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Conserved domains on  [gi|2205656898|ref|WP_240781827|]
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MULTISPECIES: glycosyltransferase [Saccharolobus]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
5-219 2.73e-38

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.


The actual alignment was detected with superfamily member cd02525:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 249  Bit Score: 135.82  E-value: 2.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   5 LVSIVIPTLNSEKTVKGTLESLQILDY--KNFEIVVVDGYSTDSTLNIVKQFVEKYG-IRIVLEERKGRGVAYNRGVLES 81
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDPrIRLIDNPKRIQSAGLNIGIRNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  82 RGKYVAFLDSDARIATsTWIKNAVRLMENDDR---IGVVFTKVFSP--------PDSKF-----LQKSIDTYLCKGFTTA 145
Cdd:cd02525    81 RGDIIIRVDAHAVYPK-DYILELVEALKRTGAdnvGGPMETIGESKfqkaiavaQSSPLgsggsAYRGGAVKIGYVDTVH 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2205656898 146 NGAiYRKDAVLKVGGFNEEMNYMQEDELLYKLTKAEYKYEVNFNDKIYHYHRDSIRSYIKQNMEAAYG-AKIFHK 219
Cdd:cd02525   160 HGA-YRREVFEKVGGFDESLVRNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKWrARTLRK 233
 
Name Accession Description Interval E-value
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
5-219 2.73e-38

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: 135.82  E-value: 2.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   5 LVSIVIPTLNSEKTVKGTLESLQILDY--KNFEIVVVDGYSTDSTLNIVKQFVEKYG-IRIVLEERKGRGVAYNRGVLES 81
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDPrIRLIDNPKRIQSAGLNIGIRNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  82 RGKYVAFLDSDARIATsTWIKNAVRLMENDDR---IGVVFTKVFSP--------PDSKF-----LQKSIDTYLCKGFTTA 145
Cdd:cd02525    81 RGDIIIRVDAHAVYPK-DYILELVEALKRTGAdnvGGPMETIGESKfqkaiavaQSSPLgsggsAYRGGAVKIGYVDTVH 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2205656898 146 NGAiYRKDAVLKVGGFNEEMNYMQEDELLYKLTKAEYKYEVNFNDKIYHYHRDSIRSYIKQNMEAAYG-AKIFHK 219
Cdd:cd02525   160 HGA-YRREVFEKVGGFDESLVRNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKWrARTLRK 233
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
2-269 6.17e-35

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: 128.32  E-value: 6.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   2 DEPLVSIVIPTLNSEKTVKGTLESLQILDY--KNFEIVVVDGYSTDSTLNIVKQFVEKYG-IRIV-LEERKGRGVAYNRG 77
Cdd:COG1215    27 DLPRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAEYPrVRVIeRPENGGKAAALNAG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  78 VLESRGKYVAFLDSDARIAtSTWIKNAVRLMENDDrigvvftkvfsppdskflqksidtylcKGFTTANGAiYRKDAVLK 157
Cdd:COG1215   107 LKAARGDIVVFLDADTVLD-PDWLRRLVAAFADPG---------------------------VGASGANLA-FRREALEE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898 158 VGGFnEEMNYMQEDELLYKLTKAEYKYEVNFNDKIYHYHRDSIRSYIKQNMEAAYGA-KIFHKLTKEKWVIRDALARLTI 236
Cdd:COG1215   158 VGGF-DEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGlQLLLKHRPLLRPRRLLLFLLLL 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2205656898 237 FFASIIFGLSLILLNIKIFLILSLLTYIILLLK 269
Cdd:COG1215   237 LLPLLLLLLLLALLALLLLLLPALLLALLLALR 269
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
7-161 3.44e-28

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 106.71  E-value: 3.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   7 SIVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKY-GIR-IVLEERKGRGVAYNRGVLESRGK 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDpRVRvIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2205656898  85 YVAFLDSDARIATStWIKNAVRLMENDDRIGVVFTKVFSPPDSKFLQKSIDTYLCKGFTTANGAIYRKDAVLKVGGF 161
Cdd:pfam00535  81 YIAFLDADDEVPPD-WLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGF 156
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
6-179 3.93e-19

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: 84.10  E-value: 3.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   6 VSIVIPTLNSEKTVKGTLESLQILDYkNFEIVVVDGYSTDSTLNIVKQFVEKygiriVLEERKGRGVAYNRGVLESRGKY 85
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALRG-DAEVIVVDGGSTDGTVEIARSLGAK-----VIHSPKGRARQMNAGAALAKGDI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  86 VAFLDSDARIAtSTWIKNAVRLMENDDRIGVVFTKVFSPPDSKF----LQKSIDTYLCkGFTTANGAIY-RKDAVLKVGG 160
Cdd:TIGR04283  75 LLFLHADTRLP-KDFLEAIRRALAKPGYVAGAFDLRFDGPGLLLrlieWGVNLRSRLT-GIPYGDQGLFvRRSLFEQIGG 152
                         170       180
                  ....*....|....*....|...
gi 2205656898 161 FnEEMNYMqED-EL---LYKLTK 179
Cdd:TIGR04283 153 F-PDIPLM-EDiELsrrLRRLGR 173
PRK10073 PRK10073
putative glycosyl transferase; Provisional
2-96 2.12e-15

