|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
4-391 |
6.24e-69 |
|
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: 221.87 E-value: 6.24e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 4 LLSISTLYPAPGRTGFGRFVARQMEALAARGdWDVTVVNPIGLPPLPLKRYAALRAIPAAERqgaitvhHPRFILLPGLS 83
Cdd:cd03798 1 VLILTNIYPNANSPGRGIFVRRQVRALSRRG-VDVEVLAPAPWGPAAARLLRKLLGEAVPPR-------DGRRLLPLKPR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 84 GPINPMLIARAVLPLARRLHaENPFDLVDAQFFYPDGPAAAKIARELGLPFAIKARGSDIHLWGDRESARRQMLDAAKQA 163
Cdd:cd03798 73 LRLLAPLRAPSLAKLLKRRR-RGPPDLIHAHFAYPAGFAAALLARLYGVPYVVTEHGSDINVFPPRSLLRKLLRWALRRA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 164 SALLSVSRALARDMAAMGMLEEHIHVHYTGLDRERFRPLERQAARQLvsaipalqvwsTGPLLLCVGALVPIKGQAIAIR 243
Cdd:cd03798 152 ARVIAVSKALAEELVALGVPRDRVDVIPNGVDPARFQPEDRGLGLPL-----------DAFVILFVGRLIPRKGIDLLLE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 244 ALTHLP---EDVRLAIAGTGGDESALKAMTRQLGLESRVQFLGAVEHDLLPQLLCAADAMVLPSEREGLANAWIEAIACG 320
Cdd:cd03798 221 AFARLAkarPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACG 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163457107 321 TPVIIPDIGGAREVVQDASAGRIVDRT-PEAIADAVMDLLENPPAQTDV----ATNAERFSWAANAATLAAIYEKA 391
Cdd:cd03798 301 LPVVATDVGGIPEVVGDPETGLLVPPGdADALAAALRRALAEPYLRELGeaarARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
3-377 |
2.03e-46 |
|
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: 162.71 E-value: 2.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 3 RLLSISTLYPaPGRTGFGRFVARQMEALAARGdWDVTVVnpiglpplplkryaALRAIPAAERQGAITVHHPRFILLPGl 82
Cdd:cd03801 1 KILLLSPELP-PPVGGAERHVRELARALAARG-HDVTVL--------------TPADPGEPPEELEDGVIVPLLPSLAA- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 83 sgpinpMLIARAVLPLARRLHAENPFDLVDAQFFYPdGPAAAKIARELGLPFAIKARGSDIHLWGDRESARRQMLDAAKQ 162
Cdd:cd03801 64 ------LLRARRLLRELRPLLRLRKFDVVHAHGLLA-ALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLARAEA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 163 ----ASALLSVSRALARDMAAM-GMLEEHIHVHYTGLDRERFRPLERQAarqlvsaipaLQVWSTGPLLLCVGALVPIKG 237
Cdd:cd03801 137 llrrADAVIAVSEALRDELRALgGIPPEKIVVIPNGVDLERFSPPLRRK----------LGIPPDRPVLLFVGRLSPRKG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 238 QAIAIRALTHLPE---DVRLAIAGTGGDESAlKAMTRQLGLESRVQFLGAVEHDLLPQLLCAADAMVLPSEREGLANAWI 314
Cdd:cd03801 207 VDLLLEALAKLLRrgpDVRLVIVGGDGPLRA-ELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVL 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163457107 315 EAIACGTPVIIPDIGGAREVVQDASAGRIVD-RTPEAIADAVMDLLENPPAQTDVATNA-----ERFSW 377
Cdd:cd03801 286 EAMAAGLPVVATDVGGLPEVVEDGEGGLVVPpDDVEALADALLRLLADPELRARLGRAArervaERFSW 354
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
222-375 |
1.22e-38 |
|
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: 135.86 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 222 TGPLLLCVGALVPIKGQAIAIRALTHLPE---DVRLAIAGTGGDESALKAMTRQLGLESRVQFLGAVEHDLLPQLLCAAD 298
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEknpNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163457107 299 AMVLPSEREGLANAWIEAIACGTPVIIPDIGGAREVVQDASAGRIVD-RTPEAIADAVMDLLENPPAQTDVATNAERF 375
Cdd:pfam00534 81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKpNNAEALAEAIDKLLEDEELRERLGENARKR 158
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
21-363 |
3.12e-36 |
|
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: 135.18 E-value: 3.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 21 RFVARQMEALAARGdWDVTVVnpiglpplplkryaALRAIPAAERQGAITVHHPRFillPGLSGPINPMLIARAVLPLAR 100
Cdd:cd03811 16 RVLLNLANALDKRG-YDVTLV--------------LLRDEGDLDKQLNGDVKLIRL---LIRVLKLIKLGLLKAILKLKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 101 RLhAENPFDLV-DAQFFYPdgpAAAKIARELGLPFAIKARGSDIHLWgDRESARRQMLDAAKQASALLSVSRALARDMAA 179
Cdd:cd03811 78 IL-KRAKPDVViSFLGFAT---YIVAKLAAARSKVIAWIHSSLSKLY-YLKKKLLLKLKLYKKADKIVCVSKGIKEDLIR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 180 -MGMLEEHIHVHYTGLDRERFRPLerqaarqlvSAIPALQVWSTGPLLLCVGALVPIKGQAIAIRALTHLPE---DVRLA 255
Cdd:cd03811 153 lGPSPPEKIEVIYNPIDIDRIRAL---------AKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKkypDVKLV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 256 IAGTGGDESALKAMTRQLGLESRVQFLGAVEhDLLPqLLCAADAMVLPSEREGLANAWIEAIACGTPVIIPDIGGAREVV 335
Cdd:cd03811 224 ILGDGPLREELEKLAKELGLAERVIFLGFQS-NPYP-YLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREIL 301
|
330 340
....*....|....*....|....*...
gi 2163457107 336 QDASAGRIVDRTPEAIADAVMDLLENPP 363
Cdd:cd03811 302 DDGENGLLVPDGDAAALAGILAALLQKK 329
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
144-377 |
8.12e-35 |
|
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: 131.72 E-value: 8.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 144 HLWGDRESARRQMLDAAKQASALLSVSRALARDMAA-MGMLEEHIHVHYTGLDRErFRPLERQAARQLVSAIPAlqvwst 222
Cdd:cd03809 120 FPKRFRLYYRLLLPISLRRADAIITVSEATRDDIIKfYGVPPEKIVVIPLGVDPS-FFPPESAAVLIAKYLLPE------ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 223 gPLLLCVGALVPIKGQAIAIRALTHLPE---DVRLAIAGTGGDESA-LKAMTRQLGLESRVQFLGAVEHDLLPQLLCAAD 298
Cdd:cd03809 193 -PYFLYVGTLEPRKNHERLLKAFALLKKqggDLKLVIVGGKGWEDEeLLDLVKKLGLGGRVRFLGYVSDEDLPALYRGAR 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 299 AMVLPSEREGlanaW----IEAIACGTPVIIPDIGGAREVVQDasAGRIVD-RTPEAIADAVMDLLENPP----AQTDVA 369
Cdd:cd03809 272 AFVFPSLYEG----FglpvLEAMACGTPVIASNISVLPEVAGD--AALYFDpLDPESIADAILRLLEDPSlreeLIRKGL 345
|
....*...
