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Conserved domains on  [gi|1119350963|ref|WP_072327751|]
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MULTISPECIES: glycosyltransferase family 2 protein [unclassified Paenibacillus]

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
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 ...
8-190 1.02e-38

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: 132.70  E-value: 1.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLRKQMAQGresalkmpsdnLEYELIVVDDGSRDGTAEAALPWAD-----KVVKHPRRRGKGA 82
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEG-----------YDYEIIVVDDGSTDGTAEIARELAArvprvRVIRLSRNFGKGA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963  83 ALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQGAADMCVA-RLTPcPGTGGFGLVRALAVRG----VRLLTGFEA 157
Cdd:cd04179    70 AVRAGFKAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGsRFVR-GGGAGMPLLRRLGSRLfnflIRLLLGVRI 148
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1119350963 158 SAPLSGQRALRAEALQALKRQ--YGGFGVEVGMFV 190
Cdd:cd04179   149 SDTQSGFRLFRREVLEALLSLleSNGFEFGLELLV 183
 
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 ...
8-190 1.02e-38

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: 132.70  E-value: 1.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLRKQMAQGresalkmpsdnLEYELIVVDDGSRDGTAEAALPWAD-----KVVKHPRRRGKGA 82
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEG-----------YDYEIIVVDDGSTDGTAEIARELAArvprvRVIRLSRNFGKGA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963  83 ALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQGAADMCVA-RLTPcPGTGGFGLVRALAVRG----VRLLTGFEA 157
Cdd:cd04179    70 AVRAGFKAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGsRFVR-GGGAGMPLLRRLGSRLfnflIRLLLGVRI 148
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1119350963 158 SAPLSGQRALRAEALQALKRQ--YGGFGVEVGMFV 190
Cdd:cd04179   149 SDTQSGFRLFRREVLEALLSLleSNGFEFGLELLV 183
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
5-216 1.01e-37

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 130.98  E-value: 1.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   5 KVTIIIPAWNEAQRLPLTLKTLRKQMAQgresalkmpsdnlEYELIVVDDGSRDGTAEAALPWAD-----KVVKHPRRRG 79
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYP-------------DFEIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963  80 KGAALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQGAADMCVARLTPCPGTGGFGLVRALAVRGVRLLTGFeaSA 159
Cdd:COG0463    70 KGAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNL--PD 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1119350963 160 PLSGQRALRAEALQALKRQyGGFGVEVGMFvDLLKLGYRVeeTEAPFMHRTTGKTWS 216
Cdd:COG0463   148 STSGFRLFRREVLEELGFD-EGFLEDTELL-RALRHGFRI--AEVPVRYRAGESKLN 200
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
7-138 8.28e-26

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: 98.62  E-value: 8.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   7 TIIIPAWNEAQRLPLTLKTLRKQmaqgresalkmpsDNLEYELIVVDDGSRDGTAEAALPWAD-----KVVKHPRRRGKG 81
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQ-------------TYPNFEIIVVDDGSTDGTVEIAEEYAKkdprvRVIRLPENRGKA 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1119350963  82 AALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQGAADMCVARLTPCPGTGGF 138
Cdd:pfam00535  68 GARNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGE 124
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
3-212 5.47e-20

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 85.52  E-value: 5.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   3 ATKVTIIIPAWNEAQRLPLTLKTLRKQMAqgresalkmpsDNLEYELIVVDDGSRDGTAEAA-----LPWADKVVKHPRR 77
Cdd:PLN02726    8 AMKYSIIVPTYNERLNIALIVYLIFKALQ-----------DVKDFEIIVVDDGSPDGTQDVVkqlqkVYGEDRILLRPRP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963  78 R--GKGAALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQGAADMCVA-RLTPCPGTGGFGLVRALAVRGVRLLTG 154
Cdd:PLN02726   77 GklGLGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGtRYVKGGGVHGWDLRRKLTSRGANVLAQ 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119350963 155 FEASA---PLSGQ-RALRAEALQAL--KRQYGGFGVEVGMFVDLLKLGYRVEETEAPFMHRTTG 212
Cdd:PLN02726  157 TLLWPgvsDLTGSfRLYKRSALEDLvsSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYG 220
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
6-102 1.03e-18

