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Conserved domains on  [gi|15599664|ref|NP_253158|]
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superoxide dismutase [Pseudomonas aeruginosa PAO1]

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];
5-197 6.03e-122

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 342.88  E-value: 6.03e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664   5 LPPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALEGTP-YAEQPVESLLRQLAglpEKLRTPVVNNGGGHANHSL 83
Cdd:COG0605   2 LPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAeLEDKSLEEIIKKLS---EELKRALRNNAGGHWNHTL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664  84 FWTVMSPQGGGRPDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLSVTPQGSLLVESSGNQDSPLMNGNTPILGL 163
Cdd:COG0605  79 FWENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLGL 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 15599664 164 DVWEHAYYLKYQNRRPEYIGAFYNVIDWREVARR 197
Cdd:COG0605 159 DVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
5-197 6.03e-122

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 342.88  E-value: 6.03e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664   5 LPPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALEGTP-YAEQPVESLLRQLAglpEKLRTPVVNNGGGHANHSL 83
Cdd:COG0605   2 LPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAeLEDKSLEEIIKKLS---EELKRALRNNAGGHWNHTL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664  84 FWTVMSPQGGGRPDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLSVTPQGSLLVESSGNQDSPLMNGNTPILGL 163
Cdd:COG0605  79 FWENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLGL 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 15599664 164 DVWEHAYYLKYQNRRPEYIGAFYNVIDWREVARR 197
Cdd:COG0605 159 DVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PRK10925 PRK10925
superoxide dismutase [Mn];
1-201 8.30e-91

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 264.86  E-value: 8.30e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664    1 MPHALPPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALEGTP-YAEQPVESLLRQLAGLPEKLRTPVVNNGGGHA 79
Cdd:PRK10925   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPeFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664   80 NHSLFWTVMspQGGGRPDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLsVTPQGSLLVESSGNQDSPLMN---- 155
Cdd:PRK10925  81 NHSLFWKGL--KKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWL-VLKGDKLAVVSTANQDSPLMGeais 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15599664  156 --GNTPILGLDVWEHAYYLKYQNRRPEYIGAFYNVIDWREVARRYAQA 201
Cdd:PRK10925 158 gaSGFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAK 205
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
96-197 1.59e-61

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: 186.48  E-value: 1.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664    96 PDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLSVTPQGSLLVESSGNQDSPLMNGNTPILGLDVWEHAYYLKYQ 175
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQ 80
                          90       100
                  ....*....|....*....|..
gi 15599664   176 NRRPEYIGAFYNVIDWREVARR 197
Cdd:pfam02777  81 NRRADYVKAFWNVVNWDEVEKR 102
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
5-197 6.03e-122

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 342.88  E-value: 6.03e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664   5 LPPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALEGTP-YAEQPVESLLRQLAglpEKLRTPVVNNGGGHANHSL 83
Cdd:COG0605   2 LPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAeLEDKSLEEIIKKLS---EELKRALRNNAGGHWNHTL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664  84 FWTVMSPQGGGRPDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLSVTPQGSLLVESSGNQDSPLMNGNTPILGL 163
Cdd:COG0605  79 FWENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLGL 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 15599664 164 DVWEHAYYLKYQNRRPEYIGAFYNVIDWREVARR 197
Cdd:COG0605 159 DVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PRK10925 PRK10925
superoxide dismutase [Mn];
1-201 8.30e-91

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 264.86  E-value: 8.30e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664    1 MPHALPPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALEGTP-YAEQPVESLLRQLAGLPEKLRTPVVNNGGGHA 79
Cdd:PRK10925   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPeFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664   80 NHSLFWTVMspQGGGRPDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLsVTPQGSLLVESSGNQDSPLMN---- 155
Cdd:PRK10925  81 NHSLFWKGL--KKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWL-VLKGDKLAVVSTANQDSPLMGeais 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15599664  156 --GNTPILGLDVWEHAYYLKYQNRRPEYIGAFYNVIDWREVARRYAQA 201
Cdd:PRK10925 158 gaSGFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAK 205
PRK10543 PRK10543
superoxide dismutase [Fe];
1-199 6.35e-65

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 198.64  E-value: 6.35e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664    1 MPHALPPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALEGTPYAEQPVESLLRQLAGlpeklrtPVVNNGGGHAN 80
Cdd:PRK10543   1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSSEG-------GVFNNAAQVWN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664   81 HSLFWTVMSPQGGGRPDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLSVTPQGSLLVESSGNQDSPLMNGNTPI 160
Cdd:PRK10543  74 HTFYWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDATPL 153
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15599664  161 LGLDVWEHAYYLKYQNRRPEYIGAFYNVIDWREVARRYA 199
Cdd:PRK10543 154 LTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLA 192
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
96-197 1.59e-61

