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Conserved domains on  [gi|1098968499|gb|JAU27641|]
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Superoxide dismutase [Mn] 1, mitochondrial [Noccaea caerulescens]

Protein Classification

PLN02471 family protein( domain architecture ID 11476866)

PLN02471 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02471 PLN02471
superoxide dismutase [Mn]
1-229 2.55e-169

superoxide dismutase [Mn]


:

Pssm-ID: 215262  Cd Length: 231  Bit Score: 465.54  E-value: 2.55e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499   1 MAIRCVASRKTLAGLKETSSRLLGFRGIQTFTLPDLPYDYSALEPAISGEIMQIHHQKHHQTYVTNYNNALEQLDQAVNK 80
Cdd:PLN02471    1 MALRTLASRKTLGGLKETSSRLLSFRGLQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499  81 GDASTVVKLQSAIKFNGGGHVNHSIFWKNLAPVNEGGGEPPKGSLGSAIDTHFGSLEGLVKKMSAEGAAVQGSGWVWLGL 160
Cdd:PLN02471   81 GDASAVVKLQSAIKFNGGGHVNHSIFWKNLAPVSEGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1098968499 161 DKELKKLVVDTTANQDPLVTKGGSLVPLVGIDVWEHAYYLQYKNVRPDYLKNVWKVINWKYASEVYDKE 229
Cdd:PLN02471  161 DKELKKLVVETTANQDPLVTKGPSLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYEKE 229
 
Name Accession Description Interval E-value
PLN02471 PLN02471
superoxide dismutase [Mn]
1-229 2.55e-169

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 465.54  E-value: 2.55e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499   1 MAIRCVASRKTLAGLKETSSRLLGFRGIQTFTLPDLPYDYSALEPAISGEIMQIHHQKHHQTYVTNYNNALEQLDQAVNK 80
Cdd:PLN02471    1 MALRTLASRKTLGGLKETSSRLLSFRGLQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499  81 GDASTVVKLQSAIKFNGGGHVNHSIFWKNLAPVNEGGGEPPKGSLGSAIDTHFGSLEGLVKKMSAEGAAVQGSGWVWLGL 160
Cdd:PLN02471   81 GDASAVVKLQSAIKFNGGGHVNHSIFWKNLAPVSEGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1098968499 161 DKELKKLVVDTTANQDPLVTKGGSLVPLVGIDVWEHAYYLQYKNVRPDYLKNVWKVINWKYASEVYDKE 229
Cdd:PLN02471  161 DKELKKLVVETTANQDPLVTKGPSLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYEKE 229
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
32-224 5.62e-96

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 278.17  E-value: 5.62e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499  32 TLPDLPYDYSALEPAISGEIMQIHHQKHHQTYVTNYNNALEQLDQAVNKGDASTVVKLQSAIK----FNGGGHVNHSIFW 107
Cdd:COG0605     1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEIIKKLSEELKralrNNAGGHWNHTLFW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499 108 KNLAPvnEGGGEPPkGSLGSAIDTHFGSLEGLVKKMSAEGAAVQGSGWVWLGLDKElKKLVVDTTANQDPLVTKGGslVP 187
Cdd:COG0605    81 ENLSP--NGGGEPT-GELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDNPLMAGG--TP 154
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1098968499 188 LVGIDVWEHAYYLQYKNVRPDYLKNVWKVINWKYASE 224
Cdd:COG0605   155 LLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEK 191
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
121-224 3.19e-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: 3.19e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499 121 PKGSLGSAIDTHFGSLEGLVKKMSAEGAAVQGSGWVWLGLDKElKKLVVDTTANQDPLVTKGgsLVPLVGIDVWEHAYYL 200
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPD-GKLEIVTTPNQDNPLTDG--LTPLLGLDVWEHAYYL 77
                          90       100
                  ....*....|....*....|....
gi 1098968499 201 QYKNVRPDYLKNVWKVINWKYASE 224
Cdd:pfam02777  78 DYQNRRADYVKAFWNVVNWDEVEK 101
 
Name Accession Description Interval E-value
PLN02471 PLN02471
superoxide dismutase [Mn]
1-229 2.55e-169

