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Conserved domains on  [gi|518937065|ref|WP_020092940|]
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MULTISPECIES: low specificity L-threonine aldolase [Methylobacterium]

Protein Classification

threonine aldolase family protein( domain architecture ID 10005169)

threonine aldolase family protein such as low-specificity L-threonine aldolase, which catalyzes cleavage of L-allo-threonine and L-threonine to glycine in a PLP-dependent manner

CATH:  3.40.640.10
Gene Ontology:  GO:0006567|GO:0004793
SCOP:  4000670

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
1-341 1.48e-134

Threonine aldolase [Amino acid transport and metabolism];


:

Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 386.34  E-value: 1.48e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065   1 MRHDdsqqFASDNYSGICPEAWAAMEAANRGHAPaYGEDAWTARAADAFRDLFETpCEVFFAFNGTAANALALAALCQSY 80
Cdd:COG2008    1 MMID----FRSDTVTGPHPEMLEAMAAANVGDDV-YGEDPTVNRLEERVAELFGK-EAALFVPSGTMANQLALRAHTRPG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065  81 HSVICADSAHVETDECGAPEFFSnGSKLLTVRTEGGKLTPEAIRGlAQNRSDIHFPRPRVVTITQPTETGQVYSLAELRA 160
Cdd:COG2008   75 DEVICHETAHIYVDEGGAPEALS-GVKLLPVPGEDGKLTPEDLEA-AIRPGDVHFPQPGLVSLENTTEGGTVYPLEELRA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065 161 LSATCRELGLALHMDGSRFANACASLGCSPADMTwrSGIDVLCFGGTKNGMHAGEAVVFFDATLAEDFGYRCKQAGQLAS 240
Cdd:COG2008  153 IAAVAREHGLPLHLDGARLFNAAAALGVSLAEIT--AGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMR 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065 241 KMRFLAAPWVGMLESGawLRNAAHGNACARRFAEAVGGLPGVRALFPVEANAVFLTMPAATMEGLRARGWRFYTFIGGGA 320
Cdd:COG2008  231 QAGFLAAQGLAALEDD--LERLAEDHAMARRLAEGLAALPGVRVPEPVETNIVFVILPDELAERLREKGVLFYPWGPGAV 308
                        330       340
                 ....*....|....*....|.
gi 518937065 321 RFMFAWDARTERVDELVGDLR 341
Cdd:COG2008  309 RLVTHWDTTEEDVDAFLAALA 329
 
Name Accession Description Interval E-value
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
1-341 1.48e-134

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 386.34  E-value: 1.48e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065   1 MRHDdsqqFASDNYSGICPEAWAAMEAANRGHAPaYGEDAWTARAADAFRDLFETpCEVFFAFNGTAANALALAALCQSY 80
Cdd:COG2008    1 MMID----FRSDTVTGPHPEMLEAMAAANVGDDV-YGEDPTVNRLEERVAELFGK-EAALFVPSGTMANQLALRAHTRPG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065  81 HSVICADSAHVETDECGAPEFFSnGSKLLTVRTEGGKLTPEAIRGlAQNRSDIHFPRPRVVTITQPTETGQVYSLAELRA 160
Cdd:COG2008   75 DEVICHETAHIYVDEGGAPEALS-GVKLLPVPGEDGKLTPEDLEA-AIRPGDVHFPQPGLVSLENTTEGGTVYPLEELRA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065 161 LSATCRELGLALHMDGSRFANACASLGCSPADMTwrSGIDVLCFGGTKNGMHAGEAVVFFDATLAEDFGYRCKQAGQLAS 240
Cdd:COG2008  153 IAAVAREHGLPLHLDGARLFNAAAALGVSLAEIT--AGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMR 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065 241 KMRFLAAPWVGMLESGawLRNAAHGNACARRFAEAVGGLPGVRALFPVEANAVFLTMPAATMEGLRARGWRFYTFIGGGA 320
Cdd:COG2008  231 QAGFLAAQGLAALEDD--LERLAEDHAMARRLAEGLAALPGVRVPEPVETNIVFVILPDELAERLREKGVLFYPWGPGAV 308
                        330       340
                 ....*....|....*....|.
gi 518937065 321 RFMFAWDARTERVDELVGDLR 341
Cdd:COG2008  309 RLVTHWDTTEEDVDAFLAALA 329
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
8-341 1.69e-130