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: 81.40  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   6 VTIIIPAWNEAQRLPLTLKTLRkqmaqgresALKMPSdnleyELIVVDDGSRDGTAEAALPWADKVVKHPRRRGK----G 81
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQ---------ALRGDA-----EVIVVDGGSTDGTVEIARSLGAKVIHSPKGRARqmnaG 66
                          90       100
                  ....*....|....*....|.
gi 1119350963  82 AALesgwneSRGDILIFLDAD 102
Cdd:TIGR04283  67 AAL------AKGDILLFLHAD 81
 
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 ...
8-190 1.02e-38

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: 132.70  E-value: 1.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLRKQMAQGresalkmpsdnLEYELIVVDDGSRDGTAEAALPWAD-----KVVKHPRRRGKGA 82
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEG-----------YDYEIIVVDDGSTDGTAEIARELAArvprvRVIRLSRNFGKGA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963  83 ALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQGAADMCVA-RLTPcPGTGGFGLVRALAVRG----VRLLTGFEA 157
Cdd:cd04179    70 AVRAGFKAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGsRFVR-GGGAGMPLLRRLGSRLfnflIRLLLGVRI 148
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1119350963 158 SAPLSGQRALRAEALQALKRQ--YGGFGVEVGMFV 190
Cdd:cd04179   149 SDTQSGFRLFRREVLEALLSLleSNGFEFGLELLV 183
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
5-216 1.01e-37

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 130.98  E-value: 1.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   5 KVTIIIPAWNEAQRLPLTLKTLRKQMAQgresalkmpsdnlEYELIVVDDGSRDGTAEAALPWAD-----KVVKHPRRRG 79
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYP-------------DFEIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963  80 KGAALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQGAADMCVARLTPCPGTGGFGLVRALAVRGVRLLTGFeaSA 159
Cdd:COG0463    70 KGAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNL--PD 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1119350963 160 PLSGQRALRAEALQALKRQyGGFGVEVGMFvDLLKLGYRVeeTEAPFMHRTTGKTWS 216
Cdd:COG0463   148 STSGFRLFRREVLEELGFD-EGFLEDTELL-RALRHGFRI--AEVPVRYRAGESKLN 200
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
8-237 5.01e-32

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: 116.48  E-value: 5.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLRKQMaqgresalkmpsDNLEYELIVVDDGSRDGTAEAALPWA-----DKVVKHPRRRGKGA 82
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAAL------------KGIDYEIIVVDDNSPDGTAEIVRELAkeyprVRLIVRPGKRGLGS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963  83 ALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQGAADMCVA-RLTPCPGTGGFGLVRALAVRG----VRLLTGFEA 157
Cdd:cd06442    69 AYIEGFKAARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGsRYVEGGGVEGWGLKRKLISRGanllARLLLGRKV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963 158 SAPLSGQRALRAEALQALKRQY--GGFGVEVGMFVDLLKLGYRVEETEAPFMHRTTGKTWSGWMHrgrqflsVGRALWQC 235
Cdd:cd06442   149 SDPTSGFRAYRREVLEKLIDSLvsKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKE-------IVEYLKGL 221

                  ..
gi 1119350963 236 WR 237
Cdd:cd06442   222 LR 223
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
8-201 6.45e-30