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 465.54  E-value: 2.55e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499   1 MAIRCVASRKTLAGLKETSSRLLGFRGIQTFTLPDLPYDYSALEPAISGEIMQIHHQKHHQTYVTNYNNALEQLDQAVNK 80
Cdd:PLN02471    1 MALRTLASRKTLGGLKETSSRLLSFRGLQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499  81 GDASTVVKLQSAIKFNGGGHVNHSIFWKNLAPVNEGGGEPPKGSLGSAIDTHFGSLEGLVKKMSAEGAAVQGSGWVWLGL 160
Cdd:PLN02471   81 GDASAVVKLQSAIKFNGGGHVNHSIFWKNLAPVSEGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1098968499 161 DKELKKLVVDTTANQDPLVTKGGSLVPLVGIDVWEHAYYLQYKNVRPDYLKNVWKVINWKYASEVYDKE 229
Cdd:PLN02471  161 DKELKKLVVETTANQDPLVTKGPSLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYEKE 229
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
32-224 5.62e-96

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 278.17  E-value: 5.62e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499  32 TLPDLPYDYSALEPAISGEIMQIHHQKHHQTYVTNYNNALEQLDQAVNKGDASTVVKLQSAIK----FNGGGHVNHSIFW 107
Cdd:COG0605     1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEIIKKLSEELKralrNNAGGHWNHTLFW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499 108 KNLAPvnEGGGEPPkGSLGSAIDTHFGSLEGLVKKMSAEGAAVQGSGWVWLGLDKElKKLVVDTTANQDPLVTKGGslVP 187
Cdd:COG0605    81 ENLSP--NGGGEPT-GELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDNPLMAGG--TP 154
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1098968499 188 LVGIDVWEHAYYLQYKNVRPDYLKNVWKVINWKYASE 224
Cdd:COG0605   155 LLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEK 191
PRK10925 PRK10925
superoxide dismutase [Mn];
30-226 2.16e-61

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 191.29  E-value: 2.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499  30 TFTLPDLPYDYSALEPAISGEIMQIHHQKHHQTYVTNYNNALEQLDQAVNKGDASTVVKL-------QSAIKFNGGGHVN 102
Cdd:PRK10925    2 SYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLdqlpadkKTVLRNNAGGHAN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499 103 HSIFWKNLAPvneggGEPPKGSLGSAIDTHFGSLEGLVKKMSAEGAAVQGSGWVWLGLDKElkKLVVDTTANQD-PLVTK 181
Cdd:PRK10925   82 HSLFWKGLKK-----GTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGD--KLAVVSTANQDsPLMGE 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1098968499 182 ---GGSLVPLVGIDVWEHAYYLQYKNVRPDYLKNVWKVINWKYASEVY 226
Cdd:PRK10925  155 aisGASGFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARF 202
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
121-224 3.19e-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: 3.19e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499 121 PKGSLGSAIDTHFGSLEGLVKKMSAEGAAVQGSGWVWLGLDKElKKLVVDTTANQDPLVTKGgsLVPLVGIDVWEHAYYL 200
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPD-GKLEIVTTPNQDNPLTDG--LTPLLGLDVWEHAYYL 77
                          90       100
                  ....*....|....*....|....
gi 1098968499 201 QYKNVRPDYLKNVWKVINWKYASE 224
Cdd:pfam02777  78 DYQNRRADYVKAFWNVVNWDEVEK 101
PRK10543 PRK10543
superoxide dismutase [Fe];
30-224 6.20e-48

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 156.27  E-value: 6.20e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499  30 TFTLPDLPYDYSALEPAISGEIMQIHHQKHHQTYVTNYNNALEqlDQAVNKGDASTVVKLQSAIKFNGGGHV-NHSIFWK 108
Cdd:PRK10543    2 SFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIK--GTAFEGKSLEEIVRSSEGGVFNNAAQVwNHTFYWN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499 109 NLAPvnEGGGEPpKGSLGSAIDTHFGSLEGLVKKMSAEGAAVQGSGWVWLGLDKELKKLVVDTTANQDPLVTkggSLVPL 188
Cdd:PRK10543   80 CLAP--NAGGEP-TGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTT---DATPL 153
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1098968499 189 VGIDVWEHAYYLQYKNVRPDYLKNVWKVINWKYASE 224
Cdd:PRK10543  154 LTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAK 189
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
30-111 6.55e-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: 134.74  E-value: 6.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499  30 TFTLPDLPYDYSALEPAISGEIMQIHHQKHHQTYVTNYNNALEQLDQAVNKGDASTVVKLQSAIKFNGGGHVNHSIFWKN 109
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIKALLGGLFNNGGGHWNHSLFWKN 80

                  ..
gi 1098968499 110 LA 111
Cdd:pfam00081  81 LS 82
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
34-231 2.79e-39

