|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
7-426 |
0e+00 |
|
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: 614.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 7 RTIAFIHPDLGIGGAERLVVDAALGLQQQGHSVIIYTSHCDKSHCFEEVKNGQLKVEVYGDFLPTNFLGRFFIVFATIRQ 86
Cdd:cd03805 1 LRVAFLHPDLGIGGAERLVVDAALALQSRGHEVTIYTSHHDPSHCFEETKDGTLPVRVRGDWLPRSIFGRFHALCAYLRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 87 LYLVIQLILqKKVNAYQLIIIDQLSTCIPLLHIFSSATLMFYCHFPDQLLAQRAGLLKKIYRLPFDLIEQFSVSAADTVV 166
Cdd:cd03805 81 LYLALYLLL-FSGEKYDVFIVDQVSACVPLLKLFRPSKILFYCHFPDQLLAQRKSLLKRLYRKPFDWLEEFTTGMADQIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 167 VNSNFTKNTFHQTFKYLSNDP-DVIYPCVDLSTIEIEDIDKKFFKTVFNEGDRFYLSINRFEKKKDVALAIKAFALSEDQ 245
Cdd:cd03805 160 VNSNFTAGVFKKTFPSLAKNPpEVLYPCVDTDSFDSTSEDPDPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 246 I--NDNVKLVICGGYDERVAENVEYLKELQSLADEYELShttiyyqeikrvsdlesfktnNSKIIFLTSISSSLKELLLE 323
Cdd:cd03805 240 LpeFENVRLVIAGGYDPRVAENVEYLEELQRLAEELLNV---------------------EDQVLFLRSISDSQKEQLLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 324 RTEMLLYTPAYEHFGIVPLEAMKLGKPVLAVNNGGPLETIKSYVagenessaTGWLKPAVPIQWATAIDESRKILQNgSV 403
Cdd:cd03805 299 SALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGV--------TGFLCEPTPEAFAEAMLKLANDPDL-AD 369
|
410 420
....*....|....*....|...
gi 6321373 404 NFERNGPLRVKKYFSREAMTQSF 426
Cdd:cd03805 370 RMGAAGRKRVKEKFSREAFAERL 392
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
9-428 |
1.01e-29 |
|
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: 119.56 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 9 IAFIHPDL--GIGGAERLVVDAALGLQQQGHSVIIYTsHCDKSHCFEEVKNGQLKVEVYGDFL------------PTNFL 74
Cdd:cd03801 2 ILLLSPELppPVGGAERHVRELARALAARGHDVTVLT-PADPGEPPEELEDGVIVPLLPSLAAllrarrllrelrPLLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 75 GRFFIVFATIRQLYLVIQLIlqKKVNAYQLIIIdqlstcipllhifssatlmFYCHFPDQLLAQRAGLLKKIYRLPFDLi 154
Cdd:cd03801 81 RKFDVVHAHGLLAALLAALL--ALLLGAPLVVT-------------------LHGAEPGRLLLLLAAERRLLARAEALL- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 155 eqfsvSAADTVVVNSNFTKNTFHQTFKYLSNDPDVIYPCVDLSTIEIEDIDKKFFKtvfnEGDRFYLSINRFEKKKDVAL 234
Cdd:cd03801 139 -----RRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSPPLRRKLGIP----PDRPVLLFVGRLSPRKGVDL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 235 AIKAFALSEDQINdNVKLVICGGYDErvaenveYLKELQSLadEYELSHttiyyqeikrvsdlesfktnnsKIIFLTSIS 314
Cdd:cd03801 210 LLEALAKLLRRGP-DVRLVIVGGDGP-------LRAELEEL--ELGLGD----------------------RVRFLGFVP 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 315 SSLKELLLERTEMLLYTPAYEHFGIVPLEAMKLGKPVLAVNNGGPLETIksyvagenESSATGWL-KPAVPIQWATAIde 393
Cdd:cd03801 258 DEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV--------EDGEGGLVvPPDDVEALADAL-- 327
|
410 420 430
....*....|....*....|....*....|....*..
