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Conserved domains on  [gi|930576750|gb|ALF94651|]
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superoxide dismutase, partial [Streptococcus anginosus subsp. anginosus]

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];
1-126 1.37e-60

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 184.18  E-value: 1.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930576750   1 NTYVNNVNAALAKHPEI-GEDLEQLLSDvetIPADIRQAVINNGGGHLNHALFWELMTPE-KTEPSAALAADLEATFGSF 78
Cdd:COG0605   30 QAYVNNLNAALEGLAELeDKSLEEIIKK---LSEELKRALRNNAGGHWNHTLFWENLSPNgGGEPTGELAAAIEADFGSF 106
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 930576750  79 EDFKASFTTAATSRFGSGWAWLVVNPDGKLEVMSTANQDTPISEGKTP 126
Cdd:COG0605  107 DAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTP 154
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
1-126 1.37e-60

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 184.18  E-value: 1.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930576750   1 NTYVNNVNAALAKHPEI-GEDLEQLLSDvetIPADIRQAVINNGGGHLNHALFWELMTPE-KTEPSAALAADLEATFGSF 78
Cdd:COG0605   30 QAYVNNLNAALEGLAELeDKSLEEIIKK---LSEELKRALRNNAGGHWNHTLFWENLSPNgGGEPTGELAAAIEADFGSF 106
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 930576750  79 EDFKASFTTAATSRFGSGWAWLVVNPDGKLEVMSTANQDTPISEGKTP 126
Cdd:COG0605  107 DAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTP 154
PRK10925 PRK10925
superoxide dismutase [Mn];
2-120 3.48e-38

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 127.73  E-value: 3.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930576750   2 TYVNNVNAALAKHPEIGE-DLEQLLSDVETIPADIRQAVINNGGGHLNHALFWELMTpEKTEPSAALAADLEATFGSFED 80
Cdd:PRK10925  34 TYVNNANAALESLPEFANlPVEELITKLDQLPADKKTVLRNNAGGHANHSLFWKGLK-KGTTLQGDLKAAIERDFGSVDN 112
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 930576750  81 FKASFTTAATSRFGSGWAWLVVNpDGKLEVMSTANQDTPI 120
Cdd:PRK10925 113 FKAEFEKAAATRFGSGWAWLVLK-GDKLAVVSTANQDSPL 151
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
63-126 3.21e-33

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: 111.75  E-value: 3.21e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930576750   63 PSAALAADLEATFGSFEDFKASFTTAATSRFGSGWAWLVVNPDGKLEVMSTANQDTPISEGKTP 126
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTP 64
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
1-126 1.37e-60

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 184.18  E-value: 1.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930576750   1 NTYVNNVNAALAKHPEI-GEDLEQLLSDvetIPADIRQAVINNGGGHLNHALFWELMTPE-KTEPSAALAADLEATFGSF 78
Cdd:COG0605   30 QAYVNNLNAALEGLAELeDKSLEEIIKK---LSEELKRALRNNAGGHWNHTLFWENLSPNgGGEPTGELAAAIEADFGSF 106
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 930576750  79 EDFKASFTTAATSRFGSGWAWLVVNPDGKLEVMSTANQDTPISEGKTP 126
Cdd:COG0605  107 DAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTP 154
PRK10925 PRK10925
superoxide dismutase [Mn];
2-120 3.48e-38

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 127.73  E-value: 3.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930576750   2 TYVNNVNAALAKHPEIGE-DLEQLLSDVETIPADIRQAVINNGGGHLNHALFWELMTpEKTEPSAALAADLEATFGSFED 80
Cdd:PRK10925  34 TYVNNANAALESLPEFANlPVEELITKLDQLPADKKTVLRNNAGGHANHSLFWKGLK-KGTTLQGDLKAAIERDFGSVDN 112
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 930576750  81 FKASFTTAATSRFGSGWAWLVVNpDGKLEVMSTANQDTPI 120
Cdd:PRK10925 113 FKAEFEKAAATRFGSGWAWLVLK-GDKLAVVSTANQDSPL 151
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
63-126 3.21e-33

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: 111.75  E-value: 3.21e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930576750   63 PSAALAADLEATFGSFEDFKASFTTAATSRFGSGWAWLVVNPDGKLEVMSTANQDTPISEGKTP 126
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTP 64
PRK10543 PRK10543
superoxide dismutase [Fe];
1-126 2.28e-26

