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Conserved domains on  [gi|1469545488|gb|RGR13875|]
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glycosyltransferase [Parabacteroides merdae]

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
PubMed:  12691742|9445404
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 ...
6-188 1.33e-81

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: 244.69  E-value: 1.33e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNEELVIAESYRRTREALHKLPVLTEIIYINDGSRDRTRLMLDEIAASDPQVKVIHFSRNFGHQPAVTAGINNCD 85
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  86 ADLAVILDADMQDPPELIPSILElQEKEQANVVYCVRKSREgEGLFKKVTAKAFYRMLNYMSDVNFPLDTGDFRLIDRKV 165
Cdd:cd04187    81 GDAVITMDADLQDPPELIPEMLA-KWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKV 158
                         170       180
                  ....*....|....*....|...
gi 1469545488 166 MDQFDRFQERGKYIRGLISWVGF 188
Cdd:cd04187   159 VDALLLLPERHRFLRGLIAWVGF 181
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
6-188 1.33e-81

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: 244.69  E-value: 1.33e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNEELVIAESYRRTREALHKLPVLTEIIYINDGSRDRTRLMLDEIAASDPQVKVIHFSRNFGHQPAVTAGINNCD 85
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  86 ADLAVILDADMQDPPELIPSILElQEKEQANVVYCVRKSREgEGLFKKVTAKAFYRMLNYMSDVNFPLDTGDFRLIDRKV 165
Cdd:cd04187    81 GDAVITMDADLQDPPELIPEMLA-KWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKV 158
                         170       180
                  ....*....|....*....|...
gi 1469545488 166 MDQFDRFQERGKYIRGLISWVGF 188
Cdd:cd04187   159 VDALLLLPERHRFLRGLIAWVGF 181
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-216 6.32e-47

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 156.79  E-value: 6.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   1 MKKLAVIVPCYNEELVIAESYRRTREALHKLpvlTEIIYINDGSRDRTRLMLDEIAASDPQVKVIHFSRNFGHQPAVTAG 80
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPD---FEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  81 INNCDADLAVILDADMQDPPELIPSILELQEKEQANVVYCVRKSREGEGLFKKVTAKAFYrMLNYMSdvNFPLDTGDFRL 160
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLT--NLPDSTSGFRL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1469545488 161 IDRKVMDQF---DRFQERGKYIRGLISWVGFKQVPFYYEreariAGETKYPFSKMWKFA 216
Cdd:COG0463   155 FRREVLEELgfdEGFLEDTELLRALRHGFRIAEVPVRYR-----AGESKLNLRDLLRLL 208
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
1-304 1.30e-40

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 144.11  E-value: 1.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   1 MKKLAVIVPCYNEELVIAESYRRTREALHKLPVLTEIIYINDGSRDRTRLMLDEiAASDPQVKVIH--FSRNFGHQPAVT 78
Cdd:PRK10714    5 IKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVE-AAQAPDSHIVAilLNRNYGQHSAIM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  79 AGINNCDADLAVILDADMQDPPELIPSILELQEkEQANVVYCVRKSREgEGLFKKVTAkafyRMLNYMSDVNFPLDTGDF 158
Cdd:PRK10714   84 AGFSHVTGDLIITLDADLQNPPEEIPRLVAKAD-EGYDVVGTVRQNRQ-DSWFRKTAS----KMINRLIQRTTGKAMGDY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488 159 ----RLIDRKVMDQFDRFQERGKYIRGLISWVGFKQVPFYYEREARIAGETKYPFSKMWKFATTAMLYFSKKPLRLATSL 234
Cdd:PRK10714  158 gcmlRAYRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLL 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469545488 235 GFIAVLVGIVLAVWF-TLGKIYGFSNAETGWTSIMTSVIFFGGVQLLTVGVLGQYIGILFDEIKARPEYII 304
Cdd:PRK10714  238 GSIIAIGGFSLAVLLvVLRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFV 308
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
6-168 2.83e-31

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: 114.80  E-value: 2.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNEELVIAESYRRTREALHKLpvlTEIIYINDGSRDRTRLMLDEIAASDPQVKVIHFSRNFGHQPAVTAGINNCD 85
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPN---FEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  86 ADLAVILDADMQDPPELIPSILELQEKEQANVVYCVRKSREGEGLFKKVT-----AKAFYRMLNYMSDVNFPLDTGDFRL 160
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFAL 158

                  ....*...
gi 1469545488 161 IDRKVMDQ 168
Cdd:pfam00535 159 YRREALEE 166
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
4-74 1.34e-06

