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Conserved domains on  [gi|40363251|gb|AAH50378|]
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Glutathione peroxidase 3 (plasma) [Homo sapiens]

Protein Classification

glutathione peroxidase( domain architecture ID 10085912)

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

CATH:  3.40.30.10
EC:  1.11.1.-
Gene Ontology:  GO:0043295|GO:0004602|GO:0006979
SCOP:  4000042

Graphical summary

 Zoom to residue level

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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 ...
39-211 9.45e-70

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 [Multi-domain]  Cd Length: 152  Bit Score: 210.06  E-value: 9.45e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251  39 TIYEYGALTIDGEEyIPFKQYAGKYVLFVNVASYUGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEILPT 118
Cdd:cd00340   1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251 119 LKYVRPgggfvPNFQLFEKGDVNGEKEQKFYTFLKNSCPptsellgtsdrlfwePMKVHDIRWNFEKFLVGPDGIPIMRW 198
Cdd:cd00340  80 CETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAP---------------GLLGKDIKWNFTKFLVDRDGEVVKRF 139
                       170
                ....*....|...
gi 40363251 199 HHRTTVSNVKMDI 211
Cdd:cd00340 140 APTTDPEELEKDI 152
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
39-211 9.45e-70

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 [Multi-domain]  Cd Length: 152  Bit Score: 210.06  E-value: 9.45e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251  39 TIYEYGALTIDGEEyIPFKQYAGKYVLFVNVASYUGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEILPT 118
Cdd:cd00340   1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251 119 LKYVRPgggfvPNFQLFEKGDVNGEKEQKFYTFLKNSCPptsellgtsdrlfwePMKVHDIRWNFEKFLVGPDGIPIMRW 198
Cdd:cd00340  80 CETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAP---------------GLLGKDIKWNFTKFLVDRDGEVVKRF 139
                       170
                ....*....|...
gi 40363251 199 HHRTTVSNVKMDI 211
Cdd:cd00340 140 APTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
40-153 1.98e-59

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 182.55  E-value: 1.98e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251    40 IYEYGALTIDGEeYIPFKQYAGKYVLFVNVASYUGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEIlptl 119
Cdd:pfam00255   1 IYEFSAKDIDGE-PVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 40363251   120 KYVRPgGGFVPNFQLFEKGDVNGEKEQKFYTFLK 153
Cdd:pfam00255  76 KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
39-203 1.50e-52

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 166.79  E-value: 1.50e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251  39 TIYEYGALTIDGEEyIPFKQYAGKYVLFVNVASYUGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEILP- 117
Cdd:COG0386   3 SIYDFSVTTLDGEP-VSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEf 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251 118 -TLKY-VrpgggfvpNFQLFEKGDVNGEKEQKFYTFLKNScppTSELLGTSdrlfwepmkvhDIRWNFEKFLVGPDGIPI 195
Cdd:COG0386  82 cSLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEE---APGLLGGG-----------DIKWNFTKFLIDRDGNVV 139

                ....*...
gi 40363251 196 MRWHHRTT 203
Cdd:COG0386 140 ARFAPTTK 147
btuE PRK10606
putative glutathione peroxidase; Provisional
36-198 5.27e-38

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 130.28  E-value: 5.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251   36 ISGTIYEYGALTIDGEEyIPFKQYAGKYVLFVNVASYUGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEI 115
Cdd:PRK10606   1 MQDSILTTVVTTIDGEV-TTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251  116 lptLKYVRpgGGFVPNFQLFEKGDVNGEKEQKFYTFLKNSCPptsELLGTSDRLFWE--------PMKVHDIRWNFEKFL 187
Cdd:PRK10606  80 ---KTYCR--TTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAP---TAVAPEESGFYArmvskgraPLYPDDILWNFEKFL 151
                        170
                 ....*....|.
gi 40363251  188 VGPDGIPIMRW 198
Cdd:PRK10606 152 VGRDGQVIQRF 162
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
41-213 5.67e-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 [Multi-domain]  Cd Length: 153  Bit Score: 95.67  E-value: 5.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251    41 YEYGALTIDGEeYIPFKQYAGKYVLFVNVASYUGLTGQ-YIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEIlptL 119
Cdd:TIGR02540   3 YSFEVKDARGR-TVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEI---E 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251   120 KYVRPGGGFvpNFQLFEKGDVNGEKEQKFYTFLKNSCPPtsellgtsdrlfwEPmkvhdiRWNFEKFLVGPDGIPIMRWH 199
Cdd:TIGR02540  79 SFARRNYGV--TFPMFSKIKILGSEAEPAFRFLVDSSKK-------------EP------RWNFWKYLVNPEGQVVKFWR 137
                         170
                  ....*....|....
gi 40363251   200 HRTTVSNVKMDILS 213
Cdd:TIGR02540 138 PEEPVEEIRPEITA 151
 
