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Conserved domains on  [gi|534751162|gb|EQP04073|]
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L-ribulose-5-phosphate 4-epimerase SgbE [Escherichia coli HVH 53 (4-0631051)]

Protein Classification

L-ribulose-5-phosphate 4-epimerase( domain architecture ID 10793637)

L-ribulose-5-phosphate 4-epimerase catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond cleavage analogous to a class II aldolase reaction)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-231 9.04e-177

L-ribulose-5-phosphate 4-epimerase; Reviewed


:

Pssm-ID: 183459  Cd Length: 231  Bit Score: 484.32  E-value: 9.04e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   1 MLEQLKADVLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIATGKVVEGRKKPSSDTPTH 80
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  81 LALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRQMTAEEINGEYEYQTGEVIIKTFEERGLNP 160
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 534751162 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPAMQNELLDKHYLRKHGTNAYYGQ 231
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ 231
 
Name Accession Description Interval E-value
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-231 9.04e-177

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183459  Cd Length: 231  Bit Score: 484.32  E-value: 9.04e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   1 MLEQLKADVLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIATGKVVEGRKKPSSDTPTH 80
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  81 LALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRQMTAEEINGEYEYQTGEVIIKTFEERGLNP 160
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 534751162 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPAMQNELLDKHYLRKHGTNAYYGQ 231
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ 231
araD TIGR00760
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ...
 1-231 6.04e-166

L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very close homologs of araD, the established L-ribulose-5-phosphate 4-epimerase of E. coli. SgbE, part of an operon for L-xylulose metabolism, also has L-ribulose-5-phosphate 4-epimerase activity; L-xylulose-5-phosphate may be converted into L-ribulose-5-phosphate by another product of that operon. The homolog to this family from Mycobacterium smegmatis is flanked by putative araB and araA genes, consistent with it also being araD. [Energy metabolism, Sugars]


Pssm-ID: 129843  Cd Length: 231  Bit Score: 456.98  E-value: 6.04e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162    1 MLEQLKADVLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIATGKVVEGRKKPSSDTPTH 80
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   81 LALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRQMTAEEINGEYEYQTGEVIIKTFEERGLNP 160
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 534751162  161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPAMQNELLDKHYLRKHGTNAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 3-223 1.06e-95

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


Pssm-ID: 238232 [Multi-domain]  Cd Length: 209  Bit Score: 278.48  E-value: 1.06e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   3 EQLKADVLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIAtGKVVEGrKKPSSDTPTHLA 82
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  83 LYRRYAEIGGIVHTHSRHATIWSQAGL-DLPAWGTTHADYFYGAIPCTRQMTAEeingeyeyqTGEVIIKTFEERGlnPA 161
Cdd:cd00398   79 LYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQRALG--FP 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 534751162 162 QIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPAMQNELLDKHYLRKH 223
Cdd:cd00398  148 NSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-224 2.16e-65

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 201.21  E-value: 2.16e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   1 MLEQLKADVLAANLALPVHHLVTFTWGNVSA-VDETRqwMVIKPSGVEYNVMTADDMVVVEIAtGKVVEGRKKPSSDTPT 79
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVrLDDDR--FLITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  80 HLALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRQMTA--EEIngeyeyqtGEVIIKTFEERg 157
Cdd:COG0235   79 HLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPgtEEL--------AEAIAEALGDR- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 534751162 158 lnpaqiPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPaMQNELLDKHYlRKHG 224
Cdd:COG0235  150 ------PAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV-LSDEEIDKLA-RKFG 208
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 7-196 3.87e-57

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 179.28  E-value: 3.87e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162    7 ADVLAANLALPVHHLVTFTWGNVSAVDETRQwMVIKPSGVEYNVMTADDMVVVEIAtGKVVEGRKKPSSDTPTHLALYRR 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGDG-FLITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   87 YAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRQMTAEEIngeyeyQTGEVIIKTFEERglnpaqIPAV 166
Cdd:pfam00596  79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALGGD------RKAV 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 534751162  167 LVHSHGPFAWGKNAADAVHNAVVLEECAYM 196
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEI 176
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-196 4.40e-56

