|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
2-343 |
4.71e-129 |
|
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: 372.39 E-value: 4.71e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 2 KIAILAPPYLPIPPNGYGGVERIVYYLTEGLVKKGHDVTLFAPGDSKVSSQVFSTFPFSLG-NSGEIKNKPY---LPLLQ 77
Cdd:cd03802 1 RIAQVSPPRGPVPPGKYGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSAPLVAVIPRALRlDPIPQESKLAellEALEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 78 YIDcfkkASGFDIIHNHAEHMAMFFADLVTTPVVHTLHSTLvegetLEEKRKVLLRFKNHNFVSISDNQREGLKELNFAG 157
Cdd:cd03802 81 QLR----ASDFDVIHNHSYDWLPPFAPLIGTPFVTTLHGPS-----IPPSLAIYAAEPPVNYVSISDAQRAATPPIDYLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 158 TVYNGIDIHKYSYIEKPrGDYLLWVGRITRKKGPLSAIEVAKKVSIPLVIAAAIDPVEKLFFEEEVKPqidGKTVSFVGE 237
Cdd:cd03802 152 VVHNGLDPADYRFQPDP-EDYLAFLGRIAPEKGLEDAIRVARRAGLPLKIAGKVRDEDYFYYLQEPLP---GPRIEFIGE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 238 LHGESLNKLYGNALCTLFPITWHEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGFIVDDLYQMIEAVKNIDKIKRK 317
Cdd:cd03802 228 VGHDEKQELLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDSVEEMAEAIANIDRIDRA 307
|
330 340
....*....|....*....|....*.
gi 1083527485 318 KCRERVVEKFTIEKMVNHYEDIYSKL 343
Cdd:cd03802 308 ACRRYAEDRFSAARMADRYEALYRKV 333
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-340 |
1.54e-57 |
|
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: 190.44 E-value: 1.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 2 KIAILAPPYLPippnGYGGVERIVYYLTEGLVKKGHDVTLFAPGDSKVSSQVFSTFPFSLGNSGEIKNKPYLPLLQYIDC 81
Cdd:cd03801 1 KILLLSPELPP----PVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 82 FKKASGFDIIHNHAEHMAMFFADL---VTTPVVHTLHSTLVEGETLEE--KRKVL-----LRFKNHNFVSISDNQREGLK 151
Cdd:cd03801 77 LLRLRKFDVVHAHGLLAALLAALLallLGAPLVVTLHGAEPGRLLLLLaaERRLLaraeaLLRRADAVIAVSEALRDELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 152 ELNFAG-----TVYNGIDIHKYS------YIEKPRGDYLLWVGRITRKKGPLSAIEVAKKV-----SIPLVIAAAIDPVE 215
Cdd:cd03801 157 ALGGIPpekivVIPNGVDLERFSpplrrkLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLlrrgpDVRLVIVGGDGPLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 216 KLFFEEEVKpqiDGKTVSFVGELHGESLNKLYGNALCTLFPiTWHEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTG 295
Cdd:cd03801 237 AELEELELG---LGDRVRFLGFVPDEELPALYAAADVFVLP-SRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGG 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1083527485 296 FIVD-----DLYQ-MIEAVKNIDKIKR--KKCRERVVEKFTIEKMVNHYEDIY 340
Cdd:cd03801 313 LVVPpddveALADaLLRLLADPELRARlgRAARERVAERFSWERVAERLLDLY 365
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
2-322 |
3.80e-30 |
|
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: 117.84 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 2 KIAILappylpIPPNGYGGVERIVYYLTEGLVKKGHDVTLFAPGDS-----KVSSQVFST-FPFSLGNSGEIKNKPYLPL 75
Cdd:cd03811 1 KILFV------IPSLSGGGAERVLLNLANALDKRGYDVTLVLLRDEgdldkQLNGDVKLIrLLIRVLKLIKLGLLKAILK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 76 LQYIdcFKKASgFDIIHNHAEHMAMFFA--DLVTTPVVHTLHSTLVEGETLEEK--RKVLLRFKNHNFVSISDNQREGLK 151
Cdd:cd03811 75 LKRI--LKRAK-PDVVISFLGFATYIVAklAAARSKVIAWIHSSLSKLYYLKKKllLKLKLYKKADKIVCVSKGIKEDLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 152 ELNFAG-----TVYNGIDIH-------KYSYIEKPRGDYLLWVGRITRKKGPLSAIEVAKKV-----SIPLVIAAAIDPV 214
Cdd:cd03811 152 RLGPSPpekieVIYNPIDIDriralakEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLrkkypDVKLVILGDGPLR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 215 EKLffEEEVKPQIDGKTVSFVGELhgESLNKLYGNALCTLFPITwHEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVT 294
Cdd:cd03811 232 EEL--EKLAKELGLAERVIFLGFQ--SNPYPYLKKADLFVLSSR-YEGFPNVLLEAMALGTPVVSTDCPGPREILDDGEN 306
|
330 340 350
....*....|....*....|....*....|...
gi 1083527485 295 GFIVDD-----LYQMIEAVKNIDKIKRKKCRER 322
Cdd:cd03811 307 GLLVPDgdaaaLAGILAALLQKKLDAALRERLA 339
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
2-337 |
1.16e-29 |
|
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: 116.54 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 2 KIAILAppylpippNGYGGVERIVYYLTEGLVKKGHDVTLFAPGDSKVSSQV----FSTFPFSLGNSGEIKNKPYLPLLQ 77
Cdd:cd03808 1 KILFIV--------NVDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELkelgVKVIDIPILRRGINPLKDLKALFK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 78 YIDCFKKaSGFDIIHNH---AEHMAMFFADLV-TTPVVHTLHST-LVEGETLEEKR------KVLLRFKNHNFVsISDNQ 146
Cdd:cd03808 73 LYKLLKK-EKPDIVHCHtpkPGILGRLAARLAgVPKVIYTVHGLgFVFTEGKLLRLlyllleKLALLFTDKVIF-VNEDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 147 REGLKELNFAG----TVYNGI----DIHKYSYIEKPRGDY-LLWVGRITRKKGPLSAIEVAKKVSIP-----LVIAAAID 212
Cdd:cd03808 151 RDLAIKKGIIKkkktVLIPGSgvdlDRFQYSPESLPSEKVvFLFVARLLKDKGIDELIEAAKILKKKgpnvrFLLVGDGE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 213 PveKLFFEEEVKPQIDGKTVSFVGelHGESLNKLYGNALCTLFPiTWHEPFGLVMVESMACGTPVIAYRIGSTSEVIEDG 292
Cdd:cd03808 231 L--ENPSEILIEKLGLEGRIEFLG--FRSDVPELLAESDVFVLP-SYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDG 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1083527485 293 VTGFIV-----DDLYQMIEA-VKNIDKIKR--KKCRERVVEKFTIEKMVNHYE 337
Cdd:cd03808 306 VNGFLVppgdvEALADAIEKlIEDPELRKEmgEAARKRVEEKFDEEKVVNKLL 358
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
14-333 |
5.70e-27 |
|
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: 108.90 E-value: 5.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 14 PPNgYGGVERIVYYLTEGLVKKGHDVTLFAPGDSKVSS-QVFSTFPFSLGNS-GEIKNKPYLPLlqYIDCFKK-ASGFDI 90
