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Conserved domains on  [gi|487749226|ref|WP_001831217|]
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MULTISPECIES: superoxide dismutase [Staphylococcus]

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];
4-194 1.87e-119

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 336.33  E-value: 1.87e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226   4 ELPNLPYAYDALEPHIDKQTMEIHHDKHHNTYVTKLNSAVEGT-DLEAKSIEEIVANLDSvpsNIQTAVRNNGGGHLNHS 82
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLaELEDKSLEEIIKKLSE---ELKRALRNNAGGHWNHT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226  83 LFWELLSPN--SEEKGEVVDKIKEQWGSLDEFKKEFADKAAARFGSGWAWLVVN-NGQLEIVTTPNQDNPITEGKTPILG 159
Cdd:COG0605   78 LFWENLSPNggGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDkDGKLEIVSTPNQDNPLMAGGTPLLG 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 487749226 160 LDVWEHAYYLKYQNKRPDYINAFWNVVNWEKVNEL 194
Cdd:COG0605  158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-194 1.87e-119

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 336.33  E-value: 1.87e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226   4 ELPNLPYAYDALEPHIDKQTMEIHHDKHHNTYVTKLNSAVEGT-DLEAKSIEEIVANLDSvpsNIQTAVRNNGGGHLNHS 82
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLaELEDKSLEEIIKKLSE---ELKRALRNNAGGHWNHT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226  83 LFWELLSPN--SEEKGEVVDKIKEQWGSLDEFKKEFADKAAARFGSGWAWLVVN-NGQLEIVTTPNQDNPITEGKTPILG 159
Cdd:COG0605   78 LFWENLSPNggGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDkDGKLEIVSTPNQDNPLMAGGTPLLG 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 487749226 160 LDVWEHAYYLKYQNKRPDYINAFWNVVNWEKVNEL 194
Cdd:COG0605  158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PRK10925 PRK10925
superoxide dismutase [Mn];
1-199 1.57e-89

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 261.39  E-value: 1.57e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226   1 MAFELPNLPYAYDALEPHIDKQTMEIHHDKHHNTYVTKLNSAVEG-TDLEAKSIEEIVANLDSVPSNIQTAVRNNGGGHL 79
Cdd:PRK10925   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESlPEFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226  80 NHSLFWELLSPNSEEKGEVVDKIKEQWGSLDEFKKEFADKAAARFGSGWAWLVVNNGQLEIVTTPNQDNPI----TEGKT 155
Cdd:PRK10925  81 NHSLFWKGLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDKLAVVSTANQDSPLmgeaISGAS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 487749226 156 --PILGLDVWEHAYYLKYQNKRPDYINAFWNVVNWEKVNELYNATK 199
Cdd:PRK10925 161 gfPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 95-193 2.68e-63

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: 191.10  E-value: 2.68e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226   95 KGEVVDKIKEQWGSLDEFKKEFADKAAARFGSGWAWLVVN-NGQLEIVTTPNQDNPITEGKTPILGLDVWEHAYYLKYQN 173
Cdd:pfam02777   2 TGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDpDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQN 81

                          90       100
                  ....*....|....*....|
gi 487749226  174 KRPDYINAFWNVVNWEKVNE 193
Cdd:pfam02777  82 RRADYVKAFWNVVNWDEVEK 101
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-194 1.87e-119

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 336.33  E-value: 1.87e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226   4 ELPNLPYAYDALEPHIDKQTMEIHHDKHHNTYVTKLNSAVEGT-DLEAKSIEEIVANLDSvpsNIQTAVRNNGGGHLNHS 82
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLaELEDKSLEEIIKKLSE---ELKRALRNNAGGHWNHT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226  83 LFWELLSPN--SEEKGEVVDKIKEQWGSLDEFKKEFADKAAARFGSGWAWLVVN-NGQLEIVTTPNQDNPITEGKTPILG 159
Cdd:COG0605   78 LFWENLSPNggGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDkDGKLEIVSTPNQDNPLMAGGTPLLG 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 487749226 160 LDVWEHAYYLKYQNKRPDYINAFWNVVNWEKVNEL 194
Cdd:COG0605  158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PRK10925 PRK10925
superoxide dismutase [Mn];
1-199 1.57e-89