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 376.29  E-value: 1.69e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065   8 QFASDNYSGICPEAWAAMEAANRGHApAYGEDAWTARAADAFRDLFETpCEVFFAFNGTAANALALAALCQSYHSVICAD 87
Cdd:cd06502    1 DFRSDTVTGPTPEMLEAMAAANVGDD-VYGEDPTTAKLEARAAELFGK-EAALFVPSGTAANQLALAAHTQPGGSVICHE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065  88 SAHVETDECGAPEFFSnGSKLLTVRTEGGKLTPEAIRGLAQNRSDIHFPRPRVVTITQPTETGQVYSLAELRALSATCRE 167
Cdd:cd06502   79 TAHIYTDEAGAPEFLS-GVKLLPVPGENGKLTPEDLEAAIRPRDDIHFPPPSLVSLENTTEGGTVYPLDELKAISALAKE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065 168 LGLALHMDGSRFANACASLGCspADMTWRSGIDVLCFGGTKNGMHAGEAVVFFDATLAEDFGYRCKQAGQLASKMRFLAA 247
Cdd:cd06502  158 NGLPLHLDGARLANAAAALGV--ALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGFLAA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065 248 PWVGMLESGAWLRNAAHGNACARRFAEAVGGLP--------GVRALFPVEANAVFLTMPAATMEGlRARGWRFYTFIGGG 319
Cdd:cd06502  236 AGLAALENDLWLRRLRHDHEMARRLAEALEELGglesevqtNIVLLDPVEANAVFVELSKEAIER-RGEGVLFYAWGEGG 314
                        330       340
                 ....*....|....*....|..
gi 518937065 320 ARFMFAWDARTERVDELVGDLR 341
Cdd:cd06502  315 VRFVTHWDTTEEDVDELLSALK 336
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
8-300 2.17e-76

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 236.73  E-value: 2.17e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065    8 QFASDNYSGICPEAWAAMEAANRGHApAYGEDAWTARAADAFRDLFETPCEVFFAfNGTAANALALAALCQSYHSVICAD 87
Cdd:pfam01212   1 DLRSDTVTGPTPAMREAMAAAMVGDE-VYGGDPTVNRLEDRVAELFGKEAALFVP-SGTAANQLALMAHCQRGDEVICGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065   88 SAHVETDECGAPEFFsNGSKLLTVRT-EGGKLTPEAIRGLAQNRSDIHFPRPRVVTITQPTET--GQVYSLAELRALSAT 164
Cdd:pfam01212  79 PAHIHFDETGGHAEL-GGVQPRPLDGdEAGNMDLEDLEAAIREVGADIFPPTGLISLENTHNSagGQVVSLENLREIAAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065  165 CRELGLALHMDGSRFANACASLGCSPADMTwrSGIDVLCFGGTKNGMHAGEAVVFFDatlaEDF-GYRCKQAGQLASKMR 243
Cdd:pfam01212 158 AREHGIPVHLDGARFANAAVALGVIVKEIT--SYADSVTMCLSKGLGAPVGSVLAGS----DDFiAKAIRQRKYLGGGLR 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065  244 ---FLAAPWVGMLESGAWLrnAAHGNACARRFAEAVGGLPGVRAlFPVEANAVFLTMPAA 300
Cdd:pfam01212 232 qagVLAAAGLRALEEGVAR--LARDHATARRLAEGLELLRLAIP-RRVYTNTHMVYVAAA 288
PLN02721 PLN02721
threonine aldolase
83-298 7.56e-13

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 68.56  E-value: 7.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065  83 VICADSAHVETDECGAPEFFSnGSKLLTVR-TEGGKLTPEAIRGLAQNRSDIHFPRPRVVTI--TQPTETGQVYSLAELR 159
Cdd:PLN02721  83 VILGDNSHIHLYENGGISTLG-GVHPRTVKnNEDGTMDLDAIEAAIRPKGDDHFPTTRLICLenTHANCGGRCLSVEYTD 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065 160 ALSATCRELGLALHMDGSRFANACASLG------CSPADmtwrsGIDVLCFGGTknGMHAGEAVV----FFDA--TLAED 227
Cdd:PLN02721 162 KVGELAKRHGLKLHIDGARIFNASVALGvpvhrlVKAAD-----SVSVCLSKGL--GAPVGSVIVgsksFIRKakRLRKT 234
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518937065 228 FGYRCKQAGQLAskmrflAAPWVGMLESGAWLRNaAHGNacARRFAEAVGGLPGVRA-LFPVEANAVFLTMP 298
Cdd:PLN02721 235 LGGGMRQVGVLA------AAALVALQENVPKLED-DHKK--AKLLAEGLNQIKGLRVnVAAVETNIVYFDIT 297
 
