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Conserved domains on  [gi|488289993|ref|WP_002361201|]
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MULTISPECIES: superoxide dismutase [Enterococcus]

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];
4-197 6.33e-133

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 370.61  E-value: 6.33e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993   4 TLPELPYAYDALEPYIDVETMHLHHDKHHNTYVTNLNAAIEKHPELGEKSVEDLISDmnaIPEDIRTAVRNNGGGHANHT 83
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEIIKK---LSEELKRALRNNAGGHWNHT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993  84 FFWEIMAPNAGGQPTGAIKEAIDETFGSFDEMKAAFKTAATGRFGSGWAWLVVN-NGKLEITSTPNQDSPLMDGQTPVLG 162
Cdd:COG0605   78 LFWENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDkDGKLEIVSTPNQDNPLMAGGTPLLG 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488289993 163 LDVWEHAYYLKYKNVRPDYIEAFWNVVNWDKVNEL 197
Cdd:COG0605  158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-197 6.33e-133

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 370.61  E-value: 6.33e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993   4 TLPELPYAYDALEPYIDVETMHLHHDKHHNTYVTNLNAAIEKHPELGEKSVEDLISDmnaIPEDIRTAVRNNGGGHANHT 83
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEIIKK---LSEELKRALRNNAGGHWNHT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993  84 FFWEIMAPNAGGQPTGAIKEAIDETFGSFDEMKAAFKTAATGRFGSGWAWLVVN-NGKLEITSTPNQDSPLMDGQTPVLG 162
Cdd:COG0605   78 LFWENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDkDGKLEIVSTPNQDNPLMAGGTPLLG 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488289993 163 LDVWEHAYYLKYKNVRPDYIEAFWNVVNWDKVNEL 197
Cdd:COG0605  158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PRK10925 PRK10925
superoxide dismutase [Mn];
1-202 1.97e-95

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 276.42  E-value: 1.97e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993   1 MTYTLPELPYAYDALEPYIDVETMHLHHDKHHNTYVTNLNAAIEKHPELGEKSVEDLISDMNAIPEDIRTAVRNNGGGHA 80
Cdd:PRK10925   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993  81 NHTFFWEIMapNAGGQPTGAIKEAIDETFGSFDEMKAAFKTAATGRFGSGWAWLVVNNGKLEITSTPNQDSPLMDGQT-- 158
Cdd:PRK10925  81 NHSLFWKGL--KKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDKLAVVSTANQDSPLMGEAIsg 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488289993 159 ----PVLGLDVWEHAYYLKYKNVRPDYIEAFWNVVNWDKVNELFAAAK 202
Cdd:PRK10925 159 asgfPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 97-196 3.33e-68

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: 203.43  E-value: 3.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993   97 PTGAIKEAIDETFGSFDEMKAAFKTAATGRFGSGWAWLVVN-NGKLEITSTPNQDSPLMDGQTPVLGLDVWEHAYYLKYK 175
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDpDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQ 80

                          90       100
                  ....*....|....*....|.
gi 488289993  176 NVRPDYIEAFWNVVNWDKVNE 196
Cdd:pfam02777  81 NRRADYVKAFWNVVNWDEVEK 101
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-197 6.33e-133

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 370.61  E-value: 6.33e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993   4 TLPELPYAYDALEPYIDVETMHLHHDKHHNTYVTNLNAAIEKHPELGEKSVEDLISDmnaIPEDIRTAVRNNGGGHANHT 83
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEIIKK---LSEELKRALRNNAGGHWNHT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993  84 FFWEIMAPNAGGQPTGAIKEAIDETFGSFDEMKAAFKTAATGRFGSGWAWLVVN-NGKLEITSTPNQDSPLMDGQTPVLG 162
Cdd:COG0605   78 LFWENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDkDGKLEIVSTPNQDNPLMAGGTPLLG 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488289993 163 LDVWEHAYYLKYKNVRPDYIEAFWNVVNWDKVNEL 197
Cdd:COG0605  158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PRK10925 PRK10925
superoxide dismutase [Mn];
1-202 1.97e-95

