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Conserved domains on  [gi|1788517916|ref|WP_158008548|]
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glycosyltransferase [Lactococcus lactis]

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]; ...
 2-214 2.53e-37

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 132.13  E-value: 2.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYFEKDNGGLSSARNFGLEKISGD 81
Cdd:COG0463     5 SVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAARGD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916  82 FVGFLDSDDYIDNDLYEIMINSLDSS-IKIVECDFIWEYENGKSVLDKTSEYNSIKDLMVNGRVVAWNKIYNVEWLEKIN 160
Cdd:COG0463    85 YIAFLDADDQLDPEKLEELVAALEEGpADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFRLFRREVLEELG 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1788517916 161 ikFKEGLLYEdlNFFFKIVPHLTSISEVStvknsfVHYVQHKGTITSDNSLNIL 214
Cdd:COG0463   165 --FDEGFLED--TELLRALRHGFRIAEVP------VRYRAGESKLNLRDLLRLL 208
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 2-214 2.53e-37

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 132.13  E-value: 2.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYFEKDNGGLSSARNFGLEKISGD 81
Cdd:COG0463     5 SVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAARGD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916  82 FVGFLDSDDYIDNDLYEIMINSLDSS-IKIVECDFIWEYENGKSVLDKTSEYNSIKDLMVNGRVVAWNKIYNVEWLEKIN 160
Cdd:COG0463    85 YIAFLDADDQLDPEKLEELVAALEEGpADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFRLFRREVLEELG 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1788517916 161 ikFKEGLLYEdlNFFFKIVPHLTSISEVStvknsfVHYVQHKGTITSDNSLNIL 214
Cdd:COG0463   165 --FDEGFLED--TELLRALRHGFRIAEVP------VRYRAGESKLNLRDLLRLL 208
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 1-206 2.24e-35

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 130.17  E-value: 2.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   1 MSIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIfKYFEKDNGGLSSARNFGLEKISG 80
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHV-RLLHQANAGVSVARNTGLAVATG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916  81 DFVGFLDSDDYIDNDLYEIMIN-SLDSSIKIVECDFIWEYENGK--------------SVLDKTS----EYNSIKDLMvn 141
Cdd:PRK10073   87 KYVAFPDADDVVYPTMYETLMTmALEDDLDVAQCNADWCFRDTGetwqsipsdrlrstGVLSGPDwlrmALSSRRWTH-- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916 142 grvVAWNKIYNVEWLEKINIKFKEGLLYEDLNF-----------------FFKIVPHLTSISEVSTVKNSFVHYVQHKGT 204
Cdd:PRK10073  165 ---VVWLGVYRRDFIVKNNIKFEPGLHHQDIPWttevmfnalrvryteqsLYKYYLHDTSVSRLPRQGNKNLNYQRHYIK 241


                  ..
gi 1788517916 205 IT 206
Cdd:PRK10073  242 IT 243
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 3-101 3.85e-33

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: 119.53  E-value: 3.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   3 IIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYFEKDNGGLSSARNFGLEKISGDF 82
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                          90
                  ....*....|....*....
gi 1788517916  83 VGFLDSDDYIDNDLYEIMI 101
Cdd:cd00761    81 ILFLDADDLLLPDWLERLV 99
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 2-105 1.07e-32

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: 118.65  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYFEKDNGGLSSARNFGLEKISGD 81
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100
                  ....*....|....*....|....
gi 1788517916  82 FVGFLDSDDYIDNDLYEIMINSLD 105
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALE 104
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
2-95 6.40e-11

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 62.12  E-value: 6.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYKEI---EIILVNDGSTDNSKDIAVSYCERFPNIF--KYFEKDNGGLSSARNFGLE 76
Cdd:NF038302    4 TVAIPTYNGANRLPEVLERLRSQIGTESlswEIIVVDNNSTDNTAQVVQEYQKNWPSPYplRYCFEPQQGAAFARQRAIQ 83

