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Conserved domains on  [gi|446626300|ref|WP_000703646|]
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glycosyltransferase family 2 protein [Escherichia coli]

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

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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 1.16e-83

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: 249.70  E-value: 1.16e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   5 LVVPVFNEEEAIPIFYKTVREFEELKPYEVEIVFINDGSKDATESIINALAVSDPLVFPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300  85 GDAVIPIDVDLQDPIEVIPHLIEKWQGGADMVLAKRSDRStDSALKRKSAEWFYKLHNKISNPKIEENVGDFRLMSRDVV 164
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                        170       180
                 ....*....|....*....|.
gi 446626300 165 ENIKLMPERNLFMKGVLSWVG 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 1.16e-83

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: 249.70  E-value: 1.16e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   5 LVVPVFNEEEAIPIFYKTVREFEELKPYEVEIVFINDGSKDATESIINALAVSDPLVFPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300  85 GDAVIPIDVDLQDPIEVIPHLIEKWQGGADMVLAKRSDRStDSALKRKSAEWFYKLHNKISNPKIEENVGDFRLMSRDVV 164
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                        170       180
                 ....*....|....*....|.
gi 446626300 165 ENIKLMPERNLFMKGVLSWVG 185
Cdd:cd04187  160 DALLLLPERHRFLRGLIAWVG 180
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
2-302 1.76e-56

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 185.32  E-value: 1.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   2 KISLVVPVFNEEEAIP-IFYKTVREFEEL-KPYEveIVFINDGSKDATESIINALA-VSDPLVFPLSFTRNFGKEPALFA 78
Cdd:PRK10714   7 KVSVVIPVYNEQESLPeLIRRTTAACESLgKEYE--ILLIDDGSSDNSAEMLVEAAqAPDSHIVAILLNRNYGQHSAIMA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300  79 GLDHATGDAVIPIDVDLQDPIEVIPHLIEKWQGGADMVLAKRSDRStDSalkrksaeWFYKLHNKISNPKIE----ENVG 154
Cdd:PRK10714  85 GFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQ-DS--------WFRKTASKMINRLIQrttgKAMG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300 155 DFRLM----SRDVVENIKLMPERNLFMKGVLSWVGGRTDVVEYARAERVAGDSKFNGWKLWNLALEGITSFSTVPLRMWT 230
Cdd:PRK10714 156 DYGCMlrayRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLS 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446626300 231 YIGLIVAVLSFLYGAWMIFDTLVFGN--AVRGYPSLLVSILFLGGIQLIGIGVLGEYIGRIYVEVKSRPRYIIK 302
Cdd:PRK10714 236 LLGSIIAIGGFSLAVLLVVLRLTFGPqwAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQ 309
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-214 8.86e-40

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 138.30  E-value: 8.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   1 MKISLVVPVFNEEEAIPifyKTVREFEELKPYEVEIVFINDGSKDATESIINALAVSDPLVFPLSFTRNFGKEPALFAGL 80
Cdd:COG0463    2 PLVSVVIPTYNEEEYLE---EALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300  81 DHATGDAVIPIDVDLQDPIEVIPHLIEKWQ-GGADMVLAKRSDRSTDSALKRKSAEWFYkLHNKISNpkIEENVGDFRLM 159
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALEeGPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLTN--LPDSTSGFRLF 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446626300 160 SRDVVENIKLmpERNLFMKGVLSWVGGRTDVVEYARAERVAGDSKFNGWKLWNLA 214
Cdd:COG0463  156 RREVLEELGF--DEGFLEDTELLRALRHGFRIAEVPVRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-165 1.32e-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: 107.87  E-value: 1.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300    4 SLVVPVFNEEEAIPIFYKTVREfeeLKPYEVEIVFINDGSKDATESIINALAVSDPLVFPLSFTRNFGKEPALFAGLDHA 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN---QTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   84 TGDAVIPIDVDLQDPIEVIPHLIEKW-QGGADMVLAKRSDRSTDSALKRKS-----AEWFYKLHNKISNPKIEENVGDFR 157
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALeEDGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*...
gi 446626300  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 1.16e-83