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 276.42  E-value: 1.97e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993   1 MTYTLPELPYAYDALEPYIDVETMHLHHDKHHNTYVTNLNAAIEKHPELGEKSVEDLISDMNAIPEDIRTAVRNNGGGHA 80
Cdd:PRK10925   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993  81 NHTFFWEIMapNAGGQPTGAIKEAIDETFGSFDEMKAAFKTAATGRFGSGWAWLVVNNGKLEITSTPNQDSPLMDGQT-- 158
Cdd:PRK10925  81 NHSLFWKGL--KKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDKLAVVSTANQDSPLMGEAIsg 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488289993 159 ----PVLGLDVWEHAYYLKYKNVRPDYIEAFWNVVNWDKVNELFAAAK 202
Cdd:PRK10925 159 asgfPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
PRK10543 PRK10543
superoxide dismutase [Fe];
1-200 5.80e-71

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 214.05  E-value: 5.80e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993   1 MTYTLPELPYAYDALEPYIDVETMHLHHDKHHNTYVTNLNAAIeKHPELGEKSVEDLISDMNAipedirtAVRNNGGGHA 80
Cdd:PRK10543   1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLI-KGTAFEGKSLEEIVRSSEG-------GVFNNAAQVW 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993  81 NHTFFWEIMAPNAGGQPTGAIKEAIDETFGSFDEMKAAFKTAATGRFGSGWAWLVVN-NGKLEITSTPNQDSPLMDGQTP 159
Cdd:PRK10543  73 NHTFYWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNaDGKLAIVSTSNAGTPLTTDATP 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 488289993 160 VLGLDVWEHAYYLKYKNVRPDYIEAFWNVVNWDKVNELFAA 200
Cdd:PRK10543 153 LLTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 97-196 3.33e-68

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: 203.43  E-value: 3.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993   97 PTGAIKEAIDETFGSFDEMKAAFKTAATGRFGSGWAWLVVN-NGKLEITSTPNQDSPLMDGQTPVLGLDVWEHAYYLKYK 175
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDpDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQ 80

                          90       100
                  ....*....|....*....|.
gi 488289993  176 NVRPDYIEAFWNVVNWDKVNE 196
Cdd:pfam02777  81 NRRADYVKAFWNVVNWDEVEK 101
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 6-196 2.83e-66

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 201.94  E-value: 2.83e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993   6 PELPYAYDALEPYIDVETMHLHHDKHHNTYVTNLNAAIEKHPeLGEKSVEDLISDMNAipedirtAVRNNGGGHANHTFF 85
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTP-LENKTLEELIKEYSG-------AVFNNAAQIWNHNFY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993  86 WEIMAPNAGGQPTGAIKEAIDETFGSFDEMKAAFKTAATGRFGSGWAWLVV-NNGKLEITSTPNQDSPLMDGQ-TPVLGL 163
Cdd:PTZ00078  73 WLSMGPNGGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLkNDGKLEIVQTHDAGNPIKDNTgKPLLTC 152

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488289993 164 DVWEHAYYLKYKNVRPDYIEAFWNVVNWDKVNE 196
Cdd:PTZ00078 153 DIWEHAYYIDYRNDRASYVNSWWNKVNWDFANK 185
PLN02471 PLN02471
superoxide dismutase [Mn]
 2-199 5.44e-61

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 189.73  E-value: 5.44e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993   2 TYTLPELPYAYDALEPYIDVETMHLHHDKHHNTYVTNLNAAIEKHPELGEKSvedlisDMNAIPEdIRTAVRNNGGGHAN 81
Cdd:PLN02471  30 TFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKG------DASAVVK-LQSAIKFNGGGHVN 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993  82 HTFFWEIMAP--NAGGQ-PTGAIKEAIDETFGSFDEMKAAFKTAATGRFGSGWAWLVVNNG--KLEITSTPNQDSPLMDG 156
Cdd:PLN02471 103 HSIFWKNLAPvsEGGGEpPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKElkKLVVETTANQDPLVTKG 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488289993 157 QT--PVLGLDVWEHAYYLKYKNVRPDYIEAFWNVVNWDKVNELFA 199
Cdd:PLN02471 183 PSlvPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYE 227
PLN02685 PLN02685
iron superoxide dismutase
 9-202 4.88e-53

