NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16130283|ref|NP_416852|]
View 

bactoprenol glucosyl transferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135621)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
SCOP:  3000077

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
5-185 6.26e-86

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


:

Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 255.48  E-value: 6.26e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   5 LVVPVFNEEEAIPIFYKTVREFEELKSYEVEIVFINDGSKDATESIINALAVSDPLVVPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04187   1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283  85 GDAIIPIDVDLQDPIEVIPHLIEKWQAGADMVLAKRSDRStDGRLKRKTAEWFYKLHNKISNPKIEENVGDFRLMSRDVV 164
Cdd:cd04187  81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                       170       180
                ....*....|....*....|.
gi 16130283 165 ENIKLMPERNLFMKGILSWVG 185
Cdd:cd04187 160 DALLLLPERHRFLRGLIAWVG 180
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
5-185 6.26e-86

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 255.48  E-value: 6.26e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   5 LVVPVFNEEEAIPIFYKTVREFEELKSYEVEIVFINDGSKDATESIINALAVSDPLVVPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04187   1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283  85 GDAIIPIDVDLQDPIEVIPHLIEKWQAGADMVLAKRSDRStDGRLKRKTAEWFYKLHNKISNPKIEENVGDFRLMSRDVV 164
Cdd:cd04187  81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                       170       180
                ....*....|....*....|.
gi 16130283 165 ENIKLMPERNLFMKGILSWVG 185
Cdd:cd04187 160 DALLLLPERHRFLRGLIAWVG 180
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
2-304 4.92e-51

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 171.07  E-value: 4.92e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283    2 KISLVVPVFNEEEAIPIFYKTVREFEELKSYEVEIVFINDGSKDATESIINALA-VSDPLVVPLSFTRNFGKEPALFAGL 80
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAqAPDSHIVAILLNRNYGQHSAIMAGF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   81 DHATGDAIIPIDVDLQDPIEVIPHLIEKWQAGADMVLAKRSDRSTdgrlkrktaEWFYKLHNKISNPKIE----ENVGDF 156
Cdd:PRK10714  87 SHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQD---------SWFRKTASKMINRLIQrttgKAMGDY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283  157 RLM----SRDVVENIKLMPERNLFMKGILSWVGGKTDIVEYVRAERIAGDTKFNGWKLWNLALEGITSFSTFPLRIWTYI 232
Cdd:PRK10714 158 GCMlrayRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLL 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130283  233 GLVVASVAFIYGAWMILDTIIFGN--AVRGYPSLLVSILFLGGIQMIGIGVLGEYIGRTYIETKKRPKYIIKRV 304
Cdd:PRK10714 238 GSIIAIGGFSLAVLLVVLRLTFGPqwAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQV 311
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-214 1.17e-40

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 140.61  E-value: 1.17e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   1 MKISLVVPVFNEEEAIPifyKTVREFEELKSYEVEIVFINDGSKDATESIINALAVSDPLVVPLSFTRNFGKEPALFAGL 80
Cdd:COG0463   2 PLVSVVIPTYNEEEYLE---EALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283  81 DHATGDAIIPIDVDLQDPIEVIPHLIEKWQA-GADMVLAKRSDRSTDGRLKRKTAEWFYkLHNKISNpkIEENVGDFRLM 159
Cdd:COG0463  79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLTN--LPDSTSGFRLF 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16130283 160 SRDVVENIKLmPERNLFMKGILsWVGGKTDIVEYVRAERIAGDTKFNGWKLWNLA 214
Cdd:COG0463 156 RREVLEELGF-DEGFLEDTELL-RALRHGFRIAEVPVRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-165 3.79e-28

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 106.71  E-value: 3.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283     4 SLVVPVFNEEEAIPIFYKTVREfeeLKSYEVEIVFINDGSKDATESIINALAVSDPLVVPLSFTRNFGKEPALFAGLDHA 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN---QTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283    84 TGDAIIPIDVDLQDPIEVIPHLIEKWQA-GADMVLAKRSDRSTDGRLKRKT-----AEWFYKLHNKISNPKIEENVGDFR 157
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*...
gi 16130283   158 LMSRDVVE 165
Cdd:pfam00535 158 LYRREALE 165
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
5-185 6.26e-86