Name Accession Description Interval E-value
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
1-341 1.48e-134

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 386.34  E-value: 1.48e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065   1 MRHDdsqqFASDNYSGICPEAWAAMEAANRGHAPaYGEDAWTARAADAFRDLFETpCEVFFAFNGTAANALALAALCQSY 80
Cdd:COG2008    1 MMID----FRSDTVTGPHPEMLEAMAAANVGDDV-YGEDPTVNRLEERVAELFGK-EAALFVPSGTMANQLALRAHTRPG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065  81 HSVICADSAHVETDECGAPEFFSnGSKLLTVRTEGGKLTPEAIRGlAQNRSDIHFPRPRVVTITQPTETGQVYSLAELRA 160
Cdd:COG2008   75 DEVICHETAHIYVDEGGAPEALS-GVKLLPVPGEDGKLTPEDLEA-AIRPGDVHFPQPGLVSLENTTEGGTVYPLEELRA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065 161 LSATCRELGLALHMDGSRFANACASLGCSPADMTwrSGIDVLCFGGTKNGMHAGEAVVFFDATLAEDFGYRCKQAGQLAS 240
Cdd:COG2008  153 IAAVAREHGLPLHLDGARLFNAAAALGVSLAEIT--AGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMR 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065 241 KMRFLAAPWVGMLESGawLRNAAHGNACARRFAEAVGGLPGVRALFPVEANAVFLTMPAATMEGLRARGWRFYTFIGGGA 320
Cdd:COG2008  231 QAGFLAAQGLAALEDD--LERLAEDHAMARRLAEGLAALPGVRVPEPVETNIVFVILPDELAERLREKGVLFYPWGPGAV 308
                        330       340
                 ....*....|....*....|.
gi 518937065 321 RFMFAWDARTERVDELVGDLR 341
Cdd:COG2008  309 RLVTHWDTTEEDVDAFLAALA 329
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
8-341 1.69e-130

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 376.29  E-value: 1.69e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065   8 QFASDNYSGICPEAWAAMEAANRGHApAYGEDAWTARAADAFRDLFETpCEVFFAFNGTAANALALAALCQSYHSVICAD 87
Cdd:cd06502    1 DFRSDTVTGPTPEMLEAMAAANVGDD-VYGEDPTTAKLEARAAELFGK-EAALFVPSGTAANQLALAAHTQPGGSVICHE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065  88 SAHVETDECGAPEFFSnGSKLLTVRTEGGKLTPEAIRGLAQNRSDIHFPRPRVVTITQPTETGQVYSLAELRALSATCRE 167
Cdd:cd06502   79 TAHIYTDEAGAPEFLS-GVKLLPVPGENGKLTPEDLEAAIRPRDDIHFPPPSLVSLENTTEGGTVYPLDELKAISALAKE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065 168 LGLALHMDGSRFANACASLGCspADMTWRSGIDVLCFGGTKNGMHAGEAVVFFDATLAEDFGYRCKQAGQLASKMRFLAA 247
Cdd:cd06502  158 NGLPLHLDGARLANAAAALGV--ALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGFLAA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065 248 PWVGMLESGAWLRNAAHGNACARRFAEAVGGLP--------GVRALFPVEANAVFLTMPAATMEGlRARGWRFYTFIGGG 319
Cdd:cd06502  236 AGLAALENDLWLRRLRHDHEMARRLAEALEELGglesevqtNIVLLDPVEANAVFVELSKEAIER-RGEGVLFYAWGEGG 314
                        330       340
                 ....*....|....*....|..
gi 518937065 320 ARFMFAWDARTERVDELVGDLR 341
Cdd:cd06502  315 VRFVTHWDTTEEDVDELLSALK 336
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
8-300 2.17e-76

