|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10543 |
PRK10543 |
superoxide dismutase [Fe]; |
1-193 |
5.26e-142 |
|
superoxide dismutase [Fe];
Pssm-ID: 182534 Cd Length: 193 Bit Score: 393.16 E-value: 5.26e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 1 MSFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGGVFNNAAQVWNHTFYWNC 80
Cdd:PRK10543 1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSSEGGVFNNAAQVWNHTFYWNC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWE 160
Cdd:PRK10543 81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDATPLLTVDVWE 160
|
170 180 190
....*....|....*....|....*....|...
gi 15831619 161 HAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
Cdd:PRK10543 161 HAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
|
|
| SodA |
COG0605 |
Superoxide dismutase [Inorganic ion transport and metabolism]; |
4-190 |
4.40e-122 |
|
Superoxide dismutase [Inorganic ion transport and metabolism];
Pssm-ID: 440370 [Multi-domain] Cd Length: 192 Bit Score: 342.49 E-value: 4.40e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 4 ELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTA-FEGKSLEEIIRSS----EGGVFNNAAQVWNHTFYW 78
Cdd:COG0605 1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAeLEDKSLEEIIKKLseelKRALRNNAGGHWNHTLFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 79 NCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDV 158
Cdd:COG0605 81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLGLDV 160
|
170 180 190
....*....|....*....|....*....|..
gi 15831619 159 WEHAYYIDYRNARPGYLEHFWALVNWEFVAKN 190
Cdd:COG0605 161 WEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
|
|
| Sod_Fe_C |
pfam02777 |
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ... |
89-190 |
2.21e-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: 183.40 E-value: 2.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 89 PTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWEHAYYIDYR 168
Cdd:pfam02777 1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQ 80
|
90 100
....*....|....*....|..
gi 15831619 169 NARPGYLEHFWALVNWEFVAKN 190
Cdd:pfam02777 81 NRRADYVKAFWNVVNWDEVEKR 102
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10543 |
PRK10543 |
superoxide dismutase [Fe]; |
1-193 |
5.26e-142 |
|
superoxide dismutase [Fe];
Pssm-ID: 182534 Cd Length: 193 Bit Score: 393.16 E-value: 5.26e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 1 MSFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGGVFNNAAQVWNHTFYWNC 80
Cdd:PRK10543 1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSSEGGVFNNAAQVWNHTFYWNC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWE 160
Cdd:PRK10543 81 LAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDATPLLTVDVWE 160
|
170 180 190
....*....|....*....|....*....|...
gi 15831619 161 HAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
Cdd:PRK10543 161 HAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
|
|
| SodA |
COG0605 |
Superoxide dismutase [Inorganic ion transport and metabolism]; |
4-190 |
4.40e-122 |
|
Superoxide dismutase [Inorganic ion transport and metabolism];
Pssm-ID: 440370 [Multi-domain] Cd Length: 192 Bit Score: 342.49 E-value: 4.40e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 4 ELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTA-FEGKSLEEIIRSS----EGGVFNNAAQVWNHTFYW 78
Cdd:COG0605 1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAeLEDKSLEEIIKKLseelKRALRNNAGGHWNHTLFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 79 NCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDV 158
Cdd:COG0605 81 ENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLGLDV 160
|
170 180 190
....*....|....*....|....*....|..
gi 15831619 159 WEHAYYIDYRNARPGYLEHFWALVNWEFVAKN 190
Cdd:COG0605 161 WEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
|
|
| PTZ00078 |
PTZ00078 |
Superoxide dismutase [Fe]; Provisional |
6-193 |
9.18e-93 |
|
Superoxide dismutase [Fe]; Provisional
Pssm-ID: 185432 [Multi-domain] Cd Length: 193 Bit Score: 268.58 E-value: 9.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 6 PALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGGVFNNAAQVWNHTFYWNCLAPNA 85
Cdd:PTZ00078 1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLENKTLEELIKEYSGAVFNNAAQIWNHNFYWLSMGPNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 86 GGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTD-ATPLLTVDVWEHAYY 164
Cdd:PTZ00078 81 GGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPIKDNtGKPLLTCDIWEHAYY 160
|
170 180
....*....|....*....|....*....