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 255.48  E-value: 6.26e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   5 LVVPVFNEEEAIPIFYKTVREFEELKSYEVEIVFINDGSKDATESIINALAVSDPLVVPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04187   1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283  85 GDAIIPIDVDLQDPIEVIPHLIEKWQAGADMVLAKRSDRStDGRLKRKTAEWFYKLHNKISNPKIEENVGDFRLMSRDVV 164
Cdd:cd04187  81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                       170       180
                ....*....|....*....|.
gi 16130283 165 ENIKLMPERNLFMKGILSWVG 185
Cdd:cd04187 160 DALLLLPERHRFLRGLIAWVG 180
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
5-185 1.43e-57

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 183.16  E-value: 1.43e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   5 LVVPVFNEEEAIPIFYKTVREFEElKSYEVEIVFINDGSKDATESIINALAVSDPLVVPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04179   1 VVIPAYNEEENIPELVERLLAVLE-EGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAAR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283  85 GDAIIPIDVDLQDPIEVIPHLIEK-WQAGADMVLAKRSDR---STDGRLKRKTAEWFYKLHNKISNPKIEENVGDFRLMS 160
Cdd:cd04179  80 GDIVVTMDADLQHPPEDIPKLLEKlLEGGADVVIGSRFVRgggAGMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLFR 159
                       170       180
                ....*....|....*....|....*
gi 16130283 161 RDVVENIKLMPERNLFMKGILSWVG 185
Cdd:cd04179 160 REVLEALLSLLESNGFEFGLELLVG 184
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
2-304 4.92e-51

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 171.07  E-value: 4.92e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283    2 KISLVVPVFNEEEAIPIFYKTVREFEELKSYEVEIVFINDGSKDATESIINALA-VSDPLVVPLSFTRNFGKEPALFAGL 80
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAqAPDSHIVAILLNRNYGQHSAIMAGF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   81 DHATGDAIIPIDVDLQDPIEVIPHLIEKWQAGADMVLAKRSDRSTdgrlkrktaEWFYKLHNKISNPKIE----ENVGDF 156
Cdd:PRK10714  87 SHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQD---------SWFRKTASKMINRLIQrttgKAMGDY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283  157 RLM----SRDVVENIKLMPERNLFMKGILSWVGGKTDIVEYVRAERIAGDTKFNGWKLWNLALEGITSFSTFPLRIWTYI 232
Cdd:PRK10714 158 GCMlrayRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLL 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130283  233 GLVVASVAFIYGAWMILDTIIFGN--AVRGYPSLLVSILFLGGIQMIGIGVLGEYIGRTYIETKKRPKYIIKRV 304
Cdd:PRK10714 238 GSIIAIGGFSLAVLLVVLRLTFGPqwAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQV 311
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-214 1.17e-40

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 140.61  E-value: 1.17e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   1 MKISLVVPVFNEEEAIPifyKTVREFEELKSYEVEIVFINDGSKDATESIINALAVSDPLVVPLSFTRNFGKEPALFAGL 80
Cdd:COG0463   2 PLVSVVIPTYNEEEYLE---EALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283  81 DHATGDAIIPIDVDLQDPIEVIPHLIEKWQA-GADMVLAKRSDRSTDGRLKRKTAEWFYkLHNKISNpkIEENVGDFRLM 159
Cdd:COG0463  79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLTN--LPDSTSGFRLF 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16130283 160 SRDVVENIKLmPERNLFMKGILsWVGGKTDIVEYVRAERIAGDTKFNGWKLWNLA 214
Cdd:COG0463 156 RREVLEELGF-DEGFLEDTELL-RALRHGFRIAEVPVRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-165 3.79e-28

