|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
2-443 |
6.68e-54 |
|
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: 184.07 E-value: 6.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 2 KILLVNKYFY--RKGGAETYFFALAEGLKSLGHEVAFFSMqhpNNEPSYWSKYFVSeKDYVGKISAFQQAKEAATLIYSL 79
Cdd:cd03823 1 KILLVNSLYPpqRVGGAEISVHDLAEALVAEGHEVAVLTA---GVGPPGQATVARS-VVRYRRAPDETLPLALKRRGYEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 80 ES------KRKFEALLEEFQPDVIHMNNVhRQLTLSILDApyLKKHRVPVVYTAHDYILLCPAYTMVDGNGkvcddcldr 153
Cdd:cd03823 77 FEtynpglRRLLARLLEDFRPDVVHTHNL-SGLGASLLDA--ARDLGIPVVHTLHDYWLLCPRQFLFKKGG--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 154 rfihavkktcvkgskaksglafleaeflkhhhsydkiDKIIAPSEFMKSKLDEGGYAG-RTVAMQNFLTtsqmdMAHKVT 232
Cdd:cd03823 145 -------------------------------------DAVLAPSRFTANLHEANGLFSaRISVIPNAVE-----PDLAPP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 233 NTDKFNTVDPYFLFFGRLSKEKGILTLVKAFLQaagllplagaveqsetegghlvanCLPSNWTLHIVGDGPERQtieml 312
Cdd:cd03823 183 PRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKR------------------------LPREDIELVIAGHGPLSD----- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 313 IKSAgsEAENRIKLLGYKTGENLQREVGNARFSVLCSEWRENMPYSGLESLAAQTPVIGANIGGIPELVVEGETGFKFES 392
Cdd:cd03823 234 ERQI--EGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAP 311
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1540018338 393 GNQDDLARTLTKAAQvDAGRYASMQEScgryVEERCRQDMYVRQLEDVYRG 443
Cdd:cd03823 312 GDAEDLAAAMRRLLT-DPALLERLRAG----AEPPRSTESQAEEYLKLYRD 357
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-442 |
1.41e-47 |
|
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: 167.71 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 2 KILLV-NKYFYRKGGAETYFFALAEGLKSLGHEVAFFSMQHPNNEPSYWSKYFVSEKDYVGKIsafqqAKEAATLIysle 80
Cdd:cd03801 1 KILLLsPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAA-----LLRARRLL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 81 skRKFEALLEEFQPDVIHMNNVHrqltLSILDAPYLKKHRVPVVYTAHDYILLCPAYTMVDgngkvcddclDRRFIHAVK 160
Cdd:cd03801 72 --RELRPLLRLRKFDVVHAHGLL----AALLAALLALLLGAPLVVTLHGAEPGRLLLLLAA----------ERRLLARAE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 161 KTcvkgskaksglafleaeflkhhhsYDKIDKIIAPSEFMKSKLDE--GGYAGRTVAMQNFLTTSQMDMAHKVTNTDKFN 238
Cdd:cd03801 136 AL------------------------LRRADAVIAVSEALRDELRAlgGIPPEKIVVIPNGVDLERFSPPLRRKLGIPPD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 239 tvDPYFLFFGRLSKEKGILTLVKAFLQAAGLLPlagaveqsetegghlvanclpsNWTLHIVG-DGPERQTIEMLIKsag 317
Cdd:cd03801 192 --RPVLLFVGRLSPRKGVDLLLEALAKLLRRGP----------------------DVRLVIVGgDGPLRAELEELEL--- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 318 sEAENRIKLLGYKTGENLQREVGNARFSVLCSEWrENMPYSGLESLAAQTPVIGANIGGIPELVVEGETGFKFESGNQDD 397
Cdd:cd03801 245 -GLGDRVRFLGFVPDEELPALYAAADVFVLPSRY-EGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEA 322
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1540018338 398 LARTLTKAAQvDAGRYASMQESCGRYVEERCRQDMYVRQLEDVYR 442
Cdd:cd03801 323 LADALLRLLA-DPELRARLGRAARERVAERFSWERVAERLLDLYR 366
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
2-430 |
7.55e-35 |
|
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: 132.87 E-value: 7.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 2 KILLVNkYFYRKGGAETYFFALAEGLKSLGHEVAFFSMQHPNNEPSYWSKYFvsekdyvgKISAFQQAKEAATLIYSLES 81
Cdd:cd03811 1 KILFVI-PSLSGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDV--------KLIRLLIRVLKLIKLGLLKA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 82 KRKFEALLEEFQPDVIHmnnVHRQLTLSILDApyLKKHRVPVVYTAHDYillcpaytmvdgngkvcddcldrrFIHAVKk 161
Cdd:cd03811 72 ILKLKRILKRAKPDVVI---SFLGFATYIVAK--LAAARSKVIAWIHSS------------------------LSKLYY- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 162 tcvkgSKAKSGLAFLeaeflkhhhSYDKIDKIIAPSEFMKSKLDEGGYAG--RTVAMQNFLTTSQM-DMAHKVTNTDKFN 238
Cdd:cd03811 122 -----LKKKLLLKLK---------LYKKADKIVCVSKGIKEDLIRLGPSPpeKIEVIYNPIDIDRIrALAKEPILNEPED 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 239 TvdPYFLFFGRLSKEKGILTLVKAFlqaagllplagaveqseteggHLVANCLPsNWTLHIVGDGPERQTIEMLIKSAGs 318
Cdd:cd03811 188 G--PVILAVGRLDPQKGHDLLIEAF---------------------AKLRKKYP-DVKLVILGDGPLREELEKLAKELG- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 319 eAENRIKLLGYKTgeNLQREVGNARFSVLCSEWrENMPYSGLESLAAQTPVIGANIGGIPELVVEGETGFKFESGNQDDL 398
Cdd:cd03811 243 -LAERVIFLGFQS--NPYPYLKKADLFVLSSRY-EGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAAL 318
|
410 420 430
....*....|....*....|....*....|..
