NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|161078179|ref|NP_001097742|]
View 

uncharacterized protein Dmel_CG6567 [Drosophila melanogaster]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 7-221 2.86e-35

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam02230:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 217  Bit Score: 124.80  E-value: 2.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179    7 TVNATGKHTASVIFFHGSGDTGpnvLEWvrFLIGR-NLEYPHIKIIYPTAPKQKYTPLDGELSNVWFDRKSVNIAASESK 85
Cdd:pfam02230   6 VVSPRDPAQATVIFLHGLGDSG---HGW--ADAAKtEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179   86 KSMSQCYDAVNQLIDEEVASGIPLNRIVVGGFSMGGALALHTGYHLRRSLAGVFAHSSFL-NRGSVVYDSLANGKDesFP 164
Cdd:pfam02230  81 AGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLpLPTKFPSHPNLVTKK--TP 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 161078179  165 ELRMyHGERDTLVPKDWGLETFENLTKLGVKGTFHPLRNTLHELKTASITDLQQWIY 221
Cdd:pfam02230 159 IFLI-HGEEDPVVPLALGKLAKEYLKTSLNKVELKIYEGLAHSICGREMQDIKKFLS 214
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 7-221 2.86e-35

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 124.80  E-value: 2.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179    7 TVNATGKHTASVIFFHGSGDTGpnvLEWvrFLIGR-NLEYPHIKIIYPTAPKQKYTPLDGELSNVWFDRKSVNIAASESK 85
Cdd:pfam02230   6 VVSPRDPAQATVIFLHGLGDSG---HGW--ADAAKtEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179   86 KSMSQCYDAVNQLIDEEVASGIPLNRIVVGGFSMGGALALHTGYHLRRSLAGVFAHSSFL-NRGSVVYDSLANGKDesFP 164
Cdd:pfam02230  81 AGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLpLPTKFPSHPNLVTKK--TP 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 161078179  165 ELRMyHGERDTLVPKDWGLETFENLTKLGVKGTFHPLRNTLHELKTASITDLQQWIY 221
Cdd:pfam02230 159 IFLI-HGEEDPVVPLALGKLAKEYLKTSLNKVELKIYEGLAHSICGREMQDIKKFLS 214
YpfH COG0400
Predicted esterase [General function prediction only];
11-225 1.85e-27

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 103.83  E-value: 1.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179  11 TGKHTASVIFFHGSGDTGPNVLEwvrflIGRNLEYPHIKIIYPTAPkqkyTPLDGElSNVWFDRKSVNIAASEskKSMSQ 90
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLP-----LAPELALPGAAVLAPRAP----VPEGPG-GRAWFDLSFLEGREDE--EGLAA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179  91 CYDAVNQLIDE-EVASGIPLNRIVVGGFSMGGALALHTGYHLRRSLAGVFAHSsflnrGSVVYDSLANGKDESFPELRMY 169
Cdd:COG0400   69 AAEALAAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALS-----GYLPGEEALPAPEAALAGTPVF 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161078179 170 --HGERDTLVPKDWGLETFENLTKLGVKGTFHpLRNTLHELKTASITDLQQWIYEKLP 225
Cdd:COG0400  144 laHGTQDPVIPVERAREAAEALEAAGADVTYR-EYPGGHEISPEELADARAWLAERLA 200
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 86-137 9.09e-03

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 35.55  E-value: 9.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161078179  86 KSMSQCYDAVNQLIDEEVASGiPLNRIVVGGFSMGGALALHTGYHLRRSLAG 137
Cdd:cd00741    5 KAARSLANLVLPLLKSALAQY-PDYKIHVTGHSLGGALAGLAGLDLRGRGLG 55
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 7-221 2.86e-35

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 124.80  E-value: 2.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179    7 TVNATGKHTASVIFFHGSGDTGpnvLEWvrFLIGR-NLEYPHIKIIYPTAPKQKYTPLDGELSNVWFDRKSVNIAASESK 85
Cdd:pfam02230   6 VVSPRDPAQATVIFLHGLGDSG---HGW--ADAAKtEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179   86 KSMSQCYDAVNQLIDEEVASGIPLNRIVVGGFSMGGALALHTGYHLRRSLAGVFAHSSFL-NRGSVVYDSLANGKDesFP 164
Cdd:pfam02230  81 AGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLpLPTKFPSHPNLVTKK--TP 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 161078179  165 ELRMyHGERDTLVPKDWGLETFENLTKLGVKGTFHPLRNTLHELKTASITDLQQWIY 221
Cdd:pfam02230 159 IFLI-HGEEDPVVPLALGKLAKEYLKTSLNKVELKIYEGLAHSICGREMQDIKKFLS 214
YpfH COG0400
Predicted esterase [General function prediction only];
11-225 1.85e-27