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 106.71  E-value: 3.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283     4 SLVVPVFNEEEAIPIFYKTVREfeeLKSYEVEIVFINDGSKDATESIINALAVSDPLVVPLSFTRNFGKEPALFAGLDHA 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN---QTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283    84 TGDAIIPIDVDLQDPIEVIPHLIEKWQA-GADMVLAKRSDRSTDGRLKRKT-----AEWFYKLHNKISNPKIEENVGDFR 157
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*...
gi 16130283   158 LMSRDVVE 165
Cdd:pfam00535 158 LYRREALE 165
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
5-212 1.82e-19

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 84.89  E-value: 1.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   5 LVVPVFNEEEAIPIFykTVREFEELKSYEVEIVFINDGSKDATESIINALAVSDPLVVPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd06442   1 IIIPTYNERENIPEL--IERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAAR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283  85 GDAIIPIDVDLQDPIEVIPHLIEK-WQAGADMVLAKR--SDRSTDGR-LKRK----TAEWFYKLhnkISNPKIEENVGDF 156
Cdd:cd06442  79 GDVIVVMDADLSHPPEYIPELLEAqLEGGADLVIGSRyvEGGGVEGWgLKRKlisrGANLLARL---LLGRKVSDPTSGF 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130283 157 RLMSRDVVENI--KLMPERNLF---MKGILSWVGGKtdIVE--YVRAERIAGDTKFNGWKLWN 212
Cdd:cd06442 156 RAYRREVLEKLidSLVSKGYKFqleLLVRARRLGYR--IVEvpITFVDREHGESKLGGKEIVE 216
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
5-132 2.68e-19

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 84.16  E-value: 2.68e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   5 LVVPVFNEEEAIPIFYKTVREF-EELKSYEVEIVFINDGSKDATESIINALAVSDPLVVP-LSFTRNFGKEPALFAGLDH 82
Cdd:cd04188   1 VVIPAYNEEKRLPPTLEEAVEYlEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRvLTLPKNRGKGGAVRAGMLA 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 16130283  83 ATGDAIIPIDVDLQDPIEVIPHLIE-KWQAGADMVLAKRSDRSTDGRLKRK 132
Cdd:cd04188  81 ARGDYILFADADLATPFEELEKLEEaLKTSGYDIAIGSRAHLASAAVVKRS 131
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-167 3.28e-17

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 79.36  E-value: 3.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283    1 MKISLVVPVFNEEEAIPIFYKTVRE-FEELKSYEveIVFINDGSKDATESIINAL--AVSDPLVVPLSFTRNFGKEPALF 77
Cdd:PLN02726   9 MKYSIIVPTYNERLNIALIVYLIFKaLQDVKDFE--IIVVDDGSPDGTQDVVKQLqkVYGEDRILLRPRPGKLGLGTAYI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   78 AGLDHATGDAIIPIDVDLQDPIEVIPHLIEKWQA-GADMVLAKRSdRSTDG----RLKRK-TAEWFYKLHNKISNPKIEE 151
Cdd:PLN02726  87 HGLKHASGDFVVIMDADLSHHPKYLPSFIKKQREtGADIVTGTRY-VKGGGvhgwDLRRKlTSRGANVLAQTLLWPGVSD 165
                        170
                 ....*....|....*.
gi 16130283  152 NVGDFRLMSRDVVENI 167
Cdd:PLN02726 166 LTGSFRLYKRSALEDL 181
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-295 8.32e-14

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 70.54  E-value: 8.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   1 MKISLVVPVFNEEEAIPifyKTVREFEELK--SYEVEIVFINDGSKDATESIINALAVSDPLVVPLSFTRNFGKEPALFA 78
Cdd:COG1215  29 PRVSVIIPAYNEEAVIE---ETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNA 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283  79 GLDHATGDAIIPIDvdlqdpieviphliekwqagADMVLAKrsdrstdgrlkrktaEWFYKLHNKISNPKIeENVGDFRL 158
Cdd:COG1215 106 GLKAARGDIVVFLD--------------------ADTVLDP---------------DWLRRLVAAFADPGV-GASGANLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283 159 MSRDVVENIKLMPERNLFMKGILSWV----GGKTDIVEYVRAERIAGDTKFNGWK-------------LWNLALEGITSF 221
Cdd:COG1215 150 FRREALEEVGGFDEDTLGEDLDLSLRllraGYRIVYVPDAVVYEEAPETLRALFRqrrrwargglqllLKHRPLLRPRRL 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130283 222 STFPLRIWTYIGLVVASVAFIYGAWMILDTIIFGNAVRGYPSLLVSILFLGGIQMIGIGVLGEYIGRTYIETKK 295
Cdd:COG1215 230 LLFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-109 1.87e-13

