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Conserved domains on  [gi|120591128|gb|ABM34568|]
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esterase, PHB depolymerase family [Paracidovorax citrulli AAC00-1]

Protein Classification

PHB depolymerase family esterase( domain architecture ID 10564707)

PHB (polyhydroxybutyrate) depolymerase family esterase belongs to the alpha/beta hydrolase superfamily, similar to Paucimonas lemoignei poly(3-hydroxyalkanoate) depolymerase C that is specific for poly(hydroxyalkanoic acid) consisting of monomers of four or five carbon atoms and for P-nitrophenylbutyrate as substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Esterase_phd pfam10503
Esterase PHB depolymerase; This family of proteins include acetyl xylan esterases (AXE), ...
107-323 2.18e-112

Esterase PHB depolymerase; This family of proteins include acetyl xylan esterases (AXE), feruloyl esterases (FAE), and poly(3-hydroxybutyrate) (PHB) depolymerases.


:

Pssm-ID: 431322 [Multi-domain]  Cd Length: 222  Bit Score: 327.40  E-value: 2.18e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  107 LAYRLYLPPEVPGDGAPRPMVVMLHGCTQHAEDFAAGTRMNALARELGVVVLYPEQTQRANAQKCWNWFKPQHQQRGRGE 186
Cdd:pfam10503   1 LAYALYLPPEAAGDGAPMPLVVMLHGCKQHADDFAAGTRINALADELGFAVLYPEQSKHAHAHKCWNWFDEQGAARGGGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  187 PAVIAALARSIATAHRVDPARVYVAGLSAGGAMADVVGHCYPDVFAAVGVHSGLPYGCAADVASALSAMRSGPGPAPGAT 266
Cdd:pfam10503  81 AASIAALAKAIAAAHRLDGARVYLAGLSAGAALAALLAHCYPDVFAAVGLHSGLPFGCAADAASALDAMRRGPGPAPGAL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 120591128  267 TGARST-----ALPTIVFHGDADTTVHVRNAESLVAALRSGSGRGAASGAAAAPRVTRGQSG 323
Cdd:pfam10503 161 IDAASDvrsypALPAIIFHGDADSTVASANADQLTAAFLRGNGFGAASGAAAAGETREEQQG 222
 
Name Accession Description Interval E-value
Esterase_phd pfam10503
Esterase PHB depolymerase; This family of proteins include acetyl xylan esterases (AXE), ...
107-323 2.18e-112

Esterase PHB depolymerase; This family of proteins include acetyl xylan esterases (AXE), feruloyl esterases (FAE), and poly(3-hydroxybutyrate) (PHB) depolymerases.


Pssm-ID: 431322 [Multi-domain]  Cd Length: 222  Bit Score: 327.40  E-value: 2.18e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  107 LAYRLYLPPEVPGDGAPRPMVVMLHGCTQHAEDFAAGTRMNALARELGVVVLYPEQTQRANAQKCWNWFKPQHQQRGRGE 186
Cdd:pfam10503   1 LAYALYLPPEAAGDGAPMPLVVMLHGCKQHADDFAAGTRINALADELGFAVLYPEQSKHAHAHKCWNWFDEQGAARGGGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  187 PAVIAALARSIATAHRVDPARVYVAGLSAGGAMADVVGHCYPDVFAAVGVHSGLPYGCAADVASALSAMRSGPGPAPGAT 266
Cdd:pfam10503  81 AASIAALAKAIAAAHRLDGARVYLAGLSAGAALAALLAHCYPDVFAAVGLHSGLPFGCAADAASALDAMRRGPGPAPGAL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 120591128  267 TGARST-----ALPTIVFHGDADTTVHVRNAESLVAALRSGSGRGAASGAAAAPRVTRGQSG 323
Cdd:pfam10503 161 IDAASDvrsypALPAIIFHGDADSTVASANADQLTAAFLRGNGFGAASGAAAAGETREEQQG 222
LpqC COG3509
Poly(3-hydroxybutyrate) depolymerase [Secondary metabolites biosynthesis, transport and ...
50-387 3.38e-48