gi 6321373 394 sRKILQNGSVNFE--RNGPLRVKKYFSREAMTQSFEE 428
Cdd:cd03801 328 -LRLLADPELRARlgRAARERVAERFSWERVAERLLD 363
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
216-412 |
8.39e-26 |
|
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: 103.12 E-value: 8.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 216 GDRFYLSINRFEKKKDVALAIKAFALSEDQiNDNVKLVICGgydervaeNVEYLKELQSLADEYELSHTTIYYQEIKRvS 295
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEK-NPNLKLVIAG--------DGEEEKRLKKLAEKLGLGDNVIFLGFVSD-E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 296 DLESFKtNNSKIIFLTSIssslkelllertemllytpaYEHFGIVPLEAMKLGKPVLAVNNGGPLETIKSYVAGEnessa 375
Cdd:pfam00534 71 DLPELL-KIADVFVLPSR--------------------YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGF----- 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 6321373 376 tgWLKPAVPIQWATAIDesrKILQNG--SVNFERNGPLR 412
Cdd:pfam00534 125 --LVKPNNAEALAEAID---KLLEDEelRERLGENARKR 158
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
9-369 |
1.81e-25 |
|
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: 107.06 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 9 IAFIHPDLGIGGAERLVVDAALGLQQQGHSVIIYtSHCDKSHCFEEVKNGQLKVEVYGDFLPTNFLGRffivFATIRQLY 88
Cdd:cd03811 2 ILFVIPSLSGGGAERVLLNLANALDKRGYDVTLV-LLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGL----LKAILKLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 89 LVIqlilqkKVNAYQLIIIDQLSTCIPLLHIFSSATLMFYCH--FPDQLLAQRAGLLKKIYRLPFdlieqfsvsaADTVV 166
Cdd:cd03811 77 RIL------KRAKPDVVISFLGFATYIVAKLAAARSKVIAWIhsSLSKLYYLKKKLLLKLKLYKK----------ADKIV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 167 VNSNFTKNTFHQTFKYLSNDPDVIYPCVDLSTIEIEDIDKKFFktvFNEGDRFYLSINRFEKKKDVALAIKAFALSEDQi 246
Cdd:cd03811 141 CVSKGIKEDLIRLGPSPPEKIEVIYNPIDIDRIRALAKEPILN---EPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKK- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 247 NDNVKLVICGGYDERvaenveylKELQSLADEYELSHttiyyqeikrvsdlesfktnnsKIIFLTSISSSLKelLLERTE 326
Cdd:cd03811 217 YPDVKLVILGDGPLR--------EELEKLAKELGLAE----------------------RVIFLGFQSNPYP--YLKKAD 264
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 6321373 327 MLLYTPAYEHFGIVPLEAMKLGKPVLAVNNGGPLETIKSYVAG 369
Cdd:cd03811 265 LFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENG 307
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
76-425 |
1.26e-18 |
|
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: 87.42 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 76 RFFIVFATIRQLYLVIQLILQKKVNAYQLIIidqLSTCIPLLHIFSSATLMFYCH--FPDQLLAQRAGLLKKIYRLPFDL 153
Cdd:cd03809 58 LGVIKIKLWRELALLRWLQILLPKKDKPDLL---HSPHNTAPLLLKGCPQVVTIHdlIPLRYPEFFPKRFRLYYRLLLPI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 154 ieqfSVSAADTVVVNSNFTKNtfhQTFKYLSNDPD---VIYPCVDLSTIEIEDIDKKFFKtvFNEGDRFYLSINRFEKKK 230
Cdd:cd03809 135 ----SLRRADAIITVSEATRD---DIIKFYGVPPEkivVIPLGVDPSFFPPESAAVLIAK--YLLPEPYFLYVGTLEPRK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 231 DVALAIKAFALSEDQiNDNVKLVICGGYDERVAENVEYLKELQSladeyelshttiyyqeikrvsdlesfktnNSKIIFL 310
Cdd:cd03809 206 NHERLLKAFALLKKQ-GGDLKLVIVGGKGWEDEELLDLVKKLGL-----------------------------GGRVRFL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 311 TSISSSLKELLLERTEMLLYtPA-YEHFGIVPLEAMKLGKPVLAVnNGGPLETIksyvAGENessatGWL-KPAVPIQWA 388
Cdd:cd03809 256 GYVSDEDLPALYRGARAFVF-PSlYEGFGLPVLEAMACGTPVIAS-NISVLPEV----AGDA-----ALYfDPLDPESIA 324
|
330 340 350
....*....|....*....|....*....|....*....
gi 6321373 389 TAIdesRKILQNGSVNFE--RNGPLRVKKyFSREAMTQS 425
Cdd:cd03809 325 DAI---LRLLEDPSLREEliRKGLERAKK-FSWEKTAEK 359
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
9-437 |
2.59e-18 |
|
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: 86.14 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 9 IAFIHPDLG-IGGAERLVVDAALGLQQQGHSVIIYTSHCDKSHCFEEVkNGQLKVEvygdFLPTNFLGRFFIVFATIRQL 87
Cdd:cd03820 2 IAIVIPSISnAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYEL-DDNIKIK----NLGDRKYSHFKLLLKYFKKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 88 YLVIQLIlqkKVNAYQlIIIDQLSTCIPLLHIFSSATLMFYC-HFpdQLLAQRAGLLKKIYRLpfdlieqFSVSAADTVV 166
