|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
7-375 |
5.97e-66 |
|
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
Pssm-ID: 340831 [Multi-domain] Cd Length: 366 Bit Score: 213.55 E-value: 5.97e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 7 KICMLGHkRIPSREGGIEIVVEELATRMVALGHEVT--CYNRSGHHVSGKEFDQHKNKEYKGVKLKTIFTLnIKGIaams 84
Cdd:cd03801 1 KILLLSP-ELPPPVGGAERHVRELARALAARGHDVTvlTPADPGEPPEELEDGVIVPLLPSLAALLRARRL-LREL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 85 ssvfgGIRAAFGKYDIVHFHA-EGPCAMLWLPKLFGKRCVATIHGLDHQREKWNKLASTYIMLGEKCAVKFADEIIVLSE 163
Cdd:cd03801 75 -----RPLLRLRKFDVVHAHGlLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLARAEALLRRADAVIAVSE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 164 SVQNYFEDIYG---RKTRFIPNGVKkIEIKSAGLITEKYGLTKDSYILFLGRLVPEKGIRYLIEAFKDVQTDK---KLII 237
Cdd:cd03801 150 ALRDELRALGGippEKIVVIPNGVD-LERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGpdvRLVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 238 AGGSsdtDEFANELKELAKG-DERIIFTGFVQGQELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNISECTEV 316
Cdd:cd03801 229 VGGD---GPLRAELEELELGlGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEV 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752923616 317 VEDK--AMIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEFICSKYNWDKIVQETLNLYR 375
Cdd:cd03801 306 VEDGegGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
7-372 |
1.46e-38 |
|
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 141.35 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 7 KICMLGhKRIPSREGGIEIVVEELATRMVALGHEVTCYNRSGHhvsgKEFDQHKNKEYKGVKLKTIFtlnIKGIAAMSSS 86
Cdd:cd03809 1 KILIDG-RSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPL----PGELLRLLREYPELSLGVIK---IKLWRELALL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 87 VFGGIR-AAFGKYDIVH-FHAEGPcamlwlPKLFGKRCVATIHGLDHQREK----WNKLASTYIMLgeKCAVKFADEIIV 160
Cdd:cd03809 73 RWLQILlPKKDKPDLLHsPHNTAP------LLLKGCPQVVTIHDLIPLRYPeffpKRFRLYYRLLL--PISLRRADAIIT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 161 LSESVQNYFEDIYG---RKTRFIPNGVKKI--EIKSAGLITEKYGLTKDsYILFLGRLVPEKGIRYLIEAF---KDVQTD 232
Cdd:cd03809 145 VSEATRDDIIKFYGvppEKIVVIPLGVDPSffPPESAAVLIAKYLLPEP-YFLYVGTLEPRKNHERLLKAFallKKQGGD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 233 KKLIIAGGSSDTDEFANELKELAKGDERIIFTGFVQGQELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNISE 312
Cdd:cd03809 224 LKLVIVGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISV 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752923616 313 CTEVVEDKAMIFKKSDVSDLKIRLEEACNQSEmvkvLKNQATE---FICSKYNWDKIVQETLN 372
Cdd:cd03809 304 LPEVAGDAALYFDPLDPESIADAILRLLEDPS----LREELIRkglERAKKFSWEKTAEKTLE 362
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
21-369 |
1.77e-37 |
|
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.
Pssm-ID: 340847 [Multi-domain] Cd Length: 351 Bit Score: 138.14 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 21 GGIEIVVEELATRMVALGHEVTCYnrsghhvsgkEFDQHKNKEY----KGVKLKTIFTLNIKGIAAMSS--SVFGGIRAA 94
Cdd:cd03820 13 GGAERVAINLANHLAKKGYDVTII----------SLDSAEKPPFyeldDNIKIKNLGDRKYSHFKLLLKyfKKVRRLRKY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 95 F--GKYDIV-HFHaegPCAMLWLPKLF-GKRCVATIHgldHQREKWNKLASTYimLGEKCAVKFADEIIVLSESVQNYFE 170
Cdd:cd03820 83 LknNKPDVViSFR---TSLLTFLALIGlKSKLIVWEH---NNYEAYNKGLRRL--LLRRLLYKRADKIVVLTEADKLKKY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 171 DIYGRKTRFIPNGVKKIEIKSAGLITEKYgltkdsyILFLGRLVPEKGIRYLIEAFKDVQTDK---KLIIAGGSSDTDEF 247
Cdd:cd03820 155 KQPNSNVVVIPNPLSFPSEEPSTNLKSKR-------ILAVGRLTYQKGFDLLIEAWALIAKKHpdwKLRIYGDGPEREEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 248 ANELKELAKGDeRIIFTGFVQgqELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNIseCT---EVVEDK--AM 322
Cdd:cd03820 228 EKLIDKLGLED-RVKLLGPTK--NIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDC--PTgpsEIIEDGenGL 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1752923616 323 IFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEFIcSKYNWDKIVQE 369
Cdd:cd03820 303 LVPNGDVDALAEALLRLMEDEELRKKMGKNARKNA-ERFSIEKIIKQ 348
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
7-371 |
2.74e-37 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
Pssm-ID: 340837 [Multi-domain] Cd Length: 358 Bit Score: 137.73 E-value: 2.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 7 KICMLGHkripsREGGIEIVVEELATRMVALGHEVTCynrsghhVSGKEFDQHKNKEYKGVKLKTIFTLNiKGIaamssS 86
Cdd:cd03808 1 KILFIVN-----VDGGFQSFRLPLIKALVKKGYEVHV-------IAPDGDKLSDELKELGVKVIDIPILR-RGI-----N 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 87 VFGGIRAAF--------GKYDIVHFHAEGPC--AMLWLPKLFGKRCVATIHGLDHQREKWNKLASTYIMLgEKCAVKFAD 156
Cdd:cd03808 63 PLKDLKALFklykllkkEKPDIVHCHTPKPGilGRLAARLAGVPKVIYTVHGLGFVFTEGKLLRLLYLLL-EKLALLFTD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 157 EIIVLSESVQNYFediygrKTRFIPNGVKKIEIKSAGLITEKYGLTKDSY------ILFLGRLVPEKGIRYLIEAF---K 227
Cdd:cd03808 142 KVIFVNEDDRDLA------IKKGIIKKKKTVLIPGSGVDLDRFQYSPESLpsekvvFLFVARLLKDKGIDELIEAAkilK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 228 DVQTDKKLIIAGGSSDTDEFANELKELAKgDERIIFTGFVQgqELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIV 307
Cdd:cd03808 216 KKGPNVRFLLVGDGELENPSEILIEKLGL-EGRIEFLGFRS--DVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVIT 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752923616 308 SNISECTEVVEDK--AMIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEFICSKYNWDKIVQETL 371
Cdd:cd03808 293 TDVPGCRELVIDGvnGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
|
|
| GT4-like |
cd04955 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
7-369 |
6.18e-33 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in certain bacteria and Archaea.
