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Conserved domains on  [gi|505408676|ref|WP_015595778|]
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glycosyltransferase [Bacillus sp. 1NLA3E]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11421525)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  16037492|18518825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 2-218 5.08e-46

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 155.25  E-value: 5.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   2 NPKISIIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRIIVI-HKENGGQSSARNRGIDL 80
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIrLERNRGKGAARNAGLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676  81 AKGDYIGFIDSDDWIDKDMYEVLYKKAIETDTDISACNiieyqkdstkRLFCNDSTYQIYDRNSAMNEIFLNQRLTYSPC 160
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGS----------RLIREGESDLRRLGSRLFNLVRLLTNLPDSTS 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505408676 161 N-KIYKKDLFNCLRFKEGYiLEDMDFAyKIIHQSNKIFYTGqamYNYRYNDKSTLRKTF 218
Cdd:COG0463  151 GfRLFRREVLEELGFDEGF-LEDTELL-RALRHGFRIAEVP---VRYRAGESKLNLRDL 204
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 2-218 5.08e-46

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 155.25  E-value: 5.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   2 NPKISIIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRIIVI-HKENGGQSSARNRGIDL 80
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIrLERNRGKGAARNAGLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676  81 AKGDYIGFIDSDDWIDKDMYEVLYKKAIETDTDISACNiieyqkdstkRLFCNDSTYQIYDRNSAMNEIFLNQRLTYSPC 160
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGS----------RLIREGESDLRRLGSRLFNLVRLLTNLPDSTS 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505408676 161 N-KIYKKDLFNCLRFKEGYiLEDMDFAyKIIHQSNKIFYTGqamYNYRYNDKSTLRKTF 218
Cdd:COG0463  151 GfRLFRREVLEELGFDEGF-LEDTELL-RALRHGFRIAEVP---VRYRAGESKLNLRDL 204
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 3-273 1.50e-42

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 149.81  E-value: 1.50e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   3 PKISIIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRIIVIHKENGGQSSARNRGIDLAK 82
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTGLAVAT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676  83 GDYIGFIDSDDWIDKDMYEVLYKKAIETDTDISACN--IIEYQKDSTKRLFCND--STYQIYDRNSAMNEIFLNQRLTYS 158
Cdd:PRK10073  86 GKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNadWCFRDTGETWQSIPSDrlRSTGVLSGPDWLRMALSSRRWTHV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676 159 PCNKIYKKDLF--NCLRFKEGYILEDMDFAYKIIHQSNKIFYTGQAMYNYRYNDKSTLRktfsKKRLDEYSVRkemyafy 236
Cdd:PRK10073 166 VWLGVYRRDFIvkNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSR----LPRQGNKNLN------- 234

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 505408676 237 lenypaqadevYAEWFLKGLELYINIEKYYRNEKKQY 273
Cdd:PRK10073 235 -----------YQRHYIKITRMLEKLNRRYADKIKIY 260
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-171 6.88e-39

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: 135.22  E-value: 6.88e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676    6 SIIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRIIVIH-KENGGQSSARNRGIDLAKGD 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRlPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   85 YIGFIDSDDWIDKDMYEVLYKKAIETDTDISACNIIEYQKDSTKRLFCNDSTYQIYDRNSAMNEIFLNqRLTYSPCNKIY 164
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLN-LPFLIGGFALY 159


                  ....*..
gi 505408676  165 KKDLFNC 171
Cdd:pfam00535 160 RREALEE 166
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 7-117 2.34e-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: 115.30  E-value: 2.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   7 IIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRII-VIHKENGGQSSARNRGIDLAKGDY 85
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIrVINEENQGLAAARNAGLKAARGEY 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 505408676  86 IGFIDSDDWIDKDMYEVLYKKAIEtDTDISAC 117
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLA-DPEADAV 111
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
 3-92 8.54e-07

mycofactocin system glycosyltransferase; Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.