gi 2163457107 370 TNAERFSW 377
Cdd:cd03809 346 ERAKKFSW 353
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
85-363 |
2.43e-33 |
|
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: 127.82 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 85 PINPMLIARAVLPLARRLHAENPfDLVDAQFFYPD--GPAAAKIARelGLPFAIKARGSDIHLWGDReSARRQMLDAAKQ 162
Cdd:cd03807 58 GLSSGKDPGVLLRLAKLIRKRNP-DVVHTWMYHADliGGLAAKLAG--GVKVIWSVRSSNIPQRLTR-LVRKLCLLLSKF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 163 ASALLSVSRALARDMAAMGMLEEHIHVHYTGLDRERFRPLERQAARqlvsAIPALQVWSTGPLLLCVGALVPIKGQAIAI 242
Cdd:cd03807 134 SPATVANSSAVAEFHQEQGYAKNKIVVIYNGIDLFKLSPDDASRAR----ARRRLGLAEDRRVIGIVGRLHPVKDHSDLL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 243 RALTHLPE---DVRLAIAGTGGDESALKAMTRQLGLESRVQFLGAVEHdlLPQLLCAADAMVLPSEREGLANAWIEAIAC 319
Cdd:cd03807 210 RAAALLVEthpDLRLLLVGRGPERPNLERLLLELGLEDRVHLLGERSD--VPALLPAMDIFVLSSRTEGFPNALLEAMAC 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2163457107 320 GTPVIIPDIGGAREVVQDaSAGRIVD-RTPEAIADAVMDLLENPP 363
Cdd:cd03807 288 GLPVVATDVGGAAELVDD-GTGFLVPaGDPQALADAIRALLEDPE 331
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
91-376 |
1.58e-32 |
|
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: 125.85 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 91 IARAVLPLARRLHAENPFDLVDAQ--FFYpdGPAAAKIARELGLPF--------------AIKARGsdihlwGDRESARR 154
Cdd:cd03817 68 IPFPFKKAVIDRIKELGPDIIHTHtpFSL--GKLGLRIARKLKIPIvhtyhtmyedylhyIPKGKL------LVKAVVRK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 155 QMLDAAKQASALLSVSRALARDMAAMGmLEEHIHVHYTGLDRERFRPLERQAARQlvsaipALQVWSTGPLLLCVGALVP 234
Cdd:cd03817 140 LVRRFYNHTDAVIAPSEKIKDTLREYG-VKGPIEVIPNGIDLDKFEKPLNTEERR------KLGLPPDEPILLYVGRLAK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 235 IKGQAIAIRALTHLPE--DVRLAIAGTGGDESALKAMTRQLGLESRVQFLGAVEHDLLPQLLCAADAMVLPSEREGLANA 312
Cdd:cd03817 213 EKNIDFLLRAFAELKKepNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLV 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163457107 313 WIEAIACGTPVIIPDIGGAREVVQDASAGRIVDRTPEAIADAVMDLLENPPAQTDVATNAERFS 376
Cdd:cd03817 293 YLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDETLAEKLLHLRENLELLRKLSKNAEISA 356
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
18-362 |
5.01e-30 |
|
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: 118.47 E-value: 5.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 18 GFGRFVARQMEALAARGdWDVTVVNPIGLpplplkryaalRAIPAAERQGAITVHHPRfillpgLSGPINPMLIARAVLP 97
Cdd:cd03808 11 GFQSFRLPLIKALVKKG-YEVHVIAPDGD-----------KLSDELKELGVKVIDIPI------LRRGINPLKDLKALFK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 98 LARRLHAENPfDLVDAQF----FYpdGPAAAKIARelglpfaIKARGSDIHLWG--DRESARRQMLD------AAKQASA 165
Cdd:cd03808 73 LYKLLKKEKP-DIVHCHTpkpgIL--GRLAARLAG-------VPKVIYTVHGLGfvFTEGKLLRLLYllleklALLFTDK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 166 LLSVSRALARDMAAMGML-EEHIHVHY-TGLDRERFRPLERQAArqlvsaipalqvwSTGPLLLCVGALVPIKGQAIAIR 243
Cdd:cd03808 143 VIFVNEDDRDLAIKKGIIkKKKTVLIPgSGVDLDRFQYSPESLP-------------SEKVVFLFVARLLKDKGIDELIE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 244 ALTHLPE---DVRLAIAGTGGDESALKAMTRQLGLESRVQFLGAVEHdlLPQLLCAADAMVLPSEREGLANAWIEAIACG 320
Cdd:cd03808 210 AAKILKKkgpNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSD--VPELLAESDVFVLPSYREGLPRSLLEAMAAG 287
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2163457107 321 TPVIIPDIGGAREVVQDASAGRIVD-RTPEAIADAVMDLLENP 362
Cdd:cd03808 288 RPVITTDVPGCRELVIDGVNGFLVPpGDVEALADAIEKLIEDP 330
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
22-377 |
1.34e-29 |
|
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: 118.11 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 22 FVARQMEALAARGdWDVTVVNpiglpplplkryaalRAIPaaERQGAITVHHPRFILLPGLSGPIN--------PMLIAR 93
Cdd:cd03800 26 YVLELARALAELG-YQVDIFT---------------RRIS--PADPEVVEIAPGARVIRVPAGPPEylpkeelwPYLEEF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 94 AVLPLARRLHAENPFDLVDAQFFYpDGPAAAKIARELGLPF--------AIKARGSDIhlwGDRESARRQM---LDAAKQ 162
Cdd:cd03800 88 ADGLLRFIAREGGRYDLIHSHYWD-SGLVGALLARRLGVPLvhtfhslgRVKYRHLGA---QDTYHPSLRItaeEQILEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 163 ASALLSVSRALARDMAAM-GMLEEHIHVHYTGLDRERFRPLERQAARQLVSAIPALqvwstGPLLLCVGALVPIKGQAIA 241
Cdd:cd03800 164 ADRVIASTPQEADELISLyGADPSRINVVPPGVDLERFFPVDRAEARRARLLLPPD-----KPVVLALGRLDPRKGIDTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 242 IRALTHLP---EDVRLAIAGTG------GDESALKAMTRQLGLESRVQFLGAVEHDLLPQLLCAADAMVLPSEREGLANA 312
Cdd:cd03800 239 VRAFAQLPelrELANLVLVGGPsddplsMDREELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLT 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163457107 313 WIEAIACGTPVIIPDIGGAREVVQDASAGRIVD-RTPEAIADAVMDLLENPPAQTDVATNA-----ERFSW 377
Cdd:cd03800 319 AIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDpHDPEALAAALRRLLDDPALWQRLSRAGlerarAHYTW 389
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
223-361 |
9.85e-29 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 109.14 E-value: 9.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 223 GPLLLCVGALVP-IKGQAIAIRALTHL---PEDVRLAIAGtGGDESALKAMTRqlGLESRVQFLGAVEHdlLPQLLCAAD 298
Cdd:pfam13692 1 RPVILFVGRLHPnVKGVDYLLEAVPLLrkrDNDVRLVIVG-DGPEEELEELAA--GLEDRVIFTGFVED--LAELLAAAD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163457107 299 AMVLPSEREGLANAWIEAIACGTPVIIPDIGGAREVVqDASAGRIVD-RTPEAIADAVMDLLEN 361
Cdd:pfam13692 76 VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPpGDPEALAEAILRLLED 138
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
8-377 |
2.78e-28 |
|
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: 113.93 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 8 STLYPAPGrtGFGRFVARQMEALAARGDwDVTVVNPiglpplplkryaalRAIPAAERqgaitvHHPRFILLPGLSGPIN 87