Pssm-ID: 340858 [Multi-domain] Cd Length: 379 Bit Score: 126.46 E-value: 6.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 7 KICMLGHKRIPSREGGIEIVVEELATRMVA--LGHEVTCynrSGHHVSGKEFdqhknkEYKGVKLKTIFTLNIKGIAAMS 84
Cdd:cd04955 1 HIFIIGSRGLPAKYGGFETFVEKLTERQQSdnIKYHVAC---LSENSKQQHF------EYNGADCFYVKVPKIGPARAIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 85 SSVFGGIRA---------AFGKYDIVHFHAeGPCAMLWLP---KLFGKRCVATiHGLDHQREKWNKLASTYIMLGEKCAV 152
Cdd:cd04955 72 YDIAALNYAlkyikeqniKNPIFYILACRI-GPFIAPYIKkihKLGGKLFVNP-DGLEWKRAKWSLPVRKYWKFSESLMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 153 KFADEIIVLSESVQNYFEDIYGR-KTRFIPNGVKK------IEIKSAGLITEKYGLTKDSYILFLGRLVPEKGIRYLIEA 225
Cdd:cd04955 150 KHADLLICDSKNIEKYIRKEYGKsNTTFIAYGTDTlksslsDEDEKVREWYKEKGVKPGKYYLIVGRFVPENNYETMIRE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 226 FKDVQTDKKLIIAGGSSDTDEFANELKELA-KGDERIIFTGFVQGQE-LEELYSNAYIYTLPSDLEGMPLSLLEAMSYGN 303
Cdd:cd04955 230 FMKSSTKRDLVIITNVEGNAYYELLLKKTAfDHDERIKFVGTVYDQElLKYIRENAFAYLHGHEVGGTNPSLLEALGSTD 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752923616 304 CCIVSNISECTEVVEDKAMIFKKSDVSDLkIRLEEACNQSEMVKvLKNQATEFICSKYNWDKIVQE 369
Cdd:cd04955 310 LNLLLDVGFNREVAEDAALYWKKEPLASL-IDEVDNLNPDEISD-LGKKAKQRIEEAYTWEKIVDE 373
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
21-372 |
9.54e-33 |
|
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.
Pssm-ID: 340848 [Multi-domain] Cd Length: 377 Bit Score: 125.94 E-value: 9.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 21 GGIEIVVEELATRMVALGHEVT--CYNRSGHHVSGKEFDQHKNKEYKGVKLktiftlNIKGIAAMSSSVFGGIRAAFG-- 96
Cdd:cd03821 14 GGPVKVVLRLAAALAALGHEVTivSTGDGYESLVVEENGRYIPPQDGFASI------PLLRQGAGRTDFSPGLPNWLRrn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 97 --KYDIVHFHAegpcamLW---------LPKLFGKRCVATIHG-LDH---QREKWNKLAstYIMLGEKCAVKFADEIIVL 161
Cdd:cd03821 88 lrEYDVVHIHG------VWtytslaackLARRRGIPYVVSPHGmLDPwalQQKHWKKRI--ALHLIERRNLNNAALVHFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 162 SESVQNYFEDI-YGRKTRFIPNGVKKIEIKSAGLITEKYGLTKDS-YILFLGRLVPEKGIRYLIEAFKDVQ---TDKKLI 236
Cdd:cd03821 160 SEQEADELRRFgLEPPIAVIPNGVDIPEFDPGLRDRRKHNGLEDRrIILFLGRIHPKKGLDLLIRAARKLAeqgRDWHLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 237 IAGgsSDTDEFANELKELAK--GDERIIFTGFVQGQELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSniSEC- 313
Cdd:cd03821 240 IAG--PDDGAYPAFLQLQSSlgLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVIT--DKCg 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752923616 314 -TEVVEDKAMIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEF--ICSKYNWDKIVQETLN 372
Cdd:cd03821 316 lSELVEAGCGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRArqVEENFSWEAVAGQLGE 377
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
16-320 |
2.04e-32 |
|
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.
Pssm-ID: 340839 [Multi-domain] Cd Length: 351 Bit Score: 124.78 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 16 IPS-REGGIEIVVEELATRMVALGHEVTCYNRSGhhvsGKEFDQHKNKEYKGVKLKTIFTLNIKGIaamSSSVFGGIRAA 94
Cdd:cd03811 6 IPSlSGGGAERVLLNLANALDKRGYDVTLVLLRD----EGDLDKQLNGDVKLIRLLIRVLKLIKLG---LLKAILKLKRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 95 F--GKYDIVHFHAEGPCAMLWLPKLFGKRCVATIHG-LDHQREKWNKLASTYIMLgekcavKFADEIIVLSESVQNYFED 171
Cdd:cd03811 79 LkrAKPDVVISFLGFATYIVAKLAAARSKVIAWIHSsLSKLYYLKKKLLLKLKLY------KKADKIVCVSKGIKEDLIR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 172 IYG---RKTRFIPNGVKKIEIKSAGLITEKYGLTKDSYILFLGRLVPEKGIRYLIEAFKDVQTDK---KLIIAGGSSDTD 245
Cdd:cd03811 153 LGPsppEKIEVIYNPIDIDRIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYpdvKLVILGDGPLRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 246 EFANELKELaKGDERIIFTGFVqgqeleelySNAY-------IYTLPSDLEGMPLSLLEAMSYGNCCIVSNISECTEVVE 318
Cdd:cd03811 233 ELEKLAKEL-GLAERVIFLGFQ---------SNPYpylkkadLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILD 302
|
..
gi 1752923616 319 DK 320
Cdd:cd03811 303 DG 304
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
21-375 |
9.89e-32 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 122.81 E-value: 9.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 21 GGIEIVVEELATRMVALGHEVTCYNRSGHHVSGKEfdqhknKEYKGVKLKTIftlnikGIAAMSSsVFGGIRAAF----G 96
Cdd:cd03807 12 GGAETMLLRLLEHMDKSRFEHVVISLTGDGVLGEE------LLAAGVPVVCL------GLSSGKD-PGVLLRLAKlirkR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 97 KYDIVHFHAEGpcAMLWLP---KLFGKRCV-ATIHGLDHQREK-----WNKLASTYImlgekcavkFADEIIVLSESVQN 167
Cdd:cd03807 79 NPDVVHTWMYH--ADLIGGlaaKLAGGVKViWSVRSSNIPQRLtrlvrKLCLLLSKF---------SPATVANSSAVAEF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 168 YFEDIYG-RKTRFIPNGVKK----IEIKSAGLITEKYGLTKDSYIL-FLGRLVPEKGIRYLIEAFKDVQT---DKKLIIA 238
Cdd:cd03807 148 HQEQGYAkNKIVVIYNGIDLfklsPDDASRARARRRLGLAEDRRVIgIVGRLHPVKDHSDLLRAAALLVEthpDLRLLLV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 239 GGSSDTDEFANELKELAKGDeRIIFTGfvQGQELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNISECTEVVE 318
Cdd:cd03807 228 GRGPERPNLERLLLELGLED-RVHLLG--ERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVD 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752923616 319 DKA-MIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEFICSKYNWDKIVQETLNLYR 375
Cdd:cd03807 305 DGTgFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
96-375 |
2.68e-28 |
|
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.
