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Conserved domains on  [gi|521101615|ref|WP_020432486|]
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MULTISPECIES: superoxide dismutase [Fe] [Vibrio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10543 super family cl29657
superoxide dismutase [Fe];
1-193 3.04e-124

superoxide dismutase [Fe];


The actual alignment was detected with superfamily member PRK10543:

Pssm-ID: 182534  Cd Length: 193  Bit Score: 348.48  E-value: 3.04e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615   1 MAFELPALPYAKDALEPHISAETLDYHHGKHHNTYVVKLNGLIPGTEFEGKTLEEIIKTSTGGVFNNAAQIWNHTFYWHC 80
Cdd:PRK10543   1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSSEGGVFNNAAQVWNHTFYWNC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615  81 LSPNGGGEPTGAVADAINAAFGSFEEFKAKFTDSAINNFGSSWTWLVKKADGSLAITNTSNAGTPLTEEGvTPLLTVDLW 160
Cdd:PRK10543  81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDA-TPLLTVDVW 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 521101615 161 EHAYYIDYRNVRPDYMNGFWALVNWEFVAANLA 193
Cdd:PRK10543 160 EHAYYIDYRNARPGYLEHFWALVNWEFVAKNLA 192
 
Name Accession Description Interval E-value
PRK10543 PRK10543
superoxide dismutase [Fe];
1-193 3.04e-124

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 348.48  E-value: 3.04e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615   1 MAFELPALPYAKDALEPHISAETLDYHHGKHHNTYVVKLNGLIPGTEFEGKTLEEIIKTSTGGVFNNAAQIWNHTFYWHC 80
Cdd:PRK10543   1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSSEGGVFNNAAQVWNHTFYWNC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615  81 LSPNGGGEPTGAVADAINAAFGSFEEFKAKFTDSAINNFGSSWTWLVKKADGSLAITNTSNAGTPLTEEGvTPLLTVDLW 160
Cdd:PRK10543  81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDA-TPLLTVDVW 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 521101615 161 EHAYYIDYRNVRPDYMNGFWALVNWEFVAANLA 193
Cdd:PRK10543 160 EHAYYIDYRNARPGYLEHFWALVNWEFVAKNLA 192
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-191 2.68e-116

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 328.24  E-value: 2.68e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615   4 ELPALPYAKDALEPHISAETLDYHHGKHHNTYVVKLNGLIPGT-EFEGKTLEEIIKTS----TGGVFNNAAQIWNHTFYW 78
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLaELEDKSLEEIIKKLseelKRALRNNAGGHWNHTLFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615  79 HCLSPNGGGEPTGAVADAINAAFGSFEEFKAKFTDSAINNFGSSWTWLVKKADGSLAITNTSNAGTPLTeEGVTPLLTVD 158
Cdd:COG0605   81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLM-AGGTPLLGLD 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 521101615 159 LWEHAYYIDYRNVRPDYMNGFWALVNWEFVAAN 191
Cdd:COG0605  160 VWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 89-191 3.03e-57

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: 175.31  E-value: 3.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615   89 PTGAVADAINAAFGSFEEFKAKFTDSAINNFGSSWTWLVKKADGSLAITNTSNAGTPLTeEGVTPLLTVDLWEHAYYIDY 168
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLT-DGLTPLLGLDVWEHAYYLDY 79

                          90       100
                  ....*....|....*....|...
gi 521101615  169 RNVRPDYMNGFWALVNWEFVAAN 191
Cdd:pfam02777  80 QNRRADYVKAFWNVVNWDEVEKR 102
 
Name Accession Description Interval E-value
PRK10543 PRK10543
superoxide dismutase [Fe];
1-193 3.04e-124

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 348.48  E-value: 3.04e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615   1 MAFELPALPYAKDALEPHISAETLDYHHGKHHNTYVVKLNGLIPGTEFEGKTLEEIIKTSTGGVFNNAAQIWNHTFYWHC 80
Cdd:PRK10543   1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSSEGGVFNNAAQVWNHTFYWNC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615  81 LSPNGGGEPTGAVADAINAAFGSFEEFKAKFTDSAINNFGSSWTWLVKKADGSLAITNTSNAGTPLTEEGvTPLLTVDLW 160
Cdd:PRK10543  81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDA-TPLLTVDVW 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 521101615 161 EHAYYIDYRNVRPDYMNGFWALVNWEFVAANLA 193
Cdd:PRK10543 160 EHAYYIDYRNARPGYLEHFWALVNWEFVAKNLA 192
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-191 2.68e-116