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 176.67  E-value: 4.40e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162     9 VLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIATGKVVEG-RKKPSSDTPTHLALYRRY 87
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGgGPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162    88 AEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGA-IPCTRQMTAEEINGEYEYQTGEVIIKTFEERglnpaqiPAV 166
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGGeIPYAPYAGPGTELAEEGAELAEALAEALPDR-------PAV 153

                          170       180       190
                   ....*....|....*....|....*....|
gi 534751162   167 LVHSHGPFAWGKNAADAVHNAVVLEECAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
 
Name Accession Description Interval E-value
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-231 9.04e-177

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183459  Cd Length: 231  Bit Score: 484.32  E-value: 9.04e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   1 MLEQLKADVLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIATGKVVEGRKKPSSDTPTH 80
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  81 LALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRQMTAEEINGEYEYQTGEVIIKTFEERGLNP 160
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 534751162 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPAMQNELLDKHYLRKHGTNAYYGQ 231
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ 231
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
1-231 5.04e-168

L-ribulose-5-phosphate 4-epimerase AraD;


Pssm-ID: 236181  Cd Length: 231  Bit Score: 462.00  E-value: 5.04e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   1 MLEQLKADVLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIAtGKVVEGRKKPSSDTPTH 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLE-GNVVEGKLKPSSDTPTH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  81 LALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRQMTAEEINGEYEYQTGEVIIKTFEERGLNP 160
Cdd:PRK08193  80 LVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 534751162 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPAMQNELLDKHYLRKHGTNAYYGQ 231
Cdd:PRK08193 160 AAVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQQTLLDKHYLRKHGKNAYYGQ 230
araD TIGR00760
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ...
 1-231 6.04e-166

L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very close homologs of araD, the established L-ribulose-5-phosphate 4-epimerase of E. coli. SgbE, part of an operon for L-xylulose metabolism, also has L-ribulose-5-phosphate 4-epimerase activity; L-xylulose-5-phosphate may be converted into L-ribulose-5-phosphate by another product of that operon. The homolog to this family from Mycobacterium smegmatis is flanked by putative araB and araA genes, consistent with it also being araD. [Energy metabolism, Sugars]


Pssm-ID: 129843  Cd Length: 231  Bit Score: 456.98  E-value: 6.04e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162    1 MLEQLKADVLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIATGKVVEGRKKPSSDTPTH 80
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   81 LALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRQMTAEEINGEYEYQTGEVIIKTFEERGLNP 160
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 534751162  161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPAMQNELLDKHYLRKHGTNAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-231 1.50e-128

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 106181  Cd Length: 231  Bit Score: 362.51  E-value: 1.50e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   1 MLEQLKADVLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIATGKVVEGRKKPSSDTPTH 80
Cdd:PRK13213   1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLATGKVVEGDKKPSSDTDTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  81 LALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRQMTAEEINGEYEYQTGEVIIKTFEERGLNP 160
Cdd:PRK13213  81 LVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGDYEHETGKVIVETFAEQGLRA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 534751162 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPAMQNELLDKHYLRKHGTNAYYGQ 231
Cdd:PRK13213 161 ADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGVGDMQQTLLDKHYLRKHGAAAYYGQ 231
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 2-231 9.16e-123

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183460  Cd Length: 228  Bit Score: 347.56  E-value: 9.16e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   2 LEQLKADVLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIaTGKVVEGRKKPSSDTPTHL 81
Cdd:PRK12348   1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDM-SGKVVEGEYRPSSDTATHL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  82 ALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRQMTAEEINGEYEYQTGEVIIKTFEERglNPA 161
Cdd:PRK12348  80 ELYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGNA--EPL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162 162 QIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPAMQNELLDKHYLRKHGTNAYYGQ 231
Cdd:PRK12348 158 HTPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGINPQLNHIDSYLMNKHFMRKHGPNAYYGQ 227
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 1-231 1.51e-111

