|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02685 |
PLN02685 |
iron superoxide dismutase |
5-296 |
0e+00 |
|
iron superoxide dismutase
Pssm-ID: 215369 Cd Length: 299 Bit Score: 560.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 5 AVTATPSSLLYSPLLLPSQGPNRRMQWKrnGKRRLGTKVAVSGVITAGFELKPPPYPLDALEPHMSRETLDYHWGKHHKT 84
Cdd:PLN02685 1 AVTATPASLSLSPALLPSQGPSRRMQWK--GKRRTCTRKAVSGVITAKFELKPPPYPLDALEPHMSRETLEYHWGKHHRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 85 YVENLNKQILGTDLDALSLEEVVLLSYNKGNMLPAFNNAAQAWNHEFFWESIQPGGGGKPTGELLRLIERDFGSFEEFLE 164
Cdd:PLN02685 79 YVDNLNKQIVGTELDGMSLEDVVLITYNKGDMLPAFNNAAQAWNHEFFWESMKPGGGGKPSGELLQLIERDFGSFERFVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 165 RFKSAAASNFGSGWTWLAYKANRLDVANAVNPLPKEEDKKLVIVKTPNAVNPLVWDYS---------HAYYLDFENRRAE 235
Cdd:PLN02685 159 EFKSAAATQFGSGWAWLAYKANRLDVGNAVNPCPSEEDKKLVVVKSPNAVNPLVWDYSplltidvweHAYYLDFQNRRPD 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039019855 236 YINTFMEKLVSWETVSTRLESAIARAVQREQEGTETEDEENPDDEVPEVYLDSDIDVSEVD 296
Cdd:PLN02685 239 YISTFMEKLVSWEAVSARLESAKARAAQREQEETRTEDEEEPDSEAVEMYLDSDIDVSEVD 299
|
|
| SodA |
COG0605 |
Superoxide dismutase [Inorganic ion transport and metabolism]; |
54-253 |
3.50e-87 |
|
Superoxide dismutase [Inorganic ion transport and metabolism];
Pssm-ID: 440370 [Multi-domain] Cd Length: 192 Bit Score: 258.52 E-value: 3.50e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 54 ELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGT-DLDALSLEEVVLLSYNKGNMlPAFNNAAQAWNHEFF 132
Cdd:COG0605 1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLaELEDKSLEEIIKKLSEELKR-ALRNNAGGHWNHTLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 133 WESIQPGGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKAnrldvanavnplpkeeDKKLVIVKTPN 212
Cdd:COG0605 80 WENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDK----------------DGKLEIVSTPN 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039019855 213 AVNPLVWDYS---------HAYYLDFENRRAEYINTFMeKLVSWETVSTR 253
Cdd:COG0605 144 QDNPLMAGGTpllgldvweHAYYLDYQNRRPDYVDAFW-NVVNWDFVEKR 192
|
|
| Sod_Fe_C |
pfam02777 |
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ... |
144-253 |
1.08e-38 |
|
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: 131.78 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 144 PTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKAnrldvanavnplpkeeDKKLVIVKTPNAVNPLVWD--- 220
Cdd:pfam02777 1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP----------------DGKLEIVTTPNQDNPLTDGltp 64
|
90 100 110
....*....|....*....|....*....|....*....
gi 1039019855 221 ------YSHAYYLDFENRRAEYINTFMeKLVSWETVSTR 253
Cdd:pfam02777 65 llgldvWEHAYYLDYQNRRADYVKAFW-NVVNWDEVEKR 102
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02685 |
PLN02685 |
iron superoxide dismutase |
5-296 |
0e+00 |
|
iron superoxide dismutase
Pssm-ID: 215369 Cd Length: 299 Bit Score: 560.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 5 AVTATPSSLLYSPLLLPSQGPNRRMQWKrnGKRRLGTKVAVSGVITAGFELKPPPYPLDALEPHMSRETLDYHWGKHHKT 84
Cdd:PLN02685 1 AVTATPASLSLSPALLPSQGPSRRMQWK--GKRRTCTRKAVSGVITAKFELKPPPYPLDALEPHMSRETLEYHWGKHHRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 85 YVENLNKQILGTDLDALSLEEVVLLSYNKGNMLPAFNNAAQAWNHEFFWESIQPGGGGKPTGELLRLIERDFGSFEEFLE 164
Cdd:PLN02685 79 YVDNLNKQIVGTELDGMSLEDVVLITYNKGDMLPAFNNAAQAWNHEFFWESMKPGGGGKPSGELLQLIERDFGSFERFVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 165 RFKSAAASNFGSGWTWLAYKANRLDVANAVNPLPKEEDKKLVIVKTPNAVNPLVWDYS---------HAYYLDFENRRAE 235
Cdd:PLN02685 159 EFKSAAATQFGSGWAWLAYKANRLDVGNAVNPCPSEEDKKLVVVKSPNAVNPLVWDYSplltidvweHAYYLDFQNRRPD 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039019855 236 YINTFMEKLVSWETVSTRLESAIARAVQREQEGTETEDEENPDDEVPEVYLDSDIDVSEVD 296
Cdd:PLN02685 239 YISTFMEKLVSWEAVSARLESAKARAAQREQEETRTEDEEEPDSEAVEMYLDSDIDVSEVD 299
|
|
| PLN02184 |