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 48.28  E-value: 1.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469545488   4 LAVIVPCYNEELVIAesyrRTREALHKLPVLTEIIYINDGSRDRTRlmldEIAASDPqVKVIHFSRNFGHQ 74
Cdd:TIGR04283   1 LSIIIPVLNEAATLP----ELLADLQALRGDAEVIVVDGGSTDGTV----EIARSLG-AKVIHSPKGRARQ 62
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
6-188 1.33e-81

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: 244.69  E-value: 1.33e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNEELVIAESYRRTREALHKLPVLTEIIYINDGSRDRTRLMLDEIAASDPQVKVIHFSRNFGHQPAVTAGINNCD 85
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  86 ADLAVILDADMQDPPELIPSILElQEKEQANVVYCVRKSREgEGLFKKVTAKAFYRMLNYMSDVNFPLDTGDFRLIDRKV 165
Cdd:cd04187    81 GDAVITMDADLQDPPELIPEMLA-KWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKV 158
                         170       180
                  ....*....|....*....|...
gi 1469545488 166 MDQFDRFQERGKYIRGLISWVGF 188
Cdd:cd04187   159 VDALLLLPERHRFLRGLIAWVGF 181
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
6-188 5.53e-62

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: 194.71  E-value: 5.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNEELVIAESYRRTREALHKLPVLtEIIYINDGSRDRTRLMLDEIAASDPQVKVIHFSRNFGHQPAVTAGINNCD 85
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGYDY-EIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  86 ADLAVILDADMQDPPELIPSILELQEKEQANVVYCVRKSREG---EGLFKKVTAKAFYRMLNYMSDVNFPLDTGDFRLID 162
Cdd:cd04179    80 GDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGgagMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLFR 159
                         170       180
                  ....*....|....*....|....*.
gi 1469545488 163 RKVMDQFDRFQERGKYIRGLISWVGF 188
Cdd:cd04179   160 REVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-216 6.32e-47

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 156.79  E-value: 6.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   1 MKKLAVIVPCYNEELVIAESYRRTREALHKLpvlTEIIYINDGSRDRTRLMLDEIAASDPQVKVIHFSRNFGHQPAVTAG 80
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPD---FEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  81 INNCDADLAVILDADMQDPPELIPSILELQEKEQANVVYCVRKSREGEGLFKKVTAKAFYrMLNYMSdvNFPLDTGDFRL 160
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLT--NLPDSTSGFRL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1469545488 161 IDRKVMDQF---DRFQERGKYIRGLISWVGFKQVPFYYEreariAGETKYPFSKMWKFA 216
Cdd:COG0463   155 FRREVLEELgfdEGFLEDTELLRALRHGFRIAEVPVRYR-----AGESKLNLRDLLRLL 208
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
1-304 1.30e-40

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 144.11  E-value: 1.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   1 MKKLAVIVPCYNEELVIAESYRRTREALHKLPVLTEIIYINDGSRDRTRLMLDEiAASDPQVKVIH--FSRNFGHQPAVT 78
Cdd:PRK10714    5 IKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVE-AAQAPDSHIVAilLNRNYGQHSAIM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  79 AGINNCDADLAVILDADMQDPPELIPSILELQEkEQANVVYCVRKSREgEGLFKKVTAkafyRMLNYMSDVNFPLDTGDF 158
Cdd:PRK10714   84 AGFSHVTGDLIITLDADLQNPPEEIPRLVAKAD-EGYDVVGTVRQNRQ-DSWFRKTAS----KMINRLIQRTTGKAMGDY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488 159 ----RLIDRKVMDQFDRFQERGKYIRGLISWVGFKQVPFYYEREARIAGETKYPFSKMWKFATTAMLYFSKKPLRLATSL 234
Cdd:PRK10714  158 gcmlRAYRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLL 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469545488 235 GFIAVLVGIVLAVWF-TLGKIYGFSNAETGWTSIMTSVIFFGGVQLLTVGVLGQYIGILFDEIKARPEYII 304
Cdd:PRK10714  238 GSIIAIGGFSLAVLLvVLRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFV 308
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
6-168 2.83e-31

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: 114.80  E-value: 2.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNEELVIAESYRRTREALHKLpvlTEIIYINDGSRDRTRLMLDEIAASDPQVKVIHFSRNFGHQPAVTAGINNCD 85
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPN---FEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  86 ADLAVILDADMQDPPELIPSILELQEKEQANVVYCVRKSREGEGLFKKVT-----AKAFYRMLNYMSDVNFPLDTGDFRL 160
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRAsritlSRLPFFLGLRLLGLNLPFLIGGFAL 158

                  ....*...
gi 1469545488 161 IDRKVMDQ 168
Cdd:pfam00535 159 YRREALEE 166
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
6-215 4.07e-23