Cdd:cd03820 77 RRLRKYL---KNNKPD-VVISFRTSLLTFLALIGLKSKLIVWeHN--NYEAYNKGLRRLLLRR-------LLYKRADKIV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 167 VNSNFTKNTFHQTFKylsNDPDVIY-PCVDLSTIEIEDIDKKFFktvfnegdrfyLSINRFEKKKDVALAIKAFALSEDQ 245
Cdd:cd03820 144 VLTEADKLKKYKQPN---SNVVVIPnPLSFPSEEPSTNLKSKRI-----------LAVGRLTYQKGFDLLIEAWALIAKK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 246 iNDNVKLVICGGYDERvaenveylKELQSLADEYELSHTTIYYQEIKRVSDLESfktnNSKIIFLTSissslkelllert 325
Cdd:cd03820 210 -HPDWKLRIYGDGPER--------EELEKLIDKLGLEDRVKLLGPTKNIAEEYA----NSSIFVLSS------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 326 emllytpAYEHFGIVPLEAMKLGKPVLAVN-NGGPLETIKSyvaGENessatGWLkpaVPIQWATAIDESRKILQNgsvn 404
Cdd:cd03820 264 -------RYEGFPMVLLEAMAYGLPIISFDcPTGPSEIIED---GEN-----GLL---VPNGDVDALAEALLRLME---- 321
|
410 420 430
....*....|....*....|....*....|....*
gi 6321373 405 ferNGPLRVKkyFSREAMTQSFEENVEKVI--WKE 437
Cdd:cd03820 322 ---DEELRKK--MGKNARKNAERFSIEKIIkqWEE 351
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
7-363 |
3.96e-18 |
|
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: 86.51 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 7 RTIAFIHP--DLGiGGAERLVVDAALGLQQQG--HSVIIYTSHCDKSHC--FEEVKNgQLKVEVYGDflptnflgRFFIV 80
Cdd:cd03806 1 ITVGFFHPycNAG-GGGERVLWCAVKATQKAYpnNICVIYTGDTDSSPEeiLEKVES-RFNIDLDSP--------RIVFF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 81 FATIRQL-----YLVIQLILQkkvnAYQLII--IDQLSTCIP--------------LLHIFSSATLMFYCHFP------- 132
Cdd:cd03806 71 LLKYRKLveaktYPRFTLLGQ----ALGSMIlgFEALLKLVPdvfidtmgypftypLVRLLGGCPVVAYVHYPtistdml 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 133 ------------DQLLAQRAGL--LKKIYRLPFDLIEQFSVSAADTVVVNSNFTKNTFHQTFKYlSNDPDVIYPCVDLST 198
Cdd:cd03806 147 nkvrsreasynnDSTIARSSVLsiAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKR-NIKPSIVYPPCDTEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 199 IEIEDIDKKffktvfneGDRFY-LSINRFEKKKDVALAIKAFAL----SEDQINDNVKLVICGGYdeRVAENVEYLKELQ 273
Cdd:cd03806 226 LTKLPIDEK--------TRENQiLSIAQFRPEKNHPLQLRAFAEllkrLPESIRSNPKLVLIGSC--RNEEDKERVEALK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 274 SLADEYELSHttiyyqeikrvsdlesfktnnsKIIFLTSISSSLKELLLERTEMLLYTPAYEHFGIVPLEAMKLGKPVLA 353
Cdd:cd03806 296 LLAKELILED----------------------SVEFVVDAPYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLA 353
|
410
....*....|
gi 6321373 354 VNNGGPLETI 363
Cdd:cd03806 354 HASAGPLLDI 363
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
154-418 |
1.53e-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: 84.60 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 154 IEQFSVSAADTVVVNsnfTKNTFHQTFKYLSNDPD---VIYPCVDLSTI-EIEDIDKKFFKTVFNEGDRFYLSINRFEKK 229
Cdd:cd03800 156 AEEQILEAADRVIAS---TPQEADELISLYGADPSrinVVPPGVDLERFfPVDRAEARRARLLLPPDKPVVLALGRLDPR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 230 KDVALAIKAFALSEDqINDNVKLVICGGY----DERVAENVEYLKELQSLADEYELShttiyyqeiKRVSDLESFKTNNS 305
Cdd:cd03800 233 KGIDTLVRAFAQLPE-LRELANLVLVGGPsddpLSMDREELAELAEELGLIDRVRFP---------GRVSRDDLPELYRA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 306 KIIFLTsissslkelllertemllyTPAYEHFGIVPLEAMKLGKPVLAVNNGGPLETIKSYVagenessaTGWLKPAV-P 384
Cdd:cd03800 303 ADVFVV-------------------PSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGR--------TGLLVDPHdP 355
|
250 260 270
....*....|....*....|....*....|....*.
gi 6321373 385 IQWATAIdesRKILQNGSVN--FERNGPLRVKKYFS 418
Cdd:cd03800 356 EALAAAL---RRLLDDPALWqrLSRAGLERARAHYT 388
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
19-197 |
3.81e-15 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 73.34 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 19 GGAERLVVDAALGLQQQGHSVIIYTSHCDKSHCFEEVKNGQLKVEVYGdflptnFLGRFFIVFATIRQLYLVIqlilqkK 98
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLP------LPPRLLRSLAFLRRLRRLL------R 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 99 VNAYQLIIIDQLSTCIPLLHIFSSAT---LMFYCHFPDQLLaQRAGLLKKIYRLPFDLIEQFSVSAADTVVVNSNFTKNT 175
Cdd:pfam13439 69 RERPDVVHAHSPFPLGLAALAARLRLgipLVVTYHGLFPDY-KRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADE 147
|
170 180
....*....|....*....|..