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 75.47  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   2 DEPLVSIVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKYG-IRIVLEERKGRGVAYNRGVLE 80
Cdd:PRK10073    4 STPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPhVRLLHQANAGVSVARNTGLAV 83
                          90
                  ....*....|....*.
gi 2205656898  81 SRGKYVAFLDSDARIA 96
Cdd:PRK10073   84 ATGKYVAFPDADDVVY 99
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
7-106 9.35e-15

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 73.29  E-value: 9.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   7 SIVIPTLNSEKTVKGTLESLQ---ILDYKNFEIVVVDGYSTDSTLNIVKQFVEK----YGIRIVLEERKGRGVAYNRGVL 79
Cdd:NF038302    4 TVAIPTYNGANRLPEVLERLRsqiGTESLSWEIIVVDNNSTDNTAQVVQEYQKNwpspYPLRYCFEPQQGAAFARQRAIQ 83
                          90       100
                  ....*....|....*....|....*..
gi 2205656898  80 ESRGKYVAFLDSDaRIATSTWIKNAVR 106
Cdd:NF038302   84 EAKGELIGFLDDD-NLPAPNWVAAAYA 109
 
Name Accession Description Interval E-value
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
5-219 2.73e-38

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: 135.82  E-value: 2.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   5 LVSIVIPTLNSEKTVKGTLESLQILDY--KNFEIVVVDGYSTDSTLNIVKQFVEKYG-IRIVLEERKGRGVAYNRGVLES 81
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDPrIRLIDNPKRIQSAGLNIGIRNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  82 RGKYVAFLDSDARIATsTWIKNAVRLMENDDR---IGVVFTKVFSP--------PDSKF-----LQKSIDTYLCKGFTTA 145
Cdd:cd02525    81 RGDIIIRVDAHAVYPK-DYILELVEALKRTGAdnvGGPMETIGESKfqkaiavaQSSPLgsggsAYRGGAVKIGYVDTVH 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2205656898 146 NGAiYRKDAVLKVGGFNEEMNYMQEDELLYKLTKAEYKYEVNFNDKIYHYHRDSIRSYIKQNMEAAYG-AKIFHK 219
Cdd:cd02525   160 HGA-YRREVFEKVGGFDESLVRNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKWrARTLRK 233
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
2-269 6.17e-35

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: 128.32  E-value: 6.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   2 DEPLVSIVIPTLNSEKTVKGTLESLQILDY--KNFEIVVVDGYSTDSTLNIVKQFVEKYG-IRIV-LEERKGRGVAYNRG 77
Cdd:COG1215    27 DLPRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAEYPrVRVIeRPENGGKAAALNAG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  78 VLESRGKYVAFLDSDARIAtSTWIKNAVRLMENDDrigvvftkvfsppdskflqksidtylcKGFTTANGAiYRKDAVLK 157
Cdd:COG1215   107 LKAARGDIVVFLDADTVLD-PDWLRRLVAAFADPG---------------------------VGASGANLA-FRREALEE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898 158 VGGFnEEMNYMQEDELLYKLTKAEYKYEVNFNDKIYHYHRDSIRSYIKQNMEAAYGA-KIFHKLTKEKWVIRDALARLTI 236
Cdd:COG1215   158 VGGF-DEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGlQLLLKHRPLLRPRRLLLFLLLL 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2205656898 237 FFASIIFGLSLILLNIKIFLILSLLTYIILLLK 269
Cdd:COG1215   237 LLPLLLLLLLLALLALLLLLLPALLLALLLALR 269
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
2-239 8.13e-34

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 122.79  E-value: 8.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   2 DEPLVSIVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKyGIRIV-LEERKGRGVAYNRGVLE 80
Cdd:COG1216     1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFP-RVRVIrNPENLGFAAARNLGLRA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  81 SRGKYVAFLDSDARIaTSTWIKNAVRlmenddrigvvftkvfsppdskflqksidtylckgfttANGAIYRKDAVLKVGG 160
Cdd:COG1216    80 AGGDYLLFLDDDTVV-EPDWLERLLA--------------------------------------AACLLIRREVFEEVGG 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898 161 FNEEMNYMQED-ELLYKLTKAEYKYEVNFNDKIYHYHRDSIRSYIKQNMEAAYGAKIFHKLTKEKWVIRDALARLTIFFA 239
Cdd:COG1216   121 FDERFFLYGEDvDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYYLGRNRLLFLRKHGPRPLLRLALLRGLRLRLR 200
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
4-201 1.94e-32

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 119.42  E-value: 1.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   4 PLVSIVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKYG-IRIV-LEERKGRGVAYNRGVLES 81
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPrIRVIrLERNRGKGAARNAGLAAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  82 RGKYVAFLDSDARIaTSTWIKNAVRLMENDDrIGVVFTKVFSPPDSKFLQK------SIDTYLCKGFTTANGA-IYRKDA 154
Cdd:COG0463    82 RGDYIAFLDADDQL-DPEKLEELVAALEEGP-ADLVYGSRLIREGESDLRRlgsrlfNLVRLLTNLPDSTSGFrLFRREV 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2205656898 155 VLKVgGFNEEMNymqEDELLYKLTKAEYKyeVNFNDKIYHYHRDSIR 201
Cdd:COG0463   160 LEEL-GFDEGFL---EDTELLRALRHGFR--IAEVPVRYRAGESKLN 200
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
8-183 2.90e-31

