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Conserved domains on  [gi|488197620|ref|WP_002268828|]
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glycosyltransferase family 8 protein [Streptococcus mutans]

Protein Classification

glycosyltransferase family 8 protein( domain architecture ID 11444513)

glycosyltransferase family 8 protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Escherichia coli lipopolysaccharide 1,2-glucosyltransferase, which adds the glucose(II) group on the galactose(I) group of LPS

CATH:  3.90.550.10
CAZY:  GT8
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1-271 1.56e-87

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 262.60  E-value: 1.56e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620   1 MTESSINLLFSIDNRFVEQFKVTLYSLYQNTSNKNLKIYMLQKELLADHKA-IERFCYQLGLSYEPIIIGEEDFKDAPVS 79
Cdd:COG1442    1 MNKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKErLEALAAKYNVSIEFIDVDDELLKDLPVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620  80 DRYPETIYYRLLAQDYLPKNLDKILYLDADILCLNDIVPLYQMDMKNYIYAAASH-VSDKSITDIVNKLRLNnfEAEGYF 158
Cdd:COG1442   81 KHISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDgTVTGSQKKRAKRLGLP--DDDGYF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620 159 NSGVLLMNLEQCRQKIKPQDIMNYISRKGNTLLLPDQDVLNALYGTKTHLIPDEiYNYDARYNIIYFTRSLGeWDLDWVI 238
Cdd:COG1442  159 NSGVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPR-YNYQYSLYYELKDKSNK-KELLEAR 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 488197620 239 ENTVFLHFCGKDKPWRKDYKGRYAALYKHYQHR 271
Cdd:COG1442  237 KNPVIIHYTGPTKPWHKWCTHPYADLYWEYLKK 269
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1-271 1.56e-87

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 262.60  E-value: 1.56e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620   1 MTESSINLLFSIDNRFVEQFKVTLYSLYQNTSNKNLKIYMLQKELLADHKA-IERFCYQLGLSYEPIIIGEEDFKDAPVS 79
Cdd:COG1442    1 MNKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKErLEALAAKYNVSIEFIDVDDELLKDLPVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620  80 DRYPETIYYRLLAQDYLPKNLDKILYLDADILCLNDIVPLYQMDMKNYIYAAASH-VSDKSITDIVNKLRLNnfEAEGYF 158
Cdd:COG1442   81 KHISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDgTVTGSQKKRAKRLGLP--DDDGYF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620 159 NSGVLLMNLEQCRQKIKPQDIMNYISRKGNTLLLPDQDVLNALYGTKTHLIPDEiYNYDARYNIIYFTRSLGeWDLDWVI 238
Cdd:COG1442  159 NSGVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPR-YNYQYSLYYELKDKSNK-KELLEAR 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 488197620 239 ENTVFLHFCGKDKPWRKDYKGRYAALYKHYQHR 271
Cdd:COG1442  237 KNPVIIHYTGPTKPWHKWCTHPYADLYWEYLKK 269
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
6-255 1.86e-70

A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.


Pssm-ID: 133037 [Multi-domain]  Cd Length: 248  Bit Score: 217.47  E-value: 1.86e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620   6 INLLFSIDNRFVEQFKVTLYSLYQNTSNKNLKIYMLQKELLADHK-AIERFCYQLGLSYEPIIIGEEDFKDAP-VSDRYP 83
Cdd:cd04194    1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKkKLKELLKKYNSSIEFIKIDNDDFKFFPaTTDHIS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620  84 ETIYYRLLAQDYLPkNLDKILYLDADILCLNDIVPLYQMDMKNYIYAAASHVSDKSITDivNKLRLNNFEAEGYFNSGVL 163
Cdd:cd04194   81 YATYYRLLIPDLLP-DYDKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKK--RKRRLGGYDDGSYFNSGVL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620 164 LMNLEQCRQKIKPQDIMNYISRKGNTLLLPDQDVLNALYGTKTHLIPdEIYNYDARYNIIYFTRSLGEWDLDWVIENTVF 243
Cdd:cd04194  158 LINLKKWREENITEKLLELIKEYGGRLIYPDQDILNAVLKDKILYLP-PRYNFQTGFYYLLKKKSKEEQELEEARKNPVI 236
                        250
                 ....*....|..
gi 488197620 244 LHFCGKDKPWRK 255
Cdd:cd04194  237 IHYTGSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
7-256 2.89e-34

Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.


