NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1615985769|gb|THA10091|]
View 

glycosyltransferase [Rodentibacter pneumotropicus]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 3-204 1.90e-95

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd04195:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 201  Bit Score: 278.81  E-value: 1.90e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   3 SILLSLYHKEREEYLAACLDSLIVQTCPVSEVIIVFDGAIKKSLEEIVVQYQAYLPIKIIRLKYNLGLGKALNEGLKYCS 82
Cdd:cd04195     1 SVLMSVYIKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  83 YEWIFRMDTDDVCLPDRFKKQLEYINSHPNIALLGTQVAEFDETMKSIIGVKqVPISKLEIEKFALKRNPFNHMTVAYRK 162
Cdd:cd04195    81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRR-LPTSHDDILKFARRRSPFNHPTVMFRK 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1615985769 163 SIIEKVGGYQHHLYMEDYNLWLRIIAKGYEVANLPEILVNVR 204
Cdd:cd04195   160 SKVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVKAR 201
 
Name Accession Description Interval E-value
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 3-204 1.90e-95

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: 278.81  E-value: 1.90e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   3 SILLSLYHKEREEYLAACLDSLIVQTCPVSEVIIVFDGAIKKSLEEIVVQYQAYLPIKIIRLKYNLGLGKALNEGLKYCS 82
Cdd:cd04195     1 SVLMSVYIKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  83 YEWIFRMDTDDVCLPDRFKKQLEYINSHPNIALLGTQVAEFDETMKSIIGVKqVPISKLEIEKFALKRNPFNHMTVAYRK 162
Cdd:cd04195    81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRR-LPTSHDDILKFARRRSPFNHPTVMFRK 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1615985769 163 SIIEKVGGYQHHLYMEDYNLWLRIIAKGYEVANLPEILVNVR 204
Cdd:cd04195   160 SKVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVKAR 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-219 8.82e-33

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 119.04  E-value: 8.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   1 MYSILLSLYhkEREEYLAACLDSLIVQTCPVSEVIIVFDGAIKKSLEeIVVQYQAYLP-IKIIRLKYNLGLGKALNEGLK 79
Cdd:COG0463     3 LVSVVIPTY--NEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAE-ILRELAAKDPrIRVIRLERNRGKGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  80 YCSYEWIFRMDTDDVCLPDRFKKQLEYINSHPNIALLGTQVAEFDETMKSIIGVKQvpiskLEIEKFALKRNPFNHMTVA 159
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRL-----FNLVRLLTNLPDSTSGFRL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769 160 YRKSIIEKVgGYQHHlYMEDYNLwLRIIAKGYEVANLPeilVNVRSGIQMYTRRKGLSYI 219
Cdd:COG0463   155 FRREVLEEL-GFDEG-FLEDTEL-LRALRHGFRIAEVP---VRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 3-167 3.93e-27

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: 102.86  E-value: 3.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   3 SILLSLYHkeREEYLAACLDSLIVQTCPVSEVIIVFDGAiKKSLEEIVVQY-QAYLPIKIIRLKYNLGLGKALNEGLKYC 81
Cdd:pfam00535   1 SVIIPTYN--EEKYLLETLESLLNQTYPNFEIIVVDDGS-TDGTVEIAEEYaKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  82 SYEWIFRMDTDDVCLPDRFKKQLEYINSHPNIALLGTQVAEFDET--MKSIIGVKQVPISKLEIEKFALKRNPFNHMTVA 159
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETgeYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFA 157