Cdd:cd03795 10 YPD-IGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPeKEENGIRIHRVKSfLNVASTPFSPS--YIKRFKKlAKEYDI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 91 IHNHAEH----MAMFFADlVTTPVVHTLHSTLVegetleeKRKVLLRFKN---HNF-------VSISDNQREGLKEL--- 153
Cdd:cd03795 87 IHYHFPNpladLLLFFSG-AKKPVVVHWHSDIV-------KQKKLLKLYKplmTRFlrradriIATSPNYVETSPTLref 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 154 -NFAGTVYNGIDIHKYS---------YIEKPRGDYLLWVGRITRKKGPLSAIEVAKKVSIPLVIAAAIDPVEKLffeeev 223
Cdd:cd03795 159 kNKVRVIPLGIDKNVYNiprvdfeniKREKKGKKIFLFIGRLVYYKGLDYLIEAAQYLNYPIVIGGEGPLKPDL------ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 224 KPQID---GKTVSFVGELHGESLNKLYGNALCTLFP-ITWHEPFGLVMVESMACGTPVIAYRIG-STSEVIEDGVTGFIV 298
Cdd:cd03795 233 EAQIElnlLDNVKFLGRVDDEEKVIYLHLCDVFVFPsVLRSEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVV 312
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1083527485 299 -----DDLYQMIEAVKNIDKIKR---KKCRERVVEKFTIEKMV 333
Cdd:cd03795 313 ppkdpDALAEAIDKLLSDEELREsygENAKKRFEELFTAEKMK 355
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
2-343 |
2.35e-25 |
|
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: 105.05 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 2 KIAILAPPYLPIPpngyGGVERIVYYLTEGLVKKGHDVTLFAPGDSKVSSQVFSTFPFSLGNSGEIKNKPYLPLLQ---Y 78
Cdd:cd03817 1 KIAIFTDTYLPQV----NGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEEVVRYRSFSIPIRKYHRQHIPFPFkkaV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 79 IDCFKKAsGFDIIHNHAE----HMAMFFADLVTTPVVHTLHsTLVE--------GETLEEK--RKVLLRFKNHN--FVSI 142
Cdd:cd03817 77 IDRIKEL-GPDIIHTHTPfslgKLGLRIARKLKIPIVHTYH-TMYEdylhyipkGKLLVKAvvRKLVRRFYNHTdaVIAP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 143 SDNQREGLKELNFAGTVY---NGIDIHKY--SYIEKPRGDY--------LLWVGRITRKKGPLSAIEVAKKVS----IPL 205
Cdd:cd03817 155 SEKIKDTLREYGVKGPIEvipNGIDLDKFekPLNTEERRKLglppdepiLLYVGRLAKEKNIDFLLRAFAELKkepnIKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 206 VIA---AAIDPVEKLFFEEEVkpqidGKTVSFVGELHGESLNKLYgnALCTLFPITWH-EPFGLVMVESMACGTPVIAYR 281
Cdd:cd03817 235 VIVgdgPEREELKELARELGL-----ADKVIFTGFVPREELPEYY--KAADLFVFASTtETQGLVYLEAMAAGLPVVAAK 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 282 IGSTSEVIEDGVTGFIVDDlyQMIEAVKNIDKIKRKKCRERV--------VEKFTIEKMVnhyEDIYSKL 343
Cdd:cd03817 308 DPAASELVEDGENGFLFEP--NDETLAEKLLHLRENLELLRKlsknaeisAREFAFAKSV---EKLYEEV 372
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
17-338 |
2.41e-25 |
|
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: 104.75 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 17 GYGGVERIVYYLTEGLVKKGHDVTLFAPGDSKVSSQVFS--TFPFSLGNSGEIKNKPYLPLLQYIDCFKKASGFDIIHNH 94
Cdd:cd03809 12 RLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLreYPELSLGVIKIKLWRELALLRWLQILLPKKDKPDLLHSP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 95 AEHMAMFFADlvtTPVVHTLH--STLVEGETLEEKRKVLLRF-------KNHNFVSISDNQREGLKEL------NFAgTV 159
Cdd:cd03809 92 HNTAPLLLKG---CPQVVTIHdlIPLRYPEFFPKRFRLYYRLllpislrRADAIITVSEATRDDIIKFygvppeKIV-VI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 160 YNGIDIHKYSYIEKPR--------GDYLLWVGRITRKKGPLSAIEVAKKVS-----IPLVIAAAIDP-VEKLFfeEEVKP 225
Cdd:cd03809 168 PLGVDPSFFPPESAAVliakyllpEPYFLYVGTLEPRKNHERLLKAFALLKkqggdLKLVIVGGKGWeDEELL--DLVKK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 226 QIDGKTVSFVGELHGESLNKLYGNALCTLFPiTWHEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGF-------IV 298
Cdd:cd03809 246 LGLGGRVRFLGYVSDEDLPALYRGARAFVFP-SLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDAALYFdpldpesIA 324
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1083527485 299 DDLYQMIEAvKNIDKIKRKKCRERvVEKFTIEKMVNHYED 338
Cdd:cd03809 325 DAILRLLED-PSLREELIRKGLER-AKKFSWEKTAEKTLE 362
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
2-338 |
2.76e-25 |
|
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: 104.33 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 2 KIAILAPPYlpiPPNGYGGVERIVYYLTEGLVKKGHDVTLFAP--GDSKVSSQVFSTFPFSLGNSGEIKNKPYLP----- 74
Cdd:cd03823 1 KILLVNSLY---PPQRVGGAEISVHDLAEALVAEGHEVAVLTAgvGPPGQATVARSVVRYRRAPDETLPLALKRRgyelf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 75 ----------LLQYIDCFKkasgFDIIHNHaeHMAMFFADLVTT------PVVHTLHSTLvegetLEEKRKVLLRfKNHN 138
Cdd:cd03823 78 etynpglrrlLARLLEDFR----PDVVHTH--NLSGLGASLLDAardlgiPVVHTLHDYW-----LLCPRQFLFK-KGGD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 139 -FVSIS----DN-QREGLKELNFaGTVYNGIDIHKY------SYIEKPRgdyLLWVGRITRKKGPLSAIEVAKKV---SI 203
Cdd:cd03823 146 aVLAPSrftaNLhEANGLFSARI-SVIPNAVEPDLAppprrrPGTERLR---FGYIGRLTEEKGIDLLVEAFKRLpreDI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 204 PLVIAaaidpvEKLFFEEEVKPQIDGKtVSFVGELHGESLNKLYGNALCTLFPITWHEPFGLVMVESMACGTPVIAYRIG 283
Cdd:cd03823 222 ELVIA------GHGPLSDERQIEGGRR-IAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPFGLVVREAIAAGLPVIASDLG 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083527485 284 STSEVIEDGVTGFI-----VDDLY---QMIEAVKNIDKIKRKKCRERVVEKFTIEKMVNHYED 338
Cdd:cd03823 295 GIAELIQPGVNGLLfapgdAEDLAaamRRLLTDPALLERLRAGAEPPRSTESQAEEYLKLYRD 357
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
246-345 |
6.41e-25 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 97.37 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 246 LYGNALCTLFPiTWHEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGFIVD-----DLYQ-MIEAVKNIDKIKR--K 317
Cdd:COG0438 17 LLAAADVFVLP-SRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPpgdpeALAEaILRLLEDPELRRRlgE 95
|
90 100
....*....|....*....|....*...
