NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|665402465|ref|NP_001286667|]
View 

glycogenin, isoform G [Drosophila melanogaster]

Protein Classification

glycosyltransferase family 8 protein( domain architecture ID 10118608)

glycosyltransferase family 8 protein similar to vertebrate glycogenin, which catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached to internal tyrosine residues

CATH:  3.90.550.10
Gene Ontology:  GO:0016757|GO:0005978
PubMed:  10508766|12691742

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
4-253 8.28e-116

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: 335.39  E-value: 8.28e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465   4 FAWVTLTTNDTYSLGALVLAHSLKRAKTAHQLAVLVTPNVSQAMRDRLKEVYNVVQEVNVLDSQDAANLalLSRPELGVT 83
Cdd:cd02537    1 EAYVTLLTNDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANL--LKRPRFKDT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465  84 FTKLHCWRLVQFEKCVFLDADTLVLQNCDELFERE-ELSAAPDVSWPDCFNSGVFVFKPSVDTFAQITEFAVKNGSFDGG 162
Cdd:cd02537   79 YTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLPgEFAAAPDCGWPDLFNSGVFVLKPSEETFNDLLDALQDTPSFDGG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465 163 DQGLLNQFFADWStadIKKHLPFVYNVTAYASYCYLPAfKQFRDKIKILHFAGKLKPWLIQFNSETKvasvssEYAHAQD 242
Cdd:cd02537  159 DQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETK------EKDDYNE 228
                        250
                 ....*....|.
gi 665402465 243 LIQLWWNIFCE 253
Cdd:cd02537  229 LHQWWWDIYDE 239
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
4-253 8.28e-116

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: 335.39  E-value: 8.28e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465   4 FAWVTLTTNDTYSLGALVLAHSLKRAKTAHQLAVLVTPNVSQAMRDRLKEVYNVVQEVNVLDSQDAANLalLSRPELGVT 83
Cdd:cd02537    1 EAYVTLLTNDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANL--LKRPRFKDT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465  84 FTKLHCWRLVQFEKCVFLDADTLVLQNCDELFERE-ELSAAPDVSWPDCFNSGVFVFKPSVDTFAQITEFAVKNGSFDGG 162
Cdd:cd02537   79 YTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLPgEFAAAPDCGWPDLFNSGVFVLKPSEETFNDLLDALQDTPSFDGG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465 163 DQGLLNQFFADWStadIKKHLPFVYNVTAYASYCYLPAfKQFRDKIKILHFAGKLKPWLIQFNSETKvasvssEYAHAQD 242
Cdd:cd02537  159 DQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETK------EKDDYNE 228
                        250
                 ....*....|.
gi 665402465 243 LIQLWWNIFCE 253
Cdd:cd02537  229 LHQWWWDIYDE 239
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
2-248 9.30e-41

N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 144.49  E-value: 9.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465   2 SKFAWVTLTTNDTYSLGALVLAHSLKRAKTAHQLAVLVTPNVSQAMRDRLKEVYNVVQEVNVLDSQDAANlALLSRPELG 81
Cdd:COG5597   12 SRRAYVTLVTNADYALGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAALGARLVRVDLLPTSDAFN-ARHARGRLH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465  82 VT-----------------FTKLHCWRLVQFEKCVFLDADTLVLQNCDELFEREELSAAPDV--SWPDC--FNSGVFVFK 140
Cdd:COG5597   91 GAapftkgrkpafhtpldnFCKLRLWQLVEYDRVVFIDADALVLRNIDRLFDYPEFSAAPNVyeSLADFhrLNSGVFTAR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465 141 PSVDTFAQITEFAVKNGSF-DGGDQGLLNQFFADWstadikkH-LPFVYNVTAYAsYCYLPAFKQFRDkIKILHFAGKlK 218
Cdd:COG5597  171 PSQATFEAMLARLDAPGAFwRRTDQTFLQTFFPDW-------HgLPVFMNMLQYV-WFNLPELWDWPS-IRVLHYQYE-K 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 665402465 219 PWliqfnsetkvasvssEYAHA-----QDLIQLWW 248
Cdd:COG5597  241 PW---------------QKDHAkadrlRPLIDLWH 260
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
7-221 5.57e-22