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: 114.53  E-value: 2.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   8 IVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKY--GIRIVLEERKGRGVAYNRGVLESRGKY 85
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDprVIRVINEENQGLAAARNAGLKAARGEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  86 VAFLDSDArIATSTWIKNAVRLMENDDRIGVVftkvfsppdskflqksidtylckgfTTANGAIYRKDAVLKVGGFNEEM 165
Cdd:cd00761    81 ILFLDADD-LLLPDWLERLVAELLADPEADAV-------------------------GGPGNLLFRRELLEEIGGFDEAL 134
                         170
                  ....*....|....*...
gi 2205656898 166 NYMQEDELLYKLTKAEYK 183
Cdd:cd00761   135 LSGEEDDDFLLRLLRGGK 152
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
7-161 3.44e-28

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 106.71  E-value: 3.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   7 SIVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKY-GIR-IVLEERKGRGVAYNRGVLESRGK 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDpRVRvIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2205656898  85 YVAFLDSDARIATStWIKNAVRLMENDDRIGVVFTKVFSPPDSKFLQKSIDTYLCKGFTTANGAIYRKDAVLKVGGF 161
Cdd:pfam00535  81 YIAFLDADDEVPPD-WLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGF 156
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-196 1.00e-27

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: 105.72  E-value: 1.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   8 IVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKyGIRIVLEERKGRGVAYNRGVLESRGKYVA 87
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPE-VRLIRNGENLGFGAGNNQGIREAKGDYVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  88 FLDSDARIaTSTWIKNAVRLMENDDRIGVVFTKVfsppdskflqksidtylckgfttaNGA--IYRKDAVLKVGGFNEEM 165
Cdd:cd04186    80 LLNPDTVV-EPGALLELLDAAEQDPDVGIVGPKV------------------------SGAflLVRREVFEEVGGFDEDF 134
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2205656898 166 -NYMQEDELLYKLTKAEYKYEVNFNDKIYHYH 196
Cdd:cd04186   135 fLYYEDVDLCLRARLAGYRVLYVPQAVIYHHG 166
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
8-171 7.49e-27

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: 103.85  E-value: 7.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   8 IVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKYG---IRIVLEERKGRGVAYNRGVLESRGK 84
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIrrvLVVRDKENGGKAGALNAGLRHAKGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  85 YVAFLDSDARIAtSTWIKNAVRLMENDDRIGVVFTKVFSP-PDSKFLQKSID-------------TYLCKGFTTANGAI- 149
Cdd:cd06423    81 IVVVLDADTILE-PDALKRLVVPFFADPKVGAVQGRVRVRnGSENLLTRLQAieylsifrlgrraQSALGGVLVLSGAFg 159
                         170       180
                  ....*....|....*....|...
gi 2205656898 150 -YRKDAVLKVGGFNEEMnyMQED 171
Cdd:cd06423   160 aFRREALREVGGWDEDT--LTED 180
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
6-164 2.16e-25

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: 101.11  E-value: 2.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   6 VSIVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKygiriVLEERKGRGVAYNRGVLESRGKY 85
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGVV-----VISSPKGRARQMNAGAAAARGDW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  86 VAFLDSDARIAtSTWIKNAVRLMENDDRIGVVFTKVFSPPDSKF--LQKSIDTYlCKGFTTANG--AIY-RKDAVLKVGG 160
Cdd:cd02522    76 LLFLHADTRLP-PDWDAAIIETLRADGAVAGAFRLRFDDPGPRLrlLELGANLR-SRLFGLPYGdqGLFiRRELFEELGG 153

                  ....
gi 2205656898 161 FNEE 164
Cdd:cd02522   154 FPEL 157
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
7-184 7.02e-21

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: 88.37  E-value: 7.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   7 SIVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFvEKYGIRIVLEERKGRGVAYNRGVLESRGKYV 86
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKY-EDKITYWISEPDKGIYDAMNKGIALATGDII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  87 AFLDSDARIATSTWIKNAVRLMENDDrIGVVF--TKVFSPPDSKFLQKSIDT-----YLCKGFTTANGAIYRKDAVLKVG 159
Cdd:cd06433    80 GFLNSDDTLLPGALLAVVAAFAEHPE-VDVVYgdVLLVDENGRVIGRRRPPPfldkfLLYGMPICHQATFFRRSLFEKYG 158
                         170       180
                  ....*....|....*....|....*
gi 2205656898 160 GFNEEMNYMQEDELLYKLTKAEYKY 184
Cdd:cd06433   159 GFDESYRIAADYDLLLRLLLAGKIF 183
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
6-179 3.93e-19

