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Conserved domains on  [gi|32967607|ref|NP_002074|]
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glutathione peroxidase 2 [Homo sapiens]

Protein Classification

glutathione peroxidase (domain architecture ID 10085912)

glutathione peroxidase catalyzes the reduction of hydroperoxides using GSH as a specific electron donor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
7-182 6.04e-60

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


:

Pssm-ID: 238207  Cd Length: 152  Bit Score: 187.34  E-value: 6.04e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607   7 SFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTtRDFTQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEILNS 85
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYkDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607  86 LKYVrpgggYQPTFTLVQKCEVNGQNEHPVFAYLKDKLPYPYddpfslmtdpkliiwspvrRSDVAWNFEKFLIGPEGEP 165
Cdd:cd00340  80 CETN-----YGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLL-------------------GKDIKWNFTKFLVDRDGEV 135
                       170
                ....*....|....*..
gi 32967607 166 FRRYSRTFPTINIEPDI 182
Cdd:cd00340 136 VKRFAPTTDPEELEKDI 152
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
7-182 6.04e-60

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207  Cd Length: 152  Bit Score: 187.34  E-value: 6.04e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607   7 SFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTtRDFTQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEILNS 85
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYkDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607  86 LKYVrpgggYQPTFTLVQKCEVNGQNEHPVFAYLKDKLPYPYddpfslmtdpkliiwspvrRSDVAWNFEKFLIGPEGEP 165
Cdd:cd00340  80 CETN-----YGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLL-------------------GKDIKWNFTKFLVDRDGEV 135
                       170
                ....*....|....*..
gi 32967607 166 FRRYSRTFPTINIEPDI 182
Cdd:cd00340 136 VKRFAPTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
8-120 3.38e-55

Glutathione peroxidase;


Pssm-ID: 306714  Cd Length: 108  Bit Score: 173.69  E-value: 3.38e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607     8 FYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTrDFTQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEIlnsl 86
Cdd:pfam00255   1 IYDFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLNALQERLkPRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 32967607    87 KYVRPgGGYQPTFTLVQKCEVNGQNEHPVFAYLK 120
Cdd:pfam00255  76 KYFRP-GGYGVTFPLFSKIDVNGEKEHPVYKFLK 108
BtuE COG0386
Glutathione peroxidase, house-cleaning role in reducing lipid peroxides [Defense mechanisms, ...
7-186 2.06e-40

Glutathione peroxidase, house-cleaning role in reducing lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 223463  Cd Length: 162  Bit Score: 137.37  E-value: 2.06e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607   7 SFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTRdFTQLNELQCRFPRR-LVVLGFPCNQFGHQENCQNEEILN- 84
Cdd:COG0386   4 SIYDFSVKDIDGEPVSLSDYKGKVLLIVNTASKCGFTPQ-YEGLEALYKKYKDKgFEVLGFPCNQFGGQEPGSDEEIAKf 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607  85 -SLKyvrpgggYQPTFTLVQKCEVNGQNEHPVFAYLKDklpypyDDPFSLMTdpkliiwspvrrSDVAWNFEKFLIGPEG 163
Cdd:COG0386  83 cQLN-------YGVTFPMFSKIDVNGKNAHPLYKYLKE------QKPGKLGG------------KDIKWNFTKFLVDRDG 137
                       170       180
                ....*....|....*....|...
gi 32967607 164 EPFRRYSRTFPTINIEPDIKRLL 186
Cdd:COG0386 138 NVVKRFSPKTKPEDIELAIEKLL 160
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
5-187 8.40e-35

glutathione peroxidase; Provisional


Pssm-ID: 173495  Cd Length: 183  Bit Score: 123.33  E-value: 8.40e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607    5 AKSFYDLSAISLDGEKVDFNTFRGR-AVLIENVASLUGTTTRDFTQLNELQCRFPRR-LVVLGFPCNQFGHQENCQNEEI 82
Cdd:PTZ00256  17 TKSFFEFEAIDIDGQLVQLSKFKGKkAIIVVNVACKCGLTSDHYTQLVELYKQYKSQgLEILAFPCNQFMEQEPWDEPEI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607   83 LNslkYVRPGggYQPTFTLVQKCEVNGQNEHPVFAYLKdklpypyddpfslmTDPKLIIWSPVRRSDVAWNFEKFLIGPE 162
Cdd:PTZ00256  97 KE---YVQKK--FNVDFPLFQKIEVNGENTHEIYKYLR--------------RNSELFQNNTNEARQIPWNFAKFLIDGQ 157
                        170       180
                 ....*....|....*....|....*
gi 32967607  163 GEPFRRYSRTFPTINIEPDIKRLLK 187
Cdd:PTZ00256 158 GKVVKYFSPKVNPNEMIQDIEKLLN 182
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
7-186 5.54e-25

putative glutathione peroxidase Gpx7; This model represents one of several families of known and probable glutathione peroxidases. This family is restricted to animals and designated GPX7.


