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Conserved domains on  [gi|317045668|gb|ADU90402|]
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superoxide dismutase, partial [Streptococcus equi subsp. zooepidemicus]

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];
1-177 1.69e-87

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 254.67  E-value: 1.69e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668   1 EPYFDTETMTLHHDKHHATYVANTNTALEKYPELGENLEELLadVSSIPADIRQAVINNGGGHLNHALFWELLSPE-KQE 79
Cdd:COG0605   13 EPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEI--IKKLSEELKRALRNNAGGHWNHTLFWENLSPNgGGE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668  80 VSADVAAAIDDAFGSFAAFKEQFTAAATGRFGSGWAWLVVNKAGQLEITSTANQDTPISEGKQPILALDVWEHAYYLNYR 159
Cdd:COG0605   91 PTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLGLDVWEHAYYLDYQ 170
                        170
                 ....*....|....*...
gi 317045668 160 NVRPNYIKAFFEIINWKK 177
Cdd:COG0605  171 NRRPDYVDAFWNVVNWDF 188
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
1-177 1.69e-87

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 254.67  E-value: 1.69e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668   1 EPYFDTETMTLHHDKHHATYVANTNTALEKYPELGENLEELLadVSSIPADIRQAVINNGGGHLNHALFWELLSPE-KQE 79
Cdd:COG0605   13 EPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEI--IKKLSEELKRALRNNAGGHWNHTLFWENLSPNgGGE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668  80 VSADVAAAIDDAFGSFAAFKEQFTAAATGRFGSGWAWLVVNKAGQLEITSTANQDTPISEGKQPILALDVWEHAYYLNYR 159
Cdd:COG0605   91 PTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLGLDVWEHAYYLDYQ 170
                        170
                 ....*....|....*...
gi 317045668 160 NVRPNYIKAFFEIINWKK 177
Cdd:COG0605  171 NRRPDYVDAFWNVVNWDF 188
PRK10925 PRK10925
superoxide dismutase [Mn];
1-175 2.00e-61

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 188.98  E-value: 2.00e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668   1 EPYFDTETMTLHHDKHHATYVANTNTALEKYPELGENLEELL-ADVSSIPADIRQAVINNGGGHLNHALFWELLSpEKQE 79
Cdd:PRK10925  16 EPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELiTKLDQLPADKKTVLRNNAGGHANHSLFWKGLK-KGTT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668  80 VSADVAAAIDDAFGSFAAFKEQFTAAATGRFGSGWAWLVVnKAGQLEITSTANQDTPI------SEGKQPILALDVWEHA 153
Cdd:PRK10925  95 LQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVL-KGDKLAVVSTANQDSPLmgeaisGASGFPILGLDVWEHA 173
                        170       180
                 ....*....|....*....|..
gi 317045668 154 YYLNYRNVRPNYIKAFFEIINW 175
Cdd:PRK10925 174 YYLKFQNRRPDYIKEFWNVVNW 195
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
92-177 7.97e-55

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: 168.76  E-value: 7.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668   92 FGSFAAFKEQFTAAATGRFGSGWAWLVVNKAGQLEITSTANQDTPISEGKQPILALDVWEHAYYLNYRNVRPNYIKAFFE 171
Cdd:pfam02777  13 FGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQNRRADYVKAFWN 92

                  ....*.
gi 317045668  172 IINWKK 177
Cdd:pfam02777  93 VVNWDE 98
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
1-177 1.69e-87

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 254.67  E-value: 1.69e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668   1 EPYFDTETMTLHHDKHHATYVANTNTALEKYPELGENLEELLadVSSIPADIRQAVINNGGGHLNHALFWELLSPE-KQE 79
Cdd:COG0605   13 EPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEI--IKKLSEELKRALRNNAGGHWNHTLFWENLSPNgGGE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668  80 VSADVAAAIDDAFGSFAAFKEQFTAAATGRFGSGWAWLVVNKAGQLEITSTANQDTPISEGKQPILALDVWEHAYYLNYR 159
Cdd:COG0605   91 PTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLGLDVWEHAYYLDYQ 170
                        170
                 ....*....|....*...
gi 317045668 160 NVRPNYIKAFFEIINWKK 177
Cdd:COG0605  171 NRRPDYVDAFWNVVNWDF 188
PRK10925 PRK10925
superoxide dismutase [Mn];
1-175 2.00e-61