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 171.72  E-value: 4.88e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993   9 PYAYDALEPYIDVETMHLHHDKHHNTYVTNLNAAIEKhPELGEKSVEDLI----SDMNAIPedirtaVRNNGGGHANHTF 84
Cdd:PLN02685  53 PYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQIVG-TELDGMSLEDVVlityNKGDMLP------AFNNAAQAWNHEF 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993  85 FWEIMAPNAGGQPTGAIKEAIDETFGSFDEMKAAFKTAATGRFGSGWAWLV-------VNNG----------KLEITSTP 147
Cdd:PLN02685 126 FWESMKPGGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAykanrldVGNAvnpcpseedkKLVVVKSP 205

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488289993 148 NQDSPLMDGQTPVLGLDVWEHAYYLKYKNVRPDYIEAFW-NVVNWDKVNELFAAAK 202
Cdd:PLN02685 206 NAVNPLVWDYSPLLTIDVWEHAYYLDFQNRRPDYISTFMeKLVSWEAVSARLESAK 261
PLN02622 PLN02622
iron superoxide dismutase
 3-202 4.19e-51

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 165.57  E-value: 4.19e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993   3 YTLPELPYAYDALEPYIDVETMHLHHDKHHNTYVTNLNAAIEKHPELGEKSVEDLI----SDMNAIPEdirtavRNNGGG 78
Cdd:PLN02622  48 YGLKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAKDDILYGYTMDELVkvtyNNGNPLPE------FNNAAQ 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993  79 HANHTFFWEIMAPNAGGQPTGAIKEAIDETFGSFDEMKAAFKTAATGRFGSGWAWLVV--NNGKLEITSTPNQDSPLMDG 156
Cdd:PLN02622 122 VWNHDFFWESMQPGGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLkrEERRLEVVKTSNAINPLVWD 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488289993 157 QTPVLGLDVWEHAYYLKYKNVRPDYIEAFWN-VVNWDKVNELFAAAK 202
Cdd:PLN02622 202 DIPIICLDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAMARMARAE 248
PLN02184 PLN02184
superoxide dismutase [Fe]
 3-202 1.25e-48

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 157.60  E-value: 1.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993   3 YTLPELPYAYDALEPYIDVETMHLHHDKHHNTYVTNLNAAIEKhPELGEKSVEDLISDMNAIPEDIrtAVRNNGGGHANH 82
Cdd:PLN02184  11 YVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLG-TELEGKPLEHIIHSTYNNGDLL--PAFNNAAQAWNH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993  83 TFFWEIMAPNAGGQPTGAIKEAIDETFGSFDEMKAAFKTAATGRFGSGWAWLVVNNGKLEITSTPNQDSPLMDGQTPVLG 162
Cdd:PLN02184  88 EFFWESMKPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEKLKVVKTPNAVNPLVLGSFPLLT 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 488289993 163 LDVWEHAYYLKYKNVRPDYIEAFW-NVVNWDKVNELFAAAK 202
Cdd:PLN02184 168 IDVWEHAYYLDFQNRRPDYIKTFMtNLVSWEAVSARLEAAK 208
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 2-90 5.61e-37

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: 123.57  E-value: 5.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289993    2 TYTLPELPYAYDALEPYIDVETMHLHHDKHHNTYVTNLNAAIEKHPELGEKsVEDLISdmnaipEDIRTAVRNNGGGHAN 81
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKP-LEELII------KALLGGLFNNGGGHWN 73


                  ....*....
gi 488289993   82 HTFFWEIMA 90
Cdd:pfam00081  74 HSLFWKNLS 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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