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Conserved domains on  [gi|2914416|pdb|1AP6|A]
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Chain A, MANGANESE SUPEROXIDE DISMUTASE

Protein Classification

superoxide dismutase( domain architecture ID 11427369)

superoxide dismutase eliminates superoxide radicals by catalyzing their conversion into hydrogen peroxide and oxygen

EC:  1.15.1.1
Gene Ontology:  GO:0046872|GO:0004784

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];
3-192 4.76e-105

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 299.74  E-value: 4.76e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A        3 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAFVNNLNVTEEKYQEALAK--GDVTAQI--ALQPALKFNGGGHINHSIFW 78
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKslEEIIKKLseELKRALRNNAGGHWNHTLFW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A       79 TNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLqgTTGLIPLLG 157
Cdd:COG0605  81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDnPL--MAGGTPLLG 157
                       170       180       190
                ....*....|....*....|....*....|....*
1AP6_A      158 IDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTER 192
Cdd:COG0605 158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
3-192 4.76e-105

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 299.74  E-value: 4.76e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A        3 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAFVNNLNVTEEKYQEALAK--GDVTAQI--ALQPALKFNGGGHINHSIFW 78
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKslEEIIKKLseELKRALRNNAGGHWNHTLFW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A       79 TNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLqgTTGLIPLLG 157
Cdd:COG0605  81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDnPL--MAGGTPLLG 157
                       170       180       190
                ....*....|....*....|....*....|....*
1AP6_A      158 IDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTER 192
Cdd:COG0605 158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PLN02471 PLN02471
superoxide dismutase [Mn]
3-193 1.39e-88

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 259.84  E-value: 1.39e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A         3 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAFVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLS 82
Cdd:PLN02471  32 TLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFWKNLA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A        83 P--NGGGE-PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTG-LIPLLGI 158
Cdd:PLN02471 112 PvsEGGGEpPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGPsLVPLLGI 191
                        170       180       190
                 ....*....|....*....|....*....|....*
1AP6_A       159 DVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERY 193
Cdd:PLN02471 192 DVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVY 226
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
89-192 3.38e-60

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: 183.01  E-value: 3.38e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A         89 PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKeRGHLQIAACPNQDPLQgTTGLIPLLGIDVWEHAYYLQ 168
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPL-TDGLTPLLGLDVWEHAYYLD 78
                          90       100
                  ....*....|....*....|....
1AP6_A        169 YKNVRPDYLKAIWNVINWENVTER 192
Cdd:pfam02777  79 YQNRRADYVKAFWNVVNWDEVEKR 102
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
3-192 4.76e-105

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 299.74  E-value: 4.76e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A        3 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAFVNNLNVTEEKYQEALAK--GDVTAQI--ALQPALKFNGGGHINHSIFW 78
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKslEEIIKKLseELKRALRNNAGGHWNHTLFW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A       79 TNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLqgTTGLIPLLG 157
Cdd:COG0605  81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDnPL--MAGGTPLLG 157
                       170       180       190
                ....*....|....*....|....*....|....*
1AP6_A      158 IDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTER 192
Cdd:COG0605 158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PLN02471 PLN02471
superoxide dismutase [Mn]
3-193 1.39e-88

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 259.84  E-value: 1.39e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A         3 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAFVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLS 82
Cdd:PLN02471  32 TLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFWKNLA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A        83 P--NGGGE-PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTG-LIPLLGI 158
Cdd:PLN02471 112 PvsEGGGEpPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGPsLVPLLGI 191
                        170       180       190
                 ....*....|....*....|....*....|....*
1AP6_A       159 DVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERY 193
Cdd:PLN02471 192 DVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVY 226
PRK10925 PRK10925
superoxide dismutase [Mn];
2-197 1.95e-65

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 200.15  E-value: 1.95e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A         2 HSLPDLPYDYGALEPHINAQIMQLHHSKHHAAFVNNLNVTEEKYQE--ALAKGDVTAQIALQPA-----LKFNGGGHINH 74
Cdd:PRK10925   3 YTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEfaNLPVEELITKLDQLPAdkktvLRNNAGGHANH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A        75 SIFWTNLSPngGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERghLQIAACPNQD-PL-----QG 148
Cdd:PRK10925  83 SLFWKGLKK--GTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDK--LAVVSTANQDsPLmgeaiSG 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
1AP6_A       149 TTGLiPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACK 197
Cdd:PRK10925 159 ASGF-PILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
89-192 3.38e-60

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: 183.01  E-value: 3.38e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A         89 PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKeRGHLQIAACPNQDPLQgTTGLIPLLGIDVWEHAYYLQ 168
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPL-TDGLTPLLGLDVWEHAYYLD 78
                          90       100
                  ....*....|....*....|....
1AP6_A        169 YKNVRPDYLKAIWNVINWENVTER 192
Cdd:pfam02777  79 YQNRRADYVKAFWNVVNWDEVEKR 102
PRK10543 PRK10543
superoxide dismutase [Fe];
4-195 1.45e-52