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 236.73  E-value: 2.17e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065    8 QFASDNYSGICPEAWAAMEAANRGHApAYGEDAWTARAADAFRDLFETPCEVFFAfNGTAANALALAALCQSYHSVICAD 87
Cdd:pfam01212   1 DLRSDTVTGPTPAMREAMAAAMVGDE-VYGGDPTVNRLEDRVAELFGKEAALFVP-SGTAANQLALMAHCQRGDEVICGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065   88 SAHVETDECGAPEFFsNGSKLLTVRT-EGGKLTPEAIRGLAQNRSDIHFPRPRVVTITQPTET--GQVYSLAELRALSAT 164
Cdd:pfam01212  79 PAHIHFDETGGHAEL-GGVQPRPLDGdEAGNMDLEDLEAAIREVGADIFPPTGLISLENTHNSagGQVVSLENLREIAAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065  165 CRELGLALHMDGSRFANACASLGCSPADMTwrSGIDVLCFGGTKNGMHAGEAVVFFDatlaEDF-GYRCKQAGQLASKMR 243
Cdd:pfam01212 158 AREHGIPVHLDGARFANAAVALGVIVKEIT--SYADSVTMCLSKGLGAPVGSVLAGS----DDFiAKAIRQRKYLGGGLR 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065  244 ---FLAAPWVGMLESGAWLrnAAHGNACARRFAEAVGGLPGVRAlFPVEANAVFLTMPAA 300
Cdd:pfam01212 232 qagVLAAAGLRALEEGVAR--LARDHATARRLAEGLELLRLAIP-RRVYTNTHMVYVAAA 288
PLN02721 PLN02721
threonine aldolase
83-298 7.56e-13

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 68.56  E-value: 7.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065  83 VICADSAHVETDECGAPEFFSnGSKLLTVR-TEGGKLTPEAIRGLAQNRSDIHFPRPRVVTI--TQPTETGQVYSLAELR 159
Cdd:PLN02721  83 VILGDNSHIHLYENGGISTLG-GVHPRTVKnNEDGTMDLDAIEAAIRPKGDDHFPTTRLICLenTHANCGGRCLSVEYTD 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065 160 ALSATCRELGLALHMDGSRFANACASLG------CSPADmtwrsGIDVLCFGGTknGMHAGEAVV----FFDA--TLAED 227
Cdd:PLN02721 162 KVGELAKRHGLKLHIDGARIFNASVALGvpvhrlVKAAD-----SVSVCLSKGL--GAPVGSVIVgsksFIRKakRLRKT 234
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518937065 228 FGYRCKQAGQLAskmrflAAPWVGMLESGAWLRNaAHGNacARRFAEAVGGLPGVRA-LFPVEANAVFLTMP 298
Cdd:PLN02721 235 LGGGMRQVGVLA------AAALVALQENVPKLED-DHKK--AKLLAEGLNQIKGLRVnVAAVETNIVYFDIT 297
PRK10534 PRK10534
L-threonine aldolase; Provisional
132-194 1.69e-06

L-threonine aldolase; Provisional


Pssm-ID: 236710 [Multi-domain]  Cd Length: 333  Bit Score: 48.99  E-value: 1.69e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518937065 132 DIHFPRPRVVTItQPTETGQVYSLAELRALSATCRELGLALHMDGSRFANACASLGCSPADMT 194
Cdd:PRK10534 124 DIHFARTRLLSL-ENTHNGKVLPREYLKQAWEFTRERNLALHVDGARIFNAVVAYGCELKEIT 185
tnaA PRK13238
tryptophanase;
140-232 6.72e-04

tryptophanase;


Pssm-ID: 237314  Cd Length: 460  Bit Score: 41.34  E-value: 6.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518937065 140 VVTITQPTETGQVYSLAELRALSATCRELGLALHMDGSRFA-NA---------CASLgcSPADMTWR--SGIDVLCFGGT 207
Cdd:PRK13238 182 VMTITNNSAGGQPVSMANLRAVYEIAKKYGIPVVIDAARFAeNAyfikqrepgYKDK--SIKEIAREmfSYADGLTMSAK 259
                         90       100
                 ....*....|....*....|....*.
gi 518937065 208 KNGM-HAGEAVVFFDATLAEDFGYRC 232
Cdd:PRK13238 260 KDAMvNIGGLLCFRDEDLFTECRTLC 285
 
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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