                  ....*....
gi 1615985769 160 -YRKSIIEK 167
Cdd:pfam00535 158 lYRREALEE 166
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 1-178 7.25e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 55.44  E-value: 7.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   1 MYSILLSLYHKEReeYLAACLDSLIVQTCPVSEVIIVFDGAIKKSLeEIVVQYQAYLP-IKIIRLKyNLGLGKALNEGLK 79
Cdd:PRK10073    7 KLSIIIPLYNAGK--DFRAFMESLIAQTWTALEIIIVNDGSTDNSV-EIAKHYAENYPhVRLLHQA-NAGVSVARNTGLA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  80 YCSYEWIFRMDTDDVCLPDRFKKQLEY-INSHPNIALL-GTQVAEFDETMKSIIGVKQVP----ISKLEIEKFALKRNPF 153
Cdd:PRK10073   83 VATGKYVAFPDADDVVYPTMYETLMTMaLEDDLDVAQCnADWCFRDTGETWQSIPSDRLRstgvLSGPDWLRMALSSRRW 162

                         170       180
                  ....*....|....*....|....*..
gi 1615985769 154 NHMT--VAYRKSIIEKvggyqHHLYME 178
Cdd:PRK10073  163 THVVwlGVYRRDFIVK-----NNIKFE 184
 
Name Accession Description Interval E-value
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 3-204 1.90e-95

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: 278.81  E-value: 1.90e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   3 SILLSLYHKEREEYLAACLDSLIVQTCPVSEVIIVFDGAIKKSLEEIVVQYQAYLPIKIIRLKYNLGLGKALNEGLKYCS 82
Cdd:cd04195     1 SVLMSVYIKEKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  83 YEWIFRMDTDDVCLPDRFKKQLEYINSHPNIALLGTQVAEFDETMKSIIGVKqVPISKLEIEKFALKRNPFNHMTVAYRK 162
Cdd:cd04195    81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRR-LPTSHDDILKFARRRSPFNHPTVMFRK 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1615985769 163 SIIEKVGGYQHHLYMEDYNLWLRIIAKGYEVANLPEILVNVR 204
Cdd:cd04195   160 SKVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVKAR 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-219 8.82e-33

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 119.04  E-value: 8.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   1 MYSILLSLYhkEREEYLAACLDSLIVQTCPVSEVIIVFDGAIKKSLEeIVVQYQAYLP-IKIIRLKYNLGLGKALNEGLK 79
Cdd:COG0463     3 LVSVVIPTY--NEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAE-ILRELAAKDPrIRVIRLERNRGKGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  80 YCSYEWIFRMDTDDVCLPDRFKKQLEYINSHPNIALLGTQVAEFDETMKSIIGVKQvpiskLEIEKFALKRNPFNHMTVA 159
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRL-----FNLVRLLTNLPDSTSGFRL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769 160 YRKSIIEKVgGYQHHlYMEDYNLwLRIIAKGYEVANLPeilVNVRSGIQMYTRRKGLSYI 219
Cdd:COG0463   155 FRREVLEEL-GFDEG-FLEDTEL-LRALRHGFRIAEVP---VRYRAGESKLNLRDLLRLL 208
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 2-212 3.28e-29

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: 112.14  E-value: 3.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   2 YSILLSLYHkeREEYLAACLDSLIVQTCPVS--EVIIVFDGAiKKSLEEIVVQYQA-YLPIKIIRLKYNLGLGKALNEGL 78
Cdd:COG1215    31 VSVIIPAYN--EEAVIEETLRSLLAQDYPKEklEVIVVDDGS-TDETAEIARELAAeYPRVRVIERPENGGKAAALNAGL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  79 KYCSYEWIFRMDTDDVCLPDRFKKQLEYInSHPNIALLGTqvaefdetmksiigvkqvpiskleiekfalkrnpfnhmTV 158
Cdd:COG1215   108 KAARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGASGA--------------------------------------NL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769 159 AYRKSIIEKVGGYQHHLYMEDYNLWLRIIAKGYEVANLPEILV------NVRSGIQMYTR 212
Cdd:COG1215   149 AFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVyeeapeTLRALFRQRRR 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 3-167 3.93e-27