gi 1083527485 318 KCRERVVEKFTIEKMVNHYEDIYSKLIK 345
Cdd:COG0438 96 AARERAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
3-343 |
7.89e-25 |
|
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: 103.61 E-value: 7.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 3 IAILAPPYlpiPPNGYGGVERIVYYLTEGLVKKGHDVTLFAPGD--SKVSSQVFSTF---PFSLGNSGEIKNKPYLPLLQ 77
Cdd:cd03798 1 VLILTNIY---PNANSPGRGIFVRRQVRALSRRGVDVEVLAPAPwgPAAARLLRKLLgeaVPPRDGRRLLPLKPRLRLLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 78 -----YIDCFKKASG---FDIIHNHAEHMAMFFADLV----TTPVVHTLHSTLV-EGETLEEKRKVLLRFKNHN----FV 140
Cdd:cd03798 78 plrapSLAKLLKRRRrgpPDLIHAHFAYPAGFAAALLarlyGVPYVVTEHGSDInVFPPRSLLRKLLRWALRRAarviAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 141 SISDnqREGLKELNFAGT----VYNGIDIHKYS-----YIEKPRGDYLLWVGRITRKKGPLSAIEVAKK-----VSIPLV 206
Cdd:cd03798 158 SKAL--AEELVALGVPRDrvdvIPNGVDPARFQpedrgLGLPLDAFVILFVGRLIPRKGIDLLLEAFARlakarPDVVLL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 207 IA---AAIDPVEKLFFEEEVKPQidgktVSFVGELHGESLNKLYgnALCTLFPI-TWHEPFGLVMVESMACGTPVIAYRI 282
Cdd:cd03798 236 IVgdgPLREALRALAEDLGLGDR-----VTFTGRLPHEQVPAYY--RACDVFVLpSRHEGFGLVLLEAMACGLPVVATDV 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083527485 283 GSTSEVIEDGVTGFIVDD------LYQMIEAV-KNIDKIKRKKCRERVVEKFTIEKMVNHYEDIYSKL 343
Cdd:cd03798 309 GGIPEVVGDPETGLLVPPgdadalAAALRRALaEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
2-301 |
2.33e-24 |
|
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: 101.99 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 2 KIAILAPPYLPIppngYGGVERIVYYLTEGLVKKGHDVTLFAPG-----DSKVSSQV-FSTFPFSLGNSGEIKNKPYLPL 75
Cdd:cd03814 1 RIALVTDTYHPQ----VNGVVRTLERLVDHLRRRGHEVRVVAPGpfdeaESAEGRVVsVPSFPLPFYPEYRLALPLPRRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 76 LQYIDCFkkasGFDIIHNHAE----HMAMFFADLVTTPVV---HTLHSTLVE----GETLEEKRKVLLRFKNH---NFVS 141
Cdd:cd03814 77 RRLIKEF----QPDIIHIATPgplgLAALRAARRLGLPVVtsyHTDFPEYLSyytlGPLSWLAWAYLRWFHNPfdtTLVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 142 ISDNQREgLKELNF--AGTVYNGIDI-------------HKYSYIEKPRgdyLLWVGRITRKKGplsaIEVAKKVSIPLv 206
Cdd:cd03814 153 SPSIARE-LEGHGFerVRLWPRGVDTelfhpsrrdaalrRRLGPPGRPL---LLYVGRLAPEKN----LEALLDADLPL- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 207 iaAAIDPVEKLFF--------EEEVKPQidgktVSFVGELHGESLNKLYGNALCTLFPITwHEPFGLVMVESMACGTPVI 278
Cdd:cd03814 224 --AASPPVRLVVVgdgparaeLEARGPD-----VIFTGFLTGEELARAYASADVFVFPSR-TETFGLVVLEAMASGLPVV 295
|
330 340
....*....|....*....|...
gi 1083527485 279 AYRIGSTSEVIEDGVTGFIVDDL 301
Cdd:cd03814 296 AADAGGPRDIVRPGGTGALVEPG 318
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
19-340 |
7.97e-23 |
|
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: 97.77 E-value: 7.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 19 GGVERIVYYLTEGLVKKGHDVTLFAPGDSKVSSQVFSTFPF---SLGNSGeiknKPYLP-LLQYIDCFKKaSGFDIIHNH 94
Cdd:cd03807 12 GGAETMLLRLLEHMDKSRFEHVVISLTGDGVLGEELLAAGVpvvCLGLSS----GKDPGvLLRLAKLIRK-RNPDVVHTW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 95 AEHmAMFFADLVT-----TPVVHTLHSTLvegetlEEKRKVLLRFKNHNF--------VSISDNQREGLKELNFA----G 157
Cdd:cd03807 87 MYH-ADLIGGLAAklaggVKVIWSVRSSN------IPQRLTRLVRKLCLLlskfspatVANSSAVAEFHQEQGYAknkiV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 158 TVYNGIDIHKYSY-----------IEKPRGDYLLW-VGRITRKKGPLSAIEVAKKV-----SIPLVIAAaidpveklffE 220
Cdd:cd03807 160 VIYNGIDLFKLSPddasrararrrLGLAEDRRVIGiVGRLHPVKDHSDLLRAAALLvethpDLRLLLVG----------R 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 221 EEVKPQID--------GKTVSFVGELH--GESLNKLYGNALCTLfpitwHEPFGLVMVESMACGTPVIAYRIGSTSEVIE 290
Cdd:cd03807 230 GPERPNLErlllelglEDRVHLLGERSdvPALLPAMDIFVLSSR-----TEGFPNALLEAMACGLPVVATDVGGAAELVD 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1083527485 291 DGvTGFIV-----DDLYQMIEAVKNiDKIKRKK----CRERVVEKFTIEKMVNHYEDIY 340
Cdd:cd03807 305 DG-TGFLVpagdpQALADAIRALLE-DPEKRARlgraARERIANEFSIDAMVRRYETLY 361
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
2-338 |
1.66e-22 |
|
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: 97.05 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 2 KIAILAPPYLPIppngYGGVERIVYYLTEGLVKKGHDVTLFAPGDSKVSSQV------------FSTFPFSLGNSGEIKN 69
Cdd:cd03821 1 KILHVTPSISPK----AGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVeengryippqdgFASIPLLRQGAGRTDF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 70 KPYLP--LLQYIDCFkkasgfDIIHNHA--EHMAMFFADLVT---TPVVHTLHSTLV---EGETLEEKRKVLLRFKNHN- 138
Cdd:cd03821 77 SPGLPnwLRRNLREY------DVVHIHGvwTYTSLAACKLARrrgIPYVVSPHGMLDpwaLQQKHWKKRIALHLIERRNl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 139 ---FVSISDNQREgLKELNFAGT------VYNGIDIHKY----SYIEK----PRGDYLLWVGRITRKKGPLSAIEVAKKV 201
Cdd:cd03821 151 nnaALVHFTSEQE-ADELRRFGLeppiavIPNGVDIPEFdpglRDRRKhnglEDRRIILFLGRIHPKKGLDLLIRAARKL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 202 S-----IPLVIAAAIDPVEKLFFEEEVKPQIDGKtVSFVGELHGESLNKLYGNALCTLFPiTWHEPFGLVMVESMACGTP 276
Cdd:cd03821 230 AeqgrdWHLVIAGPDDGAYPAFLQLQSSLGLGDR-VTFTGPLYGEAKWALYASADLFVLP-SYSENFGNVVAEALACGLP 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083527485 277 VIAYRIGSTSEVIEDGvTGFIVDDLYQMI-EAVKNI--DKIKRKKCRER------VVEKFTIEKMVNHYED 338
Cdd:cd03821 308 VVITDKCGLSELVEAG-CGVVVDPNVSSLaEALAEAlrDPADRKRLGEMarrarqVEENFSWEAVAGQLGE 377
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
178-322 |
6.33e-22 |
|