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: 249.70  E-value: 1.16e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   5 LVVPVFNEEEAIPIFYKTVREFEELKPYEVEIVFINDGSKDATESIINALAVSDPLVFPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300  85 GDAVIPIDVDLQDPIEVIPHLIEKWQGGADMVLAKRSDRStDSALKRKSAEWFYKLHNKISNPKIEENVGDFRLMSRDVV 164
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159
                        170       180
                 ....*....|....*....|.
gi 446626300 165 ENIKLMPERNLFMKGVLSWVG 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 4.60e-58

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: 184.70  E-value: 4.60e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   5 LVVPVFNEEEAIPIFYKTVREFEElKPYEVEIVFINDGSKDATESIINALAVSDPLVFPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLE-EGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300  85 GDAVIPIDVDLQDPIEVIPHLIEK-WQGGADMVLAKRSDR---STDSALKRKSAEWFYKLHNKISNPKIEENVGDFRLMS 160
Cdd:cd04179   80 GDIVVTMDADLQHPPEDIPKLLEKlLEGGADVVIGSRFVRgggAGMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLFR 159
                        170       180
                 ....*....|....*....|....*
gi 446626300 161 RDVVENIKLMPERNLFMKGVLSWVG 185
Cdd:cd04179  160 REVLEALLSLLESNGFEFGLELLVG 184
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
2-302 1.76e-56

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 185.32  E-value: 1.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   2 KISLVVPVFNEEEAIP-IFYKTVREFEEL-KPYEveIVFINDGSKDATESIINALA-VSDPLVFPLSFTRNFGKEPALFA 78
Cdd:PRK10714   7 KVSVVIPVYNEQESLPeLIRRTTAACESLgKEYE--ILLIDDGSSDNSAEMLVEAAqAPDSHIVAILLNRNYGQHSAIMA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300  79 GLDHATGDAVIPIDVDLQDPIEVIPHLIEKWQGGADMVLAKRSDRStDSalkrksaeWFYKLHNKISNPKIE----ENVG 154
Cdd:PRK10714  85 GFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQ-DS--------WFRKTASKMINRLIQrttgKAMG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300 155 DFRLM----SRDVVENIKLMPERNLFMKGVLSWVGGRTDVVEYARAERVAGDSKFNGWKLWNLALEGITSFSTVPLRMWT 230
Cdd:PRK10714 156 DYGCMlrayRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLS 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446626300 231 YIGLIVAVLSFLYGAWMIFDTLVFGN--AVRGYPSLLVSILFLGGIQLIGIGVLGEYIGRIYVEVKSRPRYIIK 302
Cdd:PRK10714 236 LLGSIIAIGGFSLAVLLVVLRLTFGPqwAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQ 309
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-214 8.86e-40

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 138.30  E-value: 8.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   1 MKISLVVPVFNEEEAIPifyKTVREFEELKPYEVEIVFINDGSKDATESIINALAVSDPLVFPLSFTRNFGKEPALFAGL 80
Cdd:COG0463    2 PLVSVVIPTYNEEEYLE---EALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300  81 DHATGDAVIPIDVDLQDPIEVIPHLIEKWQ-GGADMVLAKRSDRSTDSALKRKSAEWFYkLHNKISNpkIEENVGDFRLM 159
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALEeGPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLTN--LPDSTSGFRLF 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446626300 160 SRDVVENIKLmpERNLFMKGVLSWVGGRTDVVEYARAERVAGDSKFNGWKLWNLA 214
Cdd:COG0463  156 RREVLEELGF--DEGFLEDTELLRALRHGFRIAEVPVRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-165 1.32e-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: 107.87  E-value: 1.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300    4 SLVVPVFNEEEAIPIFYKTVREfeeLKPYEVEIVFINDGSKDATESIINALAVSDPLVFPLSFTRNFGKEPALFAGLDHA 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN---QTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   84 TGDAVIPIDVDLQDPIEVIPHLIEKW-QGGADMVLAKRSDRSTDSALKRKS-----AEWFYKLHNKISNPKIEENVGDFR 157
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALeEDGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*...
gi 446626300  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 4.25e-20