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: 102.86  E-value: 3.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   3 SILLSLYHkeREEYLAACLDSLIVQTCPVSEVIIVFDGAiKKSLEEIVVQY-QAYLPIKIIRLKYNLGLGKALNEGLKYC 81
Cdd:pfam00535   1 SVIIPTYN--EEKYLLETLESLLNQTYPNFEIIVVDDGS-TDGTVEIAEEYaKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  82 SYEWIFRMDTDDVCLPDRFKKQLEYINSHPNIALLGTQVAEFDET--MKSIIGVKQVPISKLEIEKFALKRNPFNHMTVA 159
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETgeYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFA 157


                  ....*....
gi 1615985769 160 -YRKSIIEK 167
Cdd:pfam00535 158 lYRREALEE 166
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 13-191 3.19e-23

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: 92.57  E-value: 3.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  13 REEYLAACLDSLIVQTCPVSEVIIVFDGAIKKSLEEIVVQYQAYLPIKIIRLKYNLGLGKALNEGLKYCSYEWIFRMDTD 92
Cdd:cd00761     8 EEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEYILFLDAD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  93 DVCLPDRFKKQLEYINSHPNIALLGTQvaefdetmksiigvkqvpiskleiekfalkrnpfnhMTVAYRKSIIEKVGGYQ 172
Cdd:cd00761    88 DLLLPDWLERLVAELLADPEADAVGGP------------------------------------GNLLFRRELLEEIGGFD 131

                         170       180
                  ....*....|....*....|.
gi 1615985769 173 HHL--YMEDYNLWLRIIAKGY 191
Cdd:cd00761   132 EALlsGEEDDDFLLRLLRGGK 152
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 3-200 1.20e-22

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: 92.27  E-value: 1.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   3 SILLSLYHKErEEYLAACLDSLIVQTCPVSEVIIVFDGAIKKSLEEIVVQYQAYLP-IKIIRLKYNLGLGKALNEGLKYC 81
Cdd:cd04184     4 SIVMPVYNTP-EKYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPrIKVVFREENGGISAATNSALELA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  82 SYEWIFRMDTDDVCLPDRFKKQLEYINSHPNIALLGTqvaefDETMKSIIGVKQVPISK--LEIEKFaLKRNPFNHMTVa 159
Cdd:cd04184    83 TGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYS-----DEDKIDEGGKRSEPFFKpdWSPDLL-LSQNYIGHLLV- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1615985769 160 YRKSIIEKVGGY-------QhhlymeDYNLWLRIIAKGYEVANLPEIL 200
Cdd:cd04184   156 YRRSLVRQVGGFregfegaQ------DYDLVLRVSEHTDRIAHIPRVL 197
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
3-201 1.83e-22

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 91.59  E-value: 1.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   3 SILLSLYHkeREEYLAACLDSLIVQTCPVSEVIIVFDGAIKKSLEeiVVQYQAYLPIKIIRLKYNLGLGKALNEGLKYCS 82
Cdd:COG1216     6 SVVIPTYN--RPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAE--LLAALAFPRVRVIRNPENLGFAAARNLGLRAAG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  83 YEWIFRMDTDDVCLPDRFKKQLEYINshpniallgtqvaefdetmksiigvkqvpiskleiekfalkrnpfnhmtVAYRK 162
Cdd:COG1216    82 GDYLLFLDDDTVVEPDWLERLLAAAC-------------------------------------------------LLIRR 112

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1615985769 163 SIIEKVGGY--QHHLYMEDYNLWLRIIAKGYEVANLPEILV 201
Cdd:COG1216   113 EVFEEVGGFdeRFFLYGEDVDLCLRLRKAGYRIVYVPDAVV 153
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 14-206 1.52e-19

