|
Name |
Accession |
Description |
Interval |
E-value |
| SodA |
COG0605 |
Superoxide dismutase [Inorganic ion transport and metabolism]; |
4-194 |
2.10e-102 |
|
Superoxide dismutase [Inorganic ion transport and metabolism];
Pssm-ID: 440370 [Multi-domain] Cd Length: 192 Bit Score: 293.19 E-value: 2.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 4 TLPELPYDYSALEPYISGEIMELHHDKHHKAYVDGANTALDKLAEARDKaDFGAI-----NKLEKDLAFNLAGHVNHSVF 78
Cdd:COG0605 1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDK-SLEEIikklsEELKRALRNNAGGHWNHTLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 79 WKNMAPKGSApeRPTDELGAAIDEFFGSFDNMKAQFTAAATGIQGSGWASLVWDPLGKRINTlQFYDHQNNLPAGSIPLL 158
Cdd:COG0605 80 WENLSPNGGG--EPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIV-STPNQDNPLMAGGTPLL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 5542132 159 QLDMWEHAFYLQYKNVKGDYVKSWWNVVNWDDVALR 194
Cdd:COG0605 157 GLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
|
|
| PLN02471 |
PLN02471 |
superoxide dismutase [Mn] |
3-188 |
7.49e-65 |
|
superoxide dismutase [Mn]
Pssm-ID: 215262 Cd Length: 231 Bit Score: 199.75 E-value: 7.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 3 YTLPELPYDYSALEPYISGEIMELHHDKHHKAYVDGANTALDKLAEARDKADFGAINKLEKDLAFNLAGHVNHSVFWKNM 82
Cdd:PLN02471 31 FTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFWKNL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 83 AP-KGSAPERPTDELGAAIDEFFGSFDNMKAQFTAAATGIQGSGWaslVWDPLGKRINTLQFYDHQNNLP-----AGSIP 156
Cdd:PLN02471 111 APvSEGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGW---VWLGLDKELKKLVVETTANQDPlvtkgPSLVP 187
|
170 180 190
....*....|....*....|....*....|..
gi 5542132 157 LLQLDMWEHAFYLQYKNVKGDYVKSWWNVVNW 188
Cdd:PLN02471 188 LLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNW 219
|
|
| Superox_dis_Halo |
NF041312 |
superoxide dismutase; |
5-198 |
9.26e-55 |
|
superoxide dismutase;
Pssm-ID: 469209 Cd Length: 196 Bit Score: 172.69 E-value: 9.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 5 LPELPYDYSALEPYISGEIMELHHDKHHKAYVDGANTALDKLAEARDKADFGAINKLEKDLAFNLAGHVNHSVFWKNMAP 84
Cdd:NF041312 2 LPPLPYDYDALEPHISEQVLTWHHDTHHQGYVNGLNSAEETLAENREAGDFSSTAGAMRNVTHNGSGHYLHTLFWENMSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 85 KGSApeRPTDELGAAIDEFFGSFDNMKAQFTAAATGiqGSGWASLVWDPLGKRINTLQFYDHQNNLPAGSIPLLQLDMWE 164
Cdd:NF041312 82 NGGG--EPEGDLADRIEEDFGSYEAWKGEFEAAAGA--AGGWALLVYDPVAKQLRNVAVDKHDQGALWGSHPILALDVWE 157
|
170 180 190
....*....|....*....|....*....|....
gi 5542132 165 HAFYLQYKNVKGDYVKSWWNVVNWDDVALRFSEA 198
Cdd:NF041312 158 HSYYYDYGPDRGSFVDAFFEVVDWDEVADEYETV 191
|
|
| Sod_Fe_C |
pfam02777 |
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ... |
92-194 |
1.23e-52 |
|
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: 164.14 E-value: 1.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 92 PTDELGAAIDEFFGSFDNMKAQFTAAATGIQGSGWASLVWDPLGKRINTlQFYDHQNNLPAGSIPLLQLDMWEHAFYLQY 171
Cdd:pfam02777 1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIV-TTPNQDNPLTDGLTPLLGLDVWEHAYYLDY 79
|
90 100
....*....|....*....|...