gi 1540018338 399 ARTLTKAAQvDAGRYASMQEsCGRYVEERCRQ 430
Cdd:cd03811 319 AGILAALLQ-KKLDAALRER-LAKAQEAVFRE 348
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
2-441 |
6.35e-26 |
|
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: 108.52 E-value: 6.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 2 KILLVNKYFY-RKGGAETYFFALAEGLKSLGHEVAFFSMQHPNNEPsywskyfvsEKDYVGKISAFQQAKEAATLIYSLE 80
Cdd:cd03817 1 KIAIFTDTYLpQVNGVATSVRNLARALEKRGHEVYVITPSDPGAED---------EEEVVRYRSFSIPIRKYHRQHIPFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 81 SKRKFEALLEEFQPDVIHmnnVHRQLTLSILDAPYLKKHRVPVVYTAH----DYillcpAYTMVDGNGKVcddcldrrfi 156
Cdd:cd03817 72 FKKAVIDRIKELGPDIIH---THTPFSLGKLGLRIARKLKIPIVHTYHtmyeDY-----LHYIPKGKLLV---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 157 havkktcvkgskaKSGLAFLEAEFlkhhhsYDKIDKIIAPSEFMKSKLDEGGYAGRTVAMQNFLttsQMDMAHKVTNTDK 236
Cdd:cd03817 134 -------------KAVVRKLVRRF------YNHTDAVIAPSEKIKDTLREYGVKGPIEVIPNGI---DLDKFEKPLNTEE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 237 FNTV-----DPYFLFFGRLSKEKGILTLVKAFlqaAGLLPLAGAveqsetegghlvanclpsnwTLHIVGDGPERQTIEM 311
Cdd:cd03817 192 RRKLglppdEPILLYVGRLAKEKNIDFLLRAF---AELKKEPNI--------------------KLVIVGDGPEREELKE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 312 LIKSAGSEAenRIKLLGY----KTGENLQRevgnARFSVLCSEwRENMPYSGLESLAAQTPVIGANIGGIPELVVEGETG 387
Cdd:cd03817 249 LARELGLAD--KVIFTGFvpreELPEYYKA----ADLFVFAST-TETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENG 321
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1540018338 388 FKFESGNqDDLARTLTKAAQvDAGRYASMQESCgryvEERCRQDMYVRQLEDVY 441
Cdd:cd03817 322 FLFEPND-ETLAEKLLHLRE-NLELLRKLSKNA----EISAREFAFAKSVEKLY 369
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
3-431 |
1.36e-25 |
|
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: 107.06 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 3 ILLVNkYFYRKGGAETYFFALAEGLKSLGHEVAFFSMQHPNNEPsyWSKYFVSEKDYVGKISAFqqakeaatliysLESK 82
Cdd:cd03819 1 ILMLT-PALEIGGAETYILDLARALAERGHRVLVVTAGGPLLPR--LRQIGIGLPGLKVPLLRA------------LLGN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 83 RKFEALLEEFQPDVIHMNnvHRQLTLSILDApyLKKHRVPVVYTAHDyillcpaytmvdgngkvcddcldRRFIHAVKKT 162
Cdd:cd03819 66 VRLARLIRRERIDLIHAH--SRAPAWLGWLA--SRLTGVPLVTTVHG-----------------------SYLATYHPKD 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 163 CVKGSKAKsglafleaeflkhhhsydkIDKIIAPSEFMKSKLDEGGYA--GRTVAMQNFLTTSQMDMAHKVTNTDKFNTV 240
Cdd:cd03819 119 FALAVRAR-------------------GDRVIAVSELVRDHLIEALGVdpERIRVIPNGVDTDRFPPEAEAEERAQLGLP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 241 D--PYFLFFGRLSKEKGILtlvkAFLQAAGLLPLAGaveqsetegghlvanclpsNWTLHIVGDGPERQTIEMLIKSAGs 318
Cdd:cd03819 180 EgkPVVGYVGRLSPEKGWL----LLVDAAAELKDEP-------------------DFRLLVAGDGPERDEIRRLVERLG- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 319 eAENRIKLLGYKtgENLQREVGNARFSVLCSEwRENMPYSGLESLAAQTPVIGANIGGIPELVVEGETGFKFESGNQDDL 398
Cdd:cd03819 236 -LRDRVTFTGFR--EDVPAALAASDVVVLPSL-HEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEAL 311
|
410 420 430
....*....|....*....|....*....|....*
gi 1540018338 399 ARTLtKAAQVDAGRYASMQE--SCGRYVEERCRQD 431
Cdd:cd03819 312 ADAI-RAAKLLPEAREKLQAaaALTEAVRELLLRV 345
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
2-404 |
5.70e-25 |
|
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: 105.37 E-value: 5.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 2 KIL-LVNKYfyrkGGAETYFFALAEGLKSLGHEVAFFSMQHPN--NEPSYWSKYFVSEKDYVGKISAFQQakeaatlIYS 78
Cdd:cd03808 1 KILfIVNVD----GGFQSFRLPLIKALVKKGYEVHVIAPDGDKlsDELKELGVKVIDIPILRRGINPLKD-------LKA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 79 LESKRKfeaLLEEFQPDVIHMN----NVhrqltLSILDApyLKKHRVPVVYTAHDYillcpAYTMVdgngkvcddcldrr 154
Cdd:cd03808 70 LFKLYK---LLKKEKPDIVHCHtpkpGI-----LGRLAA--RLAGVPKVIYTVHGL-----GFVFT-------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 155 fihavkktcvKGSKAKSGLAFLEAEFLKHHhsydkiDKIIAPSEFMKSKL-DEGGYAGRTVAMqnfLTTSQMDMAHKVTN 233
Cdd:cd03808 121 ----------EGKLLRLLYLLLEKLALLFT------DKVIFVNEDDRDLAiKKGIIKKKKTVL---IPGSGVDLDRFQYS 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 234 TDKFNTVDPYFLFFGRLSKEKGILTlvkaFLQAAGLLPLAGaveqsetegghlvanclpSNWTLHIVGDGPERQTIEMLI 313
Cdd:cd03808 182 PESLPSEKVVFLFVARLLKDKGIDE----LIEAAKILKKKG------------------PNVRFLLVGDGELENPSEILI 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 314 KSAGseAENRIKLLGYKtgENLQREVGNARFSVLCSEWrENMPYSGLESLAAQTPVIGANIGGIPELVVEGETGFKFESG 393
Cdd:cd03808 240 EKLG--LEGRIEFLGFR--SDVPELLAESDVFVLPSYR-EGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPG 314
|
410
....*....|.