Cdd:cd03814 7 DTYHPQVN--GVVRTLERLVDHLRRRGH-EVRVVAP--------------GPFDEAES------AEGRVVSVPSFPLPFY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 88 PMLiaRAVLPLARRL----HAENPfDLVDAQFFYPDGPAAAKIARELGLPFA------IKARGSDIHLWGDRESARRQML 157
Cdd:cd03814 64 PEY--RLALPLPRRVrrliKEFQP-DIIHIATPGPLGLAALRAARRLGLPVVtsyhtdFPEYLSYYTLGPLSWLAWAYLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 158 DAAKQASALLSVSRALARDMAAMGMleEHIHVHYTGLDRERFRPLERQAA-RQLVSAIPAlqvwstgPLLLCVGALVPIK 236
Cdd:cd03814 141 WFHNPFDTTLVPSPSIARELEGHGF--ERVRLWPRGVDTELFHPSRRDAAlRRRLGPPGR-------PLLLYVGRLAPEK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 237 GQAIAIRALTHLPE--DVRLAIAGTGGDESALKAMTRQlglesrVQFLGAVEHDLLPQLLCAADAMVLPSEREGLANAWI 314
Cdd:cd03814 212 NLEALLDADLPLAAspPVRLVVVGDGPARAELEARGPD------VIFTGFLTGEELARAYASADVFVFPSRTETFGLVVL 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163457107 315 EAIACGTPVIIPDIGGAREVVQDASAGRIV-DRTPEAIADAVMDLLENPPAQTDVATNA----ERFSW 377
Cdd:cd03814 286 EAMASGLPVVAADAGGPRDIVRPGGTGALVePGDAAAFAAALRALLEDPELRRRMAARAraeaERYSW 353
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
79-364 |
2.03e-27 |
|
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: 111.29 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 79 LPGLSGPINPMLIARAVLplaRRLHAENPFDLVDAQFFYPdGPAAAKIARELGLPFAIKARGSDIHLWGDRESARRQMLD 158
Cdd:cd03819 51 LPGLKVPLLRALLGNVRL---ARLIRRERIDLIHAHSRAP-AWLGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVRAR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 159 AAKQASALLSVSRALARDMAAmgmLEEHIHVHYTGLDRERFRPlerqaaRQLVSAIPALQVWSTGPLLLCVGALVPIKGQ 238
Cdd:cd03819 127 GDRVIAVSELVRDHLIEALGV---DPERIRVIPNGVDTDRFPP------EAEAEERAQLGLPEGKPVVGYVGRLSPEKGW 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 239 AIAIRALTHLPE--DVRLAIAGTGGDESALKAMTRQLGLESRVQFLGAveHDLLPQLLCAADAMVLPSEREGLANAWIEA 316
Cdd:cd03819 198 LLLVDAAAELKDepDFRLLVAGDGPERDEIRRLVERLGLRDRVTFTGF--REDVPAALAASDVVVLPSLHEEFGRVALEA 275
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2163457107 317 IACGTPVIIPDIGGAREVVQDASAGRIVDR-TPEAIADAVMDLLENPPA 364
Cdd:cd03819 276 MACGTPVVATDVGGAREIVVHGRTGLLVPPgDAEALADAIRAAKLLPEA 324
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
3-362 |
9.38e-27 |
|
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: 109.34 E-value: 9.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 3 RLLSISTLYPAPGRTGFGRFVARQMEALAARGdWDVTVVNPIGLPPLPLKRYAALRAIpaaERQGAITVHHPRFILLPGL 82
Cdd:cd03823 1 KILLVNSLYPPQRVGGAEISVHDLAEALVAEG-HEVAVLTAGVGPPGQATVARSVVRY---RRAPDETLPLALKRRGYEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 83 SGPINPMLIARavlpLARRLHAENPfDLVDAQFFYPDGPAAAKIARELGLPFAIKARgsDIHLwgdrESARRQMLDAAKq 162
Cdd:cd03823 77 FETYNPGLRRL----LARLLEDFRP-DVVHTHNLSGLGASLLDAARDLGIPVVHTLH--DYWL----LCPRQFLFKKGG- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 163 aSALLSVSRALARDMAAMGMLEEHIHVHYTGLDRERfRPLERQAARqlvsaipalqvwsTGPLLLC-VGALVPIKGQAIA 241
Cdd:cd03823 145 -DAVLAPSRFTANLHEANGLFSARISVIPNAVEPDL-APPPRRRPG-------------TERLRFGyIGRLTEEKGIDLL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 242 IRALTHLP-EDVRLAIAGTGGDESAlkamtRQLGLESRVQFLGAVEHDLLPQLLCAADAMVLPSereglanAW------- 313
Cdd:cd03823 210 VEAFKRLPrEDIELVIAGHGPLSDE-----RQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPS-------IWpepfglv 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2163457107 314 -IEAIACGTPVIIPDIGGAREVVQDASAGRIVDRT-PEAIADAVMDLLENP 362
Cdd:cd03823 278 vREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGdAEDLAAAMRRLLTDP 328
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
109-375 |
1.62e-26 |
|
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: 109.08 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 109 DLVDAQFfYPDGPAAAKIARELGLPFAIKARGSDIHLWGDRESARRQMLD--------AAKQASALLSVSRALARDMAAM 180
Cdd:cd05844 83 ALVHAHF-GRDGVYALPLARALGVPLVVTFHGFDITTSRAWLAASPGWPSqfqrhrraLQRPAALFVAVSGFIRDRLLAR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 181 GMLEEHIHVHYTGLDRERFRPLERQAArqlvsaipalqvwstGPLLLCVGALVPIKGQAIAIRA---LTHLPEDVRLAIA 257
Cdd:cd05844 162 GLPAERIHVHYIGIDPAKFAPRDPAER---------------APTILFVGRLVEKKGCDVLIEAfrrLAARHPTARLVIA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 258 GTGGDESALKAMTRQLGlesRVQFLGAVEHDLLPQLLCAADAMVLPS------EREGLANAWIEAIACGTPVIIPDIGGA 331
Cdd:cd05844 227 GDGPLRPALQALAAALG---RVRFLGALPHAEVQDWMRRAEIFCLPSvtaasgDSEGLGIVLLEAAACGVPVVSSRHGGI 303
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2163457107 332 REVVQDASAGRIV-DRTPEAIADAVMDLLENPPAQTDVATNAERF 375
Cdd:cd05844 304 PEAILDGETGFLVpEGDVDALADALQALLADRALADRMGGAARAF 348
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
9-375 |
9.96e-26 |
|
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: 107.07 E-value: 9.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 9 TLYPAPGRTGFGRFVARQMEALAARGDwDVTVVNpIGLPPLPLKRYAALRAIPAAERQGAITvhhprfillpgLSGPINP 88
Cdd:cd03821 6 TPSISPKAGGPVKVVLRLAAALAALGH-EVTIVS-TGDGYESLVVEENGRYIPPQDGFASIP-----------LLRQGAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 89 MLIARAVLPLARRLHAENpFDLVDAQ--FFYPDGpAAAKIARELGLPFAIKARGSDIHLWGDRESARRQM-----LDAAK 161
Cdd:cd03821 73 RTDFSPGLPNWLRRNLRE-YDVVHIHgvWTYTSL-AACKLARRRGIPYVVSPHGMLDPWALQQKHWKKRIalhliERRNL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 162 QASALLSVSRALARDMAAMGMLEEHIHVHYTGLDRERFRPleRQAARQLVSAIPAlqvwstGPLLLCVGALVPIKGQAIA 241
Cdd:cd03821 151 NNAALVHFTSEQEADELRRFGLEPPIAVIPNGVDIPEFDP--GLRDRRKHNGLED------RRIILFLGRIHPKKGLDLL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 242 IRALTHLPE---DVRLAIAGTG-GDESALKAMTRQLGLESRVQFLGAVEHDLLPQLLCAADAMVLPSEREGLANAWIEAI 317
Cdd:cd03821 223 IRAARKLAEqgrDWHLVIAGPDdGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEAL 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2163457107 318 ACGTPVII-PDIGGAREVVQDasAGRIVDRTPEAIADAVMDLLENPPAQTDVATNAERF 375
Cdd:cd03821 303 ACGLPVVItDKCGLSELVEAG--CGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRA 359
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
167-390 |
2.18e-25 |
|
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.