Poly(3-hydroxybutyrate) depolymerase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 226040 [Multi-domain]  Cd Length: 312  Bit Score: 165.70  E-value: 3.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  50 APGPAADPRVLDGLVREVHDPNAA-GEAREARRPASTaplqgcgeqwqsGSFSHQNRALAYRLYLPPEVPGdgaPRPMVV 128
Cdd:COG3509    1 PRTLGRLARLVLLLAVLAVAAAACsGHAALARFGSSV------------ASFDVNGLKRSYRLYVPPGLPS---GAPLVV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 129 MLHGCTQHAEDFAAGTRMNALARELGVVVLYPE-QTQRANAQKCWNWFKPQHQQRGRGEPAVIAALARSIATAHRVDPAR 207
Cdd:COG3509   66 VLHGSGGSGAGQLHGTGWDALADREGFLVAYPDgYDRAWNANGCGNWFGPADRRRGVDDVGFLRALVAKLVNEYGIDPAR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 208 VYVAGLSAGGAMADVVGHCYPDVFAAVGVHSGL-PYGCAADVASALSAMRSGPGPAPGATTGARSTAlptiVFHGDADtt 286
Cdd:COG3509  146 VYVTGLSNGGRMANRLACEYPDIFAAIAPVAGLlALGVACTPPRPVSVMAFHGTADPLNPYHGGGVP----IGRGQRD-- 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 287 vHVRNAESLVAALRSGSGRGAASGAAAAPRvtrgqsgrgaRHTRTVYTDAAGRDSLEYWQLHGAGHAWSGGSASGS---Y 363
Cdd:COG3509  220 -GVVSAADLAARWAAVNGCQAGPDTAELPD----------VGDGTDYDTCDGNARVELYTIDGGGHTWPGGTQYGPaalG 288
                        330       340
                 ....*....|....*....|....
gi 120591128 364 TDPSGVDASAEMLRFFLAHPRAAR 387
Cdd:COG3509  289 MSTRGFDATERIWRFFRQHRRDTR 312
esterase_phb TIGR01840
esterase, PHB depolymerase family; This model describes a subfamily among lipases of the ...
109-298 5.03e-44

esterase, PHB depolymerase family; This model describes a subfamily among lipases of the ab-hydrolase family. This subfamily includes bacterial depolymerases for poly(3-hydroxybutyrate) (PHB) and related polyhydroxyalkanoates (PHA), as well as acetyl xylan esterases, feruloyl esterases, and others from fungi. [Fatty acid and phospholipid metabolism, Degradation]


Pssm-ID: 273828 [Multi-domain]  Cd Length: 212  Bit Score: 151.87  E-value: 5.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  109 YRLYLPPEVPGdgaPRPMVVMLHGCTQHAEDFAAGTRMNALARELGVVVLYPEQTQRANAQKCWNWFKPQHQQRGRGEPA 188
Cdd:TIGR01840   1 MYVYVPAGLTG---PRALVLALHGCGQTASAYVIDWGWKAAADRYGFVLVAPEQTSYNSSNNCWDWFFTHHRARGTGEVE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  189 VIAALARSIATAHRVDPARVYVAGLSAGGAMADVVGHCYPDVFAAVGVHSGLPYGCAADVASALSAMRSGPGPAP----- 263
Cdd:TIGR01840  78 SLHQLIDAVKANYSIDPNRVYVTGLSAGGGMTAVLGCTYPDVFAGGASNAGLPYGEASSSISATPQMCTAATAASvcrlv 157
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 120591128  264 -GATTGARSTALPTIVFHGDADTTVHVRNAESLVAA 298
Cdd:TIGR01840 158 rGMQSEYNGPTPIMSVVHGDADYTVLPGNADEIRDA 193
 
Name Accession Description Interval E-value
Esterase_phd pfam10503
Esterase PHB depolymerase; This family of proteins include acetyl xylan esterases (AXE), ...
107-323 2.18e-112

Esterase PHB depolymerase; This family of proteins include acetyl xylan esterases (AXE), feruloyl esterases (FAE), and poly(3-hydroxybutyrate) (PHB) depolymerases.