gi 1540018338 394 NQDDLARTLTK 404
Cdd:cd03808 315 DVEALADAIEK 325
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
241-405 |
1.54e-24 |
|
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: 99.27 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 241 DPYFLFFGRLSKEKGILTLVKAFlqaaGLLPLAGaveqsetegghlvanclpSNWTLHIVGDGPERQTIEMLIKSAGseA 320
Cdd:pfam00534 2 KKIILFVGRLEPEKGLDLLIKAF----ALLKEKN------------------PNLKLVIAGDGEEEKRLKKLAEKLG--L 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 321 ENRIKLLGYKTGENLQREVGNARFSVLCSEWrENMPYSGLESLAAQTPVIGANIGGIPELVVEGETGFKFESGNQDDLAR 400
Cdd:pfam00534 58 GDNVIFLGFVSDEDLPELLKIADVFVLPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAE 136
|
....*
gi 1540018338 401 TLTKA 405
Cdd:pfam00534 137 AIDKL 141
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
3-427 |
7.39e-24 |
|
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: 102.46 E-value: 7.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 3 ILLVNKYF--YRKGGAETYFFALAEGLKSLGHEVAFFSMQHPNNEP-SYWSKYFVSEKDYVGKISAF--------QQAKE 71
Cdd:cd03798 1 VLILTNIYpnANSPGRGIFVRRQVRALSRRGVDVEVLAPAPWGPAAaRLLRKLLGEAVPPRDGRRLLplkprlrlLAPLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 72 AATLIYSLESKRKFealleefQPDVIHMNNVHRQLTLSILDApylKKHRVPVVYTAHdyillcpaytmvdgngkvCDDCL 151
Cdd:cd03798 81 APSLAKLLKRRRRG-------PPDLIHAHFAYPAGFAAALLA---RLYGVPYVVTEH------------------GSDIN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 152 DRRFIHAVKKTCVKGskaksglafleaeflkhhhsYDKIDKIIAPSEFMKSKLDE-GGYAGRTVAMQNFLTT---SQMDM 227
Cdd:cd03798 133 VFPPRSLLRKLLRWA--------------------LRRAARVIAVSKALAEELVAlGVPRDRVDVIPNGVDParfQPEDR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 228 AHKVtNTDKFntvdpYFLFFGRLSKEKGILTLVKAFLQAAGLLPlagaveqseteggHLVanclpsnwtLHIVGDGPERQ 307
Cdd:cd03798 193 GLGL-PLDAF-----VILFVGRLIPRKGIDLLLEAFARLAKARP-------------DVV---------LLIVGDGPLRE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 308 TIEMLIKSAGseAENRIKLLGYKTGENLQREVGNARFSVLCSeWRENMPYSGLESLAAQTPVIGANIGGIPELVVEGETG 387
Cdd:cd03798 245 ALRALAEDLG--LGDRVTFTGRLPHEQVPAYYRACDVFVLPS-RHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETG 321
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1540018338 388 FKFESGNQDDLARTLTKAAQVDAGRyASMQESCGRYVEER 427
Cdd:cd03798 322 LLVPPGDADALAAALRRALAEPYLR-ELGEAARARVAERF 360
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
2-414 |
1.22e-22 |
|
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: 98.46 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 2 KILLVNKYFYRKGGAETYFFALAEGLKSLGHEVAFFSMqHPNNEPSYwskYFVSEKDyvgKISAFQQAKEAA--TLIYSL 79
Cdd:cd03820 1 KIAIVIPSISNAGGAERVAINLANHLAKKGYDVTIISL-DSAEKPPF---YELDDNI---KIKNLGDRKYSHfkLLLKYF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 80 ESKRKFEALLEEFQPDVIhMNNVHRQLT-LSILDapyLKKHRVPVVYTAHDYILLcpaytmvdgngkvcddclDRRFIHA 158
Cdd:cd03820 74 KKVRRLRKYLKNNKPDVV-ISFRTSLLTfLALIG---LKSKLIVWEHNNYEAYNK------------------GLRRLLL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 159 VKKTcvkgskaksglafleaeflkhhhsYDKIDKIIAPSEFMKSKLDEGGYAgRTVAMQNFLTTSQMDMAHKVTNTdkfn 238
Cdd:cd03820 132 RRLL------------------------YKRADKIVVLTEADKLKKYKQPNS-NVVVIPNPLSFPSEEPSTNLKSK---- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 239 tvdpYFLFFGRLSKEKGILTLVKAFlqaagllplagaveqseteggHLVANCLPsNWTLHIVGDGPERQTIEMLIKSAGs 318
Cdd:cd03820 183 ----RILAVGRLTYQKGFDLLIEAW---------------------ALIAKKHP-DWKLRIYGDGPEREELEKLIDKLG- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 319 eAENRIKLLGykTGENLQREVGNARFSVLCSEWrENMPYSGLESLAAQTPVIGANI-GGIPELVVEGETGFKFESGNQDD 397
Cdd:cd03820 236 -LEDRVKLLG--PTKNIAEEYANSSIFVLSSRY-EGFPMVLLEAMAYGLPIISFDCpTGPSEIIEDGENGLLVPNGDVDA 311
|
410 420 430
....*....|....*....|....*....|
gi 1540018338 398 LARTL-------------TKAAQVDAGRYA 414
Cdd:cd03820 312 LAEALlrlmedeelrkkmGKNARKNAERFS 341
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
242-404 |
6.30e-21 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 88.34 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 242 PYFLFFGRLSKE-KGILTLVKAFlqaagllplagaveqseteggHLVANClPSNWTLHIVGDGPERQtiemlIKSAGSEA 320
Cdd:pfam13692 2 PVILFVGRLHPNvKGVDYLLEAV---------------------PLLRKR-DNDVRLVIVGDGPEEE-----LEELAAGL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 321 ENRIKLLGYKtgENLQREVGNARFSVLCSEWrENMPYSGLESLAAQTPVIGANIGGIPElVVEGETGFKFESGNQDDLAR 400
Cdd:pfam13692 55 EDRVIFTGFV--EDLAELLAAADVFVLPSLY-EGFGLKLLEAMAAGLPVVATDVGGIPE-LVDGENGLLVPPGDPEALAE 130
|
....