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: 90.41 E-value: 6.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 178 YLLWVGRITRKKGPLSAIEVAKKV-----SIPLVIAAaiDPVEKLFFEEEVKPQIDGKTVSFVGELHGESLNKLYGNALC 252
Cdd:pfam00534 4 IILFVGRLEPEKGLDLLIKAFALLkeknpNLKLVIAG--DGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083527485 253 TLFPITWhEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGFIVDDlYQMIEAVKNIDKI-----KRKKCRER 322
Cdd:pfam00534 82 FVLPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKP-NNAEALAEAIDKLledeeLRERLGEN 154
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
1-343 |
2.80e-21 |
|
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: 93.57 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 1 MKIAILAPPylpippnGYGGVERIVYYLTEGLVKKGHDVTLFApgdskvssqvfSTFPFSLGN-SGEIK----NKPYLPL 75
Cdd:cd04962 1 MKIGIVCYP-------SYGGSGVVATELGLELAERGHEVHFIS-----------SAIPFRLNLySGNIFfhevEVPNYPL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 76 LQY-----------IDCFKKAsGFDIIHNH-------AEHMA--MFFADlvtTPVVHTLHSTLVEGETLEEKRKVLLRF- 134
Cdd:cd04962 63 FEYppytlalaskiVEVAKEH-KLDVLHAHyaiphasCAYLAreILGEK---IPIVTTLHGTDITLVGYDPSLQPAVRFs 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 135 --KNHNFVSISDNQREGLKEL----NFAGTVYNGIDIHKYSYIEKPR----------GDYLLWVGRITRKKGPLSAIEV- 197
Cdd:cd04962 139 inKSDRVTAVSSSLRQETYELfdvdKDIEVIHNFIDEDVFKRKPAGAlkrrllappdEKVVIHVSNFRPVKRIDDVVRVf 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 198 ---AKKVSIPLVIAAA---IDPVEKLFFEEEVkpqidGKTVSFVGELhgESLNKLYGNALCTLFPiTWHEPFGLVMVESM 271
Cdd:cd04962 219 arvRRKIPAKLLLVGDgpeRVPAEELARELGV-----EDRVLFLGKQ--DDVEELLSIADLFLLP-SEKESFGLAALEAM 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 272 ACGTPVIAYRIGSTSEVIEDGVTGFI--VDDLYQMIEAVKNI--DKIKRKK----CRERVVEKFTIEKMVNHYEDIYSKL 343
Cdd:cd04962 291 ACGVPVVSSNAGGIPEVVKHGETGFLsdVGDVDAMAKSALSIleDDELYNRmgraARKRAAERFDPERIVPQYEAYYRRL 370
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
19-333 |
4.24e-21 |
|
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: 92.42 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 19 GGVERIVYYLTEGLVKKGHDVTLFAPGDSKV--------SSQVFSTFPFSLGNSgeIKNKPYLpllqyidcfKKASGFDI 90
Cdd:cd03819 11 GGAETYILDLARALAERGHRVLVVTAGGPLLprlrqigiGLPGLKVPLLRALLG--NVRLARL---------IRRERIDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 91 IHNHAEHMAMFFAD---LVTTPVVHTLH-STLVEGETLEekRKVLLRFKNHNFVSISDNQREGLKELNFAG-----TVYN 161
Cdd:cd03819 80 IHAHSRAPAWLGWLasrLTGVPLVTTVHgSYLATYHPKD--FALAVRARGDRVIAVSELVRDHLIEALGVDperirVIPN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 162 GIDIHKYS---------YIEKPRGDY-LLWVGRITRKKGPLSAIEVA----KKVSIPLVIAAaiDPVEKLFFEEEV-KPQ 226
Cdd:cd03819 158 GVDTDRFPpeaeaeeraQLGLPEGKPvVGYVGRLSPEKGWLLLVDAAaelkDEPDFRLLVAG--DGPERDEIRRLVeRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 227 IDGKtVSFVGelHGESLNKLYGNALCTLFPiTWHEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGFIVD--DLYQM 304
Cdd:cd03819 236 LRDR-VTFTG--FREDVPAALAASDVVVLP-SLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPpgDAEAL 311
|
330 340
....*....|....*....|....*....
gi 1083527485 305 IEAVknIDKIKRKKCRERVVEKFTIEKMV 333
Cdd:cd03819 312 ADAI--RAAKLLPEAREKLQAAAALTEAV 338
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
3-298 |
1.97e-19 |
|
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: 85.92 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 3 IAILAPPYLPippnGYGGVERIVYYLTEGLVKKGHDVTLFAPgdskvssqvfstfpfslgnsgeiknkpYLPLLQYIDCF 82
Cdd:cd01635 1 ILLVTGEYPP----LRGGLELHVRALARALAALGHEVTVLAL---------------------------LLLALRRILKK 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 83 KKASGFDIIHNHAEHMAMFFADLVT----TPVVHTLHSTLVEGETLEEKRKVLLRFKNHNFVsisdnqreglkelnfagt 158
Cdd:cd01635 50 LLELKPDVVHAHSPHAAALAALLAArllgIPIVVTVHGPDSLESTRSELLALARLLVSLPLA------------------ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 159 vyngidihkysyiekprgdYLLWVGRITRKKGPLSAIEVAKKV-----SIPLVIAAAIDPVEKLFFEEEVKpqIDGKTVS 233
Cdd:cd01635 112 -------------------DKVSVGRLVPEKGIDLLLEALALLkarlpDLVLVLVGGGGEREEEEALAAAL--GLLERVV 170
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083527485 234 FVGELHGESLNKLYGNAL-CTLFPiTWHEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGFIV 298
Cdd:cd01635 171 IIGGLVDDEVLELLLAAAdVFVLP-SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
71-338 |
1.03e-17 |
|
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: 83.44 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 71 PYLP-----LLQYIdcfKKASG-FDIIHNH---AEHMAMFFADLVTTPVVHTLHStlvegetLE-EKRKVLL-------- 132
Cdd:cd03800 82 PYLEefadgLLRFI---AREGGrYDLIHSHywdSGLVGALLARRLGVPLVHTFHS-------LGrVKYRHLGaqdtyhps 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 133 -RFK-------NHNFV-SISDNQREGLKEL--NFAG---TVYNGIDIHKYSYIEKPRGDY-----------LLWVGRITR 187
Cdd:cd03800 152 lRITaeeqileAADRViASTPQEADELISLygADPSrinVVPPGVDLERFFPVDRAEARRarlllppdkpvVLALGRLDP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 188 KKGPLSAIEVAKKvsIP-------LVIAA-------AIDPVEKLFFEEEVKpqIDGKtVSFVGELHGESLNKLYgnALCT 253
Cdd:cd03800 232 RKGIDTLVRAFAQ--LPelrelanLVLVGgpsddplSMDREELAELAEELG--LIDR-VRFPGRVSRDDLPELY--RAAD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 254 LFPIT-WHEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGFIVD--DLYQMIEAVKNI--DKIKRKKC----RERVV 324
Cdd:cd03800 305 VFVVPsLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDphDPEALAAALRRLldDPALWQRLsragLERAR 384
|
330
....*....|....