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: 84.10  E-value: 3.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   6 VSIVIPTLNSEKTVKGTLESLQILDYkNFEIVVVDGYSTDSTLNIVKQFVEKygiriVLEERKGRGVAYNRGVLESRGKY 85
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALRG-DAEVIVVDGGSTDGTVEIARSLGAK-----VIHSPKGRARQMNAGAALAKGDI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  86 VAFLDSDARIAtSTWIKNAVRLMENDDRIGVVFTKVFSPPDSKF----LQKSIDTYLCkGFTTANGAIY-RKDAVLKVGG 160
Cdd:TIGR04283  75 LLFLHADTRLP-KDFLEAIRRALAKPGYVAGAFDLRFDGPGLLLrlieWGVNLRSRLT-GIPYGDQGLFvRRSLFEQIGG 152
                         170       180
                  ....*....|....*....|...
gi 2205656898 161 FnEEMNYMqED-EL---LYKLTK 179
Cdd:TIGR04283 153 F-PDIPLM-EDiELsrrLRRLGR 173
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
4-117 9.43e-18

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: 80.70  E-value: 9.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   4 PLVSIVIPTLNSEKTVKGTLESLQILDYKN--FEIVVVDGYSTDSTLNIVKQFVEKYGIRIVLEERKGRGVAYNRGVLES 81
Cdd:cd06439    29 PTVTIIIPAYNEEAVIEAKLENLLALDYPRdrLEIIVVSDGSTDGTAEIAREYADKGVKLLRFPERRGKAAALNRALALA 108
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2205656898  82 RGKYVAFLDSDARIATSTwIKNAVRLMeNDDRIGVV 117
Cdd:cd06439   109 TGEIVVFTDANALLDPDA-LRLLVRHF-ADPSVGAV 142
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
8-92 7.00e-17

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: 76.84  E-value: 7.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   8 IVIPTLNSEKTVKGTLESLQ--ILDYKNFEIVVVDGYSTDSTLNIVKQFVEKYGIR--IVLEERKGRGVAYNRGVLESRG 83
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLavLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVrvIRLSRNFGKGAAVRAGFKAARG 80

                  ....*....
gi 2205656898  84 KYVAFLDSD 92
Cdd:cd04179    81 DIVVTMDAD 89
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
4-197 7.23e-17

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 77.24  E-value: 7.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   4 PLVSIVIPTLNS-EKTVKGTLESLQILDYKNFEIVVVDGYSTDStlnIVKQFVEKYG-----IRIV-LEERKGRGVAYNR 76
Cdd:cd04184     1 PLISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDP---EVKRVLKKYAaqdprIKVVfREENGGISAATNS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  77 GVLESRGKYVAFLDSDARIAtstwiKNA----VRLMENDDRIGVVFT---------KVFSP---PDSkflqkSIDTYLCK 140
Cdd:cd04184    78 ALELATGEFVALLDHDDELA-----PHAlyevVKALNEHPDADLIYSdedkideggKRSEPffkPDW-----SPDLLLSQ 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2205656898 141 GFTTaNGAIYRKDAVLKVGGFNEEMNYMQEDELLYKLTKAeykyevnfNDKIYH-----YHR 197
Cdd:cd04184   148 NYIG-HLLVYRRSLVRQVGGFREGFEGAQDYDLVLRVSEH--------TDRIAHiprvlYHW 200
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
8-92 6.12e-16

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: 74.91  E-value: 6.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   8 IVIPTLNSEKTVKGTLESLqiLDYKN------FEIVVVDGYSTDSTLNIVKQFVEKYG--IRIV-LEERKGRGVAYNRGV 78
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEA--VEYLEerpsfsYEIIVVDDGSKDGTAEVARKLARKNPalIRVLtLPKNRGKGGAVRAGM 78
                          90
                  ....*....|....
gi 2205656898  79 LESRGKYVAFLDSD 92
Cdd:cd04188    79 LAARGDYILFADAD 92
PRK10073 PRK10073
putative glycosyl transferase; Provisional
2-96 2.12e-15

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 75.47  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   2 DEPLVSIVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKYG-IRIVLEERKGRGVAYNRGVLE 80
Cdd:PRK10073    4 STPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPhVRLLHQANAGVSVARNTGLAV 83
                          90
                  ....*....|....*.
gi 2205656898  81 SRGKYVAFLDSDARIA 96
Cdd:PRK10073   84 ATGKYVAFPDADDVVY 99
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-208 3.17e-15

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: 73.48  E-value: 3.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   8 IVIPTLNSEKTVKGTLESLQILDY--KNFEIVVVDGYSTDSTLNIVKQFVEK-----YGIRIVLEERKGRGVAYNRGVLE 80
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYpkEKFEVILVDDHSTDGTVQILEFAAAKpnfqlKILNNSRVSISGKKNALTTAIKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  81 SRGKYVAFLDSDARIAtSTWIKNAVRLMENDDRIGVVFTKVFSPPDSKFLQ-KSIDT-----------YLCKGFtTANGA 148
Cdd:cd04192    81 AKGDWIVTTDADCVVP-SNWLLTFVAFIQKEQIGLVAGPVIYFKGKSLLAKfQRLDWlsllgliagsfGLGKPF-MCNGA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2205656898 149 --IYRKDAVLKVGGFNEEMNYMQED-ELLYKLTKAEY---KYEVNFNDKIYHYHRDSIRSYIKQNM 208
Cdd:cd04192   159 nmAYRKEAFFEVGGFEGNDHIASGDdELLLAKVASKYpkvAYLKNPEALVTTQPVTSWKELLNQRK 224
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
7-197 3.78e-15