Name Accession Description Interval E-value
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
39-211 9.45e-70

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 [Multi-domain]  Cd Length: 152  Bit Score: 210.06  E-value: 9.45e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251  39 TIYEYGALTIDGEEyIPFKQYAGKYVLFVNVASYUGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEILPT 118
Cdd:cd00340   1 SIYDFSVKDIDGEP-VSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251 119 LKYVRPgggfvPNFQLFEKGDVNGEKEQKFYTFLKNSCPptsellgtsdrlfwePMKVHDIRWNFEKFLVGPDGIPIMRW 198
Cdd:cd00340  80 CETNYG-----VTFPMFAKIDVNGENAHPLYKYLKEEAP---------------GLLGKDIKWNFTKFLVDRDGEVVKRF 139
                       170
                ....*....|...
gi 40363251 199 HHRTTVSNVKMDI 211
Cdd:cd00340 140 APTTDPEELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
40-153 1.98e-59

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 182.55  E-value: 1.98e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251    40 IYEYGALTIDGEeYIPFKQYAGKYVLFVNVASYUGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEIlptl 119
Cdd:pfam00255   1 IYEFSAKDIDGE-PVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEI---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 40363251   120 KYVRPgGGFVPNFQLFEKGDVNGEKEQKFYTFLK 153
Cdd:pfam00255  76 KYFCP-GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
39-203 1.50e-52

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 166.79  E-value: 1.50e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251  39 TIYEYGALTIDGEEyIPFKQYAGKYVLFVNVASYUGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEILP- 117
Cdd:COG0386   3 SIYDFSVTTLDGEP-VSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEf 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251 118 -TLKY-VrpgggfvpNFQLFEKGDVNGEKEQKFYTFLKNScppTSELLGTSdrlfwepmkvhDIRWNFEKFLVGPDGIPI 195
Cdd:COG0386  82 cSLNYgV--------TFPMFAKIDVNGPNAHPLYKYLKEE---APGLLGGG-----------DIKWNFTKFLIDRDGNVV 139

                ....*...
gi 40363251 196 MRWHHRTT 203
Cdd:COG0386 140 ARFAPTTK 147
btuE PRK10606
putative glutathione peroxidase; Provisional
36-198 5.27e-38

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 130.28  E-value: 5.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251   36 ISGTIYEYGALTIDGEEyIPFKQYAGKYVLFVNVASYUGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEI 115
Cdd:PRK10606   1 MQDSILTTVVTTIDGEV-TTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251  116 lptLKYVRpgGGFVPNFQLFEKGDVNGEKEQKFYTFLKNSCPptsELLGTSDRLFWE--------PMKVHDIRWNFEKFL 187
Cdd:PRK10606  80 ---KTYCR--TTWGVTFPMFSKIEVNGEGRHPLYQKLIAAAP---TAVAPEESGFYArmvskgraPLYPDDILWNFEKFL 151
                        170
                 ....*....|.
gi 40363251  188 VGPDGIPIMRW 198
Cdd:PRK10606 152 VGRDGQVIQRF 162
PLN02412 PLN02412
probable glutathione peroxidase
39-222 1.23e-32