Pssm-ID: 132132 [Multi-domain] Cd Length: 374 Bit Score: 105.96 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 167 LSVSRALARDMA-AMGMLEEHIHVHYTGLDRERFRPleRQAARQLVSAIPAlqvwsTGP---LLLCVGALVPIKGQAIAI 242
Cdd:TIGR03088 141 VAVSRDLEDWLRgPVKVPPAKIHQIYNGVDTERFHP--SRGDRSPILPPDF-----FADesvVVGTVGRLQAVKDQPTLV 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 243 RALTHL----PED---VRLAIAGTGGDESALKAMTRQLGLESRVQFLGavEHDLLPQLLCAADAMVLPSEREGLANAWIE 315
Cdd:TIGR03088 214 RAFALLvrqlPEGaerLRLVIVGDGPARGACEQMVRAAGLAHLVWLPG--ERDDVPALMQALDLFVLPSLAEGISNTILE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 316 AIACGTPVIIPDIGGAREVVQDASAGRIVDRT-PEAIADAVMDLLENPPAQTDVATNA-----ERFSWAANAATLAAIYE 389
Cdd:TIGR03088 292 AMASGLPVIATAVGGNPELVQHGVTGALVPPGdAVALARALQPYVSDPAARRAHGAAGraraeQQFSINAMVAAYAGLYD 371
|
.
gi 2163457107 390 K 390
Cdd:TIGR03088 372 Q 372
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
3-362 |
3.32e-24 |
|
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: 102.81 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 3 RLLSISTLYPaPGRTGFGRFVARQMEALAARGDwDVTVVNPIglPPLPLKRYAALRAIpaaERQGAITVHHPRFILL-PG 81
Cdd:cd03794 1 KILLISQYYP-PPKGAAAARVYELAKELVRRGH-EVTVLTPS--PNYPLGRIFAGATE---TKDGIRVIRVKLGPIKkNG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 82 LSGPINPMLI-ARAVLPLARRlhAENPFDLVDAQFFYP-DGPAAAKIARELGLPFAIkargsDIH-LWGDRESA------ 152
Cdd:cd03794 74 LIRRLLNYLSfALAALLKLLV--REERPDVIIAYSPPItLGLAALLLKKLRGAPFIL-----DVRdLWPESLIAlgvlkk 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 153 -------RRQMLDAAKQASALLSVSRALARDMAAMGMLEEHIHVHYTGLDRERFRPLERQAARQLvsaiPALQvwstGPL 225
Cdd:cd03794 147 gsllkllKKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPKDELRKK----LGLD----DKF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 226 -LLCVGALVPIKGQAIAIRALTHLPE--DVRLAIAGTGGDESALKAMTRQLGLeSRVQFLGAVEHDLLPQLLCAADAMVL 302
Cdd:cd03794 219 vVVYAGNIGKAQGLETLLEAAERLKRrpDIRFLFVGDGDEKERLKELAKARGL-DNVTFLGRVPKEEVPELLSAADVGLV 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163457107 303 P-----SEREGLANAWIEAIACGTPVIIPDIGGAREVVQDASAGRIVDRT-PEAIADAVMDLLENP 362
Cdd:cd03794 298 PlkdnpANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGdPEALADAILELLDDP 363
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
95-362 |
8.40e-21 |
|
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: 92.51 E-value: 8.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 95 VLPLARRLHAENPFDLVDAQFfYPDGPAAAKIARELGL--PFAIKARGSDIHLWGDRESAR--RQMLDaakQASALLSVS 170
Cdd:cd03799 58 LLYAIVGLNKKGAYDIIHCQF-GPLGALGALLRRLKVLkgKLVTSFRGYDISMYVILEGNKvyPQLFA---QGDLFLPNC 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 171 RALARDMAAMGMLEEHIHVHYTGLDRERFRPLERQAArqlvsaipalqvwSTGPL-LLCVGALVPIKGQAIAIRALTHLP 249
Cdd:cd03799 134 ELFKHRLIALGCDEKKIIVHRSGIDCNKFRFKPRYLP-------------LDGKIrILTVGRLTEKKGLEYAIEAVAKLA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 250 E---DVRLAIAGTGGDESALKAMTRQLGLESRVQFLGAVEHDLLPQLLCAADAMVLPS------EREGLANAWIEAIACG 320
Cdd:cd03799 201 QkypNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSvtaadgDQDGPPNTLKEAMAMG 280
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2163457107 321 TPVIIPDIGGAREVVQDASAGRIV-DRTPEAIADAVMDLLENP 362
Cdd:cd03799 281 LPVISTEHGGIPELVEDGVSGFLVpERDAEAIAEKLTYLIEHP 323
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
109-376 |
1.06e-20 |
|
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: 92.41 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 109 DLVDAQFFYPDGpAAAKIAREL---GLPFAIKARGSDIHLWGDRESARRQMLDAAKQASALLSVSRALARDMAAMGMLEE 185
Cdd:cd04962 86 DVLHAHYAIPHA-SCAYLAREIlgeKIPIVTTLHGTDITLVGYDPSLQPAVRFSINKSDRVTAVSSSLRQETYELFDVDK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 186 HIHVHYTGLDRERFRpleRQAARQLVSAIPALqvwSTGPLLLCVGALVPIKGQAIAIRALTHLPEDV--RLAIAGTGGDE 263
Cdd:cd04962 165 DIEVIHNFIDEDVFK---RKPAGALKRRLLAP---PDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIpaKLLLVGDGPER 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 264 SALKAMTRQLGLESRVQFLGAVEHdlLPQLLCAADAMVLPSEREGLANAWIEAIACGTPVIIPDIGGAREVVQDASAGRI 343
Cdd:cd04962 239 VPAEELARELGVEDRVLFLGKQDD--VEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFL 316
|
250 260 270
....*....|....*....|....*....|....*....