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: 73.05  E-value: 3.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   7 SIVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKYGIRIVLEERKGR-GVAYN--RGVLESRG 83
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNlGVARNfeSLLQAADG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  84 KYVAFLDSDariatSTWIKN----AVRLMENDDRIGVVFTKVF-----------SPPDSKFL--QKSIDTYLCKGFTTAN 146
Cdd:cd04196    81 DYVFFCDQD-----DIWLPDklerLLKAFLKDDKPLLVYSDLElvdengnpigeSFFEYQKIkpGTSFNNLLFQNVVTGC 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2205656898 147 GAIYRKDAVLKVGGFNEEMNYMQeDELLYKLtkaeykyeVNFNDKIYHYHR 197
Cdd:cd04196   156 TMAFNRELLELALPFPDADVIMH-DWWLALL--------ASAFGKVVFLDE 197
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
7-106 9.35e-15

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 73.29  E-value: 9.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   7 SIVIPTLNSEKTVKGTLESLQ---ILDYKNFEIVVVDGYSTDSTLNIVKQFVEK----YGIRIVLEERKGRGVAYNRGVL 79
Cdd:NF038302    4 TVAIPTYNGANRLPEVLERLRsqiGTESLSWEIIVVDNNSTDNTAQVVQEYQKNwpspYPLRYCFEPQQGAAFARQRAIQ 83
                          90       100
                  ....*....|....*....|....*..
gi 2205656898  80 ESRGKYVAFLDSDaRIATSTWIKNAVR 106
Cdd:NF038302   84 EAKGELIGFLDDD-NLPAPNWVAAAYA 109
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
6-243 7.08e-13

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: 66.93  E-value: 7.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   6 VSIVIPTLNSEKTVKGTLESLQ-ILDyknfEIVVVDGYSTDSTLNIVKqfveKYGIRIVLEERKGRGVAYNRGVLESRGK 84
Cdd:cd02511     2 LSVVIITKNEERNIERCLESVKwAVD----EIIVVDSGSTDRTVEIAK----EYGAKVYQRWWDGFGAQRNFALELATND 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  85 YVAFLDSDARI--ATSTWIKNAVRlmENDDRIGVVFTKVFsppdskFLQKSIdtYLCKGFTTANGAIYRKDAVLKVGGFN 162
Cdd:cd02511    74 WVLSLDADERLtpELADEILALLA--TDDYDGYYVPRRNF------FLGRWI--RHGGWYPDRQLRLFRRGKARFEDGRV 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898 163 EEmnymqedELLYKLTKaeykyEVNFNDKIYHYHRDSIRSYI-KQNMEAAYGAKIFHKLTKEKWVIRDALAR--LTIFFA 239
Cdd:cd02511   144 HE-------QVVVDGGV-----GIVLKGDILHYGYKSLEEFLeKHNRYSSLEAKDLAAKGKKRSLLKGLLLGrpLLAFLK 211

                  ....
gi 2205656898 240 SIIF 243
Cdd:cd02511   212 MYIL 215
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
8-177 1.29e-11

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: 62.21  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   8 IVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKYGIRI--VLEERKG--RGVAYNRGVLESRG 83
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIkhVWQEDEGfrKAKIRNKAIAAAKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  84 KYVAFLDSDArIATSTWIKNAVRLMEnddrigvvfTKVFSPPDSKFLQKSIDTylcKGFTTANGAIYRKDAvLKVGGFNE 163
Cdd:cd06420    81 DYLIFIDGDC-IPHPDFIADHIELAE---------PGVFLSGSRVLLNEKLTE---RGIRGCNMSFWKKDL-LAVNGFDE 146
                         170
                  ....*....|....*.
gi 2205656898 164 E-MNYMQED-ELLYKL 177
Cdd:cd06420   147 EfTGWGGEDsELVARL 162
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
4-92 1.92e-11

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 62.79  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   4 PLVSIVIPTLNSEKTVkGTLESL---QILDYKNFEIVVVDGYSTDSTLNIVKQFVEKYGI-RIVLEERKGR---GVAYNR 76
Cdd:PLN02726    9 MKYSIIVPTYNERLNI-ALIVYLifkALQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEdRILLRPRPGKlglGTAYIH 87
                          90
                  ....*....|....*.
gi 2205656898  77 GVLESRGKYVAFLDSD 92
Cdd:PLN02726   88 GLKHASGDFVVIMDAD 103
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
4-207 3.14e-10

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: 59.31  E-value: 3.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   4 PLVSIVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKYG---IRIVLEERK----GRGVAYNR 76
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPdvrLRVIRNARLlgptGKSRGLNH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  77 GVLESRGKYVAFLDSDARIATSTwIKNAVRLMEnDDRIGVVFTKVFSPPDSKFLQKSIDTYLC------------KGFTT 144
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGT-LKKYVQYFD-SPKVGAVGTPVFSLNRSTMLSALGALEFAlrhlrmmslrlaLGVLP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2205656898 145 ANGAI--YRKDAVLKVGGFNEEmNYMQED-ELLYKLTKAEYKYEVNFNDKIYHYHRDSIRSYIKQN 207
Cdd:pfam13641 160 LSGAGsaIRREVLKELGLFDPF-FLLGDDkSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQR 224
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
7-92 3.76e-10