gi 6321373 176 FHQTFKYLSNDPDVIYPCVDLS 197
Cdd:pfam13439 148 LRRLYGVPPEKIRVIPNGVDLE 169
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
8-428 |
1.73e-13 |
|
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: 71.58 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 8 TIAFIHPDLGIGGAERLVVDAALGLQQQG-HSVIIYTSHcdKSHCFEEVKNGQLKVEVYGdflptnflGRFFIVFATIRQ 86
Cdd:cd03807 1 KVAHVITGLNVGGAETMLLRLLEHMDKSRfEHVVISLTG--DGVLGEELLAAGVPVVCLG--------LSSGKDPGVLLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 87 LylvIQLILQKKVNAYQLIIIDQLStCIPLLHIFSSATLMFYC-----HFPDQllaqrAGLLKKIYRLPFDLIeQFSVSA 161
Cdd:cd03807 71 L---AKLIRKRNPDVVHTWMYHADL-IGGLAAKLAGGVKVIWSvrssnIPQRL-----TRLVRKLCLLLSKFS-PATVAN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 162 ADTVVvnsnftknTFHQTFKYLSNDPDVIYPCVDLSTIEIEDIDKKFFKTVFNEGDRFYLSIN--RFEKKKDVALAIKAF 239
Cdd:cd03807 141 SSAVA--------EFHQEQGYAKNKIVVIYNGIDLFKLSPDDASRARARRRLGLAEDRRVIGIvgRLHPVKDHSDLLRAA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 240 ALSEDQiNDNVKLVICGGYDERvaenveylKELQSLADEYELSHTTIYYQEIKRVSDlesfktnnskiifltsissslke 319
Cdd:cd03807 213 ALLVET-HPDLRLLLVGRGPER--------PNLERLLLELGLEDRVHLLGERSDVPA----------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 320 lLLERTEMLLYTPAYEHFGIVPLEAMKLGKPVLAVNNGGPLETIKsyvagenesSATGWLKPA-VPIQWATAIDESRKiL 398
Cdd:cd03807 261 -LLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVD---------DGTGFLVPAgDPQALADAIRALLE-D 329
|
410 420 430
....*....|....*....|....*....|
gi 6321373 399 QNGSVNFERNGPLRVKKYFSREAMTQSFEE 428
Cdd:cd03807 330 PEKRARLGRAARERIANEFSIDAMVRRYET 359
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
8-358 |
1.17e-12 |
|
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: 69.29 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 8 TIAFIHPD--LGIGGAERLVVDAALGLQQQGHSVIIYTSHCDKSH--CFEEVKNGQLKVEVYgdFLPTNFLGRFFIVFAT 83
Cdd:cd03794 1 KILLISQYypPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLgrIFAGATETKDGIRVI--RVKLGPIKKNGLIRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 84 IRQLYLVIQLILQKKVNAYQLIIIdqLSTCIPLLHIFSSATLMFYCH----------FPDQLLAqrAGLLKKIYRLP-FD 152
Cdd:cd03794 79 LNYLSFALAALLKLLVREERPDVI--IAYSPPITLGLAALLLKKLRGapfildvrdlWPESLIA--LGVLKKGSLLKlLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 153 LIEQFSVSAADTVVVNSNFTKNTFHQtfKYLSNDP-DVIYPCVDLStiEIEDIDKKFFKTVFNEGDRFYL----SInrfE 227
Cdd:cd03794 155 KLERKLYRLADAIIVLSPGLKEYLLR--KGVPKEKiIVIPNWADLE--EFKPPPKDELRKKLGLDDKFVVvyagNI---G 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 228 KKKDVALAIKAFALSEDqiNDNVKLVICGGYDERvaenveylKELQSLADEYELSHTTIYYqeikRVSDLEsfktnnski 307
Cdd:cd03794 228 KAQGLETLLEAAERLKR--RPDIRFLFVGDGDEK--------ERLKELAKARGLDNVTFLG----RVPKEE--------- 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 6321373 308 ifltsisssLKELLLERTEMLL-YTPAYEHFGIVP---LEAMKLGKPVLAVNNGG 358
Cdd:cd03794 285 ---------VPELLSAADVGLVpLKDNPANRGSSPsklFEYMAAGKPILASDDGG 330
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
317-434 |
5.73e-12 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 62.70 E-value: 5.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 317 LKELLLERTEMLLYTPAYEHFGIVPLEAMKLGKPVLAVNNGGPLETIKSYVagenessaTGWL-KPAVPIQWATAIdesR 395
Cdd:COG0438 13 LLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGE--------TGLLvPPGDPEALAEAI---L 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 6321373 396 KILQNGSV--NFERNGPLRVKKYFSREAMTQSFEENVEKVI 434
Cdd:COG0438 82 RLLEDPELrrRLGEAARERAEERFSWEAIAERLLALYEELL 122
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
128-369 |
5.75e-12 |
|
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: 66.92 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 128 YCHFP--------DQLLAQ-RAGLLKK--IYRLPFDLIEQFSVSAA---DTVVVNSNFTKNTFHqtfKYLSNDPDVIYPC 193
Cdd:cd03804 110 YVHSPiryawdlyHQYLAEsGLGKGIKslLASLFLHYLRLWDVRTAqrvDLFIANSQFVARRIK---KFYGRESTVIYPP 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 194 VDlstieiediDKKFfkTVFNEGDRFYLSINRFEKKKDVALAIKAFAlsedqiNDNVKLVICG-GYDervaenveyLKEL 272
Cdd:cd03804 187 VD---------TDAF--APAADKEDYYLTASRLVPYKRIDLAVEAFN------ELPKRLVVIGdGPD---------LDRL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 273 QSLADeyelshttiyyqeikrvsdlesfktnnSKIIFLTSISSSLKELLLERTEMLLYtPAYEHFGIVPLEAMKLGKPVL 352
Cdd:cd03804 241 RAMAS---------------------------PNVEFLGYQPDEVLKELLSKARAFVF-AAEEDFGIVPVEAQACGTPVI 292
|
250
....*....|....*..