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 328.24  E-value: 2.68e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615   4 ELPALPYAKDALEPHISAETLDYHHGKHHNTYVVKLNGLIPGT-EFEGKTLEEIIKTS----TGGVFNNAAQIWNHTFYW 78
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLaELEDKSLEEIIKKLseelKRALRNNAGGHWNHTLFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615  79 HCLSPNGGGEPTGAVADAINAAFGSFEEFKAKFTDSAINNFGSSWTWLVKKADGSLAITNTSNAGTPLTeEGVTPLLTVD 158
Cdd:COG0605   81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLM-AGGTPLLGLD 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 521101615 159 LWEHAYYIDYRNVRPDYMNGFWALVNWEFVAAN 191
Cdd:COG0605  160 VWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 6-194 1.95e-89

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 260.49  E-value: 1.95e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615   6 PALPYAKDALEPHISAETLDYHHGKHHNTYVVKLNGLIPGTEFEGKTLEEIIKTSTGGVFNNAAQIWNHTFYWHCLSPNG 85
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLENKTLEELIKEYSGAVFNNAAQIWNHNFYWLSMGPNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615  86 GGEPTGAVADAINAAFGSFEEFKAKFTDSAINNFGSSWTWLVKKADGSLAITNTSNAGTPLTEEGVTPLLTVDLWEHAYY 165
Cdd:PTZ00078  81 GGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPIKDNTGKPLLTCDIWEHAYY 160

                        170       180
                 ....*....|....*....|....*....
gi 521101615 166 IDYRNVRPDYMNGFWALVNWEFVAANLAK 194
Cdd:PTZ00078 161 IDYRNDRASYVNSWWNKVNWDFANKNLKK 189
PLN02685 PLN02685
iron superoxide dismutase
 3-192 8.75e-73

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 221.80  E-value: 8.75e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615   3 FELPALPYAKDALEPHISAETLDYHHGKHHNTYVVKLNGLIPGTEFEGKTLEEII-----KTSTGGVFNNAAQIWNHTFY 77
Cdd:PLN02685  47 FELKPPPYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQIVGTELDGMSLEDVVlitynKGDMLPAFNNAAQAWNHEFF 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615  78 WHCLSPNGGGEPTGAVADAINAAFGSFEEFKAKFTDSAINNFGSSWTWLVKKA----------------DGSLAITNTSN 141
Cdd:PLN02685 127 WESMKPGGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAYKAnrldvgnavnpcpseeDKKLVVVKSPN 206

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 521101615 142 AGTPLTEEgVTPLLTVDLWEHAYYIDYRNVRPDYMNGFWA-LVNWEFVAANL 192
Cdd:PLN02685 207 AVNPLVWD-YSPLLTIDVWEHAYYLDFQNRRPDYISTFMEkLVSWEAVSARL 257
PLN02622 PLN02622
iron superoxide dismutase
 3-194 2.02e-58

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 184.06  E-value: 2.02e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615   3 FELPALPYAKDALEPHISAETLDYHHGKHHNTYVVKLNGLIPGTE-FEGKTLEEIIK-TSTGG----VFNNAAQIWNHTF 76
Cdd:PLN02622  48 YGLKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAKDDiLYGYTMDELVKvTYNNGnplpEFNNAAQVWNHDF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615  77 YWHCLSPNGGGEPTGAVADAINAAFGSFEEFKAKFTDSAINNFGSSWTWLV-KKADGSLAITNTSNAGTPLTEEGVtPLL 155
Cdd:PLN02622 128 FWESMQPGGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVlKREERRLEVVKTSNAINPLVWDDI-PII 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 521101615 156 TVDLWEHAYYIDYRNVRPDYMNGFWA-LVNWEFVAANLAK 194
Cdd:PLN02622 207 CLDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAMARMAR 246
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 89-191 3.03e-57