gi 1540018338 401 TLTK 404
Cdd:pfam13692 131 AILR 134
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
242-442 |
5.99e-20 |
|
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: 90.42 E-value: 5.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 242 PYFLFFGRLSKEKGILTLVKAFLQAagllplagaveqsetegghlvanclpsNWTLHIVGDGPERQTIEMLIKSAGSEae 321
Cdd:cd03802 170 DYLAFLGRIAPEKGLEDAIRVARRA---------------------------GLPLKIAGKVRDEDYFYYLQEPLPGP-- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 322 nRIKLLGYKTGENLQREVGNARFSVLCSEWREnmPYsGL---ESLAAQTPVIGANIGGIPELVVEGETGFKfeSGNQDDL 398
Cdd:cd03802 221 -RIEFIGEVGHDEKQELLGGARALLFPINWDE--PF-GLvmiEAMACGTPVIAYRRGGLPEVIQHGETGFL--VDSVEEM 294
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1540018338 399 ARTLTKAAQVDagRYAsmqesCGRYVEERCRQDMYVRQLEDVYR 442
Cdd:cd03802 295 AEAIANIDRID--RAA-----CRRYAEDRFSAARMADRYEALYR 331
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
2-442 |
7.17e-20 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340842 [Multi-domain] Cd Length: 365 Bit Score: 90.82 E-value: 7.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 2 KILLV-NKYFYRKGGAETYFFALAEGLKSLGHEVAFFSmqhPnnEPSYWSKYFVSEKDYVGKISAFqqakEAATLIYSLE 80
Cdd:cd03814 1 RIALVtDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVA---P--GPFDEAESAEGRVVSVPSFPLP----FYPEYRLALP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 81 SKRKFEALLEEFQPDVIHmnnVHRQLTLSILDAPYLKKHRVPVVYTAHDYIllcPAYtmvdgngkvcddcLDRRfihavk 160
Cdd:cd03814 72 LPRRVRRLIKEFQPDIIH---IATPGPLGLAALRAARRLGLPVVTSYHTDF---PEY-------------LSYY------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 161 ktcvkgskaksGLAFLEA---EFLKHHHsyDKIDKIIAPSEFMKSKLDEGGYA-----GRTVamqnflttsqmdmahkvt 232
Cdd:cd03814 127 -----------TLGPLSWlawAYLRWFH--NPFDTTLVPSPSIARELEGHGFErvrlwPRGV------------------ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 233 NTDKFN--------------TVDPYFLFFGRLSKEKGILTLVKAFLQAAGLLPLagaveqseteggHLVanclpsnwtlh 298
Cdd:cd03814 176 DTELFHpsrrdaalrrrlgpPGRPLLLYVGRLAPEKNLEALLDADLPLAASPPV------------RLV----------- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 299 IVGDGPERQTIEmlikSAGSEAenriKLLGYKTGENLQREVGNARFSVLCSEwRENMPYSGLESLAAQTPVIGANIGGIP 378
Cdd:cd03814 233 VVGDGPARAELE----ARGPDV----IFTGFLTGEELARAYASADVFVFPSR-TETFGLVVLEAMASGLPVVAADAGGPR 303
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540018338 379 ELVVEGETGFKFESGNQDDLARTLTKAAQvDAGRYASMQESCGRYVEERCrQDMYVRQLEDVYR 442
Cdd:cd03814 304 DIVRPGGTGALVEPGDAAAFAAALRALLE-DPELRRRMAARARAEAERYS-WEAFLDNLLDYYA 365
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
2-442 |
7.23e-20 |
|
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: 90.84 E-value: 7.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 2 KILLVNKYFYRkGGAETYFFALAEGLKSLGHEVAFFSMQHP----NNEPSYWSKYFVSEKDYVGKISAFQQAKeaatliy 77
Cdd:cd03807 1 KVAHVITGLNV-GGAETMLLRLLEHMDKSRFEHVVISLTGDgvlgEELLAAGVPVVCLGLSSGKDPGVLLRLA------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 78 sleskrkfeALLEEFQPDVIHMNNVHRQLtLSILDAPYLKKhrVPVVYTAHDyiLLCPAYTMVdgngkvcddcldrrfih 157
Cdd:cd03807 73 ---------KLIRKRNPDVVHTWMYHADL-IGGLAAKLAGG--VKVIWSVRS--SNIPQRLTR----------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 158 AVKKTCVKGSKAksglafleaeflkhhhsydkIDKIIAPSEFMKSKLDEGGYA-GRTVAMQNF--LTTSQMDMAHKVTNT 234
Cdd:cd03807 122 LVRKLCLLLSKF--------------------SPATVANSSAVAEFHQEQGYAkNKIVVIYNGidLFKLSPDDASRARAR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 235 DKFNTVDPYFLF--FGRLSKEKGILTLVKAFLQaagllplagaveqsetegghLVANClpSNWTLHIVGDGPERQTIEML 312
Cdd:cd03807 182 RRLGLAEDRRVIgiVGRLHPVKDHSDLLRAAAL--------------------LVETH--PDLRLLLVGRGPERPNLERL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 313 IKSAGseAENRIKLLGYktGENLQREVGNARFSVLCSEwRENMPYSGLESLAAQTPVIGANIGGIPELVVEGeTGFKFES 392
Cdd:cd03807 240 LLELG--LEDRVHLLGE--RSDVPALLPAMDIFVLSSR-TEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPA 313
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1540018338 393 GNQDDLARTLTKAAQVDAGRyASMQESCGRYVEERCRQDMYVRQLEDVYR 442
Cdd:cd03807 314 GDPQALADAIRALLEDPEKR-ARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
341-442 |
5.61e-19 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 82.35 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 341 NARFSVLCSEWrENMPYSGLESLAAQTPVIGANIGGIPELVVEGETGFKFESGNQDDLARTLTKAAQvDAGRYASMQESC 420
Cdd:COG0438 20 AADVFVLPSRS-EGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLE-DPELRRRLGEAA 97
|
90 100
....*....|....*....|..