PLN02184 |
superoxide dismutase [Fe] |
43-259 |
7.22e-95 |
|
superoxide dismutase [Fe]
Pssm-ID: 177838 Cd Length: 212 Bit Score: 278.94 E-value: 7.22e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 43 VAVSGVITAGFELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGTDLDALSLEEVVLLSYNKGNMLPAFNN 122
Cdd:PLN02184 1 MAASSAVTANYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTELEGKPLEHIIHSTYNNGDLLPAFNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 123 AAQAWNHEFFWESIQPGGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKanrldvanavnplpkeeD 202
Cdd:PLN02184 81 AAQAWNHEFFWESMKPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYS-----------------N 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039019855 203 KKLVIVKTPNAVNPLVWD---------YSHAYYLDFENRRAEYINTFMEKLVSWETVSTRLESAIA 259
Cdd:PLN02184 144 EKLKVVKTPNAVNPLVLGsfplltidvWEHAYYLDFQNRRPDYIKTFMTNLVSWEAVSARLEAAKA 209
|
|
| PLN02622 |
PLN02622 |
iron superoxide dismutase |
26-259 |
1.44e-87 |
|
iron superoxide dismutase
Pssm-ID: 166263 [Multi-domain] Cd Length: 261 Bit Score: 262.26 E-value: 1.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 26 NRRMQWKRNGKRRLGTKVAVSGvitagfeLKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGTD-LDALSLE 104
Cdd:PLN02622 28 NLRNKQRRRSLQRASKVVAYYG-------LKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAKDDiLYGYTMD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 105 EVVLLSYNKGNMLPAFNNAAQAWNHEFFWESIQPGGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYk 184
Cdd:PLN02622 101 ELVKVTYNNGNPLPEFNNAAQVWNHDFFWESMQPGGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVL- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 185 anrldvanavnplpKEEDKKLVIVKTPNAVNPLVWD---------YSHAYYLDFENRRAEYINTFMEKLVSWETVSTRLE 255
Cdd:PLN02622 180 --------------KREERRLEVVKTSNAINPLVWDdipiicldvWEHAYYLDYKNDRGKYVNAFMNHLVSWNAAMARMA 245
|
....
gi 1039019855 256 SAIA 259
Cdd:PLN02622 246 RAEA 249
|
|
| SodA |
COG0605 |
Superoxide dismutase [Inorganic ion transport and metabolism]; |
54-253 |
3.50e-87 |
|
Superoxide dismutase [Inorganic ion transport and metabolism];
Pssm-ID: 440370 [Multi-domain] Cd Length: 192 Bit Score: 258.52 E-value: 3.50e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 54 ELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGT-DLDALSLEEVVLLSYNKGNMlPAFNNAAQAWNHEFF 132
Cdd:COG0605 1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLaELEDKSLEEIIKKLSEELKR-ALRNNAGGHWNHTLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 133 WESIQPGGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKAnrldvanavnplpkeeDKKLVIVKTPN 212
Cdd:COG0605 80 WENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDK----------------DGKLEIVSTPN 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039019855 213 AVNPLVWDYS---------HAYYLDFENRRAEYINTFMeKLVSWETVSTR 253
Cdd:COG0605 144 QDNPLMAGGTpllgldvweHAYYLDYQNRRPDYVDAFW-NVVNWDFVEKR 192
|
|
| PRK10543 |
PRK10543 |
superoxide dismutase [Fe]; |
53-256 |
6.18e-62 |
|
superoxide dismutase [Fe];
Pssm-ID: 182534 Cd Length: 193 Bit Score: 194.40 E-value: 6.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 53 FELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGTDLDALSLEEVVLLSynKGNMlpaFNNAAQAWNHEFF 132
Cdd:PRK10543 3 FELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSS--EGGV---FNNAAQVWNHTFY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 133 WESIQPGGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAykanrldvanavnplpKEEDKKLVIVKTPN 212
Cdd:PRK10543 78 WNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLV----------------KNADGKLAIVSTSN 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039019855 213 AVNPL-----------VWDysHAYYLDFENRRAEYINTFMeKLVSWETVSTRLES 256
Cdd:PRK10543 142 AGTPLttdatplltvdVWE--HAYYIDYRNARPGYLEHFW-ALVNWEFVAKNLAA 193
|
|
| PTZ00078 |
PTZ00078 |
Superoxide dismutase [Fe]; Provisional |