gi 2163457107 344 VDRTP-EAIADAVMDLLENPP-----AQTDVATNAERFS 376
Cdd:cd04962 317 SDVGDvDAMAKSALSILEDDElynrmGRAARKRAAERFD 355
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
191-338 |
2.63e-20 |
|
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: 91.35 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 191 YTGLDRERFR--PLERQAARQlvsaipALQVWSTGPLLLCVGALVPIKGQAIAIRALTHLPE---DVRLAIAGTGGDESA 265
Cdd:cd04951 160 YNGIDLNKFKkdINVRLKIRN------KLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILsknDFKLLIAGDGPLRNE 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163457107 266 LKAMTRQLGLESRVQFLGAveHDLLPQLLCAADAMVLPSEREGLANAWIEAIACGTPVIIPDIGGAREVVQDA 338
Cdd:cd04951 234 LERLICNLNLVDRVILLGQ--ISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDH 304
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
227-376 |
4.02e-20 |
|
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: 90.81 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 227 LCVGALVPIKGQAIAIRALTHLPEdvRLAIAGTGGDESALKAMTRqlgleSRVQFLGAVEHDLLPQLLCAADAMVLPSER 306
Cdd:cd03804 203 LTASRLVPYKRIDLAVEAFNELPK--RLVVIGDGPDLDRLRAMAS-----PNVEFLGYQPDEVLKELLSKARAFVFAAEE 275
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163457107 307 E-GLANawIEAIACGTPVIIPDIGGAREVVQDASAG-RIVDRTPEAIADAVMDLLENPPAQT--DVATNAERFS 376
Cdd:cd03804 276 DfGIVP--VEAQACGTPVIAFGKGGALETVRPGPTGiLFGEQTVESLKAAVEEFEQNFDRFKpqAIRANAERFS 347
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
166-362 |
9.71e-20 |
|
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: 89.70 E-value: 9.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 166 LLSVSRALArDMAAMGMLEEHIHVH--YTGLDRERFRPLERQAARqlvsaiPALQVWSTGPLLLCV--GALVPIKGQAIA 241
Cdd:cd03825 141 IVAPSRWLA-DMVRRSPLLKGLPVVviPNGIDTEIFAPVDKAKAR------KRLGIPQDKKVILFGaeSVTKPRKGFDEL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 242 IRALTHLPEDVRLAIAGTGGDESalkamtRQLGLESRVQFLGAVEHD-LLPQLLCAADAMVLPSEREGLANAWIEAIACG 320
Cdd:cd03825 214 IEALKLLATKDDLLLVVFGKNDP------QIVILPFDIISLGYIDDDeQLVDIYSAADLFVHPSLADNLPNTLLEAMACG 287
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2163457107 321 TPVIIPDIGGAREVVQDASAGRIVDR-TPEAIADAVMDLLENP 362
Cdd:cd03825 288 TPVVAFDTGGSPEIVQHGVTGYLVPPgDVQALAEAIEWLLANP 330
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
287-393 |
1.21e-19 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 83.89 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 287 HDLLPQLLCAADAMVLPSEREGLANAWIEAIACGTPVIIPDIGGAREVVQDASAGRIVD-RTPEAIADAVMDLLENPPAQ 365
Cdd:COG0438 11 DLLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPpGDPEALAEAILRLLEDPELR 90
|
90 100 110
....*....|....*....|....*....|...
gi 2163457107 366 TDVATNA-----ERFSWAANAATLAAIYEKAAA 393
Cdd:COG0438 91 RRLGEAAreraeERFSWEAIAERLLALYEELLA 123
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
226-377 |
1.94e-19 |
|
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: 88.45 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 226 LLCVGALVPIKG-----QAIAIRALTHlpEDVRLAIAGTGGDESALKAMTRQLGLESRVQFLGAVEHdlLPQLLCAADAM 300
Cdd:cd03820 184 ILAVGRLTYQKGfdlliEAWALIAKKH--PDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLGPTKN--IAEEYANSSIF 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 301 VLPSEREGLANAWIEAIACGTPVIIPDI-GGAREVVQDASAGRIVD-RTPEAIADAVMDLLENPPAQTDVA----TNAER 374
Cdd:cd03820 260 VLSSRYEGFPMVLLEAMAYGLPIISFDCpTGPSEIIEDGENGLLVPnGDVDALAEALLRLMEDEELRKKMGknarKNAER 339
|
...
gi 2163457107 375 FSW 377
Cdd:cd03820 340 FSI 342
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
187-344 |
1.02e-17 |
|
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: 81.68 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 187 IHVHYTGLDRERFRPLERQAARQLVSAIPALQVWstgplllcVGALVPIKGQAIAIRALTHLPE---DVRLAIAGTGGDE 263
Cdd:cd01635 82 VVTVHGPDSLESTRSELLALARLLVSLPLADKVS--------VGRLVPEKGIDLLLEALALLKArlpDLVLVLVGGGGER 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 264 SALKAMTRQLGLESRVQFLGAVEHDLLPQLL-CAADAMVLPSEREGLANAWIEAIACGTPVIIPDIGGAREVVQDASAGR 342
Cdd:cd01635 154 EEEEALAAALGLLERVVIIGGLVDDEVLELLlAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
|
..
gi 2163457107 343 IV 344
Cdd:cd01635 234 LV 235
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
223-376 |
1.76e-17 |
|
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: 83.09 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 223 GPLLLCVGALVPIKGQAIAIRALTHLpeDVRLAIAGTGGDESALKAMTRQLGLEsRVQFLGAVEHDLLPQLLCAADAMVL 302
Cdd:cd03795 191 KKIFLFIGRLVYYKGLDYLIEAAQYL--NYPIVIGGEGPLKPDLEAQIELNLLD-NVKFLGRVDDEEKVIYLHLCDVFVF 267
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163457107 303 PS-ER-EGLANAWIEAIACGTPVIIPDIG-GAREVVQDASAGRIVD-RTPEAIADAVMDLLENPPAQTDVATNAE-RFS 376
Cdd:cd03795 268 PSvLRsEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVPpKDPDALAEAIDKLLSDEELRESYGENAKkRFE 346
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
225-361 |
6.20e-17 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).
Pssm-ID: 340840 [Multi-domain] Cd Length: 357 Bit Score: 81.18 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 225 LLLC-VGALVPIKGQAIAIRALTHLPE---DVRLAIAGTGGDESALKAMTRQLGLESRVQFLGAVEHdlLPQLLCAADAM 300
Cdd:cd03812 192 LVLGhVGRFNEQKNHSFLIDIFEELKKknpNVKLVLVGEGELKEKIKEKVKELGLEDKVIFLGFRND--VSEILSAMDVF 269
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163457107 301 VLPSEREGLANAWIEAIACGTPVIIPDIGGAREVVQDASAGRIVDRTPEAIADAVMDLLEN 361
Cdd:cd03812 270 LFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITNNVEFLPLNETPSTWAEKILKLIKR 330
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
159-362 |
1.93e-16 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340841 [Multi-domain] Cd Length: 474 Bit Score: 80.84 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 159 AAKQASALLSVSRALARDMAAMGMLEEHIHVHYTGLDRERFRPLERQAARqlvsaipalqvwSTGPLLLCVGALVPIKGQ 238
Cdd:cd03813 241 AYQQADKIISLYEGNRRRQIRLGADPDKTRVIPNGIDIQRFAPAREERPE------------KEPPVVGLVGRVVPIKDV 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 239 AIAIRALTHLPE---DVRLAIAG-TGGDESAL---KAMTRQLGLESRVQFLGAVE-HDLLPQLlcaaDAMVLPSEREGLA 310
Cdd:cd03813 309 KTFIRAFKLVRRampDAEGWLIGpEDEDPEYAqecKRLVASLGLENKVKFLGFQNiKEYYPKL----GLLVLTSISEGQP 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2163457107 311 NAWIEAIACGTPVIIPDIGGAREVVQDA-----SAGRIVD-RTPEAIADAVMDLLENP 362
Cdd:cd03813 385 LVILEAMASGVPVVATDVGSCRELIYGAddalgQAGLVVPpADPEALAEALIKLLRDP 442
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
224-389 |
3.68e-16 |
|
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.