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 66.76  E-value: 1.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   6 VVPVFNEEEAIPIFYKTVREfeeLKSYEVEIVFINDGSKDATESIINALAVSDPLVVPLSFTRNFGKEPALFAGLDHATG 85
Cdd:cd00761   2 IIPAYNEEPYLERCLESLLA---QTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARG 78
                        90       100
                ....*....|....*....|....
gi 16130283  86 DAIIPIDVDlqdpIEVIPHLIEKW 109
Cdd:cd00761  79 EYILFLDAD----DLLLPDWLERL 98
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
3-167 6.68e-11

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 62.09  E-value: 6.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283    3 ISLVVPVFNEEEAIPIFYK-TVREFEELK----SYEVEIVFINDGSKDATESIinALAVSDPLVVP------LSFTRNFG 71
Cdd:PTZ00260  72 LSIVIPAYNEEDRLPKMLKeTIKYLESRSrkdpKFKYEIIIVNDGSKDKTLKV--AKDFWRQNINPnidirlLSLLRNKG 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   72 KEPALFAGLDHATGDAIIPIDVDLQDPIE----VIPHLIEKWQAGADMVLAKRSD-RSTDGRLKRK-----TAEWFYKLH 141
Cdd:PTZ00260 150 KGGAVRIGMLASRGKYILMVDADGATDIDdfdkLEDIMLKIEQNGLGIVFGSRNHlVDSDVVAKRKwyrniLMYGFHFIV 229
                        170       180
                 ....*....|....*....|....*.
gi 16130283  142 NKISNPKIEENVGDFRLMSRDVVENI 167
Cdd:PTZ00260 230 NTICGTNLKDTQCGFKLFTRETARII 255
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
5-94 6.86e-10

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 57.24  E-value: 6.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   5 LVVPVFNEEEAIPifyKTVREFEELKSYEVEIVFINDGSKDATESIINALAVSDP---LVVPLSftRNFGKEPALFAGLD 81
Cdd:cd06423   1 IIVPAYNEEAVIE---RTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIrrvLVVRDK--ENGGKAGALNAGLR 75
                        90
                ....*....|...
gi 16130283  82 HATGDAIIPIDVD 94
Cdd:cd06423  76 HAKGDIVVVLDAD 88
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
2-94 1.04e-09

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 57.98  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   2 KISLVVPVFNEEEAIPifyKTVREFEELkSY---EVEIVFINDGSKDATESIinALAVSDPLVVPLSFTRNFGKEPALFA 78
Cdd:cd06439  30 TVTIIIPAYNEEAVIE---AKLENLLAL-DYprdRLEIIVVSDGSTDGTAEI--AREYADKGVKLLRFPERRGKAAALNR 103
                        90
                ....*....|....*.
gi 16130283  79 GLDHATGDAIIPIDVD 94
Cdd:cd06439 104 ALALATGEIVVFTDAN 119
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-117 4.66e-09

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 55.38  E-value: 4.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   1 MKISLVVPVFNEEEAIPifyKTVREFEELKSYEVEIVFINDGSKDATESIINALAVSDPLVVPLSFTRNFGKepALFAGL 80
Cdd:COG1216   3 PKVSVVIPTYNRPELLR---RCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRVRVIRNPENLGFAA--ARNLGL 77
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 16130283  81 DHATGDAIIPIDVDlqdpIEVIPHLIEKWQAGADMVL 117
Cdd:COG1216  78 RAAGGDYLLFLDDD----TVVEPDWLERLLAAACLLI 110
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
3-86 1.65e-07