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: 86.82  E-value: 4.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   5 LVVPVFNEEEAIPIFykTVREFEELKPYEVEIVFINDGSKDATESIINALAVSDPLVFPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd06442    1 IIIPTYNERENIPEL--IERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAAR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300  85 GDAVIPIDVDLQDPIEVIPHLIEK-WQGGADMVLAKR---SDRSTDSALKRKSAEWFYKLHNKIS-NPKIEENVGDFRLM 159
Cdd:cd06442   79 GDVIVVMDADLSHPPEYIPELLEAqLEGGADLVIGSRyveGGGVEGWGLKRKLISRGANLLARLLlGRKVSDPTSGFRAY 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300 160 SRDVVENI--KLMPERNLF---MKGVLSWVGGRtdVVE--YARAERVAGDSKFNGWKLWN 212
Cdd:cd06442  159 RREVLEKLidSLVSKGYKFqleLLVRARRLGYR--IVEvpITFVDREHGESKLGGKEIVE 216
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
5-132 5.19e-20

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: 86.08  E-value: 5.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   5 LVVPVFNEEEAIPIFYKTVREF-EELKPYEVEIVFINDGSKDATESIINALAVSDPLVFP-LSFTRNFGKEPALFAGLDH 82
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYlEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRvLTLPKNRGKGGAVRAGMLA 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446626300  83 ATGDAVIPIDVDLQDPIEVIPHLIE-KWQGGADMVLAKRSDRSTDSALKRK 132
Cdd:cd04188   81 ARGDYILFADADLATPFEELEKLEEaLKTSGYDIAIGSRAHLASAAVVKRS 131
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-167 3.28e-15

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 73.58  E-value: 3.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   1 MKISLVVPVFNEEEAIPIFYKTVRE-FEELKPYEveIVFINDGSKDATESIINAL--AVSDPLVFPLSFTRNFGKEPALF 77
Cdd:PLN02726   9 MKYSIIVPTYNERLNIALIVYLIFKaLQDVKDFE--IIVVDDGSPDGTQDVVKQLqkVYGEDRILLRPRPGKLGLGTAYI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300  78 AGLDHATGDAVIPIDVDLQDPIEVIPHLIEKW-QGGADMVLAKRSDRSTDSA---LKRK-SAEWFYKLHNKISNPKIEEN 152
Cdd:PLN02726  87 HGLKHASGDFVVIMDADLSHHPKYLPSFIKKQrETGADIVTGTRYVKGGGVHgwdLRRKlTSRGANVLAQTLLWPGVSDL 166
                        170
                 ....*....|....*
gi 446626300 153 VGDFRLMSRDVVENI 167
Cdd:PLN02726 167 TGSFRLYKRSALEDL 181
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-282 5.55e-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: 70.93  E-value: 5.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   1 MKISLVVPVFNEEEAIPifyKTVREFEELK--PYEVEIVFINDGSKDATESIINALAVSDPLVFPLSFTRNFGKEPALFA 78
Cdd:COG1215   29 PRVSVIIPAYNEEAVIE---ETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300  79 GLDHATGDAVIPIDvdlqdpieviphliekwqggADMVLAKrsdrstdsalkrksaEWFYKLHNKISNPKIeENVGDFRL 158
Cdd:COG1215  106 GLKAARGDIVVFLD--------------------ADTVLDP---------------DWLRRLVAAFADPGV-GASGANLA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300 159 MSRDVVENIKLMPERNLFMKGVLSWV----GGRTDVVEYARAERVAGDS------KFNGWKLWNLALEGITSFSTVPLRM 228
Cdd:COG1215  150 FRREALEEVGGFDEDTLGEDLDLSLRllraGYRIVYVPDAVVYEEAPETlralfrQRRRWARGGLQLLLKHRPLLRPRRL 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446626300 229 WTYIGLIVAVLSFLYGAWMIFDTLVF--GNAVRGYPSLLVSILFLGGIQLIGIGVL 282
Cdd:COG1215  230 LLFLLLLLLPLLLLLLLLALLALLLLllPALLLALLLALRRRRLLLPLLHLLYGLL 285
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-109 1.47e-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: 67.15  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   6 VVPVFNEEEAIPIFYKTVREfeeLKPYEVEIVFINDGSKDATESIINALAVSDPLVFPLSFTRNFGKEPALFAGLDHATG 85
Cdd:cd00761    2 IIPAYNEEPYLERCLESLLA---QTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARG 78
                         90       100
                 ....*....|....*....|....
gi 446626300  86 DAVIPIDVDlqdpIEVIPHLIEKW 109
Cdd:cd00761   79 EYILFLDAD----DLLLPDWLERL 98
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
3-167 4.41e-11

