|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
16-364 |
6.86e-142 |
|
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: 407.05 E-value: 6.86e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 16 RILHCYRTFYPEsKGGLEQVVLELAQNT----HGSGVLTLAKEPGQR-MLDGKLPVLAERRWVSVASCCIGPGLVRRLFR 90
Cdd:cd03795 1 KVLHVFKFYYPD-IGGIEQVIYDLAEGLkkkgIEVDVLCFSKEKETPeKEENGIRIHRVKSFLNVASTPFSPSYIKRFKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 91 LKAK--LLHFHFPWPFGDVTYLLAGRSRPLIITYHSDIVRQRALSLLYYPLMKIFLSRADRIVATSQNYMDSSPVLADFR 168
Cdd:cd03795 80 LAKEydIIHYHFPNPLADLLLFFSGAKKPVVVHWHSDIVKQKKLLKLYKPLMTRFLRRADRIIATSPNYVETSPTLREFK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 169 SKVEVIPLGISEQEYPVPADNDLLNMEARFGKDFMLFVGVLRYYKGLEYLIRASVGRPYRVVIAGKGPEQAKLKVLADEL 248
Cdd:cd03795 160 NKVRVIPLGIDKNVYNIPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLIEAAQYLNYPIVIGGEGPLKPDLEAQIELN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 249 GADSIVFTGYISDLEKAALMKLCRAVVFPSHLRSEAFGVTLIEGLMYGKPLISCEIGTGTSYVNADGETGHVILPANPDA 328
Cdd:cd03795 240 LLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNNGETGLVVPPKDPDA 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 1997015909 329 LREAMDDLWNDPVKAEQMGQAGRLRYESLFTGERMA 364
Cdd:cd03795 320 LAEAIDKLLSDEELRESYGENAKKRFEELFTAEKMK 355
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
16-371 |
3.18e-49 |
|
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: 170.03 E-value: 3.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 16 RILHCyRTFYPESKGGLEQVVLELAQNTHGSG----VLTLAKEPGQRmldgkLPVLAERRWVSVASCCIGPGLVRRLFRL 91
Cdd:cd03801 1 KILLL-SPELPPPVGGAERHVRELARALAARGhdvtVLTPADPGEPP-----EELEDGVIVPLLPSLAALLRARRLLREL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 92 KAK-------LLHFHFPWPFGDVTYLLAGRSRPLIITYHS-DIVRQRALSLLYYPLMK---IFLSRADRIVATSQNYMDS 160
Cdd:cd03801 75 RPLlrlrkfdVVHAHGLLAALLAALLALLLGAPLVVTLHGaEPGRLLLLLAAERRLLAraeALLRRADAVIAVSEALRDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 161 spVLADF---RSKVEVIPLGISEQEYPVPADNDLLNMEARFgkdFMLFVGVLRYYKGLEYLIRA-----SVGRPYRVVIA 232
Cdd:cd03801 155 --LRALGgipPEKIVVIPNGVDLERFSPPLRRKLGIPPDRP---VLLFVGRLSPRKGVDLLLEAlakllRRGPDVRLVIV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 233 GK-GPEQAKLKVLADELGaDSIVFTGYISDLEKAALMKLCRAVVFPShlRSEAFGVTLIEGLMYGKPLISCEIGTGTSYV 311
Cdd:cd03801 230 GGdGPLRAELEELELGLG-DRVRFLGFVPDEELPALYAAADVFVLPS--RYEGFGLVVLEAMAAGLPVVATDVGGLPEVV 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 312 nADGETGHVILPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLFTGERMAAAYQKLY 371
Cdd:cd03801 307 -EDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
199-353 |
2.59e-36 |
|
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: 129.70 E-value: 2.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 199 GKDFMLFVGVLRYYKGLEYLIRA-----SVGRPYRVVIAGKGPEQAKLKVLADELGA-DSIVFTGYISDLEKAALMKLCR 272
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAfallkEKNPNLKLVIAGDGEEEKRLKKLAEKLGLgDNVIFLGFVSDEDLPELLKIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 273 AVVFPSHlrSEAFGVTLIEGLMYGKPLISCEIGtGTSYVNADGETGHVILPANPDALREAMDDLWNDPVKAEQMGQAGRL 352
Cdd:pfam00534 81 VFVLPSR--YEGFGIVLLEAMACGLPVIASDVG-GPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157
|
.
gi 1997015909 353 R 353
Cdd:pfam00534 158 R 158
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
83-369 |
2.44e-32 |
|
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: 124.78 E-value: 2.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 83 GLVRRLFRLKAKLLHFHFPwpfgdvTYLLAGRSRPLIITYHSDIVRQ------RALSLLYYPLMKIFLSRADRIVaTSQN 156
Cdd:cd03809 75 LQILLPKKDKPDLLHSPHN------TAPLLLKGCPQVVTIHDLIPLRypeffpKRFRLYYRLLLPISLRRADAII-TVSE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 157 YM--DSSPVLADFRSKVEVIPLGISEQEYPVPADNDLLNMEARfGKDFMLFVGVLRYYKGLEYLIRA-----SVGRPYRV 229
Cdd:cd03809 148 ATrdDIIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLL-PEPYFLYVGTLEPRKNHERLLKAfallkKQGGDLKL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 230 VIAG-KGPEQAKLKVLADELG-ADSIVFTGYISDLEKAALMKLCRAVVFPSHlrSEAFGVTLIEGLMYGKPLIsceIGTG 307
Cdd:cd03809 227 VIVGgKGWEDEELLDLVKKLGlGGRVRFLGYVSDEDLPALYRGARAFVFPSL--YEGFGLPVLEAMACGTPVI---ASNI 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997015909 308 TSYVNADGETGHVILPANPDALREAMDDLWNDPVKAEQMGQAGRLRyESLFTGERMAAAYQK 369
Cdd:cd03809 302 SVLPEVAGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLER-AKKFSWEKTAEKTLE 362
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
84-370 |
7.58e-32 |
|
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: 123.64 E-value: 7.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 84 LVRRLFRLKAKLLHFHFPWPFGDVTYLLAGRSR-PLIITYH-SDIVRQRALSLLYyPLMKIFLSRADRIVATSQNYMDSS 161
Cdd:cd03798 87 LLKRRRRGPPDLIHAHFAYPAGFAAALLARLYGvPYVVTEHgSDINVFPPRSLLR-KLLRWALRRAARVIAVSKALAEEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 162 PVLADFRSKVEVIPLGISEqEYPVPADNDLlnmEARFGKDFMLFVGVLRYYKGLEYLIRA-----SVGRPYRVVIAGKGP 236
Cdd:cd03798 166 VALGVPRDRVDVIPNGVDP-ARFQPEDRGL---GLPLDAFVILFVGRLIPRKGIDLLLEAfarlaKARPDVVLLIVGDGP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 237 EQAKLKVLADELG-ADSIVFTGYISDLEKAALMKLCRAVVFPShlRSEAFGVTLIEGLMYGKPLISCEIGtGTSYVNADG 315