                          90
                  ....*....|....*....
gi 1788517916  77 KISGDFVGFLDSDDYIDND 95
Cdd:NF038302   84 EAKGELIGFLDDDNLPAPN 102
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
 2-89 2.01e-08

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: 55.15  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYK--EIEIILVNDGSTDNSKDIAVSYCE------RFPNifkyfekdNGGLSSARNF 73
Cdd:TIGR03965  77 TVVVPVRNRPAGLARLLAALLALDYPrdRLEVIVVDDGSEDPVPTRAARGARlpvrviRHPR--------RQGPAAARNA 148

                          90
                  ....*....|....*.
gi 1788517916  74 GLEKISGDFVGFLDSD 89
Cdd:TIGR03965 149 GARAARTEFVAFTDSD 164
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 2-214 2.53e-37

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 132.13  E-value: 2.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYFEKDNGGLSSARNFGLEKISGD 81
Cdd:COG0463     5 SVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAARGD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916  82 FVGFLDSDDYIDNDLYEIMINSLDSS-IKIVECDFIWEYENGKSVLDKTSEYNSIKDLMVNGRVVAWNKIYNVEWLEKIN 160
Cdd:COG0463    85 YIAFLDADDQLDPEKLEELVAALEEGpADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFRLFRREVLEELG 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1788517916 161 ikFKEGLLYEdlNFFFKIVPHLTSISEVStvknsfVHYVQHKGTITSDNSLNIL 214
Cdd:COG0463   165 --FDEGFLED--TELLRALRHGFRIAEVP------VRYRAGESKLNLRDLLRLL 208
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 1-206 2.24e-35

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 130.17  E-value: 2.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   1 MSIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIfKYFEKDNGGLSSARNFGLEKISG 80
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHV-RLLHQANAGVSVARNTGLAVATG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916  81 DFVGFLDSDDYIDNDLYEIMIN-SLDSSIKIVECDFIWEYENGK--------------SVLDKTS----EYNSIKDLMvn 141
Cdd:PRK10073   87 KYVAFPDADDVVYPTMYETLMTmALEDDLDVAQCNADWCFRDTGetwqsipsdrlrstGVLSGPDwlrmALSSRRWTH-- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916 142 grvVAWNKIYNVEWLEKINIKFKEGLLYEDLNF-----------------FFKIVPHLTSISEVSTVKNSFVHYVQHKGT 204
Cdd:PRK10073  165 ---VVWLGVYRRDFIVKNNIKFEPGLHHQDIPWttevmfnalrvryteqsLYKYYLHDTSVSRLPRQGNKNLNYQRHYIK 241


                  ..
gi 1788517916 205 IT 206
Cdd:PRK10073  242 IT 243
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 3-101 3.85e-33

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: 119.53  E-value: 3.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   3 IIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYFEKDNGGLSSARNFGLEKISGDF 82
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                          90
                  ....*....|....*....
gi 1788517916  83 VGFLDSDDYIDNDLYEIMI 101
Cdd:cd00761    81 ILFLDADDLLLPDWLERLV 99
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 2-105 1.07e-32

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: 118.65  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYFEKDNGGLSSARNFGLEKISGD 81
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100
                  ....*....|....*....|....
gi 1788517916  82 FVGFLDSDDYIDNDLYEIMINSLD 105
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALE 104
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 2-179 1.33e-27

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: 109.06  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTY--KEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYFEKDNGGLSSARNFGLEKIS 79
Cdd:COG1215    32 SVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAGLKAAR 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916  80 GDFVGFLDSDDYIDNDLYEIMINSLDSSikivecdfiweyengksvldktseynsikDLMVNGRVVAWNKiynvEWLEKI 159
Cdd:COG1215   112 GDIVVFLDADTVLDPDWLRRLVAAFADP-----------------------------GVGASGANLAFRR----EALEEV 158

                         170       180
                  ....*....|....*....|
gi 1788517916 160 NiKFKEGLLYEDLNFFFKIV 179
Cdd:COG1215   159 G-GFDEDTLGEDLDLSLRLL 177
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-102 2.43e-25

