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Conserved domains on  [gi|15228896|ref|NP_191194|]
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Iron/manganese superoxide dismutase family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02471 super family cl29655
superoxide dismutase [Mn]
 33-235 8.13e-132

superoxide dismutase [Mn]


The actual alignment was detected with superfamily member PLN02471:

Pssm-ID: 215262  Cd Length: 231  Bit Score: 371.16  E-value: 8.13e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896   33 MKTASLPDLPYAYDALEPAISEEIMRLHHQKHHQTYVTQYNKALNSLRSAMADGDHSSVVKLQSLIKFNGGGHVNHAIFW 112
Cdd:PLN02471  28 LQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFW 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896  113 KNLAPVHEGGGKPPHDPLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFGLDRELKRLVVETTANQDPLVTKGSHLVP 192
Cdd:PLN02471 108 KNLAPVSEGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGPSLVP 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15228896  193 LIGIDVWEHAYYPQYKNARAEYLKNIWTVINWKYAADVFEKHT 235
Cdd:PLN02471 188 LLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYEKEC 230
 
Name Accession Description Interval E-value
PLN02471 PLN02471
superoxide dismutase [Mn]
 33-235 8.13e-132

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 371.16  E-value: 8.13e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896   33 MKTASLPDLPYAYDALEPAISEEIMRLHHQKHHQTYVTQYNKALNSLRSAMADGDHSSVVKLQSLIKFNGGGHVNHAIFW 112
Cdd:PLN02471  28 LQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFW 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896  113 KNLAPVHEGGGKPPHDPLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFGLDRELKRLVVETTANQDPLVTKGSHLVP 192
Cdd:PLN02471 108 KNLAPVSEGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGPSLVP 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15228896  193 LIGIDVWEHAYYPQYKNARAEYLKNIWTVINWKYAADVFEKHT 235
Cdd:PLN02471 188 LLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYEKEC 230
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
37-229 3.09e-84

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 248.89  E-value: 3.09e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896  37 SLPDLPYAYDALEPAISEEIMRLHHQKHHQTYVTQYNKALNSLrSAMADGDHSSVVK-----LQSLIKFNGGGHVNHAIF 111
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGL-AELEDKSLEEIIKklseeLKRALRNNAGGHWNHTLF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896 112 WKNLAPvheGGGKPPHDPLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFGLDRElKRLVVETTANQDPLVTKGshLV 191
Cdd:COG0605  80 WENLSP---NGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDNPLMAG--GT 153

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15228896 192 PLIGIDVWEHAYYPQYKNARAEYLKNIWTVINWKYAAD 229
Cdd:COG0605 154 PLLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEK 191
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 126-228 9.26e-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: 155.66  E-value: 9.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896   126 PHDPLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFGLDRElKRLVVETTANQDPLVTKGshLVPLIGIDVWEHAYYP 205
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPD-GKLEIVTTPNQDNPLTDG--LTPLLGLDVWEHAYYL 77

                          90       100
                  ....*....|....*....|...
gi 15228896   206 QYKNARAEYLKNIWTVINWKYAA 228
Cdd:pfam02777  78 DYQNRRADYVKAFWNVVNWDEVE 100
 
Name Accession Description Interval E-value
PLN02471 PLN02471
superoxide dismutase [Mn]
 33-235 8.13e-132

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 371.16  E-value: 8.13e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896   33 MKTASLPDLPYAYDALEPAISEEIMRLHHQKHHQTYVTQYNKALNSLRSAMADGDHSSVVKLQSLIKFNGGGHVNHAIFW 112
Cdd:PLN02471  28 LQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFW 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896  113 KNLAPVHEGGGKPPHDPLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFGLDRELKRLVVETTANQDPLVTKGSHLVP 192
Cdd:PLN02471 108 KNLAPVSEGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGPSLVP 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15228896  193 LIGIDVWEHAYYPQYKNARAEYLKNIWTVINWKYAADVFEKHT 235
Cdd:PLN02471 188 LLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYEKEC 230
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
37-229 3.09e-84

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 248.89  E-value: 3.09e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896  37 SLPDLPYAYDALEPAISEEIMRLHHQKHHQTYVTQYNKALNSLrSAMADGDHSSVVK-----LQSLIKFNGGGHVNHAIF 111
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGL-AELEDKSLEEIIKklseeLKRALRNNAGGHWNHTLF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896 112 WKNLAPvheGGGKPPHDPLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFGLDRElKRLVVETTANQDPLVTKGshLV 191
Cdd:COG0605  80 WENLSP---NGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDNPLMAG--GT 153

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15228896 192 PLIGIDVWEHAYYPQYKNARAEYLKNIWTVINWKYAAD 229
Cdd:COG0605 154 PLLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEK 191
PRK10925 PRK10925
superoxide dismutase [Mn];
37-232 8.58e-52

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 167.02  E-value: 8.58e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896   37 SLPDLPYAYDALEPAISEEIMRLHHQKHHQTYVTQYNKALNSLRSAMADGDHSSVVKL-------QSLIKFNGGGHVNHA 109
Cdd:PRK10925   4 TLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLdqlpadkKTVLRNNAGGHANHS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896  110 IFWKNLAPVHEGGGkpphdPLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFGLDRElkRLVVETTANQD-PLVTK-- 186
Cdd:PRK10925  84 LFWKGLKKGTTLQG-----DLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGD--KLAVVSTANQDsPLMGEai 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15228896  187 -GSHLVPLIGIDVWEHAYYPQYKNARAEYLKNIWTVINWKYAADVFE 232
Cdd:PRK10925 157 sGASGFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFA 203
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 126-228 9.26e-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: 155.66  E-value: 9.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896   126 PHDPLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFGLDRElKRLVVETTANQDPLVTKGshLVPLIGIDVWEHAYYP 205
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPD-GKLEIVTTPNQDNPLTDG--LTPLLGLDVWEHAYYL 77