Pssm-ID: 340849 [Multi-domain] Cd Length: 370 Bit Score: 79.35 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 224 PLLLCVGALVPIKGQAIAIRALTHLP---EDVRLAIAGTGGD-------ESALKAMTRQLGLESRVQF-LGAVEHDLLPQ 292
Cdd:cd03822 188 KVILTFGFIGPGKGLEILLEALPELKaefPDVRLVIAGELHPslaryegERYRKAAIEELGLQDHVDFhNNFLPEEEVPR 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 293 LLCAADAMVLP--SEREGLANAWIEAIACGTPVIIPDIGGAREVVQDASAGRIVDRTPEAIADAVMDLLENPPAQTDVAT 370
Cdd:cd03822 268 YISAADVVVLPylNTEQSSSGTLSYAIACGKPVISTPLRHAEELLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAE 347
|
170 180
....*....|....*....|...
gi 2163457107 371 NAER----FSWAANAATLAAIYE 389
Cdd:cd03822 348 RAYAyaraMTWESIADRYLRLFN 370
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
3-365 |
1.52e-15 |
|
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: 76.94 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 3 RLLSISTLYPAPGRTGFG---RFVARQMEALAARGDwDVTVVNPIGLPPLplkryAALRAIPAAerqgaitvhhprfilL 79
Cdd:cd03802 1 RIAQVSPPRGPVPPGKYGgteLVVSALTEGLVRRGH-EVTLFAPGDSHTS-----APLVAVIPR---------------A 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 80 PGLSGPINPMLIARAVLPLARRLHAeNPFDLVDAQFFYPDGPAAakiaRELGLPFAikargSDIHLWGDRESARRQMLDA 159
Cdd:cd03802 60 LRLDPIPQESKLAELLEALEVQLRA-SDFDVIHNHSYDWLPPFA----PLIGTPFV-----TTLHGPSIPPSLAIYAAEP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 160 AkqaSALLSVSRALARDMAAMgmleEHIHVHYTGLDRERFRPLERQaarqlvsaipalqvwstGPLLLCVGALVPIKG-- 237
Cdd:cd03802 130 P---VNYVSISDAQRAATPPI----DYLTVVHNGLDPADYRFQPDP-----------------EDYLAFLGRIAPEKGle 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 238 QAIAIRALTHLPedvrLAIAGTGGDESALKaMTRQLGLESRVQFLGAVEHDLLPQLLCAADAMVLPSE-REGLANAWIEA 316
Cdd:cd03802 186 DAIRVARRAGLP----LKIAGKVRDEDYFY-YLQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPINwDEPFGLVMIEA 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2163457107 317 IACGTPVIIPDIGGAREVVQDASAGRIVDrTPEAIADAVMDLLENPPAQ 365
Cdd:cd03802 261 MACGTPVIAYRRGGLPEVIQHGETGFLVD-SVEEMAEAIANIDRIDRAA 308
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
159-388 |
2.19e-15 |
|
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274943 [Multi-domain] Cd Length: 373 Bit Score: 77.05 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 159 AAKQASALLSVSRALARDMAAmgmlEEHIH--VHYTGLDRERFRPlerQAARQLVSAIPALQVwSTGPLLLCVGALVPIK 236
Cdd:TIGR04047 135 AIVEADAVLCVSAAWAAELRA----EWGIDatVVPNGVDAARFSP---AADAADAALRRRLGL-RGGPYVLAVGGIEPRK 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 237 GQAIAIRALTHLPE---DVRLAIAGT------GGDESALKAMTRQLGLE-SRVQFLGAVEHDLLPQLLCAADAMVLPSER 306
Cdd:TIGR04047 207 NTIDLLEAFALLRArrpQAQLVIAGGatlfdyDAYRREFRARAAELGVDpGPVVITGPVPDADLPALYRCADAFAFPSLK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 307 EGLANAWIEAIACGTPVIIPDIGGAREVVQDASAGRIVDRTPEAIADAVMDLLENP--PAQTD-VATNAERFSWAANAAT 383
Cdd:TIGR04047 287 EGFGLVVLEALASGIPVVASDIAPFTEYLGRFDAAWADPSDPDSIADALALALDPArrPALRAaGPELAARYTWDASARA 366
|
....*
gi 2163457107 384 LAAIY 388
Cdd:TIGR04047 367 HLEFY 371
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
187-374 |
1.32e-13 |
|
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: 71.63 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 187 IHVHYTGLDRERFRPlERQAARQLvsaiPALQVWSTGPLLLCVGA--LVPIKGQAIAIRALTHLPE---DVRLAIagTGG 261
Cdd:cd03818 181 ISVIHDGVDTDRLAP-DPAARLRL----LNGTELKAGDPVITYVArnLEPYRGFHVFMRALPRIQArrpDARVVV--VGG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 262 DESALKA-----------MTRQLGLE-SRVQFLGAVEHDLLPQLLCAADAMVLPSEREGLANAWIEAIACGTPVIIPDIG 329
Cdd:cd03818 254 DGVSYGSpppdggswkqkMLAELGVDlERVHFVGKVPYDQYVRLLQLSDAHVYLTYPFVLSWSLLEAMACGCPVIGSDTA 333
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2163457107 330 GAREVVQDASAGRIVD-RTPEAIADAVMDLLENPPAQTDVATNAER 374
Cdd:cd03818 334 PVREVIRDGRNGLLVDfFDPDALAAAVLELLEDPDRAAALRRAARR 379
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
193-364 |
2.77e-13 |
|
GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.
Pssm-ID: 411604 [Multi-domain] Cd Length: 489 Bit Score: 71.11 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 193 GLDRERFRPLerQAARQlvSAIPalqvwstgPLLLCVGALVPIKGQAIAIRAL----THLPEdVRLAIAGTGGDESALKA 268
Cdd:NF038011 288 GIDLPRLAPL--RAQRP--AGIP--------PVVGLIGRVVPIKDIKTFIRAMrtvvRAMPE-AEGWIVGPEEEDPAYAA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 269 MTRQ----LGLESRVQFLGAVE-HDLLPQLlcaaDAMVLPSEREGLANAWIEAIACGTPVIIPDIGGAREVV-----QDA 338
Cdd:NF038011 355 ECRSlvasLGLQDKVKFLGFQKiDDLLPQV----GLMVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLIegldeEDR 430
|
170 180 190
....*....|....*....|....*....|
gi 2163457107 339 ---SAGRIVD-RTPEAIADAVMDLLENPPA 364
Cdd:NF038011 431 algAAGEVVAiADPQALARAALDLLRDPQR 460
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
163-377 |
1.99e-11 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 65.12 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 163 ASALLSVSRALARDMAAMGMLE-EHIHVHYTGLDRERFRPLERQAA--RQLVSAIPAlqvwstGPLLLCVGALVPIKGQA 239
Cdd:PLN02871 206 ADLTLVTSPALGKELEAAGVTAaNRIRVWNKGVDSESFHPRFRSEEmrARLSGGEPE------KPLIVYVGRLGAEKNLD 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 240 IAIRALTHLPEdVRLAIAGTGGDESALKAMTRQLglesRVQFLGAVEHDLLPQLLCAADAMVLPSEREGLANAWIEAIAC 319
Cdd:PLN02871 280 FLKRVMERLPG-ARLAFVGDGPYREELEKMFAGT----PTVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMAS 354
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163457107 320 GTPVIIPDIGGAREVVQDASAGRI-VDRTPEAIADAV---MDLLENPPAQTDVATNA----ERFSW 377
Cdd:PLN02871 355 GVPVVAARAGGIPDIIPPDQEGKTgFLYTPGDVDDCVeklETLLADPELRERMGAAAreevEKWDW 420
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
258-362 |
2.25e-10 |
|
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: 61.71 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 258 GTGGDESALKAMTRQLGLESRVQFLGAVEHDLLPQLLC--AADAMVLPSEREGLANAWIEAIACGTPVIIPDIGGAREVV 335
Cdd:cd04946 264 GGGPLKERLEKLAENKLENVKVNFTGEVSNKEVKQLYKenDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIV 343
|
90 100
....*....|....*....|....*....