Pssm-ID: 431322 [Multi-domain]  Cd Length: 222  Bit Score: 327.40  E-value: 2.18e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  107 LAYRLYLPPEVPGDGAPRPMVVMLHGCTQHAEDFAAGTRMNALARELGVVVLYPEQTQRANAQKCWNWFKPQHQQRGRGE 186
Cdd:pfam10503   1 LAYALYLPPEAAGDGAPMPLVVMLHGCKQHADDFAAGTRINALADELGFAVLYPEQSKHAHAHKCWNWFDEQGAARGGGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  187 PAVIAALARSIATAHRVDPARVYVAGLSAGGAMADVVGHCYPDVFAAVGVHSGLPYGCAADVASALSAMRSGPGPAPGAT 266
Cdd:pfam10503  81 AASIAALAKAIAAAHRLDGARVYLAGLSAGAALAALLAHCYPDVFAAVGLHSGLPFGCAADAASALDAMRRGPGPAPGAL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 120591128  267 TGARST-----ALPTIVFHGDADTTVHVRNAESLVAALRSGSGRGAASGAAAAPRVTRGQSG 323
Cdd:pfam10503 161 IDAASDvrsypALPAIIFHGDADSTVASANADQLTAAFLRGNGFGAASGAAAAGETREEQQG 222
LpqC COG3509
Poly(3-hydroxybutyrate) depolymerase [Secondary metabolites biosynthesis, transport and ...
50-387 3.38e-48

Poly(3-hydroxybutyrate) depolymerase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 226040 [Multi-domain]  Cd Length: 312  Bit Score: 165.70  E-value: 3.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  50 APGPAADPRVLDGLVREVHDPNAA-GEAREARRPASTaplqgcgeqwqsGSFSHQNRALAYRLYLPPEVPGdgaPRPMVV 128
Cdd:COG3509    1 PRTLGRLARLVLLLAVLAVAAAACsGHAALARFGSSV------------ASFDVNGLKRSYRLYVPPGLPS---GAPLVV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 129 MLHGCTQHAEDFAAGTRMNALARELGVVVLYPE-QTQRANAQKCWNWFKPQHQQRGRGEPAVIAALARSIATAHRVDPAR 207
Cdd:COG3509   66 VLHGSGGSGAGQLHGTGWDALADREGFLVAYPDgYDRAWNANGCGNWFGPADRRRGVDDVGFLRALVAKLVNEYGIDPAR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 208 VYVAGLSAGGAMADVVGHCYPDVFAAVGVHSGL-PYGCAADVASALSAMRSGPGPAPGATTGARSTAlptiVFHGDADtt 286
Cdd:COG3509  146 VYVTGLSNGGRMANRLACEYPDIFAAIAPVAGLlALGVACTPPRPVSVMAFHGTADPLNPYHGGGVP----IGRGQRD-- 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 287 vHVRNAESLVAALRSGSGRGAASGAAAAPRvtrgqsgrgaRHTRTVYTDAAGRDSLEYWQLHGAGHAWSGGSASGS---Y 363
Cdd:COG3509  220 -GVVSAADLAARWAAVNGCQAGPDTAELPD----------VGDGTDYDTCDGNARVELYTIDGGGHTWPGGTQYGPaalG 288
                        330       340
                 ....*....|....*....|....
gi 120591128 364 TDPSGVDASAEMLRFFLAHPRAAR 387
Cdd:COG3509  289 MSTRGFDATERIWRFFRQHRRDTR 312
esterase_phb TIGR01840
esterase, PHB depolymerase family; This model describes a subfamily among lipases of the ...
109-298 5.03e-44

esterase, PHB depolymerase family; This model describes a subfamily among lipases of the ab-hydrolase family. This subfamily includes bacterial depolymerases for poly(3-hydroxybutyrate) (PHB) and related polyhydroxyalkanoates (PHA), as well as acetyl xylan esterases, feruloyl esterases, and others from fungi. [Fatty acid and phospholipid metabolism, Degradation]