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: 83.75  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  14 EEYLAACLDSLIVQTCPVSEVIIVfDGAIKKSLEEIVVQYQAYLpIKIIRLKYNlGLGKALNEGLKYCSYEWIFRMDTDD 93
Cdd:cd06433    10 AETLEETIDSVLSQTYPNIEYIVI-DGGSTDGTVDIIKKYEDKI-TYWISEPDK-GIYDAMNKGIALATGDIIGFLNSDD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  94 VCLPDRFKKQLEYINSHPNIALLGTQVAEFDETmKSIIGVKQVPISKLeieKFALKRNPFNHMTVAYRKSIIEKVGGYQH 173
Cdd:cd06433    87 TLLPGALLAVVAAFAEHPEVDVVYGDVLLVDEN-GRVIGRRRPPPFLD---KFLLYGMPICHQATFFRRSLFEKYGGFDE 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1615985769 174 HL-YMEDYNLWLRIIAKGYEVANLPEILVNVRSG 206
Cdd:cd06433   163 SYrIAADYDLLLRLLLAGKIFKYLPEVLAAFRLG 196
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 10-201 4.27e-19

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: 81.84  E-value: 4.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  10 HKEREEYLAACLDSLIVQTCPVSEVIIVFDGAIKKSLEEIVVQYQAylpIKIIRLKYNLGLGKALNEGLKYCSYEWIFRM 89
Cdd:cd04186     5 NYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPE---VRLIRNGENLGFGAGNNQGIREAKGDYVLLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  90 DTDDVCLPDRFKKQLEYINSHPNIALLGTQVAefdetmksiiGVkqvpiskleiekFALkrnpfnhmtvaYRKSIIEKVG 169
Cdd:cd04186    82 NPDTVVEPGALLELLDAAEQDPDVGIVGPKVS----------GA------------FLL-----------VRREVFEEVG 128

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1615985769 170 GYQH--HLYMEDYNLWLRIIAKGYEVANLPEILV 201
Cdd:cd04186   129 GFDEdfFLYYEDVDLCLRARLAGYRVLYVPQAVI 162
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 3-204 1.13e-14

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: 70.74  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   3 SILLSLYHKEReeYLAACLDSLIVQTCPVSEVIIVFDGAiKKSLEEIVVQYQA--YLPIKIIRLKYNLGLGKALNEGLKY 80
Cdd:cd04196     1 AVLMATYNGEK--YLREQLDSILAQTYKNDELIISDDGS-TDGTVEIIKEYIDkdPFIIILIRNGKNLGVARNFESLLQA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  81 CSYEWIFRMDTDDVCLPDRFKKQLEYINSHPNIALLGTQVAEFDETMKsIIGVKQ---VPISKLEIEKFALKRNPFNHMT 157
Cdd:cd04196    78 ADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELVDENGN-PIGESFfeyQKIKPGTSFNNLLFQNVVTGCT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1615985769 158 VAYRKSIIEKVGGYQ-HHLYMEDYnlWLRIIAKGY-EVANLPEILVNVR 204
Cdd:cd04196   157 MAFNRELLELALPFPdADVIMHDW--WLALLASAFgKVVFLDEPLILYR 203
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 3-201 6.47e-14

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: 69.57  E-value: 6.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   3 SILLSLYHKEReeYLAACLDSLIVQTCPVSEV-IIVFDGAIKKSLEEIVVQYQAYLPIkiIRLKYNLG--LGKALNEGLK 79
Cdd:cd02525     3 SIIIPVRNEEK--YIEELLESLLNQSYPKDLIeIIVVDGGSTDGTREIVQEYAAKDPR--IRLIDNPKriQSAGLNIGIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  80 YCSYEWIFRMDTDDVCLPDRFKKQLEYINSHPNIALLGTQVAEFDETMKSIIGVKQvpISKLEIEKFALKRNPFNHMTV- 158
Cdd:cd02525    79 NSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIAVAQ--SSPLGSGGSAYRGGAVKIGYVd 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1615985769 159 -----AYRKSIIEKVGGYQHHLYM-EDYNLWLRIIAKGYEVANLPEILV 201
Cdd:cd02525   157 tvhhgAYRREVFEKVGGFDESLVRnEDAELNYRLRKAGYKIWLSPDIRV 205
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 10-179 2.87e-10