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 261.39  E-value: 1.57e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226   1 MAFELPNLPYAYDALEPHIDKQTMEIHHDKHHNTYVTKLNSAVEG-TDLEAKSIEEIVANLDSVPSNIQTAVRNNGGGHL 79
Cdd:PRK10925   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESlPEFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226  80 NHSLFWELLSPNSEEKGEVVDKIKEQWGSLDEFKKEFADKAAARFGSGWAWLVVNNGQLEIVTTPNQDNPI----TEGKT 155
Cdd:PRK10925  81 NHSLFWKGLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDKLAVVSTANQDSPLmgeaISGAS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 487749226 156 --PILGLDVWEHAYYLKYQNKRPDYINAFWNVVNWEKVNELYNATK 199
Cdd:PRK10925 161 gfPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
PRK10543 PRK10543
superoxide dismutase [Fe];
1-193 2.72e-67

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 204.42  E-value: 2.72e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226   1 MAFELPNLPYAYDALEPHIDKQTMEIHHDKHHNTYVTKLNSAVEGTDLEAKSIEEIVANLDSvpsniqtAVRNNGGGHLN 80
Cdd:PRK10543   1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSSEG-------GVFNNAAQVWN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226  81 HSLFWELLSPN--SEEKGEVVDKIKEQWGSLDEFKKEFADKAAARFGSGWAWLVVN-NGQLEIVTTPNQDNPITEGKTPI 157
Cdd:PRK10543  74 HTFYWNCLAPNagGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNaDGKLAIVSTSNAGTPLTTDATPL 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 487749226 158 LGLDVWEHAYYLKYQNKRPDYINAFWNVVNWEKVNE 193
Cdd:PRK10543 154 LTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAK 189
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 95-193 2.68e-63

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: 191.10  E-value: 2.68e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226   95 KGEVVDKIKEQWGSLDEFKKEFADKAAARFGSGWAWLVVN-NGQLEIVTTPNQDNPITEGKTPILGLDVWEHAYYLKYQN 173
Cdd:pfam02777   2 TGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDpDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQN 81

                          90       100
                  ....*....|....*....|
gi 487749226  174 KRPDYINAFWNVVNWEKVNE 193
Cdd:pfam02777  82 RRADYVKAFWNVVNWDEVEK 101
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 6-193 6.31e-59

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 183.07  E-value: 6.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226   6 PNLPYAYDALEPHIDKQTMEIHHDKHHNTYVTKLNSAVEGTDLEAKSIEEIVANLDSvpsniqtAVRNNGGGHLNHSLFW 85
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLENKTLEELIKEYSG-------AVFNNAAQIWNHNFYW 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226  86 ELLSPNS--EEKGEVVDKIKEQWGSLDEFKKEFADKAAARFGSGWAWLVV-NNGQLEIVTTPNQDNPITEGK-TPILGLD 161
Cdd:PTZ00078  74 LSMGPNGggEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLkNDGKLEIVQTHDAGNPIKDNTgKPLLTCD 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 487749226 162 VWEHAYYLKYQNKRPDYINAFWNVVNWEKVNE 193
Cdd:PTZ00078 154 IWEHAYYIDYRNDRASYVNSWWNKVNWDFANK 185
PLN02471 PLN02471
superoxide dismutase [Mn]
 3-195 1.22e-57