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: 186.48  E-value: 1.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664    96 PDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLSVTPQGSLLVESSGNQDSPLMNGNTPILGLDVWEHAYYLKYQ 175
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQ 80
                          90       100
                  ....*....|....*....|..
gi 15599664   176 NRRPEYIGAFYNVIDWREVARR 197
Cdd:pfam02777  81 NRRADYVKAFWNVVNWDEVEKR 102
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
6-191 5.80e-59

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 183.45  E-value: 5.80e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664    6 PPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALEGTPYAEQPVESLLRQLAGlpeklrtPVVNNGGGHANHSLFW 85
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLENKTLEELIKEYSG-------AVFNNAAQIWNHNFYW 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664   86 TVMSPQGGGRPDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLSVTPQGSLLVESSGNQDSPLMNGN-TPILGLD 164
Cdd:PTZ00078  74 LSMGPNGGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPIKDNTgKPLLTCD 153
                        170       180
                 ....*....|....*....|....*..
gi 15599664  165 VWEHAYYLKYQNRRPEYIGAFYNVIDW 191
Cdd:PTZ00078 154 IWEHAYYIDYRNDRASYVNSWWNKVNW 180
PLN02685 PLN02685
iron superoxide dismutase
5-203 8.79e-56

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 178.66  E-value: 8.79e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664    5 LPPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALEGTPYAEQPVESLLrqLAGLPEKLRTPVVNNGGGHANHSLF 84
Cdd:PLN02685  49 LKPPPYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQIVGTELDGMSLEDVV--LITYNKGDMLPAFNNAAQAWNHEFF 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664   85 WTVMSPQGGGRPDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWL-----------SVTPQGS-----LLVESSGN 148
Cdd:PLN02685 127 WESMKPGGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLaykanrldvgnAVNPCPSeedkkLVVVKSPN 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15599664  149 QDSPLMNGNTPILGLDVWEHAYYLKYQNRRPEYIGAFYN-VIDWREVARRYAQALA 203
Cdd:PLN02685 207 AVNPLVWDYSPLLTIDVWEHAYYLDFQNRRPDYISTFMEkLVSWEAVSARLESAKA 262
PLN02471 PLN02471
superoxide dismutase [Mn]
4-203 8.49e-55

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 173.94  E-value: 8.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664    4 ALPPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALegtpyaEQPVESLLRQLAGLPEKLRTPVVNNGGGHANHSL 83
Cdd:PLN02471  32 TLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKAL------EQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSI 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664   84 FWTVMSP--QGGGR-PDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLSVTPQG-SLLVESSGNQDSPLMNGNT- 158
Cdd:PLN02471 106 FWKNLAPvsEGGGEpPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELkKLVVETTANQDPLVTKGPSl 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 15599664  159 -PILGLDVWEHAYYLKYQNRRPEYIGAFYNVIDWREVARRYAQALA 203
Cdd:PLN02471 186 vPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYEKECN 231
PLN02184 PLN02184
superoxide dismutase [Fe]
3-203 6.25e-51

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 163.76  E-value: 6.25e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664    3 HALPPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALEGTPYAEQPVESLLRQLAGLPEKLrtPVVNNGGGHANHS 82
Cdd:PLN02184  11 YVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTELEGKPLEHIIHSTYNNGDLL--PAFNNAAQAWNHE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664   83 LFWTVMSPQGGGRPDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLSVTpQGSLLVESSGNQDSPLMNGNTPILG 162
Cdd:PLN02184  89 FFWESMKPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYS-NEKLKVVKTPNAVNPLVLGSFPLLT 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15599664  163 LDVWEHAYYLKYQNRRPEYIGAFY-NVIDWREVARRYAQALA 203
Cdd:PLN02184 168 IDVWEHAYYLDFQNRRPDYIKTFMtNLVSWEAVSARLEAAKA 209
PLN02622 PLN02622
iron superoxide dismutase
3-203 7.31e-48

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 157.48  E-value: 7.31e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664    3 HALPPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALEGTP--YA---EQPVESLLRQLAGLPEklrtpvVNNGGG 77
Cdd:PLN02622  48 YGLKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAKDDilYGytmDELVKVTYNNGNPLPE------FNNAAQ 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664   78 HANHSLFWTVMSPQGGGRPDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLSVT-PQGSLLVESSGNQDSPLMNG 156
Cdd:PLN02622 122 VWNHDFFWESMQPGGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKrEERRLEVVKTSNAINPLVWD 201
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15599664  157 NTPILGLDVWEHAYYLKYQNRRPEYIGAFYN-VIDWREVARRYAQALA 203
Cdd:PLN02622 202 DIPIICLDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAMARMARAEA 249
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
2-89 2.09e-39

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: 129.73  E-value: 2.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599664     2 PHALPPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALEGTPYAEQPVESLLRQlaglpeKLRTPVVNNGGGHANH 81
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIK------ALLGGLFNNGGGHWNH 74

                  ....*...
gi 15599664    82 SLFWTVMS 89
Cdd:pfam00081  75 SLFWKNLS 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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