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 167.05  E-value: 1.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A         4 LPDLPYDYGALEPHINAQIMQLHHSKHHAAFVNNLNvteekyqeALAKGDVTAQIALQPALK------FNGGGHI-NHSI 76
Cdd:PRK10543   5 LPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLN--------NLIKGTAFEGKSLEEIVRsseggvFNNAAQVwNHTF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A        77 FWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLgFNKERGHLQIAACPNQ-DPLqgTTGLIPL 155
Cdd:PRK10543  77 YWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWL-VKNADGKLAIVSTSNAgTPL--TTDATPL 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
1AP6_A       156 LGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMA 195
Cdd:PRK10543 154 LTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
5-186 8.71e-50

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 159.95  E-value: 8.71e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A         5 PDLPYDYGALEPHINAQIMQLHHSKHHAAFVNNLNvteekyqeALAKGDVTAQIALQPALK------FNGGGHI-NHSIF 77
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLN--------GLIKGTPLENKTLEELIKeysgavFNNAAQIwNHNFY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A        78 WTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLQGTTGlIPLL 156
Cdd:PTZ00078  73 WLSMGPNGGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKND-GKLEIVQTHDAGnPIKDNTG-KPLL 150
                        170       180       190
                 ....*....|....*....|....*....|
1AP6_A       157 GIDVWEHAYYLQYKNVRPDYLKAIWNVINW 186
Cdd:PTZ00078 151 TCDIWEHAYYIDYRNDRASYVNSWWNKVNW 180
PLN02685 PLN02685
iron superoxide dismutase
8-197 2.44e-47

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 157.09  E-value: 2.44e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A         8 PYDYGALEPHINAQIMQLHHSKHHAAFVNNLN-----------VTEEKYQEALAKGDvtaqiaLQPAlkFNGGGHI-NHS 75
Cdd:PLN02685  53 PYPLDALEPHMSRETLEYHWGKHHRAYVDNLNkqivgteldgmSLEDVVLITYNKGD------MLPA--FNNAAQAwNHE 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A        76 IFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERghLQIAACPNQDPLQGTTGLI-- 153
Cdd:PLN02685 125 FFWESMKPGGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAYKANR--LDVGNAVNPCPSEEDKKLVvv 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
1AP6_A       154 --------------PLLGIDVWEHAYYLQYKNVRPDYLKA-IWNVINWENVTERYMACK 197
Cdd:PLN02685 203 kspnavnplvwdysPLLTIDVWEHAYYLDFQNRRPDYISTfMEKLVSWEAVSARLESAK 261
PLN02184 PLN02184
superoxide dismutase [Fe]
8-197 3.74e-43

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 143.73  E-value: 3.74e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A         8 PYDYGALEPHINAQIMQLHHSKHHAAFVNNLNVT------EEKYQEALAKGDVTAQiALQPALKfNGGGHINHSIFWTNL 81
Cdd:PLN02184  17 PFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQvlgtelEGKPLEHIIHSTYNNG-DLLPAFN-NAAQAWNHEFFWESM 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A        82 SPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERghLQIAACPNQ-DPLqgTTGLIPLLGIDV 160
Cdd:PLN02184  95 KPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEK--LKVVKTPNAvNPL--VLGSFPLLTIDV 170
                        170       180       190
                 ....*....|....*....|....*....|....*...
1AP6_A       161 WEHAYYLQYKNVRPDYLKA-IWNVINWENVTERYMACK 197
Cdd:PLN02184 171 WEHAYYLDFQNRRPDYIKTfMTNLVSWEAVSARLEAAK 208
PLN02622 PLN02622
iron superoxide dismutase
8-195 6.80e-42

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 141.69  E-value: 6.80e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A         8 PYDYGALEPHINAQIMQLHHSKHHAAFVNNLNvteekyqEALAKGDVTAQIALQ-----------PALKFNGGGHI-NHS 75
Cdd:PLN02622  54 PYPLDALEPYMSRRTLEVHWGEHHRGYVEGLN-------KQLAKDDILYGYTMDelvkvtynngnPLPEFNNAAQVwNHD 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A        76 IFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQ-DPLqgTTGLIP 154
Cdd:PLN02622 127 FFWESMQPGGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREERRLEVVKTSNAiNPL--VWDDIP 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
1AP6_A       155 LLGIDVWEHAYYLQYKNVRPDYLKAIWN-VINWENVTERyMA 195
Cdd:PLN02622 205 IICLDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAMAR-MA 245
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
1-82 2.37e-40

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: 132.04  E-value: 2.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AP6_A          1 KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAFVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTN 80
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIKALLGGLFNNGGGHWNHSLFWKN 80

                  ..
1AP6_A         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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