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: 110.73  E-value: 6.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLRKQMAQGRESalkmpsdnlEYELIVVDDGSRDGTAEAALPWADK------VVKHPRRRGKG 81
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPSF---------SYEIIVVDDGSKDGTAEVARKLARKnpalirVLTLPKNRGKG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963  82 AALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQGAADMCVA-RLTP-------------CPGTGGFGLVRALAVR 147
Cdd:cd04188    72 GAVRAGMLAARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGsRAHLasaavvkrswlrnLLGRGFNFLVRLLLGL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1119350963 148 GVRlLT--GFeasaplsgqRALRAEALQAL--KRQYGGFGVEVGMFVDLLKLGYRVEE 201
Cdd:cd04188   152 GIK-DTqcGF---------KLFTRDAARRLfpRLHLERWAFDVELLVLARRLGYPIEE 199
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
7-138 8.28e-26

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: 98.62  E-value: 8.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   7 TIIIPAWNEAQRLPLTLKTLRKQmaqgresalkmpsDNLEYELIVVDDGSRDGTAEAALPWAD-----KVVKHPRRRGKG 81
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQ-------------TYPNFEIIVVDDGSTDGTVEIAEEYAKkdprvRVIRLPENRGKA 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1119350963  82 AALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQGAADMCVARLTPCPGTGGF 138
Cdd:pfam00535  68 GARNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGE 124
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
5-237 4.67e-24

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: 97.50  E-value: 4.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   5 KVTIIIPAWNEAQRLPLTLKTLRKQmaqgresalKMPSDNleYELIVVDDGSRDGTAEAALPWAD-----KVVKHPRRRG 79
Cdd:COG1215    30 RVSVIIPAYNEEAVIEETLRSLLAQ---------DYPKEK--LEVIVVDDGSTDETAEIARELAAeyprvRVIERPENGG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963  80 KGAALESGWNESRGDILIFLDADlglsAKHYPLLLKPVLQGAADMCVArltpCPGTGGfglvralavrgvrlltgfeasa 159
Cdd:COG1215    99 KAAALNAGLKAARGDIVVFLDAD----TVLDPDWLRRLVAAFADPGVG----ASGANL---------------------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963 160 plsgqrALRAEALQALkrqyGGFGVEVG-----MFVDLLKLGYRVEETEAPFMHRTTGKTWSGWMhrgRQFLSVGRALWQ 234
Cdd:COG1215   149 ------AFRREALEEV----GGFDEDTLgedldLSLRLLRAGYRIVYVPDAVVYEEAPETLRALF---RQRRRWARGGLQ 215

                  ...
gi 1119350963 235 CWR 237
Cdd:COG1215   216 LLL 218
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
8-102 5.14e-21

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: 86.51  E-value: 5.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLRKQmaqgresalkmpsDNLEYELIVVDDGSRDGTAEAALPWADK------VVKHPRRRGKG 81
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLAL-------------DYPKLEVIVVDDGSTDDTLEILEELAALyirrvlVVRDKENGGKA 67
                          90       100
                  ....*....|....*....|.
gi 1119350963  82 AALESGWNESRGDILIFLDAD 102
Cdd:cd06423    68 GALNAGLRHAKGDIVVVLDAD 88
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
3-212 5.47e-20

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 85.52  E-value: 5.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   3 ATKVTIIIPAWNEAQRLPLTLKTLRKQMAqgresalkmpsDNLEYELIVVDDGSRDGTAEAA-----LPWADKVVKHPRR 77
Cdd:PLN02726    8 AMKYSIIVPTYNERLNIALIVYLIFKALQ-----------DVKDFEIIVVDDGSPDGTQDVVkqlqkVYGEDRILLRPRP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963  78 R--GKGAALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQGAADMCVA-RLTPCPGTGGFGLVRALAVRGVRLLTG 154
Cdd:PLN02726   77 GklGLGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGtRYVKGGGVHGWDLRRKLTSRGANVLAQ 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119350963 155 FEASA---PLSGQ-RALRAEALQAL--KRQYGGFGVEVGMFVDLLKLGYRVEETEAPFMHRTTG 212
Cdd:PLN02726  157 TLLWPgvsDLTGSfRLYKRSALEDLvsSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYG 220
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
8-102 7.26e-20