Pssm-ID: 340828 [Multi-domain] Cd Length: 376 Bit Score: 113.63 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 96 GKYDIVHFHA--EGPCAMLWLPKLFGKRCVATIHGLD---HQREKWNKLAstyimlgEKCAVKFADEIIVLS----ESVQ 166
Cdd:cd03798 94 GPPDLIHAHFayPAGFAAALLARLYGVPYVVTEHGSDinvFPPRSLLRKL-------LRWALRRAARVIAVSkalaEELV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 167 NYFedIYGRKTRFIPNGVKkIEIKSAGLITEKYGLTKDsYILFLGRLVPEKGIRYLIEAFK---DVQTDKKLIIAGGSSD 243
Cdd:cd03798 167 ALG--VPRDRVDVIPNGVD-PARFQPEDRGLGLPLDAF-VILFVGRLIPRKGIDLLLEAFArlaKARPDVVLLIVGDGPL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 244 TDEFANELKELAKGDeRIIFTGFVQGQELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNISECTEVVEDK--A 321
Cdd:cd03798 243 REALRALAEDLGLGD-RVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPetG 321
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1752923616 322 MIFKKSDVSDLKIRLEEACNQSEMVkVLKNQATEFICSKYNWDKIVQETLNLYR 375
Cdd:cd03798 322 LLVPPGDADALAAALRRALAEPYLR-ELGEAARARVAERFSWVKAADRIAAAYR 374
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
206-332 |
7.92e-28 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 106.44 E-value: 7.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 206 YILFLGRLVPE-KGIRYLIEAFKDVQT---DKKLIIAGGSSDtdefaNELKELAKG-DERIIFTGFVQgqELEELYSNAY 280
Cdd:pfam13692 3 VILFVGRLHPNvKGVDYLLEAVPLLRKrdnDVRLVIVGDGPE-----EELEELAAGlEDRVIFTGFVE--DLAELLAAAD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1752923616 281 IYTLPSDLEGMPLSLLEAMSYGNCCIVSNISECTEVVEDKA-MIFKKSDVSDL 332
Cdd:pfam13692 76 VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENgLLVPPGDPEAL 128
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
203-356 |
3.16e-27 |
|
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 105.43 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 203 KDSYILFLGRLVPEKGIRYLIEAFKDVQTDK---KLIIAGGSSDTDEFANELKELAKGDeRIIFTGFVQGQELEELYSNA 279
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNpnlKLVIAGDGEEEKRLKKLAEKLGLGD-NVIFLGFVSDEDLPELLKIA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752923616 280 YIYTLPSDLEGMPLSLLEAMSYGNCCIVSNISECTEVVED--KAMIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEF 356
Cdd:pfam00534 80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDgeTGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
19-318 |
9.60e-26 |
|
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.
Pssm-ID: 340846 [Multi-domain] Cd Length: 345 Bit Score: 106.29 E-value: 9.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 19 REGGIEIVVEELATRMVALGHEVTCYNRSGhhvSGKEFDQHKNKEYKGVKlKTIFT--LNIKGIAAMsssvfggIRAAfg 96
Cdd:cd03819 9 EIGGAETYILDLARALAERGHRVLVVTAGG---PLLPRLRQIGIGLPGLK-VPLLRalLGNVRLARL-------IRRE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 97 KYDIVHFHAEGPcAML--WLPKLFGKRCVATIHGLdHQREKWNKLASTYIMlgekcavKFADEIIVLSESVQNYFEDIYG 174
Cdd:cd03819 76 RIDLIHAHSRAP-AWLgwLASRLTGVPLVTTVHGS-YLATYHPKDFALAVR-------ARGDRVIAVSELVRDHLIEALG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 175 R---KTRFIPNGV--KKIEIKSAGLITEKYGLTKDSY-ILFLGRLVPEKGIRYLIEA---FKDvQTDKKLIIAGGSSDTD 245
Cdd:cd03819 147 VdpeRIRVIPNGVdtDRFPPEAEAEERAQLGLPEGKPvVGYVGRLSPEKGWLLLVDAaaeLKD-EPDFRLLVAGDGPERD 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752923616 246 EFANELKELAKGDeRIIFTGFVQgqELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNISECTEVVE 318
Cdd:cd03819 226 EIRRLVERLGLRD-RVTFTGFRE--DVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVV 295
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
17-376 |
1.69e-23 |
|
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).
Pssm-ID: 340850 [Multi-domain] Cd Length: 357 Bit Score: 100.10 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 17 PSREGGIEIVVEELATRMVALGHEVTCYnRSGHHVSGKEFDQHKNKEYKGVKLKTIFTLNIKGIAAMSSSVFGGIRAAFG 96
Cdd:cd03823 11 PQRVGGAEISVHDLAEALVAEGHEVAVL-TAGVGPPGQATVARSVVRYRRAPDETLPLALKRRGYELFETYNPGLRRLLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 97 KY------DIVHFHA--EGPCAMLWLPKLFGKRCVATIHGLD-----HQREKWNKLAstyimlgekcavkfadeiiVLSE 163
Cdd:cd03823 90 RLledfrpDVVHTHNlsGLGASLLDAARDLGIPVVHTLHDYWllcprQFLFKKGGDA-------------------VLAP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 164 SvqNYFEDIYGR------KTRFIPNGVKKiEIKSAGLITEKyglTKDSYILFLGRLVPEKGIRYLIEAFKDV-QTDKKLI 236
Cdd:cd03823 151 S--RFTANLHEAnglfsaRISVIPNAVEP-DLAPPPRRRPG---TERLRFGYIGRLTEEKGIDLLVEAFKRLpREDIELV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 237 IAGGSSDTDEfanelkELAKGDERIIFTGFVQGQELEELYSNAYIYTLPSD-LEGMPLSLLEAMSYGNCCIVSNISECTE 315
Cdd:cd03823 225 IAGHGPLSDE------RQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAE 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752923616 316 VVEDKA--MIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEficsKYNWDKIVQETLNLYRG 376
Cdd:cd03823 299 LIQPGVngLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEP----PRSTESQAEEYLKLYRD 357
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
21-184 |
3.06e-23 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 94.91 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 21 GGIEIVVEELATRMVALGHEVTCYNRSGHHVSGKEfdqhknkEYKGVKLKTIFTLNIKGIAAMSSSVFGGIRAAF-GKYD 99
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEE-------VVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRrERPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 100 IVHFHAEGP--CAMLWLPKLFGKRCVATIHGLDHQREKW---NKLASTYIMLGEKCAVKFADEIIVLSESVQNYFEDIYG 174
Cdd:pfam13439 74 VVHAHSPFPlgLAALAARLRLGIPLVVTYHGLFPDYKRLgarLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYG 153
|
170
....*....|...