gi 1083527485 325 EKFTIEKMVNHYED 338
Cdd:cd03800 385 AHYTWESVADQLLT 398
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
19-338 |
1.93e-17 |
|
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: 82.29 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 19 GGVERIVYYLTEGLVKKGHDVTL----------FAPGDSKVSSQVFSTFPFSLGNSGEIKNKPYLPLLQYIdcfkKASGF 88
Cdd:cd03820 13 GGAERVAINLANHLAKKGYDVTIisldsaekppFYELDDNIKIKNLGDRKYSHFKLLLKYFKKVRRLRKYL----KNNKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 89 DIIHNHAEHMAMFFADLVT-TPVVHTLHSTL-VEGETLEEKRKVLLRFKNHNFV---SISDNQREGLKELNFAGTVYNGI 163
Cdd:cd03820 89 DVVISFRTSLLTFLALIGLkSKLIVWEHNNYeAYNKGLRRLLLRRLLYKRADKIvvlTEADKLKKYKQPNSNVVVIPNPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 164 DIHKYSYIEKPRGDYLLWVGRITRKKGPLSAIEVAKKVS-----IPLVIAAaiDPVEKlffeEEVKPQIDGKTVSFVGEL 238
Cdd:cd03820 169 SFPSEEPSTNLKSKRILAVGRLTYQKGFDLLIEAWALIAkkhpdWKLRIYG--DGPER----EELEKLIDKLGLEDRVKL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 239 HG--ESLNKLYGNALCTLFPITWhEPFGLVMVESMACGTPVIAYRIGS-TSEVIEDGVTGFIVDDlYQMIEAVKNIDKI- 314
Cdd:cd03820 243 LGptKNIAEEYANSSIFVLSSRY-EGFPMVLLEAMAYGLPIISFDCPTgPSEIIEDGENGLLVPN-GDVDALAEALLRLm 320
|
330 340 350
....*....|....*....|....*....|.
gi 1083527485 315 ----KRKKCRER---VVEKFTIEKMVNHYED 338
Cdd:cd03820 321 edeeLRKKMGKNarkNAERFSIEKIIKQWEE 351
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
19-343 |
2.79e-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: 81.61 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 19 GGVERIVYYLTEGLVKKGHDVTLFApGDskvssqvfstfpfslgnsgeikNKPYLPLLQYIDCfkkasgfDIIHNHAEHM 98
Cdd:cd03825 13 GGAARAAYRLHQALLAYGIDSTMLV-GR----------------------KKNLISKPEFIEA-------DIIHLHWIHG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 99 AMF-FADLV----TTPVVHTLH-----------STLVEGET-----------------------LEEKRKvLLRFKNHNF 139
Cdd:cd03825 63 GYLsLKALFkllrRKPVVWTLHdmwpftggchyPMECEGWKtgcgncpnlnsyppakkdlsrqlFRRKRE-ALAKKRLTI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 140 VSISD------NQREGLKELNFAgTVYNGIDIHKYSYIEKprgdyllwvgRITRKKgplsaIEVAKKVSIPLVIAAAIDP 213
Cdd:cd03825 142 VAPSRwladmvRRSPLLKGLPVV-VIPNGIDTEIFAPVDK----------AKARKR-----LGIPQDKKVILFGAESVTK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 214 VEKLF--FEEEVK-----------------PQI---DGKTVSFvGELH-GESLNKLYgnALCTLFPI-TWHEPFGLVMVE 269
Cdd:cd03825 206 PRKGFdeLIEALKllatkddlllvvfgkndPQIvilPFDIISL-GYIDdDEQLVDIY--SAADLFVHpSLADNLPNTLLE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 270 SMACGTPVIAYRIGSTSEVIEDGVTGFIV-----DDLYQMIEAVKNIDK---IKRKKCRERVVEKFTIEKMVNHYEDIYS 341
Cdd:cd03825 283 AMACGTPVVAFDTGGSPEIVQHGVTGYLVppgdvQALAEAIEWLLANPKereSLGERARALAENHFDQRVQAQRYLELYK 362
|
..