59-257 |
6.08e-59 |
|
Superoxide dismutase [Fe]; Provisional
Pssm-ID: 185432 [Multi-domain] Cd Length: 193 Bit Score: 186.92 E-value: 6.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 59 PYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGTDLDALSLEEVVllsynKGNMLPAFNNAAQAWNHEFFWESIQP 138
Cdd:PTZ00078 4 PYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLENKTLEELI-----KEYSGAVFNNAAQIWNHNFYWLSMGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 139 GGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKanrldvanavnplpkeEDKKLVIVKTPNAVNPL- 217
Cdd:PTZ00078 79 NGGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLK----------------NDGKLEIVQTHDAGNPIk 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039019855 218 -----------VWDysHAYYLDFENRRAEYINTFMEKlVSWETVSTRLESA 257
Cdd:PTZ00078 143 dntgkplltcdIWE--HAYYIDYRNDRASYVNSWWNK-VNWDFANKNLKKL 190
|
|
| PRK10925 |
PRK10925 |
superoxide dismutase [Mn]; |
53-258 |
4.15e-40 |
|
superoxide dismutase [Mn];
Pssm-ID: 182843 Cd Length: 206 Bit Score: 138.90 E-value: 4.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 53 FELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILG-TDLDALSLEEVVllsyNKGNMLPA------FNNAAQ 125
Cdd:PRK10925 3 YTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESlPEFANLPVEELI----TKLDQLPAdkktvlRNNAGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 126 AWNHEFFWESIQPGGggKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKanrldvanavnplpkeeDKKL 205
Cdd:PRK10925 79 HANHSLFWKGLKKGT--TLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLK-----------------GDKL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 206 VIVKTPNAVNPL-----------------VWDysHAYYLDFENRRAEYINTFMEkLVSWETVSTRLESAI 258
Cdd:PRK10925 140 AVVSTANQDSPLmgeaisgasgfpilgldVWE--HAYYLKFQNRRPDYIKEFWN-VVNWDEAAARFAAKK 206
|
|
| Sod_Fe_C |
pfam02777 |
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ... |
144-253 |
1.08e-38 |
|
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: 131.78 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 144 PTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKAnrldvanavnplpkeeDKKLVIVKTPNAVNPLVWD--- 220
Cdd:pfam02777 1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDP----------------DGKLEIVTTPNQDNPLTDGltp 64
|
90 100 110
....*....|....*....|....*....|....*....
gi 1039019855 221 ------YSHAYYLDFENRRAEYINTFMeKLVSWETVSTR 253
Cdd:pfam02777 65 llgldvWEHAYYLDYQNRRADYVKAFW-NVVNWDEVEKR 102
|
|
| Sod_Fe_N |
pfam00081 |
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ... |
53-136 |
3.28e-27 |
|
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: 101.23 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 53 FELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGTDLDALSLEEVVLlsynKGNMLPAFNNAAQAWNHEFF 132
Cdd:pfam00081 2 YELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELII----KALLGGLFNNGGGHWNHSLF 77
|
....
gi 1039019855 133 WESI 136
Cdd:pfam00081 78 WKNL 81
|
|
| PLN02471 |
PLN02471 |
superoxide dismutase [Mn] |
35-251 |
1.64e-26 |
|
superoxide dismutase [Mn]
Pssm-ID: 215262 Cd Length: 231 Bit Score: 103.83 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 35 GKRRLGTKVAVSGVITagFELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQIlgTDLDAlSLEEVVLLSYNKG 114
Cdd:PLN02471 15 LKETSSRLLSFRGLQT--FTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKAL--EQLDQ-AVEKGDASAVVKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039019855 115 NMLPAFNNAAQAwNHEFFWESIQP---GGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAY--KANRLD 189
Cdd:PLN02471 90 QSAIKFNGGGHV-NHSIFWKNLAPvseGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLdkELKKLV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039019855 190 VANAVNPLPkeedkklVIVKTPNAVnPL----VWDysHAYYLDFENRRAEYINTFMeKLVSWETVS 251
Cdd:PLN02471 169 VETTANQDP-------LVTKGPSLV-PLlgidVWE--HAYYLQYKNVRPDYLKNIW-KVMNWKYAS 223
|
|
|