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Conserved domains on  [gi|446298991|ref|WP_000376846|]
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MULTISPECIES: lipopolysaccharide 1,2-glucosyltransferase RfaJ [Enterobacteriaceae]

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

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 ...
24-325 2.45e-106

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


:

Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 313.06  E-value: 2.45e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  24 TAESLNVAYGVDSNYLDGVGVSITSIVINNRHVNLDFYIIADVYNDDFFQKVEKLAEQYQLRITLYRINTDNLQCLPCTQ 103
Cdd:COG1442    2 NKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 104 VWSRAMYFRLFAFQLLGVTLNRLLYLDADVVCKGNISQLLHLEFNGAVAAVVRDVDPM--QEKAVVRLSDPElRGQYFNS 181
Cdd:COG1442   82 HISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTgsQKKRAKRLGLPD-DDGYFNS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 182 GVVYLDLKKWTEAKLTEKALSILMSKDSIYKYPDQDVMNVLLKGMTIFLPREFNTIYTIKSELKDKTHQKYKELIKEDTL 261
Cdd:COG1442  161 GVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSNKKELLEARKNPV 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446298991 262 LIHYTGATKPWHKWAIYPSVKYYKIALERSPWKDDSPRDAKSIIEFKKRYKHLlvqhHYISGLI 325
Cdd:COG1442  241 IIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHL----RYLKGIK 300
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
24-325 2.45e-106

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 313.06  E-value: 2.45e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  24 TAESLNVAYGVDSNYLDGVGVSITSIVINNRHVNLDFYIIADVYNDDFFQKVEKLAEQYQLRITLYRINTDNLQCLPCTQ 103
Cdd:COG1442    2 NKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 104 VWSRAMYFRLFAFQLLGVTLNRLLYLDADVVCKGNISQLLHLEFNGAVAAVVRDVDPM--QEKAVVRLSDPElRGQYFNS 181
Cdd:COG1442   82 HISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTgsQKKRAKRLGLPD-DDGYFNS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 182 GVVYLDLKKWTEAKLTEKALSILMSKDSIYKYPDQDVMNVLLKGMTIFLPREFNTIYTIKSELKDKTHQKYKELIKEDTL 261
Cdd:COG1442  161 GVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSNKKELLEARKNPV 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446298991 262 LIHYTGATKPWHKWAIYPSVKYYKIALERSPWKDDSPRDAKSIIEFKKRYKHLlvqhHYISGLI 325
Cdd:COG1442  241 IIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHL----RYLKGIK 300
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
16-334 2.30e-88

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 268.54  E-value: 2.30e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  16 DFRLIDENTAESLNVAYGVDSNYLDGVGVSITSIVINNRHVNLDFYIIADVYNDDFFQKVEKLAEQYQLRITLYRINTDN 95
Cdd:PRK15171  14 DFNYQPHASKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQRFSALAKQYNTRINIYLINCER 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  96 LQCLPCTQVWSRAMYFRLFAFQLLGVTLNRLLYLDADVVCKGNISQLLHLEF-NGAVAAVV--RDVDPMQEKAVVrLSDP 172
Cdd:PRK15171  94 LKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFaENEIAAVVaeGDAEWWSKRAQS-LQTP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 173 ELRGQYFNSGVVYLDLKKWTEAKLTEKALSILMSKDSIYK--YPDQDVMNVLLKGMTIFLPREFNTIYTIKSELKDkthq 250
Cdd:PRK15171 173 GLASGYFNSGFLLINIPAWAQENISAKAIEMLADPEIVSRitHLDQDVLNILLAGKVKFIDAKYNTQFSLNYELKD---- 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 251 KYKELIKEDTLLIHYTGATKPWHKWAIYPSVKYYKIALERSPWKDDSPRDAKSIIEFKKRYKHLLVQHHYISGLIAGVCY 330
Cdd:PRK15171 249 SVINPVNDETVFIHYIGPTKPWHSWADYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYINGIMNYIKY 328

                 ....
gi 446298991 331 LCRK 334
Cdd:PRK15171 329 FKEK 332
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
28-274 5.48e-79

