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Conserved domains on  [gi|1802450227|dbj|BBK61075|]
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glycosyl transferase [Amedibacterium intestinale]

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|16037492|10521532
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 ...
 7-195 1.85e-71

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: 218.89  E-value: 1.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEEVLHETARQLKEKIEimiskgTISNQSRIMFVNDGSKDKTWSIIKELHNKDSLFSGLNLSRNRGHQNALLA 86
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLE------SLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227  87 GLMTAKDlsDVTISLDADLQDDIHVIDRFIEKYHDGYDVVYGVRSSRaKDTWFKRNTALAFYRFQEKM-GVNSVYNHADY 165
Cdd:cd04187    75 GLDHARG--DAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNR-KESWLKRLTSKLFYRLINKLsGVDIPDNGGDF 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 1802450227 166 RLMSKRALEALSQFKEVNLFLRGLVPLVGF 195
Cdd:cd04187   152 RLMDRKVVDALLLLPERHRFLRGLIAWVGF 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 ...
 7-195 1.85e-71

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: 218.89  E-value: 1.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEEVLHETARQLKEKIEimiskgTISNQSRIMFVNDGSKDKTWSIIKELHNKDSLFSGLNLSRNRGHQNALLA 86
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLE------SLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227  87 GLMTAKDlsDVTISLDADLQDDIHVIDRFIEKYHDGYDVVYGVRSSRaKDTWFKRNTALAFYRFQEKM-GVNSVYNHADY 165
Cdd:cd04187    75 GLDHARG--DAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNR-KESWLKRLTSKLFYRLINKLsGVDIPDNGGDF 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 1802450227 166 RLMSKRALEALSQFKEVNLFLRGLVPLVGF 195
Cdd:cd04187   152 RLMDRKVVDALLLLPERHRFLRGLIAWVGF 181
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 7-317 1.94e-36

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 133.32  E-value: 1.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEEVLHETARQLKEKIEimiskgTISNQSRIMFVNDGSKDKTWSIIKELHNK-DSLFSGLNLSRNRGHQNALL 85
Cdd:PRK10714   10 VVIPVYNEQESLPELIRRTTAACE------SLGKEYEILLIDDGSSDNSAEMLVEAAQApDSHIVAILLNRNYGQHSAIM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227  86 AGLMTAKdlSDVTISLDADLQDDIHVIDRFIEKYHDGYDVVYGVRSSRaKDTWFKRNTALAFYRFQEKMGVNSVynhADY 165
Cdd:PRK10714   84 AGFSHVT--GDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNR-QDSWFRKTASKMINRLIQRTTGKAM---GDY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227 166 RLM----SKRALEALSQFKEVNLFLRGLVPLVGFDSCIVEYERNERFAGESKYPLKKMLSFAWDGITSFSIKPIRFVTLI 241
Cdd:PRK10714  158 GCMlrayRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227 242 GIII----FVVSILVTfycIIRKLMGD--TVDGWTFLSCSIWVLGGIQLLSIGIVGEYIGKIYSETKARPRYIIKEILDE 315
Cdd:PRK10714  238 GSIIaiggFSLAVLLV---VLRLTFGPqwAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRP 314


                  ..
gi 1802450227 316 KT 317
Cdd:PRK10714  315 SS 316
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 8-223 4.08e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 115.95  E-value: 4.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   8 VIPCYNEEEVLHET----ARQLKEKIEIMIskgtisnqsrimfVNDGSKDKTWSIIKELHNKDSLFSGLNLSRNRGHQNA 83
Cdd:COG0463     7 VIPTYNEEEYLEEAleslLAQTYPDFEIIV-------------VDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227  84 LLAGLMTAKdlSDVTISLDADLQDDIHVIDRFIEKYHD-GYDVVYGVRSSRAKDTWFKRNTALAFYRFqeKMGVNSVYNH 162
Cdd:COG0463    74 RNAGLAAAR--GDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFNLV--RLLTNLPDST 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1802450227 163 ADYRLMSKRALEALSqFKEVNLFLRGLVPLV--GFDSCIVEYERNErfaGESKYPLKKMLSFA 223
Cdd:COG0463   150 SGFRLFRREVLEELG-FDEGFLEDTELLRALrhGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-174 3.79e-21