gi 6321373 353 AVNNGGPLETIKSYVAG 369
Cdd:cd03804 293 AFGKGGALETVRPGPTG 309
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
221-370 |
2.61e-10 |
|
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: 60.50 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 221 LSINRFEKKKDVALAIKAFALSEDQINDNVKLVICGGYDERVAENVEYLKELQSLADEYELSHTTIYYQEIKRVSDLesf 300
Cdd:cd01635 114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADV--- 190
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 301 ktnnskiIFLTSIssslkelllertemllytpaYEHFGIVPLEAMKLGKPVLAVNNGGPLETIKSYVAGE 370
Cdd:cd01635 191 -------FVLPSR--------------------SEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
11-423 |
1.73e-09 |
|
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: 59.21 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 11 FIHPDlgIGGAERLVVDAALGLQQQGHSVIIYTSHCDKSHCFEEVKNGQL-KVEVYGDFLPTNFlgrffiVFATIRQLYl 89
Cdd:cd03795 8 FYYPD--IGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIRIhRVKSFLNVASTPF------SPSYIKRFK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 90 viqlilqKKVNAYQLIIIDQLSTCIPLLHIFSSATLMFYCHFPDQLLAQRAglLKKIYRlPFD--LIEQfsvsaADTVVV 167
Cdd:cd03795 79 -------KLAKEYDIIHYHFPNPLADLLLFFSGAKKPVVVHWHSDIVKQKK--LLKLYK-PLMtrFLRR-----ADRIIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 168 NS-NFTKNTfhQTFKYLSNDPDVIYPCVDLSTIEIEDIDKKFFKTVfNEGDRFYLSINRFEKKKDVALAIKAFALSedqi 246
Cdd:cd03795 144 TSpNYVETS--PTLREFKNKVRVIPLGIDKNVYNIPRVDFENIKRE-KKGKKIFLFIGRLVYYKGLDYLIEAAQYL---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 247 ndNVKLVICGGYDERvaenveylKELQSLADEYELSHTTIyyqeIKRVSDLESFKTNN-SKIIFLTSIssslkelllERT 325
Cdd:cd03795 217 --NYPIVIGGEGPLK--------PDLEAQIELNLLDNVKF----LGRVDDEEKVIYLHlCDVFVFPSV---------LRS 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 326 EMllytpayehFGIVPLEAMKLGKPVLAVNnggpLETIKSYVAGENESSATgwLKPAVPIQWATAIDesrKILQNGSV-- 403
Cdd:cd03795 274 EA---------FGIVLLEAMMCGKPVISTN----IGTGVPYVNNNGETGLV--VPPKDPDALAEAID---KLLSDEELre 335
|
410 420
....*....|....*....|
gi 6321373 404 NFERNGPLRVKKYFSREAMT 423
Cdd:cd03795 336 SYGENAKKRFEELFTAEKMK 355
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
9-381 |
7.94e-09 |
|
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: 57.36 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 9 IAFIHPDLGIGGAERLVVDAALGLQQQGHSVIIYTShcdkshcfeeVKNGQLKVEVYGDFLPTNFlGRFFIVFATIRQLY 88
Cdd:cd03819 1 ILMLTPALEIGGAETYILDLARALAERGHRVLVVTA----------GGPLLPRLRQIGIGLPGLK-VPLLRALLGNVRLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 89 LviqLILQKKVNayqliiidqlstcipLLHIFSSATLmfychfpdqLLAQragLLKKIYRLPF-------DLIEQ----- 156
Cdd:cd03819 70 R---LIRRERID---------------LIHAHSRAPA---------WLGW---LASRLTGVPLvttvhgsYLATYhpkdf 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 157 --FSVSAADTVVVNSNFTKNTFHQTFKYLSNDPDVIYPCVDLS--TIEIEDIDKKFFKTVfnEGDRFYLSINRFEKKKDV 232
Cdd:cd03819 120 alAVRARGDRVIAVSELVRDHLIEALGVDPERIRVIPNGVDTDrfPPEAEAEERAQLGLP--EGKPVVGYVGRLSPEKGW 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 233 ALAIKAFALSEDQinDNVKLVICGgyDERVAENVEYLKELQSLADeyelshttiyyqeikrvsdlesfktnnsKIIFLTS 312
Cdd:cd03819 198 LLLVDAAAELKDE--PDFRLLVAG--DGPERDEIRRLVERLGLRD----------------------------RVTFTGF 245
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321373 313 ISSSLKelLLERTEMLLYTPAYEHFGIVPLEAMKLGKPVLAVNNGGPLETIksyvagenESSATGWLKP 381
Cdd:cd03819 246 REDVPA--ALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIV--------VHGRTGLLVP 304
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