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 181.26  E-value: 1.22e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226   3 FELPNLPYAYDALEPHIDKQTMEIHHDKHHNTYVTKLNSAVEgtdleakSIEEIVANLD-SVPSNIQTAVRNNGGGHLNH 81
Cdd:PLN02471  31 FTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALE-------QLDQAVEKGDaSAVVKLQSAIKFNGGGHVNH 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226  82 SLFWELLSPNSEEKGE-----VVDKIKEQWGSLDEFKKEFADKAAARFGSGWAWLVVNNG--QLEIVTTPNQDNPITEGK 154
Cdd:PLN02471 104 SIFWKNLAPVSEGGGEpphgsLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKElkKLVVETTANQDPLVTKGP 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 487749226 155 T--PILGLDVWEHAYYLKYQNKRPDYINAFWNVVNWEKVNELY 195
Cdd:PLN02471 184 SlvPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVY 226
PLN02685 PLN02685
iron superoxide dismutase
 3-192 1.91e-54

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 175.19  E-value: 1.91e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226   3 FELPNLPYAYDALEPHIDKQTMEIHHDKHHNTYVTKLNSAVEGTDLEAKSIEEIVanLDSVPSNIQTAVRNNGGGHLNHS 82
Cdd:PLN02685  47 FELKPPPYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQIVGTELDGMSLEDVV--LITYNKGDMLPAFNNAAQAWNHE 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226  83 LFWELLSP--NSEEKGEVVDKIKEQWGSLDEFKKEFADKAAARFGSGWAWLV-------VNNG----------QLEIVTT 143
Cdd:PLN02685 125 FFWESMKPggGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAykanrldVGNAvnpcpseedkKLVVVKS 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 487749226 144 PNQDNPITEGKTPILGLDVWEHAYYLKYQNKRPDYINAFW-NVVNWEKVN 192
Cdd:PLN02685 205 PNAVNPLVWDYSPLLTIDVWEHAYYLDFQNRRPDYISTFMeKLVSWEAVS 254
PLN02184 PLN02184
superoxide dismutase [Fe]
 9-199 1.75e-51

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 164.92  E-value: 1.75e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226   9 PYAYDALEPHIDKQTMEIHHDKHHNTYVTKLNSAVEGTDLEAKSIEEIV----ANLDSVPSniqtavRNNGGGHLNHSLF 84
Cdd:PLN02184  17 PFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTELEGKPLEHIIhstyNNGDLLPA------FNNAAQAWNHEFF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226  85 WELLSPNSEEK--GEVVDKIKEQWGSLDEFKKEFADKAAARFGSGWAWLVVNNGQLEIVTTPNQDNPITEGKTPILGLDV 162
Cdd:PLN02184  91 WESMKPGGGGKpsGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEKLKVVKTPNAVNPLVLGSFPLLTIDV 170

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 487749226 163 WEHAYYLKYQNKRPDYINAFW-NVVNWEKVNELYNATK 199
Cdd:PLN02184 171 WEHAYYLDFQNRRPDYIKTFMtNLVSWEAVSARLEAAK 208
PLN02622 PLN02622
iron superoxide dismutase
 9-191 7.89e-47

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 154.40  E-value: 7.89e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226   9 PYAYDALEPHIDKQTMEIHHDKHHNTYVTKLNSAVEGTD-LEAKSIEEIVA----NLDSVPSniqtavRNNGGGHLNHSL 83
Cdd:PLN02622  54 PYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAKDDiLYGYTMDELVKvtynNGNPLPE------FNNAAQVWNHDF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226  84 FWELLSPNSEEKGE--VVDKIKEQWGSLDEFKKEFADKAAARFGSGWAWLVV--NNGQLEIVTTPNQDNPITEGKTPILG 159
Cdd:PLN02622 128 FWESMQPGGGDMPElgVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLkrEERRLEVVKTSNAINPLVWDDIPIIC 207

                        170       180       190
                 ....*....|....*....|....*....|...
gi 487749226 160 LDVWEHAYYLKYQNKRPDYINAFWN-VVNWEKV 191
Cdd:PLN02622 208 LDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAA 240
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 2-89 1.90e-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: 1.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749226    2 AFELPNLPYAYDALEPHIDKQTMEIHHDKHHNTYVTKLNSAVEGTDLEAKSIEEIVANldsvpsNIQTAVRNNGGGHLNH 81
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIK------ALLGGLFNNGGGHWNH 74


                  ....*...
gi 487749226   82 SLFWELLS 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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