Pssm-ID: 273828 [Multi-domain]  Cd Length: 212  Bit Score: 151.87  E-value: 5.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  109 YRLYLPPEVPGdgaPRPMVVMLHGCTQHAEDFAAGTRMNALARELGVVVLYPEQTQRANAQKCWNWFKPQHQQRGRGEPA 188
Cdd:TIGR01840   1 MYVYVPAGLTG---PRALVLALHGCGQTASAYVIDWGWKAAADRYGFVLVAPEQTSYNSSNNCWDWFFTHHRARGTGEVE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  189 VIAALARSIATAHRVDPARVYVAGLSAGGAMADVVGHCYPDVFAAVGVHSGLPYGCAADVASALSAMRSGPGPAP----- 263
Cdd:TIGR01840  78 SLHQLIDAVKANYSIDPNRVYVTGLSAGGGMTAVLGCTYPDVFAGGASNAGLPYGEASSSISATPQMCTAATAASvcrlv 157
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 120591128  264 -GATTGARSTALPTIVFHGDADTTVHVRNAESLVAA 298
Cdd:TIGR01840 158 rGMQSEYNGPTPIMSVVHGDADYTVLPGNADEIRDA 193
COG4099 COG4099
Predicted peptidase [General function prediction only];
103-342 2.35e-09

Predicted peptidase [General function prediction only];


Pssm-ID: 226584 [Multi-domain]  Cd Length: 387  Bit Score: 58.38  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 103 QNRALAYRLYLPPEVPGDGAPRPMVVMLHGCTQHAEDFAAGTRMN--ALA---RELGVVVLYPEqtqranaqkcWN-WFK 176
Cdd:COG4099  170 TGNELKYRLYTPKDYAPDKKYYPLVLFLHGAGQGGSDNDKVLSSGigAIAwagPEDQCFVLAPQ----------YNpIFA 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 177 PQHQQRGRGEPAVIAALARSIATAHRVDPARVYVAGLSAGGAMADVVGHCYPDVFAAVgvhsgLPYGCAADVASALSAMR 256
Cdd:COG4099  240 DSEEKTLLYLIEKIDLILEVLASTYNIDRSRIYVIGLSRGGFGTWALAEKFPDFFAAA-----VPIAGGGDRVYLVRTLK 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 257 SgpgpapgattgarstaLPTIVFHGDADTTVHVRNAESLVAALRSGSGRGAASGAAAAPRVTRGQSGRGARhtRTVYTDA 336
Cdd:COG4099  315 K----------------APIWVFHSSDDKVIPVSNSRVLYERLKALDRKVNYTAFLEGTTVLEGVDHSGVW--WATYNDA 376

                 ....*.
gi 120591128 337 AGRDSL 342
Cdd:COG4099  377 EAIEWL 382
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
109-299 4.56e-09