gi 1752923616 175 ---RKTRFIPNGV 184
Cdd:pfam13439 154 vppEKIRVIPNGV 166
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
7-368 |
3.25e-23 |
|
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
Pssm-ID: 340825 [Multi-domain] Cd Length: 391 Bit Score: 99.72 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 7 KICMLGHKRIPSrEGGIEIVVEELATRMVALGHEVTCYNRSGHHVSGKEFDqHKNKEYKGVKLKTIFTLNIKGIAAM--- 83
Cdd:cd03794 1 KILLISQYYPPP-KGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFA-GATETKDGIRVIRVKLGPIKKNGLIrrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 84 ------SSSVFGGIRAAFGKYDIVHFHAegPCAMLWLP-----KLFGKRCVATIHGL--DHQREK---WNKLASTYIMLG 147
Cdd:cd03794 79 lnylsfALAALLKLLVREERPDVIIAYS--PPITLGLAalllkKLRGAPFILDVRDLwpESLIALgvlKKGSLLKLLKKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 148 EKCAVKFADEIIVLSESVQNYFED--IYGRKTRFIPNGV--KKIEIKSAGLITEKYGLTKDSYILFLGRLVPEKGIRYLI 223
Cdd:cd03794 157 ERKLYRLADAIIVLSPGLKEYLLRkgVPKEKIIVIPNWAdlEEFKPPPKDELRKKLGLDDKFVVVYAGNIGKAQGLETLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 224 EAFKDVQTDK--KLIIAGGSSDTDEFanELKELAKGDERIIFTGFVQGQELEELYSNAYI--YTLPSDLE---GMPLSLL 296
Cdd:cd03794 237 EAAERLKRRPdiRFLFVGDGDEKERL--KELAKARGLDNVTFLGRVPKEEVPELLSAADVglVPLKDNPAnrgSSPSKLF 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752923616 297 EAMSYGNCCIVSNISECTEVVEDK--AMIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEFICSKYNWDKIVQ 368
Cdd:cd03794 315 EYMAAGKPILASDDGGSDLAVEINgcGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLAD 388
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
17-310 |
4.85e-22 |
|
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340826 [Multi-domain] Cd Length: 355 Bit Score: 95.80 E-value: 4.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 17 PSREGGIEIVVEELATRMVALGHEVT--CYNRSGHhvsGKEFDQHKNKEYKGvklKTIFTLNIKGIaamSSSVFGGIRAA 94
Cdd:cd03795 10 YPDIGGIEQVIYDLAEGLKKKGIEVDvlCFSKEKE---TPEKEENGIRIHRV---KSFLNVASTPF---SPSYIKRFKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 95 FGKYDIVHFHAEGPCA-MLWLPKLFGKRCVATIHgLDHQREKwnKLASTYIMLgEKCAVKFADEIIVLSEsvqNYFEDI- 172
Cdd:cd03795 81 AKEYDIIHYHFPNPLAdLLLFFSGAKKPVVVHWH-SDIVKQK--KLLKLYKPL-MTRFLRRADRIIATSP---NYVETSp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 173 ----YGRKTRFIPNGVKKIEI----KSAGLITEKYGLTKDsyILFLGRLVPEKGIRYLIEAFKdvQTDKKLIIAGGSSDT 244
Cdd:cd03795 154 tlreFKNKVRVIPLGIDKNVYniprVDFENIKREKKGKKI--FLFIGRLVYYKGLDYLIEAAQ--YLNYPIVIGGEGPLK 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752923616 245 DEFANELKELakGDERIIFTGFVQGQELEELYSNAYIYTLPSDL--EGMPLSLLEAMSYGNCCIVSNI 310
Cdd:cd03795 230 PDLEAQIELN--LLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVLrsEAFGIVLLEAMMCGKPVISTNI 295
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
91-366 |
6.73e-22 |
|
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.
Pssm-ID: 340844 [Multi-domain] Cd Length: 372 Bit Score: 95.81 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 91 IRAAFGKYDIVHFHAegPCAMLWLPKLFGKR----CVATIH----GLDHQREKWNKLASTYImlgEKCAVKF---ADEII 159
Cdd:cd03817 78 DRIKELGPDIIHTHT--PFSLGKLGLRIARKlkipIVHTYHtmyeDYLHYIPKGKLLVKAVV---RKLVRRFynhTDAVI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 160 VLSESVQNYF-EDIYGRKTRFIPNGV--KKIEIKSAGLITEKYGLTKDSY-ILFLGRLVPEKGIRYLIEAFKDVQTDK-- 233
Cdd:cd03817 153 APSEKIKDTLrEYGVKGPIEVIPNGIdlDKFEKPLNTEERRKLGLPPDEPiLLYVGRLAKEKNIDFLLRAFAELKKEPni 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 234 KLIIAGGSSDTDEFANELKELAKGDeRIIFTGFVQGQELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNISEC 313
Cdd:cd03817 233 KLVIVGDGPEREELKELARELGLAD-KVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAA 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752923616 314 TEVVEDK--AMIFKKSD--VSDLKIRLEEacnQSEMVKVLKNQATEFICSKYNWDKI 366
Cdd:cd03817 312 SELVEDGenGFLFEPNDetLAEKLLHLRE---NLELLRKLSKNAEISAREFAFAKSV 365
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
79-321 |
1.09e-21 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340841 [Multi-domain] Cd Length: 474 Bit Score: 96.25 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 79 GIAAMSSSVFGGIRAAFG--KYDIVHFHAEGPCAML--WLPKLFGKRCVATIHGLDHQREKWNKLASTYIM--------- 145
Cdd:cd03813 153 TLRNMLLPLFKLAIAADDlpEADLYHSVSTGYAGLLgaLARHRRGIPFLLTEHGIYTRERKIEILQSTWIMgyikklwir 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 146 ----LGeKCAVKFADEIIVLSESVQNYfEDIYG---RKTRFIPNGVKKIEIKSAGLITEKygltKDSYIL-FLGRLVPEK 217
Cdd:cd03813 233 fferLG-KLAYQQADKIISLYEGNRRR-QIRLGadpDKTRVIPNGIDIQRFAPAREERPE----KEPPVVgLVGRVVPIK 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 218 GIRYLIEAFKDVQTDKK---LIIAGGSSDTDEFANELKELAKG---DERIIFTGFvqgQELEELYSNAYIYTLPSDLEGM 291
Cdd:cd03813 307 DVKTFIRAFKLVRRAMPdaeGWLIGPEDEDPEYAQECKRLVASlglENKVKFLGF---QNIKEYYPKLGLLVLTSISEGQ 383
|
250 260 270
....*....|....*....|....*....|
gi 1752923616 292 PLSLLEAMSYGNCCIVSNISECTEVVEDKA 321
Cdd:cd03813 384 PLVILEAMASGVPVVATDVGSCRELIYGAD 413
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
13-319 |
2.31e-20 |
|
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 89.00 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 13 HKRIPSREGGIEIVVEELATRMVALGHEVTcynrsghhvsgkefdqhknkeykgvklktIFTLNIKGIAamsssvFGGIR 92
Cdd:cd01635 5 TGEYPPLRGGLELHVRALARALAALGHEVT-----------------------------VLALLLLALR------RILKK 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 93 AAFGKYDIVHFHaEGPCAMLWLP---KLFGKRCVATIHGLDHqreKWNKLASTYIMLGEKCAVKFADEiivlsesvqnyf 169
Cdd:cd01635 50 LLELKPDVVHAH-SPHAAALAALlaaRLLGIPIVVTVHGPDS---LESTRSELLALARLLVSLPLADK------------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 170 ediygrktrfipngvkkieiksaglitekygltkdsyiLFLGRLVPEKGIRYLIEAFKDV---QTDKKLIIAGGSSDTDE 246
Cdd:cd01635 114 --------------------------------------VSVGRLVPEKGIDLLLEALALLkarLPDLVLVLVGGGGEREE 155
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752923616 247 FANELKELAKGDERIIFTGFVQGQELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNISECTEVVED 319
Cdd:cd01635 156 EEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
210-375 |
2.01e-19 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 83.12 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 210 LGRLVPEKGIRYLIEAfkdvqtdkkliiaggssdtdefanelkelakgderiiftgfvqgqeleeLYSNAYIYTLPSDLE 289
Cdd:COG0438 1 MGRLVPRKGLDLLLEA-------------------------------------------------LLAAADVFVLPSRSE 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 290 GMPLSLLEAMSYGNCCIVSNISECTEVVEDK--AMIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEFICSKYNWDKIV 367
Cdd:COG0438 32 GFGLVLLEAMAAGLPVIATDVGGLPEVIEDGetGLLVPPGDPEALAEAILRLLEDPELRRRLGEAARERAEERFSWEAIA 111
|
....*...