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: 241.35  E-value: 5.48e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  28 LNVAYGVDSNYLDGVGVSITSIVINNRHVNLDFYIIADVYNDDFFQKVEKLAEQYQLRITLYRINTDNLQCLPC-TQVWS 106
Cdd:cd04194    1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFPAtTDHIS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 107 RAMYFRLFAFQLLGvTLNRLLYLDADVVCKGNISQLLHLEFNGAVAAVVRDVDPMQEKAVVRLSDPELRGQYFNSGVVYL 186
Cdd:cd04194   81 YATYYRLLIPDLLP-DYDKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKKRKRRLGGYDDGSYFNSGVLLI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 187 DLKKWTEAKLTEKALSILMSKDSIYKYPDQDVMNVLLKGMTIFLPREFNTIYTIKSELKDKTHQK-YKELIKEDTLLIHY 265
Cdd:cd04194  160 NLKKWREENITEKLLELIKEYGGRLIYPDQDILNAVLKDKILYLPPRYNFQTGFYYLLKKKSKEEqELEEARKNPVIIHY 239

                 ....*....
gi 446298991 266 TGATKPWHK 274
Cdd:cd04194  240 TGSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
29-276 2.12e-65

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: 206.79  E-value: 2.12e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991   29 NVAYGVDSNYLDGVGVSITSIVINNRHVNLDFYIIADVYNDDFFQKVEKLAEQYQLRITLY-----RINTDNLQCLPCTQ 103
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLesdikIFEYFSKLKLRSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  104 VWSRAMYFRLFAFQLLgVTLNRLLYLDADVVCKGNISQLLHLEFNGAVAAVVRD---VDPMQEKAVVRLSDPELRGQYFN 180
Cdd:pfam01501  81 YWSLLNYLRLYLPDLF-PKLDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDnyfQRYPNFSEPIILENFGPPACYFN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  181 SGVVYLDLKKWTEAKLTEKALSILM--SKDSIYKYPDQDVMNVLLKGMTIFLPREFNTIYTIKSElkdktHQKYKELIKE 258
Cdd:pfam01501 160 AGMLLFDLDAWRKENITERYIKWLNlnENRTLWKLGDQDPLNIVFYGKVKPLDPRWNVLGLGYYN-----KKKSLNEITE 234
                         250
                  ....*....|....*...
gi 446298991  259 DTLLIHYTGATKPWHKWA 276
Cdd:pfam01501 235 NAAVIHYNGPTKPWLDIA 252
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
24-325 2.45e-106

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 313.06  E-value: 2.45e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  24 TAESLNVAYGVDSNYLDGVGVSITSIVINNRHVNLDFYIIADVYNDDFFQKVEKLAEQYQLRITLYRINTDNLQCLPCTQ 103
Cdd:COG1442    2 NKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 104 VWSRAMYFRLFAFQLLGVTLNRLLYLDADVVCKGNISQLLHLEFNGAVAAVVRDVDPM--QEKAVVRLSDPElRGQYFNS 181
Cdd:COG1442   82 HISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTgsQKKRAKRLGLPD-DDGYFNS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 182 GVVYLDLKKWTEAKLTEKALSILMSKDSIYKYPDQDVMNVLLKGMTIFLPREFNTIYTIKSELKDKTHQKYKELIKEDTL 261
Cdd:COG1442  161 GVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSNKKELLEARKNPV 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446298991 262 LIHYTGATKPWHKWAIYPSVKYYKIALERSPWKDDSPRDAKSIIEFKKRYKHLlvqhHYISGLI 325
Cdd:COG1442  241 IIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHL----RYLKGIK 300
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
16-334 2.30e-88

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 268.54  E-value: 2.30e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  16 DFRLIDENTAESLNVAYGVDSNYLDGVGVSITSIVINNRHVNLDFYIIADVYNDDFFQKVEKLAEQYQLRITLYRINTDN 95
Cdd:PRK15171  14 DFNYQPHASKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQRFSALAKQYNTRINIYLINCER 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  96 LQCLPCTQVWSRAMYFRLFAFQLLGVTLNRLLYLDADVVCKGNISQLLHLEF-NGAVAAVV--RDVDPMQEKAVVrLSDP 172
Cdd:PRK15171  94 LKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFaENEIAAVVaeGDAEWWSKRAQS-LQTP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 173 ELRGQYFNSGVVYLDLKKWTEAKLTEKALSILMSKDSIYK--YPDQDVMNVLLKGMTIFLPREFNTIYTIKSELKDkthq 250
Cdd:PRK15171 173 GLASGYFNSGFLLINIPAWAQENISAKAIEMLADPEIVSRitHLDQDVLNILLAGKVKFIDAKYNTQFSLNYELKD---- 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 251 KYKELIKEDTLLIHYTGATKPWHKWAIYPSVKYYKIALERSPWKDDSPRDAKSIIEFKKRYKHLLVQHHYISGLIAGVCY 330
Cdd:PRK15171 249 SVINPVNDETVFIHYIGPTKPWHSWADYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYINGIMNYIKY 328