gi 15831619 165 IDYRNARPGYLEHFWALVNWEFVAKNLAA 193
Cdd:PTZ00078 161 IDYRNDRASYVNSWWNKVNWDFANKNLKK 189
|
|
| PLN02685 |
PLN02685 |
iron superoxide dismutase |
3-193 |
4.06e-75 |
|
iron superoxide dismutase
Pssm-ID: 215369 Cd Length: 299 Bit Score: 227.58 E-value: 4.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 3 FELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEII-----RSSEGGVFNNAAQVWNHTFY 77
Cdd:PLN02685 47 FELKPPPYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQIVGTELDGMSLEDVVlitynKGDMLPAFNNAAQAWNHEFF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 78 WNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLV----------------KNSDGKLAIVSTSN 141
Cdd:PLN02685 127 WESMKPGGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAykanrldvgnavnpcpSEEDKKLVVVKSPN 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15831619 142 AGTPLTTDATPLLTVDVWEHAYYIDYRNARPGYLEHFWA-LVNWEFVAKNLAA 193
Cdd:PLN02685 207 AVNPLVWDYSPLLTIDVWEHAYYLDFQNRRPDYISTFMEkLVSWEAVSARLES 259
|
|
| PLN02622 |
PLN02622 |
iron superoxide dismutase |
3-192 |
4.90e-61 |
|
iron superoxide dismutase
Pssm-ID: 166263 [Multi-domain] Cd Length: 261 Bit Score: 190.61 E-value: 4.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 3 FELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNN-LIKGTAFEGKSLEEIIRSSEGG-----VFNNAAQVWNHTF 76
Cdd:PLN02622 48 YGLKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKqLAKDDILYGYTMDELVKVTYNNgnplpEFNNAAQVWNHDF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 77 YWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLV-KNSDGKLAIVSTSNAGTPLTTDATPLLT 155
Cdd:PLN02622 128 FWESMQPGGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVlKREERRLEVVKTSNAINPLVWDDIPIIC 207
|
170 180 190
....*....|....*....|....*....|....*...
gi 15831619 156 VDVWEHAYYIDYRNARPGYLEHFWA-LVNWEFVAKNLA 192
Cdd:PLN02622 208 LDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAMARMA 245
|
|
| Sod_Fe_C |
pfam02777 |
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ... |
89-190 |
2.21e-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: 183.40 E-value: 2.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 89 PTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWEHAYYIDYR 168
Cdd:pfam02777 1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQ 80
|
90 100
....*....|....*....|..
gi 15831619 169 NARPGYLEHFWALVNWEFVAKN 190
Cdd:pfam02777 81 NRRADYVKAFWNVVNWDEVEKR 102
|
|
| PLN02184 |
PLN02184 |
superoxide dismutase [Fe] |
2-193 |
4.70e-58 |
|
superoxide dismutase [Fe]
Pssm-ID: 177838 Cd Length: 212 Bit Score: 181.48 E-value: 4.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 2 SFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGG-----VFNNAAQVWNHTF 76
Cdd:PLN02184 10 NYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTELEGKPLEHIIHSTYNNgdllpAFNNAAQAWNHEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 77 YWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDgKLAIVSTSNAGTPLTTDATPLLTV 156
Cdd:PLN02184 90 FWESMKPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNE-KLKVVKTPNAVNPLVLGSFPLLTI 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 15831619 157 DVWEHAYYIDYRNARPGYLEHFWA-LVNWEFVAKNLAA 193
Cdd:PLN02184 169 DVWEHAYYLDFQNRRPDYIKTFMTnLVSWEAVSARLEA 206
|
|
| PRK10925 |
PRK10925 |
superoxide dismutase [Mn]; |
1-193 |
2.95e-55 |
|
superoxide dismutase [Mn];
Pssm-ID: 182843 Cd Length: 206 Bit Score: 173.95 E-value: 2.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 1 MSFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKG-TAFEGKSLEEIIRS-------SEGGVFNNAAQVW 72
Cdd:PRK10925 1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESlPEFANLPVEELITKldqlpadKKTVLRNNAGGHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 73 NHTFYWNCLapNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDgKLAIVSTSNAGTPLTTDAT- 151
Cdd:PRK10925 81 NHSLFWKGL--KKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGD-KLAVVSTANQDSPLMGEAIs 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15831619 152 -----PLLTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA 193
Cdd:PRK10925 158 gasgfPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAA 204
|
|
| PLN02471 |
PLN02471 |
superoxide dismutase [Mn] |
2-186 |
2.24e-43 |
|
superoxide dismutase [Mn]
Pssm-ID: 215262 Cd Length: 231 Bit Score: 144.67 E-value: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 2 SFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIK--GTAFEGKSLEEIIRSSEGGVFNNAAQVwNHTFYWN 79
Cdd:PLN02471 30 TFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEqlDQAVEKGDASAVVKLQSAIKFNGGGHV-NHSIFWK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 80 CLAP--NAGGE-PTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDA---TPL 153
Cdd:PLN02471 109 NLAPvsEGGGEpPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQDPLVTKGpslVPL 188
|
170 180 190
....*....|....*....|....*....|...
gi 15831619 154 LTVDVWEHAYYIDYRNARPGYLEHFWALVNWEF 186
Cdd:PLN02471 189 LGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKY 221
|
|
| Sod_Fe_N |
pfam00081 |
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ... |
2-82 |
2.12e-41 |
|
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: 134.36 E-value: 2.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831619 2 SFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEII-RSSEGGVFNNAAQVWNHTFYWNC 80
Cdd:pfam00081 1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIiKALLGGLFNNGGGHWNHSLFWKN 80
|
..
gi 15831619 81 LA 82
Cdd:pfam00081 81 LS 82
|
|
|