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Conserved domains on  [gi|308219988|gb|ADO22403|]
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epididymis secretory sperm binding protein [Homo sapiens]

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];
27-216 1.28e-108

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 309.75  E-value: 1.28e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  27 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAK--GDVTAQI--ALQPALKFNGGGHINHSIFW 102
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKslEEIIKKLseELKRALRNNAGGHWNHTLFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988 103 TNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLqgTTGLIPLLG 181
Cdd:COG0605   81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDnPL--MAGGTPLLG 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 308219988 182 IDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTER 216
Cdd:COG0605  158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
27-216 1.28e-108

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 309.75  E-value: 1.28e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  27 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAK--GDVTAQI--ALQPALKFNGGGHINHSIFW 102
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKslEEIIKKLseELKRALRNNAGGHWNHTLFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988 103 TNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLqgTTGLIPLLG 181
Cdd:COG0605   81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDnPL--MAGGTPLLG 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 308219988 182 IDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTER 216
Cdd:COG0605  158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PLN02471 PLN02471
superoxide dismutase [Mn]
 1-217 9.31e-91

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 266.39  E-value: 9.31e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988   1 MLSRAVCGTSRQLAPVLGYLGSRQKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTA 80
Cdd:PLN02471   6 LASRKTLGGLKETSSRLLSFRGLQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  81 QIALQPALKFNGGGHINHSIFWTNLSP--NGGGE-PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERG 157
Cdd:PLN02471  86 VVKLQSAIKFNGGGHVNHSIFWKNLAPvsEGGGEpPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELK 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 308219988 158 HLQIAACPNQDPLQGTTG-LIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERY 217
Cdd:PLN02471 166 KLVVETTANQDPLVTKGPsLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVY 226
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 113-216 4.55e-61

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: 186.09  E-value: 4.55e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  113 PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKeRGHLQIAACPNQDPLQgTTGLIPLLGIDVWEHAYYLQ 192
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPL-TDGLTPLLGLDVWEHAYYLD 78

                          90       100
                  ....*....|....*....|....
gi 308219988  193 YKNVRPDYLKAIWNVINWENVTER 216
Cdd:pfam02777  79 YQNRRADYVKAFWNVVNWDEVEKR 102
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
27-216 1.28e-108

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 309.75  E-value: 1.28e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  27 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAK--GDVTAQI--ALQPALKFNGGGHINHSIFW 102
Cdd:COG0605    1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKslEEIIKKLseELKRALRNNAGGHWNHTLFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988 103 TNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLqgTTGLIPLLG 181
Cdd:COG0605   81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDnPL--MAGGTPLLG 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 308219988 182 IDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTER 216
Cdd:COG0605  158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PLN02471 PLN02471
superoxide dismutase [Mn]
 1-217 9.31e-91

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 266.39  E-value: 9.31e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988   1 MLSRAVCGTSRQLAPVLGYLGSRQKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTA 80
Cdd:PLN02471   6 LASRKTLGGLKETSSRLLSFRGLQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  81 QIALQPALKFNGGGHINHSIFWTNLSP--NGGGE-PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERG 157
Cdd:PLN02471  86 VVKLQSAIKFNGGGHVNHSIFWKNLAPvsEGGGEpPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELK 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 308219988 158 HLQIAACPNQDPLQGTTG-LIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERY 217
Cdd:PLN02471 166 KLVVETTANQDPLVTKGPsLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVY 226
PRK10925 PRK10925
superoxide dismutase [Mn];
26-221 5.08e-67

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 205.16  E-value: 5.08e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  26 HSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQE--ALAKGDVTAQIALQPA-----LKFNGGGHINH 98
Cdd:PRK10925   3 YTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEfaNLPVEELITKLDQLPAdkktvLRNNAGGHANH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  99 SIFWTNLSPngGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERghLQIAACPNQD-PL-----QG 172
Cdd:PRK10925  83 SLFWKGLKK--GTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDK--LAVVSTANQDsPLmgeaiSG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 308219988 173 TTGLiPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACK 221
Cdd:PRK10925 159 ASGF-PILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 113-216 4.55e-61

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: 186.09  E-value: 4.55e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  113 PKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKeRGHLQIAACPNQDPLQgTTGLIPLLGIDVWEHAYYLQ 192
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP-DGKLEIVTTPNQDNPL-TDGLTPLLGLDVWEHAYYLD 78