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: 94.91  E-value: 4.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNEELVIAESYRRTREALHKLPVltEIIYINDGSRDRTRLMLDEIAASDPQVKVIHFSRNFGHQPAVTAGINNCD 85
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGIDY--EIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAAR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  86 ADLAVILDADMQDPPELIPSILELQEKEQANVV----YCVRKSREGEGLFKKV---TAKAFYRMLNYM--SDVnfpldTG 156
Cdd:cd06442    79 GDVIVVMDADLSHPPEYIPELLEAQLEGGADLVigsrYVEGGGVEGWGLKRKLisrGANLLARLLLGRkvSDP-----TS 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469545488 157 DFRLIDRKVMDQ-FDRFQERG-KY-----IRGLISWVGFKQVPFYYEReaRIAGETKYPFSKMWKF 215
Cdd:cd06442   154 GFRAYRREVLEKlIDSLVSKGyKFqlellVRARRLGYRIVEVPITFVD--REHGESKLGGKEIVEY 217
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
6-143 2.03e-17

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: 79.15  E-value: 2.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNEELVIAESYRRTREALHKLPVLT-EIIYINDGSRDRTRLMLDEIAASDPQ-VKVIHFSRNFGHQPAVTAGINN 83
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPSFSyEIIVVDDGSKDGTAEVARKLARKNPAlIRVLTLPKNRGKGGAVRAGMLA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  84 CDADLAVILDADMQDPPELIPSILELQEKEQANVVYCVRKSREGEglfkKVTAKAFYRML 143
Cdd:cd04188    81 ARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHLASA----AVVKRSWLRNL 136
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-124 1.62e-16

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: 78.24  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   1 MKKLAVIVPCYNEELVIAE---SYRRTREALHKLpvltEIIYINDGSRDRTRLMLDEIAASDPQVKVIHFSRNFGHQPAV 77
Cdd:COG1215    28 LPRVSVIIPAYNEEAVIEEtlrSLLAQDYPKEKL----EVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAAL 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1469545488  78 TAGINNCDADLAVILDADMQDPPELIPSILELQEKEQANVV---YCVRKS 124
Cdd:COG1215   104 NAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASganLAFRRE 153
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
6-95 3.78e-15

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: 72.26  E-value: 3.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNEELVIaesyRRTREALHKL--PVLtEIIYINDGSRDRTRLMLDEIAASDPQVKVIHF-SRNFGHQPAVTAGIN 82
Cdd:cd06423     1 IIVPAYNEEAVI----ERTIESLLALdyPKL-EVIVVDDGSTDDTLEILEELAALYIRRVLVVRdKENGGKAGALNAGLR 75
                          90
                  ....*....|...
gi 1469545488  83 NCDADLAVILDAD 95
Cdd:cd06423    76 HAKGDIVVVLDAD 88
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-121 3.79e-14

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: 68.69  E-value: 3.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNEELVIAESYRRTREALHKLpvlTEIIYINDGSRDRTRLMLDEIAASDPQVKVIHFSRNFGHQPAVTAGINNCD 85
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPN---FEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1469545488  86 ADLAVILDADMQDPPELIPSIL-ELQEKEQANVVYCV 121
Cdd:cd00761    78 GEYILFLDADDLLLPDWLERLVaELLADPEADAVGGP 114
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
4-176 4.01e-13

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 67.40  E-value: 4.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   4 LAVIVPCYNEELVIaesyRRTREALHKLP-VLTEIIYINDGSRDRTRLMLDEIAA--SDPQVKVIHFSRNFGHQPAVTA- 79
Cdd:pfam13641   4 VSVVVPAFNEDSVL----GRVLEAILAQPyPPVEVVVVVNPSDAETLDVAEEIAArfPDVRLRVIRNARLLGPTGKSRGl 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  80 --GINNCDADLAVILDADMQDPPELIPSILELQEKEQANVVYCVRKSREGEGLFKKVTAKAFY-RMLNYMS---DVNFPL 153
Cdd:pfam13641  80 nhGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRSTMLSALGALEFAlRHLRMMSlrlALGVLP 159
                         170       180
                  ....*....|....*....|...
gi 1469545488 154 DTGDFRLIDRKVMDQFDRFQERG 176
Cdd:pfam13641 160 LSGAGSAIRREVLKELGLFDPFF 182
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-108 3.84e-12