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 59.78  E-value: 3.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   7 SIVIPTLNSE----KTVKGT---LESLQILDYK-NFEIVVVDGYSTDSTLNIVKQFVEKY-----GIRIV-LEERKGRGV 72
Cdd:PTZ00260   73 SIVIPAYNEEdrlpKMLKETikyLESRSRKDPKfKYEIIIVNDGSKDKTLKVAKDFWRQNinpniDIRLLsLLRNKGKGG 152
                          90       100
                  ....*....|....*....|
gi 2205656898  73 AYNRGVLESRGKYVAFLDSD 92
Cdd:PTZ00260  153 AVRIGMLASRGKYILMVDAD 172
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
8-92 3.94e-10

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: 58.70  E-value: 3.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   8 IVIPTLNSEKTVKGTLESL-QILDYKNFEIVVVDGYSTDSTLNIVKQFVEKYGIRIVL--EERKGRGVAYNRGVLESRGK 84
Cdd:cd06442     1 IIIPTYNERENIPELIERLdAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIvrPGKRGLGSAYIEGFKAARGD 80

                  ....*...
gi 2205656898  85 YVAFLDSD 92
Cdd:cd06442    81 VIVVMDAD 88
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
4-214 4.14e-10

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: 58.74  E-value: 4.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   4 PLVSIVIPTLN-SEKTVKGTLESLQILDYKN--FEIVVVDGYSTDSTLNIVKQFVEKYGIRIVLEERkGRGV---AYNRG 77
Cdd:cd06421     1 PTVDVFIPTYNePLEIVRKTLRAALAIDYPHdkLRVYVLDDGRRPELRALAAELGVEYGYRYLTRPD-NRHAkagNLNNA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  78 VLESRGKYVAFLDSDaRIATSTWIKNAVRLMENDDRIGVVFT--KVFSPPDSKFLQKSIDTYLC--------------KG 141
Cdd:cd06421    80 LAHTTGDFVAILDAD-HVPTPDFLRRTLGYFLDDPKVALVQTpqFFYNPDPFDWLADGAPNEQElfygviqpgrdrwgAA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898 142 FTTANGAIYRKDAVLKVGGFNEEMnyMQED-ELLYKLTKAEYKyevnfndKIYHYHR-------DSIRSYIKQNMEAAYG 213
Cdd:cd06421   159 FCCGSGAVVRREALDEIGGFPTDS--VTEDlATSLRLHAKGWR-------SVYVPEPlaaglapETLAAYIKQRLRWARG 229

                  .
gi 2205656898 214 A 214
Cdd:cd06421   230 M 230
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
6-92 1.14e-09

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 58.39  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   6 VSIVIPTLNSEKTVKGTLESLQ------ILDyknfEIVVVDGYSTDSTLNIVKQfvekYGIRIV--------LEERKGRG 71
Cdd:PRK13915   33 VSVVLPALNEEETVGKVVDSIRpllmepLVD----ELIVIDSGSTDATAERAAA----AGARVVsreeilpeLPPRPGKG 104
                          90       100
                  ....*....|....*....|.
gi 2205656898  72 VAYNRGVLESRGKYVAFLDSD 92
Cdd:PRK13915  105 EALWRSLAATTGDIVVFVDAD 125
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
19-214 6.59e-09

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 55.48  E-value: 6.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  19 VKGTLESLQILDYKNFEIVVVDGYSTDSTL-NIVKQFVEKYGIRIV---LEERKG-RGVAYNRGVLESRG--KYVAFLDS 91
Cdd:cd06435    14 VKETLDSLAALDYPNFEVIVIDNNTKDEALwKPVEAHCAQLGERFRffhVEPLPGaKAGALNYALERTAPdaEIIAVIDA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  92 DaRIATSTWIKNAVRLMEnDDRIGVVFTkvfsPPDSKFLQKSIDTYLC----KGF--------TTANGAIY-------RK 152
Cdd:cd06435    94 D-YQVEPDWLKRLVPIFD-DPRVGFVQA----PQDYRDGEESLFKRMCyaeyKGFfdigmvsrNERNAIIQhgtmcliRR 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2205656898 153 DAVLKVGGFNEEMnyMQED-ELLYKLTKAEYKyEVNFNDKIYH-YHRDSIRSYIKQNMEAAYGA 214
Cdd:cd06435   168 SALDDVGGWDEWC--ITEDsELGLRMHEAGYI-GVYVAQSYGHgLIPDTFEAFKKQRFRWAYGA 228
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
8-92 4.31e-08

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: 52.85  E-value: 4.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   8 IVIPTLNSEKTVKGTLESLQILDYKN-FEIVVVDGYSTDSTLNIVKQF---VEKYGIRIVLEER-----KGRGVAYNRGV 78
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKWrkkLEDSGVIVLVGSHnspspKGVGYAKNQAI 80
                          90
                  ....*....|....
gi 2205656898  79 LESRGKYVAFLDSD 92
Cdd:cd06913    81 AQSSGRYLCFLDSD 94
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
7-218 6.21e-07