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: 88.22  E-value: 3.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEEVLHET----ARQLKEKIEIMIskgtisnqsrimfVNDGSKDKTWSIIKELHNKDSLFSGLNLSRNRGHQN 82
Cdd:pfam00535   2 VIIPTYNEEKYLLETleslLNQTYPNFEIIV-------------VDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227  83 ALLAGLMTAKdlSDVTISLDADLQDDIHVIDRFIEKY-HDGYDVVYGVR-SSRAKDTWFKRNTALAFYRFQEKMGVNSVY 160
Cdd:pfam00535  69 ARNAGLRAAT--GDYIAFLDADDEVPPDWLEKLVEALeEDGADVVVGSRyVIFGETGEYRRASRITLSRLPFFLGLRLLG 146

                         170
                  ....*....|....*....
gi 1802450227 161 -----NHADYRLMSKRALE 174
Cdd:pfam00535 147 lnlpfLIGGFALYRREALE 165
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 8-118 1.64e-04

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: 42.11  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   8 VIPCYNEEEVLHET---ARQLKEKIEIMISKGtisnqsrimfvndGSKDKTWSIIKELHNKdslfsGLNLSRNRGHQnaL 84
Cdd:TIGR04283   4 IIPVLNEAATLPELladLQALRGDAEVIVVDG-------------GSTDGTVEIARSLGAK-----VIHSPKGRARQ--M 63

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1802450227  85 LAGLMTAKdlSDVTISLDAD--LQDD-IHVIDRFIEK 118
Cdd:TIGR04283  64 NAGAALAK--GDILLFLHADtrLPKDfLEAIRRALAK 98
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 7-195 1.85e-71

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: 218.89  E-value: 1.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEEVLHETARQLKEKIEimiskgTISNQSRIMFVNDGSKDKTWSIIKELHNKDSLFSGLNLSRNRGHQNALLA 86
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLE------SLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227  87 GLMTAKDlsDVTISLDADLQDDIHVIDRFIEKYHDGYDVVYGVRSSRaKDTWFKRNTALAFYRFQEKM-GVNSVYNHADY 165
Cdd:cd04187    75 GLDHARG--DAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNR-KESWLKRLTSKLFYRLINKLsGVDIPDNGGDF 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 1802450227 166 RLMSKRALEALSQFKEVNLFLRGLVPLVGF 195
Cdd:cd04187   152 RLMDRKVVDALLLLPERHRFLRGLIAWVGF 181
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 7-195 7.61e-49

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: 161.20  E-value: 7.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEEVLHETARQLKEKIEImiskgtiSNQSRIMFVNDGSKDKTWSIIKELHNKDSLFSGLNLSRNRGHQNALLA 86
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEE-------GYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227  87 GLMTAKDlsDVTISLDADLQDDIHVIDRFIEK-YHDGYDVVYGVRSSR---AKDTWFKRNTALAFYRFQEKM-GVNSVYN 161
Cdd:cd04179    74 GFKAARG--DIVVTMDADLQHPPEDIPKLLEKlLEGGADVVIGSRFVRgggAGMPLLRRLGSRLFNFLIRLLlGVRISDT 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1802450227 162 HADYRLMSKRALEALSQFKEVNLFLRGLVPLVGF 195
Cdd:cd04179   152 QSGFRLFRREVLEALLSLLESNGFEFGLELLVGA 185
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 7-317 1.94e-36

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 133.32  E-value: 1.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEEVLHETARQLKEKIEimiskgTISNQSRIMFVNDGSKDKTWSIIKELHNK-DSLFSGLNLSRNRGHQNALL 85
Cdd:PRK10714   10 VVIPVYNEQESLPELIRRTTAACE------SLGKEYEILLIDDGSSDNSAEMLVEAAQApDSHIVAILLNRNYGQHSAIM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227  86 AGLMTAKdlSDVTISLDADLQDDIHVIDRFIEKYHDGYDVVYGVRSSRaKDTWFKRNTALAFYRFQEKMGVNSVynhADY 165
Cdd:PRK10714   84 AGFSHVT--GDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNR-QDSWFRKTASKMINRLIQRTTGKAM---GDY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227 166 RLM----SKRALEALSQFKEVNLFLRGLVPLVGFDSCIVEYERNERFAGESKYPLKKMLSFAWDGITSFSIKPIRFVTLI 241
Cdd:PRK10714  158 GCMlrayRRHIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227 242 GIII----FVVSILVTfycIIRKLMGD--TVDGWTFLSCSIWVLGGIQLLSIGIVGEYIGKIYSETKARPRYIIKEILDE 315
Cdd:PRK10714  238 GSIIaiggFSLAVLLV---VLRLTFGPqwAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQVVRP 314


                  ..
gi 1802450227 316 KT 317
Cdd:PRK10714  315 SS 316
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 8-223 4.08e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 115.95  E-value: 4.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   8 VIPCYNEEEVLHET----ARQLKEKIEIMIskgtisnqsrimfVNDGSKDKTWSIIKELHNKDSLFSGLNLSRNRGHQNA 83
Cdd:COG0463     7 VIPTYNEEEYLEEAleslLAQTYPDFEIIV-------------VDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227  84 LLAGLMTAKdlSDVTISLDADLQDDIHVIDRFIEKYHD-GYDVVYGVRSSRAKDTWFKRNTALAFYRFqeKMGVNSVYNH 162
Cdd:COG0463    74 RNAGLAAAR--GDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFNLV--RLLTNLPDST 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1802450227 163 ADYRLMSKRALEALSqFKEVNLFLRGLVPLV--GFDSCIVEYERNErfaGESKYPLKKMLSFA 223
Cdd:COG0463   150 SGFRLFRREVLEELG-FDEGFLEDTELLRALrhGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-174 3.79e-21

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: 88.22  E-value: 3.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEEVLHET----ARQLKEKIEIMIskgtisnqsrimfVNDGSKDKTWSIIKELHNKDSLFSGLNLSRNRGHQN 82
Cdd:pfam00535   2 VIIPTYNEEKYLLETleslLNQTYPNFEIIV-------------VDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227  83 ALLAGLMTAKdlSDVTISLDADLQDDIHVIDRFIEKY-HDGYDVVYGVR-SSRAKDTWFKRNTALAFYRFQEKMGVNSVY 160
Cdd:pfam00535  69 ARNAGLRAAT--GDYIAFLDADDEVPPDWLEKLVEALeEDGADVVVGSRyVIFGETGEYRRASRITLSRLPFFLGLRLLG 146

                         170
                  ....*....|....*....
gi 1802450227 161 -----NHADYRLMSKRALE 174
Cdd:pfam00535 147 lnlpfLIGGFALYRREALE 165
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 7-149 4.39e-15

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: 72.60  E-value: 4.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEEVLhetARQLKEKIEIMISKgtISNQSRIMFVNDGSKDKTWSIIKEL-HNKDSLFSGLNLSRNRGHQNALL 85
Cdd:cd04188     1 VVIPAYNEEKRL---PPTLEEAVEYLEER--PSFSYEIIVVDDGSKDGTAEVARKLaRKNPALIRVLTLPKNRGKGGAVR 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802450227  86 AGLMTAKdlSDVTISLDADLQDDIHVIDRFIEKY-HDGYDVVYGVRSSRAKDTWFKRNtalaFYR 149
Cdd:cd04188    76 AGMLAAR--GDYILFADADLATPFEELEKLEEALkTSGYDIAIGSRAHLASAAVVKRS----WLR 134
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 7-151 3.00e-11

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: 61.09  E-value: 3.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEEVLHETARQLK----EKIEIMIskgtisnqsrimfVNDGSKDKTWSIIKEL---HNKDSLFsgLNLSRNRG 79
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLaldyPKLEVIV-------------VDDGSTDDTLEILEELaalYIRRVLV--VRDKENGG 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802450227  80 HQNALLAGLMTAKdlSDVTISLDAD--LQDD-IHVIDRFIEKYHDGYDVVYGVRSSRAKDTWFKRNTALAFYRFQ 151
Cdd:cd06423    66 KAGALNAGLRHAK--GDIVVVLDADtiLEPDaLKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIF 138
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 8-104 9.36e-10

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: 58.60  E-value: 9.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   8 VIPCYNEEEVLHETARQL------KEKIEIMIskgtisnqsrimfVNDGSKDKTWSIIKELHNKDSLFSGLNLSRNRGHQ 81
Cdd:COG1215    34 IIPAYNEEAVIEETLRSLlaqdypKEKLEVIV-------------VDDGSTDETAEIARELAAEYPRVRVIERPENGGKA 100

                          90       100
                  ....*....|....*....|...
gi 1802450227  82 NALLAGLMTAKdlSDVTISLDAD 104
Cdd:COG1215   101 AALNAGLKAAR--GDIVVFLDAD 121
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 7-224 1.21e-09

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: 57.54  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEeevlhetarqlKEKIEIMISKgtISNQSR-----IMFVNDGSKDKTWSIIKELHNKDSLFSGLNLSRNRGHQ 81
Cdd:cd06442     1 IIIPTYNE-----------RENIPELIER--LDAALKgidyeIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227  82 NALLAGLMTAkdLSDVTISLDADLQDDIHVIDRFIEKYHD-GYDVVYG---VRSSRAKDTWFKRN----TALAFYRFQEK 153
Cdd:cd06442    68 SAYIEGFKAA--RGDVIVVMDADLSHPPEYIPELLEAQLEgGADLVIGsryVEGGGVEGWGLKRKlisrGANLLARLLLG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227 154 MGVnsvynhAD----YRLMSKRALEALSQfkevNLFLRG-------LVPLVGFDSCIVE--YERNERFAGESKYPLKKML 220
Cdd:cd06442   146 RKV------SDptsgFRAYRREVLEKLID----SLVSKGykfqlelLVRARRLGYRIVEvpITFVDREHGESKLGGKEIV 215


                  ....
gi 1802450227 221 SFAW 224
Cdd:cd06442   216 EYLK 219
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 8-155 3.27e-09

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: 54.82  E-value: 3.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   8 VIPCYNEEEVLHET----ARQLKEKIEIMIskgtisnqsrimfVNDGSKDKTWSIIKELHNKDSLFSGLNLSRNRGHQNA 83
Cdd:cd00761     2 IIPAYNEEPYLERCleslLAQTYPNFEVIV-------------VDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAA 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802450227  84 LLAGLMTAKdlSDVTISLDAD--LQDDIHVIDRFIEKYHDGYDVVYGVRSSrakdtWFKRNTALAFYRFQEKMG 155
Cdd:cd00761    69 RNAGLKAAR--GEYILFLDADdlLLPDWLERLVAELLADPEADAVGGPGNL-----LFRRELLEEIGGFDEALL 135
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 5-172 7.83e-09

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 55.93  E-value: 7.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   5 LYLVIPCYNEEEVLhetARQLKEKIEIM--ISKGTISNQSRIMFVNDGSKDKTWSI----IKELHNKDSLFSGLNLSRNR 78
Cdd:PTZ00260   72 LSIVIPAYNEEDRL---PKMLKETIKYLesRSRKDPKFKYEIIIVNDGSKDKTLKVakdfWRQNINPNIDIRLLSLLRNK 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227  79 GHQNALLAGLMTAkdLSDVTISLDADLQDDIHVIDRFIEKYH----DGYDVVYGVRS------SRAKDTWFKRNTALAFY 148
Cdd:PTZ00260  149 GKGGAVRIGMLAS--RGKYILMVDADGATDIDDFDKLEDIMLkieqNGLGIVFGSRNhlvdsdVVAKRKWYRNILMYGFH 226

                         170       180
                  ....*....|....*....|....*
gi 1802450227 149 RFQEKM-GVNSVYNHADYRLMSKRA 172
Cdd:PTZ00260  227 FIVNTIcGTNLKDTQCGFKLFTRET 251
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 7-121 2.40e-07

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: 51.04  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEEVLHETARQL------KEKIEIMIskgtisnqsrimfVNDGSKDKTWSIIKE-LHNKDSLfsgLNLSRNRG 79
Cdd:cd06439    33 IIIPAYNEEAVIEAKLENLlaldypRDRLEIIV-------------VSDGSTDGTAEIAREyADKGVKL---LRFPERRG 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1802450227  80 HQNALLAGLMTAKdlSDVTISLDADLQDDIHVIDRFIEKYHD 121
Cdd:cd06439    97 KAAALNRALALAT--GEIVVFTDANALLDPDALRLLVRHFAD 136
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-151 7.81e-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: 43.05  E-value: 7.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEEVLHETARQL------KEKIEIMIskgtisnqsrimfVNDGSKDKTWSIIKELHNKDSLF-SGLNLSR--N 77
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLsaldypKEKFEVIL-------------VDDHSTDGTVQILEFAAAKPNFQlKILNNSRvsI 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1802450227  78 RGHQNALLAGLMTAKdlSDVTISLDAD---LQDDIHVIDRFIEKYHDGyDVVYGVRssrakdtwFKRNTALaFYRFQ 151
Cdd:cd04192    68 SGKKNALTTAIKAAK--GDWIVTTDADcvvPSNWLLTFVAFIQKEQIG-LVAGPVI--------YFKGKSL-LAKFQ 132
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 5-156 1.37e-04

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: 42.36  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   5 LYLVIPCYNEEEVLHETARQlkekieimISKGTISNqSRIMFVNDGSKDKTWSIIKEL-----HNKDSLFSGLNLSRNRG 79
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEA--------ILAQPYPP-VEVVVVVNPSDAETLDVAEEIaarfpDVRLRVIRNARLLGPTG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227  80 HQNALLAGLMTAKdlSDVTISLDADlqDDIHviDRFIEKY-----HDGYDVVYGVRSSRAKDTWFKRNTALAFY-RFQEK 153
Cdd:pfam13641  75 KSRGLNHGFRAVK--SDLVVLHDDD--SVLH--PGTLKKYvqyfdSPKVGAVGTPVFSLNRSTMLSALGALEFAlRHLRM 148


                  ...
gi 1802450227 154 MGV 156
Cdd:pfam13641 149 MSL 151
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 8-118 1.64e-04

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: 42.11  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   8 VIPCYNEEEVLHET---ARQLKEKIEIMISKGtisnqsrimfvndGSKDKTWSIIKELHNKdslfsGLNLSRNRGHQnaL 84
Cdd:TIGR04283   4 IIPVLNEAATLPELladLQALRGDAEVIVVDG-------------GSTDGTVEIARSLGAK-----VIHSPKGRARQ--M 63

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1802450227  85 LAGLMTAKdlSDVTISLDAD--LQDD-IHVIDRFIEK 118
Cdd:TIGR04283  64 NAGAALAK--GDILLFLHADtrLPKDfLEAIRRALAK 98
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 7-66 3.08e-04

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: 41.45  E-value: 3.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEevlhetaRQLKEKIEIMISKGTISNQSRIMFVNDGSKDKTWSIIKELHNKD 66
Cdd:cd02525     4 IIIPVRNEE-------KYIEELLESLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKD 56
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 7-121 5.66e-03

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: 37.36  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450227   7 LVIPCYNEEEVLHETARQLKEkieimiskgtISNQSRIMFVNDGSKDKTWSIIK-ELHNkdslfSGLNLSR------NRG 79
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLR----------NKPNFLVLVIDDASDDDTAGIVRlAITD-----SRVHLLRrhlpnaRTG 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1802450227  80 HQNALLAGLMTAK--------DLSDVTIS-LDADLQDDIHVIDRFIEKYHD 121
Cdd:cd06436    66 KGDALNAAYDQIRqilieegaDPERVIIAvIDADGRLDPNALEAVAPYFSD 116
 
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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