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 62.86  E-value: 4.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   3 ISLVVPVFNEEEAIPIFYK-TVREFEELKP----YEVEIVFINDGSKDATESIinALAVSDPLVFP------LSFTRNFG 71
Cdd:PTZ00260  72 LSIVIPAYNEEDRLPKMLKeTIKYLESRSRkdpkFKYEIIIVNDGSKDKTLKV--AKDFWRQNINPnidirlLSLLRNKG 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300  72 KEPALFAGLDHATGDAVIPIDVDLQDPIE----VIPHLIEKWQGGADMVLAKRSD-RSTDSALKRK-----SAEWFYKLH 141
Cdd:PTZ00260 150 KGGAVRIGMLASRGKYILMVDADGATDIDdfdkLEDIMLKIEQNGLGIVFGSRNHlVDSDVVAKRKwyrniLMYGFHFIV 229
                        170       180
                 ....*....|....*....|....*.
gi 446626300 142 NKISNPKIEENVGDFRLMSRDVVENI 167
Cdd:PTZ00260 230 NTICGTNLKDTQCGFKLFTRETARII 255
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
2-94 8.02e-10

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: 58.36  E-value: 8.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   2 KISLVVPVFNEEEAIPifyKTVREFEELK-PYE-VEIVFINDGSKDATESIinALAVSDPLVFPLSFTRNFGKEPALFAG 79
Cdd:cd06439   30 TVTIIIPAYNEEAVIE---AKLENLLALDyPRDrLEIIVVSDGSTDGTAEI--AREYADKGVKLLRFPERRGKAAALNRA 104
                         90
                 ....*....|....*
gi 446626300  80 LDHATGDAVIPIDVD 94
Cdd:cd06439  105 LALATGEIVVFTDAN 119
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
5-94 7.81e-09

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: 54.16  E-value: 7.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   5 LVVPVFNEEEAIPifyKTVREFEELKPYEVEIVFINDGSKDATESIINALAVSDP---LVFPLSftRNFGKEPALFAGLD 81
Cdd:cd06423    1 IIVPAYNEEAVIE---RTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIrrvLVVRDK--ENGGKAGALNAGLR 75
                         90
                 ....*....|...
gi 446626300  82 HATGDAVIPIDVD 94
Cdd:cd06423   76 HAKGDIVVVLDAD 88
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-108 3.61e-08

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 52.69  E-value: 3.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   1 MKISLVVPVFNEEEAIPifyKTVREFEELKPYEVEIVFINDGSKDATESIINALAVSDPLVFPLSFTRNFGKepALFAGL 80
Cdd:COG1216    3 PKVSVVIPTYNRPELLR---RCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRVRVIRNPENLGFAA--ARNLGL 77
                         90       100
                 ....*....|....*....|....*...
gi 446626300  81 DHATGDAVIPIDVDlqdpIEVIPHLIEK 108
Cdd:COG1216   78 RAAGGDYLLFLDDD----TVVEPDWLER 101
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
3-56 1.43e-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: 1.43e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446626300   3 ISLVVPVFNEEEAIPifyKTVREFEELKPYEVEIVFINDGSKDATESIINALAV 56
Cdd:cd02522    1 LSIIIPTLNEAENLP---RLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGV 51
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-98 5.55e-05