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 51.03  E-value: 1.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   3 ISLVVPVFNEEEAIPifyKTVREFEELKSYEVEIVFINDGSKDATESIinalaVSDPLVVPLSFTRNFGKEpaLFAGLDH 82
Cdd:cd02522   1 LSIIIPTLNEAENLP---RLLASLRRLNPLPLEIIVVDGGSTDGTVAI-----ARSAGVVVISSPKGRARQ--MNAGAAA 70

                ....
gi 16130283  83 ATGD 86
Cdd:cd02522  71 ARGD 74
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
2-116 3.75e-06

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 47.23  E-value: 3.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   2 KISLVVPVFNEEEAIPifyKTVREFEElKSYE---VEIVFINDGSKDATESIINALAVSDPLVVPLSftrNFGK--EPAL 76
Cdd:cd02525   1 FVSIIIPVRNEEKYIE---ELLESLLN-QSYPkdlIEIIVVDGGSTDGTREIVQEYAAKDPRIRLID---NPKRiqSAGL 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 16130283  77 FAGLDHATGDAIIPIDVDLQDPIEVIPHLIEKWQA-GADMV 116
Cdd:cd02525  74 NIGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRtGADNV 114
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
1-98 3.18e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 44.91  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283    1 MKISLVVPVFNEEEAIPIFYKTVRefEELKSYEV-EIVFINDGSKDATEsiINALA-----VSDPLVVPLsFTRNFGKEP 74
Cdd:PRK13915  31 RTVSVVLPALNEEETVGKVVDSIR--PLLMEPLVdELIVIDSGSTDATA--ERAAAagarvVSREEILPE-LPPRPGKGE 105
                         90       100
                 ....*....|....*....|....
gi 16130283   75 ALFAGLDHATGDAIIPIDVDLQDP 98
Cdd:PRK13915 106 ALWRSLAATTGDIVVFVDADLINF 129
PRK10073 PRK10073
putative glycosyl transferase; Provisional
2-107 1.95e-04

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 42.34  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283    2 KISLVVPVFNEEEAIPIFYKTVREfEELKSYEVEIVfiNDGSKDATESIINALAVSDPLVVPLSfTRNFGKEPALFAGLD 81
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAFMESLIA-QTWTALEIIIV--NDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLA 82
                         90       100
                 ....*....|....*....|....*...
gi 16130283   82 HATGD--AIIPIDvDLQDPiEVIPHLIE 107
Cdd:PRK10073  83 VATGKyvAFPDAD-DVVYP-TMYETLMT 108
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-98 2.36e-04

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 41.51  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   5 LVVPVFNEEEAIPIFYKTVREFEELKSyEVEIVFINDGSKDATESII-NALAVSDPLVVPLSFTR--NFGKEPALFAGLD 81
Cdd:cd04192   1 VVIAARNEAENLPRLLQSLSALDYPKE-KFEVILVDDHSTDGTVQILeFAAAKPNFQLKILNNSRvsISGKKNALTTAIK 79
                        90
                ....*....|....*..
gi 16130283  82 HATGDAIIPIDVDLQDP 98
Cdd:cd04192  80 AAKGDWIVTTDADCVVP 96
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
2-158 5.43e-04

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 40.73  E-value: 5.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283   2 KISLVVPVFNEEEAIPIFYKTVREFEElksyevEIVFINDGSKDATESIINALAVSdplVVPLSFtRNFGkePALFAGLD 81
Cdd:cd02511   1 TLSVVIITKNEERNIERCLESVKWAVD------EIIVVDSGSTDRTVEIAKEYGAK---VYQRWW-DGFG--AQRNFALE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130283  82 HATGDAIIPIDVD---LQDPIEVIPHLIEKWQAGA------DMVLAKRSDRSTDG-----RL--KRKTAEWFYKLHNKIS 145
Cdd:cd02511  69 LATNDWVLSLDADerlTPELADEILALLATDDYDGyyvprrNFFLGRWIRHGGWYpdrqlRLfrRGKARFEDGRVHEQVV 148
                       170
                ....*....|...
gi 16130283 146 NPKIEENVGDFRL 158
Cdd:cd02511 149 VDGGVGIVLKGDI 161
 
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