gi 5542132 172 KNVKGDYVKSWWNVVNWDDVALR 194
Cdd:pfam02777 80 QNRRADYVKAFWNVVNWDEVEKR 102
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| SodA |
COG0605 |
Superoxide dismutase [Inorganic ion transport and metabolism]; |
4-194 |
2.10e-102 |
|
Superoxide dismutase [Inorganic ion transport and metabolism];
Pssm-ID: 440370 [Multi-domain] Cd Length: 192 Bit Score: 293.19 E-value: 2.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 4 TLPELPYDYSALEPYISGEIMELHHDKHHKAYVDGANTALDKLAEARDKaDFGAI-----NKLEKDLAFNLAGHVNHSVF 78
Cdd:COG0605 1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDK-SLEEIikklsEELKRALRNNAGGHWNHTLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 79 WKNMAPKGSApeRPTDELGAAIDEFFGSFDNMKAQFTAAATGIQGSGWASLVWDPLGKRINTlQFYDHQNNLPAGSIPLL 158
Cdd:COG0605 80 WENLSPNGGG--EPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIV-STPNQDNPLMAGGTPLL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 5542132 159 QLDMWEHAFYLQYKNVKGDYVKSWWNVVNWDDVALR 194
Cdd:COG0605 157 GLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
|
|
| PLN02471 |
PLN02471 |
superoxide dismutase [Mn] |
3-188 |
7.49e-65 |
|
superoxide dismutase [Mn]
Pssm-ID: 215262 Cd Length: 231 Bit Score: 199.75 E-value: 7.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 3 YTLPELPYDYSALEPYISGEIMELHHDKHHKAYVDGANTALDKLAEARDKADFGAINKLEKDLAFNLAGHVNHSVFWKNM 82
Cdd:PLN02471 31 FTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVVKLQSAIKFNGGGHVNHSIFWKNL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 83 AP-KGSAPERPTDELGAAIDEFFGSFDNMKAQFTAAATGIQGSGWaslVWDPLGKRINTLQFYDHQNNLP-----AGSIP 156
Cdd:PLN02471 111 APvSEGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGW---VWLGLDKELKKLVVETTANQDPlvtkgPSLVP 187
|
170 180 190
....*....|....*....|....*....|..
gi 5542132 157 LLQLDMWEHAFYLQYKNVKGDYVKSWWNVVNW 188
Cdd:PLN02471 188 LLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNW 219
|
|
| Superox_dis_Halo |
NF041312 |
superoxide dismutase; |
5-198 |
9.26e-55 |
|
superoxide dismutase;
Pssm-ID: 469209 Cd Length: 196 Bit Score: 172.69 E-value: 9.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 5 LPELPYDYSALEPYISGEIMELHHDKHHKAYVDGANTALDKLAEARDKADFGAINKLEKDLAFNLAGHVNHSVFWKNMAP 84
Cdd:NF041312 2 LPPLPYDYDALEPHISEQVLTWHHDTHHQGYVNGLNSAEETLAENREAGDFSSTAGAMRNVTHNGSGHYLHTLFWENMSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 85 KGSApeRPTDELGAAIDEFFGSFDNMKAQFTAAATGiqGSGWASLVWDPLGKRINTLQFYDHQNNLPAGSIPLLQLDMWE 164
Cdd:NF041312 82 NGGG--EPEGDLADRIEEDFGSYEAWKGEFEAAAGA--AGGWALLVYDPVAKQLRNVAVDKHDQGALWGSHPILALDVWE 157
|
170 180 190
....*....|....*....|....*....|....
gi 5542132 165 HAFYLQYKNVKGDYVKSWWNVVNWDDVALRFSEA 198
Cdd:NF041312 158 HSYYYDYGPDRGSFVDAFFEVVDWDEVADEYETV 191
|
|
| Sod_Fe_C |
pfam02777 |
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ... |
92-194 |
1.23e-52 |
|
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: 164.14 E-value: 1.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 92 PTDELGAAIDEFFGSFDNMKAQFTAAATGIQGSGWASLVWDPLGKRINTlQFYDHQNNLPAGSIPLLQLDMWEHAFYLQY 171
Cdd:pfam02777 1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIV-TTPNQDNPLTDGLTPLLGLDVWEHAYYLDY 79
|
90 100
....*....|....*....|...