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 100.45  E-value: 2.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   1 MSIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYceRFPNIFKYFEKDNGGLSSARNFGLEKISG 80
Cdd:COG1216     5 VSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAAL--AFPRVRVIRNPENLGFAAARNLGLRAAGG 82

                          90       100
                  ....*....|....*....|..
gi 1788517916  81 DFVGFLDSDDYIDNDLYEIMIN 102
Cdd:COG1216    83 DYLLFLDDDTVVEPDWLERLLA 104
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 2-131 1.02e-24

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: 98.81  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNV-EKYLSKCLNSILEQTYKEIEIILVNDGSTDNS-KDIAVSYCERFPNIFKYFEKDNGGLSSARNFGLEKIS 79
Cdd:cd04184     4 SIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDPEvKRVLKKYAAQDPRIKVVFREENGGISAATNSALELAT 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1788517916  80 GDFVGFLDSDDYID-NDLYEImINSLDSSIkivECDFIWEYEngksvlDKTSE 131
Cdd:cd04184    84 GEFVALLDHDDELApHALYEV-VKALNEHP---DADLIYSDE------DKIDE 126
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 2-123 4.13e-22

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: 91.84  E-value: 4.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERfpnIFKYF-EKDNgGLSSARNFGLEKISG 80
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDK---ITYWIsEPDK-GIYDAMNKGIALATG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1788517916  81 DFVGFLDSDD-YIDNDLYEIMIN-SLDSSIKIVECDFIWEYENGK 123
Cdd:cd06433    77 DIIGFLNSDDtLLPGALLAVVAAfAEHPEVDVVYGDVLLVDENGR 121
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 3-143 7.41e-22

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: 90.36  E-value: 7.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   3 IIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYF-EKDNGGLSSARNFGLEKISGD 81
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVrDKENGGKAGALNAGLRHAKGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1788517916  82 FVGFLDSDDYIDNDLYEIMINSLDSSIKIVECDFIWEYENG-KSVLDK--TSEYNSIKDLMVNGR 143
Cdd:cd06423    81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGsENLLTRlqAIEYLSIFRLGRRAQ 145
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 2-95 6.18e-19

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: 84.21  E-value: 6.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTY--KEIEIILVNDGSTDNSKDIAVSYCERFPNIfKYFEKDNGGLSSARNFGLEKIS 79
Cdd:cd02525     3 SIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDPRI-RLIDNPKRIQSAGLNIGIRNSR 81

                          90
                  ....*....|....*.
gi 1788517916  80 GDFVGFLDSDDYIDND 95
Cdd:cd02525    82 GDIIIRVDAHAVYPKD 97
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 3-89 5.76e-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: 77.23  E-value: 5.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   3 IIIPIYNVEKYLSKCLNSILEQTYKEI--EIILVNDGSTDNSKDIAVSYCERFPNIFKYFEKDNGGLSSARNFGLEKISG 80
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGYdyEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80


                  ....*....
gi 1788517916  81 DFVGFLDSD 89
Cdd:cd04179    81 DIVVTMDAD 89
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 2-102 8.21e-17

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: 77.67  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYFEKDnGGLSSARNF--GLEKIS 79
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNG-KNLGVARNFesLLQAAD 79

                          90       100
                  ....*....|....*....|...
gi 1788517916  80 GDFVGFLDSDDYIDNDLYEIMIN 102
Cdd:cd04196    80 GDYVFFCDQDDIWLPDKLERLLK 102
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 3-106 3.12e-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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 72.21  E-value: 3.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   3 IIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYcerFPNIFKYFEKDNGGLSSARNFGLEKISGDF 82
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLREL---FPEVRLIRNGENLGFGAGNNQGIREAKGDY 77

                          90       100
                  ....*....|....*....|....
gi 1788517916  83 VGFLDSDDYIDNDLYEIMINSLDS 106
Cdd:cd04186    78 VLLLNPDTVVEPGALLELLDAAEQ 101
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 2-98 1.18e-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: 71.94  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTykeIEIILVNDGSTDNSKDIAVSYCERFpnifkyFEKDNGGLSSARNFGLEKISGD 81
Cdd:cd02511     3 SVVIITKNEERNIERCLESVKWAV---DEIIVVDSGSTDRTVEIAKEYGAKV------YQRWWDGFGAQRNFALELATND 73