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: 43.43  E-value: 5.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   5 LVVPVFNEEEAIPifyKTVREFEELK-PYE-VEIVFINDGSKDATESII-NALAVSDPLVFPLSFTR--NFGKEPALFAG 79
Cdd:cd04192    1 VVIAARNEAENLP---RLLQSLSALDyPKEkFEVILVDDHSTDGTVQILeFAAAKPNFQLKILNNSRvsISGKKNALTTA 77
                         90
                 ....*....|....*....
gi 446626300  80 LDHATGDAVIPIDVDLQDP 98
Cdd:cd04192   78 IKAAKGDWIVTTDADCVVP 96
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
1-98 6.26e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 43.75  E-value: 6.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   1 MKISLVVPVFNEEEAIPIFYKTVREfEELKPYEVEIVFINDGSKDATESIINA-----LAVSD--PLVFPLSftrnfGKE 73
Cdd:PRK13915  31 RTVSVVLPALNEEETVGKVVDSIRP-LLMEPLVDELIVIDSGSTDATAERAAAagarvVSREEilPELPPRP-----GKG 104
                         90       100
                 ....*....|....*....|....*
gi 446626300  74 PALFAGLDHATGDAVIPIDVDLQDP 98
Cdd:PRK13915 105 EALWRSLAATTGDIVVFVDADLINF 129
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
2-92 8.56e-05

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: 42.99  E-value: 8.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   2 KISLVVPVFNEEEAIPifyKTVREFEELKPYE--VEIVFINDGSKDATESIINALAVSDPLVFPLSftrNFGK--EPALF 77
Cdd:cd02525    1 FVSIIIPVRNEEKYIE---ELLESLLNQSYPKdlIEIIVVDGGSTDGTREIVQEYAAKDPRIRLID---NPKRiqSAGLN 74
                         90
                 ....*....|....*
gi 446626300  78 AGLDHATGDAVIPID 92
Cdd:cd02525   75 IGIRNSRGDIIIRVD 89
PRK10073 PRK10073
putative glycosyl transferase; Provisional
2-107 3.89e-04

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 41.57  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   2 KISLVVPVFNEEEAIPIFyktvreFEELKPYE---VEIVFINDGSKDATESIINALAVSDPLVFPLSfTRNFGKEPALFA 78
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAF------MESLIAQTwtaLEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNT 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 446626300  79 GLDHATGDAVIPIDV-DLQDPiEVIPHLIE 107
Cdd:PRK10073  80 GLAVATGKYVAFPDAdDVVYP-TMYETLMT 108
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
2-111 4.23e-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: 41.12  E-value: 4.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   2 KISLVVPVFNEEEAIPIFYKTVREFEElkpyevEIVFINDGSKDATESIINALAVSdplVFPLSFtRNFGkePALFAGLD 81
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVD------EIIVVDSGSTDRTVEIAKEYGAK---VYQRWW-DGFG--AQRNFALE 68
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446626300  82 HATGDAVIPIDVD---LQDPIEVIPHLIEKWQG 111
Cdd:cd02511   69 LATNDWVLSLDADerlTPELADEILALLATDDY 101
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
3-94 7.99e-03

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 37.23  E-value: 7.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626300   3 ISLVVPVFNEEEaiPIFYKTVREFEELKPYEveIVFINDGSKDATESIInALAVSDPLVFPLSFTRNfGKEPALFAGLDH 82
Cdd:cd06434    2 VTVIIPVYDEDP--DVFRECLRSILRQKPLE--IIVVTDGDDEPYLSIL-SQTVKYGGIFVITVPHP-GKRRALAEGIRH 75
                         90
                 ....*....|..
gi 446626300  83 ATGDAVIPIDVD 94
Cdd:cd06434   76 VTTDIVVLLDSD 87
 
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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