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 49.97  E-value: 6.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   7 SIVIPTLNSEKT--VKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKYGIRIVLEERK---GRGVAYNRGVLES 81
Cdd:pfam10111   1 SVVIPVYNGEKThwIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNAPDttySLAASRNRGTSHA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  82 RGKYVAFLDSD--------ARIATSTWIKNAVRLME----------NDDRIGVVFTKVFSPPDSKFLQKSIDTY--LCKG 141
Cdd:pfam10111  81 IGEYISFIDGDclwspdkfEKQLKIATSLALQENIQaavvlpvtdlNDESSNFLRRGGDLTASGDVLRDLLVFYspLAIF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898 142 FT-TANGAIYRKDAVLKVGGFNEEM-NYMQED-ELLYKLTKAEYKYEVNFNDKIYHYHRDSIRSYIKQNM--------EA 210
Cdd:pfam10111 161 FApNSSNALINRQAFIEVGGFDESFrGHGAEDfDIFLRLAARYPFVAVMPPQLLYRLSAKSMSPYSGFRRflgdlarqAA 240

                  ....*...
gi 2205656898 211 AYGAKIFH 218
Cdd:pfam10111 241 ACGKVLKH 248
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
4-186 7.36e-07

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 48.75  E-value: 7.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   4 PLVSIVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKYG---IRIVLEERKgRGV---AYN-- 75
Cdd:cd02520     1 PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPnvdARLLIGGEK-VGInpkVNNli 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  76 RGVLESRGKYVAFLDSDARIATSTwIKNAVRLMENDDrIGVVftkvfsppdskflqksidTYLCkgfttANGA--IYRKD 153
Cdd:cd02520    80 KGYEEARYDILVISDSDISVPPDY-LRRMVAPLMDPG-VGLV------------------TCLC-----AFGKsmALRRE 134
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2205656898 154 AVLKVGGFNEEMNYMQEDELL-YKLTKAEYKYEV 186
Cdd:cd02520   135 VLDAIGGFEAFADYLAEDYFLgKLIWRLGYRVVL 168
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
8-92 1.17e-06

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: 47.86  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   8 IVIPTLNSEKTVKGTLESL-QILD--YKNFEIVVVDGYSTDSTLNIVKQFVEKYG-IRIVLEER---KGRGVAYnrGVLE 80
Cdd:cd04187     1 IVVPVYNEEENLPELYERLkAVLEslGYDYEIIFVDDGSTDRTLEILRELAARDPrVKVIRLSRnfgQQAALLA--GLDH 78
                          90
                  ....*....|..
gi 2205656898  81 SRGKYVAFLDSD 92
Cdd:cd04187    79 ARGDAVITMDAD 90
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
8-96 1.50e-06

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


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 47.76  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   8 IVIPTLNSEKTVKGTLESLQILDyKNFEIVVVDGYSTDSTLNIVKQFVEKYGI----RIVLEERKGRGVAYNRGV----- 78
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRNK-PNFLVLVIDDASDDDTAGIVRLAITDSRVhllrRHLPNARTGKGDALNAAYdqirq 79
                          90       100
                  ....*....|....*....|....
gi 2205656898  79 -LESRGK-----YVAFLDSDARIA 96
Cdd:cd06436    80 iLIEEGAdpervIIAVIDADGRLD 103
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
4-184 6.66e-06

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: 46.53  E-value: 6.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   4 PLVSIVIPTLNSEKTVKGTLESLQILDY-KN-FEIVVVDGySTDSTLNIVKQFVEKY---GIRIVLEERKGRgVAYNRGV 78
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYpKDrLEIQVLDD-STDETVRLAREIVEEYaaqGVNIKHVRRADR-TGYKAGA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  79 LE-----SRGKYVAFLDSDARiATSTWIKNAVRLMENDDrIGVVFTKV-FSPPDSKFLQK----SID------------T 136
Cdd:cd06437    79 LAegmkvAKGEYVAIFDADFV-PPPDFLQKTPPYFADPK-LGFVQTRWgHINANYSLLTRvqamSLDyhftieqvarssT 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2205656898 137 YLCKGFttaNGA--IYRKDAVLKVGGFNEEMnyMQED-ELLYKLTKAEYKY 184
Cdd:cd06437   157 GLFFNF---NGTagVWRKECIEDAGGWNHDT--LTEDlDLSYRAQLKGWKF 202
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
2-92 6.84e-06

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 46.91  E-value: 6.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   2 DEPLVSIVIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYStdSTLNIVKQFVEKYG---IRIVLEERK-GRGVAYNRG 77
Cdd:PRK10018    3 DNPLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCS--TSWEQLQQYVTALNdprITYIHNDINsGACAVRNQA 80
                          90
                  ....*....|....*
gi 2205656898  78 VLESRGKYVAFLDSD 92
Cdd:PRK10018   81 IMLAQGEYITGIDDD 95
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
7-175 1.17e-05