gi 1540018338 421 GRYVEERCRQDMYVRQLEDVYR 442
Cdd:COG0438 98 RERAEERFSWEAIAERLLALYE 119
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
285-442 |
9.40e-18 |
|
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: 84.33 E-value: 9.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 285 HLVANCLPSnwTLHIVGDGPERQTIEMLIKSAGseAENRIKLLGYKtgENLQREVGNARFSVLCSEwRENMPYSGLESLA 364
Cdd:cd04962 219 ARVRRKIPA--KLLLVGDGPERVPAEELARELG--VEDRVLFLGKQ--DDVEELLSIADLFLLPSE-KESFGLAALEAMA 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 365 AQTPVIGANIGGIPELVVEGETGFKFESGNQDDLARtltKAAQV--DAGRYASMQESCGRYVEERCRQDMYVRQLEDVYR 442
Cdd:cd04962 292 CGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAK---SALSIleDDELYNRMGRAARKRAAERFDPERIVPQYEAYYR 368
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-438 |
1.14e-17 |
|
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: 84.32 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 2 KILLVNKYFYR-KGGAETYFFALAEGLKSLGHEVAFFSmqHPNNEPSYWSKYFVSEKD-----------YVGKISAFQQA 69
Cdd:cd03794 1 KILLISQYYPPpKGAAAARVYELAKELVRRGHEVTVLT--PSPNYPLGRIFAGATETKdgirvirvklgPIKKNGLIRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 70 KEAATLIYSLESKRkfeaLLEEFQPDVIHMnnVHRQLTLSILDAPYLKKHRVPVVYTAHDYillcpaytMVDgngkvcdd 149
Cdd:cd03794 79 LNYLSFALAALLKL----LVREERPDVIIA--YSPPITLGLAALLLKKLRGAPFILDVRDL--------WPE-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 150 cldrrfiHAVKKTCVKGSKAKSGLAFLEaeflkhHHSYDKIDKIIAPSEFMKSKLDEGGYAGRTVA-------MQNFLTT 222
Cdd:cd03794 137 -------SLIALGVLKKGSLLKLLKKLE------RKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIvipnwadLEEFKPP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 223 SQMDMAHKVTNTDKFNtvdpyFLFFGRLSKEKGILTLVKAFLQAAGLlplagaveqsetegghlvanclpSNWTLHIVGD 302
Cdd:cd03794 204 PKDELRKKLGLDDKFV-----VVYAGNIGKAQGLETLLEAAERLKRR-----------------------PDIRFLFVGD 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 303 GPERQTIEMLIKSAGSeaeNRIKLLGYKTGENLQREVGNARFSVLCseWRENMPYSG------LESLAAQTPVIGANIGG 376
Cdd:cd03794 256 GDEKERLKELAKARGL---DNVTFLGRVPKEEVPELLSAADVGLVP--LKDNPANRGsspsklFEYMAAGKPILASDDGG 330
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540018338 377 IPELVVEGETGFKFESGNQDDLARTLTKAAQvDAGRYASMQESCGRYVEERCRQDMYVRQLE 438
Cdd:cd03794 331 SDLAVEINGCGLVVEPGDPEALADAILELLD-DPELRRAMGENGRELAEEKFSREKLADRLL 391
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
193-440 |
1.86e-17 |
|
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: 83.66 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 193 IIAPSEFMKSKLDEGGY-AGRTVamqnflttsqmdMAHKVTNTDKFNTVD-----PYFLFFGRLSKEKGILTLVKAFLQA 266
Cdd:cd05844 147 FVAVSGFIRDRLLARGLpAERIH------------VHYIGIDPAKFAPRDpaeraPTILFVGRLVEKKGCDVLIEAFRRL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 267 AGLLPLAGAVeqsetegghlvanclpsnwtlhIVGDGPERQTIEMLIKSAGseaenRIKLLGYKTGENLQREVGNARFSV 346
Cdd:cd05844 215 AARHPTARLV----------------------IAGDGPLRPALQALAAALG-----RVRFLGALPHAEVQDWMRRAEIFC 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 347 LCSEW-----RENMPYSGLESLAAQTPVIGANIGGIPELVVEGETGFKFESGNQDDLARTLtKAAQVDAGRYASMQESCG 421
Cdd:cd05844 268 LPSVTaasgdSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADAL-QALLADRALADRMGGAAR 346
|
250
....*....|....*....
gi 1540018338 422 RYVEERCRQDMYVRQLEDV 440
Cdd:cd05844 347 AFVCEQFDIRVQTAKLEAI 365
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
244-390 |
3.76e-14 |
|
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: 71.67 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 244 FLFFGRLSKEKGILTLVKAFLQAAGLLPlagaveqsetegghlvanclpsNWTLHIVGDGPERQTIEMLIKSAGseAENR 323
Cdd:cd01635 113 KVSVGRLVPEKGIDLLLEALALLKARLP----------------------DLVLVLVGGGGEREEEEALAAALG--LLER 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540018338 324 IKLLGYKTGENLQREVGNArfS--VLCSEWRENMPYSGLESLAAQTPVIGANIGGIPELVVEGETGFKF 390
Cdd:cd01635 169 VVIIGGLVDDEVLELLLAA--AdvFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
14-204 |
1.17e-13 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 68.71 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 14 GGAETYFFALAEGLKSLGHEVAFFSMQHPNNEPSYWSKYFVSEKDYVGKISAFQqakeaatliYSLESKRKFEALLEEFQ 93
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLL---------RSLAFLRRLRRLLRRER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 94 PDVIHmnnVHRQLTLSILDAPYLKKHRVPVVYTAHDYIllcpaytmvdgngkvcddcLDRRFIHAvkktcvkgskAKSGL 173
Cdd:pfam13439 72 PDVVH---AHSPFPLGLAALAARLRLGIPLVVTYHGLF-------------------PDYKRLGA----------RLSPL 119
|
170 180 190
....*....|....*....|....*....|.