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: 93.54  E-value: 5.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465    7 VTLTTNDTYSLGALVLAHS-LKRAKTAHQLAVLVTPNVSQAMRDR---LKEVYNVVQEVNVLDSQD----AANLALLSRP 78
Cdd:pfam01501   2 IALALDKNYLLGASVSIKSlLKNNSDFALNFHIFTDDIPVENLDIlnwLASSYKPVLPLLESDIKIfeyfSKLKLRSPKY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465   79 ELGVTFTKLHCWRL-VQFEKCVFLDADTLVLQNCDELFE----------------------REELSAAPDVSWPDCFNSG 135
Cdd:pfam01501  82 WSLLNYLRLYLPDLfPKLDKILYLDADIVVQGDLSPLWDidlggkvlaavednyfqrypnfSEPIILENFGPPACYFNAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465  136 VFVFKPSVDTFAQITEFAVKNGSFDG-------GDQGLLNQFFAD-WstadikKHLPFVYNVTAYASYCYLPAFKQFRDK 207
Cdd:pfam01501 162 MLLFDLDAWRKENITERYIKWLNLNEnrtlwklGDQDPLNIVFYGkV------KPLDPRWNVLGLGYYNKKKSLNEITEN 235
                         250
                  ....*....|....
gi 665402465  208 IKILHFAGKLKPWL 221
Cdd:pfam01501 236 AAVIHYNGPTKPWL 249
PLN00176 PLN00176
galactinol synthase
2-251 3.63e-20

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 89.75  E-value: 3.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465   2 SKFAWVT-LTTNDTYSLGALVLAHSLKRAKTAHQLAVLVTPNVSQAMRDRLKEVYNVVQE---VNVLDSQDAanlalLSR 77
Cdd:PLN00176  21 AKRAYVTfLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILVSQGCIVREiepVYPPENQTQ-----FAM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465  78 PELGVTFTKLHCWRLVQFEKCVFLDADTLVLQNCDELFEREE--LSAAPD------------------------VSWPD- 130
Cdd:PLN00176  96 AYYVINYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLPDgyFYAVMDcfcektwshtpqykigycqqcpdkVTWPAe 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465 131 -------CFNSGVFVFKPSVDTFAQITEFAVKNGSFDGGDQGLLNQFFadwstADIKKHLPFVYNvtayasycyLPAFKQ 203
Cdd:PLN00176 176 lgpppplYFNAGMFVFEPSLSTYEDLLETLKITPPTPFAEQDFLNMFF-----RDIYKPIPPVYN---------LVLAML 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 665402465 204 FR-------DKIKILHF-AGKLKPWliQFNSetKVASVSSEyaHAQDLIQLWWNIF 251
Cdd:PLN00176 242 WRhpenvelDKVKVVHYcAAGSKPW--RYTG--KEENMDRE--DIKMLVKKWWDIY 291
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
4-253 8.28e-116

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: 335.39  E-value: 8.28e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465   4 FAWVTLTTNDTYSLGALVLAHSLKRAKTAHQLAVLVTPNVSQAMRDRLKEVYNVVQEVNVLDSQDAANLalLSRPELGVT 83
Cdd:cd02537    1 EAYVTLLTNDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANL--LKRPRFKDT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465  84 FTKLHCWRLVQFEKCVFLDADTLVLQNCDELFERE-ELSAAPDVSWPDCFNSGVFVFKPSVDTFAQITEFAVKNGSFDGG 162
Cdd:cd02537   79 YTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLPgEFAAAPDCGWPDLFNSGVFVLKPSEETFNDLLDALQDTPSFDGG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465 163 DQGLLNQFFADWStadIKKHLPFVYNVTAYASYCYLPAfKQFRDKIKILHFAGKLKPWLIQFNSETKvasvssEYAHAQD 242
Cdd:cd02537  159 DQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETK------EKDDYNE 228
                        250
                 ....*....|.
gi 665402465 243 LIQLWWNIFCE 253
Cdd:cd02537  229 LHQWWWDIYDE 239
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
5-220 2.14e-43

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: 150.28  E-value: 2.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465   5 AWVTLTTNDTYSLGALVLAHSLKRAKTAHQLAVLVTPNVSQAMRDRLK---EVYNVVQEVNVLDSQDAANLALLSRPELG 81
Cdd:cd00505    2 AIVIVATGDEYLRGAIVLMKSVLRHRTKPLRFHVLTNPLSDTFKAALDnlrKLYNFNYELIPVDILDSVDSEHLKRPIKI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465  82 VTFTKLHCWRLVQ-FEKCVFLDADTLVLQNCDELFER----EELSAAPDVSWP----------------DCFNSGVFVFK 140
Cdd:cd00505   82 VTLTKLHLPNLVPdYDKILYVDADILVLTDIDELWDTplggQELAAAPDPGDRregkyyrqkrshlagpDYFNSGVFVVN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465 141 PSVDTFAQITEFAVKNGSF-----DGGDQGLLNQFFADWstADIKKHLPFVYNVTAYASYCYLPAFKQFRDKIKILHFAG 215
Cdd:cd00505  162 LSKERRNQLLKVALEKWLQslsslSGGDQDLLNTFFKQV--PFIVKSLPCIWNVRLTGCYRSLNCFKAFVKNAKVIHFNG 239

                 ....*
gi 665402465 216 KLKPW 220
Cdd:cd00505  240 PTKPW 244
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
2-248 9.30e-41

N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 144.49  E-value: 9.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465   2 SKFAWVTLTTNDTYSLGALVLAHSLKRAKTAHQLAVLVTPNVSQAMRDRLKEVYNVVQEVNVLDSQDAANlALLSRPELG 81
Cdd:COG5597   12 SRRAYVTLVTNADYALGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAALGARLVRVDLLPTSDAFN-ARHARGRLH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465  82 VT-----------------FTKLHCWRLVQFEKCVFLDADTLVLQNCDELFEREELSAAPDV--SWPDC--FNSGVFVFK 140
Cdd:COG5597   91 GAapftkgrkpafhtpldnFCKLRLWQLVEYDRVVFIDADALVLRNIDRLFDYPEFSAAPNVyeSLADFhrLNSGVFTAR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465 141 PSVDTFAQITEFAVKNGSF-DGGDQGLLNQFFADWstadikkH-LPFVYNVTAYAsYCYLPAFKQFRDkIKILHFAGKlK 218
Cdd:COG5597  171 PSQATFEAMLARLDAPGAFwRRTDQTFLQTFFPDW-------HgLPVFMNMLQYV-WFNLPELWDWPS-IRVLHYQYE-K 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 665402465 219 PWliqfnsetkvasvssEYAHA-----QDLIQLWW 248
Cdd:COG5597  241 PW---------------QKDHAkadrlRPLIDLWH 260
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
7-221 5.57e-22

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: 93.54  E-value: 5.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465    7 VTLTTNDTYSLGALVLAHS-LKRAKTAHQLAVLVTPNVSQAMRDR---LKEVYNVVQEVNVLDSQD----AANLALLSRP 78
Cdd:pfam01501   2 IALALDKNYLLGASVSIKSlLKNNSDFALNFHIFTDDIPVENLDIlnwLASSYKPVLPLLESDIKIfeyfSKLKLRSPKY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465   79 ELGVTFTKLHCWRL-VQFEKCVFLDADTLVLQNCDELFE----------------------REELSAAPDVSWPDCFNSG 135
Cdd:pfam01501  82 WSLLNYLRLYLPDLfPKLDKILYLDADIVVQGDLSPLWDidlggkvlaavednyfqrypnfSEPIILENFGPPACYFNAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465  136 VFVFKPSVDTFAQITEFAVKNGSFDG-------GDQGLLNQFFAD-WstadikKHLPFVYNVTAYASYCYLPAFKQFRDK 207
Cdd:pfam01501 162 MLLFDLDAWRKENITERYIKWLNLNEnrtlwklGDQDPLNIVFYGkV------KPLDPRWNVLGLGYYNKKKSLNEITEN 235
                         250
                  ....*....|....
gi 665402465  208 IKILHFAGKLKPWL 221
Cdd:pfam01501 236 AAVIHYNGPTKPWL 249
PLN00176 PLN00176
galactinol synthase
2-251 3.63e-20

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 89.75  E-value: 3.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465   2 SKFAWVT-LTTNDTYSLGALVLAHSLKRAKTAHQLAVLVTPNVSQAMRDRLKEVYNVVQE---VNVLDSQDAanlalLSR 77
Cdd:PLN00176  21 AKRAYVTfLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILVSQGCIVREiepVYPPENQTQ-----FAM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465  78 PELGVTFTKLHCWRLVQFEKCVFLDADTLVLQNCDELFEREE--LSAAPD------------------------VSWPD- 130
Cdd:PLN00176  96 AYYVINYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLPDgyFYAVMDcfcektwshtpqykigycqqcpdkVTWPAe 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465 131 -------CFNSGVFVFKPSVDTFAQITEFAVKNGSFDGGDQGLLNQFFadwstADIKKHLPFVYNvtayasycyLPAFKQ 203
Cdd:PLN00176 176 lgpppplYFNAGMFVFEPSLSTYEDLLETLKITPPTPFAEQDFLNMFF-----RDIYKPIPPVYN---------LVLAML 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 665402465 204 FR-------DKIKILHF-AGKLKPWliQFNSetKVASVSSEyaHAQDLIQLWWNIF 251
Cdd:PLN00176 242 WRhpenvelDKVKVVHYcAAGSKPW--RYTG--KEENMDRE--DIKMLVKKWWDIY 291
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
7-220 3.38e-19

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 86.57  E-value: 3.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465   7 VTLTTNDTYSLGALVLAHSLKRAKTAHQLAV-LVTPNVSQAMRDRLKEV---YNVVQEVNVLDSQDAANLALLSR--PEl 80
Cdd:COG1442    8 IVFAIDDNYLPGLGVSIASLLENNPDRPYDFhILTDGLSDENKERLEALaakYNVSIEFIDVDDELLKDLPVSKHisKA- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465  81 gvTFTKLHCWRLV--QFEKCVFLDADTLVLQNCDELFERE----ELSAAPDVSWP----------------DCFNSGVFV 138
Cdd:COG1442   87 --TYYRLLIPELLpdDYDKVLYLDADTLVLGDLSELWDIDlggnLLAAVRDGTVTgsqkkrakrlglpdddGYFNSGVLL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465 139 FKPSV----DTFAQITEFAVKNGS-FDGGDQGLLNQFFADWstadiKKHLPFVYNVTAYASYCYLPAFKQF-----RDKI 208
Cdd:COG1442  165 INLKKwreeNITEKALEFLKENPDkLKYPDQDILNIVLGGK-----VKFLPPRYNYQYSLYYELKDKSNKKelleaRKNP 239
                        250
                 ....*....|..
gi 665402465 209 KILHFAGKLKPW 220
Cdd:COG1442  240 VIIHYTGPTKPW 251
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
9-220 1.02e-14

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: 73.02  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465   9 LTTNDTYSLGALVLAHSLKRAKTAHQLAVLV-TPNVSQAMRDRLKEV---YNVVQE-VNVLDSQDAANLALLSRpelgvt 83
Cdd:cd04194    5 FAIDDNYAPYLAVTIKSILANNSKRDYDFYIlNDDISEENKKKLKELlkkYNSSIEfIKIDNDDFKFFPATTDH------ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465  84 FTKLHCWRLV------QFEKCVFLDADTLVLQNCDELFERE----ELSAAPDVSWPDC---------------FNSGVFV 138
Cdd:cd04194   79 ISYATYYRLLipdllpDYDKVLYLDADIIVLGDLSELFDIDlgdnLLAAVRDPFIEQEkkrkrrlggyddgsyFNSGVLL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465 139 F-------KpsvDTFAQITEFAVKNGSFDG-GDQGLLNQFFADwstaDIKkHLPFVYNVTAYASYCYLPAFKQF------ 204
Cdd:cd04194  159 InlkkwreE---NITEKLLELIKEYGGRLIyPDQDILNAVLKD----KIL-YLPPRYNFQTGFYYLLKKKSKEEqeleea 230
                        250
                 ....*....|....*.
gi 665402465 205 RDKIKILHFAGKLKPW 220
Cdd:cd04194  231 RKNPVIIHYTGSDKPW 246
GT8_GNT1 cd06914
GNT1 is a fungal enzyme that belongs to the GT 8 family; N-acetylglucosaminyltransferase is a ...
4-253 6.19e-14

GNT1 is a fungal enzyme that belongs to the GT 8 family; N-acetylglucosaminyltransferase is a fungal enzyme that catalyzes the addition of N-acetyl-D-glucosamine to mannotetraose side chains by an alpha 1-2 linkage during the synthesis of mannan. The N-acetyl-D-glucosamine moiety in mannan plays a role in the attachment of mannan to asparagine residues in proteins. The mannotetraose and its N-acetyl-D-glucosamine derivative side chains of mannan are the principle immunochemical determinants on the cell surface. N-acetylglucosaminyltransferase is a member of glycosyltransferase family 8, which are, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed, retaining glycosyltransferases.


Pssm-ID: 133064  Cd Length: 278  Bit Score: 71.30  E-value: 6.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465   4 FAWVTLTTNDTYSLGALVLAHSLKRAKTAHQLAVLVTP------NVSQAMRDRLKEVYNVV--QEVNVLDSQDAANLAll 75
Cdd:cd06914    1 YAYVNYATNADYLCNALILFEQLRRLGSKAKLVLLVPEtlldrnLDDFVRRDLLLARDKVIvkLIPVIIASGGDAYWA-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465  76 srpelgVTFTKLHCWRLVQFEKCVFLDADTLVLQNCDELFE-REELS-AAPDVSWPdcFNSGVFVFKPSVDTFAQITEFA 153
Cdd:cd06914   79 ------KSLTKLRAFNQTEYDRIIYFDSDSIIRHPMDELFFlPNYIKfAAPRAYWK--FASHLMVIKPSKEAFKELMTEI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402465 154 VKNGSFDGG--DQGLLNQFFadwstADIKKHLPFVYNVTAYASYCYLPafKQFRDK------------------------ 207
Cdd:cd06914  151 LPAYLNKKNeyDMDLINEEF-----YNSKQLFKPSVLVLPHRQYGLLT--GEFREKlhksflsnaqhlyekwdpddvfke 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665402465 208 IKILHF-AGKL-KPWLIQFNSET------KVASVSSEYAHAQDLIQLWWNIFCE 253
Cdd:cd06914  224 SKVIHFsDSPLpKPWNYNNLEDIyciekiYCKMVKPRLEDDCRACDLWNSLYAD 277
 
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