                          90       100
                  ....*....|....*....|...
gi 15228896   206 QYKNARAEYLKNIWTVINWKYAA 228
Cdd:pfam02777  78 DYQNRRADYVKAFWNVVNWDEVE 100
PRK10543 PRK10543
superoxide dismutase [Fe];
38-231 4.27e-42

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 141.63  E-value: 4.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896   38 LPDLPYAYDALEPAISEEIMRLHHQKHHQTYVTQYNKALNSlrSAMADGDHSSVVKLQSLIKFNGGGHV-NHAIFWKNLA 116
Cdd:PRK10543   5 LPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKG--TAFEGKSLEEIVRSSEGGVFNNAAQVwNHTFYWNCLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896  117 PvhEGGGKPPHDpLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFGLDRELKRLVVETTANQDPLVTKGShlvPLIGI 196
Cdd:PRK10543  83 P--NAGGEPTGK-VAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDAT---PLLTV 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 15228896  197 DVWEHAYYPQYKNARAEYLKNIWTVINWKYAADVF 231
Cdd:PRK10543 157 DVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNL 191
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 39-227 1.79e-38

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 132.60  E-value: 1.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896   39 PDLPYAYDALEPAISEEIMRLHHQKHHQTYVTQYNKALNslRSAMADGDHSSVVKLQSLIKFNGGGHV-NHAIFWKNLAP 117
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIK--GTPLENKTLEELIKEYSGAVFNNAAQIwNHNFYWLSMGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896  118 vhEGGGKPpHDPLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFGLDRELKRLVVETTANQDPLvtKGSHLVPLIGID 197
Cdd:PTZ00078  79 --NGGGEP-TGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPI--KDNTGKPLLTCD 153

                        170       180       190
                 ....*....|....*....|....*....|
gi 15228896  198 VWEHAYYPQYKNARAEYLKNIWTVINWKYA 227
Cdd:PTZ00078 154 IWEHAYYIDYRNDRASYVNSWWNKVNWDFA 183
PLN02622 PLN02622
iron superoxide dismutase
 42-228 2.37e-34

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 123.97  E-value: 2.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896   42 PYAYDALEPAISEEIMRLHHQKHHQTYVTQYNKALnslrsamADGDHSSVVKLQSLIK-----------FNGGGHV-NHA 109
Cdd:PLN02622  54 PYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQL-------AKDDILYGYTMDELVKvtynngnplpeFNNAAQVwNHD 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896  110 IFWKNLAPvheGGGKPPHDPLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFGLDRELKRLVVETTANQ-DPLVTKGs 188
Cdd:PLN02622 127 FFWESMQP---GGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREERRLEVVKTSNAiNPLVWDD- 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15228896  189 hlVPLIGIDVWEHAYYPQYKNARAEYLKNIWT-VINWKYAA 228
Cdd:PLN02622 203 --IPIICLDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAM 241
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 37-116 5.08e-32

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: 112.01  E-value: 5.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896    37 SLPDLPYAYDALEPAISEEIMRLHHQKHHQTYVTQYNKALNSLRSAMADGDHSSVVKLQSLIKFNGGGHVNHAIFWKNLA 116
Cdd:pfam00081   3 ELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIKALLGGLFNNGGGHWNHSLFWKNLS 82
PLN02685 PLN02685
iron superoxide dismutase
 42-225 8.48e-31

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 115.48  E-value: 8.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896   42 PYAYDALEPAISEEIMRLHHQKHHQTYVTQYNKALnsLRSAMADGDHSSVV-----KLQSLIKFNGGGHV-NHAIFWKNL 115
Cdd:PLN02685  53 PYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQI--VGTELDGMSLEDVVlitynKGDMLPAFNNAAQAwNHEFFWESM 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896  116 APvheGGGKPPHDPLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFG-----LD----------RELKRLVVETTANQ 180
Cdd:PLN02685 131 KP---GGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAykanrLDvgnavnpcpsEEDKKLVVVKSPNA 207

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15228896  181 -DPLVTKGShlvPLIGIDVWEHAYYPQYKNARAEYLKN-IWTVINWK 225
Cdd:PLN02685 208 vNPLVWDYS---PLLTIDVWEHAYYLDFQNRRPDYISTfMEKLVSWE 251
PLN02184 PLN02184
superoxide dismutase [Fe]
 42-232 1.86e-27

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 104.44  E-value: 1.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896   42 PYAYDALEPAISEEIMRLHHQKHHQTYVTQYNKALNSLR---SAMADGDHSSVVKLQSLIKFNGGGHV-NHAIFWKNLAP 117
Cdd:PLN02184  17 PFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTElegKPLEHIIHSTYNNGDLLPAFNNAAQAwNHEFFWESMKP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228896  118 vheGGGKPPHDPLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFGLDRElKRLVVETTANQDPLVTkGShlVPLIGID 197
Cdd:PLN02184  97 ---GGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNE-KLKVVKTPNAVNPLVL-GS--FPLLTID 169

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15228896  198 VWEHAYYPQYKNARAEYLKNIWT-VINWKYAADVFE 232
Cdd:PLN02184 170 VWEHAYYLDFQNRRPDYIKTFMTnLVSWEAVSARLE 205
 
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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