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: 82.94  E-value: 7.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLRKQmaqgresalkmpsDNLEYELIVVDDGSRDGTAEAALPWADK-----VVKHPRRRGKGA 82
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQ-------------TYPNFEVIVVDDGSTDGTLEILEEYAKKdprviRVINEENQGLAA 67
                          90       100
                  ....*....|....*....|
gi 1119350963  83 ALESGWNESRGDILIFLDAD 102
Cdd:cd00761    68 ARNAGLKAARGEYILFLDAD 87
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
8-103 1.23e-19

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: 82.91  E-value: 1.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLRKQMAQgresalkmpsDNLEYELIVVDDGSRDGTAEAALPWAD-----KVVKHPRRRGKGA 82
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLES----------LGYDYEIIFVDDGSTDRTLEILRELAArdprvKVIRLSRNFGQQA 70
                          90       100
                  ....*....|....*....|.
gi 1119350963  83 ALESGWNESRGDILIFLDADL 103
Cdd:cd04187    71 ALLAGLDHARGDAVITMDADL 91
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
5-102 7.08e-19

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: 82.63  E-value: 7.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   5 KVTIIIPAWNEAQRLPLTLKTLRkqmaqgresALKMPSDNLEyeLIVVDDGSRDGTAEAALPWADKVVK---HPRRRGKG 81
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAKLENLL---------ALDYPRDRLE--IIVVSDGSTDGTAEIAREYADKGVKllrFPERRGKA 98
                          90       100
                  ....*....|....*....|.
gi 1119350963  82 AALESGWNESRGDILIFLDAD 102
Cdd:cd06439    99 AALNRALALATGEIVVFTDAN 119
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
6-102 1.03e-18

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: 81.40  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   6 VTIIIPAWNEAQRLPLTLKTLRkqmaqgresALKMPSdnleyELIVVDDGSRDGTAEAALPWADKVVKHPRRRGK----G 81
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQ---------ALRGDA-----EVIVVDGGSTDGTVEIARSLGAKVIHSPKGRARqmnaG 66
                          90       100
                  ....*....|....*....|.
gi 1119350963  82 AALesgwneSRGDILIFLDAD 102
Cdd:TIGR04283  67 AAL------AKGDILLFLHAD 81
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
7-119 3.77e-17

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 79.04  E-value: 3.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   7 TIIIPAWNEAQRLPLTLKTLRKQMAQGRESALKMpsdnlEYELIVVDDGSRDGTAEAALPWAD---------KVVKHPRR 77
Cdd:PTZ00260   73 SIVIPAYNEEDRLPKMLKETIKYLESRSRKDPKF-----KYEIIIVNDGSKDKTLKVAKDFWRqninpnidiRLLSLLRN 147
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1119350963  78 RGKGAALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQ 119
Cdd:PTZ00260  148 KGKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLK 189
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
5-102 9.44e-17

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 75.80  E-value: 9.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   5 KVTIIIPAWNEAQRLPLTLKTLRKQmaqgresalkmpsDNLEYELIVVDDGSRDGTAEAALPWAD---KVVKHPRRRGKG 81
Cdd:COG1216     4 KVSVVIPTYNRPELLRRCLESLLAQ-------------TYPPFEVIVVDNGSTDGTAELLAALAFprvRVIRNPENLGFA 70
                          90       100
                  ....*....|....*....|.
gi 1119350963  82 AALESGWNESRGDILIFLDAD 102
Cdd:COG1216    71 AARNLGLRAAGGDYLLFLDDD 91
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
4-195 8.29e-16