                 ....
gi 446298991 331 LCRK 334
Cdd:PRK15171 329 FKEK 332
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
28-274 5.48e-79

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: 241.35  E-value: 5.48e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  28 LNVAYGVDSNYLDGVGVSITSIVINNRHVNLDFYIIADVYNDDFFQKVEKLAEQYQLRITLYRINTDNLQCLPC-TQVWS 106
Cdd:cd04194    1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFPAtTDHIS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 107 RAMYFRLFAFQLLGvTLNRLLYLDADVVCKGNISQLLHLEFNGAVAAVVRDVDPMQEKAVVRLSDPELRGQYFNSGVVYL 186
Cdd:cd04194   81 YATYYRLLIPDLLP-DYDKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKKRKRRLGGYDDGSYFNSGVLLI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 187 DLKKWTEAKLTEKALSILMSKDSIYKYPDQDVMNVLLKGMTIFLPREFNTIYTIKSELKDKTHQK-YKELIKEDTLLIHY 265
Cdd:cd04194  160 NLKKWREENITEKLLELIKEYGGRLIYPDQDILNAVLKDKILYLPPRYNFQTGFYYLLKKKSKEEqELEEARKNPVIIHY 239

                 ....*....
gi 446298991 266 TGATKPWHK 274
Cdd:cd04194  240 TGSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
29-276 2.12e-65

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: 206.79  E-value: 2.12e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991   29 NVAYGVDSNYLDGVGVSITSIVINNRHVNLDFYIIADVYNDDFFQKVEKLAEQYQLRITLY-----RINTDNLQCLPCTQ 103
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLesdikIFEYFSKLKLRSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  104 VWSRAMYFRLFAFQLLgVTLNRLLYLDADVVCKGNISQLLHLEFNGAVAAVVRD---VDPMQEKAVVRLSDPELRGQYFN 180
Cdd:pfam01501  81 YWSLLNYLRLYLPDLF-PKLDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDnyfQRYPNFSEPIILENFGPPACYFN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  181 SGVVYLDLKKWTEAKLTEKALSILM--SKDSIYKYPDQDVMNVLLKGMTIFLPREFNTIYTIKSElkdktHQKYKELIKE 258
Cdd:pfam01501 160 AGMLLFDLDAWRKENITERYIKWLNlnENRTLWKLGDQDPLNIVFYGKVKPLDPRWNVLGLGYYN-----KKKSLNEITE 234
                         250
                  ....*....|....*...
gi 446298991  259 DTLLIHYTGATKPWHKWA 276
Cdd:pfam01501 235 NAAVIHYNGPTKPWLDIA 252
Glyco_transf_8C pfam08437
Glycosyl transferase family 8 C-terminal; This domain is found at the C-terminus of the Pfam: ...
279-332 5.17e-19

Glycosyl transferase family 8 C-terminal; This domain is found at the C-terminus of the Pfam: PF01501 domain in bacterial glucosyltransferase and galactosyltransferase proteins.


Pssm-ID: 429997 [Multi-domain]  Cd Length: 54  Bit Score: 79.27  E-value: 5.17e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446298991  279 PSVKYYKIALERSPWKDDSPRDAKSIIEFKKRYKHLLVQHHYISGLIAGVCYLC 332
Cdd:pfam08437   1 PSAKYFLKAYEASPWKDVPLLPPRTSKEMKKKAKHLFKQGKYISGIIWYIKYLY 54
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
30-274 3.55e-16

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: 76.71  E-value: 3.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  30 VAYGVDSNYLDGVGVSITSIVINNRHvNLDFYIIADVYNDDFFQKVEKLAEQYQLRITLYRIN--TDNLQCLPCTQVWSR 107
Cdd:cd00505    4 VIVATGDEYLRGAIVLMKSVLRHRTK-PLRFHVLTNPLSDTFKAALDNLRKLYNFNYELIPVDilDSVDSEHLKRPIKIV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 108 AmYFRLFAFQLLGvTLNRLLYLDADVVCKGNISQLLHLEFNGAVAAVVRDV-DPMQEKAVVRLSDPELRGQYFNSGVVYL 186
Cdd:cd00505   83 T-LTKLHLPNLVP-DYDKILYVDADILVLTDIDELWDTPLGGQELAAAPDPgDRREGKYYRQKRSHLAGPDYFNSGVFVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 187 DLKKWTEAKLTEKALS-ILMSKDSIyKYPDQDVMNVLLKGMTI---FLPREFNTIYT-IKSELkdkthqKYKELIKEDTL 261
Cdd:cd00505  161 NLSKERRNQLLKVALEkWLQSLSSL-SGGDQDLLNTFFKQVPFivkSLPCIWNVRLTgCYRSL------NCFKAFVKNAK 233
                        250
                 ....*....|...
gi 446298991 262 LIHYTGATKPWHK 274
Cdd:cd00505  234 VIHFNGPTKPWNK 246
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
110-275 1.55e-08