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: 58.01  E-value: 2.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  10 HKErEEYLAACLDSLIVQTCPVSEVIIVFDGAiKKSLEEIVVQYQA--YLPIKIIRLKYNLGLGKALNEGLKYCSYEWIF 87
Cdd:cd06423     6 YNE-EAVIERTIESLLALDYPKLEVIVVDDGS-TDDTLEILEELAAlyIRRVLVVRDKENGGKAGALNAGLRHAKGDIVV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  88 RMDTDDV--------CLPDRFKKQ--------LEYINSHPNIaLLGTQVAEFDetmkSIIGVKQvpiskleiekfaLKRN 151
Cdd:cd06423    84 VLDADTIlepdalkrLVVPFFADPkvgavqgrVRVRNGSENL-LTRLQAIEYL----SIFRLGR------------RAQS 146

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1615985769 152 PFNHMTV------AYRKSIIEKVGGYQHHLYMED 179
Cdd:cd06423   147 ALGGVLVlsgafgAFRREALREVGGWDEDTLTED 180
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 8-202 4.42e-10

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


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 58.45  E-value: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   8 LYHKEREEyLAACLDSLIVQTCPvsevIIVFD--GAIKKSLEEIVVQYQaylpIKIIRLKYNLGLGKALNEGLKY---CS 82
Cdd:cd02526     5 TYNPDLSK-LKELLAALAEQVDK----VVVVDnsSGNDIELRLRLNSEK----IELIHLGENLGIAKALNIGIKAaleNG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  83 YEWIFRMDTDDVCLPDRFKKQLEYINS---HPNIALLGTQVaeFDETMKSIIGVKQVPISKLEIEKFALKRnPFNHMTV- 158
Cdd:cd02526    76 ADYVLLFDQDSVPPPDMVEKLLAYKILsdkNSNIGAVGPRI--IDRRTGENSPGVRKSGYKLRIQKEGEEG-LKEVDFLi 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1615985769 159 ----AYRKSIIEKVGGYQHHLYME--DYNLWLRIIAKGYEVANLPEILVN 202
Cdd:cd02526   153 tsgsLISLEALEKVGGFDEDLFIDyvDTEWCLRARSKGYKIYVVPDAVLK 202
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 1-215 6.57e-10

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 57.77  E-value: 6.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   1 MYSILLSLYHkeREEYLAACLDSLIVQTCPVSEVIIVFDG---AIKKSLEEIVVQYQAyLPIKIIRLKYNLGLG---KAL 74
Cdd:pfam13641   3 DVSVVVPAFN--EDSVLGRVLEAILAQPYPPVEVVVVVNPsdaETLDVAEEIAARFPD-VRLRVIRNARLLGPTgksRGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  75 NEGLKYCSYEWIFRMDTDDVCLPDRFKKQLEYInSHPNIALLGTQV-AEFDETMKSIIGVKQVPISKLEIEKFALKRN-- 151
Cdd:pfam13641  80 NHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF-DSPKVGAVGTPVfSLNRSTMLSALGALEFALRHLRMMSLRLALGvl 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1615985769 152 PFNHMTVAYRKSIIEKVGGYQHHLYM-EDYNLWLRIIAKGYEVANLPEILVNV--RSGIQMYTRRKG 215
Cdd:pfam13641 159 PLSGAGSAIRREVLKELGLFDPFFLLgDDKSLGRRLRRHGWRVAYAPDAAVRTvfPTYLAASIKQRA 225
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 14-197 1.03e-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: 57.30  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  14 EEYLAACLDSLIVQTCPVS--EVIIVFDGAIKKSLEEIVVQYQ-AYLPIKIIRLKYNLGLGK--ALNEGLKYCSYEWIFR 88
Cdd:cd04192     9 AENLPRLLQSLSALDYPKEkfEVILVDDHSTDGTVQILEFAAAkPNFQLKILNNSRVSISGKknALTTAIKAAKGDWIVT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  89 MDTDDVCLPDRFKKQLEYINSHPNIALLG-------------TQVAEFDETMKSIIGVkqvpiSKLEIEKFALKRNpfnh 155
Cdd:cd04192    89 TDADCVVPSNWLLTFVAFIQKEQIGLVAGpviyfkgksllakFQRLDWLSLLGLIAGS-----FGLGKPFMCNGAN---- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1615985769 156 mtVAYRKSIIEKVGGYQHHLYM--EDYNLWLRIIAKGY-EVANLP 197
Cdd:cd04192   160 --MAYRKEAFFEVGGFEGNDHIasGDDELLLAKVASKYpKVAYLK 202
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 1-178 7.25e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 55.44  E-value: 7.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   1 MYSILLSLYHKEReeYLAACLDSLIVQTCPVSEVIIVFDGAIKKSLeEIVVQYQAYLP-IKIIRLKyNLGLGKALNEGLK 79
Cdd:PRK10073    7 KLSIIIPLYNAGK--DFRAFMESLIAQTWTALEIIIVNDGSTDNSV-EIAKHYAENYPhVRLLHQA-NAGVSVARNTGLA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  80 YCSYEWIFRMDTDDVCLPDRFKKQLEY-INSHPNIALL-GTQVAEFDETMKSIIGVKQVP----ISKLEIEKFALKRNPF 153
Cdd:PRK10073   83 VATGKYVAFPDADDVVYPTMYETLMTMaLEDDLDVAQCnADWCFRDTGETWQSIPSDRLRstgvLSGPDWLRMALSSRRW 162