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 103.83  E-value: 1.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179  11 TGKHTASVIFFHGSGDTGPNVLEwvrflIGRNLEYPHIKIIYPTAPkqkyTPLDGElSNVWFDRKSVNIAASEskKSMSQ 90
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLP-----LAPELALPGAAVLAPRAP----VPEGPG-GRAWFDLSFLEGREDE--EGLAA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179  91 CYDAVNQLIDE-EVASGIPLNRIVVGGFSMGGALALHTGYHLRRSLAGVFAHSsflnrGSVVYDSLANGKDESFPELRMY 169
Cdd:COG0400   69 AAEALAAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALS-----GYLPGEEALPAPEAALAGTPVF 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161078179 170 --HGERDTLVPKDWGLETFENLTKLGVKGTFHpLRNTLHELKTASITDLQQWIYEKLP 225
Cdd:COG0400  144 laHGTQDPVIPVERAREAAEALEAAGADVTYR-EYPGGHEISPEELADARAWLAERLA 200
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
9-206 3.54e-13

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 66.05  E-value: 3.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179   9 NATGKHTAsVIFFHGSG------DTGPNVLEWvrflIGRNLEYPHIKIIYPTAPKQKY-TPLDgelsnvwfdrksvniaa 81
Cdd:COG0657    8 GAKGPLPV-VVYFHGGGwvsgskDTHDPLARR----LAARAGAAVVSVDYRLAPEHPFpAALE----------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179  82 seskksmsQCYDAVNQLIDEEVASGIPLNRIVVGGFSMGGALALHTGYHLRRS----LAGVFAHSSFLN-RGSVVYDSLA 156
Cdd:COG0657   66 --------DAYAALRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALRARDRggprPAAQVLIYPVLDlTASPLRADLA 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 161078179 157 NgkdesFPELRMYHGERDTLVpkDWGLETFENLTKLGVKGTFHPLRNTLH 206
Cdd:COG0657  138 G-----LPPTLIVTGEADPLV--DESEALAAALRAAGVPVELHVYPGGGH 180
COG4099 COG4099
Predicted peptidase [General function prediction only];
18-193 2.59e-08

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 52.66  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179  18 VIFFHGSGDTGPN---VLEW--VRFLIGRNLE-YPHIkIIYPTAPKQKYtpldgelsnvWFDRKSVniaaseskksmsqc 91
Cdd:COG4099   52 VLFLHGAGERGTDnekQLTHgaPKFINPENQAkFPAI-VLAPQCPEDDY----------WSDTKAL-------------- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179  92 yDAVNQLIDEEVAS-GIPLNRIVVGGFSMGGALALHTGYHLRRSLAGVFAHSSFLNRGSVvyDSLANgkdesFPeLRMYH 170
Cdd:COG4099  107 -DAVLALLDDLIAEyRIDPDRIYLTGLSMGGYGTWDLAARYPDLFAAAVPICGGGDPANA--ANLKK-----VP-VWIFH 177

                        170       180
                 ....*....|....*....|...
gi 161078179 171 GERDTLVPKDWGLETFENLTKLG 193
Cdd:COG4099  178 GAKDDVVPVEESRAMVEALKAAG 200
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
93-222 9.11e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 51.17  E-value: 9.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179  93 DAVNQLIDEevaSGIPLNRIVVGGFSMGGALALHTGYHLRRSLAGVFAHSSFLN-----RGSVVYDSLANGKDESFPELR 167
Cdd:COG1506   79 AAIDYLAAR---PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDlrsyyGTTREYTERLMGGPWEDPEAY 155

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161078179 168 -----------------MYHGERDTLVPKDWGLETFENLTKLGVKGTFHPLRNTLHELKTASITDLQQWIYE 222
Cdd:COG1506  156 aarsplayadklktpllLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLERILD 227
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
110-206 6.60e-06

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 45.73  E-value: 6.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179 110 NRIVVGGFSMGGALALHTGYHLRRSLAGV-FAhssflnrGSVVYDSLANGKDESFPELRMYHGERDTLVPKDWGLETFEN 188
Cdd:COG0412  109 GRVGVVGFCFGGGLALLAAARGPDLAAAVsFY-------GGLPADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAA 181