Cdd:cd03798 242 LREALRALAEDLGlGDRVTFTGRLPHEQVPAYYRACDVFVLPS--RHEGFGLVLLEAMACGLPVVATDVG-GIPEVVGDP 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1997015909 316 ETGHVILPANPDALREAMDDLWNDPVKaEQMGQAGRLRYESLFT----GERMAAAYQKL 370
Cdd:cd03798 319 ETGLLVPPGDADALAAALRRALAEPYL-RELGEAARARVAERFSwvkaADRIAAAYRDV 376
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
16-346 |
1.92e-31 |
|
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: 122.08 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 16 RILHCYRTFypeSKGGLEQVVLELAQNTHGSG---VLTLAKEPGQRMLDGKLPVLAERRWVSVASCcIGPGLVRRLFRLK 92
Cdd:cd03811 1 KILFVIPSL---SGGGAERVLLNLANALDKRGydvTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKL-IKLGLLKAILKLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 93 AKL--------LHFHFPWPFgdVTYLLAGRSRPLIITYHSDIVRQRALSLLYYpLMKIFLSRADRIVATSQNYMDS-SPV 163
Cdd:cd03811 77 RILkrakpdvvISFLGFATY--IVAKLAAARSKVIAWIHSSLSKLYYLKKKLL-LKLKLYKKADKIVCVSKGIKEDlIRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 164 LADFRSKVEVIPLGISEQEYPVPADNDLLNMeaRFGKDFMLFVGVLRYYKGLEYLIRAsVGR------PYRVVIAGKGPE 237
Cdd:cd03811 154 GPSPPEKIEVIYNPIDIDRIRALAKEPILNE--PEDGPVILAVGRLDPQKGHDLLIEA-FAKlrkkypDVKLVILGDGPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 238 QAKLKVLADELG-ADSIVFTGYISDLekAALMKLCRAVVFPShlRSEAFGVTLIEGLMYGKPLISCEIGtGTSYVNADGE 316
Cdd:cd03811 231 REELEKLAKELGlAERVIFLGFQSNP--YPYLKKADLFVLSS--RYEGFPNVLLEAMALGTPVVSTDCP-GPREILDDGE 305
|
330 340 350
....*....|....*....|....*....|
gi 1997015909 317 TGHVILPANPDALREAMDDLWNDPVKAEQM 346
Cdd:cd03811 306 NGLLVPDGDAAALAGILAALLQKKLDAALR 335
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
95-367 |
2.00e-28 |
|
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: 114.64 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 95 LLHFHFpWPFGDVTYLLAGRSR-PLIITYHSDIVRQRALSLLYYPLM--------KIFLSRADRIVATSQNYMDSSPVLA 165
Cdd:cd03800 104 LIHSHY-WDSGLVGALLARRLGvPLVHTFHSLGRVKYRHLGAQDTYHpslritaeEQILEAADRVIASTPQEADELISLY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 166 D-FRSKVEVIPLGISEQEY-PVPADNDLLnmeARFGKDF----MLFVGVLRYYKGLEYLIRA-----SVGRPYRVVIAG- 233
Cdd:cd03800 183 GaDPSRINVVPPGVDLERFfPVDRAEARR---ARLLLPPdkpvVLALGRLDPRKGIDTLVRAfaqlpELRELANLVLVGg 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 234 -KGPEQAK----LKVLADELG-ADSIVFTGYISDLEKAALMKLCRAVVFPSHlrSEAFGVTLIEGLMYGKPLISCEIGtG 307
Cdd:cd03800 260 pSDDPLSMdreeLAELAEELGlIDRVRFPGRVSRDDLPELYRAADVFVVPSL--YEPFGLTAIEAMACGTPVVATAVG-G 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 308 TSYVNADGETGHVILPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLFTGERMAAAY 367
Cdd:cd03800 337 LQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQL 396
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
15-353 |
6.89e-28 |
|
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: 112.06 E-value: 6.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 15 LRILHCYRTfypeskGGLEQVVLELAQNTHGSG----VLTLA--KEPGQRMLDGKLPVLaERRWVSVasccigPGLVRRL 88
Cdd:cd03819 2 LMLTPALEI------GGAETYILDLARALAERGhrvlVVTAGgpLLPRLRQIGIGLPGL-KVPLLRA------LLGNVRL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 89 FRLKAK----LLHFH---FPWpfgdVTYLLAGRSR-PLIITYHSDivrqRALSLLYYPLMKIFLSRADRIVATS----QN 156
Cdd:cd03819 69 ARLIRReridLIHAHsraPAW----LGWLASRLTGvPLVTTVHGS----YLATYHPKDFALAVRARGDRVIAVSelvrDH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 157 YMDSSPVLADfrsKVEVIPLGISEQEY-PVPADNDLLNMEARFGKDFMLFVGVLRYYKGLEYLIRASV----GRPYRVVI 231
Cdd:cd03819 141 LIEALGVDPE---RIRVIPNGVDTDRFpPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAelkdEPDFRLLV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 232 AGKGPEQAKLKVLADELG-ADSIVFTGYISDLekAALMKLCRAVVFPShlRSEAFGVTLIEGLMYGKPLISCEIGTGTSY 310
Cdd:cd03819 218 AGDGPERDEIRRLVERLGlRDRVTFTGFREDV--PAALAASDVVVLPS--LHEEFGRVALEAMACGTPVVATDVGGAREI 293
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1997015909 311 VNAdGETGHVILPANPDALREAMDDLWNDPVKAEQMGQAGRLR 353
Cdd:cd03819 294 VVH-GRTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAALT 335
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
85-367 |
4.00e-27 |
|
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: 110.38 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 85 VRRLFR-LKAKLLHFHFPWPfgdVTY-LLAGR--SRPLIIT----YHSDIVRQRALSLLYYPLMKIFLSRADRIVATSQN 156
Cdd:cd03808 73 LYKLLKkEKPDIVHCHTPKP---GILgRLAARlaGVPKVIYtvhgLGFVFTEGKLLRLLYLLLEKLALLFTDKVIFVNED 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 157 YMDSSPVL--ADFRSKVEVIPLGISEQEYPvPADNDLLNMEARFgkdfmLFVGVLRYYKGLEYLIRA-----SVGRPYRV 229
Cdd:cd03808 150 DRDLAIKKgiIKKKKTVLIPGSGVDLDRFQ-YSPESLPSEKVVF-----LFVARLLKDKGIDELIEAakilkKKGPNVRF 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 230 VIAGKGPEQAKLKVLADELGADSIV-FTGYISDLekAALMKLCRAVVFPSHlrSEAFGVTLIEGLMYGKPLISCEIGtGT 308
Cdd:cd03808 224 LLVGDGELENPSEILIEKLGLEGRIeFLGFRSDV--PELLAESDVFVLPSY--REGLPRSLLEAMAAGRPVITTDVP-GC 298
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1997015909 309 SYVNADGETGHVILPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLFTGERMAAAY 367
Cdd:cd03808 299 RELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKL 357