gi 1540018338 174 AFLEAEFLKhhHSYDKIDKIIAPSEFMKSKL 204
Cdd:pfam13439 120 RRLLRRLER--RLLRRADRVIAVSEAVADEL 148
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
2-427 |
1.48e-13 |
|
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: 71.54 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 2 KILLVNKYFY-RKGGAETYFFALAEGLKSLGHEVAFFSMqhpNNEPSYWSKYFvsekdYVGKISAFQQAKEAATLIYSLE 80
Cdd:cd03795 1 KVLHVFKFYYpDIGGIEQVIYDLAEGLKKKGIEVDVLCF---SKEKETPEKEE-----NGIRIHRVKSFLNVASTPFSPS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 81 SKRKFEALLEEfqPDVIHmnnVHRQLTLSILdAPYLKKHRVPVVYTAHDYIL----LCPAYtmvdgngkvcdDCLDRRFI 156
Cdd:cd03795 73 YIKRFKKLAKE--YDIIH---YHFPNPLADL-LLFFSGAKKPVVVHWHSDIVkqkkLLKLY-----------KPLMTRFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 157 HAVKKTCVKGSKAKSglaflEAEFLKHHhsydKIDKIIAPSefmksKLDEGGYAGRTVAMQNflttsqmdmaHKVTNTDK 236
Cdd:cd03795 136 RRADRIIATSPNYVE-----TSPTLREF----KNKVRVIPL-----GIDKNVYNIPRVDFEN----------IKREKKGK 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 237 fntvdPYFLFFGRLSKEKGILTLVKAflqAAGLlplagaveqsetegghlvanclpsNWTLHIVGDGPERQTIEMLIKSA 316
Cdd:cd03795 192 -----KIFLFIGRLVYYKGLDYLIEA---AQYL------------------------NYPIVIGGEGPLKPDLEAQIELN 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 317 GSEaenRIKLLGYKTGENLQREVGNARFSVLCSEWR-ENMPYSGLESLAAQTPVIGANIG-GIPELVVEGETGFKFESGN 394
Cdd:cd03795 240 LLD---NVKFLGRVDDEEKVIYLHLCDVFVFPSVLRsEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVPPKD 316
|
410 420 430
....*....|....*....|....*....|...
gi 1540018338 395 QDDLARTLTKAAQvDAGRYASMQESCGRYVEER 427
Cdd:cd03795 317 PDALAEAIDKLLS-DEELRESYGENAKKRFEEL 348
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
2-439 |
1.95e-13 |
|
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: 71.63 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 2 KILLVNKYFYRK-GGAETYFFALAEGLKSLGHEVAFFSMqhpnnEPSYWS------KYFVSEKDYVGKISAFQQAKEAAT 74
Cdd:cd03821 1 KILHVTPSISPKaGGPVKVVLRLAAALAALGHEVTIVST-----GDGYESlvveenGRYIPPQDGFASIPLLRQGAGRTD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 75 LIYSLESKRKFEALleefQPDVIHMNNVhRQLTLSILdAPYLKKHRVPVVYTAHdyillcpayTMVDGngkvcddcLDRR 154
Cdd:cd03821 76 FSPGLPNWLRRNLR----EYDVVHIHGV-WTYTSLAA-CKLARRRGIPYVVSPH---------GMLDP--------WALQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 155 FIHAVKKTCVkgskaksglafleaeFLKHHHSYDKIDKIIAPSEFMKSKLDEGGYAGRTVAMQNFLTTSQMDMAHKvtNT 234
Cdd:cd03821 133 QKHWKKRIAL---------------HLIERRNLNNAALVHFTSEQEADELRRFGLEPPIAVIPNGVDIPEFDPGLR--DR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 235 DKFNTVD--PYFLFFGRLSKEKGILTLVKAF--LQAAGLlplagaveqsetegghlvanclpsNWTLHIVG-DGPERQTI 309
Cdd:cd03821 196 RKHNGLEdrRIILFLGRIHPKKGLDLLIRAArkLAEQGR------------------------DWHLVIAGpDDGAYPAF 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 310 EMLIKSAGseAENRIKLLGYKTGENLQREVGNARFSVLCSEwRENMPYSGLESLAAQTPVIGANIGGIPELVVEGeTGFK 389
Cdd:cd03821 252 LQLQSSLG--LGDRVTFTGPLYGEAKWALYASADLFVLPSY-SENFGNVVAEALACGLPVVITDKCGLSELVEAG-CGVV 327
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1540018338 390 FESgNQDDLARTLTKAAQVDAGRyASMQESC--GRYVEERCRQDMYVRQLED 439
Cdd:cd03821 328 VDP-NVSSLAEALAEALRDPADR-KRLGEMArrARQVEENFSWEAVAGQLGE 377
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
10-430 |
6.29e-13 |
|
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: 69.70 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 10 FYRKGGAETYFFALAEGLKSLGHEVAFFSMQHPNNEPSYWSKYFVSEKDYVGKISAFQQAKEAATLIYSLESKRKfeall 89
Cdd:cd03809 10 AQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDK----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 90 eefqPDVIHMNNvhrqltlsilDAPYLKKHRVPVVYTAHDYI-LLCPAYTMvdgngkvcddcLDRRFIH-AVKKTCVKGS 167
Cdd:cd03809 85 ----PDLLHSPH----------NTAPLLLKGCPQVVTIHDLIpLRYPEFFP-----------KRFRLYYrLLLPISLRRA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 168 kaksglafleaeflkhhhsydkiDKIIAPSEFMKSKLDE--GGYAGRTVAMQNFLTTSQMDMAHKVTNTDKFNTVDPYFL 245
Cdd:cd03809 140 -----------------------DAIITVSEATRDDIIKfyGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLPEPYFL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 246 FFGRLSKEKGILTLVKAFLQAAGLLPLAgaveqseteggHLVanclpsnwtlhIVG-DGPERQTIEMLIKSAGSeaENRI 324