Pssm-ID: 279798 [Multi-domain]  Cd Length: 252  Bit Score: 124.36  E-value: 2.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620    7 NLLFSIDNRFVEQFKVTLYSLYQNTSNKNLKIYMLQKELLADHKAIERfcyQLGLSYEPIIIGEE---------DFKDAP 77
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILN---WLASSYKPVLPLLEsdikifeyfSKLKLR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620   78 VSDRYPETIYYRLLAQDYLPKnLDKILYLDADILCLNDIVPLYQMDMKNYIYAAashVSDKSITDIVNK---LRLNNFEA 154
Cdd:pfam01501  78 SPKYWSLLNYLRLYLPDLFPK-LDKILYLDADIVVQGDLSPLWDIDLGGKVLAA---VEDNYFQRYPNFsepIILENFGP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620  155 EG-YFNSGVLLMNLEQCRQkikpQDIMNY------ISRKGNTLLLPDQDVLNALYGTKTHLIpdeiynyDARYNIIYFTR 227
Cdd:pfam01501 154 PAcYFNAGMLLFDLDAWRK----ENITERyikwlnLNENRTLWKLGDQDPLNIVFYGKVKPL-------DPRWNVLGLGY 222
                         250       260
                  ....*....|....*....|....*....
gi 488197620  228 SLGEWDLDWVIENTVFLHFCGKDKPWRKD 256
Cdd:pfam01501 223 YNKKKSLNEITENAAVIHYNGPTKPWLDI 251
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
4-255 1.13e-19

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 87.11  E-value: 1.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620   4 SSINLLFSIDNRFVEQFKVTLYSLYQNTSNKNLKIYMLQKELLADHKAieRFcYQLGLSYEPII----IGEEDFKDAPVS 79
Cdd:PRK15171  24 NSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQ--RF-SALAKQYNTRIniylINCERLKSLPST 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620  80 DRYPETIYYRLLAQDYLPKNLDKILYLDADILCLNDIVPLYQMDM-KNYIYAAASHVSDKSITDIVNKLRLNNFeAEGYF 158
Cdd:PRK15171 101 KNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFaENEIAAVVAEGDAEWWSKRAQSLQTPGL-ASGYF 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620 159 NSGVLLMNLEQCRQkikpqdimNYISRKGNTLLL----------PDQDVLNALYGTKTHLIpDEIYNydARYNIIYftrS 228
Cdd:PRK15171 180 NSGFLLINIPAWAQ--------ENISAKAIEMLAdpeivsrithLDQDVLNILLAGKVKFI-DAKYN--TQFSLNY---E 245
                        250       260
                 ....*....|....*....|....*..
gi 488197620 229 LGEWDLDWVIENTVFLHFCGKDKPWRK 255
Cdd:PRK15171 246 LKDSVINPVNDETVFIHYIGPTKPWHS 272
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1-271 1.56e-87

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 262.60  E-value: 1.56e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620   1 MTESSINLLFSIDNRFVEQFKVTLYSLYQNTSNKNLKIYMLQKELLADHKA-IERFCYQLGLSYEPIIIGEEDFKDAPVS 79
Cdd:COG1442    1 MNKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKErLEALAAKYNVSIEFIDVDDELLKDLPVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620  80 DRYPETIYYRLLAQDYLPKNLDKILYLDADILCLNDIVPLYQMDMKNYIYAAASH-VSDKSITDIVNKLRLNnfEAEGYF 158
Cdd:COG1442   81 KHISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDgTVTGSQKKRAKRLGLP--DDDGYF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620 159 NSGVLLMNLEQCRQKIKPQDIMNYISRKGNTLLLPDQDVLNALYGTKTHLIPDEiYNYDARYNIIYFTRSLGeWDLDWVI 238
Cdd:COG1442  159 NSGVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPR-YNYQYSLYYELKDKSNK-KELLEAR 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 488197620 239 ENTVFLHFCGKDKPWRKDYKGRYAALYKHYQHR 271
Cdd:COG1442  237 KNPVIIHYTGPTKPWHKWCTHPYADLYWEYLKK 269
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
6-255 1.86e-70

A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.


Pssm-ID: 133037 [Multi-domain]  Cd Length: 248  Bit Score: 217.47  E-value: 1.86e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620   6 INLLFSIDNRFVEQFKVTLYSLYQNTSNKNLKIYMLQKELLADHK-AIERFCYQLGLSYEPIIIGEEDFKDAP-VSDRYP 83
Cdd:cd04194    1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKkKLKELLKKYNSSIEFIKIDNDDFKFFPaTTDHIS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620  84 ETIYYRLLAQDYLPkNLDKILYLDADILCLNDIVPLYQMDMKNYIYAAASHVSDKSITDivNKLRLNNFEAEGYFNSGVL 163
Cdd:cd04194   81 YATYYRLLIPDLLP-DYDKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKK--RKRRLGGYDDGSYFNSGVL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620 164 LMNLEQCRQKIKPQDIMNYISRKGNTLLLPDQDVLNALYGTKTHLIPdEIYNYDARYNIIYFTRSLGEWDLDWVIENTVF 243
Cdd:cd04194  158 LINLKKWREENITEKLLELIKEYGGRLIYPDQDILNAVLKDKILYLP-PRYNFQTGFYYLLKKKSKEEQELEEARKNPVI 236
                        250
                 ....*....|..
gi 488197620 244 LHFCGKDKPWRK 255
Cdd:cd04194  237 IHYTGSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
7-256 2.89e-34

Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.