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
28-372 |
6.76e-27 |
|
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: 109.71 E-value: 6.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 28 SKGGLEQVVLELAQNTHGSG----VLTLakepgqrMLDGKLPVLAERRWVSVAscCIG------PGLVRRLFRL----KA 93
Cdd:cd03807 10 NVGGAETMLLRLLEHMDKSRfehvVISL-------TGDGVLGEELLAAGVPVV--CLGlssgkdPGVLLRLAKLirkrNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 94 KLLHFHFPWP--FGDVTYLLAGrSRPLIITYHSDIVRQRALSLLYypLMKIFLSRADR-IVATSQnymDSSPVLADF--- 167
Cdd:cd03807 81 DVVHTWMYHAdlIGGLAAKLAG-GVKVIWSVRSSNIPQRLTRLVR--KLCLLLSKFSPaTVANSS---AVAEFHQEQgya 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 168 RSKVEVIPLGISEQEY-PVPADNDLLNMEARFGKDFMLFVGVLRYY--KGLEYLIRA-----SVGRPYRVVIAGKGPEQA 239
Cdd:cd03807 155 KNKIVVIYNGIDLFKLsPDDASRARARRRLGLAEDRRVIGIVGRLHpvKDHSDLLRAaallvETHPDLRLLLVGRGPERP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 240 KLKVLADELG-ADSIVFTGYISDLekAALMKlcRAVVFPSHLRSEAFGVTLIEGLMYGKPLISCEIGtGTSYVnADGETG 318
Cdd:cd03807 235 NLERLLLELGlEDRVHLLGERSDV--PALLP--AMDIFVLSSRTEGFPNALLEAMACGLPVVATDVG-GAAEL-VDDGTG 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1997015909 319 HVILPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLFTGERMAAAYQKLYT 372
Cdd:cd03807 309 FLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
266-376 |
5.27e-25 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 98.52 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 266 ALMKLCRAVVFPShlRSEAFGVTLIEGLMYGKPLISCEIGtGTSYVNADGETGHVILPANPDALREAMDDLWNDPVKAEQ 345
Cdd:COG0438 16 ALLAAADVFVLPS--RSEGFGLVLLEAMAAGLPVIATDVG-GLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRR 92
|
90 100 110
....*....|....*....|....*....|.
gi 1997015909 346 MGQAGRLRYESLFTGERMAAAYQKLYTQVLE 376
Cdd:COG0438 93 LGEAARERAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
16-368 |
8.97e-25 |
|
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: 103.99 E-value: 8.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 16 RILHCYRTFYPEsKGGLEQVVLELAQNTHGSG----VLTLA--KEPGQRMLDGKL-----------PVLAERRWVSVasc 78
Cdd:cd03821 1 KILHVTPSISPK-AGGPVKVVLRLAAALAALGhevtIVSTGdgYESLVVEENGRYippqdgfasipLLRQGAGRTDF--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 79 CIGPGLVRRLFRLKAKLLHFHFPW--PFGDVTYLLAGRSRPLIITYHSDIV-----RQRALSLLYYPL-MKIFLSRADRI 150
Cdd:cd03821 77 SPGLPNWLRRNLREYDVVHIHGVWtyTSLAACKLARRRGIPYVVSPHGMLDpwalqQKHWKKRIALHLiERRNLNNAALV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 151 VATSQNYMDSSPVLAdFRSKVEVIPLGISEQEYPvPADNDLLNMEARFGKDFMLFVGVLRYYKGLEYLIRASV-----GR 225
Cdd:cd03821 157 HFTSEQEADELRRFG-LEPPIAVIPNGVDIPEFD-PGLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARklaeqGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 226 PYRVVIAGKGP--EQAKLKVLADELGADSIVFTGYISDLEKAALMKLCRAVVFPSHlrSEAFGVTLIEGLMYGKP-LISC 302
Cdd:cd03821 235 DWHLVIAGPDDgaYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSY--SENFGNVVAEALACGLPvVITD 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1997015909 303 EIGtGTSYVNADGetGHVILPaNPDALREA---MDDLWNDPVKAEQMGQAGRLrYESLFTGERMAAAYQ 368
Cdd:cd03821 313 KCG-LSELVEAGC--GVVVDP-NVSSLAEAlaeALRDPADRKRLGEMARRARQ-VEENFSWEAVAGQLG 376
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
80-374 |
1.00e-23 |
|
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: 100.82 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 80 IGPGLVRRLFRLKAKLLHFHFPWPFGDVTYLLAGRSR-PLIITYH---SDI---VRQRALSLLYY--PLMKIFLSRADRI 150
Cdd:cd03817 72 FKKAVIDRIKELGPDIIHTHTPFSLGKLGLRIARKLKiPIVHTYHtmyEDYlhyIPKGKLLVKAVvrKLVRRFYNHTDAV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 151 VATS-------QNYMDSSPVladfrskvEVIPLGISEQEYPVPADNDLLNmEARFGKDFM--LFVGVLRYYKGLEYLIRA 221
Cdd:cd03817 152 IAPSekikdtlREYGVKGPI--------EVIPNGIDLDKFEKPLNTEERR-KLGLPPDEPilLYVGRLAKEKNIDFLLRA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 222 SVG----RPYRVVIAGKGPEQAKLKVLADELG-ADSIVFTGYISDLEKAALMKLCRAVVFPSHlrSEAFGVTLIEGLMYG 296
Cdd:cd03817 223 FAElkkePNIKLVIVGDGPEREELKELARELGlADKVIFTGFVPREELPEYYKAADLFVFAST--TETQGLVYLEAMAAG 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1997015909 297 KPLIsCEIGTGTSYVNADGETGHVIlPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLftgeRMAAAYQKLYTQV 374
Cdd:cd03817 301 LPVV-AAKDPAASELVEDGENGFLF-EPNDETLAEKLLHLRENLELLRKLSKNAEISAREF----AFAKSVEKLYEEV 372
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
111-355 |
1.36e-23 |
|
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: 100.39 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 111 LAGRSRPLIITYHS------DIVRQRALSLLYYPlmkiflsRADRIVATSQNYMDSSPVLadFRSKVEVIPLGISEqeyp 184
Cdd:cd03820 104 LIGLKSKLIVWEHNnyeaynKGLRRLLLRRLLYK-------RADKIVVLTEADKLKKYKQ--PNSNVVVIPNPLSF---- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 185 vPADNDLLNMEA-RFgkdfmLFVGVLRYYKGLEYLIRASVGRP-----YRVVIAGKGPEQAKLKVLADELG-ADSIVFTG 257
Cdd:cd03820 171 -PSEEPSTNLKSkRI-----LAVGRLTYQKGFDLLIEAWALIAkkhpdWKLRIYGDGPEREELEKLIDKLGlEDRVKLLG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 258 YISDLEKaalmKLCRA--VVFPShlRSEAFGVTLIEGLMYGKPLISCEIGTGTSYVNADGETGHVILPANPDALREAMDD 335
Cdd:cd03820 245 PTKNIAE----EYANSsiFVLSS--RYEGFPMVLLEAMAYGLPIISFDCPTGPSEIIEDGENGLLVPNGDVDALAEALLR 318