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 188.98  E-value: 2.00e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668   1 EPYFDTETMTLHHDKHHATYVANTNTALEKYPELGENLEELL-ADVSSIPADIRQAVINNGGGHLNHALFWELLSpEKQE 79
Cdd:PRK10925  16 EPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELiTKLDQLPADKKTVLRNNAGGHANHSLFWKGLK-KGTT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668  80 VSADVAAAIDDAFGSFAAFKEQFTAAATGRFGSGWAWLVVnKAGQLEITSTANQDTPI------SEGKQPILALDVWEHA 153
Cdd:PRK10925  95 LQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVL-KGDKLAVVSTANQDSPLmgeaisGASGFPILGLDVWEHA 173
                        170       180
                 ....*....|....*....|..
gi 317045668 154 YYLNYRNVRPNYIKAFFEIINW 175
Cdd:PRK10925 174 YYLKFQNRRPDYIKEFWNVVNW 195
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
92-177 7.97e-55

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: 168.76  E-value: 7.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668   92 FGSFAAFKEQFTAAATGRFGSGWAWLVVNKAGQLEITSTANQDTPISEGKQPILALDVWEHAYYLNYRNVRPNYIKAFFE 171
Cdd:pfam02777  13 FGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQNRRADYVKAFWN 92

                  ....*.
gi 317045668  172 IINWKK 177
Cdd:pfam02777  93 VVNWDE 98
PRK10543 PRK10543
superoxide dismutase [Fe];
1-176 4.05e-43

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 142.01  E-value: 4.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668   1 EPYFDTETMTLHHDKHHATYVANTNTALEKYPELGENleelladVSSIPADIRQAVINNGGGHLNHALFWELLSPEK-QE 79
Cdd:PRK10543  16 APHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKS-------LEEIVRSSEGGVFNNAAQVWNHTFYWNCLAPNAgGE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668  80 VSADVAAAIDDAFGSFAAFKEQFTAAATGRFGSGWAWLVVNKAGQLEITSTANQDTPISEGKQPILALDVWEHAYYLNYR 159
Cdd:PRK10543  89 PTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDATPLLTVDVWEHAYYIDYR 168
                        170
                 ....*....|....*..
gi 317045668 160 NVRPNYIKAFFEIINWK 176
Cdd:PRK10543 169 NARPGYLEHFWALVNWE 185
PLN02471 PLN02471
superoxide dismutase [Mn]
1-176 4.85e-43

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 143.12  E-value: 4.85e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668   1 EPYFDTETMTLHHDKHHATYVANTNTALEKYpelgeNLEELLADVSSIpADIRQAVINNGGGHLNHALFWELLSPEKQ-- 78
Cdd:PLN02471  44 EPAISGEIMQLHHQKHHQTYVTNYNKALEQL-----DQAVEKGDASAV-VKLQSAIKFNGGGHVNHSIFWKNLAPVSEgg 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668  79 --EVSADVAAAIDDAFGSFAAFKEQFTAAATGRFGSGWAWLVVNK-AGQLEITSTANQDTPISEGKQ--PILALDVWEHA 153
Cdd:PLN02471 118 gePPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKeLKKLVVETTANQDPLVTKGPSlvPLLGIDVWEHA 197
                        170       180
                 ....*....|....*....|...
gi 317045668 154 YYLNYRNVRPNYIKAFFEIINWK 176
Cdd:PLN02471 198 YYLQYKNVRPDYLKNIWKVMNWK 220
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
2-175 5.27e-41