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 45.38  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   7 SIVIPTLNSEKTV--KGTLESLqildYKNF----EIVVV-DGYSTDSTLNIVKQFVEKYGIRIV-LEERKGRGVAYNRGV 78
Cdd:cd04195     1 SVLMSVYIKEKPEflREALESI----LKQTlppdEVVLVkDGPVTQSLNEVLEEFKRKLPLKVVpLEKNRGLGKALNEGL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  79 LESRGKYVAFLDSDaRIATSTWIKNAVRLMENDDRIGVVFTKVFsppDSKFLQKSIDTYlcKGFTTANGAI--------- 149
Cdd:cd04195    77 KHCTYDWVARMDTD-DISLPDRFEKQLDFIEKNPEIDIVGGGVL---EFDSDGNDIGKR--RLPTSHDDILkfarrrspf 150
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2205656898 150 ------YRKDAVLKVGGFNEEmnYMQEDELLY 175
Cdd:cd04195   151 nhptvmFRKSKVLAVGGYQDL--PLVEDYALW 180
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
18-165 7.62e-05

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 43.43  E-value: 7.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  18 TVKGTLESLQILDYKNFEIVVVDGySTDSTLNIVKQFVEKYGIRIVLEERKGRGVAYNRGV---LESRGKYVAFLDSDAR 94
Cdd:cd02526     9 DLSKLKELLAALAEQVDKVVVVDN-SSGNDIELRLRLNSEKIELIHLGENLGIAKALNIGIkaaLENGADYVLLFDQDSV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  95 IATSTWIK--NAVRLMENDDRIGVV---FTKVFSPPDSKFLQKSIDTYLCKG----------FTTANGAIYRKDAVLKVG 159
Cdd:cd02526    88 PPPDMVEKllAYKILSDKNSNIGAVgprIIDRRTGENSPGVRKSGYKLRIQKegeeglkevdFLITSGSLISLEALEKVG 167

                  ....*.
gi 2205656898 160 GFNEEM 165
Cdd:cd02526   168 GFDEDL 173
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
9-197 1.57e-04

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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 41.85  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   9 VIPTLNSEKTVKGTLESLQILDYKNFEIVVVDGYSTDSTLNIVKQFVEKYGIR-IVLEERKGRGVAYNRGV---LESRGK 84
Cdd:cd04185     2 VVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLDNIVyLRLPENLGGAGGFYEGVrraYELGYD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898  85 YVAFLDSDArIATSTWIKNAVRLMENDDRiGVVFTKVFSpPDSKFlqksidtylckgfttaNGAIYRKDAVLKVGGFNEE 164
Cdd:cd04185    82 WIWLMDDDA-IPDPDALEKLLAYADKDNP-QFLAPLVLD-PDGSF----------------VGVLISRRVVEKIGLPDKE 142
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2205656898 165 MnYMQEDELLY--KLTKAEYKYEVNfNDKIYHYHR 197
Cdd:cd04185   143 F-FIWGDDTEYtlRASKAGPGIYVP-DAVVVHKTA 175
Glyco_tranf_2_5 pfam13712
Glycosyltransferase like family; Members of this family of prokaryotic proteins include ...
73-117 4.60e-04

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


Pssm-ID: 463964 [Multi-domain]  Cd Length: 210  Bit Score: 40.68  E-value: 4.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2205656898  73 AYNRGVLESRGKYVAFLDSDARIATSTWIKNAVRLMENDDRIGVV 117
Cdd:pfam13712  44 AYNEAMSASDAKYKVYIHQDVFIINKDFIEDLLSIFKKDPSIGMI 88
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
6-121 5.41e-04

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: 40.70  E-value: 5.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   6 VSIVIPTLNSEKTV-KGTLESlqILDYKNFEIVVV-DGYSTDStLNIVKQFVEKYGIRIVLEERKGRGVAYNRGVLESRG 83
Cdd:cd06434     2 VTVIIPVYDEDPDVfRECLRS--ILRQKPLEIIVVtDGDDEPY-LSILSQTVKYGGIFVITVPHPGKRRALAEGIRHVTT 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2205656898  84 KYVAFLDSDArIATSTWIKNAVRLMEnDDRIGVVFTKV 121
Cdd:cd06434    79 DIVVLLDSDT-VWPPNALPEMLKPFE-DPKVGGVGTNQ 114
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
7-91 4.17e-03

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: 38.34  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   7 SIVIPTLNSE-----KTVKGTLESLQILDYKnfEIVVVDGYSTDSTLNI-VKQFVEKY--GIRIV-LEERKGRGVAYNRG 77
Cdd:cd02510     1 SVIIIFHNEAlstllRTVHSVINRTPPELLK--EIILVDDFSDKPELKLlLEEYYKKYlpKVKVLrLKKREGLIRARIAG 78
                          90
                  ....*....|....
gi 2205656898  78 VLESRGKYVAFLDS 91
Cdd:cd02510    79 ARAATGDVLVFLDS 92
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
8-93 6.02e-03

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: 37.20  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656898   8 IVIPTLNSEKTVKGTLESLQILDYK--NFEIVVVDGYSTDSTLNIVKQfvekYGIrIVLE----ERKGRGVAYNRGV--- 78
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSLKAQDYPreLYRIFVVADNCTDDTAQVARA----AGA-TVLErhdpERRGKGYALDFGFrhl 75
                          90
                  ....*....|....*
gi 2205656898  79 LESRGKYVAFLDSDA 93
Cdd:cd06438    76 LNLADDPDAVVVFDA 90
 
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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