|
Name |
Accession |
Description |
Interval |
E-value |
| SodA |
COG0605 |
Superoxide dismutase [Inorganic ion transport and metabolism]; |
1-136 |
1.29e-63 |
|
Superoxide dismutase [Inorganic ion transport and metabolism];
Pssm-ID: 440370 [Multi-domain] Cd Length: 192 Bit Score: 192.27 E-value: 1.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100022 1 HHDKHHQTYVNNANAALEKHPEI-GEDLEALLADvesIPADIRQALINNGGGHLNHALFWELMTPE-KTAPSAELAAAID 78
Cdd:COG0605 24 HHDKHHQAYVNNLNAALEGLAELeDKSLEEIIKK---LSEELKRALRNNAGGHWNHTLFWENLSPNgGGEPTGELAAAIE 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1686100022 79 ATFGSLEEFQAAFTAAATTRFGSGWAWLVVNKEGKLEVTSTANQDTPISEGKKPILGL 136
Cdd:COG0605 101 ADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLGL 158
|
|
| PRK10925 |
PRK10925 |
superoxide dismutase [Mn]; |
1-136 |
1.34e-43 |
|
superoxide dismutase [Mn];
Pssm-ID: 182843 Cd Length: 206 Bit Score: 141.98 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100022 1 HHDKHHQTYVNNANAALEKHPEIGE-DLEALLADVESIPADIRQALINNGGGHLNHALFWELMTpEKTAPSAELAAAIDA 79
Cdd:PRK10925 27 HHTKHHQTYVNNANAALESLPEFANlPVEELITKLDQLPADKKTVLRNNAGGHANHSLFWKGLK-KGTTLQGDLKAAIER 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1686100022 80 TFGSLEEFQAAFTAAATTRFGSGWAWLVVnKEGKLEVTSTANQDTPI------SEGKKPILGL 136
Cdd:PRK10925 106 DFGSVDNFKAEFEKAAATRFGSGWAWLVL-KGDKLAVVSTANQDSPLmgeaisGASGFPILGL 167
|
|
| Sod_Fe_C |
pfam02777 |
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ... |
69-136 |
3.33e-29 |
|
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: 102.12 E-value: 3.33e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1686100022 69 PSAELAAAIDATFGSLEEFQAAFTAAATTRFGSGWAWLVVNKEGKLEVTSTANQDTPISEGKKPILGL 136
Cdd:pfam02777 1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTPLLGL 68
|
|
| Superox_dis_Halo |
NF041312 |
superoxide dismutase; |
1-136 |
1.75e-16 |
|
superoxide dismutase;
Pssm-ID: 469209 Cd Length: 196 Bit Score: 71.77 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100022 1 HHDKHHQTYVNNANAALEkhpEIGEDLEAllADVESIPADIRQaLINNGGGHLNHALFWELMTPEKTA-PSAELAAAIDA 79
Cdd:NF041312 24 HHDTHHQGYVNGLNSAEE---TLAENREA--GDFSSTAGAMRN-VTHNGSGHYLHTLFWENMSPNGGGePEGDLADRIEE 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1686100022 80 TFGSLEEFQAAFTAAATTrfGSGWAWLVVNKEGK-LEVTSTANQDTPISEGKKPILGL 136
Cdd:NF041312 98 DFGSYEAWKGEFEAAAGA--AGGWALLVYDPVAKqLRNVAVDKHDQGALWGSHPILAL 153
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| SodA |
COG0605 |
Superoxide dismutase [Inorganic ion transport and metabolism]; |
1-136 |
1.29e-63 |
|
Superoxide dismutase [Inorganic ion transport and metabolism];
Pssm-ID: 440370 [Multi-domain] Cd Length: 192 Bit Score: 192.27 E-value: 1.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100022 1 HHDKHHQTYVNNANAALEKHPEI-GEDLEALLADvesIPADIRQALINNGGGHLNHALFWELMTPE-KTAPSAELAAAID 78
Cdd:COG0605 24 HHDKHHQAYVNNLNAALEGLAELeDKSLEEIIKK---LSEELKRALRNNAGGHWNHTLFWENLSPNgGGEPTGELAAAIE 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1686100022 79 ATFGSLEEFQAAFTAAATTRFGSGWAWLVVNKEGKLEVTSTANQDTPISEGKKPILGL 136