                          90
                  ....*....|....*..
gi 1788517916  82 FVGFLDSDDYIDNDLYE 98
Cdd:cd02511    74 WVLSLDADERLTPELAD 90
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 3-89 1.84e-14

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: 70.20  E-value: 1.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   3 IIIPIYNVEKYLSKC---LNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIfkyfekdnGGLSSARNFG----- 74
Cdd:cd04187     1 IVVPVYNEEENLPELyerLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRV--------KVIRLSRNFGqqaal 72

                          90
                  ....*....|....*...
gi 1788517916  75 ---LEKISGDFVGFLDSD 89
Cdd:cd04187    73 lagLDHARGDAVITMDAD 90
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 3-89 1.30e-13

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: 68.36  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   3 IIIPIYNVEKYLSKCLNSILE----QTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYFE-KDNGGLSSARNFGLEK 77
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEyleeRPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLTlPKNRGKGGAVRAGMLA 80

                          90
                  ....*....|..
gi 1788517916  78 ISGDFVGFLDSD 89
Cdd:cd04188    81 ARGDYILFADAD 92
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 2-95 1.49e-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: 69.15  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTY--KEIEIILVNDGSTDNSKDIAVSYCERfpNIFKYFEKDNGGLSSARNFGLEKIS 79
Cdd:cd06439    32 TIIIPAYNEEAVIEAKLENLLALDYprDRLEIIVVSDGSTDGTAEIAREYADK--GVKLLRFPERRGKAAALNRALALAT 109

                          90
                  ....*....|....*.
gi 1788517916  80 GDFVGFLDSDDYIDND 95
Cdd:cd06439   110 GEIVVFTDANALLDPD 125
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 3-206 1.95e-13

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: 68.25  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   3 IIIPIYNVEKYLSKCLNSILEQTYK-EIEIILVNDGSTDNSKDIAVSYCERFPNIFKYFEKDNG------GLSSARNFGL 75
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEgTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHnspspkGVGYAKNQAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916  76 EKISGDFVGFLDSDDYIDNDLYEIMIN-SLDSSIKIVECDFIWEYENgkSVLDKTSEYNSIK-DLMV------NGRVVA- 146
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEaALQHPNSIIGCQVRRIPED--STERYTRWINTLTrEQLLtqvytsHGPTVIm 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788517916 147 --WnkIYNVEWLEKINiKFKEG--LLYEDLNFFFKivpHLTSISEVSTVKNSFVHYVQHKGTIT 206
Cdd:cd06913   159 ptW--FCSREWFSHVG-PFDEGgkGVPEDLLFFYE---HLRKGGGVYRVDRCLLLYRYHPGATT 216
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 3-89 4.84e-12

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: 63.37  E-value: 4.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   3 IIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYF-EKDNG-GLSSARNFGLEKISG 80
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIKHVwQEDEGfRKAKIRNKAIAAAKG 80


                  ....*....
gi 1788517916  81 DFVGFLDSD 89
Cdd:cd06420    81 DYLIFIDGD 89
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
2-95 6.40e-11

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 62.12  E-value: 6.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYKEI---EIILVNDGSTDNSKDIAVSYCERFPNIF--KYFEKDNGGLSSARNFGLE 76
Cdd:NF038302    4 TVAIPTYNGANRLPEVLERLRSQIGTESlswEIIVVDNNSTDNTAQVVQEYQKNWPSPYplRYCFEPQQGAAFARQRAIQ 83

                          90
                  ....*....|....*....
gi 1788517916  77 KISGDFVGFLDSDDYIDND 95
Cdd:NF038302   84 EAKGELIGFLDDDNLPAPN 102
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 2-90 9.30e-10

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: 57.32  E-value: 9.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEK--YLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYFEKDNGGLSSARNFGLEKIS 79
Cdd:cd04195     1 SVLMSVYIKEKpeFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80

                          90
                  ....*....|.
gi 1788517916  80 GDFVGFLDSDD 90
Cdd:cd04195    81 YDWVARMDTDD 91
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 2-88 2.93e-09

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: 57.21  E-value: 2.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEK-YLSKCLNSILEQTYKE--IEIILVNDGST-DNSKDIAVSYCERFPNIFKYFEKDN-GGLSSARNFGLE 76
Cdd:cd02510     1 SVIIIFHNEALsTLLRTVHSVINRTPPEllKEIILVDDFSDkPELKLLLEEYYKKYLPKVKVLRLKKrEGLIRARIAGAR 80

                          90
                  ....*....|..
gi 1788517916  77 KISGDFVGFLDS 88
Cdd:cd02510    81 AATGDVLVFLDS 92
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
 2-89 2.01e-08

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: 55.15  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYK--EIEIILVNDGSTDNSKDIAVSYCE------RFPNifkyfekdNGGLSSARNF 73
Cdd:TIGR03965  77 TVVVPVRNRPAGLARLLAALLALDYPrdRLEVIVVDDGSEDPVPTRAARGARlpvrviRHPR--------RQGPAAARNA 148

                          90
                  ....*....|....*.
gi 1788517916  74 GLEKISGDFVGFLDSD 89
Cdd:TIGR03965 149 GARAARTEFVAFTDSD 164
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 2-112 2.23e-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: 54.21  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEK--YLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCE-RFPNIFKYFEKDNGGLSSARNFGLEKI 78
Cdd:pfam10111   1 SVVIPVYNGEKthWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDhNLQVYYPNAPDTTYSLAASRNRGTSHA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1788517916  79 SGDFVGFLDSDDYIDNDLYEIMInSLDSSIKIVE 112
Cdd:pfam10111  81 IGEYISFIDGDCLWSPDKFEKQL-KIATSLALQE 113
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 2-89 3.31e-08

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 53.97  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSIL---EQTYKEIEIILVNDGSTDNSKDIAVSYCERFPN-IFKYFEKDNGGLSSARNFGLEK 77
Cdd:PRK10714    9 SVVIPVYNEQESLPELIRRTTaacESLGKEYEILLIDDGSSDNSAEMLVEAAQAPDShIVAILLNRNYGQHSAIMAGFSH 88

                          90
                  ....*....|..
gi 1788517916  78 ISGDFVGFLDSD 89
Cdd:PRK10714   89 VTGDLIITLDAD 100
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 3-89 6.96e-08

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: 52.29  E-value: 6.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   3 IIIPIYNVEKYLSKCLNSILEQTY--KEIEIILVNDGSTDNSKDI-AVSYCERFPNIFKYFEKD--NGGLSSARNFGLEK 77
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYpkEKFEVILVDDHSTDGTVQIlEFAAAKPNFQLKILNNSRvsISGKKNALTTAIKA 80

                          90
                  ....*....|..
gi 1788517916  78 ISGDFVGFLDSD 89
Cdd:cd04192    81 AKGDWIVTTDAD 92
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 2-46 1.07e-07

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 51.80  E-value: 1.07e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIA 46
Cdd:cd02522     2 SIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIA 46
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 3-111 1.25e-07

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


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 50.68  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   3 IIIPIYNVEKYLSKCLNSILEQTYK--EIEIILVNDGSTDNSKDIAVSY----CERfpnifkyFEKDNGGLSSARNFGLE 76
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSLKAQDYPreLYRIFVVADNCTDDTAQVARAAgatvLER-------HDPERRGKGYALDFGFR 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1788517916  77 KISG-----DFVGFLDSDDYIDNDLYEIMINSLDSSIKIV 111
Cdd:cd06438    74 HLLNladdpDAVVVFDADNLVDPNALEELNARFAAGARVV 113
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 2-107 2.90e-07