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: 54.57  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 110 YFRLFAFQLlgVTLNRLLYLDADVVCKGNISQLLhlEFNGAVAAVvrdvdpmqekAVVRLSDpelrgqYFNSGVVYLDLK 189
Cdd:cd02537   79 YTKLRLWNL--TEYDKVVFLDADTLVLRNIDELF--DLPGEFAAA----------PDCGWPD------LFNSGVFVLKPS 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 190 KWTEAKLTEKalsilMSKDSIYKYPDQDVMNVLLKGMTIF--LPREFNTI----YTIKSELKDKTHQKykelikedtlLI 263
Cdd:cd02537  139 EETFNDLLDA-----LQDTPSFDGGDQGLLNSYFSDRGIWkrLPFTYNALkplrYLHPEALWFGDEIK----------VV 203
                        170
                 ....*....|..
gi 446298991 264 HYTGATKPWHKW 275
Cdd:cd02537  204 HFIGGDKPWSWW 215
GT8_like_1 cd06429
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ...
36-277 9.70e-08

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: 52.39  E-value: 9.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991  36 SNYLDGVGVSITSIVINNRHVNLDFYIIADVYNDD----FFQKVEKLAEQYQLRITLYRINTDNLQCLPCTQVWS----- 106
Cdd:cd06429    8 DNRLAAAVVINSSISNNKDPSNLVFHIVTDNQNYGamrsWFDLNPLKIATVKVLNFDDFKLLGKVKVDSLMQLESeadts 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 107 -----RAMYFRLFAFQ-----LLGVTLNRLLYLDADVVCKGNISQLLHLEFNGAVAAVVRDVdpmqekavvrlsdpelrg 176
Cdd:cd06429   88 nlkqrKPEYISLLNFArfylpELFPKLEKVIYLDDDVVVQKDLTELWNTDLGGGVAGAVETS------------------ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 177 qyFNSGVVYLDLKKWTEAKLTEkALSILMSKDSiykypdqdVMNVLLKGMtIFLPREFNTIYTIKSELKDKTHQK---YK 253
Cdd:cd06429  150 --WNPGVNVVNLTEWRRQNVTE-TYEKWMELNQ--------EEEVTLWKL-ITLPPGLIVFYGLTSPLDPSWHVRglgYN 217
                        250       260
                 ....*....|....*....|....*...
gi 446298991 254 ELIKEDTL----LIHYTGATKPWHKWAI 277
Cdd:cd06429  218 YGIRPQDIkaaaVLHFNGNMKPWLRTAI 245
PLN02718 PLN02718
Probable galacturonosyltransferase
123-272 3.83e-04

Probable galacturonosyltransferase


Pssm-ID: 178320 [Multi-domain]  Cd Length: 603  Bit Score: 42.19  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 123 LNRLLYLDADVVCKGNISQLLHLEFNGAVAAVV---RDVDP--MQEKAVVRLSDPELRGQY------FNSGVVYLDLKKW 191
Cdd:PLN02718 418 LNKIVLFDHDVVVQRDLSRLWSLDMKGKVVGAVetcLEGEPsfRSMDTFINFSDPWVAKKFdpkactWAFGMNLFDLEEW 497
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446298991 192 TEAKLTekalsilmskdSIY-KYPDQDVMNVLLKGMTifLPREFNTIYTIKSELKDKTHQ---KYKELIKEDTL----LI 263
Cdd:PLN02718 498 RRQKLT-----------SVYhKYLQLGVKRPLWKAGS--LPIGWLTFYNQTVALDKRWHVlglGHESGVGASDIeqaaVI 564

                 ....*....
gi 446298991 264 HYTGATKPW 272
Cdd:PLN02718 565 HYDGVMKPW 573
 
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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