Cdd:COG0605 101 ADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLGL 158
|
|
| PRK10925 |
PRK10925 |
superoxide dismutase [Mn]; |
1-136 |
1.34e-43 |
|
superoxide dismutase [Mn];
Pssm-ID: 182843 Cd Length: 206 Bit Score: 141.98 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100022 1 HHDKHHQTYVNNANAALEKHPEIGE-DLEALLADVESIPADIRQALINNGGGHLNHALFWELMTpEKTAPSAELAAAIDA 79
Cdd:PRK10925 27 HHTKHHQTYVNNANAALESLPEFANlPVEELITKLDQLPADKKTVLRNNAGGHANHSLFWKGLK-KGTTLQGDLKAAIER 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1686100022 80 TFGSLEEFQAAFTAAATTRFGSGWAWLVVnKEGKLEVTSTANQDTPI------SEGKKPILGL 136
Cdd:PRK10925 106 DFGSVDNFKAEFEKAAATRFGSGWAWLVL-KGDKLAVVSTANQDSPLmgeaisGASGFPILGL 167
|
|
| Sod_Fe_C |
pfam02777 |
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ... |
69-136 |
3.33e-29 |
|
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: 102.12 E-value: 3.33e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1686100022 69 PSAELAAAIDATFGSLEEFQAAFTAAATTRFGSGWAWLVVNKEGKLEVTSTANQDTPISEGKKPILGL 136
Cdd:pfam02777 1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTPLLGL 68
|
|
| PLN02471 |
PLN02471 |
superoxide dismutase [Mn] |
1-136 |
3.53e-26 |
|
superoxide dismutase [Mn]
Pssm-ID: 215262 Cd Length: 231 Bit Score: 98.06 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100022 1 HHDKHHQTYVNNANAALEKHPEIGEDLEAlladveSIPADIRQALINNGGGHLNHALFWELMTPEKTA----PSAELAAA 76
Cdd:PLN02471 55 HHQKHHQTYVTNYNKALEQLDQAVEKGDA------SAVVKLQSAIKFNGGGHVNHSIFWKNLAPVSEGggepPHGSLGWA 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1686100022 77 IDATFGSLEEFQAAFTAAATTRFGSGWAWLVVNKEG-KLEVTSTANQDTPISEGKK--PILGL 136
Cdd:PLN02471 129 IDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELkKLVVETTANQDPLVTKGPSlvPLLGI 191
|
|
| PRK10543 |
PRK10543 |
superoxide dismutase [Fe]; |
1-134 |
2.66e-25 |
|
superoxide dismutase [Fe];
Pssm-ID: 182534 Cd Length: 193 Bit Score: 94.63 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100022 1 HHDKHHQTYVNNANAALEKHPEIGEDLEALLADVESipadirqALINNGGGHLNHALFWELMTPEKTA-PSAELAAAIDA 79
Cdd:PRK10543 27 HYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSSEG-------GVFNNAAQVWNHTFYWNCLAPNAGGePTGKVAEAIAA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1686100022 80 TFGSLEEFQAAFTAAATTRFGSGWAWLVVNKEGKLEVTSTANQDTPISEGKKPIL 134
Cdd:PRK10543 100 SFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDATPLL 154
|
|
| PTZ00078 |
PTZ00078 |
Superoxide dismutase [Fe]; Provisional |
1-136 |
6.97e-23 |
|
Superoxide dismutase [Fe]; Provisional
Pssm-ID: 185432 [Multi-domain] Cd Length: 193 Bit Score: 88.69 E-value: 6.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100022 1 HHDKHHQTYVNNANAALEKHPEIGEDLEALLADVESipadirqALINNGGGHLNHALFWELMTPEKTA-PSAELAAAIDA 79
Cdd:PTZ00078 22 HYSKHHAGYVNKLNGLIKGTPLENKTLEELIKEYSG-------AVFNNAAQIWNHNFYWLSMGPNGGGePTGEIKEKIDE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1686100022 80 TFGSLEEFQAAFTAAATTRFGSGWAWLVVNKEGKLEVTSTANQDTPISEGK-KPILGL 136