|
250 260
....*....|....*....|
gi 1997015909 336 LWNDPVKAEQMGQAGRLRYE 355
Cdd:cd03820 319 LMEDEELRKKMGKNARKNAE 338
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
204-339 |
2.11e-23 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 94.50 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 204 LFVGVL-RYYKGLEYLIRA-----SVGRPYRVVIAGKGPEQaKLKVLADELgADSIVFTGYISDLekAALMKLCRAVVFP 277
Cdd:pfam13692 5 LFVGRLhPNVKGVDYLLEAvpllrKRDNDVRLVIVGDGPEE-ELEELAAGL-EDRVIFTGFVEDL--AELLAAADVFVLP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997015909 278 ShlRSEAFGVTLIEGLMYGKPLISCEIGtGTSYVnADGETGHVILPANPDALREAMDDLWND 339
Cdd:pfam13692 81 S--LYEGFGLKLLEAMAAGLPVVATDVG-GIPEL-VDGENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
95-367 |
5.32e-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: 99.34 E-value: 5.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 95 LLHFHFPWPFGDVTYLLAGRSRPLIITYHSDIVRQRALSL----------LYYPLMKIFLSRADRIVATSQNYMDSSPVL 164
Cdd:cd03794 102 IIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLIALgvlkkgsllkLLKKLERKLYRLADAIIVLSPGLKEYLLRK 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 165 ADFRSKVEVIPLGISEQEYPVPADNDLLNMEARfGKDFML-FVGVLRYYKGLEYLIRA----SVGRPYRVVIAGKGPEQA 239
Cdd:cd03794 182 GVPKEKIIVIPNWADLEEFKPPPKDELRKKLGL-DDKFVVvYAGNIGKAQGLETLLEAaerlKRRPDIRFLFVGDGDEKE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 240 KLKVLADELGADSIVFTGYISDLEKAALMKLCRAVVFP---SHLRSEAFGVTLIEGLMYGKPLISCEIGTGTSYVnADGE 316
Cdd:cd03794 261 RLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLVPlkdNPANRGSSPSKLFEYMAAGKPILASDDGGSDLAV-EING 339
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1997015909 317 TGHVILPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLFTGERMAAAY 367
Cdd:cd03794 340 CGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRL 390
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
51-351 |
1.02e-21 |
|
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: 95.21 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 51 LAKEPGQRMLDGKLPVLAERRWVSVASCCIGPGLVRRLFRLKAKLLHFHFPwpFGDVTYL-LAGR-SRPLIITYH-SDIV 127
Cdd:cd05844 40 APFDGVALRALGGSGPLRWLRQMAQRLLGWSAPRLGGAAGLAPALVHAHFG--RDGVYALpLARAlGVPLVVTFHgFDIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 128 RQRALSL------LYYPLMKIFLSR-ADRIVATSQNYMDSSPVLADFRSKVEVIPLGISEQEYpVPADndllnmeARFGK 200
Cdd:cd05844 118 TSRAWLAaspgwpSQFQRHRRALQRpAALFVAVSGFIRDRLLARGLPAERIHVHYIGIDPAKF-APRD-------PAERA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 201 DFMLFVGVLRYYKGLEYLIRA------SVGRPyRVVIAGKGPEQAKLKVLAdeLGADSIVFTGYISDLEKAALMKLCRAV 274
Cdd:cd05844 190 PTILFVGRLVEKKGCDVLIEAfrrlaaRHPTA-RLVIAGDGPLRPALQALA--AALGRVRFLGALPHAEVQDWMRRAEIF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 275 VFPSHL----RSEAFGVTLIEGLMYGKPLISCEIGTGTSYVnADGETGHVILPANPDALREAMDDLWNDPVKAEQMGQAG 350
Cdd:cd05844 267 CLPSVTaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEAI-LDGETGFLVPEGDVDALADALQALLADRALADRMGGAA 345
|
.
gi 1997015909 351 R 351
Cdd:cd05844 346 R 346
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
147-364 |
5.88e-19 |
|
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: 87.64 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 147 ADRIVA----TSQNYMDSSPVLADfrSKVEVI--PLGISEQEypvPADNDLLNMEARFGKDFMLFVGVLRYY--KGLEYL 218
Cdd:cd03805 155 ADQIVVnsnfTAGVFKKTFPSLAK--NPPEVLypCVDTDSFD---STSEDPDPGDLIAKSNKKFFLSINRFErkKNIALA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 219 IRA--------SVGRPYRVVIAG----KGPEQ----AKLKVLADELG--ADSIVFTGYISDLEKAALMKLCRAVVF-PSH 279
Cdd:cd03805 230 IEAfaklkqklPEFENVRLVIAGgydpRVAENveylEELQRLAEELLnvEDQVLFLRSISDSQKEQLLSSALALLYtPSN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 280 lrsEAFGVTLIEGLMYGKPLISCEIGTGTSYVNaDGETGhVILPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLFT 359
Cdd:cd03805 310 ---EHFGIVPLEAMYAGKPVIACNSGGPLETVV-EGVTG-FLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFS 384
|
....*
gi 1997015909 360 GERMA 364
Cdd:cd03805 385 REAFA 389
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
84-374 |
6.33e-19 |
|
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: 87.02 E-value: 6.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 84 LVRRLFRLKAKLLHFHFPWPFGDVTYL---LAGRSRPLIITYH-SDIvrqralSLL-----YYPLMKIFLSRADRIVATS 154
Cdd:cd04962 76 IVEVAKEHKLDVLHAHYAIPHASCAYLareILGEKIPIVTTLHgTDI------TLVgydpsLQPAVRFSINKSDRVTAVS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 155 QNYMDSSPVLADFRSKVEVIPLGISEQEYPvPADNDLLNmEARFGKD---FMLFVGVLRYYKGLEYLIR--ASVGR--PY 227
Cdd:cd04962 150 SSLRQETYELFDVDKDIEVIHNFIDEDVFK-RKPAGALK-RRLLAPPdekVVIHVSNFRPVKRIDDVVRvfARVRRkiPA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 228 RVVIAGKGPEQAKLKVLADELGA-DSIVFTGYISDLEKaaLMKLCRAVVFPSHlrSEAFGVTLIEGLMYGKPLISCEIGt 306
Cdd:cd04962 228 KLLLVGDGPERVPAEELARELGVeDRVLFLGKQDDVEE--LLSIADLFLLPSE--KESFGLAALEAMACGVPVVSSNAG- 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1997015909 307 GTSYVNADGETGHVILPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLFTGERMAAAYQKLYTQV 374
Cdd:cd04962 303 GIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
150-374 |