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 224423 [Multi-domain]  Cd Length: 620  Bit Score: 57.92  E-value: 4.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 109 YRLYLPPEVPGDGAPRPMVVMLHGCTQHAEDFAAGTRMNALArELGVVVLYPEQtqRANAQKCWNWFKPQHQQRGRGEPA 188
Cdd:COG1506  379 HGWLYKPPGFDPRKKYPLIVYIHGGPSAQVGYSFNPEIQVLA-SAGYAVLAPNY--RGSTGYGREFADAIRGDWGGVDLE 455
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 189 VIAALARSIATAHRVDPARVYVAGLSAGGAMADVVGHCYPDVFAAVGVHSG-----LPYGCAADVASALSAMRSGPGPAP 263
Cdd:COG1506  456 DLIAAVDALVKLPLVDPERIGITGGSYGGYMTLLAATKTPRFKAAVAVAGGvdwllYFGESTEGLRFDPEENGGGPPEDR 535
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 120591128 264 GATTgARSTAL-------PTIVFHGDADTTVHVRNAESLVAAL 299
Cdd:COG1506  536 EKYE-DRSPIFyadniktPLLLIHGEEDDRVPIEQAEQLVDAL 577
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
148-299 3.68e-06

Prolyl oligopeptidase family;


Pssm-ID: 425609 [Multi-domain]  Cd Length: 213  Bit Score: 47.22  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  148 ALARELGVVVLYPEQtqRANAQKCWNWFKPQHQQRGRGEPAVIAALARSIATAHRVDPARVYVAGLSAGGAMADVVGHCY 227
Cdd:pfam00326   8 QLLADRGYVVAIANG--RGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQGYTDPDRLAIWGGSYGGYLTGAALNQR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128  228 PDVF----AAVGVHSGLPYGCAADVASALSAMRSGPGPAPGATTGARSTAL---------PTIVFHGDADTTVHVRNAES 294
Cdd:pfam00326  86 PDLFkaavAHVPVVDWLAYMSDTSLPFTERYMEWGNPWDNEEGYDYLSPYSpadnvkvypPLLLIHGLLDDRVPPWQSLK 165

                  ....*
gi 120591128  295 LVAAL 299
Cdd:pfam00326 166 LVAAL 170
YpfH COG0400
Predicted esterase [General function prediction only];
111-299 3.42e-05

Predicted esterase [General function prediction only];


Pssm-ID: 223477 [Multi-domain]  Cd Length: 207  Bit Score: 44.22  E-value: 3.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 111 LYLPPEVPGDGAPRPMVVMLHGCTQHAEDFAAGTRMNA-LARELGVVVLYPEQtqraNAQKCWNWFKPQHQQRGRGEPAv 189
Cdd:COG0400    5 PFIPRIEKPGDPAAPLLILLHGLGGDELDLVPLPELILpNATLVSPRGPVAEN----GGPRFFRRYDEGSFDQEDLDLE- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 190 IAALARSI---ATAHRVDPARVYVAGLSAGGAMAdvvghcypdvfAAVGVHSGLPYGCAAdvasALSAMRSGPGPAPGAT 266
Cdd:COG0400   80 TEKLAEFLeelAEEYGIDSSRIILIGFSQGANIA-----------LSLGLTLPGLFAGAI----LFSGMLPLEPELLPDL 144
                        170       180       190
                 ....*....|....*....|....*....|...
gi 120591128 267 TGArstalPTIVFHGDADTTVHVRNAESLVAAL 299
Cdd:COG0400  145 AGT-----PILLSHGTEDPVVPLALAEALAEYL 172
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
118-249 2.59e-03

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 223489 [Multi-domain]  Cd Length: 236  Bit Score: 38.90  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120591128 118 PGDGAPRPMVVMLHGC---TQHAEDFAagtrmNALARElGVVVLYP-----------EQTQRANAQKCWNWFKPQHQQRG 183
Cdd:COG0412   21 PAGAGGFPGVIVLHEIfglNPHIRDVA-----RRLAKA-GYVVLAPdlygrqgdptdIEDEPAELETGLVERVDPAEVLA 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 120591128 184 RGEpAVIAALARsiatAHRVDPARVYVAGLSAGGAMADVVGHCYPDVFAAVGVHSGLPYGCAADVA 249
Cdd:COG0412   95 DID-AALDYLAR----QPQVDPKRIGVVGFCMGGGLALLAATRAPEVKAAVAFYGGLIADDTADAP 155
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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