Pssm-ID: 274884 [Multi-domain]  Cd Length: 466  Bit Score: 50.14  E-value: 8.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676    3 PKISIIVPVFNVERFIHDCVDSILGQTF-KDF-ELILVNDGSIDRSGDICDEYSKKDDRIIViHKENGGQSSARNRGIDL 80
Cdd:TIGR03965  74 PSVTVVVPVRNRPAGLARLLAALLALDYpRDRlEVIVVDDGSEDPVPTRAARGARLPVRVIR-HPRRQGPAAARNAGARA 152

                          90
                  ....*....|..
gi 505408676   81 AKGDYIGFIDSD 92
Cdd:TIGR03965 153 ARTEFVAFTDSD 164
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 2-218 5.08e-46

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 155.25  E-value: 5.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   2 NPKISIIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRIIVI-HKENGGQSSARNRGIDL 80
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIrLERNRGKGAARNAGLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676  81 AKGDYIGFIDSDDWIDKDMYEVLYKKAIETDTDISACNiieyqkdstkRLFCNDSTYQIYDRNSAMNEIFLNQRLTYSPC 160
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGS----------RLIREGESDLRRLGSRLFNLVRLLTNLPDSTS 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505408676 161 N-KIYKKDLFNCLRFKEGYiLEDMDFAyKIIHQSNKIFYTGqamYNYRYNDKSTLRKTF 218
Cdd:COG0463  151 GfRLFRREVLEELGFDEGF-LEDTELL-RALRHGFRIAEVP---VRYRAGESKLNLRDL 204
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 3-273 1.50e-42

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 149.81  E-value: 1.50e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   3 PKISIIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRIIVIHKENGGQSSARNRGIDLAK 82
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTGLAVAT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676  83 GDYIGFIDSDDWIDKDMYEVLYKKAIETDTDISACN--IIEYQKDSTKRLFCND--STYQIYDRNSAMNEIFLNQRLTYS 158
Cdd:PRK10073  86 GKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNadWCFRDTGETWQSIPSDrlRSTGVLSGPDWLRMALSSRRWTHV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676 159 PCNKIYKKDLF--NCLRFKEGYILEDMDFAYKIIHQSNKIFYTGQAMYNYRYNDKSTLRktfsKKRLDEYSVRkemyafy 236
Cdd:PRK10073 166 VWLGVYRRDFIvkNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSR----LPRQGNKNLN------- 234

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 505408676 237 lenypaqadevYAEWFLKGLELYINIEKYYRNEKKQY 273
Cdd:PRK10073 235 -----------YQRHYIKITRMLEKLNRRYADKIKIY 260
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-171 6.88e-39

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: 135.22  E-value: 6.88e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676    6 SIIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRIIVIH-KENGGQSSARNRGIDLAKGD 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRlPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   85 YIGFIDSDDWIDKDMYEVLYKKAIETDTDISACNIIEYQKDSTKRLFCNDSTYQIYDRNSAMNEIFLNqRLTYSPCNKIY 164
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLN-LPFLIGGFALY 159


                  ....*..
gi 505408676  165 KKDLFNC 171
Cdd:pfam00535 160 RREALEE 166
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 7-117 2.34e-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: 115.30  E-value: 2.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   7 IIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRII-VIHKENGGQSSARNRGIDLAKGDY 85
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIrVINEENQGLAAARNAGLKAARGEY 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 505408676  86 IGFIDSDDWIDKDMYEVLYKKAIEtDTDISAC 117
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLA-DPEADAV 111
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 3-120 4.24e-30

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: 115.99  E-value: 4.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   3 PKISIIVPVFNVERFIHDCVDSILGQTF--KDFELILVNDGSIDRSGDICDEYSKKDDRIIVIHKE-NGGQSSARNRGID 79
Cdd:COG1215   29 PRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPeNGGKAAALNAGLK 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 505408676  80 LAKGDYIGFIDSDDWIDKDMYEVLYKKAIETDTDISACNII 120
Cdd:COG1215  109 AARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGANLA 149
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 3-114 1.45e-26

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: 103.82  E-value: 1.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   3 PKISIIVPVFNV-ERFIHDCVDSILGQTFKDFELILVNDGSIDRS-GDICDEYSKKDDRI-IVIHKENGGQSSARNRGID 79
Cdd:cd04184    1 PLISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDPEvKRVLKKYAAQDPRIkVVFREENGGISAATNSALE 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 505408676  80 LAKGDYIGFIDSDDWIDKD-MYEVLykKAIETDTDI 114
Cdd:cd04184   81 LATGEFVALLDHDDELAPHaLYEVV--KALNEHPDA 114
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-107 1.51e-26

