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Conserved domains on  [gi|18401659|ref|NP_565666|]
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copper/zinc superoxide dismutase 2 [Arabidopsis thaliana]

Protein Classification

superoxide dismutase family protein( domain architecture ID 840)

superoxide dismutase family protein may catalyze the conversion of superoxide radicals to molecular oxygen

CATH:  2.60.40.200
Gene Ontology:  GO:0006801|GO:0046872
PubMed:  8176730
SCOP:  4007548

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cu-Zn_Superoxide_Dismutase super family cl00891
Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of ...
66-213 2.71e-68

Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene causes familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Cytoplasmic and periplasmic SODs exist as dimers, whereas chloroplastic and extracellular enzymes exist as tetramers. Structure supports independent functional evolution in prokaryotes (P-class) and eukaryotes (E-class) [PMID:.8176730].


The actual alignment was detected with superfamily member PLN02386:

Pssm-ID: 469976 [Multi-domain]  Cd Length: 152  Bit Score: 206.30  E-value: 2.71e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401659   66 KAVAVLKGTSDVEGVVTLTQDDSGPTTVNVRITGLTPGPHGFHLHEFGDTTNGCISTGPHFNPNNMTHGAPEDECRHAGD 145
Cdd:PLN02386   3 KAVAVLNSSEGVKGTIFFTQEGDGPTTVTGSLSGLKPGLHGFHVHALGDTTNGCMSTGPHFNPAGKEHGAPEDENRHAGD 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18401659  146 LGNINANADGVAETTIVDNQIPLTGPNSVVGRAFVVHELKDDLGKGGHELSLTTGNAGGRLACGVIGL 213
Cdd:PLN02386  83 LGNVTVGDDGTATFTIVDKQIPLTGPNSIVGRAVVVHADPDDLGKGGHELSKSTGNAGGRVACGIIGL 150
 
Name Accession Description Interval E-value
PLN02386 PLN02386
superoxide dismutase [Cu-Zn]
66-213 2.71e-68

superoxide dismutase [Cu-Zn]


Pssm-ID: 166027 [Multi-domain]  Cd Length: 152  Bit Score: 206.30  E-value: 2.71e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401659   66 KAVAVLKGTSDVEGVVTLTQDDSGPTTVNVRITGLTPGPHGFHLHEFGDTTNGCISTGPHFNPNNMTHGAPEDECRHAGD 145
Cdd:PLN02386   3 KAVAVLNSSEGVKGTIFFTQEGDGPTTVTGSLSGLKPGLHGFHVHALGDTTNGCMSTGPHFNPAGKEHGAPEDENRHAGD 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18401659  146 LGNINANADGVAETTIVDNQIPLTGPNSVVGRAFVVHELKDDLGKGGHELSLTTGNAGGRLACGVIGL 213
Cdd:PLN02386  83 LGNVTVGDDGTATFTIVDKQIPLTGPNSIVGRAVVVHADPDDLGKGGHELSKSTGNAGGRVACGIIGL 150
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
77-211 1.03e-66

Copper/zinc superoxide dismutase (SODC); 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 copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.


Pssm-ID: 459663  Cd Length: 129  Bit Score: 201.25  E-value: 1.03e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401659    77 VEGVVTLTQDDSGPTTVNVRITGLTPGPHGFHLHEFGDTTNGCISTGPHFNPNNMTHGAPEDECRHAGDLGNINANADGV 156
Cdd:pfam00080   1 VSGTVTFTQAGGGPVRVTGNLTGLTPGKHGFHIHEFGDCTNGCTSAGGHFNPTGKQHGGPNDDGRHVGDLGNITADADGV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18401659   157 AETTIVDNQIPLTGPNSVVGRAFVVHELKDDLGKgghelsLTTGNAGGRLACGVI 211
Cdd:pfam00080  81 ATVEFTDSLISLSGGNSIIGRALVVHAGPDDLGT------QPTGNAGARIACGVI 129
Cu-Zn_Superoxide_Dismutase cd00305
Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of ...
65-208 6.91e-64

Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene causes familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Cytoplasmic and periplasmic SODs exist as dimers, whereas chloroplastic and extracellular enzymes exist as tetramers. Structure supports independent functional evolution in prokaryotes (P-class) and eukaryotes (E-class) [PMID:.8176730].