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 97.33  E-value: 2.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930576750   1 NTYVNNVNAALAKHPEIGEDLEQLLSDVETipadirqAVINNGGGHLNHALFWELMTPEK-TEPSAALAADLEATFGSFE 79
Cdd:PRK10543  33 QTYVTNLNNLIKGTAFEGKSLEEIVRSSEG-------GVFNNAAQVWNHTFYWNCLAPNAgGEPTGKVAEAIAASFGSFA 105
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 930576750  80 DFKASFTTAATSRFGSGWAWLVVNPDGKLEVMSTANQDTPISEGKTP 126
Cdd:PRK10543 106 DFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDATP 152
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
2-122 3.95e-23

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 88.69  E-value: 3.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930576750   2 TYVNNVNAALAKHPEIGEDLEQLLSDVETipadirqAVINNGGGHLNHALFWELMTPEKT-EPSAALAADLEATFGSFED 80
Cdd:PTZ00078  29 GYVNKLNGLIKGTPLENKTLEELIKEYSG-------AVFNNAAQIWNHNFYWLSMGPNGGgEPTGEIKEKIDEKFGSFDN 101
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 930576750  81 FKASFTTAATSRFGSGWAWLVVNPDGKLEVMSTANQDTPISE 122
Cdd:PTZ00078 102 FKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPIKD 143
PLN02622 PLN02622
iron superoxide dismutase
3-126 4.84e-19

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 79.67  E-value: 4.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930576750   3 YVNNVNAALAKHPEI-GEDLEQLL----SDVETIPAdirqavINNGGGHLNHALFWELMTPEKTE-PSAALAADLEATFG 76
Cdd:PLN02622  80 YVEGLNKQLAKDDILyGYTMDELVkvtyNNGNPLPE------FNNAAQVWNHDFFWESMQPGGGDmPELGVLEQIEKDFG 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 930576750  77 SFEDFKASFTTAATSRFGSGWAWLVVN-PDGKLEVMSTANQDTPISEGKTP 126
Cdd:PLN02622 154 SFTNFREKFTEAALTLFGSGWVWLVLKrEERRLEVVKTSNAINPLVWDDIP 204
PLN02685 PLN02685
iron superoxide dismutase
2-120 4.91e-18

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 77.35  E-value: 4.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930576750   2 TYVNNVNAALakhpeIGEDLEQL-LSDVETIP---ADIRQAvINNGGGHLNHALFWELMTPEKT-EPSAALAADLEATFG 76
Cdd:PLN02685  78 AYVDNLNKQI-----VGTELDGMsLEDVVLITynkGDMLPA-FNNAAQAWNHEFFWESMKPGGGgKPSGELLQLIERDFG 151
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 930576750  77 SFEDFKASFTTAATSRFGSGWAWLV-----------VNP-----DGKLEVMSTANQDTPI 120
Cdd:PLN02685 152 SFERFVEEFKSAAATQFGSGWAWLAykanrldvgnaVNPcpseeDKKLVVVKSPNAVNPL 211
PLN02471 PLN02471
superoxide dismutase [Mn]
2-125 8.11e-17

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 73.02  E-value: 8.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930576750   2 TYVNNVNAALakhpeigEDLEQLL--SDVETIpADIRQAVINNGGGHLNHALFWELMTPEKT----EPSAALAADLEATF 75
Cdd:PLN02471  62 TYVTNYNKAL-------EQLDQAVekGDASAV-VKLQSAIKFNGGGHVNHSIFWKNLAPVSEgggePPHGSLGWAIDEHF 133
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 930576750  76 GSFEDFKASFTTAATSRFGSGWAWLVVNPDG-KLEVMSTANQDTPISEGKT 125
Cdd:PLN02471 134 GSLEALVKKMSAEGAAVQGSGWVWLGLDKELkKLVVETTANQDPLVTKGPS 184
PLN02184 PLN02184
superoxide dismutase [Fe]
3-126 6.63e-15

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 67.85  E-value: 6.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930576750   3 YVNNVNAALAKHPEIGEDLEQLLSDV----ETIPAdirqavINNGGGHLNHALFWELMTPEKT-EPSAALAADLEATFGS 77
Cdd:PLN02184  43 YVDNLKKQVLGTELEGKPLEHIIHSTynngDLLPA------FNNAAQAWNHEFFWESMKPGGGgKPSGELLALLERDFTS 116
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 930576750  78 FEDFKASFTTAATSRFGSGWAWLVVNPDgKLEVMSTANQDTPISEGKTP 126
Cdd:PLN02184 117 YEKFYEEFNAAAATQFGAGWAWLAYSNE-KLKVVKTPNAVNPLVLGSFP 164
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
1-57 1.33e-14

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: 63.86  E-value: 1.33e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 930576750    1 NTYVNNVNAALAKHPEIGEDLEqllsdvETIPADIRQAVINNGGGHLNHALFWELMT 57
Cdd:pfam00081  32 QTYVNNLNAALEGLEEARKPLE------ELIIKALLGGLFNNGGGHWNHSLFWKNLS 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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