gi 2163457107 336 QDASAGRIVDR--TPEAIADAVMDLLENP 362
Cdd:cd04946 344 ENETNGLLLDKdpTPNEIVSSIMKFYLDG 372
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
18-197 |
1.06e-09 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 57.16 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 18 GFGRFVARQMEALAARGdWDVTVVNPiglpplplkryaalrAIPAAERQGAITVHHPRFILLPGLSGPInpmLIARAVLP 97
Cdd:pfam13439 2 GVERYVLELARALARRG-HEVTVVTP---------------GGPGPLAEEVVRVVRVPRVPLPLPPRLL---RSLAFLRR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 98 LARRLHAENPfDLVDAQFFYPDGPAAAKIARELGLPF-------AIKARGSDIHLWGDRESARRQMLDAAKQASALLSVS 170
Cdd:pfam13439 63 LRRLLRRERP-DVVHAHSPFPLGLAALAARLRLGIPLvvtyhglFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVS 141
|
170 180
....*....|....*....|....*...
gi 2163457107 171 RALARDMAA-MGMLEEHIHVHYTGLDRE 197
Cdd:pfam13439 142 EAVADELRRlYGVPPEKIRVIPNGVDLE 169
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
229-376 |
1.74e-08 |
|
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: 55.39 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 229 VGALVPIKGQAIAIRALTHLPE---DVRLAIAGTGGDESALKAMTRQLGLESRVQFLGAveHDLLPQLLCAADAMVLPSE 305
Cdd:cd04949 166 ISRLAPEKQLDHLIEAVAKAVKkvpEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGY--HSNLDQEYQDAYLSLLTSQ 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163457107 306 REGLANAWIEAIACGTPVIIPDIG-GAREVVQDASAG-RIVDRTPEAIADAVMDLLENPPAQTDVAT----NAERFS 376
Cdd:cd04949 244 MEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGyLIEKNNIDALADKIIELLNDPEKLQQFSEesykIAEKYS 320
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
242-355 |
7.42e-08 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 53.95 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 242 IRALTHLPEDVRLAIAGTGGDESALKAMTRQLGLESRVQFLGAVEH--DLLPQLLCAADAMVLPSEREGLANAWIEAIAC 319
Cdd:PRK09922 201 FDGLSQTTGEWQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQpwEVVQQKIKNVSALLLTSKFEGFPMTLLEAMSY 280
|
90 100 110
....*....|....*....|....*....|....*..
gi 2163457107 320 GTPVIIPD-IGGAREVVQDASAGRIVdrTPEAIADAV 355
Cdd:PRK09922 281 GIPCISSDcMSGPRDIIKPGLNGELY--TPGNIDEFV 315
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
236-362 |
2.87e-07 |
|
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: 52.21 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 236 KGQAIAIRAL----THLPE--DVRLAIAGtGGD----------ESALKAMTRQLGLESRVQFLGAVEHDLLPQLLCAADA 299
Cdd:cd03805 224 KNIALAIEAFaklkQKLPEfeNVRLVIAG-GYDprvaenveylEELQRLAEELLNVEDQVLFLRSISDSQKEQLLSSALA 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163457107 300 MVLPSEREGLANAWIEAIACGTPVIIPDIGGAREVVQDASAGRIVDRTPEAIADAVMDLLENP 362
Cdd:cd03805 303 LLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLANDP 365
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
229-395 |
3.67e-07 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 51.86 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 229 VGALVPIKGQAIAIRA---LTHLPEDVRLAIAGTGGDESALKAMTRQLGLESRVQFLGAVEHDLLPQLLCAADAMVLPSE 305
Cdd:cd03796 199 ISRLVYRKGIDLLVGIiprICKKHPNVRFIIGGDGPKRIELEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 306 REGLANAWIEAIACGTPVIIPDIGGAREVVQDaSAGRIVDRTPEAIADAVMDLLEN-PPAQTDVATNAER----FSWAAN 380
Cdd:cd03796 279 TEAFCIAIVEAASCGLLVVSTRVGGIPEVLPP-DMILLAEPDPEDIVRKLEEAISIlRTGKHDPWSFHNRvkkmYSWEDV 357
|
170
....*....|....*
gi 2163457107 381 AATLAAIYEKAAARP 395
Cdd:cd03796 358 ARRTEKVYDRILSTP 372
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
225-377 |
1.06e-06 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 50.17 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 225 LLLCVGALVPIKGQAIAIRALTHLPE---DVRLAIAG-----TGGDESALKAMTRQLG--LESRVQFLGAVEHDLLPQLL 294
Cdd:PRK15484 195 VLLYAGRISPDKGILLLMQAFEKLATahsNLKLVVVGdptasSKGEKAAYQKKVLEAAkrIGDRCIMLGGQPPEKMHNYY 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 295 CAADAMVLPSE-REGLANAWIEAIACGTPVIIPDIGGAREVVQDASAGRIVDR--TPEAIADAVMDLLENpPAQTDVATN 371
Cdd:PRK15484 275 PLADLVVVPSQvEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLAEpmTSDSIISDINRTLAD-PELTQIAEQ 353
|
170
....*....|.
gi 2163457107 372 AERF-----SW 377
Cdd:PRK15484 354 AKDFvfskySW 364
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
17-193 |
3.84e-06 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 46.63 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 17 TGFGRFVARQMEALAARGdWDVTVVNPiglpplplkryaALRAIPAAERQGAITVHHprfILLPGLSGPINPMLIARAVl 96
Cdd:pfam13579 1 GGIGVYVLELARALAALG-HEVRVVTP------------GGPPGRPELVGDGVRVHR---LPVPPRPSPLADLAALRRL- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 97 plaRRLHAENPFDLVDAQFFYPdGPAAAKIARELGLPFAIKARGSDIHLWGDRESARRQMLD--AAKQASALLSVSRALA 174
Cdd:pfam13579 64 ---RRLLRAERPDVVHAHSPTA-GLAARLARRRRGVPLVVTVHGLALDYGSGWKRRLARALErrLLRRADAVVVVSEAEA 139
|
170
....*....|....*....