Pssm-ID: 238186  Cd Length: 144  Bit Score: 194.79  E-value: 6.91e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401659  65 KKAVAVLKG-TSDVEGVVTLTQDDSGpTTVNVRITGLTPGPHGFHLHEFGDTTNGCISTGPHFNPNNMTHGAPEDECRHA 143
Cdd:cd00305   1 VSAVAVLKGpDGKVVGTVTFTQQSGG-VTITGELSGLTPGLHGFHIHEFGDCTNGCTSAGGHFNPFGKKHGGPNDEGRHA 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18401659 144 GDLGNINANADGVAETTIVDNQIPLTGPNSVVGRAFVVHELKDDLGKGGHELSLTTGNAGGRLAC 208
Cdd:cd00305  80 GDLGNIVADKDGVATVSVLDPLISLKGGNSIIGRSLVVHAGQDDLGKGPDELSGGTGNAGVRVAC 144
SodC COG2032
Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];
62-212 7.50e-49

Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 441635  Cd Length: 171  Bit Score: 157.34  E-value: 7.50e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401659  62 SAAKKAVAVLKGTSD--VEGVVTLTQDDSGpTTVNVRITGLTPGPHGFHLHEFGD-TTNGCISTGPHFNPNNMTHGAPED 138
Cdd:COG2032  23 AAAKTATATLVDTGDgkVVGTVTFTETPGG-VLVTVELSGLPPGEHGFHIHEKGDcSAPDFKSAGGHFNPTGTKHGGPNP 101
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18401659 139 ECRHAGDLGNINANADGVAETTIVDNQIPLTGPNSVVGRAFVVHELKDDLGkgghelSLTTGNAGGRLACGVIG 212
Cdd:COG2032 102 DGPHAGDLPNLYVDADGTATLEVLAPRLTLGGLNDLDGRALIIHAGPDDYS------TQPSGNAGARIACGVIK 169
 
Name Accession Description Interval E-value
PLN02386 PLN02386
superoxide dismutase [Cu-Zn]
66-213 2.71e-68

superoxide dismutase [Cu-Zn]


Pssm-ID: 166027 [Multi-domain]  Cd Length: 152  Bit Score: 206.30  E-value: 2.71e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401659   66 KAVAVLKGTSDVEGVVTLTQDDSGPTTVNVRITGLTPGPHGFHLHEFGDTTNGCISTGPHFNPNNMTHGAPEDECRHAGD 145
Cdd:PLN02386   3 KAVAVLNSSEGVKGTIFFTQEGDGPTTVTGSLSGLKPGLHGFHVHALGDTTNGCMSTGPHFNPAGKEHGAPEDENRHAGD 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18401659  146 LGNINANADGVAETTIVDNQIPLTGPNSVVGRAFVVHELKDDLGKGGHELSLTTGNAGGRLACGVIGL 213
Cdd:PLN02386  83 LGNVTVGDDGTATFTIVDKQIPLTGPNSIVGRAVVVHADPDDLGKGGHELSKSTGNAGGRVACGIIGL 150
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
77-211 1.03e-66

Copper/zinc superoxide dismutase (SODC); 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 copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.


Pssm-ID: 459663  Cd Length: 129  Bit Score: 201.25  E-value: 1.03e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401659    77 VEGVVTLTQDDSGPTTVNVRITGLTPGPHGFHLHEFGDTTNGCISTGPHFNPNNMTHGAPEDECRHAGDLGNINANADGV 156
Cdd:pfam00080   1 VSGTVTFTQAGGGPVRVTGNLTGLTPGKHGFHIHEFGDCTNGCTSAGGHFNPTGKQHGGPNDDGRHVGDLGNITADADGV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18401659   157 AETTIVDNQIPLTGPNSVVGRAFVVHELKDDLGKgghelsLTTGNAGGRLACGVI 211
Cdd:pfam00080  81 ATVEFTDSLISLSGGNSIIGRALVVHAGPDDLGT------QPTGNAGARIACGVI 129
Cu-Zn_Superoxide_Dismutase cd00305
Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of ...
65-208 6.91e-64

Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene causes familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Cytoplasmic and periplasmic SODs exist as dimers, whereas chloroplastic and extracellular enzymes exist as tetramers. Structure supports independent functional evolution in prokaryotes (P-class) and eukaryotes (E-class) [PMID:.8176730].


Pssm-ID: 238186  Cd Length: 144  Bit Score: 194.79  E-value: 6.91e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401659  65 KKAVAVLKG-TSDVEGVVTLTQDDSGpTTVNVRITGLTPGPHGFHLHEFGDTTNGCISTGPHFNPNNMTHGAPEDECRHA 143
Cdd:cd00305   1 VSAVAVLKGpDGKVVGTVTFTQQSGG-VTITGELSGLTPGLHGFHIHEFGDCTNGCTSAGGHFNPFGKKHGGPNDEGRHA 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18401659 144 GDLGNINANADGVAETTIVDNQIPLTGPNSVVGRAFVVHELKDDLGKGGHELSLTTGNAGGRLAC 208
Cdd:cd00305  80 GDLGNIVADKDGVATVSVLDPLISLKGGNSIIGRSLVVHAGQDDLGKGPDELSGGTGNAGVRVAC 144
PLN02642 PLN02642
copper, zinc superoxide dismutase
66-213 9.13e-58