222-426 |
2.52e-08 |
|
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: 56.19 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 222 SINRFEKKKDVALAIKAFALSEDQINDnVKLVICGGYDErvaeNVEYLKELQSLADEYELSHTTIYyQEIKRVSDLESFk 301
Cdd:cd03813 298 LVGRVVPIKDVKTFIRAFKLVRRAMPD-AEGWLIGPEDE----DPEYAQECKRLVASLGLENKVKF-LGFQNIKEYYPK- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 302 tnnSKIIFLTSISsslkelllertemllytpayEHFGIVPLEAMKLGKPVLAVNNGGPLETIksYVAGENESSATGWLKP 381
Cdd:cd03813 371 ---LGLLVLTSIS--------------------EGQPLVILEAMASGVPVVATDVGSCRELI--YGADDALGQAGLVVPP 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6321373 382 AVPIQWATAIdesRKILQNGSV--NFERNGPLRVKKYFSREAMTQSF 426
Cdd:cd03813 426 ADPEALAEAL---IKLLRDPELrqAFGEAGRKRVEKYYTLEGMIDSY 469
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
162-430 |
6.60e-08 |
|
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: 54.59 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 162 ADTVVVNSNFTKNTFHqtfKYLSNDPDVIYPC-VDLSTIEIEDIDKKFFKTVFNEGDRFYLSINRFEKKKDVALAIKAFA 240
Cdd:cd03817 148 TDAVIAPSEKIKDTLR---EYGVKGPIEVIPNgIDLDKFEKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 241 LSEDQINdnVKLVICGGYDERvaenveylKELQSLADEYELShttiyyqeikrvsdlesfktnnSKIIFLTSISSSLKEL 320
Cdd:cd03817 225 ELKKEPN--IKLVIVGDGPER--------EELKELARELGLA----------------------DKVIFTGFVPREELPE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 321 LLERTEMLLYTPAYEHFGIVPLEAMKLGKPVLAVNNGGPLETIKSyvaGENessatGWLKPAVPIQWATAIDESRKILQN 400
Cdd:cd03817 273 YYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVED---GEN-----GFLFEPNDETLAEKLLHLRENLEL 344
|
250 260 270
....*....|....*....|....*....|
gi 6321373 401 GSVnFERNGPLRVKKYFSREAmTQSFEENV 430
Cdd:cd03817 345 LRK-LSKNAEISAREFAFAKS-VEKLYEEV 372
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
157-428 |
2.81e-07 |
|
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: 52.74 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 157 FSVSAADTVVVNSNFTKNTFHQTFKyLSNDPDVIYPCVDLS---TIEIEDIDKKFFKTvfnEGDRFYLSINRFEKKKDVA 233
Cdd:cd04962 137 FSINKSDRVTAVSSSLRQETYELFD-VDKDIEVIHNFIDEDvfkRKPAGALKRRLLAP---PDEKVVIHVSNFRPVKRID 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 234 LAIKAFALSEDQINdnVKLVICGGYDERVaenveylkELQSLADEYELSHTTIYYQEIKRVSDLESFktnnskiifltsi 313
Cdd:cd04962 213 DVVRVFARVRRKIP--AKLLLVGDGPERV--------PAEELARELGVEDRVLFLGKQDDVEELLSI------------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 314 sSSLKELLLERtemllytpayEHFGIVPLEAMKLGKPVLAVNNGGPLETIKsyvagENEssaTGWLKPAVPIQWATaiDE 393
Cdd:cd04962 270 -ADLFLLPSEK----------ESFGLAALEAMACGVPVVSSNAGGIPEVVK-----HGE---TGFLSDVGDVDAMA--KS 328
|
250 260 270
....*....|....*....|....*....|....*..
gi 6321373 394 SRKILQNGSV--NFERNGPLRVKKYFSREAMTQSFEE 428
Cdd:cd04962 329 ALSILEDDELynRMGRAARKRAAERFDPERIVPQYEA 365
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
195-383 |
5.50e-07 |
|
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: 51.55 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 195 DLSTIEIEDIDKKFFKtvfNEGDRFYLS-INRFEKKKDVALAIKAFALSEDQINDnVKLVICGGydervaenveylkelq 273
Cdd:cd03792 177 DLSPADIRYYLEKPFV---IDPERPYILqVARFDPSKDPLGVIDAYKLFKRRAEE-PQLVICGH---------------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 274 SLADEYELShttIYYQEIKRVSDLesfktnnSKIIFLTSISSSLKEL--LLERTEMLLYTPAYEHFGIVPLEAMKLGKPV 351
Cdd:cd03792 237 GAVDDPEGS---VVYEEVMEYAGD-------DHDIHVLRLPPSDQEInaLQRAATVVLQLSTREGFGLTVSEALWKGKPV 306
|
170 180 190
....*....|....*....|....*....|..