gi 1752923616 368 QETLNLYR 375
Cdd:COG0438 112 ERLLALYE 119
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
92-365 |
3.48e-18 |
|
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340860 [Multi-domain] Cd Length: 365 Bit Score: 84.81 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 92 RAAFGKYDIVHFHAeGPCAMLWLP--KLFGKRCVATIHGLD-HQREKW---NKLASTYIMLGEKCAVKFADEIIVLSESV 165
Cdd:cd05844 76 GAAGLAPALVHAHF-GRDGVYALPlaRALGVPLVVTFHGFDiTTSRAWlaaSPGWPSQFQRHRRALQRPAALFVAVSGFI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 166 QNyfediygrktRFIPNGV--KKIEIKSAGLITEKYGLT----KDSYILFLGRLVPEKGIRYLIEAFKDVQT---DKKLI 236
Cdd:cd05844 155 RD----------RLLARGLpaERIHVHYIGIDPAKFAPRdpaeRAPTILFVGRLVEKKGCDVLIEAFRRLAArhpTARLV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 237 IAGGSSDTdefaNELKELAKGDERIIFTGFVQGQELEELYSNAYIYTLPS------DLEGMPLSLLEAMSYGNCCIVSNI 310
Cdd:cd05844 225 IAGDGPLR----PALQALAAALGRVRFLGALPHAEVQDWMRRAEIFCLPSvtaasgDSEGLGIVLLEAAACGVPVVSSRH 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752923616 311 SECTEVVED--KAMIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEFICSKYNWDK 365
Cdd:cd05844 301 GGIPEAILDgeTGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFDIRV 357
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
174-375 |
6.06e-17 |
|
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.
Pssm-ID: 340851 [Multi-domain] Cd Length: 364 Bit Score: 81.22 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 174 GRKTRFIPNGVKkIEI---KSAGLITEKYGLTKDSYILFLGRLV---PEKGIRYLIEAFKD-VQTDKKLIIAGGSSDtde 246
Cdd:cd03825 160 GLPVVVIPNGID-TEIfapVDKAKARKRLGIPQDKKVILFGAESvtkPRKGFDELIEALKLlATKDDLLLVVFGKND--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 247 fanelKELAKGDERIIFTGFV-QGQELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNISECTEVVEDKA--MI 323
Cdd:cd03825 236 -----PQIVILPFDIISLGYIdDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVtgYL 310
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752923616 324 FKKSDVSDLKIRLEEACNQSEMVKVLKNQATEFICSKYNWDKIVQETLNLYR 375
Cdd:cd03825 311 VPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYK 362
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
21-372 |
1.55e-16 |
|
sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
Pssm-ID: 340830 [Multi-domain] Cd Length: 398 Bit Score: 80.36 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 21 GGIEIVVEELATRMVALGHEVTCYNR--SGHHVSGKEFDQHKN------KEYKGVKLKTIFTLnikgIAAMSSSVFGGIR 92
Cdd:cd03800 21 GGQNVYVLELARALAELGYQVDIFTRriSPADPEVVEIAPGARvirvpaGPPEYLPKEELWPY----LEEFADGLLRFIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 93 AAFGKYDIVHFH--AEGPCAMLwLPKLFGKRCVATIHGLD-----HQREKWNKLASTYIMlGEKCAVKFADEIIVLS--- 162
Cdd:cd03800 97 REGGRYDLIHSHywDSGLVGAL-LARRLGVPLVHTFHSLGrvkyrHLGAQDTYHPSLRIT-AEEQILEAADRVIASTpqe 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 163 --ESVQNYfeDIYGRKTRFIPNGVkKIEI-----KSAGLITEKYGLTKDSYILFLGRLVPEKGIRYLIEAF---KDVQTD 232
Cdd:cd03800 175 adELISLY--GADPSRINVVPPGV-DLERffpvdRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFaqlPELREL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 233 KKLIIAGGSSD--TDEFANELKELAKgDERII----FTGFVQGQELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCI 306
Cdd:cd03800 252 ANLVLVGGPSDdpLSMDREELAELAE-ELGLIdrvrFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVV 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752923616 307 VSNISECTEVVEDK--AMIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEFICSKYNWDKIVQETLN 372
Cdd:cd03800 331 ATAVGGLQDIVRDGrtGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQLLT 398
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
175-376 |
1.93e-16 |
|
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.
Pssm-ID: 340857 [Multi-domain] Cd Length: 360 Bit Score: 79.80 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 175 RKTRFIPNGVK----KIEIKSAGLITEKYGLTKDSYILF-LGRLVPEKGIRYLIEAFKDV---QTDKKLIIAGGSSDTDE 246
Cdd:cd04951 154 NKSVPVYNGIDlnkfKKDINVRLKIRNKLNLKNDEFVILnVGRLTEAKDYPNLLLAISELilsKNDFKLLIAGDGPLRNE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 247 FANELKELaKGDERIIFTGFVQgqELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNISECTEVVEDKAMIFKK 326
Cdd:cd04951 234 LERLICNL-NLVDRVILLGQIS--NISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHNYVVPV 310
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752923616 327 SDVSDLKIRLEEACNQSEMVKVLKNQATEFICSKYNWDKIVQETLNLYRG 376
Cdd:cd04951 311 SDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFSINTIVNEWERLYSG 360
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
52-310 |
1.73e-14 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).
Pssm-ID: 340840 [Multi-domain] Cd Length: 357 Bit Score: 73.86 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 52 SGKEFDQHKNKEYKGVKLKTIFTLNIK--GIAAMSSSVFGGIRAAF-----GKYDIVHFHA-EGPCAMLWLPKLFGKRC- 122
Cdd:cd03812 28 SKIEFDFLATSDDKGEYDEELEELGGKifYIPPKKKNIIKYFIKLLklikkEKYDIVHVHGsSSNGIILLLAAKAGVPVr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 123 VATIHGLDHQREKWNKLastYIMLGEKCAVKFADEIIVLSESVQNY-FEDIYGRKTRFIPNGV-----KKIEIKSAgLIT 196
Cdd:cd03812 108 IAHSHNTKDSSIKLRKI---RKNVLKKLIERLSTKYLACSEDAGEWlFGEVENGKFKVIPNGIdiekyKFNKEKRR-KRR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 197 EKYGLTKDSYILFLGRLVPEKGIRYLIEAF---KDVQTDKKLIIAGgssdTDEFANELKELAKG---DERIIFTGFVQgq 270
Cdd:cd03812 184 KLLILEDKLVLGHVGRFNEQKNHSFLIDIFeelKKKNPNVKLVLVG----EGELKEKIKEKVKElglEDKVIFLGFRN-- 257
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1752923616 271 ELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNI 310
Cdd:cd03812 258 DVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDT 297
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
7-302 |
2.22e-14 |
|
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.
Pssm-ID: 340832 [Multi-domain] Cd Length: 333 Bit Score: 73.48 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 7 KICMLGHKRI---PSREGGIEIVVEELATRMVALGHEVTCYNRSGHHVSGKefdqhkNKEYKGVKLKTIFTLNIKGIAAM 83
Cdd:cd03802 1 RIAQVSPPRGpvpPGKYGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSAP------LVAVIPRALRLDPIPQESKLAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 84 SSSVFGGIRAafGKYDIVHFHAegPCAMLWLPKLFGKRCVATIHGldhqrekwNKLASTYIMLGEKCAVKFadeiIVLSE 163
Cdd:cd03802 75 LEALEVQLRA--SDFDVIHNHS--YDWLPPFAPLIGTPFVTTLHG--------PSIPPSLAIYAAEPPVNY----VSISD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 164 SVQNYFEDIYGRKTrfIPNGVkkiEIKSAGLITEKYGltkdsYILFLGRLVPEKGIRYLIEAFKdvQTDKKLIIAGGSSD 243
Cdd:cd03802 139 AQRAATPPIDYLTV--VHNGL---DPADYRFQPDPED-----YLAFLGRIAPEKGLEDAIRVAR--RAGLPLKIAGKVRD 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 244 TDEFaNELKELAKGdERIIFTGFVQGQELEELYSNAYIYTLPSDL-EGMPLSLLEAMSYG 302
Cdd:cd03802 207 EDYF-YYLQEPLPG-PRIEFIGEVGHDEKQELLGGARALLFPINWdEPFGLVMIEAMACG 264
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
97-375 |
2.09e-13 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340859 [Multi-domain] Cd Length: 370 Bit Score: 70.84 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 97 KYDIVHFHAEGP---CAMLwLPKLFGK--RCVATIHGLDhqrekwnklastYIMLGE----KCAVKFA----DEIIVLSE 163
Cdd:cd04962 84 KLDVLHAHYAIPhasCAYL-AREILGEkiPIVTTLHGTD------------ITLVGYdpslQPAVRFSinksDRVTAVSS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 164 SVQNYFEDIYG--RKTRFIPNGVK--KIEIKSAGLITEKYGLTKDSYILF-LGRLVPEKGIRYLIEAFKDVQ--TDKKLI 236
Cdd:cd04962 151 SLRQETYELFDvdKDIEVIHNFIDedVFKRKPAGALKRRLLAPPDEKVVIhVSNFRPVKRIDDVVRVFARVRrkIPAKLL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 237 IAGGSSDTDEFANELKELAKGDeRIIFTGFVQgqELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNISECTEV 316
Cdd:cd04962 231 LVGDGPERVPAEELARELGVED-RVLFLGKQD--DVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEV 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752923616 317 VEDKAMIFkKSDVSD--------LKIrLEEACNQSEMVKVLKNQATEFICSKynwdKIVQETLNLYR 375
Cdd:cd04962 308 VKHGETGF-LSDVGDvdamaksaLSI-LEDDELYNRMGRAARKRAAERFDPE----RIVPQYEAYYR 368
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
94-375 |
3.14e-13 |
|
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.
Pssm-ID: 340849 [Multi-domain] Cd Length: 370 Bit Score: 70.11 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 94 AFGKYDIVHF--------HAEGPcAMLWLPKLFGKRCVATIHGLDHQREKWNKLASTYIMLGEKcavkfADEIIVLSESV 165
Cdd:cd03822 72 NFKKPDVVHIqhefgifgGKYGL-YALGLLLHLRIPVITTLHTVLDLSDPGKQALKVLFRIATL-----SERVVVMAPIS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 166 QNYFEDIY---GRKTRFIPNGVkkIEIKSAGLITEK--YGLTKDSYILFLGRLVPEKGIRYLIEAFKDVQ---TDKKLII 237
Cdd:cd03822 146 RFLLVRIKlipAVNIEVIPHGV--PEVPQDPTTALKrlLLPEGKKVILTFGFIGPGKGLEILLEALPELKaefPDVRLVI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 238 AGG---SSDTDEFANELK----ELAKGDERIIFTGFVQGQELEELYSNAYIYTLP--SDLEGMPLSLLEAMSYGNCCIVS 308
Cdd:cd03822 224 AGElhpSLARYEGERYRKaaieELGLQDHVDFHNNFLPEEEVPRYISAADVVVLPylNTEQSSSGTLSYAIACGKPVIST 303
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752923616 309 NI-SECTEVVEDKAMIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEFICSkYNWDKIVQETLNLYR 375
Cdd:cd03822 304 PLrHAEELLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARA-MTWESIADRYLRLFN 370
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
99-375 |
3.75e-12 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340842 [Multi-domain] Cd Length: 365 Bit Score: 66.93 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 99 DIVHFHAEGP---CAMLWLPKLfGKRCVATIHgldhqrEKWNKLASTYIMLG-EKCAVKF-------ADEIIVLSESVQN 167
Cdd:cd03814 86 DIIHIATPGPlglAALRAARRL-GLPVVTSYH------TDFPEYLSYYTLGPlSWLAWAYlrwfhnpFDTTLVPSPSIAR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 168 YFEDIYGRKTRFIPNGVKKI----EIKSAGLiTEKYGLTKDSYILFLGRLVPEKGIRYLIEAF---KDVQTDKKLIIAGG 240
Cdd:cd03814 159 ELEGHGFERVRLWPRGVDTElfhpSRRDAAL-RRRLGPPGRPLLLYVGRLAPEKNLEALLDADlplAASPPVRLVVVGDG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 241 SsdtdefanELKELAKGDERIIFTGFVQGQELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNISECTEVVEDK 320
Cdd:cd03814 238 P--------ARAELEARGPDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPG 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752923616 321 --AMIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEFIcSKYNWDKIVQETLNLYR 375
Cdd:cd03814 310 gtGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEA-ERYSWEAFLDNLLDYYA 365
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
157-368 |
9.17e-11 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 62.89 E-value: 9.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 157 EIIVLSESVQNYFEDiygrktrFIPNGvkKIEIKSAGLITEKYGLTK-------------DSYILFLGRLVPEKGIRYLI 223
Cdd:PRK15484 142 KIIVPSQFLKKFYEE-------RLPNA--DISIVPNGFCLETYQSNPqpnlrqqlnispdETVLLYAGRISPDKGILLLM 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 224 EAFKDVQTDK---KLIIAG-----GSSDTDEFANELKELAKG-DERIIFTGFVQGQELEELYSNAYIYTLPSDL-EGMPL 293
Cdd:PRK15484 213 QAFEKLATAHsnlKLVVVGdptasSKGEKAAYQKKVLEAAKRiGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVeEAFCM 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 294 SLLEAMSYGNCCIVSNISECTEVVEDKAMIFK-------KSDVSDLKIRLEEacnqSEMVKVLKNqATEFICSKYNWDKI 366
Cdd:PRK15484 293 VAVEAMAAGKPVLASTKGGITEFVLEGITGYHlaepmtsDSIISDINRTLAD----PELTQIAEQ-AKDFVFSKYSWEGV 367
|
..
gi 1752923616 367 VQ 368
Cdd:PRK15484 368 TQ 369
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
21-183 |
1.13e-10 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 59.34 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 21 GGIEIVVEELATRMVALGHEVTCYNRSGhhvSGKEFDQHKNkeykGV---KLKTIFTLNIKGIAAMSSSVFGGIRAafGK 97
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGG---PPGRPELVGD----GVrvhRLPVPPRPSPLADLAALRRLRRLLRA--ER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 98 YDIVHFH-AEGPCAMLWLPKLFGKRCVATIHGLDHQREKWnkLASTYIMLGEKCAVKFADEIIVLSESVQNYFEDIYGR- 175
Cdd:pfam13579 72 PDVVHAHsPTAGLAARLARRRRGVPLVVTVHGLALDYGSG--WKRRLARALERRLLRRADAVVVVSEAEAELLRALGVPa 149
|
....*....
gi 1752923616 176 -KTRFIPNG 183
Cdd:pfam13579 150 aRVVVVPNG 158
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
156-302 |
1.47e-10 |
|
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.
Pssm-ID: 340855 [Multi-domain] Cd Length: 328 Bit Score: 61.93 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 156 DEIIVLSESVQNYFEDIYGRKTRF--IPNGVKKIEIKSAGLITEKygltkdSY-ILFLGRLVPEKGIRYLIEAFKDVQT- 231
Cdd:cd04949 115 DAIIVSTEQQKQDLSERFNKYPPIftIPVGYVDQLDTAESNHERK------SNkIITISRLAPEKQLDHLIEAVAKAVKk 188
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752923616 232 --DKKLIIAGGSSDTDEFANELKELaKGDERIIFTGFVQGqeLEELYSNAYIYTLPSDLEGMPLSLLEAMSYG 302
Cdd:cd04949 189 vpEITLDIYGYGEEREKLKKLIEEL-HLEDNVFLKGYHSN--LDQEYQDAYLSLLTSQMEGFGLTLMEAIGHG 258
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
156-356 |
1.94e-10 |
|
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.
Pssm-ID: 340833 [Multi-domain] Cd Length: 356 Bit Score: 61.53 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 156 DEIIVLSESVQNYFEDIYGRKTRFI--PNGVKKIEIKSaglitekyglTKDSYILFLGRLVPEKGIRYLIEAFKdvQTDK 233
Cdd:cd03804 159 DLFIANSQFVARRIKKFYGRESTVIypPVDTDAFAPAA----------DKEDYYLTASRLVPYKRIDLAVEAFN--ELPK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 234 KLIIAGGSSDTDefanELKelAKGDERIIFTGFVQGQELEELYSNAYIYTLPSDlEGMPLSLLEAMSYGNCCIVSNISEC 313
Cdd:cd03804 227 RLVVIGDGPDLD----RLR--AMASPNVEFLGYQPDEVLKELLSKARAFVFAAE-EDFGIVPVEAQACGTPVIAFGKGGA 299
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1752923616 314 TEVVED--KAMIFKKSDVSDLKIRLEEACNQSEMVKV--LKNQATEF 356
Cdd:cd03804 300 LETVRPgpTGILFGEQTVESLKAAVEEFEQNFDRFKPqaIRANAERF 346
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
96-369 |
4.20e-10 |
|
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.
Pssm-ID: 340829 [Multi-domain] Cd Length: 350 Bit Score: 60.54 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 96 GKYDIVHFH---AEGPCAMLWLPKLFGKRCVATIHGLDHQREKWNKLASTYIMLgekcavkFADEIIVLSESvqNYFedi 172
Cdd:cd03799 69 GAYDIIHCQfgpLGALGALLRRLKVLKGKLVTSFRGYDISMYVILEGNKVYPQL-------FAQGDLFLPNC--ELF--- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 173 ygrKTRFIPNGV--KKIEIKSAGLITEKYGLtKDSY--------ILFLGRLVPEKGIRYLIEAFKDVQTDKKLI---IAG 239
Cdd:cd03799 137 ---KHRLIALGCdeKKIIVHRSGIDCNKFRF-KPRYlpldgkirILTVGRLTEKKGLEYAIEAVAKLAQKYPNIeyqIIG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 240 GSSDTDEFANELKELAKGDeRIIFTGFVQGQELEELYSNAYIYTLPS------DLEGMPLSLLEAMSYGNCCIVSNISEC 313
Cdd:cd03799 213 DGDLKEQLQQLIQELNIGD-CVKLLGWKPQEEIIEILDEADIFIAPSvtaadgDQDGPPNTLKEAMAMGLPVISTEHGGI 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752923616 314 TEVVEDKAMIF--KKSDVSDLKIRLEEACNQSEMVKVLKNQATEFICSKYNWDKIVQE 369
Cdd:cd03799 292 PELVEDGVSGFlvPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDINKLNDE 349
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
152-319 |
3.31e-08 |
|
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.
Pssm-ID: 340854 [Multi-domain] Cd Length: 401 Bit Score: 54.77 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 152 VKFADEIIVLSESVQNYFEDIYgrktrfiPNGVKKIEIKSAGLITEKYG----LTKDSYILFLGRLVPEKGIRYLIEAFK 227
Cdd:cd04946 175 VSYLDAVFLISKEGKDYLQKCY-------PAYKEKIFVSRLGVSDKEQYskvkKEGDLRLVSCSSIVPVKRIDLIIETLN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 228 DVQTDKKLI------IAGGSsdtdeFANELKELAKG---DERIIFTGFVQGQELEELY--SNAYIYTLPSDLEGMPLSLL 296
Cdd:cd04946 248 SLCVAHPSIciswthIGGGP-----LKERLEKLAENkleNVKVNFTGEVSNKEVKQLYkeNDVDVFVNVSESEGIPVSIM 322
|
170 180
....*....|....*....|...
gi 1752923616 297 EAMSYGNCCIVSNISECTEVVED 319
Cdd:cd04946 323 EAISFGIPVIATNVGGTREIVEN 345
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
187-309 |
8.07e-08 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 53.56 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 187 IEIKSAGLITEKYGLTKDsyILFLGRLVPE--KGIRYLIEAFKDVQTDKKLIIAGGSSDtDEFANELKELAKGDERIIFT 264
Cdd:PRK09922 165 VEIKTIIIPPPERDKPAV--FLYVGRLKFEgqKNVKELFDGLSQTTGEWQLHIIGDGSD-FEKCKAYSRELGIEQRIIWH 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1752923616 265 GFvQGQELEELYSNAYIYT---LPSDLEGMPLSLLEAMSYGNCCIVSN 309
Cdd:PRK09922 242 GW-QSQPWEVVQQKIKNVSallLTSKFEGFPMTLLEAMSYGIPCISSD 288
|
|
| Glyco4_Geo_Pelo |
NF038229 |
GPMC system family 4 glycosyltransferase; Members of this family are family 4 ... |
99-311 |
1.50e-07 |
|
GPMC system family 4 glycosyltransferase; Members of this family are family 4 glycosyltransferases of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family.
Pssm-ID: 439530 [Multi-domain] Cd Length: 338 Bit Score: 52.68 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 99 DIVH-FHA--EGPCAmLWLPKLFGKRCVATIHG-------LDHQREkwnklastyIMLGekcAVKFADEIIVLSESV--- 165
Cdd:NF038229 57 DIIHaFHAyrSGRVW-LELARALGIPYLVTLTGtdvnealDPDRRP---------ETLR---VLRGAAAIVAFNPLVrer 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 166 -QNYFEDIYGrKTRFIPNGVkkiEIKSAGLITEKYGLTKDSYILFL--GRLVPEKGIRYLIEAFKDVQTDK---KLIIAG 239
Cdd:NF038229 124 lGQHLPPLAA-KLVVIPQGV---ELGGEPFPLRELGLFDSDEFVFLlpAGLRPVKGVLFLLEMLAPLHAEDprlRLAFAG 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752923616 240 GSSDTdEFANELKELAKGDERIIFTGFVQGQELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNIS 311
Cdd:NF038229 200 PVLDE-EYAAAFFAALARRPWARYLGEIPHDAMGALYRRADVVLNNSLFEGMANALLEAMALGRPVLARDIP 270
|
|
| DUF1972 |
pfam09314 |
Domain of unknown function (DUF1972); Members of this family of functionally uncharacterized ... |
10-183 |
3.60e-07 |
|
Domain of unknown function (DUF1972); Members of this family of functionally uncharacterized domains are found in bacterial glycosyltransferases and rhamnosyltransferases.
Pssm-ID: 430520 Cd Length: 186 Bit Score: 49.79 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 10 MLGHKRIPSREGGIEIVVEELatrmvalghevTCYNRSG---HHVSGKEFDQHKNK--EYKGVKLKTIFTLNIKG----- 79
Cdd:pfam09314 6 IIGSRGLPAKYGGFETFVEKL-----------TEYQKNKsikYHVACLSENSAKSEhfEYNGADCFTIKVPKIGParvia 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 80 --IAAMSSSVfGGIRAAFGKYDIVHFHAEGPCAMLWL-----PKLFGKRCVATiHGLDHQREKWNKLASTYIMLGEKCAV 152
Cdd:pfam09314 75 ydIMAINYAL-KYIKDHNIKEPIFYILGNTIGPFIAHfarkiHKLGGKLYVNP-DGLEWKRAKWSAPVRQYLKFSEKLMT 152
|
170 180 190
....*....|....*....|....*....|..
gi 1752923616 153 KFADEIIVLSESVQNYFEDIYGR-KTRFIPNG 183
Cdd:pfam09314 153 KYADLLISDNKGIEKYIHDEYGNpKTTYIAYG 184
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
99-308 |
2.81e-06 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 49.10 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 99 DIVHFH----AEGPCAMLWLPKLFGK---RCVATIHGLDHQ-------REKWNKLASTYIMLG---------EKCAVKFA 155
Cdd:cd03791 130 DIIHANdwhtALVPAYLKTRYRGPGFkkiKTVFTIHNLAYQglfpldtLAELGLPPELFHIDGlefygqinfLKAGIVYA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 156 DEIIVLSESvqnYFEDI----YG---------RKTRF--IPNGV-----------------------KKIEIKSAglITE 197
Cdd:cd03791 210 DRVTTVSPT---YAKEIltpeYGegldgvlraRAGKLsgILNGIdydewnpatdklipanysandleGKAENKAA--LQK 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 198 KYGLTKDSYIL---FLGRLVPEKGIRYLIEAFKD-VQTDKKLIIAG-GSSDTDEFANELKELAKGDERiiftgFVQGqel 272
Cdd:cd03791 285 ELGLPVDPDAPlfgFVGRLTEQKGVDLILDALPElLEEGGQLVVLGsGDPEYEQAFRELAERYPGKVA-----VVIG--- 356
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1752923616 273 eelYSNA---YIYTLpSDLEGMP-------LSLLEAMSYGNCCIVS 308
Cdd:cd03791 357 ---FDEAlahRIYAG-ADFFLMPsrfepcgLVQMYAMRYGTLPIVR 398
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
207-374 |
5.04e-05 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 44.92 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 207 ILFLGRLVPEKGIRYLIEA-------FKDVqtdkKLIIAGGSSDTDEFaNELKELAKGDERIIFTGFVQGQELEELYSNA 279
Cdd:cd03796 196 IVVISRLVYRKGIDLLVGIiprickkHPNV----RFIIGGDGPKRIEL-EEMREKYQLQDRVELLGAVPHEEVRDVLVQG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 280 YIYTLPSDLEGMPLSLLEAMSYGNCCIVSNISECTEVVEDKAMIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEFICS 359
Cdd:cd03796 271 HIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPDPEDIVRKLEEAISILRTGKHDPWSFHNRVKK 350
|
170
....*....|....*
gi 1752923616 360 KYNWDKIVQETLNLY 374
Cdd:cd03796 351 MYSWEDVARRTEKVY 365
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
207-302 |
5.98e-05 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 44.70 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 207 ILFLGRLVPEKGIRYLIEAFKDVQTDKKLIIAGGSsdtdeFANELKELAKGdERIIFTGFVQGQELEELYSNAYIYTLPS 286
Cdd:PLN02871 266 IVYVGRLGAEKNLDFLKRVMERLPGARLAFVGDGP-----YREELEKMFAG-TPTVFTGMLQGDELSQAYASGDVFVMPS 339
|
90
....*....|....*.
gi 1752923616 287 DLEGMPLSLLEAMSYG 302
Cdd:PLN02871 340 ESETLGFVVLEAMASG 355
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
206-310 |
1.89e-04 |
|
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.
Pssm-ID: 340823 [Multi-domain] Cd Length: 378 Bit Score: 43.08 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 206 YILFLGRLVPEKGIRYLIEA---FKDVQTDKKLIIAGGSSDTD----EFANELKELAKGDERIIFTGFVQG-QELEELYS 277
Cdd:cd03792 199 YILQVARFDPSKDPLGVIDAyklFKRRAEEPQLVICGHGAVDDpegsVVYEEVMEYAGDDHDIHVLRLPPSdQEINALQR 278
|
90 100 110
....*....|....*....|....*....|...
gi 1752923616 278 NAYIYTLPSDLEGMPLSLLEAMSYGNCCIVSNI 310
Cdd:cd03792 279 AATVVLQLSTREGFGLTVSEALWKGKPVIATPA 311
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
251-320 |
4.91e-04 |
|
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).
Pssm-ID: 340845 [Multi-domain] Cd Length: 396 Bit Score: 41.96 E-value: 4.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752923616 251 LKELAKGDERIIFTGFVQGQELEELY--SNAYIY-TLPSDLEgmpLSLLEAMSYGNCCIVSNISECTEVVEDK 320
Cdd:cd03818 273 LAELGVDLERVHFVGKVPYDQYVRLLqlSDAHVYlTYPFVLS---WSLLEAMACGCPVIGSDTAPVREVIRDG 342
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
97-375 |
3.76e-03 |
|
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.
Pssm-ID: 132132 [Multi-domain] Cd Length: 374 Bit Score: 38.94 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 97 KYDIVH------FHAEGPCAMLWLPklfgkrcvATIHG--------LDHQREKWNKLastyimlgEKCAVKFADEIIVLS 162
Cdd:TIGR03088 81 RPDIVHtrnlaaLEAQLPAALAGVP--------ARIHGehgrdvfdLDGSNWKYRWL--------RRLYRPLIHHYVAVS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 163 ESVQNYFEDIYG---RKTRFIPNGVKKIEIKSAGLITEK---YGLTKDSYILFL--GRLVPEKGIRYLIEAF-------K 227
Cdd:TIGR03088 145 RDLEDWLRGPVKvppAKIHQIYNGVDTERFHPSRGDRSPilpPDFFADESVVVGtvGRLQAVKDQPTLVRAFallvrqlP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 228 DVQTDKKLIIAGGSSDTDEFANELKelAKGDERII-FTGfvQGQELEELYSNAYIYTLPSDLEGMPLSLLEAMSYGNCCI 306
Cdd:TIGR03088 225 EGAERLRLVIVGDGPARGACEQMVR--AAGLAHLVwLPG--ERDDVPALMQALDLFVLPSLAEGISNTILEAMASGLPVI 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752923616 307 VSNISECTEVVED--KAMIFKKSDVSDLKIRLEEACNQSEMVKVLKNQATEFICSKYNWDKIVQETLNLYR 375
Cdd:TIGR03088 301 ATAVGGNPELVQHgvTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSINAMVAAYAGLYD 371
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
206-309 |
5.92e-03 |
|
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.
Pssm-ID: 340834 [Multi-domain] Cd Length: 392 Bit Score: 38.34 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752923616 206 YILFLGRLVPEKGIRYLIEAFKDVQTDK------KLIIAGGSsDTD-----EFANELKELAKG----DERIIFTGFVQGQ 270
Cdd:cd03805 213 FFLSINRFERKKNIALAIEAFAKLKQKLpefenvRLVIAGGY-DPRvaenvEYLEELQRLAEEllnvEDQVLFLRSISDS 291
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1752923616 271 ELEELYSNA--YIYTlPSDlE--GM-PLsllEAMSYGNCCIVSN 309
Cdd:cd03805 292 QKEQLLSSAlaLLYT-PSN-EhfGIvPL---EAMYAGKPVIACN 330
|
|
| |