                          90       100
                  ....*....|....*....|....
gi 308219988  193 YKNVRPDYLKAIWNVINWENVTER 216
Cdd:pfam02777  79 YQNRRADYVKAFWNVVNWDEVEKR 102
PRK10543 PRK10543
superoxide dismutase [Fe];
28-219 2.53e-54

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 172.44  E-value: 2.53e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  28 LPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNvteekyqeALAKGDVTAQIALQPALK------FNGGGHI-NHSI 100
Cdd:PRK10543   5 LPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLN--------NLIKGTAFEGKSLEEIVRsseggvFNNAAQVwNHTF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988 101 FWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLgFNKERGHLQIAACPNQ-DPLqgTTGLIPL 179
Cdd:PRK10543  77 YWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWL-VKNADGKLAIVSTSNAgTPL--TTDATPL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 308219988 180 LGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMA 219
Cdd:PRK10543 154 LTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 29-210 4.95e-52

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 166.50  E-value: 4.95e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  29 PDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNvteekyqeALAKGDVTAQIALQPALK------FNGGGHI-NHSIF 101
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLN--------GLIKGTPLENKTLEELIKeysgavFNNAAQIwNHNFY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988 102 WTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKErGHLQIAACPNQD-PLQGTTGlIPLL 180
Cdd:PTZ00078  73 WLSMGPNGGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKND-GKLEIVQTHDAGnPIKDNTG-KPLL 150

                        170       180       190
                 ....*....|....*....|....*....|
gi 308219988 181 GIDVWEHAYYLQYKNVRPDYLKAIWNVINW 210
Cdd:PTZ00078 151 TCDIWEHAYYIDYRNDRASYVNSWWNKVNW 180
PLN02685 PLN02685
iron superoxide dismutase
 32-221 3.38e-48

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 160.17  E-value: 3.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  32 PYDYGALEPHINAQIMQLHHSKHHAAYVNNLN-----------VTEEKYQEALAKGDvtaqiaLQPAlkFNGGGHI-NHS 99
Cdd:PLN02685  53 PYPLDALEPHMSRETLEYHWGKHHRAYVDNLNkqivgteldgmSLEDVVLITYNKGD------MLPA--FNNAAQAwNHE 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988 100 IFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERghLQIAACPNQDPLQGTTGLI-- 177
Cdd:PLN02685 125 FFWESMKPGGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAYKANR--LDVGNAVNPCPSEEDKKLVvv 202

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 308219988 178 --------------PLLGIDVWEHAYYLQYKNVRPDYLKA-IWNVINWENVTERYMACK 221
Cdd:PLN02685 203 kspnavnplvwdysPLLTIDVWEHAYYLDFQNRRPDYISTfMEKLVSWEAVSARLESAK 261
PLN02184 PLN02184
superoxide dismutase [Fe]
 32-221 3.53e-44

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 147.20  E-value: 3.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  32 PYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVT------EEKYQEALAKGDVTAQiALQPALKfNGGGHINHSIFWTNL 105
Cdd:PLN02184  17 PFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQvlgtelEGKPLEHIIHSTYNNG-DLLPAFN-NAAQAWNHEFFWESM 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988 106 SPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERghLQIAACPNQ-DPLqgTTGLIPLLGIDV 184
Cdd:PLN02184  95 KPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEK--LKVVKTPNAvNPL--VLGSFPLLTIDV 170

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 308219988 185 WEHAYYLQYKNVRPDYLKA-IWNVINWENVTERYMACK 221
Cdd:PLN02184 171 WEHAYYLDFQNRRPDYIKTfMTNLVSWEAVSARLEAAK 208
PLN02622 PLN02622
iron superoxide dismutase
 10-219 3.68e-43

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 145.93  E-value: 3.68e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  10 SRQLAPVLGYLGsrqkhsLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNvteekyqEALAKGDVTAQIALQ---- 85
Cdd:PLN02622  38 LQRASKVVAYYG------LKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLN-------KQLAKDDILYGYTMDelvk 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988  86 -------PALKFNGGGHI-NHSIFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERG 157
Cdd:PLN02622 105 vtynngnPLPEFNNAAQVwNHDFFWESMQPGGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREER 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308219988 158 HLQIAACPNQ-DPLqgTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWN-VINWENVTERyMA 219
Cdd:PLN02622 185 RLEVVKTSNAiNPL--VWDDIPIICLDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAMAR-MA 245
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 25-106 2.46e-42

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: 137.82  E-value: 2.46e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308219988   25 KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTN 104
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIKALLGGLFNNGGGHWNHSLFWKN 80


                  ..
gi 308219988  105 LS 106
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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