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 103.92  E-value: 1.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   1 MNPKISIIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRIIViHKENGGQSSARNRGIDL 80
Cdd:COG1216    1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRVRVIR-NPENLGFAAARNLGLRA 79

                         90       100
                 ....*....|....*....|....*..
gi 505408676  81 AKGDYIGFIDSDDWIDKDMYEVLYKKA 107
Cdd:COG1216   80 AGGDYLLFLDDDTVVEPDWLERLLAAA 106
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 4-114 8.12e-25

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: 100.38  E-value: 8.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   4 KISIIVPVFNVERFIHDCVDSILGQTF--KDFELILVNDGSIDRSGDICDEYSKKDDRIIVIHKENGGQSSARNRGIDLA 81
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRIQSAGLNIGIRNS 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 505408676  82 KGDYIGFIDSDDWIDKDMYEVLYKKAIETDTDI 114
Cdd:cd02525   81 RGDIIIRVDAHAVYPKDYILELVEALKRTGADN 113
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 6-213 2.91e-23

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: 94.92  E-value: 2.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   6 SIIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRIIVihKENGGQSSARNRGIDLAKGDY 85
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWIS--EPDKGIYDAMNKGIALATGDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676  86 IGFIDSDDW-IDKDMYEVLYKKAIETDTDISACNIIEYQKDSTKRLfcndstyqiYDRNSAMNEIFLNQRLTYSPCNKIY 164
Cdd:cd06433   79 IGFLNSDDTlLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIG---------RRRPPPFLDKFLLYGMPICHQATFF 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505408676 165 KKDLF-NCLRFKEGY-ILEDMDFAYKIIHQSNKIFYTGQAMYNYRYNDKST 213
Cdd:cd06433  150 RRSLFeKYGGFDESYrIAADYDLLLRLLLAGKIFKYLPEVLAAFRLGGVSS 200
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 7-117 3.18e-23

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: 94.22  E-value: 3.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   7 IIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDR--IIVIHKENGGQSSARNRGIDLAKGD 84
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRrvLVVRDKENGGKAGALNAGLRHAKGD 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 505408676  85 YIGFIDSDDWIDKDMYEVLYKKAIEtDTDISAC 117
Cdd:cd06423   81 IVVVLDADTILEPDALKRLVVPFFA-DPKVGAV 112
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 7-114 9.04e-22

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: 90.71  E-value: 9.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   7 IIVPVFNVERFIHDCVDSIL--GQTFKDFELILVNDGSIDRSGDICDEYSKKDDRIIVI-HKENGGQSSARNRGIDLAKG 83
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLavLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIrLSRNFGKGAAVRAGFKAARG 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 505408676  84 DYIGFIDSDDWIDKDMYEVLYKKAIETDTDI 114
Cdd:cd04179   81 DIVVTMDADLQHPPEDIPKLLEKLLEGGADV 111
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 7-219 2.52e-20

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: 87.51  E-value: 2.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   7 IIVPVFNVERFIHDCVDSILGQTFKD-FELILVNDGSIDRSGDICDEYSKKDDRI----IVIHKENG---GQSSARNRGI 78
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKWRKKLEDSgvivLVGSHNSPspkGVGYAKNQAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676  79 DLAKGDYIGFIDSDDWIDKDMYEVLYKKAIETDTDISACNIIEYQKDSTKRL--FCNDSTyqiydRNSAMNEIFLNQRLT 156
Cdd:cd06913   81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYtrWINTLT-----REQLLTQVYTSHGPT 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505408676 157 YSPCNKIYKKDLFNCL-RFKEG--YILEDMDFAYKIIHQSNKIFYTGQAMYNYRYNDKSTlrkTFS 219
Cdd:cd06913  156 VIMPTWFCSREWFSHVgPFDEGgkGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGAT---THS 218
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-94 5.63e-18

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: 81.14  E-value: 5.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   6 SIIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRIIVIHKENGGQSSARN--RGIDLAKG 83
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNLGVARNfeSLLQAADG 80

                         90
                 ....*....|..
gi 505408676  84 DYIGFIDSDD-W 94
Cdd:cd04196   81 DYVFFCDQDDiW 92
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-117 9.39e-18

