64

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 15241373   224 LLTIDTWEHAYYLDFENRRAEYINTFMeKLVSWETVSTR 262
Cdd:pfam02777  65 LLGLDVWEHAYYLDYQNRRADYVKAFW-NVVNWDEVEKR 102
PRK10925 PRK10925
superoxide dismutase [Mn];
53-267 3.83e-45

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 152.00  E-value: 3.83e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373   53 FELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILG-TDLDALSLEEVVllsyNKGNMLPA------FNNAAQ 125
Cdd:PRK10925   3 YTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESlPEFANLPVEELI----TKLDQLPAdkktvlRNNAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373  126 AWNHEFFWESIQPGGggKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKanrldvanavnplpkeeDKKL 205
Cdd:PRK10925  79 HANHSLFWKGLKKGT--TLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLK-----------------GDKL 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15241373  206 VIVKTPNAVNPLVWDY------SPLLTIDTWEHAYYLDFENRRAEYINTFMEkLVSWETVSTRLESAI 267
Cdd:PRK10925 140 AVVSTANQDSPLMGEAisgasgFPILGLDVWEHAYYLKFQNRRPDYIKEFWN-VVNWDEAAARFAAKK 206
PLN02471 PLN02471
superoxide dismutase [Mn]
 35-260 1.66e-32

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 120.01  E-value: 1.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373   35 GKRRLGTKVAVSGVITagFELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQIlgTDLDAlSLEEVVLLSYNKG 114
Cdd:PLN02471  15 LKETSSRLLSFRGLQT--FTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKAL--EQLDQ-AVEKGDASAVVKL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373  115 NMLPAFNNAAQAwNHEFFWESIQP---GGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAykanrLDva 191
Cdd:PLN02471  90 QSAIKFNGGGHV-NHSIFWKNLAPvseGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLG-----LD-- 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15241373  192 navnplpkEEDKKLVIVKTPNAvNPLVW---DYSPLLTIDTWEHAYYLDFENRRAEYINTFMeKLVSWETVS 260
Cdd:PLN02471 162 --------KELKKLVVETTANQ-DPLVTkgpSLVPLLGIDVWEHAYYLQYKNVRPDYLKNIW-KVMNWKYAS 223
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 53-136 3.77e-27

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: 101.23  E-value: 3.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241373    53 FELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGTDLDALSLEEVVLlsynKGNMLPAFNNAAQAWNHEFF 132
Cdd:pfam00081   2 YELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELII----KALLGGLFNNGGGHWNHSLF 77


                  ....
gi 15241373   133 WESI 136
Cdd:pfam00081  78 WKNL 81
 
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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