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 136.46  E-value: 5.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668   2 PYFDTETMTLHHDKHHATYVANTNTALEKYPELGENLEELLADVSSipadirqAVINNGGGHLNHALFWELLSPEKQ-EV 80
Cdd:PTZ00078  12 PHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLENKTLEELIKEYSG-------AVFNNAAQIWNHNFYWLSMGPNGGgEP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668  81 SADVAAAIDDAFGSFAAFKEQFTAAATGRFGSGWAWLVVNKAGQLEITSTANQDTPISE--GKqPILALDVWEHAYYLNY 158
Cdd:PTZ00078  85 TGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPIKDntGK-PLLTCDIWEHAYYIDY 163
                        170
                 ....*....|....*..
gi 317045668 159 RNVRPNYIKAFFEIINW 175
Cdd:PTZ00078 164 RNDRASYVNSWWNKVNW 180
PLN02622 PLN02622
iron superoxide dismutase
1-175 2.34e-35

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 123.97  E-value: 2.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668   1 EPYFDTETMTLHHDKHHATYVANTNTALEKYPELGENLEELLADVS-----SIPAdirqavINNGGGHLNHALFWELLSP 75
Cdd:PLN02622  61 EPYMSRRTLEVHWGEHHRGYVEGLNKQLAKDDILYGYTMDELVKVTynngnPLPE------FNNAAQVWNHDFFWESMQP 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668  76 EKQEVSAD-VAAAIDDAFGSFAAFKEQFTAAATGRFGSGWAWLVVNKAG-QLEITSTANQDTPISEGKQPILALDVWEHA 153
Cdd:PLN02622 135 GGGDMPELgVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREErRLEVVKTSNAINPLVWDDIPIICLDVWEHA 214
                        170       180
                 ....*....|....*....|...
gi 317045668 154 YYLNYRNVRPNYIKAFFE-IINW 175
Cdd:PLN02622 215 YYLDYKNDRGKYVNAFMNhLVSW 237
PLN02685 PLN02685
iron superoxide dismutase
1-176 3.09e-30

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 111.63  E-value: 3.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668   1 EPYFDTETMTLHHDKHHATYVANTN-----TALEKYPELGENLEELLADvSSIPAdirqavINNGGGHLNHALFWELLSP 75
Cdd:PLN02685  60 EPHMSRETLEYHWGKHHRAYVDNLNkqivgTELDGMSLEDVVLITYNKG-DMLPA------FNNAAQAWNHEFFWESMKP 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668  76 EKQ-EVSADVAAAIDDAFGSFAAFKEQFTAAATGRFGSGWAWLVVnKAGQLEITSTANQdTPISEGKQ------------ 142
Cdd:PLN02685 133 GGGgKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAY-KANRLDVGNAVNP-CPSEEDKKlvvvkspnavnp 210
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 317045668 143 ------PILALDVWEHAYYLNYRNVRPNYIKAFFE-IINWK 176
Cdd:PLN02685 211 lvwdysPLLTIDVWEHAYYLDFQNRRPDYISTFMEkLVSWE 251
PLN02184 PLN02184
superoxide dismutase [Fe]
1-176 6.53e-27

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 100.98  E-value: 6.53e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668   1 EPYFDTETMTLHHDKHHATYVANTN-----TALEKYPELGENLEELLaDVSSIPAdirqavINNGGGHLNHALFWELLSP 75
Cdd:PLN02184  24 EPHMSKQTLEFHWGKHHRAYVDNLKkqvlgTELEGKPLEHIIHSTYN-NGDLLPA------FNNAAQAWNHEFFWESMKP 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317045668  76 EKQ-EVSADVAAAIDDAFGSFAAFKEQFTAAATGRFGSGWAWLVVNKaGQLEITSTANQDTPISEGKQPILALDVWEHAY 154
Cdd:PLN02184  97 GGGgKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSN-EKLKVVKTPNAVNPLVLGSFPLLTIDVWEHAY 175
                        170       180
                 ....*....|....*....|...
gi 317045668 155 YLNYRNVRPNYIKAFF-EIINWK 176
Cdd:PLN02184 176 YLDFQNRRPDYIKTFMtNLVSWE 198
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
1-74 7.98e-20

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: 78.89  E-value: 7.98e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317045668    1 EPYFDTETMTLHHDKHHATYVANTNTALEKYPelgenlEELLADVSSIPADIRQAVINNGGGHLNHALFWELLS 74
Cdd:pfam00081  15 EPHISKETMEIHHTKHHQTYVNNLNAALEGLE------EARKPLEELIIKALLGGLFNNGGGHWNHSLFWKNLS 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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