1.19e-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: 83.54 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 150 IVATSQ---NYMDSSPVLADFrsKVEVIPLGISEQEyPVPADNDLLNMEARFGKDFM--LFV--GVLRYYKGLEYLIRA- 221
Cdd:cd03825 141 IVAPSRwlaDMVRRSPLLKGL--PVVVIPNGIDTEI-FAPVDKAKARKRLGIPQDKKviLFGaeSVTKPRKGFDELIEAl 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 222 ---SVGRPYRVVIAGKGPEQaklkvlaDELGADSIVFTGYISDLEKaaLMKLCRAV---VFPShlRSEAFGVTLIEGLMY 295
Cdd:cd03825 218 kllATKDDLLLVVFGKNDPQ-------IVILPFDIISLGYIDDDEQ--LVDIYSAAdlfVHPS--LADNLPNTLLEAMAC 286
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1997015909 296 GKPLISCEIGtGTSYVNADGETGHVILPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLFTGERMAAAYQKLYTQV 374
Cdd:cd03825 287 GTPVVAFDTG-GSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYKDL 364
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
16-371 |
1.57e-16 |
|
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: 80.07 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 16 RILHCYRTFYPESKGGLEQVVLELAQNTHGSG----VLTLAKEPGQ------------RMLDGKLPVLAERRWVSVA--- 76
Cdd:cd03823 1 KILLVNSLYPPQRVGGAEISVHDLAEALVAEGhevaVLTAGVGPPGqatvarsvvryrRAPDETLPLALKRRGYELFety 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 77 SCCIGPGLVRRLFRLKAKLLHFHFPWPFG-DVTYLLAGRSRPLIITYHSdivrqralsllYYPL-MKIFLSRA--DRIVA 152
Cdd:cd03823 81 NPGLRRLLARLLEDFRPDVVHTHNLSGLGaSLLDAARDLGIPVVHTLHD-----------YWLLcPRQFLFKKggDAVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 153 TSQNYMDSSPVLADFRSKVEVIPLGISEQEYP----VPADNDLlnmeaRFGkdfmlFVGVLRYYKGLEYLIRAsVGR--- 225
Cdd:cd03823 150 PSRFTANLHEANGLFSARISVIPNAVEPDLAPpprrRPGTERL-----RFG-----YIGRLTEEKGIDLLVEA-FKRlpr 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 226 -PYRVVIAGKGPEQAKLKVLADElgadSIVFTGYISDLEKAALMKLCRAVVFPShLRSEAFGVTLIEGLMYGKPLISCEI 304
Cdd:cd03823 219 eDIELVIAGHGPLSDERQIEGGR----RIAFLGRVPTDDIKDFYEKIDVLVVPS-IWPEPFGLVVREAIAAGLPVIASDL 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1997015909 305 GtGTSYVNADGETGHVILPANPDALREAMDDLWNDPVKAEQMgqagRLRYESLFTGERMAAAYQKLY 371
Cdd:cd03823 294 G-GIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERL----RAGAEPPRSTESQAEEYLKLY 355
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
114-371 |
1.01e-15 |
|
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: 78.15 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 114 RSRPLIITYHSDIVRQRALSLL----------------YYPLMKIFLSRADRIVATSQNYMDSSPVLADFRSKVEVIPLG 177
Cdd:cd03813 196 RGIPFLLTEHGIYTRERKIEILqstwimgyikklwirfFERLGKLAYQQADKIISLYEGNRRRQIRLGADPDKTRVIPNG 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 178 ISEQEYPvPAdndllnMEARFGKDFMLFVGVLRY--YKGLEYLIRA-----SVGRPYRVVIAGKGPEQ----AKLKVLAD 246
Cdd:cd03813 276 IDIQRFA-PA------REERPEKEPPVVGLVGRVvpIKDVKTFIRAfklvrRAMPDAEGWLIGPEDEDpeyaQECKRLVA 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 247 ELGADSIV-FTGYISDLEKAALMKLcraVVFPShlRSEAFGVTLIEGLMYGKPLISCEIGTGTSYV----NADGETGHVI 321
Cdd:cd03813 349 SLGLENKVkFLGFQNIKEYYPKLGL---LVLTS--ISEGQPLVILEAMASGVPVVATDVGSCRELIygadDALGQAGLVV 423
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1997015909 322 LPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLFTGERMAAAYQKLY 371
Cdd:cd03813 424 PPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLY 473
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
145-335 |
3.60e-15 |
|
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: 75.78 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 145 SRADRIVATSQNYmdSSPVLADFRSKVEVIplgiseqeYPvPADNDLLNMEARfGKDFMLFVGVLRYYKGLEYLIRASVG 224
Cdd:cd03804 156 QRVDLFIANSQFV--ARRIKKFYGRESTVI--------YP-PVDTDAFAPAAD-KEDYYLTASRLVPYKRIDLAVEAFNE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 225 RPYRVVIAGKGPEQAKLKVLAdelgADSIVFTGYISDLEKAALMKLCRAVVFPShlrSEAFGVTLIEGLMYGKPLISCEI 304
Cdd:cd03804 224 LPKRLVVIGDGPDLDRLRAMA----SPNVEFLGYQPDEVLKELLSKARAFVFAA---EEDFGIVPVEAQACGTPVIAFGK 296
|
170 180 190
....*....|....*....|....*....|.
gi 1997015909 305 GtGTSYVNADGETGHVILPANPDALREAMDD 335
Cdd:cd03804 297 G-GALETVRPGPTGILFGEQTVESLKAAVEE 326
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
30-374 |
1.34e-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: 73.86 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 30 GGLEQVVLELAQ--NTHGSGVLTLAkePGQRMLDGKL------PVLAERRWVSVASCCIGPGLVRRLFRLKAKLLHFHFP 101
Cdd:cd03802 18 GGTELVVSALTEglVRRGHEVTLFA--PGDSHTSAPLvaviprALRLDPIPQESKLAELLEALEVQLRASDFDVIHNHSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 102 WPFGDVTYLLagrSRPLIITYH-SDIVRQRALSLLYYPLMKIFLSRADRivatsqNYMDSSPVLAdfrskveVIPLGISE 180
Cdd:cd03802 96 DWLPPFAPLI---GTPFVTTLHgPSIPPSLAIYAAEPPVNYVSISDAQR------AATPPIDYLT-------VVHNGLDP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 181 QEYPVPADndllnmearfGKDFMLFVGvlRYY--KGLEYLIRAS--VGRPyrVVIAGKGPEQAKLKVLADELGADSIVFT 256
Cdd:cd03802 160 ADYRFQPD----------PEDYLAFLG--RIApeKGLEDAIRVArrAGLP--LKIAGKVRDEDYFYYLQEPLPGPRIEFI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 257 GYISDLEKAALMKLCRAVVFPShLRSEAFGVTLIEGLMYGKPLISCEIGtGTSYVNADGETGhvILPANPDALREAMDDL 336
Cdd:cd03802 226 GEVGHDEKQELLGGARALLFPI-NWDEPFGLVMIEAMACGTPVIAYRRG-GLPEVIQHGETG--FLVDSVEEMAEAIANI 301
|
330 340 350
....*....|....*....|....*....|....*...