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: 79.14  E-value: 9.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   7 IIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKkddRIIVIH-KENGGQSSARNRGIDLAKGDY 85
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFP---EVRLIRnGENLGFGAGNNQGIREAKGDY 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 505408676  86 IGFIDSDDWIDKDMYEVLYkKAIETDTDISAC 117
Cdd:cd04186   78 VLLLNPDTVVEPGALLELL-DAAEQDPDVGIV 108
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 7-92 6.77e-16

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: 74.44  E-value: 6.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   7 IIVPVFNVERFIHDC---VDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRIIVIH-KENGGQSSARNRGIDLAK 82
Cdd:cd04187    1 IVVPVYNEEENLPELyerLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRlSRNFGQQAALLAGLDHAR 80

                         90
                 ....*....|
gi 505408676  83 GDYIGFIDSD 92
Cdd:cd04187   81 GDAVITMDAD 90
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 4-114 1.05e-14

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: 72.32  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   4 KISIIVPVFNVERFIHDCVDSIlgQTFKDfELILVNDGSIDRSGDICDEYSKKddriiVIHKENGGQSSARNRGIDLAKG 83
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESV--KWAVD-EIIVVDSGSTDRTVEIAKEYGAK-----VYQRWWDGFGAQRNFALELATN 72

                         90       100       110
                 ....*....|....*....|....*....|.
gi 505408676  84 DYIGFIDSDDWIDKDMYEVLyKKAIETDTDI 114
Cdd:cd02511   73 DWVLSLDADERLTPELADEI-LALLATDDYD 102
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 7-114 1.82e-14

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: 71.06  E-value: 1.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   7 IIVPVFN----VERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDDRII-VIH-KENGGQSSARNRGIDL 80
Cdd:cd04188    1 VVIPAYNeekrLPPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIrVLTlPKNRGKGGAVRAGMLA 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 505408676  81 AKGDYIGFIDSDDWIDKDMYEVLYKKAIETDTDI 114
Cdd:cd04188   81 ARGDYILFADADLATPFEELEKLEEALKTSGYDI 114
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 3-98 1.30e-13

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: 69.53  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   3 PKISIIVPVFNVERFIHDCVDSILGQTFKD--FELILVNDGSIDRSGDICDEYSKKDDRIIvIHKENGGQSSARNRGIDL 80
Cdd:cd06439   29 PTVTIIIPAYNEEAVIEAKLENLLALDYPRdrLEIIVVSDGSTDGTAEIAREYADKGVKLL-RFPERRGKAAALNRALAL 107

                         90
                 ....*....|....*...
gi 505408676  81 AKGDYIGFIDSDDWIDKD 98
Cdd:cd06439  108 ATGEIVVFTDANALLDPD 125
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 7-114 8.53e-12

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: 63.71  E-value: 8.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   7 IIVPVFNVERFIHDCVDSILGQTFK-DFELILVNDGSIDRSGDICDEYSKKDDRIIVIH-KENGGQSSARNRGIDLAKGD 84
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGiDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVrPGKRGLGSAYIEGFKAARGD 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 505408676  85 YIGFIDSDDWIDKDMYEVLYKKAIETDTDI 114
Cdd:cd06442   81 VIVVMDADLSHPPEYIPELLEAQLEGGADL 110
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 3-98 2.80e-11

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: 62.39  E-value: 2.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676    3 PKISIIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDE----YSKKDDRIIVIHKENG--GQSSARNR 76
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEiaarFPDVRLRVIRNARLLGptGKSRGLNH 81

                          90       100
                  ....*....|....*....|..
gi 505408676   77 GIDLAKGDYIGFIDSDDWIDKD 98
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPG 103
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 5-189 4.80e-11

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: 61.43  E-value: 4.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   5 ISIIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICdeyskKDDRIIVIHKENGgqssaR----NRGIDL 80
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIA-----RSAGVVVISSPKG-----RarqmNAGAAA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676  81 AKGDYIGFIDSDDWIDKDMYEVLYKKAIETDTDISACniieyqkdstkrlfcndsTYQIYDRNSAMNEIFL--NqrlTYS 158
Cdd:cd02522   71 ARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAF------------------RLRFDDPGPRLRLLELgaN---LRS 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 505408676 159 PCNKIY--------KKDLFNCL-RFKEGYILEDMDFAYKI 189
Cdd:cd02522  130 RLFGLPygdqglfiRRELFEELgGFPELPLMEDVELVRRL 169
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 7-95 5.84e-10