                         90
                 ....*....|....*...
gi 161078179 189 LTKLGVKGTFHPLRNTLH 206
Cdd:COG0412  182 LAAAGVDVELHVYPGAGH 199
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
87-220 7.93e-05

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 42.30  E-value: 7.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179  87 SMSQCYDAVNQLIDEevASGIPLNRIVVGGFSMGGALALHTGYHLRRSLAGVFAHSSFLNRGSVVYDSLANGKD----ES 162
Cdd:COG2267   78 SFDDYVDDLRAALDA--LRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRAlrlaEA 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161078179 163 FPELR----MYHGERDTLVPKDWGLETFENLTKlgvKGTFHPLRNTLHEL-----KTASITDLQQWI 220
Cdd:COG2267  156 LARIDvpvlVLHGGADRVVPPEAARRLAARLSP---DVELVLLPGARHELlnepaREEVLAAILAWL 219
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 18-206 9.60e-05

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 42.20  E-value: 9.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179   18 VIFFHGSGdtgpnvlewvrFLIGrNLEYPH--------------IKIIYPTAPKQKYtPldgelsnvwfdrksvniAASE 83
Cdd:pfam07859   1 LVYFHGGG-----------FVLG-SADTHDrlcrrlaaeagavvVSVDYRLAPEHPF-P-----------------AAYD 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179   84 skksmsQCYDAVNQLIDEEVASGIPLNRIVVGGFSMGGALALHTGYHLRRS----LAGV--------------------F 139
Cdd:pfam07859  51 ------DAYAALRWLAEQAAELGADPSRIAVAGDSAGGNLAAAVALRARDEglpkPAGQvliypgtdlrtespsylareF 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179  140 AHSSFLNRGSVVY------------DSLAN----GKDESFPELRMYHGERDTLvpKDWGLETFENLTKLGVKGTFHPLRN 203
Cdd:pfam07859 125 ADGPLLTRAAMDWfwrlylpgadrdDPLASplfaSDLSGLPPALVVVAEFDPL--RDEGEAYAERLRAAGVPVELIEYPG 202


                  ...
gi 161078179  204 TLH 206
Cdd:pfam07859 203 MPH 205
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
110-138 1.57e-03

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 38.77  E-value: 1.57e-03
                         10        20
                 ....*....|....*....|....*....
gi 161078179 110 NRIVVGGFSMGGALALHTGYHlRRSLAGV 138
Cdd:COG1647   84 DKVIVIGLSMGGLLALLLAAR-YPDVAGL 111
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 95-187 5.16e-03

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 37.29  E-value: 5.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179  95 VNQLIDEEVAS-GIPLNRIVVGGFSMGGALAlhtgYHLRRSLAGVFA----HSSfLNRGSVVYDSLANGKDESfpeLRMY 169
Cdd:COG3509  118 IAALVDDLAARyGIDPKRVYVTGLSAGGAMA----YRLACEYPDVFAavapVAG-LPYGAASDAACAPGRPVP---VLVI 189

                         90
                 ....*....|....*...
gi 161078179 170 HGERDTLVPKDWGLETFE 187
Cdd:COG3509  190 HGTADPTVPYAGAEETLA 207
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 106-187 5.50e-03

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 37.20  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078179 106 GIPLNRIVVGGFSMGGALALHTGYHLRR-----------SLAGVFAH------------SSFLNRgsVVYDSLANGKDES 162
Cdd:COG1073  105 GVDPERIGLLGISLGGGYALNAAATDPRvkavildspftSLEDLAAQrakeargaylpgVPYLPN--VRLASLLNDEFDP 182

                         90       100       110
                 ....*....|....*....|....*....|..
gi 161078179 163 FPELR-------MYHGERDTLVPKDWGLETFE 187
Cdd:COG1073  183 LAKIEkisrpllFIHGEKDEAVPFYMSEDLYE 214
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 86-137 9.09e-03

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 35.55  E-value: 9.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161078179  86 KSMSQCYDAVNQLIDEEVASGiPLNRIVVGGFSMGGALALHTGYHLRRSLAG 137
Cdd:cd00741    5 KAARSLANLVLPLLKSALAQY-PDYKIHVTGHSLGGALAGLAGLDLRGRGLG 55
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH