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Conserved domains on  [gi|518491542|ref|WP_019661749|]
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MULTISPECIES: glycosyltransferase family 2 protein [Stenotrophomonas]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135280)

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|12200473|10508766
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 8-185 2.94e-48

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: 157.35  E-value: 2.94e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   8 VVVPVFNERDNVAPLVAEITAALRGRLPFEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQSGQSTAVRTGVKHARA 87
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  88 PWIATLDGDGQNDPADIPKllAARDAADAQVKLFAGWRVNRQ----DSSSKRWASRWANAIRARMLRDDTPDTGCGIKLF 163
Cdd:cd04179   81 DIVVTMDADLQHPPEDIPK--LLEKLLEGGADVVIGSRFVRGggagMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLF 158

                        170       180
                 ....*....|....*....|..
gi 518491542 164 ERSAFLDLPYFDHMHRYLPALM 185
Cdd:cd04179  159 RREVLEALLSLLESNGFEFGLE 180
 
Name Accession Description Interval E-value
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 8-185 2.94e-48

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: 157.35  E-value: 2.94e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   8 VVVPVFNERDNVAPLVAEITAALRGRLPFEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQSGQSTAVRTGVKHARA 87
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  88 PWIATLDGDGQNDPADIPKllAARDAADAQVKLFAGWRVNRQ----DSSSKRWASRWANAIRARMLRDDTPDTGCGIKLF 163
Cdd:cd04179   81 DIVVTMDADLQHPPEDIPK--LLEKLLEGGADVVIGSRFVRGggagMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLF 158

                        170       180
                 ....*....|....*....|..
gi 518491542 164 ERSAFLDLPYFDHMHRYLPALM 185
Cdd:cd04179  159 RREVLEALLSLLESNGFEFGLE 180
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 3-210 5.87e-43

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 144.46  E-value: 5.87e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   3 QPELSVVVPVFNERDNVAPLVAEITAALRGrlPFEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQSGQSTAVRTGV 82
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYP--DFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  83 KHARAPWIATLDGDGQNDPADIPKllAARDAADAQVKLFAGWRVNRQDSS-SKRWASRWANAIRARMlrdDTPDTGCGIK 161
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEE--LVAALEEGPADLVYGSRLIREGESdLRRLGSRLFNLVRLLT---NLPDSTSGFR 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518491542 162 LFERSAFLDLPyFDHMHRYLPAL--MQRAGWKTTSVPVNHRhrtAGVSKYN 210
Cdd:COG0463  154 LFRREVLEELG-FDEGFLEDTELlrALRHGFRIAEVPVRYR---AGESKLN 200
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-168 1.93e-24

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: 95.15  E-value: 1.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542    7 SVVVPVFNERDNVAPLVAEITAalRGRLPFEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQSGQSTAVRTGVKHAR 86
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN--QTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   87 APWIATLDGDGQNDPADIPKLLAARDAADAQVklFAGWRVNRQDS------SSKRWASRWANAIRARMLRDDTPDTGCGI 160
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADV--VVGSRYVIFGEtgeyrrASRITLSRLPFFLGLRLLGLNLPFLIGGF 156


                  ....*...
gi 518491542  161 KLFERSAF 168
Cdd:pfam00535 157 ALYRREAL 164
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 5-210 4.44e-21

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 89.79  E-value: 4.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   5 ELSVVVPVFNERDNVAPLVAEITAALRG-RLPFEIVYIDDHSRDDTLAVLQGlKATTPE---LRVLHHVNQsGQSTAVRT 80
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTTAACESlGKEYEILLIDDGSSDNSAEMLVE-AAQAPDshiVAILLNRNY-GQHSAIMA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  81 GVKHARAPWIATLDGDGQNDPADIPKLLAARDAADAQVKLFagwRVNRQDSSSKRWASRWANAIRARMLRDDTPDTGCGI 160
Cdd:PRK10714  85 GFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTV---RQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCML 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 518491542 161 KLFER---SAFLdlpyfdHMHR---YLPALMQRAGWKTTSVPVNHRHRTAGVSKYN 210
Cdd:PRK10714 162 RAYRRhivDAML------HCHErstFIPILANTFARRAIEIPVHHAEREFGDSKYS 211
 
Name Accession Description Interval E-value
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 8-185 2.94e-48

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: 157.35  E-value: 2.94e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   8 VVVPVFNERDNVAPLVAEITAALRGRLPFEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQSGQSTAVRTGVKHARA 87
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  88 PWIATLDGDGQNDPADIPKllAARDAADAQVKLFAGWRVNRQ----DSSSKRWASRWANAIRARMLRDDTPDTGCGIKLF 163
Cdd:cd04179   81 DIVVTMDADLQHPPEDIPK--LLEKLLEGGADVVIGSRFVRGggagMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRLF 158

                        170       180
                 ....*....|....*....|..
gi 518491542 164 ERSAFLDLPYFDHMHRYLPALM 185
Cdd:cd04179  159 RREVLEALLSLLESNGFEFGLE 180
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 8-189 8.83e-47

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: 153.40  E-value: 8.83e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   8 VVVPVFNERDNVAPLVAEITAALRG-RLPFEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQSGQSTAVRTGVKHAR 86
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESlGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  87 APWIATLDGDGQNDPADIPKLLAARDAADAQVklfAGWRVNRQDSSSKRWASRWANAIRARMLRDDTPDTGCGIKLFERS 166
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVV---YGVRKNRKESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRK 157

                        170       180
                 ....*....|....*....|...
gi 518491542 167 AFLDLPYFDHMHRYLPALMQRAG 189
Cdd:cd04187  158 VVDALLLLPERHRFLRGLIAWVG 180
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 3-210 5.87e-43

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 144.46  E-value: 5.87e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   3 QPELSVVVPVFNERDNVAPLVAEITAALRGrlPFEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQSGQSTAVRTGV 82
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYP--DFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  83 KHARAPWIATLDGDGQNDPADIPKllAARDAADAQVKLFAGWRVNRQDSS-SKRWASRWANAIRARMlrdDTPDTGCGIK 161
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEE--LVAALEEGPADLVYGSRLIREGESdLRRLGSRLFNLVRLLT---NLPDSTSGFR 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518491542 162 LFERSAFLDLPyFDHMHRYLPAL--MQRAGWKTTSVPVNHRhrtAGVSKYN 210
Cdd:COG0463  154 LFRREVLEELG-FDEGFLEDTELlrALRHGFRIAEVPVRYR---AGESKLN 200
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 8-228 3.06e-30

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: 111.86  E-value: 3.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   8 VVVPVFNERDNVAPLVAEITAALRGrLPFEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQSGQSTAVRTGVKHARA 87
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKG-IDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  88 PWIATLDGDGQNDPADIPKLLAARDAADAQVKL---------FAGWRVNRqdssskRWASRWANAIRARMLRDDTPDTGC 158
Cdd:cd06442   80 DVIVVMDADLSHPPEYIPELLEAQLEGGADLVIgsryvegggVEGWGLKR------KLISRGANLLARLLLGRKVSDPTS 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518491542 159 GIKLFERSAFLDLPyfDHM----HRYLPALMQRAGWKTTS---VPVNHRHRTAGVSKynnLGRAlVGIRDLRGVAWL 228
Cdd:cd06442  154 GFRAYRREVLEKLI--DSLvskgYKFQLELLVRARRLGYRiveVPITFVDREHGESK---LGGK-EIVEYLKGLLRL 224
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-168 1.93e-24

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: 95.15  E-value: 1.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542    7 SVVVPVFNERDNVAPLVAEITAalRGRLPFEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQSGQSTAVRTGVKHAR 86
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN--QTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   87 APWIATLDGDGQNDPADIPKLLAARDAADAQVklFAGWRVNRQDS------SSKRWASRWANAIRARMLRDDTPDTGCGI 160
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADV--VVGSRYVIFGEtgeyrrASRITLSRLPFFLGLRLLGLNLPFLIGGF 156


                  ....*...
gi 518491542  161 KLFERSAF 168
Cdd:pfam00535 157 ALYRREAL 164
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 8-201 1.02e-23

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: 94.56  E-value: 1.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   8 VVVPVFNERDNVAPLVAEITAALRGRLPF--EIVYIDDHSRDDTLAVLQGLKATTPEL-RVLHHVNQSGQSTAVRTGVKH 84
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYLEERPSFsyEIIVVDDGSKDGTAEVARKLARKNPALiRVLTLPKNRGKGGAVRAGMLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  85 ARAPWIATLDGDGQNDPADIPKLLAARDAADAQV----KLFAGWRVNRQDSSSKRWASRWANAIRARMLRDDTPDTGCGI 160
Cdd:cd04188   81 ARGDYILFADADLATPFEELEKLEEALKTSGYDIaigsRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLGLGIKDTQCGF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 518491542 161 KLFERSAFLDLpyFDHMH--RY-----LPALMQRAGWKTTSVPVNHRH 201
Cdd:cd04188  161 KLFTRDAARRL--FPRLHleRWafdveLLVLARRLGYPIEEVPVRWVE 206
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 5-210 4.44e-21

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 89.79  E-value: 4.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   5 ELSVVVPVFNERDNVAPLVAEITAALRG-RLPFEIVYIDDHSRDDTLAVLQGlKATTPE---LRVLHHVNQsGQSTAVRT 80
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTTAACESlGKEYEILLIDDGSSDNSAEMLVE-AAQAPDshiVAILLNRNY-GQHSAIMA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  81 GVKHARAPWIATLDGDGQNDPADIPKLLAARDAADAQVKLFagwRVNRQDSSSKRWASRWANAIRARMLRDDTPDTGCGI 160
Cdd:PRK10714  85 GFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTV---RQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCML 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 518491542 161 KLFER---SAFLdlpyfdHMHR---YLPALMQRAGWKTTSVPVNHRHRTAGVSKYN 210
Cdd:PRK10714 162 RAYRRhivDAML------HCHErstFIPILANTFARRAIEIPVHHAEREFGDSKYS 211
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 2-196 6.06e-20

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: 86.33  E-value: 6.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   2 SQPELSVVVPVFNERDNVAPLVAEITAALRGRLPFEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQSGQSTAVRTG 81
Cdd:COG1215   27 DLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAG 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  82 VKHARAPWIATLDGDGQNDPadipkllaardaadaqvklfagwrvnrqdssskrwasRWANAIRARMLRDDTPDTGCGIk 161
Cdd:COG1215  107 LKAARGDIVVFLDADTVLDP-------------------------------------DWLRRLVAAFADPGVGASGANL- 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 518491542 162 LFERSAFLDLPYFDHMH----RYLPALMQRAGWKTTSVP 196
Cdd:COG1215  149 AFRREALEEVGGFDEDTlgedLDLSLRLLRAGYRIVYVP 187
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 4-228 1.67e-17

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 78.59  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   4 PELSVVVPVFNERDNVAPLVAEITAALRGRLPFEIVYIDDHSRDDTLAVLQGLKATTPELRVL--HHVNQSGQSTAVRTG 81
Cdd:PLN02726   9 MKYSIIVPTYNERLNIALIVYLIFKALQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILlrPRPGKLGLGTAYIHG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  82 VKHARAPWIATLDGDGQNDPADIPKLLAARDAADAQVKL---------FAGWRVNRqdssskRWASRWANAIRARMLRDD 152
Cdd:PLN02726  89 LKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTgtryvkgggVHGWDLRR------KLTSRGANVLAQTLLWPG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542 153 TPDTGCGIKLFERSAFLDL-------PYFDHMHRYLPAlmQRAGWKTTSVPVNHRHRTAGVSKYNnlGRALVGIrdLRGV 225
Cdd:PLN02726 163 VSDLTGSFRLYKRSALEDLvssvvskGYVFQMEIIVRA--SRKGYRIEEVPITFVDRVYGESKLG--GSEIVQY--LKGL 236


                 ...
gi 518491542 226 AWL 228
Cdd:PLN02726 237 LYL 239
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 8-96 4.61e-15

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: 70.23  E-value: 4.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   8 VVVPVFNERDNVAPLVAEITAAlrGRLPFEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQSGQSTAVRTGVKHARA 87
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQ--TYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARG 78


                 ....*....
gi 518491542  88 PWIATLDGD 96
Cdd:cd00761   79 EYILFLDAD 87
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
2-96 1.02e-13

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 67.33  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   2 SQPELSVVVPVFNERDNVAPLVAEITAALRGrlPFEIVYIDDHSRDDTLAVLQGLKAttPELRVLHHVNQSGQSTAVRTG 81
Cdd:COG1216    1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYP--PFEVIVVDNGSTDGTAELLAALAF--PRVRVIRNPENLGFAAARNLG 76

                         90
                 ....*....|....*
gi 518491542  82 VKHARAPWIATLDGD 96
Cdd:COG1216   77 LRAAGGDYLLFLDDD 91
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 7-175 5.01e-12

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: 63.40  E-value: 5.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   7 SVVVPVFNERDNVAPLVAEITAALRGRLPFEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQSgQSTAVRTGVKHAR 86
Cdd:cd02525    3 SIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRI-QSAGLNIGIRNSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  87 APWIATLDGDgqndpADIPK---LLAARDAADAQVKLFAGWRVNRQDSSSKR---WA--SRWANAIRARMLRDDTP---D 155
Cdd:cd02525   82 GDIIIRVDAH-----AVYPKdyiLELVEALKRTGADNVGGPMETIGESKFQKaiaVAqsSPLGSGGSAYRGGAVKIgyvD 156

                        170       180
                 ....*....|....*....|
gi 518491542 156 TGCGIkLFERSAFLDLPYFD 175
Cdd:cd02525  157 TVHHG-AYRREVFEKVGGFD 175
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 6-178 8.57e-12

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 63.63  E-value: 8.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   6 LSVVVPVFNERDNVAPLVAEITAALRGRLP------FEIVYIDDHSRDDTLAVLQGL----KATTPELRVLHHVNQSGQS 75
Cdd:PTZ00260  72 LSIVIPAYNEEDRLPKMLKETIKYLESRSRkdpkfkYEIIIVNDGSKDKTLKVAKDFwrqnINPNIDIRLLSLLRNKGKG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542  76 TAVRTGVKHARAPWIATLDGDGQNDPADIPKLLAARDAADAQ-VKLFAGWRVNRQDSSSKRWASRWANA-------IRAR 147
Cdd:PTZ00260 152 GAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQNgLGIVFGSRNHLVDSDVVAKRKWYRNIlmygfhfIVNT 231

                        170       180       190
                 ....*....|....*....|....*....|.
gi 518491542 148 MLRDDTPDTGCGIKLFERSAFLDLpyFDHMH 178
Cdd:PTZ00260 232 ICGTNLKDTQCGFKLFTRETARII--FPSLH 260
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 8-101 1.71e-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: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   8 VVVPVFNERDNVAPLvaeITAALRGRLP-FEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQ-SGQSTAVRTGVKHA 85
Cdd:cd06423    1 IIVPAYNEEAVIERT---IESLLALDYPkLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEnGGKAGALNAGLRHA 77

                         90
                 ....*....|....*.
gi 518491542  86 RAPWIATLDGDGQNDP 101
Cdd:cd06423   78 KGDIVVVLDADTILEP 93
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 8-96 2.85e-09

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: 55.37  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   8 VVVPVFNERDNVAPLVAEITAALRGRLPFEIVYIDDHSRDDTLAVLQGLKA-TTPELRVLH--HVNQSGQSTAVRTGVKH 84
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYPKEKFEVILVDDHSTDGTVQILEFAAAkPNFQLKILNnsRVSISGKKNALTTAIKA 80

                         90
                 ....*....|..
gi 518491542  85 ARAPWIATLDGD 96
Cdd:cd04192   81 AKGDWIVTTDAD 92
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-96 5.06e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 49.66  E-value: 5.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   2 SQPELSVVVPVFNERDNVAPLVAEITAALRGRLpfEIVYIDDHSRDDTLAVLQGLKATTPELRVLHHVNQsGQSTAVRTG 81
Cdd:PRK10073   4 STPKLSIIIPLYNAGKDFRAFMESLIAQTWTAL--EIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANA-GVSVARNTG 80

                         90
                 ....*....|....*
gi 518491542  82 VKHARAPWIATLDGD 96
Cdd:PRK10073  81 LAVATGKYVAFPDAD 95
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 6-90 6.49e-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: 48.72  E-value: 6.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   6 LSVVVPVFNERDNVAPLVAeiTAALRGRLPFEIVYIDDHSRDDTLAVLQGLKAttpelrvlhHVNQSGQSTAV--RTGVK 83
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLA--SLRRLNPLPLEIIVVDGGSTDGTVAIARSAGV---------VVISSPKGRARqmNAGAA 69


                 ....*..
gi 518491542  84 HARAPWI 90
Cdd:cd02522   70 AARGDWL 76
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 6-96 3.52e-06

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: 46.51  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   6 LSVVVPVFNERDNvaplvaeITAALRGRLPF--EIVYIDDHSRDDTLAVLQGLKAttpelRVLHHVNQsGQSTAVRTGVK 83
Cdd:cd02511    2 LSVVIITKNEERN-------IERCLESVKWAvdEIIVVDSGSTDRTVEIAKEYGA-----KVYQRWWD-GFGAQRNFALE 68

                         90
                 ....*....|...
gi 518491542  84 HARAPWIATLDGD 96
Cdd:cd02511   69 LATNDWVLSLDAD 81
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 7-52 1.15e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 45.29  E-value: 1.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 518491542   7 SVVVPVFNERDNVAPLVAEITAALRGRLPFEIVYIDDHSRDDTLAV 52
Cdd:PRK13915  34 SVVLPALNEEETVGKVVDSIRPLLMEPLVDELIVIDSGSTDATAER 79
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 3-96 1.38e-05

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: 44.67  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542    3 QPELSVVVPVFNERDNVAPLVAEITAALRGrlPFEIVYIDDHSRDDTLAVLQGLKATTP--ELRVLHHVNQSGQSTAVRT 80
Cdd:pfam13641   1 PPDVSVVVPAFNEDSVLGRVLEAILAQPYP--PVEVVVVVNPSDAETLDVAEEIAARFPdvRLRVIRNARLLGPTGKSRG 78

                          90
                  ....*....|....*....
gi 518491542   81 ---GVKHARAPWIATLDGD 96
Cdd:pfam13641  79 lnhGFRAVKSDLVVLHDDD 97
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 4-101 9.94e-05

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 42.30  E-value: 9.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   4 PELSVVVPVFNERDNVAPLVaEITAAL---RGRLpfEIVYIDDhSRDDTLAVLQGL----KATTPELRVLHHVNQSG-QS 75
Cdd:cd06437    1 PMVTVQLPVFNEKYVVERLI-EAACALdypKDRL--EIQVLDD-STDETVRLAREIveeyAAQGVNIKHVRRADRTGyKA 76

                         90       100
                 ....*....|....*....|....*.
gi 518491542  76 TAVRTGVKHARAPWIATLDGDGQNDP 101
Cdd:cd06437   77 GALAEGMKVAKGEYVAIFDADFVPPP 102
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 2-101 3.97e-04

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: 40.64  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491542   2 SQPELSVVVPVFNERDNVAPLVAEITAALRGRLPFEIVYIDDHSRDDTLAVLQGLKAttPELRVLHHVNQSGQSTAVRTG 81
Cdd:cd06439   27 YLPTVTIIIPAYNEEAVIEAKLENLLALDYPRDRLEIIVVSDGSTDGTAEIAREYAD--KGVKLLRFPERRGKAAALNRA 104

                         90       100
                 ....*....|....*....|
gi 518491542  82 VKHARAPWIATLDGDGQNDP 101
Cdd:cd06439  105 LALATGEIVVFTDANALLDP 124
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 33-96 3.59e-03

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 37.17  E-value: 3.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518491542  33 RLPFEIVYIDDHSRDDTLAVLQGLKATTPeLRVLH--HVNQSGQSTAVRT-GVKHARAPWIATLDGD 96
Cdd:cd06420   24 ILPFEVIIADDGSTEETKELIEEFKSQFP-IPIKHvwQEDEGFRKAKIRNkAIAAAKGDYLIFIDGD 89
 
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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