Pssm-ID: 279798 [Multi-domain]  Cd Length: 252  Bit Score: 124.36  E-value: 2.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620    7 NLLFSIDNRFVEQFKVTLYSLYQNTSNKNLKIYMLQKELLADHKAIERfcyQLGLSYEPIIIGEE---------DFKDAP 77
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILN---WLASSYKPVLPLLEsdikifeyfSKLKLR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620   78 VSDRYPETIYYRLLAQDYLPKnLDKILYLDADILCLNDIVPLYQMDMKNYIYAAashVSDKSITDIVNK---LRLNNFEA 154
Cdd:pfam01501  78 SPKYWSLLNYLRLYLPDLFPK-LDKILYLDADIVVQGDLSPLWDIDLGGKVLAA---VEDNYFQRYPNFsepIILENFGP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620  155 EG-YFNSGVLLMNLEQCRQkikpQDIMNY------ISRKGNTLLLPDQDVLNALYGTKTHLIpdeiynyDARYNIIYFTR 227
Cdd:pfam01501 154 PAcYFNAGMLLFDLDAWRK----ENITERyikwlnLNENRTLWKLGDQDPLNIVFYGKVKPL-------DPRWNVLGLGY 222
                         250       260
                  ....*....|....*....|....*....
gi 488197620  228 SLGEWDLDWVIENTVFLHFCGKDKPWRKD 256
Cdd:pfam01501 223 YNKKKSLNEITENAAVIHYNGPTKPWLDI 251
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
4-255 1.13e-19

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 87.11  E-value: 1.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620   4 SSINLLFSIDNRFVEQFKVTLYSLYQNTSNKNLKIYMLQKELLADHKAieRFcYQLGLSYEPII----IGEEDFKDAPVS 79
Cdd:PRK15171  24 NSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQ--RF-SALAKQYNTRIniylINCERLKSLPST 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620  80 DRYPETIYYRLLAQDYLPKNLDKILYLDADILCLNDIVPLYQMDM-KNYIYAAASHVSDKSITDIVNKLRLNNFeAEGYF 158
Cdd:PRK15171 101 KNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFaENEIAAVVAEGDAEWWSKRAQSLQTPGL-ASGYF 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620 159 NSGVLLMNLEQCRQkikpqdimNYISRKGNTLLL----------PDQDVLNALYGTKTHLIpDEIYNydARYNIIYftrS 228
Cdd:PRK15171 180 NSGFLLINIPAWAQ--------ENISAKAIEMLAdpeivsrithLDQDVLNILLAGKVKFI-DAKYN--TQFSLNY---E 245
                        250       260
                 ....*....|....*....|....*..
gi 488197620 229 LGEWDLDWVIENTVFLHFCGKDKPWRK 255
Cdd:PRK15171 246 LKDSVINPVNDETVFIHYIGPTKPWHS 272
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
26-255 6.47e-18

Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis; Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.


Pssm-ID: 132996 [Multi-domain]  Cd Length: 246  Bit Score: 80.56  E-value: 6.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620  26 SLYQNTSnKNLKIYMLQKELL-ADHKAIERFCYQLGLSYEPIIIGEEDFKDAPVSDRYPETIYYRLLAQDYLPKNLDKIL 104
Cdd:cd00505   22 SVLRHRT-KPLRFHVLTNPLSdTFKAALDNLRKLYNFNYELIPVDILDSVDSEHLKRPIKIVTLTKLHLPNLVPDYDKIL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620 105 YLDADILCLNDIVPLYQMDMKNYIYAAASHVSDKSITDiVNKLRLNNFEAEGYFNSGVLLMNLEQCRQKikpqDIMNYIS 184
Cdd:cd00505  101 YVDADILVLTDIDELWDTPLGGQELAAAPDPGDRREGK-YYRQKRSHLAGPDYFNSGVFVVNLSKERRN----QLLKVAL 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488197620 185 RKGNTLLLP----DQDVLNALYgtktHLIPDEIYNYDARYNIiyftRSLGEWD-LDWVIE---NTVFLHFCGKDKPWRK 255
Cdd:cd00505  176 EKWLQSLSSlsggDQDLLNTFF----KQVPFIVKSLPCIWNV----RLTGCYRsLNCFKAfvkNAKVIHFNGPTKPWNK 246
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
101-267 1.78e-12

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.