gi 5542132 172 KNVKGDYVKSWWNVVNWDDVALR 194
Cdd:pfam02777 80 QNRRADYVKAFWNVVNWDEVEKR 102
|
|
| PRK10925 |
PRK10925 |
superoxide dismutase [Mn]; |
3-199 |
3.10e-50 |
|
superoxide dismutase [Mn];
Pssm-ID: 182843 Cd Length: 206 Bit Score: 161.63 E-value: 3.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 3 YTLPELPYDYSALEPYISGEIMELHHDKHHKAYVDGANTALDKLAEARDKADFGAINKLEKDLA-------FNLAGHVNH 75
Cdd:PRK10925 3 YTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPAdkktvlrNNAGGHANH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 76 SVFWKNMApKGSAPERPtdeLGAAIDEFFGSFDNMKAQFTAAATGIQGSGWASLVWDplGKRINTLQFYDHQNNLPAGSI 155
Cdd:PRK10925 83 SLFWKGLK-KGTTLQGD---LKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLK--GDKLAVVSTANQDSPLMGEAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5542132 156 ------PLLQLDMWEHAFYLQYKNVKGDYVKSWWNVVNWDDVALRFSEAR 199
Cdd:PRK10925 157 sgasgfPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
|
|
| PTZ00078 |
PTZ00078 |
Superoxide dismutase [Fe]; Provisional |
6-198 |
6.33e-42 |
|
Superoxide dismutase [Fe]; Provisional
Pssm-ID: 185432 [Multi-domain] Cd Length: 193 Bit Score: 139.92 E-value: 6.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 6 PELPYDYSALEPYISGEIMELHHDKHHKAYVDGANTALDKLA------EARDKADFGAInklekdlaFNLAGHV-NHSVF 78
Cdd:PTZ00078 1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPlenktlEELIKEYSGAV--------FNNAAQIwNHNFY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 79 WKNMAPKGSApeRPTDELGAAIDEFFGSFDNMKAQFTAAATGIQGSGWASLVWDPLGKrINTLQFYDHQNNLPAGS-IPL 157
Cdd:PTZ00078 73 WLSMGPNGGG--EPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGK-LEIVQTHDAGNPIKDNTgKPL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 5542132 158 LQLDMWEHAFYLQYKNVKGDYVKSWWNVVNWDDVALRFSEA 198
Cdd:PTZ00078 150 LTCDIWEHAYYIDYRNDRASYVNSWWNKVNWDFANKNLKKL 190
|
|
| Sod_Fe_N |
pfam00081 |
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ... |
3-83 |
2.77e-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: 2.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 3 YTLPELPYDYSALEPYISGEIMELHHDKHHKAYVDGANTALDKLAEARDKADFGAINKLEKDLAFNLAGHVNHSVFWKNM 82
Cdd:pfam00081 2 YELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIKALLGGLFNNGGGHWNHSLFWKNL 81
|
.