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: 57.59  E-value: 5.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   7 IIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSIDRSGDICDEYSKKDD-RII-VIHKENGGQSSA-RNRGIDLAKG 83
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPiPIKhVWQEDEGFRKAKiRNKAIAAAKG 80

                         90
                 ....*....|....*..
gi 505408676  84 DYIGFIDSD-----DWI 95
Cdd:cd06420   81 DYLIFIDGDciphpDFI 97
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-95 2.01e-09

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 56.91  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   7 IIVPVFNVERFIHDCVDSILGQTFKD--FELILVNDGSIDRSGDICD-EYSKKDDRIIVIH---KENGGQSSARNRGIDL 80
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYPKekFEVILVDDHSTDGTVQILEfAAAKPNFQLKILNnsrVSISGKKNALTTAIKA 80

                         90       100
                 ....*....|....*....|
gi 505408676  81 AKGDYIGFIDSD-----DWI 95
Cdd:cd04192   81 AKGDWIVTTDADcvvpsNWL 100
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
2-93 2.31e-08

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 54.23  E-value: 2.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   2 NPKISIIVPVFNVERFIHDCVDSILGQTFKDFELILVNDGSidRSGDICDEYSKK--DDRIIVIHKE-NGGQSSARNRGI 78
Cdd:PRK10018   4 NPLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCS--TSWEQLQQYVTAlnDPRITYIHNDiNSGACAVRNQAI 81

                         90
                 ....*....|....*
gi 505408676  79 DLAKGDYIGFIDSDD 93
Cdd:PRK10018  82 MLAQGEYITGIDDDD 96
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 6-131 6.11e-08

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: 53.05  E-value: 6.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676    6 SIIVPVFNVERfIHDCVDSILGQTF---KDFELILVNDGSIDRSGDICDEYSKKDDRIIVIHKENG--GQSSARNRGIDL 80
Cdd:pfam10111   1 SVVIPVYNGEK-THWIQERILNQTFqydPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNAPDTtySLAASRNRGTSH 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 505408676   81 AKGDYIGFIDSDDWIDKDMYEVLYK----KAIETDTDIS-ACNIIEYQKDSTKRLF 131
Cdd:pfam10111  80 AIGEYISFIDGDCLWSPDKFEKQLKiatsLALQENIQAAvVLPVTDLNDESSNFLR 135
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 6-91 1.82e-07

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: 51.82  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   6 SIIVPVFNVER-FIHDCVDSILGQTFKDF--ELILVNDGSiDRsGDICDE----YSKKDDRIIVIH-KENGGQSSARNRG 77
Cdd:cd02510    1 SVIIIFHNEALsTLLRTVHSVINRTPPELlkEIILVDDFS-DK-PELKLLleeyYKKYLPKVKVLRlKKREGLIRARIAG 78

                         90
                 ....*....|....
gi 505408676  78 IDLAKGDYIGFIDS 91
Cdd:cd02510   79 ARAATGDVLVFLDS 92
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 4-92 6.03e-07

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 50.50  E-value: 6.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   4 KISIIVPVFN--------VERFIHDCvdsilGQTFKDFELILVNDGSIDRSGDICDEYSKKDDR--IIVIHKENGGQSSA 73
Cdd:PRK10714   7 KVSVVIPVYNeqeslpelIRRTTAAC-----ESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDShiVAILLNRNYGQHSA 81

                         90
                 ....*....|....*....
gi 505408676  74 RNRGIDLAKGDYIGFIDSD 92
Cdd:PRK10714  82 IMAGFSHVTGDLIITLDAD 100
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
 3-92 8.54e-07

mycofactocin system glycosyltransferase; Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.