Cdd:PTZ00078 95 KFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPIKDNTgKPLLTC 152
|
|
| Sod_Fe_N |
pfam00081 |
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ... |
1-63 |
4.99e-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: 78.12 E-value: 4.99e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1686100022 1 HHDKHHQTYVNNANAALEKHPEIGEDLEalladvESIPADIRQALINNGGGHLNHALFWELMT 63
Cdd:pfam00081 26 HHTKHHQTYVNNLNAALEGLEEARKPLE------ELIIKALLGGLFNNGGGHWNHSLFWKNLS 82
|
|
| PLN02685 |
PLN02685 |
iron superoxide dismutase |
1-131 |
5.74e-19 |
|
iron superoxide dismutase
Pssm-ID: 215369 Cd Length: 299 Bit Score: 80.43 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100022 1 HHDKHHQTYVNNANAALekhpeIGEDLEAL-LADVESIPADIRQAL--INNGGGHLNHALFWELMTPEKTA-PSAELAAA 76
Cdd:PLN02685 71 HWGKHHRAYVDNLNKQI-----VGTELDGMsLEDVVLITYNKGDMLpaFNNAAQAWNHEFFWESMKPGGGGkPSGELLQL 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1686100022 77 IDATFGSLEEFQAAFTAAATTRFGSGWAWLVVnKEGKLEVTSTANQdTPISEGKK 131
Cdd:PLN02685 146 IERDFGSFERFVEEFKSAAATQFGSGWAWLAY-KANRLDVGNAVNP-CPSEEDKK 198
|
|
| PLN02622 |
PLN02622 |
iron superoxide dismutase |
1-136 |
1.23e-17 |
|
iron superoxide dismutase
Pssm-ID: 166263 [Multi-domain] Cd Length: 261 Bit Score: 76.20 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100022 1 HHDKHHQTYVNNANAALEKHPEI-GEDLEALLA----DVESIPAdirqalINNGGGHLNHALFWELMTPEK-TAPSAELA 74
Cdd:PLN02622 72 HWGEHHRGYVEGLNKQLAKDDILyGYTMDELVKvtynNGNPLPE------FNNAAQVWNHDFFWESMQPGGgDMPELGVL 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1686100022 75 AAIDATFGSLEEFQAAFTAAATTRFGSGWAWLVVNK-EGKLEVTSTANQDTPISEGKKPILGL 136
Cdd:PLN02622 146 EQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKReERRLEVVKTSNAINPLVWDDIPIICL 208
|
|
| Superox_dis_Halo |
NF041312 |
superoxide dismutase; |
1-136 |
1.75e-16 |
|
superoxide dismutase;
Pssm-ID: 469209 Cd Length: 196 Bit Score: 71.77 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100022 1 HHDKHHQTYVNNANAALEkhpEIGEDLEAllADVESIPADIRQaLINNGGGHLNHALFWELMTPEKTA-PSAELAAAIDA 79
Cdd:NF041312 24 HHDTHHQGYVNGLNSAEE---TLAENREA--GDFSSTAGAMRN-VTHNGSGHYLHTLFWENMSPNGGGePEGDLADRIEE 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1686100022 80 TFGSLEEFQAAFTAAATTrfGSGWAWLVVNKEGK-LEVTSTANQDTPISEGKKPILGL 136
Cdd:NF041312 98 DFGSYEAWKGEFEAAAGA--AGGWALLVYDPVAKqLRNVAVDKHDQGALWGSHPILAL 153
|
|
| PLN02184 |
PLN02184 |
superoxide dismutase [Fe] |
1-134 |
2.36e-14 |
|
superoxide dismutase [Fe]
Pssm-ID: 177838 Cd Length: 212 Bit Score: 66.69 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100022 1 HHDKHHQTYVNNANAALEKHPEIGEDLEALLADV----ESIPAdirqalINNGGGHLNHALFWELMTPEKTA-PSAELAA 75
Cdd:PLN02184 35 HWGKHHRAYVDNLKKQVLGTELEGKPLEHIIHSTynngDLLPA------FNNAAQAWNHEFFWESMKPGGGGkPSGELLA 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1686100022 76 AIDATFGSLEEFQAAFTAAATTRFGSGWAWLVVNKEgKLEVTSTANQDTPISEGKKPIL 134
Cdd:PLN02184 109 LLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNE-KLKVVKTPNAVNPLVLGSFPLL 166
|
|
|