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 74.95  E-value: 8.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   4 TKVTIIIPAWNEAQRLPLTLKTLRKQMAQGresalkmpsdnLEYELIVVDDGSRDGTAEAA-------LPWADKVVKHPR 76
Cdd:PRK13915   31 RTVSVVLPALNEEETVGKVVDSIRPLLMEP-----------LVDELIVIDSGSTDATAERAaaagarvVSREEILPELPP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963  77 RRGKGAALESGWNESRGDILIFLDADL-GLSAKHYPLLLKPVLQGAADMCVA-------RLTPCPGTGGFGLVRALAVRG 148
Cdd:PRK13915  100 RPGKGEALWRSLAATTGDIVVFVDADLiNFDPMFVPGLLGPLLTDPGVHLVKafyrrplRVSGGVDATGGGRVTELVARP 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1119350963 149 V-RL----LTGFeaSAPLSGQRALRAEALQALkRQYGGFGVEVGMFVDLLKL 195
Cdd:PRK13915  180 LlNLlrpeLAGF--VQPLGGEYAGRRELLESL-PFVPGYGVEIGLLIDTLDR 228
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
6-102 7.30e-15

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: 71.06  E-value: 7.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   6 VTIIIPAWNEAQRLPLTLKTLRKQMAQgresalkmpsdnlEYELIVVDDGSRDGTAEAALPWADKVVKHPRRRGK----G 81
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPL-------------PLEIIVVDGGSTDGTVAIARSAGVVVISSPKGRARqmnaG 67
                          90       100
                  ....*....|....*....|.
gi 1119350963  82 AALesgwneSRGDILIFLDAD 102
Cdd:cd02522    68 AAA------ARGDWLLFLHAD 82
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-102 1.63e-13

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: 67.31  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLrkqmaqgreSALKMPSDNleYELIVVDDGSRDGTAEAALPWADK-----VVKHPRRR---G 79
Cdd:cd04192     1 VVIAARNEAENLPRLLQSL---------SALDYPKEK--FEVILVDDHSTDGTVQILEFAAAKpnfqlKILNNSRVsisG 69
                          90       100
                  ....*....|....*....|...
gi 1119350963  80 KGAALESGWNESRGDILIFLDAD 102
Cdd:cd04192    70 KKNALTTAIKAAKGDWIVTTDAD 92
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
5-146 7.44e-13

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: 66.10  E-value: 7.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   5 KVTIIIPAWNEAQRLPLTLKTLRKQmaqgresalKMPSDNleYELIVVDDGSRDGTAE-----AALPWADKVVKHPRRRg 79
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQ---------SYPKDL--IEIIVVDGGSTDGTREivqeyAAKDPRIRLIDNPKRI- 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119350963  80 KGAALESGWNESRGDILIFLDADlGLSAKHYPL-LLKPVLQGAADmCVARLTPCPGTGGFGLVRALAV 146
Cdd:cd02525    69 QSAGLNIGIRNSRGDIIIRVDAH-AVYPKDYILeLVEALKRTGAD-NVGGPMETIGESKFQKAIAVAQ 134
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
5-120 3.94e-11

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 61.68  E-value: 3.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   5 KVTIIIPAWNEAQRLPLTL-KTLR--KQMAQgresalkmpsdnlEYELIVVDDGSRDGTAEAALPWADKVVKH------P 75
Cdd:PRK10714    7 KVSVVIPVYNEQESLPELIrRTTAacESLGK-------------EYEILLIDDGSSDNSAEMLVEAAQAPDSHivaillN 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1119350963  76 RRRGKGAALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQG 120
Cdd:PRK10714   74 RNYGQHSAIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEG 118
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
7-102 6.15e-08

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 51.39  E-value: 6.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   7 TIIIPAWNEAQRLPLTLKTLRKQmaqgresalkmpsDNLEYELIVVDDGSRDGTAE---AALPWADKVVKHPrrrGKG-- 81
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQ-------------TYPNIEYIVIDGGSTDGTVDiikKYEDKITYWISEP---DKGiy 64
                          90       100
                  ....*....|....*....|.
gi 1119350963  82 AALESGWNESRGDILIFLDAD 102
Cdd:cd06433    65 DAMNKGIALATGDIIGFLNSD 85
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
8-102 2.12e-07