Pssm-ID: 274884 [Multi-domain]  Cd Length: 466  Bit Score: 50.14  E-value: 8.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676    3 PKISIIVPVFNVERFIHDCVDSILGQTF-KDF-ELILVNDGSIDRSGDICDEYSKKDDRIIViHKENGGQSSARNRGIDL 80
Cdd:TIGR03965  74 PSVTVVVPVRNRPAGLARLLAALLALDYpRDRlEVIVVDDGSEDPVPTRAARGARLPVRVIR-HPRRQGPAAARNAGARA 152

                          90
                  ....*....|..
gi 505408676   81 AKGDYIGFIDSD 92
Cdd:TIGR03965 153 ARTEFVAFTDSD 164
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 6-130 1.87e-06

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: 47.69  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   6 SIIVPVFNVER--FIHDCVDSILGQTFKDFELILVNDGSIDRSGD-ICDEYSKKDDRIIVIHKENGGQSSARNRGIDLAK 82
Cdd:cd04195    1 SVLMSVYIKEKpeFLREALESILKQTLPPDEVVLVKDGPVTQSLNeVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 505408676  83 GDYIGFIDSDDWIDKDMYEVLYKKAIETDT-DISACNIIEYQKDSTKRL 130
Cdd:cd04195   81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEiDIVGGGVLEFDSDGNDIG 129
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 5-111 2.54e-06

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 48.61  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   5 ISIIVPVFNVE----RFIHDCVDSILGQTFKD----FELILVNDGSIDRSGDICDEYSKKD-----DRIIVIHKENGGQS 71
Cdd:PTZ00260  72 LSIVIPAYNEEdrlpKMLKETIKYLESRSRKDpkfkYEIIIVNDGSKDKTLKVAKDFWRQNinpniDIRLLSLLRNKGKG 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 505408676  72 SARNRGIDLAKGDYIGFIDSDDWIDKDMYEVLYKKAIETD 111
Cdd:PTZ00260 152 GAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIE 191
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 5-98 7.58e-06

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: 46.48  E-value: 7.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   5 ISIIVPVF--NVERFIhDCVDSILGQtfKDFELILVNDGSIDRSGDIcDEYSKKDDRIIVIHKENGGQSSARNRGIDLAK 82
Cdd:cd06434    2 VTVIIPVYdeDPDVFR-ECLRSILRQ--KPLEIIVVTDGDDEPYLSI-LSQTVKYGGIFVITVPHPGKRRALAEGIRHVT 77

                         90
                 ....*....|....*.
gi 505408676  83 GDYIGFIDSDDWIDKD 98
Cdd:cd06434   78 TDIVVLLDSDTVWPPN 93
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 2-92 9.60e-06

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 46.23  E-value: 9.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   2 NPKISIIVPVFNvER--------FIHDCVDSilgqtFKDFELILVNDGSIDRSGDICDEYSK--KDDRIIVIHK-ENGGQ 70
Cdd:PLN02726   8 AMKYSIIVPTYN-ERlnialivyLIFKALQD-----VKDFEIIVVDDGSPDGTQDVVKQLQKvyGEDRILLRPRpGKLGL 81

                         90       100
                 ....*....|....*....|..
gi 505408676  71 SSARNRGIDLAKGDYIGFIDSD 92
Cdd:PLN02726  82 GTAYIHGLKHASGDFVVIMDAD 103
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
 3-98 3.64e-05

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: 43.74  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676   3 PKISIIVPVFNVERFIHDCVDSILGQTFKDFELIL-VNDGSiDRSGDI----CDEYSKKDDRIIVIHKENGGQSSARN-- 75
Cdd:cd02520    1 PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILFcVQDED-DPAIPVvrklIAKYPNVDARLLIGGEKVGINPKVNNli 79

                         90       100
                 ....*....|....*....|...
gi 505408676  76 RGIDLAKGDYIGFIDSDDWIDKD 98
Cdd:cd02520   80 KGYEEARYDILVISDSDISVPPD 102
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 21-122 4.88e-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: 40.70  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505408676  21 CVDSILGQTFKDFELILVNDGSIDRSGDICDEYsKKDDRIIVIH-KENGGQSSARNRGIDLA---KGDYIGFIDSDDWID 96
Cdd:cd04185   15 CLDALLAQTRPPDHIIVIDNASTDGTAEWLTSL-GDLDNIVYLRlPENLGGAGGFYEGVRRAyelGYDWIWLMDDDAIPD 93

                         90       100
                 ....*....|....*....|....*.
gi 505408676  97 KDMYEVLYKKAIETDTDISACNIIEY 122
Cdd:cd04185   94 PDALEKLLAYADKDNPQFLAPLVLDP 119
 
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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