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 64.24  E-value: 3.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   1 MKKLAVIVPCYNeelviaeSYRRTREALHKL----PVLTEIIYINDGSRDRTRLMLDEIAasDPQVKVIHFSRNFGHQPA 76
Cdd:COG1216     2 RPKVSVVIPTYN-------RPELLRRCLESLlaqtYPPFEVIVVDNGSTDGTAELLAALA--FPRVRVIRNPENLGFAAA 72
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1469545488  77 VTAGINNCDADLAVILDADMQDPPELIPSILE 108
Cdd:COG1216    73 RNLGLRAAGGDYLLFLDDDTVVEPDWLERLLA 104
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-168 1.40e-11

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 63.18  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   1 MKKLAVIVPCYNEELVIAESYRRTREALHKlPVLTEIIYINDGSRDRTRLMLDEIAAS--DPQVKVIHFSRNFGHQPAVT 78
Cdd:PLN02726    8 AMKYSIIVPTYNERLNIALIVYLIFKALQD-VKDFEIIVVDDGSPDGTQDVVKQLQKVygEDRILLRPRPGKLGLGTAYI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  79 AGINNCDADLAVILDADMQDPPELIPSILELQEKEQANVVYCVRkSREGEG-----LFKKVTAkafyRMLNYM------- 146
Cdd:PLN02726   87 HGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTR-YVKGGGvhgwdLRRKLTS----RGANVLaqtllwp 161
                         170       180
                  ....*....|....*....|....
gi 1469545488 147 --SDVnfpldTGDFRLIDRKVMDQ 168
Cdd:PLN02726  162 gvSDL-----TGSFRLYKRSALED 180
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
6-139 2.60e-11

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: 62.63  E-value: 2.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNEELVIaesyRRTREALHK---LPVLTEIIYINDGSRDRTRLMLDEIAASDPQVKVIHfsrNFG-HQP-AVTAG 80
Cdd:cd02525     4 IIIPVRNEEKYI----EELLESLLNqsyPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLID---NPKrIQSaGLNIG 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1469545488  81 INNCDADLAVILDADMQDPPELIPSILELQEKEQANVVYCVRKSReGEGLFKKVTAKAF 139
Cdd:cd02525    77 IRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETI-GESKFQKAIAVAQ 134
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-133 1.09e-10

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: 60.38  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNEelviAESYRRTREALHKL---PVLTEIIYINDGSRDRTRLMLDEIAA-SDPQVKVIHFSR--NFGHQPAVTA 79
Cdd:cd04192     1 VVIAARNE----AENLPRLLQSLSALdypKEKFEVILVDDHSTDGTVQILEFAAAkPNFQLKILNNSRvsISGKKNALTT 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1469545488  80 GINNCDADLAVILDADMQDPPELIPSILELQEKEQAN-VVYCVRKsREGEGLFKK 133
Cdd:cd04192    77 AIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGlVAGPVIY-FKGKSLLAK 130
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
3-95 8.89e-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: 57.98  E-value: 8.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   3 KLAVIVPCYNEELVIAE--------SYRRtrealHKLpvltEIIYINDGSRDRTrlmlDEIAAS--DPQVKVIHFSRNFG 72
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAklenllalDYPR-----DRL----EIIVVSDGSTDGT----AEIAREyaDKGVKLLRFPERRG 96
                          90       100
                  ....*....|....*....|...
gi 1469545488  73 HQPAVTAGINNCDADLAVILDAD 95
Cdd:cd06439    97 KAAALNRALALATGEIVVFTDAN 119
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
3-125 1.64e-09

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: 56.91  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   3 KLAVIVPCYNEELVIaesyRRTREALHklPVLTEIIYINDGSRDRTRlmldEIAASdPQVKVIHFS-RNFGHQpaVTAGI 81
Cdd:cd02511     1 TLSVVIITKNEERNI----ERCLESVK--WAVDEIIVVDSGSTDRTV----EIAKE-YGAKVYQRWwDGFGAQ--RNFAL 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1469545488  82 NNCDADLAVILDADMQDPPELIPSILELQEKEQANVVYCVRKSR 125
Cdd:cd02511    68 ELATNDWVLSLDADERLTPELADEILALLATDDYDGYYVPRRNF 111
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-131 6.12e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 56.21  E-value: 6.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   3 KLAVIVPCYNEE----LVIAESYRRTREALhklpvltEIIYINDGSRDRTRLMLDEIAASDPQVKVIHfSRNFGHQPAVT 78
Cdd:PRK10073    7 KLSIIIPLYNAGkdfrAFMESLIAQTWTAL-------EIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVARN 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1469545488  79 AGINNCDADLAVILDADMQDPPELIPSILELQEKE-----QANVVYCVRKSREGEGLF 131
Cdd:PRK10073   79 TGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDdldvaQCNADWCFRDTGETWQSI 136
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
4-164 5.68e-07