Pssm-ID: 131592  Cd Length: 153  Bit Score: 96.83  E-value: 5.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607     7 SFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTRDFTQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEILNS 85
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELgPSHFNVLAFPCNQFGESEPDSSKEIESF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607    86 LKyvrpgGGYQPTFTLVQKCEVNGQNEHPVFAYLKDklpypyddpfSLMTDPKliiwspvrrsdvaWNFEKFLIGPEGEP 165
Cdd:TIGR02540  81 AR-----RNYGVTFPMFSKIKILGSEAEPAFRFLVD----------SSKKEPR-------------WNFWKYLVNPEGQV 132
                         170       180
                  ....*....|....*....|.
gi 32967607   166 FRRYSRTFPTINIEPDIKRLL 186
Cdd:TIGR02540 133 VKFWRPEEPVEEIRPEITALV 153
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
7-182 6.04e-60

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207  Cd Length: 152  Bit Score: 187.34  E-value: 6.04e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607   7 SFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTtRDFTQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEILNS 85
Cdd:cd00340   1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYkDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607  86 LKYVrpgggYQPTFTLVQKCEVNGQNEHPVFAYLKDKLPYPYddpfslmtdpkliiwspvrRSDVAWNFEKFLIGPEGEP 165
Cdd:cd00340  80 CETN-----YGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLL-------------------GKDIKWNFTKFLVDRDGEV 135
                       170
                ....*....|....*..
gi 32967607 166 FRRYSRTFPTINIEPDI 182
Cdd:cd00340 136 VKRFAPTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
8-120 3.38e-55

Glutathione peroxidase;


Pssm-ID: 306714  Cd Length: 108  Bit Score: 173.69  E-value: 3.38e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607     8 FYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTrDFTQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEIlnsl 86
Cdd:pfam00255   1 IYDFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLNALQERLkPRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 32967607    87 KYVRPgGGYQPTFTLVQKCEVNGQNEHPVFAYLK 120
Cdd:pfam00255  76 KYFRP-GGYGVTFPLFSKIDVNGEKEHPVYKFLK 108
BtuE COG0386
Glutathione peroxidase, house-cleaning role in reducing lipid peroxides [Defense mechanisms, ...
7-186 2.06e-40

Glutathione peroxidase, house-cleaning role in reducing lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 223463  Cd Length: 162  Bit Score: 137.37  E-value: 2.06e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607   7 SFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTRdFTQLNELQCRFPRR-LVVLGFPCNQFGHQENCQNEEILN- 84
Cdd:COG0386   4 SIYDFSVKDIDGEPVSLSDYKGKVLLIVNTASKCGFTPQ-YEGLEALYKKYKDKgFEVLGFPCNQFGGQEPGSDEEIAKf 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607  85 -SLKyvrpgggYQPTFTLVQKCEVNGQNEHPVFAYLKDklpypyDDPFSLMTdpkliiwspvrrSDVAWNFEKFLIGPEG 163
Cdd:COG0386  83 cQLN-------YGVTFPMFSKIDVNGKNAHPLYKYLKE------QKPGKLGG------------KDIKWNFTKFLVDRDG 137
                       170       180
                ....*....|....*....|...
gi 32967607 164 EPFRRYSRTFPTINIEPDIKRLL 186
Cdd:COG0386 138 NVVKRFSPKTKPEDIELAIEKLL 160
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
5-187 8.40e-35

glutathione peroxidase; Provisional


Pssm-ID: 173495  Cd Length: 183  Bit Score: 123.33  E-value: 8.40e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607    5 AKSFYDLSAISLDGEKVDFNTFRGR-AVLIENVASLUGTTTRDFTQLNELQCRFPRR-LVVLGFPCNQFGHQENCQNEEI 82
Cdd:PTZ00256  17 TKSFFEFEAIDIDGQLVQLSKFKGKkAIIVVNVACKCGLTSDHYTQLVELYKQYKSQgLEILAFPCNQFMEQEPWDEPEI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607   83 LNslkYVRPGggYQPTFTLVQKCEVNGQNEHPVFAYLKdklpypyddpfslmTDPKLIIWSPVRRSDVAWNFEKFLIGPE 162
Cdd:PTZ00256  97 KE---YVQKK--FNVDFPLFQKIEVNGENTHEIYKYLR--------------RNSELFQNNTNEARQIPWNFAKFLIDGQ 157
                        170       180
                 ....*....|....*....|....*
gi 32967607  163 GEPFRRYSRTFPTINIEPDIKRLLK 187
Cdd:PTZ00256 158 GKVVKYFSPKVNPNEMIQDIEKLLN 182
PLN02412 PLN02412
probable glutathione peroxidase
6-186 1.17e-28