gi 1997015909 337 wndpvkAEQMGQAGRLRYESLFTGERMAAAYQKLYTQV 374
Cdd:cd03802 302 ------DRIDRAACRRYAEDRFSAARMADRYEALYRKV 333
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
84-372 |
1.59e-14 |
|
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: 73.96 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 84 LVRRLFRLKAK---LLHFHFPWPFGDVTYLLA--GRSR----PLIITYHSDIVRQRALSLLYYPLMKIFLSRADRIVATS 154
Cdd:cd03822 64 YFRLLDHLNFKkpdVVHIQHEFGIFGGKYGLYalGLLLhlriPVITTLHTVLDLSDPGKQALKVLFRIATLSERVVVMAP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 155 QNYMDSSPVLADFRSKVEVIPLGISEQEY-PVPADNDLLNMEarfGKDFMLFVGVLRYYKGLEYLI------RASVGRPY 227
Cdd:cd03822 144 ISRFLLVRIKLIPAVNIEVIPHGVPEVPQdPTTALKRLLLPE---GKKVILTFGFIGPGKGLEILLealpelKAEFPDVR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 228 RVVIAGKGPEQAK------LKVLADELGADSIVF--TGYISDLEKAALMKLCRAVVFPSHLRSEAFGVTLIEGLMYGKPL 299
Cdd:cd03822 221 LVIAGELHPSLARyegeryRKAAIEELGLQDHVDfhNNFLPEEEVPRYISAADVVVLPYLNTEQSSSGTLSYAIACGKPV 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1997015909 300 ISCEIGTGTSyVNADGEtGHVILPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLfTGERMAAAYQKLYT 372
Cdd:cd03822 301 ISTPLRHAEE-LLADGR-GVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAM-TWESIADRYLRLFN 370
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
95-318 |
9.47e-13 |
|
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: 67.43 E-value: 9.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 95 LLHFHFPWPFGDVTYLLAGRSRPLIITYHSDIVRQRALSLLYYPLMKIFLSRADRIVATSQNYMDSSPVLADFRSKVEVI 174
Cdd:cd01635 3 LVTGEYPPLRGGLELHVRALARALAALGHEVTVLALLLLALRRILKKLLELKPDVVHAHSPHAAALAALLAARLLGIPIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 175 P---LGISEQEYPVPADNDLLNMEARFGKDFmLFVGVLRYYKGLEYLIRA-----SVGRPYRVVIAGKGPEQAKLKVLAD 246
Cdd:cd01635 83 VtvhGPDSLESTRSELLALARLLVSLPLADK-VSVGRLVPEKGIDLLLEAlallkARLPDLVLVLVGGGGEREEEEALAA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1997015909 247 ELGA--DSIVFTGYISDLEKAALMKLCRAVVFPShlRSEAFGVTLIEGLMYGKPLISCEIGtGTSYVNADGETG 318
Cdd:cd01635 162 ALGLleRVVIIGGLVDDEVLELLLAAADVFVLPS--RSEGFGLVLLEAMAAGKPVIATDVG-GIPEFVVDGENG 232
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
30-178 |
2.37e-12 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 64.48 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 30 GGLEQVVLELAQNTHGSG----VLTLAKEPGQRMLDGKLPVLAERRWVSVASCCIGPGLVRRLFRLKAK----LLHFHFP 101
Cdd:pfam13439 1 GGVERYVLELARALARRGhevtVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRerpdVVHAHSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 102 WPFGDVTYLLAGRSR-PLIITYHSDI-------VRQRALSLLYYPLMKIFLSRADRIVATSQNYMDSspVLADF---RSK 170
Cdd:pfam13439 81 FPLGLAALAARLRLGiPLVVTYHGLFpdykrlgARLSPLRRLLRRLERRLLRRADRVIAVSEAVADE--LRRLYgvpPEK 158
|
....*...
gi 1997015909 171 VEVIPLGI 178
Cdd:pfam13439 159 IRVIPNGV 166
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
150-358 |
4.30e-12 |
|
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: 66.56 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 150 IVATSQNYMDsspVLADF--RSKVEVIPLGISEQeypvpADNDLLNMEARFGKdfMLFVGVLRYYKGLEYLIRAsVGRPY 227
Cdd:cd04949 118 IVSTEQQKQD---LSERFnkYPPIFTIPVGYVDQ-----LDTAESNHERKSNK--IITISRLAPEKQLDHLIEA-VAKAV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 228 RVV------IAGKGPEQAKLKVLADELGA-DSIVFTGYISDLekAALMKLCRAVVFPSHlrSEAFGVTLIEGLMYGKPLI 300
Cdd:cd04949 187 KKVpeitldIYGYGEEREKLKKLIEELHLeDNVFLKGYHSNL--DQEYQDAYLSLLTSQ--MEGFGLTLMEAIGHGLPVV 262
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1997015909 301 SCEIGTGTSYVNADGETGHVILPANPDALREAMDDLWNDPVKAEQMGQ-----AGRLRYESLF 358
Cdd:cd04949 263 SYDVKYGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEesykiAEKYSTENVM 325
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
196-370 |
4.07e-10 |
|
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: 60.80 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 196 ARF--GKDFMlfvGVLRYYKgleyLIRASVGRPyRVVIAG----KGPEQAKL--KVLADELGADSI-VFTGYISDLEKAA 266
Cdd:cd03792 204 ARFdpSKDPL---GVIDAYK----LFKRRAEEP-QLVICGhgavDDPEGSVVyeEVMEYAGDDHDIhVLRLPPSDQEINA 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 267 LMKLCRAVVFPShlRSEAFGVTLIEGLMYGKPLISCEIGtGTSYVNADGETGHVILPANPDALReaMDDLWNDPVKAEQM 346
Cdd:cd03792 276 LQRAATVVLQLS--TREGFGLTVSEALWKGKPVIATPAG-GIPLQVIDGETGFLVNSVEGAAVR--ILRLLTDPELRRKM 350
|
170 180
....*....|....*....|....*.
gi 1997015909 347 GQAGR--LRYESLFTGErmAAAYQKL 370
Cdd:cd03792 351 GLAARehVRDNFLITGN--LRAWLYL 374
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
30-177 |
1.29e-09 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 56.64 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 30 GGLEQVVLELAQNTHGSG----VLTLAKEPGQRMLDGkLPVLAERRWVSVASccIGPGLVRRLFRLKAKLLHF-----HF 100
Cdd:pfam13579 1 GGIGVYVLELARALAALGhevrVVTPGGPPGRPELVG-DGVRVHRLPVPPRP--SPLADLAALRRLRRLLRAErpdvvHA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 101 PWPFGDVTYLLAGRSR--PLIITYHSDIVRQ--RALSLLYYPLMKIFLSRADRIVATSQNYMDSSPVLADFRSKVEVIPL 176
Cdd:pfam13579 78 HSPTAGLAARLARRRRgvPLVVTVHGLALDYgsGWKRRLARALERRLLRRADAVVVVSEAEAELLRALGVPAARVVVVPN 157
|
.
gi 1997015909 177 G 177
Cdd:pfam13579 158 G 158
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
235-371 |
1.45e-06 |
|
GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.