                         170       180
                  ....*....|....*....|....*..
gi 1615985769 154 NHMT--VAYRKSIIEKvggyqHHLYME 178
Cdd:PRK10073  163 THVVwlGVYRRDFIVK-----NNIKFE 184
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 13-120 8.70e-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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 54.18  E-value: 8.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  13 REEYLAACLDSLIVQTCPVSEVIIVfDGAIKKSLEEIVVQYQAYLPIKIIRLKYNLGLGKALNEGLKY---CSYEWIFRM 89
Cdd:cd04185     8 RLDLLKECLDALLAQTRPPDHIIVI-DNASTDGTAEWLTSLGDLDNIVYLRLPENLGGAGGFYEGVRRayeLGYDWIWLM 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1615985769  90 DTDDVCLPDRFKKQLEYINSHPNIALLGTQV 120
Cdd:cd04185    87 DDDAIPDPDALEKLLAYADKDNPQFLAPLVL 117
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 14-120 9.65e-07

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: 48.61  E-value: 9.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  14 EEYLAACLDSLIVQTCPVSEVIIVFDGAIKKSLEEIVVQYQAYL-----PIKIIRLKYN--LGLGKALNEGLKYCSYEWI 86
Cdd:cd06913     9 EQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLedsgvIVLVGSHNSPspKGVGYAKNQAIAQSSGRYL 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1615985769  87 FRMDTDDVCLPDRFKKQLEYINSHPNiALLGTQV 120
Cdd:cd06913    89 CFLDSDDVMMPQRIRLQYEAALQHPN-SIIGCQV 121
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 13-208 1.23e-06

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: 47.57  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  13 REEYLAACLDSLIVQTCPVSEVIIVFDGAiKKSLEEIVVQYQAYLPIKIIRLKY-NLG--LGKALNEGLKYCSYEWIFRM 89
Cdd:cd06420     8 RPEALELVLKSVLNQSILPFEVIIADDGS-TEETKELIEEFKSQFPIPIKHVWQeDEGfrKAKIRNKAIAAAKGDYLIFI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  90 DTDdvCLPDRfkkqlEYINSHPNIALLGTQVaefdetmksiIGvKQVPISKLEIEKFalkrnpFNHMTVAYRKSIIEKVG 169
Cdd:cd06420    87 DGD--CIPHP-----DFIADHIELAEPGVFL----------SG-SRVLLNEKLTERG------IRGCNMSFWKKDLLAVN 142