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: 50.45  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFK---YFEKDNG--GLSSARNFGLE 76
Cdd:pfam13641   5 SVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLrviRNARLLGptGKSRGLNHGFR 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1788517916  77 KISGDFVGFLDSDDYIDNDLYEIMINSLDSS 107
Cdd:pfam13641  85 AVKSDLVVLHDDDSVLHPGTLKKYVQYFDSP 115
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 2-89 6.79e-06

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 46.61  E-value: 6.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNvekylsKCLNSIL--------EQTYKEIEIILVNDGSTDNSKDIAVSycerfpnIFKYFEKDNG-------- 65
Cdd:PLN02726   12 SIIVPTYN------ERLNIALivylifkaLQDVKDFEIIVVDDGSPDGTQDVVKQ-------LQKVYGEDRIllrprpgk 78

                          90       100
                  ....*....|....*....|....*
gi 1788517916  66 -GLSSARNFGLEKISGDFVGFLDSD 89
Cdd:PLN02726   79 lGLGTAYIHGLKHASGDFVVIMDAD 103
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
 2-126 1.49e-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: 44.90  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   2 SIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDIAVSYCERFPNIFKYF---EKDNGGLSSARNF--GLE 76
Cdd:cd02520     4 SILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLligGEKVGINPKVNNLikGYE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1788517916  77 KISGDFVGFLDSDDYIDNDLYEIMINSL-DSSIKIVECDFIweyeNGKSVL 126
Cdd:cd02520    84 EARYDILVISDSDISVPPDYLRRMVAPLmDPGVGLVTCLCA----FGKSMA 130
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 8-45 1.66e-05

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


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 44.93  E-value: 1.66e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1788517916   8 YNVEKYLSKCLNSILEQTYKEIEIILVNDGSTDNSKDI 45
Cdd:cd04185     6 YNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEW 43
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 3-89 2.35e-05

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: 44.83  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   3 IIIPIYNVEKYLSKCLNSILEQTYK-EIEIILVNDGSTDNSKDIAVSYCERFPNIFKYFEKDNGGLSSARNFGLEKISGD 81
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGiDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGD 80


                  ....*...
gi 1788517916  82 FVGFLDSD 89
Cdd:cd06442    81 VIVVMDAD 88
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 1-89 4.03e-05

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 44.17  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   1 MSIIIPIYN-VEKYLSKCLNSILEQtyKEIEIILVNDGSTDNSKDIaVSYCERFPNIFKYFEKdNGGLSSARNFGLEKIS 79
Cdd:cd06434     2 VTVIIPVYDeDPDVFRECLRSILRQ--KPLEIIVVTDGDDEPYLSI-LSQTVKYGGIFVITVP-HPGKRRALAEGIRHVT 77

                          90
                  ....*....|
gi 1788517916  80 GDFVGFLDSD 89
Cdd:cd06434    78 TDIVVLLDSD 87
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 1-111 1.07e-04

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 43.22  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   1 MSIIIPIYNVEKYLSKCLNSI---LEQTYKE-----IEIILVNDGSTDNSKDIAVSYCER--FPNI-FKYFE-KDNGGLS 68
Cdd:PTZ00260   72 LSIVIPAYNEEDRLPKMLKETikyLESRSRKdpkfkYEIIIVNDGSKDKTLKVAKDFWRQniNPNIdIRLLSlLRNKGKG 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1788517916  69 SARNFGLEKISGDFVGFLDSDDYID----NDLYEIMINSLDSSIKIV 111
Cdd:PTZ00260  152 GAVRIGMLASRGKYILMVDADGATDiddfDKLEDIMLKIEQNGLGIV 198
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
1-90 5.58e-04

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 40.75  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788517916   1 MSIIIPIYNVEKYLSKCLNSILEQTYKEIEIILVNDGSTdnSKDIAVSYCERF--PNIfKYFEKD-NGGLSSARNFGLEK 77
Cdd:PRK10018    7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCST--SWEQLQQYVTALndPRI-TYIHNDiNSGACAVRNQAIML 83

                          90
                  ....*....|...
gi 1788517916  78 ISGDFVGFLDSDD 90
Cdd:PRK10018   84 AQGEYITGIDDDD 96
 
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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