L-ribulose-5-phosphate 4-epimerase; Provisional


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 319.47  E-value: 1.51e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   1 MLEQLKADVLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIaTGKVVEGRKKPSSDTPTH 80
Cdd:PRK13145   2 NLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDL-DGNVVEGDLNPSSDLPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  81 LALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRQMTAEEINGEYEYQTGEVIIKTFEERGLNP 160
Cdd:PRK13145  81 VELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGAYEKETGSVIIEEFEKRGLDP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 534751162 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPAMQNELLDKHYLRKHGTNAYYGQ 231
Cdd:PRK13145 161 MAVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQINPRVEPAPQYIMDKHYLRKHGPNAYYGQ 231
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 3-223 1.06e-95

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


Pssm-ID: 238232 [Multi-domain]  Cd Length: 209  Bit Score: 278.48  E-value: 1.06e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   3 EQLKADVLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIAtGKVVEGrKKPSSDTPTHLA 82
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  83 LYRRYAEIGGIVHTHSRHATIWSQAGL-DLPAWGTTHADYFYGAIPCTRQMTAEeingeyeyqTGEVIIKTFEERGlnPA 161
Cdd:cd00398   79 LYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQRALG--FP 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 534751162 162 QIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPAMQNELLDKHYLRKH 223
Cdd:cd00398  148 NSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-224 2.16e-65

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 201.21  E-value: 2.16e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   1 MLEQLKADVLAANLALPVHHLVTFTWGNVSA-VDETRqwMVIKPSGVEYNVMTADDMVVVEIAtGKVVEGRKKPSSDTPT 79
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVrLDDDR--FLITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  80 HLALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRQMTA--EEIngeyeyqtGEVIIKTFEERg 157
Cdd:COG0235   79 HLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPgtEEL--------AEAIAEALGDR- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 534751162 158 lnpaqiPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPaMQNELLDKHYlRKHG 224
Cdd:COG0235  150 ------PAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV-LSDEEIDKLA-RKFG 208
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 1-231 3.17e-63

L-ribulose-5-phosphate 4-epimerase; Validated


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 196.38  E-value: 3.17e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   1 MLEQLKADVLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIaTGKVVEGRKKPSSDTPTH 80
Cdd:PRK06557   7 MVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDL-DGNVVEGDLKPSSDTASH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  81 LALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCT--RQMTAEEIngeyeyqtGEVIIKTfeergL 158
Cdd:PRK06557  86 LYVYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVGpfALIGDEAI--------GKGIVET-----L 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 534751162 159 NPAQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQLPAMQNElLDKHYLRKHGTnayYGQ 231
Cdd:PRK06557 153 KGGRSPAVLMQNHGVFTIGKDAEDAVKAAVMVEEVARTVHIARQLGEPIPIPQEE-IDRLYDRYQNV---YGQ 221
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 7-196 3.87e-57

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 179.28  E-value: 3.87e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162    7 ADVLAANLALPVHHLVTFTWGNVSAVDETRQwMVIKPSGVEYNVMTADDMVVVEIAtGKVVEGRKKPSSDTPTHLALYRR 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGDG-FLITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   87 YAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRQMTAEEIngeyeyQTGEVIIKTFEERglnpaqIPAV 166
Cdd:pfam00596  79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALGGD------RKAV 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 534751162  167 LVHSHGPFAWGKNAADAVHNAVVLEECAYM 196
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEI 176
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-196 4.40e-56

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 176.67  E-value: 4.40e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162     9 VLAANLALPVHHLVTFTWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIATGKVVEG-RKKPSSDTPTHLALYRRY 87
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGgGPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162    88 AEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGA-IPCTRQMTAEEINGEYEYQTGEVIIKTFEERglnpaqiPAV 166
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGGeIPYAPYAGPGTELAEEGAELAEALAEALPDR-------PAV 153