gi 5542132 83 A 83
Cdd:pfam00081 82 S 82
|
|
| PLN02622 |
PLN02622 |
iron superoxide dismutase |
1-198 |
2.18e-40 |
|
iron superoxide dismutase
Pssm-ID: 166263 [Multi-domain] Cd Length: 261 Bit Score: 138.22 E-value: 2.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 1 AVYTLPELPYDYSALEPYISGEIMELHHDKHHKAYVDGANTALDK-------LAEARDKADFGAINKLEKdlaFNLAGHV 73
Cdd:PLN02622 46 AYYGLKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAKddilygyTMDELVKVTYNNGNPLPE---FNNAAQV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 74 -NHSVFWKNMAPKGSapERPTDELGAAIDEFFGSFDNMKAQFTAAATGIQGSGWASLVWDPLGKRINTLQFYDHQNNLPA 152
Cdd:PLN02622 123 wNHDFFWESMQPGGG--DMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREERRLEVVKTSNAINPLVW 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 5542132 153 GSIPLLQLDMWEHAFYLQYKNVKGDYVKSWWN-VVNWDDVALRFSEA 198
Cdd:PLN02622 201 DDIPIICLDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAMARMARA 247
|
|
| PRK10543 |
PRK10543 |
superoxide dismutase [Fe]; |
3-196 |
3.91e-38 |
|
superoxide dismutase [Fe];
Pssm-ID: 182534 Cd Length: 193 Bit Score: 130.07 E-value: 3.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 3 YTLPELPYDYSALEPYISGEIMELHHDKHHKAYVDGANTaLDKLAEARDKAdFGAINKLEKDLAFNLAGHV-NHSVFWKN 81
Cdd:PRK10543 3 FELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNN-LIKGTAFEGKS-LEEIVRSSEGGVFNNAAQVwNHTFYWNC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 82 MAPKGSApeRPTDELGAAIDEFFGSFDNMKAQFTAAATGIQGSGWASLVWDPLGKrINTLQFYDHQNNLPAGSIPLLQLD 161
Cdd:PRK10543 81 LAPNAGG--EPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGK-LAIVSTSNAGTPLTTDATPLLTVD 157
|
170 180 190
....*....|....*....|....*....|....*
gi 5542132 162 MWEHAFYLQYKNVKGDYVKSWWNVVNWDDVALRFS 196
Cdd:PRK10543 158 VWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLA 192
|
|
| PLN02685 |
PLN02685 |
iron superoxide dismutase |
1-199 |
2.41e-33 |
|
iron superoxide dismutase
Pssm-ID: 215369 Cd Length: 299 Bit Score: 120.88 E-value: 2.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 1 AVYTLPELPYDYSALEPYISGEIMELHHDKHHKAYVDGAN-----TALDKLaeARDKADFGAINKLEKDLAFNLAGHV-N 74
Cdd:PLN02685 45 AKFELKPPPYPLDALEPHMSRETLEYHWGKHHRAYVDNLNkqivgTELDGM--SLEDVVLITYNKGDMLPAFNNAAQAwN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 75 HSVFWKNMAPKGSApeRPTDELGAAIDEFFGSFDNMKAQFTAAATGIQGSGWASLVW-----------DPL----GKRIN 139
Cdd:PLN02685 123 HEFFWESMKPGGGG--KPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAYkanrldvgnavNPCpseeDKKLV 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5542132 140 TLQFYDHQNNLPAGSIPLLQLDMWEHAFYLQYKNVKGDYVKSWW-NVVNWDDVALRFSEAR 199
Cdd:PLN02685 201 VVKSPNAVNPLVWDYSPLLTIDVWEHAYYLDFQNRRPDYISTFMeKLVSWEAVSARLESAK 261
|
|
| PLN02184 |
PLN02184 |
superoxide dismutase [Fe] |
1-201 |
5.00e-31 |
|
superoxide dismutase [Fe]
Pssm-ID: 177838 Cd Length: 212 Bit Score: 112.53 E-value: 5.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 1 AVYTLPELPYDYSALEPYISGEIMELHHDKHHKAYVDG-ANTALDKLAEAR--DKADFGAINKLEKDLAFNLAGHV-NHS 76
Cdd:PLN02184 9 ANYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNlKKQVLGTELEGKplEHIIHSTYNNGDLLPAFNNAAQAwNHE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542132 77 VFWKNMAPKGSApeRPTDELGAAIDEFFGSFDNMKAQFTAAATGIQGSGWASLVWdpLGKRINTLQFYDHQNNLPAGSIP 156
Cdd:PLN02184 89 FFWESMKPGGGG--KPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAY--SNEKLKVVKTPNAVNPLVLGSFP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 5542132 157 LLQLDMWEHAFYLQYKNVKGDYVKSWW-NVVNWDDVALRFSEARVA 201
Cdd:PLN02184 165 LLTIDVWEHAYYLDFQNRRPDYIKTFMtNLVSWEAVSARLEAAKAA 210
|
|
|