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: 175.31  E-value: 3.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615   89 PTGAVADAINAAFGSFEEFKAKFTDSAINNFGSSWTWLVKKADGSLAITNTSNAGTPLTeEGVTPLLTVDLWEHAYYIDY 168
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLT-DGLTPLLGLDVWEHAYYLDY 79

                          90       100
                  ....*....|....*....|...
gi 521101615  169 RNVRPDYMNGFWALVNWEFVAAN 191
Cdd:pfam02777  80 QNRRADYVKAFWNVVNWDEVEKR 102
PLN02184 PLN02184
superoxide dismutase [Fe]
 9-192 3.62e-55

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 174.17  E-value: 3.62e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615   9 PYAKDALEPHISAETLDYHHGKHHNTYVVKLNGLIPGTEFEGKTLEEIIKTSTGG-----VFNNAAQIWNHTFYWHCLSP 83
Cdd:PLN02184  17 PFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTELEGKPLEHIIHSTYNNgdllpAFNNAAQAWNHEFFWESMKP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615  84 NGGGEPTGAVADAINAAFGSFEEFKAKFTDSAINNFGSSWTWLVkKADGSLAITNTSNAGTPLTeEGVTPLLTVDLWEHA 163
Cdd:PLN02184  97 GGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLA-YSNEKLKVVKTPNAVNPLV-LGSFPLLTIDVWEHA 174

                        170       180       190
                 ....*....|....*....|....*....|
gi 521101615 164 YYIDYRNVRPDYMNGFWA-LVNWEFVAANL 192
Cdd:PLN02184 175 YYLDFQNRRPDYIKTFMTnLVSWEAVSARL 204
PRK10925 PRK10925
superoxide dismutase [Mn];
1-193 5.68e-53

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 168.18  E-value: 5.68e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615   1 MAFELPALPYAKDALEPHISAETLDYHHGKHHNTYVVKLNGLIPG-TEFEGKTLEEIIKT-------STGGVFNNAAQIW 72
Cdd:PRK10925   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESlPEFANLPVEELITKldqlpadKKTVLRNNAGGHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615  73 NHTFYWHCLSPngGGEPTGAVADAINAAFGSFEEFKAKFTDSAINNFGSSWTWLVKKADgSLAITNTSNAGTPLTEEGVT 152
Cdd:PRK10925  81 NHSLFWKGLKK--GTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGD-KLAVVSTANQDSPLMGEAIS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 521101615 153 -----PLLTVDLWEHAYYIDYRNVRPDYMNGFWALVNWEFVAANLA 193
Cdd:PRK10925 158 gasgfPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFA 203
PLN02471 PLN02471
superoxide dismutase [Mn]
 3-187 1.78e-41

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 139.66  E-value: 1.78e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615   3 FELPALPYAKDALEPHISAETLDYHHGKHHNTYVVKLNGLIPGTE--FEGKTLEEIIKTSTGGVFNNAAQIwNHTFYWHC 80
Cdd:PLN02471  31 FTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDqaVEKGDASAVVKLQSAIKFNGGGHV-NHSIFWKN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615  81 LSP--NGGGE-PTGAVADAINAAFGSFEEFKAKFTDSAINNFGSSWTWL-VKKADGSLAITNTSNAgTPLTEEG--VTPL 154
Cdd:PLN02471 110 LAPvsEGGGEpPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLgLDKELKKLVVETTANQ-DPLVTKGpsLVPL 188

                        170       180       190
                 ....*....|....*....|....*....|...
gi 521101615 155 LTVDLWEHAYYIDYRNVRPDYMNGFWALVNWEF 187
Cdd:PLN02471 189 LGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKY 221
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 2-82 1.67e-38

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: 127.04  E-value: 1.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521101615    2 AFELPALPYAKDALEPHISAETLDYHHGKHHNTYVVKLNGLIPGTEFEGKTLEEII-KTSTGGVFNNAAQIWNHTFYWHC 80
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIiKALLGGLFNNGGGHWNHSLFWKN 80


                  ..
gi 521101615   81 LS 82
Cdd:pfam00081  81 LS 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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