Cdd:cd03809 197 YVGTLEPRKNHERLLKAFALLKKQGGDL-----------KLV-----------IVGgKGWEDEELLDLVKKLGL--GGRV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 325 KLLGYKTGENLQREVGNARFSVLCSEWrENMPYSGLESLAAQTPVIGANIGGIPELVveGETGFKFESGNQDDLARTLTK 404
Cdd:cd03809 253 RFLGYVSDEDLPALYRGARAFVFPSLY-EGFGLPVLEAMACGTPVIASNISVLPEVA--GDAALYFDPLDPESIADAILR 329
|
410 420 430
....*....|....*....|....*....|
gi 1540018338 405 AAQvDAGRYASMQESC----GRYVEERCRQ 430
Cdd:cd03809 330 LLE-DPSLREELIRKGleraKKFSWEKTAE 358
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
64-442 |
4.08e-12 |
|
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: 67.36 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 64 SAFQQAKEAATLIYslESKRKFEALLEEFQPDVIHMNNVHRQLtLSILDAPYLKkHRVPVVYTAHD---------YILLC 134
Cdd:cd03825 24 QALLAYGIDSTMLV--GRKKNLISKPEFIEADIIHLHWIHGGY-LSLKALFKLL-RRKPVVWTLHDmwpftggchYPMEC 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 135 PAYTMVDGNGKVCDD----CLDR-RFIHAVKKtcvkgsKAKSGLAFLeaeflkhhhsydkidkIIAPSEFMKSKLDE-GG 208
Cdd:cd03825 100 EGWKTGCGNCPNLNSyppaKKDLsRQLFRRKR------EALAKKRLT----------------IVAPSRWLADMVRRsPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 209 YAGRTVA-MQNFLTTSQMDMAHKVTNTDKFNTV-DPYFLFFGRLSKE---KGILTLVKAFLQAAGLlplagaveqseteg 283
Cdd:cd03825 158 LKGLPVVvIPNGIDTEIFAPVDKAKARKRLGIPqDKKVILFGAESVTkprKGFDELIEALKLLATK-------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 284 ghlvANCLpsnwtLHIVGDGPERqtiemlIKSAGSEAENriklLGYKTGENLQREVGNA-----RFSVLcsewrENMPYS 358
Cdd:cd03825 224 ----DDLL-----LVVFGKNDPQ------IVILPFDIIS----LGYIDDDEQLVDIYSAadlfvHPSLA-----DNLPNT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 359 GLESLAAQTPVIGANIGGIPELVVEGETGFKFESGNQDDLARTLTKAAQvDAGRYASMQESCGRYVEERCRQDMYVRQLE 438
Cdd:cd03825 280 LLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLA-NPKERESLGERARALAENHFDQRVQAQRYL 358
|
....
gi 1540018338 439 DVYR 442
Cdd:cd03825 359 ELYK 362
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
244-399 |
8.86e-11 |
|
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: 63.09 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 244 FLFFGRLSKEKGILTLVKAFLQAAGLLPlagaveqsetegghlvanclpsNWTLHIVGDGPERQTIEMLIKSagSEAENR 323
Cdd:cd04949 163 IITISRLAPEKQLDHLIEAVAKAVKKVP----------------------EITLDIYGYGEEREKLKKLIEE--LHLEDN 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540018338 324 IKLLGYKTgeNLQREVGNARFSVLCSEWrENMPYSGLESLAAQTPVIGANIG-GIPELVVEGETGFKFESGNQDDLA 399
Cdd:cd04949 219 VFLKGYHS--NLDQEYQDAYLSLLTSQM-EGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALA 292
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
14-381 |
9.13e-11 |
|
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: 63.23 E-value: 9.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 14 GGAETYFFALAEGLKSLGHEVAFFSMQHPNNepsywskyfVSEKDYVGKISAFQQAKEAATLIYSLESKRKFealLEEFQ 93
Cdd:cd04951 12 GGAEKQTVLLADQMFIRGHDVNIVYLTGEVE---------VKPLNNNIIIYNLGMDKNPRSLLKALLKLKKI---ISAFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 94 PDVIHMNNVHRQLTLSILDAPYlkkHRVPVVYTAHD------YILLCPAYT--MVDGNGKVCDDCLDrrfihavkktcvk 165
Cdd:cd04951 80 PDVVHSHMFHANIFARFLRMLY---PIPLLICTAHNkneggrIRMFIYRLTdfLCDITTNVSREALD------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 166 gskaksglafleaEFLKHHhsydkidkiiapsEFMKSKldeggyagrTVAMQNFLTTSQM--DMAHKVTNTDKFNTVDPY 243
Cdd:cd04951 144 -------------EFIAKK-------------AFSKNK---------SVPVYNGIDLNKFkkDINVRLKIRNKLNLKNDE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 244 FLFF--GRLSKEKGILTLVKAFLqaagllplagaveqseteggHLVANCLpsNWTLHIVGDGPERQTIEMLIKSAGseAE 321
Cdd:cd04951 189 FVILnvGRLTEAKDYPNLLLAIS--------------------ELILSKN--DFKLLIAGDGPLRNELERLICNLN--LV 244
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 322 NRIKLLGYKTgeNLQREVGNARFSVLCSEWrENMPYSGLESLAAQTPVIGANIGGIPELV 381
Cdd:cd04951 245 DRVILLGQIS--NISEYYNAADLFVLSSEW-EGFGLVVAEAMACERPVVATDAGGVAEVV 301
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
299-437 |
1.70e-10 |
|
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.