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1615985769 170 GyqhhlYMEDYNLWlriiakGYEVANLPEILVNvrSGIQ 208
Cdd:cd06420   143 G-----FDEEFTGW------GGEDSELVARLLN--SGIK 168
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 14-98 1.59e-06

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 48.05  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  14 EEYLAACLDSliVQTCpVSEVIIVFDGAIKKSLEeIVVQYQAylpiKIIRLKYNlGLGKALNEGLKYCSYEWIFRMDTDD 93
Cdd:cd02511    12 ERNIERCLES--VKWA-VDEIIVVDSGSTDRTVE-IAKEYGA----KVYQRWWD-GFGAQRNFALELATNDWVLSLDADE 82


                  ....*
gi 1615985769  94 VCLPD 98
Cdd:cd02511    83 RLTPE 87
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 3-206 1.83e-06

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: 48.04  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   3 SILLSLYHKEREEYLAACLDSLIVQTCPVSEVIIVFDGAIKKSLEEI----VVQYQAYLPIKIirlKYNLGLGKALNEGL 78
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVssikDHNLQVYYPNAP---DTTYSLAASRNRGT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  79 KYCSYEWIFRMDTDDVCLPDRFKKQLEYINS-----HPNIALLGTQVAEFDETMKSIIGVKQVPISKLEIEKFALKRNPF 153
Cdd:pfam10111  78 SHAIGEYISFIDGDCLWSPDKFEKQLKIATSlalqeNIQAAVVLPVTDLNDESSNFLRRGGDLTASGDVLRDLLVFYSPL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1615985769 154 ------NHMTVAYRKSIIEKVGGYQHHLY---MEDYNLWLRIIAKGYEVANLP-EILVNVRSG 206
Cdd:pfam10111 158 aiffapNSSNALINRQAFIEVGGFDESFRghgAEDFDIFLRLAARYPFVAVMPpQLLYRLSAK 220
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 14-92 1.45e-04

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: 41.69  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769  14 EEYLAAC---LDSLIVQTCPVSEVIIVFDGAIKKSLEEIVVQYQAYLPIKIIRLKYNLGLGKALNEGLKYCSYEWIFRMD 90
Cdd:cd04187     9 EENLPELyerLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHARGDAVITMD 88


                  ..
gi 1615985769  91 TD 92
Cdd:cd04187    89 AD 90
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 2-105 2.44e-04

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 41.61  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1615985769   2 YSILLSLYHkEREEylAACLDSLI---VQTCPVSEVIIVFDGAiKKSLEEIVVQYQAYLPIKIIRLKY---NLGLGKALN 75
Cdd:PLN02726   11 YSIIVPTYN-ERLN--IALIVYLIfkaLQDVKDFEIIVVDDGS-PDGTQDVVKQLQKVYGEDRILLRPrpgKLGLGTAYI 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1615985769  76 EGLKYCSYEWIFRMDTD----DVCLPDRFKKQLE 105
Cdd:PLN02726   87 HGLKHASGDFVVIMDADlshhPKYLPSFIKKQRE 120
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 33-92 1.44e-03

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: 38.70  E-value: 1.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1615985769  33 EVIIVFDGAIKKSLEeIVVQYQAYLP--IKIIRLKYNLGLGKALNEGLKYCSYEWIFRMDTD 92
Cdd:cd04188    32 EIIVVDDGSKDGTAE-VARKLARKNPalIRVLTLPKNRGKGGAVRAGMLAARGDYILFADAD 92
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 33-92 4.88e-03

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: 37.51  E-value: 4.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1615985769  33 EVIIVFDGAIKKSLEeIVVQYQA-YLPIKIIRLKYNLGLGKALNEGLKYCSYEWIFRMDTD 92
Cdd:cd06442    29 EIIVVDDNSPDGTAE-IVRELAKeYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDAD 88
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH