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Conserved domains on  [gi|242041119|ref|XP_002467954|]
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galactinol synthase 2 [Sorghum bicolor]

Protein Classification

glycosyltransferase family 8 protein( domain architecture ID 10791266)

glycosyltransferase family 8 protein similar to galactinol synthase that catalyzes the first step in the biosynthesis of raffinose family oligosaccharides (RFOs) in plants

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
PLN00176 PLN00176
galactinol synthase
1-349 0e+00

galactinol synthase


:

Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 689.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119   1 MAPELAGKMTAKAAAAAAAAAVtkpatRAYVTFLAGDGDYWKGVVGLAKGLRKARSAYPLVVAVLPDVPESHRRILVSQG 80
Cdd:PLN00176   1 MAPELTVKKIAASPKALAKPAK-----RAYVTFLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILVSQG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  81 CIVREIEPVYPPENQTQFAMAYYVINYSKLRIWEFVEYERMVYLDADIQVFENVDELFELEKGYFYAVMDCFCEKTWSHT 160
Cdd:PLN00176  76 CIVREIEPVYPPENQTQFAMAYYVINYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLPDGYFYAVMDCFCEKTWSHT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 161 PQYKIGYCQQCPDKVAWPatAELGPPPALYFNAGMFVHEPSMATAKALLDTLRVTPPTPFAEQDFLNMFFRDQYRPIPNV 240
Cdd:PLN00176 156 PQYKIGYCQQCPDKVTWP--AELGPPPPLYFNAGMFVFEPSLSTYEDLLETLKITPPTPFAEQDFLNMFFRDIYKPIPPV 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 241 YNLVLAMLWRHPENVQLEKVKAVHYCAAGSKPWRFTGKEPNMDREDIKMLVKKWWDIYNDETLDFKGLLPlppadadadD 320
Cdd:PLN00176 234 YNLVLAMLWRHPENVELDKVKVVHYCAAGSKPWRYTGKEENMDREDIKMLVKKWWDIYNDESLDYKNFVP---------A 304
                        330       340
                 ....*....|....*....|....*....
gi 242041119 321 EVEAVAKKPLRAALAEAGTVKYVTAPSAA 349
Cdd:PLN00176 305 DEEEVKLQPFIAALSEAGVVSYVPAPSAA 333
 
Name Accession Description Interval E-value
PLN00176 PLN00176
galactinol synthase
1-349 0e+00

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 689.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119   1 MAPELAGKMTAKAAAAAAAAAVtkpatRAYVTFLAGDGDYWKGVVGLAKGLRKARSAYPLVVAVLPDVPESHRRILVSQG 80
Cdd:PLN00176   1 MAPELTVKKIAASPKALAKPAK-----RAYVTFLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILVSQG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  81 CIVREIEPVYPPENQTQFAMAYYVINYSKLRIWEFVEYERMVYLDADIQVFENVDELFELEKGYFYAVMDCFCEKTWSHT 160
Cdd:PLN00176  76 CIVREIEPVYPPENQTQFAMAYYVINYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLPDGYFYAVMDCFCEKTWSHT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 161 PQYKIGYCQQCPDKVAWPatAELGPPPALYFNAGMFVHEPSMATAKALLDTLRVTPPTPFAEQDFLNMFFRDQYRPIPNV 240
Cdd:PLN00176 156 PQYKIGYCQQCPDKVTWP--AELGPPPPLYFNAGMFVFEPSLSTYEDLLETLKITPPTPFAEQDFLNMFFRDIYKPIPPV 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 241 YNLVLAMLWRHPENVQLEKVKAVHYCAAGSKPWRFTGKEPNMDREDIKMLVKKWWDIYNDETLDFKGLLPlppadadadD 320
Cdd:PLN00176 234 YNLVLAMLWRHPENVELDKVKVVHYCAAGSKPWRYTGKEENMDREDIKMLVKKWWDIYNDESLDYKNFVP---------A 304
                        330       340
                 ....*....|....*....|....*....
gi 242041119 321 EVEAVAKKPLRAALAEAGTVKYVTAPSAA 349
Cdd:PLN00176 305 DEEEVKLQPFIAALSEAGVVSYVPAPSAA 333
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
28-300 2.01e-87

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: 262.97  E-value: 2.01e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  28 RAYVTFLAGDgDYWKGVVGLAKGLRKARSAYPLVVAVLPDVPESHRRILVSQGCIVREIEPVYPPENQTQFAMAYYVINY 107
Cdd:cd02537    1 EAYVTLLTND-DYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANLLKRPRFKDTY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 108 SKLRIWEFVEYERMVYLDADIQVFENVDELFELEkGYFYAVMDCFCektwshtpqykigycqqcPDkvawpataelgppp 187
Cdd:cd02537   80 TKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLP-GEFAAAPDCGW------------------PD-------------- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 188 alYFNAGMFVHEPSMATAKALLDTLRVTPPTPFAEQDFLNMFFRD--QYRPIPNVYNLVLAMLWRHPE-NVQLEKVKAVH 264
Cdd:cd02537  127 --LFNSGVFVLKPSEETFNDLLDALQDTPSFDGGDQGLLNSYFSDrgIWKRLPFTYNALKPLRYLHPEaLWFGDEIKVVH 204
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 242041119 265 YCaAGSKPWRFTGKEPNMDREDIKMLVKKWWDIYND 300
Cdd:cd02537  205 FI-GGDKPWSWWRDPETKEKDDYNELHQWWWDIYDE 239
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
31-277 1.25e-47

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: 161.34  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119   31 VTFLAGDGDYWKGVVGLAKGLRK-ARSAYPLVVAVLPDVPESHRRILVSQGCIVREIEPVYPPENQTQF---------AM 100
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKnNSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDIKIFEyfsklklrsPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  101 AYYVINYSKLRIWE-FVEYERMVYLDADIQVFENVDELFELEKG--YFYAVMDcfcektwshtpqykiGYCQQCPDKVAW 177
Cdd:pfam01501  81 YWSLLNYLRLYLPDlFPKLDKILYLDADIVVQGDLSPLWDIDLGgkVLAAVED---------------NYFQRYPNFSEP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  178 PATAELGPPPAlYFNAGMFVHEPS-------MATAKALLDTLRVTPPTPFAEQDFLNMFFRDQYRPIPNVYNLVLAM--L 248
Cdd:pfam01501 146 IILENFGPPAC-YFNAGMLLFDLDawrkeniTERYIKWLNLNENRTLWKLGDQDPLNIVFYGKVKPLDPRWNVLGLGyyN 224
                         250       260
                  ....*....|....*....|....*....
gi 242041119  249 WRHPENVQLEKVKAVHYCaAGSKPWRFTG 277
Cdd:pfam01501 225 KKKSLNEITENAAVIHYN-GPTKPWLDIA 252
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
28-314 8.87e-17

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


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 79.39  E-value: 8.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  28 RAYVTfLAGDGDYWKGVVGLAKGLRKARSAYPLVVAVLPDVPESHRRILVSQGCIVREIE--PVYPPENQ---------- 95
Cdd:COG5597   14 RAYVT-LVTNADYALGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAALGARLVRVDllPTSDAFNArhargrlhga 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  96 ------TQFAMAYYVINYSKLRIWEFVEYERMVYLDADIQVFENVDELFelekgyfyavmdcfcektwshtpqykigycq 169
Cdd:COG5597   93 apftkgRKPAFHTPLDNFCKLRLWQLVEYDRVVFIDADALVLRNIDRLF------------------------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 170 qcpdkvAWPataELGPPPALY--------FNAGMFVHEPSMATAKALLDTLRVtpPTPF---AEQDFLNMFFRDqYRPIP 238
Cdd:COG5597  142 ------DYP---EFSAAPNVYesladfhrLNSGVFTARPSQATFEAMLARLDA--PGAFwrrTDQTFLQTFFPD-WHGLP 209
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242041119 239 NVYNLVLAMLWRHPENVQLEKVKAVHYcaAGSKPWRftGKEPNMDRedIKMLVKKWWDIYNDETLDFKGLLPLPPA 314
Cdd:COG5597  210 VFMNMLQYVWFNLPELWDWPSIRVLHY--QYEKPWQ--KDHAKADR--LRPLIDLWHAYAGGGPIPDLASLPNPTG 279
 
Name Accession Description Interval E-value
PLN00176 PLN00176
galactinol synthase
1-349 0e+00

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 689.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119   1 MAPELAGKMTAKAAAAAAAAAVtkpatRAYVTFLAGDGDYWKGVVGLAKGLRKARSAYPLVVAVLPDVPESHRRILVSQG 80
Cdd:PLN00176   1 MAPELTVKKIAASPKALAKPAK-----RAYVTFLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILVSQG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  81 CIVREIEPVYPPENQTQFAMAYYVINYSKLRIWEFVEYERMVYLDADIQVFENVDELFELEKGYFYAVMDCFCEKTWSHT 160
Cdd:PLN00176  76 CIVREIEPVYPPENQTQFAMAYYVINYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLPDGYFYAVMDCFCEKTWSHT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 161 PQYKIGYCQQCPDKVAWPatAELGPPPALYFNAGMFVHEPSMATAKALLDTLRVTPPTPFAEQDFLNMFFRDQYRPIPNV 240
Cdd:PLN00176 156 PQYKIGYCQQCPDKVTWP--AELGPPPPLYFNAGMFVFEPSLSTYEDLLETLKITPPTPFAEQDFLNMFFRDIYKPIPPV 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 241 YNLVLAMLWRHPENVQLEKVKAVHYCAAGSKPWRFTGKEPNMDREDIKMLVKKWWDIYNDETLDFKGLLPlppadadadD 320
Cdd:PLN00176 234 YNLVLAMLWRHPENVELDKVKVVHYCAAGSKPWRYTGKEENMDREDIKMLVKKWWDIYNDESLDYKNFVP---------A 304
                        330       340
                 ....*....|....*....|....*....
gi 242041119 321 EVEAVAKKPLRAALAEAGTVKYVTAPSAA 349
Cdd:PLN00176 305 DEEEVKLQPFIAALSEAGVVSYVPAPSAA 333
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
28-300 2.01e-87

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: 262.97  E-value: 2.01e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  28 RAYVTFLAGDgDYWKGVVGLAKGLRKARSAYPLVVAVLPDVPESHRRILVSQGCIVREIEPVYPPENQTQFAMAYYVINY 107
Cdd:cd02537    1 EAYVTLLTND-DYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANLLKRPRFKDTY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 108 SKLRIWEFVEYERMVYLDADIQVFENVDELFELEkGYFYAVMDCFCektwshtpqykigycqqcPDkvawpataelgppp 187
Cdd:cd02537   80 TKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLP-GEFAAAPDCGW------------------PD-------------- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 188 alYFNAGMFVHEPSMATAKALLDTLRVTPPTPFAEQDFLNMFFRD--QYRPIPNVYNLVLAMLWRHPE-NVQLEKVKAVH 264
Cdd:cd02537  127 --LFNSGVFVLKPSEETFNDLLDALQDTPSFDGGDQGLLNSYFSDrgIWKRLPFTYNALKPLRYLHPEaLWFGDEIKVVH 204
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 242041119 265 YCaAGSKPWRFTGKEPNMDREDIKMLVKKWWDIYND 300
Cdd:cd02537  205 FI-GGDKPWSWWRDPETKEKDDYNELHQWWWDIYDE 239
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
31-277 1.25e-47

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: 161.34  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119   31 VTFLAGDGDYWKGVVGLAKGLRK-ARSAYPLVVAVLPDVPESHRRILVSQGCIVREIEPVYPPENQTQF---------AM 100
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKnNSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDIKIFEyfsklklrsPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  101 AYYVINYSKLRIWE-FVEYERMVYLDADIQVFENVDELFELEKG--YFYAVMDcfcektwshtpqykiGYCQQCPDKVAW 177
Cdd:pfam01501  81 YWSLLNYLRLYLPDlFPKLDKILYLDADIVVQGDLSPLWDIDLGgkVLAAVED---------------NYFQRYPNFSEP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  178 PATAELGPPPAlYFNAGMFVHEPS-------MATAKALLDTLRVTPPTPFAEQDFLNMFFRDQYRPIPNVYNLVLAM--L 248
Cdd:pfam01501 146 IILENFGPPAC-YFNAGMLLFDLDawrkeniTERYIKWLNLNENRTLWKLGDQDPLNIVFYGKVKPLDPRWNVLGLGyyN 224
                         250       260
                  ....*....|....*....|....*....
gi 242041119  249 WRHPENVQLEKVKAVHYCaAGSKPWRFTG 277
Cdd:pfam01501 225 KKKSLNEITENAAVIHYN-GPTKPWLDIA 252
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
28-314 8.87e-17

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


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 79.39  E-value: 8.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  28 RAYVTfLAGDGDYWKGVVGLAKGLRKARSAYPLVVAVLPDVPESHRRILVSQGCIVREIE--PVYPPENQ---------- 95
Cdd:COG5597   14 RAYVT-LVTNADYALGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAALGARLVRVDllPTSDAFNArhargrlhga 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  96 ------TQFAMAYYVINYSKLRIWEFVEYERMVYLDADIQVFENVDELFelekgyfyavmdcfcektwshtpqykigycq 169
Cdd:COG5597   93 apftkgRKPAFHTPLDNFCKLRLWQLVEYDRVVFIDADALVLRNIDRLF------------------------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 170 qcpdkvAWPataELGPPPALY--------FNAGMFVHEPSMATAKALLDTLRVtpPTPF---AEQDFLNMFFRDqYRPIP 238
Cdd:COG5597  142 ------DYP---EFSAAPNVYesladfhrLNSGVFTARPSQATFEAMLARLDA--PGAFwrrTDQTFLQTFFPD-WHGLP 209
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242041119 239 NVYNLVLAMLWRHPENVQLEKVKAVHYcaAGSKPWRftGKEPNMDRedIKMLVKKWWDIYNDETLDFKGLLPLPPA 314
Cdd:COG5597  210 VFMNMLQYVWFNLPELWDWPSIRVLHY--QYEKPWQ--KDHAKADR--LRPLIDLWHAYAGGGPIPDLASLPNPTG 279
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
107-299 7.80e-16

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 76.94  E-value: 7.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 107 YSKLRIWEFV--EYERMVYLDADIQVFENVDELFE--LEKGYFYAVMDCFCEKTWSHTPQYkigycqqcpdkvawpatae 182
Cdd:COG1442   88 YYRLLIPELLpdDYDKVLYLDADTLVLGDLSELWDidLGGNLLAAVRDGTVTGSQKKRAKR------------------- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 183 LG-PPPALYFNAG-MFVHEPSM---ATAKALLDTLRVTPPT-PFAEQDFLNMFFRDQYRPIPNVYNLVLAMLWRHPENVQ 256
Cdd:COG1442  149 LGlPDDDGYFNSGvLLINLKKWreeNITEKALEFLKENPDKlKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSN 228
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 242041119 257 LEKVKA-------VHYCAAgSKPWRFTGKEPnmdredikmLVKKWWDIYN 299
Cdd:COG1442  229 KKELLEarknpviIHYTGP-TKPWHKWCTHP---------YADLYWEYLK 268
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
117-275 4.18e-15

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: 73.79  E-value: 4.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 117 EYERMVYLDADIQVFENVDELFELEKG--YFYAVMDCFCEKTWSHTPQYKigycqqcpdkvawpataelGPPPALYFNAG 194
Cdd:cd04194   95 DYDKVLYLDADIIVLGDLSELFDIDLGdnLLAAVRDPFIEQEKKRKRRLG-------------------GYDDGSYFNSG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 195 -MFVHEPSMATAK---ALLDTLRVTPPTPFA-EQDFLNMFFRDQYRPIPNVYNLVLAMLWRHPEN----VQLEKVKA--- 262
Cdd:cd04194  156 vLLINLKKWREENiteKLLELIKEYGGRLIYpDQDILNAVLKDKILYLPPRYNFQTGFYYLLKKKskeeQELEEARKnpv 235
                        170
                 ....*....|....
gi 242041119 263 -VHYCAAGsKPWRF 275
Cdd:cd04194  236 iIHYTGSD-KPWNK 248
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
31-273 1.80e-09

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: 57.45  E-value: 1.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  31 VTFLAGDGDYWKGVVGLAKGLRKARSAyPLVVAVLPDvPESHRR------ILVSQGCIVREIEPVYPPENQTQFAMAYYV 104
Cdd:cd00505    3 IVIVATGDEYLRGAIVLMKSVLRHRTK-PLRFHVLTN-PLSDTFkaaldnLRKLYNFNYELIPVDILDSVDSEHLKRPIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 105 I-NYSKLRIWEFV-EYERMVYLDADIQVFENVDELFELEKGYFYAVMDCFCEkTWSHTPQYKigycqqcpDKVAWPATAE 182
Cdd:cd00505   81 IvTLTKLHLPNLVpDYDKILYVDADILVLTDIDELWDTPLGGQELAAAPDPG-DRREGKYYR--------QKRSHLAGPD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119 183 lgpppalYFNAGMFVHEPSMATAKALL-DTLR----VTPPTPFAEQDFLNMFFRDQYRPI---PNVYNLVLamLW----- 249
Cdd:cd00505  152 -------YFNSGVFVVNLSKERRNQLLkVALEkwlqSLSSLSGGDQDLLNTFFKQVPFIVkslPCIWNVRL--TGcyrsl 222
                        250       260
                 ....*....|....*....|....
gi 242041119 250 RHPENVqLEKVKAVHYCaAGSKPW 273
Cdd:cd00505  223 NCFKAF-VKNAKVIHFN-GPTKPW 244
GT8_GNT1 cd06914
GNT1 is a fungal enzyme that belongs to the GT 8 family; N-acetylglucosaminyltransferase is a ...
29-140 1.47e-07

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: 52.04  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242041119  29 AYVTFlAGDGDYWKGVVGLAKGLRKARSAYPLVVAVLPDVPE-----SHRRIL--VSQGCIVREIEPVYPPENQTQFAMA 101
Cdd:cd06914    2 AYVNY-ATNADYLCNALILFEQLRRLGSKAKLVLLVPETLLDrnlddFVRRDLllARDKVIVKLIPVIIASGGDAYWAKS 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 242041119 102 YyvinySKLRIWEFVEYERMVYLDADIQVFENVDELFEL 140
Cdd:cd06914   81 L-----TKLRAFNQTEYDRIIYFDSDSIIRHPMDELFFL 114
 
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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