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 49.52  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLRkqmaqgresALKMPSDNleYELIVVDDGSRDGTAEAALPWADKVVK--HPRRRGKGAALE 85
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSLK---------AQDYPREL--YRIFVVADNCTDDTAQVARAAGATVLErhDPERRGKGYALD 69
                          90       100
                  ....*....|....*....|..
gi 1119350963  86 SGWNESRG-----DILIFLDAD 102
Cdd:cd06438    70 FGFRHLLNladdpDAVVVFDAD 91
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-123 5.42e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 49.66  E-value: 5.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   3 ATKVTIIIPAWNEAQRLPLTLKTLRKQmaqgRESALkmpsdnleyELIVVDDGSRDGTAEAALPWADKV----VKHPRRR 78
Cdd:PRK10073    5 TPKLSIIIPLYNAGKDFRAFMESLIAQ----TWTAL---------EIIIVNDGSTDNSVEIAKHYAENYphvrLLHQANA 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1119350963  79 GKGAALESGWNESRGDILIFLDADLGLSAKHYPLLLKPVLQGAAD 123
Cdd:PRK10073   72 GVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLD 116
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-102 1.98e-06

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: 46.40  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLRKQmaqgresalkmpsDNLEYELIVVDDGSRDGTAEAALPWADKVVKH--PRRRGKGAALE 85
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQ-------------TYPDFEVIVVDNASTDGSVELLRELFPEVRLIrnGENLGFGAGNN 67
                          90
                  ....*....|....*..
gi 1119350963  86 SGWNESRGDILIFLDAD 102
Cdd:cd04186    68 QGIREAKGDYVLLLNPD 84
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
5-102 8.92e-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: 45.36  E-value: 8.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   5 KVTIIIPAWNEAQRLPLTLKTLRKQMAqgresalkmpsdnleyELIVVDDGSRDGTAEAALPWADKVVKHPRR---RGKG 81
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVKWAVD----------------EIIVVDSGSTDRTVEIAKEYGAKVYQRWWDgfgAQRN 64
                          90       100
                  ....*....|....*....|.
gi 1119350963  82 AALESgwneSRGDILIFLDAD 102
Cdd:cd02511    65 FALEL----ATNDWVLSLDAD 81
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
6-116 3.88e-05

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: 43.40  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   6 VTIIIPAWNEAqrLPLTLKTLRkqmaqgreSALKMPSDnleyELIVVDDGSRDGTAE---AALPWADKVVKHPRRRGKGA 82
Cdd:cd06434     2 VTVIIPVYDED--PDVFRECLR--------SILRQKPL----EIIVVTDGDDEPYLSilsQTVKYGGIFVITVPHPGKRR 67
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1119350963  83 ALESGWNESRGDILIFLDADLGLSAKHYPLLLKP 116
Cdd:cd06434    68 ALAEGIRHVTTDIVVLLDSDTVWPPNALPEMLKP 101
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
8-102 4.99e-05

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: 42.56  E-value: 4.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLRKQmaqgresalkmpsDNLEYELIVVDDGSRDGTAEAALPWADKV---VKH---------- 74
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQ-------------SILPFEVIIADDGSTEETKELIEEFKSQFpipIKHvwqedegfrk 67
                          90       100
                  ....*....|....*....|....*...
gi 1119350963  75 PRRRGKGAAlesgwnESRGDILIFLDAD 102
Cdd:cd06420    68 AKIRNKAIA------AAKGDYLIFIDGD 89
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
7-101 7.16e-05