Pssm-ID: 411604 [Multi-domain] Cd Length: 489 Bit Score: 49.93 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 235 GPEQ------AKLKVLADELG-ADSIVFTGY--ISD-LEKAALMKLCRAvvfpshlrSEAFGVTLIEGLMYGKPLISCEI 304
Cdd:NF038011 344 GPEEedpayaAECRSLVASLGlQDKVKFLGFqkIDDlLPQVGLMVLSSI--------SEALPLVVLEAFAAGVPVVTTDV 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1997015909 305 GTGTSYVN-------ADGETGHVILPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLFTGERMAAAYQKLY 371
Cdd:NF038011 416 GSCRQLIEgldeedrALGAAGEVVAIADPQALARAALDLLRDPQRWQAAQAAGLARVERYYTEELMFDRYRELY 489
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
86-312 |
1.51e-06 |
|
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: 49.60 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 86 RRLFRLKAK----LLHFHFPwpFGDVTYLLAGRS---RPLIITYHSDIVRQRALSLLYYPLMKIFLSR-ADRIVATS--- 154
Cdd:cd03812 70 IKLLKLIKKekydIVHVHGS--SSNGIILLLAAKagvPVRIAHSHNTKDSSIKLRKIRKNVLKKLIERlSTKYLACSeda 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 155 QNYMDSSpvlaDFRSKVEVIPLGIseqeypvPADNDLLNMEARFGKDFMLF---------VGVLRYYKGLEYLIRA---- 221
Cdd:cd03812 148 GEWLFGE----VENGKFKVIPNGI-------DIEKYKFNKEKRRKRRKLLIledklvlghVGRFNEQKNHSFLIDIfeel 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 222 -SVGRPYRVVIAGKGPEQAKLKVLADELG-ADSIVFTGYISDLEKaaLMKLCRAVVFPSHLrsEAFGVTLIEGLMYGKPL 299
Cdd:cd03812 217 kKKNPNVKLVLVGEGELKEKIKEKVKELGlEDKVIFLGFRNDVSE--ILSAMDVFLFPSLY--EGLPLVAVEAQASGLPC 292
|
250 260
....*....|....*....|
gi 1997015909 300 I-------SCEIGTGTSYVN 312
Cdd:cd03812 293 LlsdtitkECDITNNVEFLP 312
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
170-358 |
1.79e-06 |
|
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: 49.37 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 170 KVEVIPLGISEQEYPVPADNDLLNmearfGKDFMLFVGVLRYYKGLEYLIRA-----SVGRPYRVVIAGKGPEQAKLKVL 244
Cdd:cd03799 149 KIIVHRSGIDCNKFRFKPRYLPLD-----GKIRILTVGRLTEKKGLEYAIEAvaklaQKYPNIEYQIIGDGDLKEQLQQL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 245 ADELGADSIV-FTGYISDLEKAALMKLCRAVVFPSHLRS----EAFGVTLIEGLMYGKPLISCEIGtGTSYVNADGETGH 319
Cdd:cd03799 224 IQELNIGDCVkLLGWKPQEEIIEILDEADIFIAPSVTAAdgdqDGPPNTLKEAMAMGLPVISTEHG-GIPELVEDGVSGF 302
|
170 180 190
....*....|....*....|....*....|....*....
gi 1997015909 320 VILPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLF 358
Cdd:cd03799 303 LVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEY 341
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
227-346 |
9.15e-06 |
|
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: 47.05 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 227 YRVVIAGKGPEQAKLKVLADELG-ADSIVFTGYISDLEKaaLMKLCRAVVFPShlRSEAFGVTLIEGLMYGKPLISCEIG 305
Cdd:cd04951 220 FKLLIAGDGPLRNELERLICNLNlVDRVILLGQISNISE--YYNAADLFVLSS--EWEGFGLVVAEAMACERPVVATDAG 295
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1997015909 306 tGTSYVNADGEtgHVILPANPDALREAMDDLWNDPVKAEQM 346
Cdd:cd04951 296 -GVAEVVGDHN--YVVPVSDPQLLAEKIKEIFDMSDEERDI 333
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
178-355 |
9.74e-06 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 47.09 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 178 ISEQEYPVPADNDLLNMEARFGKDfmlfVGVLRYYKGLEYLIRAS-------VGRPYRVVIAGKGPEQAKLKVLADELGA 250
Cdd:PRK15484 182 NLRQQLNISPDETVLLYAGRISPD----KGILLLMQAFEKLATAHsnlklvvVGDPTASSKGEKAAYQKKVLEAAKRIGD 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 251 DSIVFTGyISDLEKAALMKLCRAVVFPSHLRsEAFGVTLIEGLMYGKPLISCEIGTGTSYVnADGETG-HVILPANPDAL 329
Cdd:PRK15484 258 RCIMLGG-QPPEKMHNYYPLADLVVVPSQVE-EAFCMVAVEAMAAGKPVLASTKGGITEFV-LEGITGyHLAEPMTSDSI 334
|
170 180
....*....|....*....|....*.
gi 1997015909 330 REAMDDLWNDPVKAEQMGQAGRLRYE 355
Cdd:PRK15484 335 ISDINRTLADPELTQIAEQAKDFVFS 360
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
117-351 |
3.01e-05 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 45.86 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 117 PLIITYHSDI---VRQRALSLLYYP---LMKIFLSRADRIVATS---QNYMDSSPVLAdfRSKVEVIPLGI-SEQEYPVP 186
Cdd:PLN02871 170 PLVMSYHTHVpvyIPRYTFSWLVKPmwdIIRFLHRAADLTLVTSpalGKELEAAGVTA--ANRIRVWNKGVdSESFHPRF 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 187 ADNDllnMEARF-----GKDFMLFVGVLRYYKGLEYLIRASVGRP-YRVVIAGKGPEQAKLKVLADELGAdsiVFTGYIS 260
Cdd:PLN02871 248 RSEE---MRARLsggepEKPLIVYVGRLGAEKNLDFLKRVMERLPgARLAFVGDGPYREELEKMFAGTPT---VFTGMLQ 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 261 DLEKAALMKLCRAVVFPSHlrSEAFGVTLIEGLMYGKPLISCEIGTGTSYVNAD--GETGHVILPANPDALREAMDDLWN 338
Cdd:PLN02871 322 GDELSQAYASGDVFVMPSE--SETLGFVVLEAMASGVPVVAARAGGIPDIIPPDqeGKTGFLYTPGDVDDCVEKLETLLA 399
|
250
....*....|...
gi 1997015909 339 DPVKAEQMGQAGR 351
Cdd:PLN02871 400 DPELRERMGAAAR 412
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
170-325 |
2.06e-04 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 43.16 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 170 KVEVIPLGISEQEY-----PVPADNDLLNMEARFGKDFMLFVGVLRYY--KGLEYLIRAsVGR---PYRVVIAGKGPEQA 239
Cdd:PRK09922 145 KEQMMARGISAQRIsviynPVEIKTIIIPPPERDKPAVFLYVGRLKFEgqKNVKELFDG-LSQttgEWQLHIIGDGSDFE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 240 KLKVLADELG-ADSIVFTGYISDLEKAALMKLCR--AVVFPSHLrsEAFGVTLIEGLMYGKPLISCEIGTGTSYVNADGE 316
Cdd:PRK09922 224 KCKAYSRELGiEQRIIWHGWQSQPWEVVQQKIKNvsALLLTSKF--EGFPMTLLEAMSYGIPCISSDCMSGPRDIIKPGL 301
|
....*....
gi 1997015909 317 TGHVILPAN 325
Cdd:PRK09922 302 NGELYTPGN 310
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
86-154 |
3.21e-04 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 40.38 E-value: 3.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1997015909 86 RRLFRLKAK----LLHFHFPWPFGDVTYLLAGRSR--PLIITYH-SDIVRQRALSLLYYPLMKIFLSRADRIVATS 154
Cdd:pfam13477 64 FRLKKLIKKikpdVVHVHYAKPYGLLAGLAARLSGfpPVVLSAWgLDVYKFPNKSRLKKLLLKLNLKKATLIISTS 139
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
139-373 |
4.30e-04 |
|
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: 42.17 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 139 LMKIFLSRADRIVATSQNY------------MDssPVLADFRSKVEVIPLGISEQEY--------PVPADNDLLNM---- 194
Cdd:cd03791 201 FLKAGIVYADRVTTVSPTYakeiltpeygegLD--GVLRARAGKLSGILNGIDYDEWnpatdkliPANYSANDLEGkaen 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 195 ----EARFG----KDFML--FVGVLRYYKGLEYL---IRASVGRPYRVVIAGKGPE--QAKLKVLADELGADSIVFTGY- 258
Cdd:cd03791 279 kaalQKELGlpvdPDAPLfgFVGRLTEQKGVDLIldaLPELLEEGGQLVVLGSGDPeyEQAFRELAERYPGKVAVVIGFd 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 259 ------I---SDLekaALMklcravvfPShlRSEAFGVTLIEGLMYGKPLISCEIG----TGTSYVNADGE-TGHVILPA 324
Cdd:cd03791 359 ealahrIyagADF---FLM--------PS--RFEPCGLVQMYAMRYGTLPIVRRTGgladTVFDYDPETGEgTGFVFEDY 425
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1997015909 325 NPDALREAMD---DLWNDPVKAEQMGQAGrlrYESLFTGERMAAAYQKLYTQ 373
Cdd:cd03791 426 DAEALLAALRralALYRNPELWRKLQKNA---MKQDFSWDKSAKEYLELYRS 474
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
165-367 |
1.61e-03 |
|
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: 40.42 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 165 ADFRSKVEVIPLGI-SEQEYPVP-ADNDLLNM-EARFGKDFMLFVG-VLRYYKG----LEYLIRASVGRP-YRVVIAGK- 234
Cdd:cd03818 175 AAYRDRISVIHDGVdTDRLAPDPaARLRLLNGtELKAGDPVITYVArNLEPYRGfhvfMRALPRIQARRPdARVVVVGGd 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 235 ---------GPEQAKLKVLADELGADS-IVFTGYISDLEKAALMKLCRAVVFPshLRSEAFGVTLIEGLMYGKPLIscei 304
Cdd:cd03818 255 gvsygspppDGGSWKQKMLAELGVDLErVHFVGKVPYDQYVRLLQLSDAHVYL--TYPFVLSWSLLEAMACGCPVI---- 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1997015909 305 GTGTSYVN---ADGETGHVILPANPDALREAMDDLWNDPVKAEQMGQAGRLRYESLFTGERMAAAY 367
Cdd:cd03818 329 GSDTAPVReviRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCLARY 394
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
233-372 |
1.64e-03 |
|
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: 40.14 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 233 GKGPEQAKLKVLAD-ELGADSIVFTGYISDLEKAALMKLCRAVVFPSHLRSEAFGVTLIEGLMYGKPLISCEIGtGTSYV 311
Cdd:cd04946 264 GGGPLKERLEKLAEnKLENVKVNFTGEVSNKEVKQLYKENDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVG-GTREI 342
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1997015909 312 NADGETGhvILPANPDALREAMDDLWN---DPVKAEQMGQAGRLRYESLFTGERMaaaYQKLYT 372
Cdd:cd04946 343 VENETNG--LLLDKDPTPNEIVSSIMKfylDGGDYKTMKISARECWEERFNAEVN---YSKFAN 401
|
|
| GT9_LPS_heptosyltransferase |
cd03789 |
lipopolysaccharide heptosyltransferase and similar proteins; Lipopolysaccharide ... |
218-290 |
4.00e-03 |
|
lipopolysaccharide heptosyltransferase and similar proteins; Lipopolysaccharide heptosyltransferase (2.4.99.B6) is involved in the biosynthesis of lipooligosaccharide (LOS). Lipopolysaccharide (LPS) is a major component of the outer membrane of gram-negative bacteria. LPS heptosyltransferase transfers heptose molecules from ADP-heptose to 3-deoxy-D-manno-octulosonic acid (KDO), a part of the inner core component of LPS. This family also contains lipopolysaccharide 1,2-N-acetylglucosaminetransferase EC 2.4.1.56 and belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic 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: 340821 Cd Length: 277 Bit Score: 38.48 E-value: 4.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1997015909 218 LIRASVGRPYRVVIAGKGPEQAKLKVLADELGADSIVFTGYISDLEKAALMKLCRAVVF----PSHLRSeAFGVTLI 290
Cdd:cd03789 144 LADRLADEGYRVVLFGGPAEEELAEEIAAALGARVVNLAGKTSLRELAALLARADLVVGndsgPMHLAA-ALGTPTV 219
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
225-371 |
6.35e-03 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 38.48 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 225 RPY-RVVIAGKGPEQAKLKVLADELG-ADSIVFTG-------YISDLEKAALMKlcravvfpshlRSEAFGVTLIEGLMY 295
Cdd:PRK15179 546 HPKvRFIMVGGGPLLESVREFAQRLGmGERILFTGlsrrvgyWLTQFNAFLLLS-----------RFEGLPNVLIEAQFS 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997015909 296 GKPLISCEIGtGTSYVNADGETGHvILPAN----PDaLREAMDDLWNDPVKAEQMGQAGRLRYESLFTGERMAAAYQKLY 371
Cdd:PRK15179 615 GVPVVTTLAG-GAGEAVQEGVTGL-TLPADtvtaPD-VAEALARIHDMCAADPGIARKAADWASARFSLNQMIASTVRCY 691
|
|
| |