probable glutathione peroxidase


Pssm-ID: 166053  Cd Length: 167  Bit Score: 107.00  E-value: 1.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607    6 KSFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTRDFTQLNELQCRFPRR-LVVLGFPCNQFGHQENCQNEEILN 84
Cdd:PLN02412   7 KSIYDFTVKDIRGNDVSLSEYSGKVLLIVNVASKCGLTHSNYKELNVLYEKYKNQgFEILAFPCNQFLGQEPGSNEEIQE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607   85 SLKYVrpgggYQPTFTLVQKCEVNGQNEHPVFAYLKDKLPYPYDDPfslmtdpkliiwspvrrsdVAWNFEKFLIGPEGE 164
Cdd:PLN02412  87 TVCTM-----FKAEFPIFDKVDVNGKNTAPLYKYLKSEKGGLFGDA-------------------IKWNFTKFLVNKEGK 142
                        170       180
                 ....*....|....*....|..
gi 32967607  165 PFRRYSRTFPTINIEPDIKRLL 186
Cdd:PLN02412 143 VVERYAPTTSPLKIEKDIQNLL 164
btuE PRK10606
putative glutathione peroxidase; Provisional
7-170 2.79e-26

putative glutathione peroxidase; Provisional


Pssm-ID: 182585  Cd Length: 183  Bit Score: 101.00  E-value: 2.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607    7 SFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTRdFTQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEIlns 85
Cdd:PRK10606   4 SILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQ-YEQLENIQKAWaDQGFVVLGFPCNQFLGQEPGSDEEI--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607   86 LKYVRpgGGYQPTFTLVQKCEVNGQNEHPVFAYLKDKLPY---PYDDPFSLMTDPKLiiWSPVRRSDVAWNFEKFLIGPE 162
Cdd:PRK10606  80 KTYCR--TTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAPTavaPEESGFYARMVSKG--RAPLYPDDILWNFEKFLVGRD 155

                 ....*...
gi 32967607  163 GEPFRRYS 170
Cdd:PRK10606 156 GQVIQRFS 163
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
7-186 5.54e-25

putative glutathione peroxidase Gpx7; This model represents one of several families of known and probable glutathione peroxidases. This family is restricted to animals and designated GPX7.


Pssm-ID: 131592  Cd Length: 153  Bit Score: 96.83  E-value: 5.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607     7 SFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTRDFTQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEILNS 85
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELgPSHFNVLAFPCNQFGESEPDSSKEIESF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607    86 LKyvrpgGGYQPTFTLVQKCEVNGQNEHPVFAYLKDklpypyddpfSLMTDPKliiwspvrrsdvaWNFEKFLIGPEGEP 165
Cdd:TIGR02540  81 AR-----RNYGVTFPMFSKIKILGSEAEPAFRFLVD----------SSKKEPR-------------WNFWKYLVNPEGQV 132
                         170       180
                  ....*....|....*....|.
gi 32967607   166 FRRYSRTFPTINIEPDIKRLL 186
Cdd:TIGR02540 133 VKFWRPEEPVEEIRPEITALV 153
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
6-186 7.31e-25

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021  Cd Length: 236  Bit Score: 98.43  E-value: 7.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607    6 KSFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTRDFTQLNELQCRFPRR-LVVLGFPCNQFGHQENCQNEEILN 84
Cdd:PLN02399  77 KSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQgFEILAFPCNQFGGQEPGSNPEIKQ 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607   85 sLKYVRpgggYQPTFTLVQKCEVNGQNEHPVFAYLKDKLPYPYDDpfslmtdpkLIiwspvrrsdvAWNFEKFLIGPEGE 164
Cdd:PLN02399 157 -FACTR----FKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGD---------LI----------KWNFEKFLVDKNGK 212
                        170       180
                 ....*....|....*....|..
gi 32967607  165 PFRRYSRTFPTINIEPDIKRLL 186
Cdd:PLN02399 213 VVERYPPTTSPFQIEKDIQKLL 234
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
6-188 5.80e-24

glutathione peroxidase; Provisional


Pssm-ID: 240248  Cd Length: 199  Bit Score: 95.30  E-value: 5.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607    6 KSFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTRDFTQLNELQCRF-PRRLVVLGFPCNQFGHQENCQNEEIL- 83
Cdd:PTZ00056  17 KSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFnPLGLEILAFPTSQFLNQEFPNTKDIRk 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967607   84 ----NSLKYvrpgggyqPTFTLvqkCEVNGQNEHPVFAYLKDKLPYPYDDPFSLmtdpkliiwspvrrSDVAWNFEKFLI 159
Cdd:PTZ00056  97 fndkNKIKY--------NFFEP---IEVNGENTHELFKFLKANCDSMHDENGTL--------------KAIGWNFGKFLV 151
                        170       180       190
                 ....*....|....*....|....*....|
gi 32967607  160 GPEGEPFR-RYSRTFPtINIEPDIKRLLKV 188
Cdd:PTZ00056 152 NKSGNVVAyFSPRTEP-LELEKKIAELLGV 180
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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