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 42.96  E-value: 7.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   7 TIIIPAWNEAqRLPLtLKTLRkqmaqgreSALKMPSDNLEYELIVVDDGSRDGTAEAAL--------PWAdKVVKHPRRR 78
Cdd:cd02510     1 SVIIIFHNEA-LSTL-LRTVH--------SVINRTPPELLKEIILVDDFSDKPELKLLLeeyykkylPKV-KVLRLKKRE 69
                          90       100
                  ....*....|....*....|...
gi 1119350963  79 GKGAALESGWNESRGDILIFLDA 101
Cdd:cd02510    70 GLIRARIAGARAATGDVLVFLDS 92
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
8-107 1.44e-04

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: 41.60  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLRKQMAQGResalkmpsdnleyeLIVVDDGSRDGTAEAALPWAD----KVVKHPR---RRGK 80
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRNKPNFL--------------VLVIDDASDDDTAGIVRLAITdsrvHLLRRHLpnaRTGK 66
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1119350963  81 GAALESGWN----------ESRGDILI-FLDADLGLSA 107
Cdd:cd06436    67 GDALNAAYDqirqilieegADPERVIIaVIDADGRLDP 104
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
14-102 5.35e-04

Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative glucosyltransferases,


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 38.00  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963  14 NEAQRLPLTLKTLRkqmAQGREsalkmpsdnleyELIVVDDGSRDGTAEAALPWADKVVKHPRRRGKGAALESGW----- 88
Cdd:pfam13704   2 NEADILPQWLAHHL---ALGFD------------HIYVYDNGSDDGTAEILARLPDVSILRSDLSYKDARFQVDWrnall 66
                          90
                  ....*....|....*
gi 1119350963  89 -NESRGDILIFLDAD 102
Cdd:pfam13704  67 aRYAEADWVLVVDAD 81
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
5-102 7.23e-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: 7.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   5 KVTIIIPAWNEAqrLPLTLKTLRkqmaqgreSALKMPSDNLEYELIVVDDGSRDGTAEAALPWADKVVKH----PRRRG- 79
Cdd:cd06421     2 TVDVFIPTYNEP--LEIVRKTLR--------AALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEYGYRyltrPDNRHa 71
                          90       100
                  ....*....|....*....|...
gi 1119350963  80 KGAALESGWNESRGDILIFLDAD 102
Cdd:cd06421    72 KAGNLNNALAHTTGDFVAILDAD 94
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
6-102 1.10e-03

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: 39.28  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   6 VTIIIPAWNEAQRLpltLKTLRKQMAQGRESalkmpsdnleYELIVVDDGSRDGTAE------AALPWADKVVKHPRR-- 77
Cdd:pfam13641   4 VSVVVPAFNEDSVL---GRVLEAILAQPYPP----------VEVVVVVNPSDAETLDvaeeiaARFPDVRLRVIRNARll 70
                          90       100
                  ....*....|....*....|....*..
gi 1119350963  78 --RGKGAALESGWNESRGDILIFLDAD 102
Cdd:pfam13641  71 gpTGKSRGLNHGFRAVKSDLVVLHDDD 97
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
48-102 2.17e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 38.00  E-value: 2.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119350963  48 ELIVVDDGSRDGTAEAALPWADK------VVKHPRRRGKGAALESGWNESRGDILIFLDAD 102
Cdd:cd04196    29 ELIISDDGSTDGTVEIIKEYIDKdpfiiiLIRNGKNLGVARNFESLLQAADGDYVFFCDQD 89
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
8-102 3.20e-03

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 37.82  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119350963   8 IIIPAWNEAQRLPLTLKTLRKQMAQGresalkmpsdnlEYELIVVDDGSRDGTAEAALPWADKVVKH-----------PR 76
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEG------------TLELSVFNDASTDKSAEIIEKWRKKLEDSgvivlvgshnsPS 68
                          90       100
                  ....*....|....*....|....*.
gi 1119350963  77 RRGKGAALESGWNESRGDILIFLDAD 102
Cdd:cd06913    69 PKGVGYAKNQAIAQSSGRYLCFLDSD 94
 
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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