gi 1083527485 342 KL 343
Cdd:cd03825 363 DL 364
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
157-340 |
5.42e-16 |
|
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: 78.53 E-value: 5.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 157 GTVYNGIDIHKYSYIEKPR----GDYLLWVGRITRKKGPLSAIEVAKKVS--IPLVIAAAIDPV-EKLFFEEEVKPQIDG 229
Cdd:cd03813 270 RVIPNGIDIQRFAPAREERpekePPVVGLVGRVVPIKDVKTFIRAFKLVRraMPDAEGWLIGPEdEDPEYAQECKRLVAS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 230 ----KTVSFVGELH-GESLNKLygnALCTLFPITwhEPFGLVMVESMACGTPVIAYRIGSTSEVIED-----GVTGFIVD 299
Cdd:cd03813 350 lgleNKVKFLGFQNiKEYYPKL---GLLVLTSIS--EGQPLVILEAMASGVPVVATDVGSCRELIYGaddalGQAGLVVP 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1083527485 300 --DLYQMIEAVKNI--DKIKR----KKCRERVVEKFTIEKMVNHYEDIY 340
Cdd:cd03813 425 paDPEALAEALIKLlrDPELRqafgEAGRKRVEKYYTLEGMIDSYRKLY 473
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
174-327 |
5.45e-16 |
|
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: 78.10 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 174 PRGDYLLWVGRITRKKGPLSAIEVAKKVSIPLVIAAAIDPVEKLffeeevkPQIDGKTVSFVGELHGESLNKLYGNALCT 253
Cdd:cd03804 197 DKEDYYLTASRLVPYKRIDLAVEAFNELPKRLVVIGDGPDLDRL-------RAMASPNVEFLGYQPDEVLKELLSKARAF 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 254 LFPITwhEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGFI-----VDDLYQMIEA-VKNIDKIKRKKCRERvVEKF 327
Cdd:cd03804 270 VFAAE--EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILfgeqtVESLKAAVEEfEQNFDRFKPQAIRAN-AERF 346
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
176-308 |
7.37e-16 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 73.31 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 176 GDYLLWVGRIT-RKKGPLSAIEVakkvsIPLVIAAAIDPveKLFF-----EEEVKPQIDG--KTVSFVGELhgESLNKLY 247
Cdd:pfam13692 1 RPVILFVGRLHpNVKGVDYLLEA-----VPLLRKRDNDV--RLVIvgdgpEEELEELAAGleDRVIFTGFV--EDLAELL 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083527485 248 GNALCTLFPITWhEPFGLVMVESMACGTPVIAYRIGSTSEVIeDGVTGFIV--DDLYQMIEAV 308
Cdd:pfam13692 72 AAADVFVLPSLY-EGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVppGDPEALAEAI 132
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
17-342 |
3.45e-15 |
|
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: 75.56 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 17 GYGGVERIVYYLTEGLVKKGHDVT-LFAPGDSKVSSQVFSTFPFSLGNSGEIKN--KPYLPLLQYIDCFKKasgfDIIHN 93
Cdd:cd04951 10 GLGGAEKQTVLLADQMFIRGHDVNiVYLTGEVEVKPLNNNIIIYNLGMDKNPRSllKALLKLKKIISAFKP----DVVHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 94 HAEHmAMFFADLV-----TTPVVHTLHSTLVEGETleekRKVLLRFKNhnFVS-ISDN-QREGLKEL--------NFAGT 158
Cdd:cd04951 86 HMFH-ANIFARFLrmlypIPLLICTAHNKNEGGRI----RMFIYRLTD--FLCdITTNvSREALDEFiakkafskNKSVP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 159 VYNGIDIHKYSY----IEKPRGDY--------LLWVGRITRKK---GPLSAIE--VAKKVSIPLVIA---AAIDPVEKLF 218
Cdd:cd04951 159 VYNGIDLNKFKKdinvRLKIRNKLnlkndefvILNVGRLTEAKdypNLLLAISelILSKNDFKLLIAgdgPLRNELERLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 219 FEEEVKpqidgKTVSFVGELhgESLNKLYGNALCTLFPITWhEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGFIV 298
Cdd:cd04951 239 CNLNLV-----DRVILLGQI--SNISEYYNAADLFVLSSEW-EGFGLVVAEAMACERPVVATDAGGVAEVVGDHNYVVPV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1083527485 299 DDLYQMIEAVKNI-------DKIKRKKcRERVVEKFTIEKMVNHYEDIYSK 342
Cdd:cd04951 311 SDPQLLAEKIKEIfdmsdeeRDILGNK-NEYIAKNFSINTIVNEWERLYSG 360
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-337 |
8.24e-14 |
|
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: 71.60 E-value: 8.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 2 KIAILAPPYLPIppngYGGVERIVYYLTEGLVKKGHDVTLFAPG-----DSKVSSQVFS-----TFPFSLGNSGeiKNKP 71
Cdd:cd03794 1 KILLISQYYPPP----KGAAAARVYELAKELVRRGHEVTVLTPSpnyplGRIFAGATETkdgirVIRVKLGPIK--KNGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 72 YLPLLQYID--------CFKKASGFDIIHNHA----EHMAMFFADLVT-TPVVHTLHSTLVEG--ETLEEKRKVLLRFKN 136
Cdd:cd03794 75 IRRLLNYLSfalaallkLLVREERPDVIIAYSppitLGLAALLLKKLRgAPFILDVRDLWPESliALGVLKKGSLLKLLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 137 H----------NFVSISDNQREGLKELNFAG----TVYNGID------IHKYSYIEKPRGD---YLLWVGRITRKKGPLS 193
Cdd:cd03794 155 KlerklyrladAIIVLSPGLKEYLLRKGVPKekiiVIPNWADleefkpPPKDELRKKLGLDdkfVVVYAGNIGKAQGLET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 194 AIEVAKKVS----IPLVIAAAIDPVE--KLFFEEEVKPqidgkTVSFVGELHGESLNKLYGNALCTLFPI-TWHEPFGLV 266
Cdd:cd03794 235 LLEAAERLKrrpdIRFLFVGDGDEKErlKELAKARGLD-----NVTFLGRVPKEEVPELLSAADVGLVPLkDNPANRGSS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 267 ---MVESMACGTPVIAYRIGSTSEVIEDGVTGFIVD-----DLYQMIEAVKNiDKIKRKKC----RERVVEKFTIEKMVN 334
Cdd:cd03794 310 pskLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEpgdpeALADAILELLD-DPELRRAMgengRELAEEKFSREKLAD 388
|
...
gi 1083527485 335 HYE 337
Cdd:cd03794 389 RLL 391
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
19-165 |
9.47e-14 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 68.33 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 19 GGVERIVYYLTEGLVKKGHDVTLFAPGDSKVSSQ------VFSTFPFSLGNSGEIKNKPYLPLLQYIdcfkKASGFDIIH 92
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEevvrvvRVPRVPLPLPPRLLRSLAFLRRLRRLL----RRERPDVVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 93 NHAEHMAMFFADLVT----TPVVHTLHSTLVEGETLEEKRKVLLRFKN----------HNFVSISDNQREGLKELNFAG- 157
Cdd:pfam13439 77 AHSPFPLGLAALAARlrlgIPLVVTYHGLFPDYKRLGARLSPLRRLLRrlerrllrraDRVIAVSEAVADELRRLYGVPp 156
|
170
....*....|..
gi 1083527485 158 ----TVYNGIDI 165
Cdd:pfam13439 157 ekirVIPNGVDL 168
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
131-339 |
2.18e-13 |
|
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: 70.17 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 131 LLRFKNHNFVSISDNQREGLKELNF-AGTV---YNGIDIHKYSYIEK-PRGDYLLWVGRITRKKGPLSAIEV-----AKK 200
Cdd:cd05844 139 ALQRPAALFVAVSGFIRDRLLARGLpAERIhvhYIGIDPAKFAPRDPaERAPTILFVGRLVEKKGCDVLIEAfrrlaARH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 201 VSIPLVIAAaiDPVEKLFFEEEVKPqidGKTVSFVGEL-HGESLNKLYGNALCTLFPITW----HEPFGLVMVESMACGT 275
Cdd:cd05844 219 PTARLVIAG--DGPLRPALQALAAA---LGRVRFLGALpHAEVQDWMRRAEIFCLPSVTAasgdSEGLGIVLLEAAACGV 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083527485 276 PVIAYRIGSTSEVIEDGVTGFIV-----DDLYQMIEAVKNIDKIKRK---KCRERVVEKFTIEKMVNHYEDI 339
Cdd:cd05844 294 PVVSSRHGGIPEAILDGETGFLVpegdvDALADALQALLADRALADRmggAARAFVCEQFDIRVQTAKLEAI 365
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
261-344 |
2.23e-12 |
|
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: 67.44 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 261 EPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGFIV--DDLYQMIEA----VKNIDKIKRKKC--RERVVEKFTIEKM 332
Cdd:TIGR03088 283 EGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVppGDAVALARAlqpyVSDPAARRAHGAagRARAEQQFSINAM 362
|
90
....*....|..