                          170       180       190
                   ....*....|....*....|....*....|
gi 534751162   167 LVHSHGPFAWGKNAADAVHNAVVLEECAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
25-194 7.27e-22

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 89.42  E-value: 7.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  25 TWGNVSAVDETRQWMVIKPSGVEYNVMTADDMVVVEIaTGKVVEGRKKPSSDTPTHLALYRRYAEIGGIVHTHSRHATIW 104
Cdd:PRK06833  26 TGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDL-DGKVVEGERKPSSELDMHLIFYRNREDINAIVHTHSPYATTL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162 105 SQAGLDLPAwgTTHADYFYGA-IPCTRQMTaeeingeyeYQTGEVIIKTFEerGLNPAQipAVLVHSHGPFAWGKNAADA 183
Cdd:PRK06833 105 ACLGWELPA--VHYLIAVAGPnVRCAEYAT---------FGTKELAENAFE--AMEDRR--AVLLANHGLLAGANNLKNA 169

                        170
                 ....*....|.
gi 534751162 184 VHNAVVLEECA 194
Cdd:PRK06833 170 FNIAEEIEFCA 180
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 9-194 2.03e-16

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 75.06  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162   9 VLAANLALPVHHLVTFTWGNVSAVDETRQwMVIKPSGVEYNVMTADDMVVVEiATGKVVEGR--KKPSSDTPTHLALYRR 86
Cdd:PRK05874  11 VLAAAKDMLRRGLVEGTAGNISARRSDGN-VVITPSSVDYAEMLLHDLVLVD-AGGAVLHAKdgRSPSTELNLHLACYRA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  87 YAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTrqmtaeEINGEYEYQTGEVIIKTFEERGlnpaqipAV 166
Cdd:PRK05874  89 FDDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRCT------EYAASGTPEVGRNAVRALEGRA-------AA 155

                        170       180
                 ....*....|....*....|....*...
gi 534751162 167 LVHSHGPFAWGKNAADAVHNAVVLEECA 194
Cdd:PRK05874 156 LIANHGLVAVGPRPDQVLRVTALVERTA 183
PRK08130 PRK08130
putative aldolase; Validated
 27-206 1.48e-13

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 67.21  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  27 GNVSAVDETRQWMvIKPSGVEYNVMTADDMVVVEiATGKVVEGrKKPSSDTPTHLALYRRYAEIGGIVHTHSRHATIWS- 105
Cdd:PRK08130  28 GNISARLDDGGWL-VTPTGSCLGRLDPARLSKVD-ADGNWLSG-DKPSKEVPLHRAIYRNNPECGAVVHLHSTHLTALSc 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162 106 QAGLD----LPAWgtthADYFY---GAIPCTRQM------TAEEIngeyeyqtgeviiktfeeRGLNPaQIPAVLVHSHG 172
Cdd:PRK08130 105 LGGLDptnvLPPF----TPYYVmrvGHVPLIPYYrpgdpaIAEAL------------------AGLAA-RYRAVLLANHG 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 534751162 173 PFAWGKNAADAVHNAVVLEECAYMGLFSHQLAPQ 206
Cdd:PRK08130 162 PVVWGSSLEAAVNATEELEETAKLILLLGGRPPR 195
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
25-105 9.07e-13

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 64.57  E-value: 9.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  25 TWGNVSA-VDETRQWmvIKPSGVEYNVMTADDMVVVEIATGKVVEGRKkPSSDTPTHLALYRRYAEIGGIVHTHSRHATI 103
Cdd:PRK09220  26 TSGNMSVrLDEQHCA--ITVSGKDKGSLTAEDFLQVDIAGNAVPSGRK-PSAETLLHTQLYRLFPEIGAVLHTHSVNATV 102


                 ..
gi 534751162 104 WS 105
Cdd:PRK09220 103 LS 104
PRK08660 PRK08660
aldolase;
19-193 4.39e-11