copper, zinc superoxide dismutase


Pssm-ID: 178248  Cd Length: 164  Bit Score: 179.89  E-value: 9.13e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401659   66 KAVAVLKGTSDVEGVVTLTQDDSGPTTVNVRITGLTPGPHGFHLHEFGDTTNGCISTGPHFNPNNMTHGAPEDECRHAGD 145
Cdd:PLN02642   9 RAVALIAGDNNVRGCLQFVQDIFGTTHVTGKISGLSPGFHGFHIHSFGDTTNGCISTGPHFNPLNRVHGPPNEEERHAGD 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18401659  146 LGNINANADGVAETTIVDNQIPLTGPNSVVGRAFVVHELKDDLGKGGHELSLTTGNAGGRLACGVIGL 213
Cdd:PLN02642  89 LGNILAGSDGVAEILIKDKHIPLSGQYSILGRAVVVHADPDDLGKGGHKLSKSTGNAGSRVGCGIIGL 156
SodC COG2032
Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];
62-212 7.50e-49

Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 441635  Cd Length: 171  Bit Score: 157.34  E-value: 7.50e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401659  62 SAAKKAVAVLKGTSD--VEGVVTLTQDDSGpTTVNVRITGLTPGPHGFHLHEFGD-TTNGCISTGPHFNPNNMTHGAPED 138
Cdd:COG2032  23 AAAKTATATLVDTGDgkVVGTVTFTETPGG-VLVTVELSGLPPGEHGFHIHEKGDcSAPDFKSAGGHFNPTGTKHGGPNP 101
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18401659 139 ECRHAGDLGNINANADGVAETTIVDNQIPLTGPNSVVGRAFVVHELKDDLGkgghelSLTTGNAGGRLACGVIG 212
Cdd:COG2032 102 DGPHAGDLPNLYVDADGTATLEVLAPRLTLGGLNDLDGRALIIHAGPDDYS------TQPSGNAGARIACGVIK 169
PLN02957 PLN02957
copper, zinc superoxide dismutase
61-192 3.00e-17

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 77.10  E-value: 3.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401659   61 VSAAkkaVAVLKGTsDVEGVVTLTQDDSGPTTVNVRITGLTPGPHGFHLHEFGDTTNGCISTGPHFNPNNMTHGApedec 140
Cdd:PLN02957  80 VSAA---VAEFKGP-DIFGVVRFAQVSMELARIEAAFSGLSPGTHGWSINEYGDLTRGAASTGKVYNPSDDDTDE----- 150
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18401659  141 RHAGDLGNINANADGVAETTIVDNQIPLTgpnSVVGRAFVVHELKDDLGKGG 192
Cdd:PLN02957 151 EPLGDLGTLEADENGEATFSGTKEKLKVW---DLIGRSLAVYATADKSGPGI 199
PRK10290 PRK10290
superoxide dismutase [Cu-Zn] SodC2;
72-211 7.55e-09

superoxide dismutase [Cu-Zn] SodC2;


Pssm-ID: 182357 [Multi-domain]  Cd Length: 173  Bit Score: 53.31  E-value: 7.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401659   72 KGTSDVEGVVTLTQDDSGpTTVNVRITGLTPGPHGFHLHEFGD--------TTNGCISTGPHFNPNNM-THGAPEDEcRH 142
Cdd:PRK10290  32 QGVGQSIGSVTITETDKG-LEFSPDLKALPPGEHGFHIHAKGScqpatkdgKASAAEAAGGHLDPQNTgKHEGPEGA-GH 109
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18401659  143 AGDLGNINANADGVAETTIVDNQipLTGPNSVVGRAFVVHELKDDLGKGGHELslttGNAGGRLACGVI 211
Cdd:PRK10290 110 LGDLPALVVNNDGKATDPVIAPR--LKSLDEVKDKALMVHVGGDNMSDQPKPL----GGGGERYACGVI 172
PRK15388 PRK15388
superoxide dismutase [Cu-Zn];
73-211 9.71e-08

superoxide dismutase [Cu-Zn];


Pssm-ID: 185286  Cd Length: 177  Bit Score: 50.08  E-value: 9.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401659   73 GTSDVEGVVTLTQDDSGpTTVNVRITGLTPGPHGFHLHE----FGDTTNG----CISTGPHFNPNNM-THGAPEDECRHA 143
Cdd:PRK15388  35 GTGENIGEITVSETPYG-LLFTPHLNGLTPGIHGFHVHTnpscMPGMKDGkevpALMAGGHLDPEKTgKHLGPYNDKGHL 113
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18401659  144 GDLGNINANADGVAETTIVDNQipLTGPNSVVGRAFVVHELKDDLGKGGHELslttGNAGGRLACGVI 211
Cdd:PRK15388 114 GDLPGLVVNADGTATYPLLAPR--LKSLSELKGHSLMIHKGGDNYSDKPAPL----GGGGARFACGVI 175
 
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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