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 50.15  E-value: 5.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   4 LAVIVPCYNEELVIAESYRRT----REALHKLPVLT-EIIYINDGSRDRT-----RLMLDEIaASDPQVKVIHFSRNFGH 73
Cdd:PTZ00260   72 LSIVIPAYNEEDRLPKMLKETikylESRSRKDPKFKyEIIIVNDGSKDKTlkvakDFWRQNI-NPNIDIRLLSLLRNKGK 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488  74 QPAVTAGINNCDADLAVILDAD----MQDPPELIPSILELQEKEQANVVYCVRKSREGEGL-----FKKVTAKAFYRMLN 144
Cdd:PTZ00260  151 GGAVRIGMLASRGKYILMVDADgatdIDDFDKLEDIMLKIEQNGLGIVFGSRNHLVDSDVVakrkwYRNILMYGFHFIVN 230
                         170       180
                  ....*....|....*....|
gi 1469545488 145 YMSDVNFPLDTGDFRLIDRK 164
Cdd:PTZ00260  231 TICGTNLKDTQCGFKLFTRE 250
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
4-74 1.34e-06

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 48.28  E-value: 1.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469545488   4 LAVIVPCYNEELVIAesyrRTREALHKLPVLTEIIYINDGSRDRTRlmldEIAASDPqVKVIHFSRNFGHQ 74
Cdd:TIGR04283   1 LSIIIPVLNEAATLP----ELLADLQALRGDAEVIVVDGGSTDGTV----EIARSLG-AKVIHSPKGRARQ 62
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
6-65 3.07e-06

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 46.99  E-value: 3.07e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNEELVIAesyrRTREALHKLPVLTEIIYINDGSRDRTrLMLDEIAASDPQVKVI 65
Cdd:cd06436     1 VLVPCLNEEAVIQ----RTLASLLRNKPNFLVLVIDDASDDDT-AGIVRLAITDSRVHLL 55
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
3-120 1.83e-05

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 44.89  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   3 KLAVIVPCYNEEL---------VIAESYRRTrealhklpvltEIIYINDGSRDR-TRLMLDEIAASDPQVKVIHFSRNfG 72
Cdd:cd04184     2 LISIVMPVYNTPEkylreaiesVRAQTYPNW-----------ELCIADDASTDPeVKRVLKKYAAQDPRIKVVFREEN-G 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1469545488  73 HQPAVT-AGINNCDADLAVILDADmqDppELIPS-----ILELQEKEQANVVYC 120
Cdd:cd04184    70 GISAATnSALELATGEFVALLDHD--D--ELAPHalyevVKALNEHPDADLIYS 119
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
3-96 8.66e-04

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 39.86  E-value: 8.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   3 KLAVIVPCYNEELVIAesyRRT-REALH-KLPVLTEIIYI-NDGSRDRTRLMLDEIAAsdpQVKVIHFSRNFGHQpaVTA 79
Cdd:cd06421     2 TVDVFIPTYNEPLEIV---RKTlRAALAiDYPHDKLRVYVlDDGRRPELRALAAELGV---EYGYRYLTRPDNRH--AKA 73
                          90       100
                  ....*....|....*....|..
gi 1469545488  80 G-INN----CDADLAVILDADM 96
Cdd:cd06421    74 GnLNNalahTTGDFVAILDADH 95
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-112 4.14e-03

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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 37.15  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   6 VIVPCYNeelviaeSYRRTREALHKLPVLT----EIIYINDGSRDRTRlmlDEIAASDPQVKVIHFSRNFGHQPAVTAGI 81
Cdd:cd04186     1 IIIVNYN-------SLEYLKACLDSLLAQTypdfEVIVVDNASTDGSV---ELLRELFPEVRLIRNGENLGFGAGNNQGI 70
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1469545488  82 NNCDADLAVILDADMQDPPELIPSILELQEK 112
Cdd:cd04186    71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQ 101
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
4-122 4.41e-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: 38.00  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545488   4 LAVIVPCYNEELVIAESYRRTREALHKLpvltEIIYINDGsRDRTRLMLDEIAASDPQVKVIHFSRNfGHQPAVTAGINN 83
Cdd:cd06434     2 VTVIIPVYDEDPDVFRECLRSILRQKPL----EIIVVTDG-DDEPYLSILSQTVKYGGIFVITVPHP-GKRRALAEGIRH 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1469545488  84 CDADLAVILDADMQDPPELIPSILELQEKEQ-ANVVYCVR 122
Cdd:cd06434    76 VTTDIVVLLDSDTVWPPNALPEMLKPFEDPKvGGVGTNQR 115
 
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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