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 116.24  E-value: 1.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251   39 TIYEYGALTIDGEEyIPFKQYAGKYVLFVNVASYUGLT-GQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEILP 117
Cdd:PLN02412   8 SIYDFTVKDIGGND-VSLNQYKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251  118 TLKYVrpgggFVPNFQLFEKGDVNGEKEQKFYTFLKNScppTSELLGTSdrlfwepmkvhdIRWNFEKFLVGPDGIPIMR 197
Cdd:PLN02412  87 TVCTR-----FKAEFPIFDKVDVNGKNTAPLYKYLKAE---KGGLFGDA------------IKWNFTKFLVSKEGKVVQR 146
                        170       180
                 ....*....|....*....|....*
gi 40363251  198 WHHRTTVSNVKMDIlsymrrQAALG 222
Cdd:PLN02412 147 YAPTTSPLKIEKDI------QNLLG 165
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
39-212 5.56e-32

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 114.86  E-value: 5.56e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251   39 TIYEYGALTIDGEEyIPFKQYAGKYV-LFVNVASYUGLTGQ-YIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEIl 116
Cdd:PTZ00256  19 SFFEFEAIDIDGQL-VQLSKFKGKKAiIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEI- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251  117 ptLKYVRPggGFVPNFQLFEKGDVNGEKEQKFYTFLKNScpptSELLGTSDRlfwepmKVHDIRWNFEKFLVGPDGIPIM 196
Cdd:PTZ00256  97 --KEYVQK--KFNVDFPLFQKIEVNGENTHEIYKYLRRN----SELFQNNTN------EARQIPWNFAKFLIDGQGKVVK 162
                        170
                 ....*....|....*.
gi 40363251  197 RWHHRTTVSNVKMDIL 212
Cdd:PTZ00256 163 YFSPKVNPNEMIQDIE 178
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
39-211 4.21e-30

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 111.53  E-value: 4.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251   39 TIYEYGALTIDGEEyIPFKQYAGKYVLFVNVASYUGLTG-QYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEIlP 117
Cdd:PLN02399  78 SVHDFTVKDIDGKD-VALSKFKGKVLLIVNVASKCGLTSsNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEI-K 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251  118 TLKYVRpgggFVPNFQLFEKGDVNGEKEQKFYTFLKNScppTSELLGTSdrlfwepmkvhdIRWNFEKFLVGPDGIPIMR 197
Cdd:PLN02399 156 QFACTR----FKAEFPIFDKVDVNGPSTAPVYQFLKSN---AGGFLGDL------------IKWNFEKFLVDKNGKVVER 216
                        170
                 ....*....|....
gi 40363251  198 WHHRTTVSNVKMDI 211
Cdd:PLN02399 217 YPPTTSPFQIEKDI 230
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
41-213 5.67e-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 [Multi-domain]  Cd Length: 153  Bit Score: 95.67  E-value: 5.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251    41 YEYGALTIDGEeYIPFKQYAGKYVLFVNVASYUGLTGQ-YIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEIlptL 119
Cdd:TIGR02540   3 YSFEVKDARGR-TVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEI---E 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251   120 KYVRPGGGFvpNFQLFEKGDVNGEKEQKFYTFLKNSCPPtsellgtsdrlfwEPmkvhdiRWNFEKFLVGPDGIPIMRWH 199
Cdd:TIGR02540  79 SFARRNYGV--TFPMFSKIKILGSEAEPAFRFLVDSSKK-------------EP------RWNFWKYLVNPEGQVVKFWR 137
                         170
                  ....*....|....
gi 40363251   200 HRTTVSNVKMDILS 213
Cdd:TIGR02540 138 PEEPVEEIRPEITA 151
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
37-192 2.34e-23

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 92.99  E-value: 2.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40363251   37 SGTIYEYGALTIDGEEYiPFKQYAGKYVLFVNVASYUGLTGQYIE-LNALQEELAPFGLVILGFPCNQFGKQEpgensei 115
Cdd:PTZ00056  16 RKSIYDYTVKTLEGTTV-PMSSLKNKVLMITNSASKCGLTKKHVDqMNRLHSVFNPLGLEILAFPTSQFLNQE------- 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40363251  116 LPTLKYVRP-GGGFVPNFQLFEKGDVNGEKEQKFYTFLKNSCPptsellgtsdRLFWEPMKVHDIRWNFEKFLVGPDG 192
Cdd:PTZ00056  88 FPNTKDIRKfNDKNKIKYNFFEPIEVNGENTHELFKFLKANCD----------SMHDENGTLKAIGWNFGKFLVNKSG 155
 
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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