gi 6321373 352 LAVNNGGpletIKSYVagenESSATGWLKPAV 383
Cdd:cd03792 307 IATPAGG----IPLQV----IDGETGFLVNSV 330
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
227-400 |
7.80e-07 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 48.28 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 227 EKKKDVALAIKAFALSEDQiNDNVKLVICGGYDERvaenveylkELQSLADEYElshttiyyqeikrvsdlesfktnnSK 306
Cdd:pfam13692 12 PNVKGVDYLLEAVPLLRKR-DNDVRLVIVGDGPEE---------ELEELAAGLE------------------------DR 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 307 IIFLTSISSslKELLLERTEMLLYTPAYEHFGIVPLEAMKLGKPVLAVNNGGPLETIKsyvaGENessatGWL-KPAVPI 385
Cdd:pfam13692 58 VIFTGFVED--LAELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVD----GEN-----GLLvPPGDPE 126
|
170
....*....|....*
gi 6321373 386 QWATAIdesRKILQN 400
Cdd:pfam13692 127 ALAEAI---LRLLED 138
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
9-433 |
8.48e-07 |
|
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: 50.75 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 9 IAFIHPDLG------IGGAERLVVDAALGLQQQGHSVIIYTSHCDKSHCfeevkngQLkVEVYGDFLPTNFLGRFFIVFA 82
Cdd:cd03802 2 IAQVSPPRGpvppgkYGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSA-------PL-VAVIPRALRLDPIPQESKLAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 83 tirqlylvIQLILQKKVNAYQLIIIdqlstcipllHIfssatlmfycHFPDQLLAQrAGLLKKiyrlPFDLIEQFSVSAA 162
Cdd:cd03802 74 --------LLEALEVQLRASDFDVI----------HN----------HSYDWLPPF-APLIGT----PFVTTLHGPSIPP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 163 dtvvvNSNFTKNTFHQTFKYLSNDPDVIYPCVDLSTIEIEDIDKKFFKTVFNEGDrFYLSINRFEKKKDVALAIKAFALS 242
Cdd:cd03802 121 -----SLAIYAAEPPVNYVSISDAQRAATPPIDYLTVVHNGLDPADYRFQPDPED-YLAFLGRIAPEKGLEDAIRVARRA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 243 edqindNVKLVICGGYDERvaenvEYLKELQSLADEyelshttiyyqeikrvsdlesfktnnSKIIFLTSISSSLKELLL 322
Cdd:cd03802 195 ------GLPLKIAGKVRDE-----DYFYYLQEPLPG--------------------------PRIEFIGEVGHDEKQELL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 323 ERTEMLLYTPAY-EHFGIVPLEAMKLGKPVLAVNNGGPLETIKSYVagenessaTGWLKPAVP--IQWATAIDE-SRKIL 398
Cdd:cd03802 238 GGARALLFPINWdEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGE--------TGFLVDSVEemAEAIANIDRiDRAAC 309
|
410 420 430
....*....|....*....|....*....|....*
gi 6321373 399 QngsvnferngpLRVKKYFSREAMTQSFEENVEKV 433
Cdd:cd03802 310 R-----------RYAEDRFSAARMADRYEALYRKV 333
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
221-369 |
1.01e-06 |
|
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: 50.84 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 221 LSINRFEKKKDVALAIKAFALSEDQINDnVKLVICGGYDERVAenVEYLKELQSLADEYELsHTTIYYQEIKRVsdlesf 300
Cdd:cd03798 204 LFVGRLIPRKGIDLLLEAFARLAKARPD-VVLLIVGDGPLREA--LRALAEDLGLGDRVTF-TGRLPHEQVPAY------ 273
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321373 301 kTNNSKIIFLTSISsslkelllertemllytpayEHFGIVPLEAMKLGKPVLAVNNGGPLETIKSYVAG 369
Cdd:cd03798 274 -YRACDVFVLPSRH--------------------EGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETG 321
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
9-364 |
1.58e-06 |
|
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: 50.29 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 9 IAFIHpdLGIGGAERLVVDAALGLQQQGHSVIIYTShcdkshcfeEVKNGQLKVEVYG-DFLPTNFLGRFFIVFATIRQL 87
Cdd:cd03808 2 ILFIV--NVDGGFQSFRLPLIKALVKKGYEVHVIAP---------DGDKLSDELKELGvKVIDIPILRRGINPLKDLKAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 88 YLVIQLIlqKKVNaYQLIIidqLSTCIPLLH-----IFSSATLMFY------CHFPDQllaqraGLLKKIYRLpfdlIEQ 156
Cdd:cd03808 71 FKLYKLL--KKEK-PDIVH---CHTPKPGILgrlaaRLAGVPKVIYtvhglgFVFTEG------KLLRLLYLL----LEK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 157 FSVSAADTVVVNSNFTKNTFHQTFKYLSNDPDVIYPC-VDLSTIE--IEDIDKKFFKTVFnegdrfylsINRFEKKKDVA 233
Cdd:cd03808 135 LALLFTDKVIFVNEDDRDLAIKKGIIKKKKTVLIPGSgVDLDRFQysPESLPSEKVVFLF---------VARLLKDKGID 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 234 LAIKAFALsEDQINDNVKLVICGGYDERvaenveylKELQSLADEYELSHTTIYYqeiKRVSDLESFkTNNSKIIFLTSI 313
Cdd:cd03808 206 ELIEAAKI-LKKKGPNVRFLLVGDGELE--------NPSEILIEKLGLEGRIEFL---GFRSDVPEL-LAESDVFVLPSY 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 6321373 314 ssslkelllertemllytpaYEHFGIVPLEAMKLGKPVLAVNNGGPLETIK 364
Cdd:cd03808 273 --------------------REGLPRSLLEAMAAGRPVITTDVPGCRELVI 303
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
19-352 |
2.94e-06 |
|
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: 49.29 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 19 GGAERLVVDAALGLQQQGHSVIIYTshcdkshcfeevkngqlkvevYGDF---LPTNFLGRFFIVFATIRQLYLVIQLIL 95
Cdd:cd03821 14 GGPVKVVLRLAAALAALGHEVTIVS---------------------TGDGyesLVVEENGRYIPPQDGFASIPLLRQGAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 96 QKKVNAYQLIIIDQLSTCIPLLHI------FSSATLMF-------YCHFP----DQLLAQRAGLLKKIYRLpfdLIEQFS 158
Cdd:cd03821 73 RTDFSPGLPNWLRRNLREYDVVHIhgvwtyTSLAACKLarrrgipYVVSPhgmlDPWALQQKHWKKRIALH---LIERRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 159 VSAADTVVVNSnfTKNTFHQTFKYLSNDPDVIYPCVDLSTIEIEDIDKKFFKTVfnEGDRFYLSINRFEKKKDVALAIKA 238
Cdd:cd03821 150 LNNAALVHFTS--EQEADELRRFGLEPPIAVIPNGVDIPEFDPGLRDRRKHNGL--EDRRIILFLGRIHPKKGLDLLIRA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 239 FALSEDQINDnVKLVICGgYDERvaenvEYLKELQSLADeyelshttiyyqeikrvsdlesfKTNNSKIIFLTSISSSLK 318
Cdd:cd03821 226 ARKLAEQGRD-WHLVIAG-PDDG-----AYPAFLQLQSS-----------------------LGLGDRVTFTGPLYGEAK 275
|
330 340 350
....*....|....*....|....*....|....
gi 6321373 319 ELLLERTEMLLYTPAYEHFGIVPLEAMKLGKPVL 352
Cdd:cd03821 276 WALYASADLFVLPSYSENFGNVVAEALACGLPVV 309
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
9-366 |
3.43e-05 |
|
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: 45.90 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 9 IAFIHPDLGIGGAERLVVDAALGLQQQGHSV-IIYTSHCDkshcfeEVKNGQLKVEVYGDFLPTNFLGrffivfatirql 87
Cdd:cd04951 2 ILYVITGLGLGGAEKQTVLLADQMFIRGHDVnIVYLTGEV------EVKPLNNNIIIYNLGMDKNPRS------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 88 yLVIQLILQKKvnayqliIIDQLSTCIPLLHIFSSATL--MFYCHFPDQLLAQRA------GLLK-KIYRLPFDLieqfs 158
Cdd:cd04951 64 -LLKALLKLKK-------IISAFKPDVVHSHMFHANIFarFLRMLYPIPLLICTAhnknegGRIRmFIYRLTDFL----- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 159 vSAADTVVVNSNFTKNTFHQTFKYLSNDPdvIYPCVDLSTIEIEDIDKKFFKTVFN--EGDRFYLSINRFEKKKDVALAI 236
Cdd:cd04951 131 -CDITTNVSREALDEFIAKKAFSKNKSVP--VYNGIDLNKFKKDINVRLKIRNKLNlkNDEFVILNVGRLTEAKDYPNLL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 237 KAFaLSEDQINDNVKLVICGGYDERvaenveylKELQSLADEYELSHTTIYYQEIKRVSDLesfkTNNSKIIFLTSisss 316
Cdd:cd04951 208 LAI-SELILSKNDFKLLIAGDGPLR--------NELERLICNLNLVDRVILLGQISNISEY----YNAADLFVLSS---- 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 6321373 317 lkelllertemllytpAYEHFGIVPLEAMKLGKPVLAVNNGGPLETIKSY 366
Cdd:cd04951 271 ----------------EWEGFGLVVAEAMACERPVVATDAGGVAEVVGDH 304
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
165-432 |
7.25e-05 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 45.17 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 165 VVVNSNFTKNtFHQtfKYLSNDPDVIYP-CVDLSTIEIEDIDKKFFKTVFNEGDRFYLSINRFEKKKDVALAIKAF-ALS 242
Cdd:PRK15484 143 IIVPSQFLKK-FYE--ERLPNADISIVPnGFCLETYQSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFeKLA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 243 EDQinDNVKLVICGGY-DERVAENVEYLKELQSLADEY------------ELSHTtiYYqeikRVSDLesfktnnskiif 309
Cdd:PRK15484 220 TAH--SNLKLVVVGDPtASSKGEKAAYQKKVLEAAKRIgdrcimlggqppEKMHN--YY----PLADL------------ 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 310 lTSISSSLKElllertemllytpayeHFGIVPLEAMKLGKPVLAVNNGGPLETIKsyvagENEssaTGWlKPAVPIQWAT 389
Cdd:PRK15484 280 -VVVPSQVEE----------------AFCMVAVEAMAAGKPVLASTKGGITEFVL-----EGI---TGY-HLAEPMTSDS 333
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 6321373 390 AIDESRKILQNGSV-NFERNGPLRVKKYFSREAMTQSFEENVEK 432
Cdd:PRK15484 334 IISDINRTLADPELtQIAEQAKDFVFSKYSWEGVTQRFEEQIHN 377
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
332-369 |
1.24e-03 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 41.50 E-value: 1.24e-03
10 20 30
....*....|....*....|....*....|....*....
gi 6321373 332 PA-YEHFGIVPLEAMKLGKPVLAVNNGGPLETIKSYVAG 369
Cdd:PLN00142 673 PAlYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSG 711
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
335-418 |
4.21e-03 |
|
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: 39.24 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321373 335 EHFGIVPLEAMKLGKPVLAVNNGGPLETIKsyvageneSSATGWLKP-------AVPIQWATAIDESRKILQNGS---VN 404
Cdd:cd03825 274 DNLPNTLLEAMACGTPVVAFDTGGSPEIVQ--------HGVTGYLVPpgdvqalAEAIEWLLANPKERESLGERAralAE 345
|
90
....*....|....
gi 6321373 405 FERNGPLRVKKYFS 418
Cdd:cd03825 346 NHFDQRVQAQRYLE 359
|
|
| |