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 59.59  E-value: 4.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  19 HHLVTFTWGNVSAVDETRqwMVIKPSGVEYNVMTADDMVVVEI-ATGKVVegrKKPSSDTPTHLALYRRyAEIGGIVHTH 97
Cdd:PRK08660  15 HGLVSSHFGNISVRTGDG--LLITRTGSMLDEITEGDVIEVGIdDDGSVD---PLASSETPVHRAIYRR-TSAKAIVHAH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  98 SRHATIWS-QAGLDLPAWGTTHadYFYGAIPCTRQMTAEEingeyeyQTGEVIIKTFEERGlnpaqipAVLVHSHGPFAW 176
Cdd:PRK08660  89 PPYAVALSlLEDEIVPLDSEGL--YFLGTIPVVGGDIGSG-------ELAENVARALSEHK-------GVVVRGHGTFAI 152

                        170
                 ....*....|....*..
gi 534751162 177 GKNAADAVHNAVVLEEC 193
Cdd:PRK08660 153 GKTLEEAYIYTSQLEHS 169
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
25-128 1.25e-10

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 58.98  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  25 TWGNVSAvdETRQWMVIKPSGVEYNVMTADDMVVVEiATGKVVEGrKKPSSDTPTHLALYRRYAEIGGIVHTHSRHATIW 104
Cdd:PRK08087  26 TAGNVSV--RYQDGMLITPTGIPYEKLTESHIVFVD-GNGKHEEG-KLPSSEWRFHMAAYQTRPDANAVVHNHAVHCTAV 101

                         90       100       110
                 ....*....|....*....|....*....|.
gi 534751162 105 SQAGLDLPAW-------GTTHadyfygaIPC 128
Cdd:PRK08087 102 SILNRPIPAIhymiaaaGGNS-------IPC 125
PRK06357 PRK06357
hypothetical protein; Provisional
 27-128 1.57e-07

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 50.16  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  27 GNVS---AVDETRQWMVIKP---SGVEYNVMTADDMVVVEIATGKVVEGRKKPSSDTPTHLALYRRYAEIGGIVHTHSRH 100
Cdd:PRK06357  28 GNISvrmTAEKNKEYIIMTPtlmSEAKLCDLSPYQILVVDLNTGEVIEGVGRVTREINMHEAAYVANPKIKCVYHSHAKE 107

                         90       100
                 ....*....|....*....|....*...
gi 534751162 101 ATIWSQAGLDLPawGTTHADYFYGAIPC 128
Cdd:PRK06357 108 SMFWATLGLEMP--NLTEATQKLGKIPT 133
PRK08333 PRK08333
aldolase;
41-194 8.39e-05

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 42.12  E-value: 8.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  41 IKPSGVEYNVMTADDMVVVEIaTGKVVEGrKKPSSDTPTHLALYRRYAEIGGIVHTHSRHATIWSQA-GLDLPAWgTTHA 119
Cdd:PRK08333  38 IKATGSVMDELTREQVAVIDL-NGNQLSS-VRPSSEYRLHLAVYRNRPDVRAIAHLHPPYSIVASTLlEEELPII-TPEA 114

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 534751162 120 DYFYGAIPCTRQMTAEEIngEYEYQTGEVIiktfeerglnpAQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECA 194
Cdd:PRK08333 115 ELYLKKIPILPFRPAGSV--ELAEQVAEAM-----------KEYDAVIMERHGIVTVGRSLREAFYKAELVEESA 176
PRK06486 PRK06486
aldolase;
41-124 9.75e-04

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 39.31  E-value: 9.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751162  41 IKPSGVEYNVMTADDMVVVEIAtGKVVEGRKKPSsdtPT----HLALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGT 116
Cdd:PRK06486  64 VNPYGYAFSEITASDLLICDFD-GNVLAGRGEPE---ATaffiHARIHRAIPRAKAAFHTHMPYATALSLTEGRPLTTLG 139


                 ....*...
gi 534751162 117 THADYFYG 124
Cdd:PRK06486 140 QTALKFYG 147
 
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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