gi 2163457107 175 RDMAAMGMLEEHIHVHYTG 193
Cdd:pfam13579 140 ELLRALGVPAARVVVVPNG 158
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
221-345 |
8.75e-06 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 47.77 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 221 STGPLLLCVGALVPIKGQAIAIRALTHLPEdVRLAIAGTGGDESALKAMTRQLGLESRVQFLGaVEHDLlPQLLCAADAM 300
Cdd:PRK15490 400 TIGGVFRFVGDKNPFAWIDFAARYLQHHPA-TRFVLVGDGDLRAEAQKRAEQLGILERILFVG-ASRDV-GYWLQKMNVF 476
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2163457107 301 VLPSEREGLANAWIEAIACGTPVIIPDIGGAREVVQDASAGRIVD 345
Cdd:PRK15490 477 ILFSRYEGLPNVLIEAQMVGVPVISTPAGGSAECFIEGVSGFILD 521
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
252-341 |
1.20e-05 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 47.34 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 252 VRLAIAGTGGDESALKAMTRQLGLESRVQFLGAVEHdlLPQLLCAADAMVLPSEREGLANAWIEAIACGTPVIIPDIGGA 331
Cdd:PRK15179 549 VRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRR--VGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGA 626
|
90
....*....|
gi 2163457107 332 REVVQDASAG 341
Cdd:PRK15179 627 GEAVQEGVTG 636
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
29-362 |
2.13e-05 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 46.39 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 29 ALAARGDwDVTVVNPIGLPPLPLKRYAA-LRAIPAAERQGAITVHHPRFILLPGLSGPINPMLIARAVLPLARRLHAENP 107
Cdd:cd03784 23 ALAARGH-EVTVATPPFNFADLVEAAGLtFVPVGDDPDELELDSETNLGPDSLLELLRRLLKAADELLDDLLAALRSSWK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 108 FDLVDAQFFypdGPAAAKIARELGLPFAIKARGSDIHLWGDRESARRQMLDAAKQASALLSVSRALA--RDMAAMGMLEE 185
Cdd:cd03784 102 PDLVIADPF---AYAGPLVAEELGIPSVRLFTGPATLLSAYLHPFGVLNLLLSSLLEPELFLDPLLEvlDRLRERLGLPP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 186 HIHVHYTGLDRER-------FRPLERQAARQLVSAIPALQVWSTGPL-----------------LLC---VGALVPIKGQ 238
Cdd:cd03784 179 FSLVLLLLRLVPPlyvigptFPSLPPDRPRLPSVLGGLRIVPKNGPLpdelwewldkqpprsvvYVSfgsMVRDLPEELL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 239 AIAIRALTHLPEDVRLAIAGTGGDESAlkamtrqlGLESRVQFLGAVehdllPQLLcaadamVLPSEREGL------ANA 312
Cdd:cd03784 259 ELIAEALASLGQRFLWVVGPDPLGGLE--------RLPDNVLVVKWV-----PQDE------LLAHPAVGAfvthggWNS 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2163457107 313 WIEAIACGTP-VIIP---DIGGAREVVQDASAGRIVDR---TPEAIADAVMDLLENP 362
Cdd:cd03784 320 TLEALYAGVPmVVVPlfaDQPNNAARVEELGAGVELDKdelTAEELAKAVREVLEDE 376
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
241-375 |
3.70e-04 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 42.27 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 241 AIRALTHLPeDVRLAIAGTGGDESALKAMTRQLGLeSRVQFLGAVEHDLLPQLLCAADAMVLPsEREGLANAWIEA---- 316
Cdd:PRK10307 250 AARRLRDRP-DLIFVICGQGGGKARLEKMAQCRGL-PNVHFLPLQPYDRLPALLKMADCHLLP-QKAGAADLVLPSkltn 326
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163457107 317 -IACGTPVII---PDIGGAREVvqdASAGRIVD-RTPEAIADAVMDLLENPPAQTDVATNAERF 375
Cdd:PRK10307 327 mLASGRNVVAtaePGTELGQLV---EGIGVCVEpESVEALVAAIAALARQALLRPKLGTVAREY 387
|
|
| KdtA |
COG1519 |
3-deoxy-D-manno-octulosonic-acid transferase [Cell wall/membrane/envelope biogenesis]; ... |
314-375 |
1.44e-03 |
|
3-deoxy-D-manno-octulosonic-acid transferase [Cell wall/membrane/envelope biogenesis]; 3-deoxy-D-manno-octulosonic-acid transferase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 441128 [Multi-domain] Cd Length: 424 Bit Score: 40.51 E-value: 1.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163457107 314 IEAIACGTPVII-PDIGGAREVVQD---ASAGRIVdRTPEAIADAVMDLLENPPAQTDVATNAERF 375
Cdd:COG1519 338 LEPAALGKPVLFgPHTFNFAEAAELliaAGAAIQV-ADAEELAAAVLALLADPELRAAMGAAARAV 402
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
219-374 |
2.96e-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: 39.61 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 219 VWSTGPLLLCVGALVPIKGQAIAIRA---LTHLPEDVRLAIAGTGGD---ESAL---KAMTRQlGLESRVQFLGAVEHD- 288
Cdd:cd03792 193 IDPERPYILQVARFDPSKDPLGVIDAyklFKRRAEEPQLVICGHGAVddpEGSVvyeEVMEYA-GDDHDIHVLRLPPSDq 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 289 LLPQLLCAADAMVLPSEREGLANAWIEAIACGTPVIIPDIGGAREVVQDASAGRIVDrTPEAIADAVMDLLENPPAQTDV 368
Cdd:cd03792 272 EINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVN-SVEGAAVRILRLLTDPELRRKM 350
|
....*.
gi 2163457107 369 ATNAER 374
Cdd:cd03792 351 GLAARE 356
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
185-377 |
4.08e-03 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 39.08 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 185 EHIHVHYTGLDRERfRPLERQAARQLVSaipaLQVWSTGPLLLCVGALVPIKG---QAIAIRALTHlpEDVRLAIAGTG- 260
Cdd:cd03791 261 KLIPANYSANDLEG-KAENKAALQKELG----LPVDPDAPLFGFVGRLTEQKGvdlILDALPELLE--EGGQLVVLGSGd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 261 -GDESALKAMTRQLGLESRVqFLGAVEHdlLPQLLCA-ADAMVLPSERE--GLaNAwIEAIACGTPVIIPDIGGAREVVQ 336
Cdd:cd03791 334 pEYEQAFRELAERYPGKVAV-VIGFDEA--LAHRIYAgADFFLMPSRFEpcGL-VQ-MYAMRYGTLPIVRRTGGLADTVF 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2163457107 337 DASA------GRIVDR-TPEAIADAV---MDLLENPPAQTDVATNA--ERFSW 377
Cdd:cd03791 409 DYDPetgegtGFVFEDyDAEALLAALrraLALYRNPELWRKLQKNAmkQDFSW 461
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
261-362 |
4.43e-03 |
|
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). 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: 340861 [Multi-domain] Cd Length: 364 Bit Score: 38.84 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 261 GDESALK-AMTRQLGLESRVQFLGAVEHdlLPQLLCAADAMVlpSEREGLANAwiEAIACGTPVIIPDIGGAREV----- 334
Cdd:cd17507 233 GKNKKLYeKLSGLEEDYINVRVLGYVDD--MNELMAASDLVI--TKPGGLTIS--EALARGLPVIIYDPIPGQEEenadf 306
|
90 100
....*....|....*....|....*...
gi 2163457107 335 VQDASAGRIVdRTPEAIADAVMDLLENP 362
Cdd:cd17507 307 LENNGAGIIA-RDPEELLEIVARLIDPP 333
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
239-376 |
9.55e-03 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 37.53 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163457107 239 AIAIRALTHLpeDVRLAIAGTGGDESALKAmtrqlgLESRVQFLGAVEHD-LLPQllcaADAMVLPsereGLANAWIEAI 317
Cdd:COG1819 139 RAVLEALADL--GVRVVVTTGGLDPAELGP------LPDNVRVVDYVPQDaLLPR----ADAVVHH----GGAGTTAEAL 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163457107 318 ACGTP-VIIPDIG-----GARevVQDASAGRIVDR---TPEAIADAVMDLLENPpaqtDVATNAERFS 376
Cdd:COG1819 203 RAGVPqVVVPFGGdqplnAAR--VERLGAGLALPPrrlTAEALRAALRRLLADP----SYRERAARLA 264
|
|
| |