gi 1083527485 333 VNHYEDIYSKLI 344
Cdd:TIGR03088 363 VAAYAGLYDQLL 374
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
63-343 |
8.07e-12 |
|
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: 65.39 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 63 NSGEIKNKPYLPLLQYIDCFKKASGFDIIHNHAEHMAMFFADL-----VTTPVVHTlHSTLVEGETLEEKRKVLLRFKNH 137
Cdd:cd03812 56 FYIPPKKKNIIKYFIKLLKLIKKEKYDIVHVHGSSSNGIILLLaakagVPVRIAHS-HNTKDSSIKLRKIRKNVLKKLIE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 138 ----NFVSISDNQREGLKELNFAG---TVYNGIDIHKYSYIEKPRGDYLLW-----------VGRITRKKGPLSAIEVAK 199
Cdd:cd03812 135 rlstKYLACSEDAGEWLFGEVENGkfkVIPNGIDIEKYKFNKEKRRKRRKLliledklvlghVGRFNEQKNHSFLIDIFE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 200 KV-----SIPLVIAAAIDPVEKLffEEEVKPQIDGKTVSFVGELhgESLNKLYGNALCTLFPITWhEPFGLVMVESMACG 274
Cdd:cd03812 215 ELkkknpNVKLVLVGEGELKEKI--KEKVKELGLEDKVIFLGFR--NDVSEILSAMDVFLFPSLY-EGLPLVAVEAQASG 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 275 TPVIAYRIGSTSEVIEDGVTGFIVDDLYQM-IEAVKNIDKIKRKKCRERVVEKFtiEKMVNHYEDIYSKL 343
Cdd:cd03812 290 LPCLLSDTITKECDITNNVEFLPLNETPSTwAEKILKLIKRKRRINKEINKEKK--ELGYDDESLELTLL 357
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
246-332 |
5.59e-11 |
|
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: 62.99 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 246 LYGNALCTLF-PItwHEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGFIVD-----DLYQMIEAVKNIDKIKR--K 317
Cdd:cd03805 296 LLSSALALLYtPS--NEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEptpeaFAEAMLKLANDPDLADRmgA 373
|
90
....*....|....*
gi 1083527485 318 KCRERVVEKFTIEKM 332
Cdd:cd03805 374 AGRKRVKEKFSREAF 388
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
219-327 |
1.24e-08 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 56.26 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 219 FEEEVKPQIDGKTVSFVGELHGESLNKLYGNALCTLFPiTWHEPFGLVMVESMACGTPVIAYRIGSTSEVI---EDGVTG 295
Cdd:PLN02871 301 YREELEKMFAGTPTVFTGMLQGDELSQAYASGDVFVMP-SESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTG 379
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1083527485 296 FI-----VDDLYQMIEAVKNIDKIK---RKKCRERvVEKF 327
Cdd:PLN02871 380 FLytpgdVDDCVEKLETLLADPELRermGAAAREE-VEKW 418
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
170-329 |
1.25e-08 |
|
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: 55.79 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 170 YIEKPrgdYLLWVGRITRKKGPLSAIEVAKKV----SIP-LVIA---AAIDPVEKLFFEEEVKPQIDGKTVSFVGELHGE 241
Cdd:cd03792 194 DPERP---YILQVARFDPSKDPLGVIDAYKLFkrraEEPqLVICghgAVDDPEGSVVYEEVMEYAGDDHDIHVLRLPPSD 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 242 SL-NKLYGNALCTLFPITwHEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGFIVDD-------LYQMIEAVKNIDK 313
Cdd:cd03792 271 QEiNALQRAATVVLQLST-REGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSvegaavrILRLLTDPELRRK 349
|
170
....*....|....*.
gi 1083527485 314 IkRKKCRERVVEKFTI 329
Cdd:cd03792 350 M-GLAAREHVRDNFLI 364
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
179-337 |
2.14e-07 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 52.10 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 179 LLWVGRITRKKGPLSAIEVAKKV-----SIPLVIAAaiDPV-----EKLFFEEEVKPQID--GKTVSFVGELHGESLNKL 246
Cdd:PRK15484 196 LLYAGRISPDKGILLLMQAFEKLatahsNLKLVVVG--DPTasskgEKAAYQKKVLEAAKriGDRCIMLGGQPPEKMHNY 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 247 YGNALCTLFPITWHEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGF----------IVDDLYQMIeAVKNIDKIKr 316
Cdd:PRK15484 274 YPLADLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYhlaepmtsdsIISDINRTL-ADPELTQIA- 351
|
170 180
....*....|....*....|.
gi 1083527485 317 KKCRERVVEKFTIEKMVNHYE 337
Cdd:PRK15484 352 EQAKDFVFSKYSWEGVTQRFE 372
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
31-332 |
8.33e-07 |
|
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: 50.14 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 31 GLVKKGHDVTLFA--PGDSKVSSQVFSTFpfslgnsgeikNKPYLPLLQYIDCFKKASGFDIIHNH----------AEHM 98
Cdd:cd03799 23 GLIDRGHEVDIYAvnPGDLVKRHPDVEKY-----------NVPSLNLLYAIVGLNKKGAYDIIHCQfgplgalgalLRRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 99 AMFFADLVTTpvvhtLHSTLVEGETLEEKRKVLLRF--KNHNFVSISDNQREGL-------KELNFAGTvynGIDIHKYS 169
Cdd:cd03799 92 KVLKGKLVTS-----FRGYDISMYVILEGNKVYPQLfaQGDLFLPNCELFKHRLialgcdeKKIIVHRS---GIDCNKFR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 170 YieKPRGD------YLLWVGRITRKKGPLSAIEVAKKV-----SIPLVIAAAIDpveklfFEEEVKPQID----GKTVSF 234
Cdd:cd03799 164 F--KPRYLpldgkiRILTVGRLTEKKGLEYAIEAVAKLaqkypNIEYQIIGDGD------LKEQLQQLIQelniGDCVKL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 235 VGELHGESLNKLYGNALCTLFP-ITW----HEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGFIVDDLYQMIEAVK 309
Cdd:cd03799 236 LGWKPQEEIIEILDEADIFIAPsVTAadgdQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEK 315
|
330 340 350
....*....|....*....|....*....|.