Pssm-ID: 340829 [Multi-domain] Cd Length: 350 Bit Score: 62.47 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 299 IVGDGPERQTIEMLIKSAgsEAENRIKLLGYKTGENLQREVGNARF----SVLCSEWRENMPYSGL-ESLAAQTPVIGAN 373
Cdd:cd03799 210 IIGDGDLKEQLQQLIQEL--NIGDCVKLLGWKPQEEIIEILDEADIfiapSVTAADGDQDGPPNTLkEAMAMGLPVISTE 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540018338 374 IGGIPELVVEGETGFKFESGNQDDLARTLTKAAQVDAgRYASMQESCGRYVEERCRQDMYVRQL 437
Cdd:cd03799 288 HGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPA-IWPEMGKAGRARVEEEYDINKLNDEL 350
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
297-432 |
6.73e-10 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 60.88 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 297 LHIVGDGPERQTIEMLIKsaGSEAEnrikLLGYKTGENLQREVGNARFSVLCSEwRENMPYSGLESLAAQTPVIGANIGG 376
Cdd:PLN02871 293 LAFVGDGPYREELEKMFA--GTPTV----FTGMLQGDELSQAYASGDVFVMPSE-SETLGFVVLEAMASGVPVVAARAGG 365
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1540018338 377 IPELV---VEGETGFKFESGNQDDLARTLTKAAQVDAGRyasmqESCGRyveeRCRQDM 432
Cdd:PLN02871 366 IPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPELR-----ERMGA----AAREEV 415
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
188-388 |
3.08e-08 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 55.57 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 188 DKIDKIIAPSEFMKSKLDEGGYAGRTVAMQNFLTTSQMDMAHKVTNTDKFN--TVDPYFLFFGRLSKEKGILTLVKAFLQ 265
Cdd:PRK15484 138 DKNAKIIVPSQFLKKFYEERLPNADISIVPNGFCLETYQSNPQPNLRQQLNisPDETVLLYAGRISPDKGILLLMQAFEK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 266 AAGLlplagaveqsetegghlvanclPSNWTLHIVGD-----GPERQTIEMLIKSAGSEAENRIKLLGYKTGENLQREVG 340
Cdd:PRK15484 218 LATA----------------------HSNLKLVVVGDptassKGEKAAYQKKVLEAAKRIGDRCIMLGGQPPEKMHNYYP 275
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1540018338 341 NARFSVLCSEWRENMPYSGLESLAAQTPVIGANIGGIPELVVEGETGF 388
Cdd:PRK15484 276 LADLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGY 323
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
234-398 |
3.20e-08 |
|
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: 55.37 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 234 TDKFNTVDP---YFLFFGRLSKEKGILTLVKAFLQaaglLPLagaveqseteggHLVanclpsnwtlhIVGDGPERQTIE 310
Cdd:cd03804 189 TDAFAPAADkedYYLTASRLVPYKRIDLAVEAFNE----LPK------------RLV-----------VIGDGPDLDRLR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 311 mliksagSEAENRIKLLGYKTGENLQREVGNARFSVLCSEwrENMPYSGLESLAAQTPVIGANIGGIPELVVEGETGFKF 390
Cdd:cd03804 242 -------AMASPNVEFLGYQPDEVLKELLSKARAFVFAAE--EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILF 312
|
....*...
gi 1540018338 391 ESGNQDDL 398
Cdd:cd03804 313 GEQTVESL 320
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
245-402 |
7.34e-07 |
|
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: 51.09 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 245 LFFGRLSKEKGILTLVKAFLQAAGLLPLAgaveqsetegghlvanclpsnwTLHIVGdGPERQ-----TIEMLIKSAGSE 319
Cdd:cd03800 224 LALGRLDPRKGIDTLVRAFAQLPELRELA----------------------NLVLVG-GPSDDplsmdREELAELAEELG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 320 AENRIKLLGYKTgenlQREVG---NARFSVLCSEWREnmPYsGL---ESLAAQTPVIGANIGGIPELVVEGETGFKFESG 393
Cdd:cd03800 281 LIDRVRFPGRVS----RDDLPelyRAADVFVVPSLYE--PF-GLtaiEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPH 353
|
....*....
gi 1540018338 394 NQDDLARTL 402
Cdd:cd03800 354 DPEALAAAL 362
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
295-427 |
2.89e-05 |
|
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: 46.30 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 295 WTlHIvGDGPERQTIEMLIKSagsEAEN-RIKLLGY---KTGENLQREvGNARFSVLCSEwRENMPYSGLESLAAQTPVI 370
Cdd:cd04946 260 WT-HI-GGGPLKERLEKLAEN---KLENvKVNFTGEvsnKEVKQLYKE-NDVDVFVNVSE-SEGIPVSIMEAISFGIPVI 332
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540018338 371 GANIGGIPELVVEGETGFKFESG-NQDDLARTLTKAAQVDaGRYASMQESCGRYVEER 427
Cdd:cd04946 333 ATNVGGTREIVENETNGLLLDKDpTPNEIVSSIMKFYLDG-GDYKTMKISARECWEER 389
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
293-404 |
3.19e-04 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 42.78 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 293 SNWTLHIVGDGPERQTIEMLIKSAGseAENRIKLLGYKTG--ENLQREVGNARFSVLCSEWrENMPYSGLESLAAQTPVI 370
Cdd:PRK09922 209 GEWQLHIIGDGSDFEKCKAYSRELG--IEQRIIWHGWQSQpwEVVQQKIKNVSALLLTSKF-EGFPMTLLEAMSYGIPCI 285
|
90 100 110
....*....|....*....|....*....|....*
gi 1540018338 371 GANIGGIPE-LVVEGETGFKFESGNQDDLARTLTK 404
Cdd:PRK09922 286 SSDCMSGPRdIIKPGLNGELYTPGNIDEFVGKLNK 320
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
360-392 |
1.08e-03 |
|
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.
Pssm-ID: 340834 [Multi-domain] Cd Length: 392 Bit Score: 41.04 E-value: 1.08e-03
10 20 30
....*....|....*....|....*....|...
gi 1540018338 360 LESLAAQTPVIGANIGGIPELVVEGETGFKFES 392
Cdd:cd03805 317 LEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP 349
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
357-434 |
1.49e-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: 40.81 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540018338 357 YSGLESLAAQTPVIGANIGGIPELVVEGETGFKFESGNQDDLartltkAAQV-----DAGRYASMQESCGRYVEERCRQD 431
Cdd:cd03818 315 WSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDAL------AAAVlelleDPDRAAALRRAARRTVERSDSLD 388
|
...
gi 1540018338 432 MYV 434
Cdd:cd03818 389 VCL 391
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
352-388 |
4.33e-03 |
|
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: 39.23 E-value: 4.33e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1540018338 352 RENMPYSGLESLAAQTPVIGANIGGIPELVVEGETGF 388
Cdd:cd03792 289 REGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGF 325
|
|
| |