Pssm-ID: 133018 [Multi-domain]  Cd Length: 240  Bit Score: 65.36  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620 101 DKILYLDADILCLNDIVPLYqmDMKNYIYAAASHVSDKsitdivnklrlnnfeaegYFNSGVLLmnleqcrqkIKP---- 176
Cdd:cd02537   91 DKVVFLDADTLVLRNIDELF--DLPGEFAAAPDCGWPD------------------LFNSGVFV---------LKPseet 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620 177 -QDIMNYISRKGnTLLLPDQDVLNALYGTKTHLIP-DEIYNYDARYniiYFTRSLGEWDLDwvieNTVFLHFCGKDKPWR 254
Cdd:cd02537  142 fNDLLDALQDTP-SFDGGDQGLLNSYFSDRGIWKRlPFTYNALKPL---RYLHPEALWFGD----EIKVVHFIGGDKPWS 213
                        170
                 ....*....|...
gi 488197620 255 KDYKGRYAALYKH 267
Cdd:cd02537  214 WWRDPETKEKDDY 226
GT8_like_1 cd06429
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ...
81-268 4.50e-09

GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of glycosyltransferase family 8 with unknown function: Glycosyltransferase family 8 comprises enzymes with a number of known activities; lipopolysaccharide galactosyltransferase lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase and inositol 1-alpha-galactosyltransferase. It is classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed.


Pssm-ID: 133051 [Multi-domain]  Cd Length: 257  Bit Score: 55.86  E-value: 4.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620  81 RYPETIYYRLLAQDYLP---KNLDKILYLDADILCLNDIVPLYQMDMKNYIYAAASHVsdksitdivnklrlnnfeaegy 157
Cdd:cd06429   92 RKPEYISLLNFARFYLPelfPKLEKVIYLDDDVVVQKDLTELWNTDLGGGVAGAVETS---------------------- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620 158 FNSGVLLMNLEQCRQkikpQDI-------MNYISRKGNTL--LLPDQDVLNALYGTkthlipdeIYNYDARYNIIYFTRS 228
Cdd:cd06429  150 WNPGVNVVNLTEWRR----QNVtetyekwMELNQEEEVTLwkLITLPPGLIVFYGL--------TSPLDPSWHVRGLGYN 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 488197620 229 LGEWDLDwvIENTVFLHFCGKDKPWRKDYKGRYAALY-KHY 268
Cdd:cd06429  218 YGIRPQD--IKAAAVLHFNGNMKPWLRTAIPSYKELWeKYL 256
GT8_like_2 cd06430
GT8_like_2 represents a subfamily of GT8 with unknown function; A subfamily of ...
89-221 8.87e-06

GT8_like_2 represents a subfamily of GT8 with unknown function; A subfamily of glycosyltransferase family 8 with unknown function: Glycosyltransferase family 8 comprises enzymes with a number of known activities; lipopolysaccharide galactosyltransferase lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase and inositol 1-alpha-galactosyltransferase. It is classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed.


Pssm-ID: 133052  Cd Length: 304  Bit Score: 46.30  E-value: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488197620  89 RLLAQDYLPkNLDKILYLDADILCLNDIVPLYQMDMK---NYIYAAASHVSDKSITdivnklRLNNFEAEGYF-----NS 160
Cdd:cd06430   87 RLFLPSLLP-DVDSLLYVDTDILFLRPVEEIWSFLKKfnsTQLAAMAPEHEEPNIG------WYNRFARHPYYgktgvNS 159
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488197620 161 GVLLMNLEQCRQKIKPQDiMNYISRKGNTLLLP------------DQDVLNALYgtktHLIPDEIYNYDARYN 221
Cdd:cd06430  160 GVMLMNLTRMRRKYFKND-MTPVGLRWEEILMPlykkyklkitwgDQDLINIIF----HHNPEMLYVFPCHWN 227
PLN02910 PLN02910
polygalacturonate 4-alpha-galacturonosyltransferase
95-131 2.20e-03

polygalacturonate 4-alpha-galacturonosyltransferase


Pssm-ID: 215493 [Multi-domain]  Cd Length: 657  Bit Score: 39.16  E-value: 2.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 488197620  95 YLPK---NLDKILYLDADILCLNDIVPLYQMDMKNYIYAA 131
Cdd:PLN02910 467 YLPEvypKLEKILFLDDDIVVQKDLTPLWSIDMQGMVNGA 506
 
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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