gi 1083527485 310 NIDKIKR--------KKCRERVVEKFTIEKM 332
Cdd:cd03799 316 LTYLIEHpaiwpemgKAGRARVEEEYDINKL 346
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
28-294 |
2.90e-06 |
|
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274943 [Multi-domain] Cd Length: 373 Bit Score: 48.55 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 28 LTEGLVKKGHDVTLFAPGDS--------KVSSQVFstfPFSlGNSGEIKNKPYLPLLQYIDCFKK--ASGFDIIHNH--- 94
Cdd:TIGR04047 21 LAEALTALGHDVTVWALAADgfgffrdpPCAVRLV---PVA-PAPGDTDAMVEQRIARSIDHLRAhfARGFDVVHAQdci 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 95 -AEHMAMFFADLVTTPVVHTLHS----TLVEGETLEEKRKVLLRfknhNFVSISDNQREGLKElNF---AGTVYNGIDIH 166
Cdd:TIGR04047 97 sGNALATLRAEGLIPGFVRTVHHlddfDDPRLAACQERAIVEAD----AVLCVSAAWAAELRA-EWgidATVVPNGVDAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 167 KYSYIEKPR------------GDYLLWVGRITRKKGPLSAIE-----VAKKVSIPLVIAAAI-----DPVEKLFFEEEVK 224
Cdd:TIGR04047 172 RFSPAADAAdaalrrrlglrgGPYVLAVGGIEPRKNTIDLLEafallRARRPQAQLVIAGGAtlfdyDAYRREFRARAAE 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083527485 225 PQIDGKTVSFVGELHGESLNKLYGNALCTLFPITwHEPFGLVMVESMACGTPVIAYRIGS-TSEVIEDGVT 294
Cdd:TIGR04047 252 LGVDPGPVVITGPVPDADLPALYRCADAFAFPSL-KEGFGLVVLEALASGIPVVASDIAPfTEYLGRFDAA 321
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
260-299 |
2.91e-06 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 49.21 E-value: 2.91e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1083527485 260 HEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVTGFIVD 299
Cdd:PLN00142 676 YEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHID 715
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
261-340 |
4.45e-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: 48.33 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 261 EPFGLVMVESMACGTPVIAYRIGSTSEVIEDGV------TGFIVD--DLYQMIEAVKN-IDKIKRKKCRERVVEK----- 326
Cdd:cd03791 379 EPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYDpetgegTGFVFEdyDAEALLAALRRaLALYRNPELWRKLQKNamkqd 458
|
90
....*....|....
gi 1083527485 327 FTIEKMVNHYEDIY 340
Cdd:cd03791 459 FSWDKSAKEYLELY 472
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
19-122 |
2.37e-05 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 43.93 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 19 GGVERIVYYLTEGLVKKGHDVTLFAPGDSKVSSQV----FSTFPFSLGNSGEIKNKPYLP--LLQYIdcfkKASGFDIIH 92
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELvgdgVRVHRLPVPPRPSPLADLAALrrLRRLL----RAERPDVVH 76
|
90 100 110
....*....|....*....|....*....|...
gi 1083527485 93 NHAEH---MAMFFADLVTTPVVHTLHSTLVEGE 122
Cdd:pfam13579 77 AHSPTaglAARLARRRRGVPLVVTVHGLALDYG 109
|
|
| GT4-like |
cd04955 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
176-340 |
2.89e-05 |
|
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: 45.57 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 176 GDYLLWVGRITRKKGPLSAIE--VAKKVSIPLVIaaaIDPVEKLFFEEEV--KPQID-GKTVSFVGELH-GESLNKLYGN 249
Cdd:cd04955 208 GKYYLIVGRFVPENNYETMIRefMKSSTKRDLVI---ITNVEGNAYYELLlkKTAFDhDERIKFVGTVYdQELLKYIREN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 250 ALCTLFPitwHEPFGL--VMVESMACGTPVIAYRIGSTSEVIEDGVTGFIVDDLYQMIEAVKNIDKIK----RKKCRERV 323
Cdd:cd04955 285 AFAYLHG---HEVGGTnpSLLEALGSTDLNLLLDVGFNREVAEDAALYWKKEPLASLIDEVDNLNPDEisdlGKKAKQRI 361
|
170
....*....|....*..
gi 1083527485 324 VEKFTIEKMVNHYEDIY 340
Cdd:cd04955 362 EEAYTWEKIVDEYEELF 378
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
216-299 |
3.75e-05 |
|
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: 45.05 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 216 KLFFEEEVkpQIDGKTVSFVGELHGESLNKLYGNALCTLFPItwhEPFGLV--MVESMACGTPVIAYRIGSTSEVIEDGV 293
Cdd:cd03818 269 KQKMLAEL--GVDLERVHFVGKVPYDQYVRLLQLSDAHVYLT---YPFVLSwsLLEAMACGCPVIGSDTAPVREVIRDGR 343
|
....*.
gi 1083527485 294 TGFIVD 299
Cdd:cd03818 344 NGLLVD 349
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
220-335 |
1.76e-04 |
|
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: 43.22 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 220 EEEVKPQIDGK----TVSFVGELHGESLNKLYGNALCTLF-PITWHEPFGLVMVESMACGTPVIAYRIGSTSEVIEDGVT 294
Cdd:cd04946 269 KERLEKLAENKlenvKVNFTGEVSNKEVKQLYKENDVDVFvNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETN 348
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1083527485 295 GFIVDD---LYQMIEAVKNID------KIKRKKCRERVVEKFTIEkmVNH 335
Cdd:cd04946 349 GLLLDKdptPNEIVSSIMKFYldggdyKTMKISARECWEERFNAE--VNY 396
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
261-331 |
1.97e-04 |
|
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: 42.67 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 261 EPFGLVMVESMACGTPVIAYRI--GStSEVIEDGVTGF-----IVDDLYQ-MIEAVKNIDKIKR--KKCRErVVEKFTIE 330
Cdd:cd04949 245 EGFGLTLMEAIGHGLPVVSYDVkyGP-SELIEDGENGYlieknNIDALADkIIELLNDPEKLQQfsEESYK-IAEKYSTE 322
|
.
gi 1083527485 331 K 331
Cdd:cd04949 323 N 323
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
259-331 |
5.86e-04 |
|
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.
Pssm-ID: 340835 [Multi-domain] Cd Length: 419 Bit Score: 41.44 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 259 WHEPFGLVMVESMACGTPVIAYRIGSTSEVI----EDGVTGFIVDDL----YQMIEAVK--NIDKIKRKKCRERVVEKFT 328
Cdd:cd03806 333 WNEHFGIGVVEYMAAGLIPLAHASAGPLLDIvvpwDGGPTGFLASTPeeyaEAIEKILTlsEEERLQRREAARSSAERFS 412
|
...
gi 1083527485 329 IEK 331
Cdd:cd03806 413 DEE 415
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
266-336 |
7.57e-04 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 41.22 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527485 266 VMVESMACGTPVIAYRIGSTSEVIEDGVTGFIVDDLYQM--------IEAVKNIDKIKRKKCRER---VVEKFTIEKMVN 334
Cdd:PRK15490 488 VLIEAQMVGVPVISTPAGGSAECFIEGVSGFILDDAQTVnldqacryAEKLVNLWRSRTGICQQTqsfLQERFTVEHMVG 567
|
..
gi 1083527485 335 HY 336
Cdd:PRK15490 568 TF 569
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
269-328 |
3.99e-03 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 36.04 E-value: 3.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083527485 269 ESMACGTPVIAYRIGSTSEVIEDGVTGFIVDDLYQMIEAVKN-------IDKIkRKKCRERVVEKFT 328
Cdd:pfam13524 18 EAAACGAPLLTDRTPGLEELFEPGEEILLYRDPEELAEKIRYllehpeeRRAI-AAAGRERVLAEHT 83
|
|
| |