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 134.15  E-value: 2.79e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499  34 PDLPYDYSALEPAISGEIMQIHHQKHHQTYVTNYNNALEQldQAVNKGDASTVVKLQSAIKFNGGGHV-NHSIFWKNLAP 112
Cdd:PTZ00078    1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKG--TPLENKTLEELIKEYSGAVFNNAAQIwNHNFYWLSMGP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499 113 vnEGGGEPpKGSLGSAIDTHFGSLEGLVKKMSAEGAAVQGSGWVWLGLDKELKKLVVDTTANQDPLvtKGGSLVPLVGID 192
Cdd:PTZ00078   79 --NGGGEP-TGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPI--KDNTGKPLLTCD 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1098968499 193 VWEHAYYLQYKNVRPDYLKNVWKVINWKYASEVYDKEFK 231
Cdd:PTZ00078  154 IWEHAYYIDYRNDRASYVNSWWNKVNWDFANKNLKKLMQ 192
PLN02685 PLN02685
iron superoxide dismutase
7-223 1.22e-38

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 135.51  E-value: 1.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499   7 ASRKTLAGLKETSSRLLGFRGIQT--FTLPDLPYDYSALEPAISGEIMQIHHQKHHQTYVTNYNNALE-------QLDQA 77
Cdd:PLN02685   21 PSRRMQWKGKRRTCTRKAVSGVITakFELKPPPYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQIVgteldgmSLEDV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499  78 V----NKGDASTVvklqsaikFNGGGHV-NHSIFWKNLAPvneGGGEPPKGSLGSAIDTHFGSLEGLVKKMSAEGAAVQG 152
Cdd:PLN02685  101 VlityNKGDMLPA--------FNNAAQAwNHEFFWESMKP---GGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499 153 SGWVWLG-----LD----------KELKKLVVDTTANQ-DPLVTkggSLVPLVGIDVWEHAYYLQYKNVRPDYLKN-VWK 215
Cdd:PLN02685  170 SGWAWLAykanrLDvgnavnpcpsEEDKKLVVVKSPNAvNPLVW---DYSPLLTIDVWEHAYYLDFQNRRPDYISTfMEK 246

                  ....*...
gi 1098968499 216 VINWKYAS 223
Cdd:PLN02685  247 LVSWEAVS 254
PLN02622 PLN02622
iron superoxide dismutase
17-222 1.83e-36

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 128.98  E-value: 1.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499  17 ETSSRLLGFRGIQTftlPdlPYDYSALEPAISGEIMQIHHQKHHQTYVTNYNNALEQ--------LDQAV----NKGDAS 84
Cdd:PLN02622   39 QRASKVVAYYGLKT---P--PYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAKddilygytMDELVkvtyNNGNPL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499  85 TvvklqsaiKFNGGGHV-NHSIFWKNLAPvneGGGEPPKGSLGSAIDTHFGSLEGLVKKMSAEGAAVQGSGWVWLGLDKE 163
Cdd:PLN02622  114 P--------EFNNAAQVwNHDFFWESMQP---GGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKRE 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098968499 164 LKKLVVDTTANQ-DPLVTKGgslVPLVGIDVWEHAYYLQYKNVRPDYLkNVW--KVINWKYA 222
Cdd:PLN02622  183 ERRLEVVKTSNAiNPLVWDD---IPIICLDVWEHAYYLDYKNDRGKYV-NAFmnHLVSWNAA 240
PLN02184 PLN02184
superoxide dismutase [Fe]
31-223 8.09e-29

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 107.91  E-value: 8.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499  31 FTLPDLPYDYSALEPAISGEIMQIHHQKHHQTYVTNYNNAL---EQLDQAVNKGDASTVVKLQSAIKFNGGGHV-NHSIF 106
Cdd:PLN02184   11 YVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVlgtELEGKPLEHIIHSTYNNGDLLPAFNNAAQAwNHEFF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098968499 107 WKNLAPvneGGGEPPKGSLGSAIDTHFGSLEGLVKKMSAEGAAVQGSGWVWLGLDKELKKlVVDTTANQDPLVTkgGSLv 186
Cdd:PLN02184   91 WESMKP---GGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEKLK-VVKTPNAVNPLVL--GSF- 163
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1098968499 187 PLVGIDVWEHAYYLQYKNVRPDYLKN-VWKVINWKYAS 223
Cdd:PLN02184  164 PLLTIDVWEHAYYLDFQNRRPDYIKTfMTNLVSWEAVS 201
 
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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