|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
14-379 |
6.11e-59 |
|
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: 196.22 E-value: 6.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 14 LLEVLEPGGGGSGRHFLDLCRGMHVRGHHVEAIysPVRAEDGFVRELKAlglpaiHAVGMRRAPGPSDWSCLRAIN--RI 91
Cdd:cd03801 5 LSPELPPPVGGAERHVRELARALAARGHDVTVL--TPADPGEPPEELED------GVIVPLLPSLAALLRARRLLRelRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 92 IRTAGPFDVIHGHSSKAGALTRLRLPGRHVPRVYTPHAFRTMDPTLGRGG--RLIYGAIETLlarFFTDHLVAVSGDEFA 169
Cdd:cd03801 77 LLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAerRLLARAEALL---RRADAVIAVSEALRD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 170 HALSI-GISGKGMSVIVNGVDTPSPDMAqtVRASFGIPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGS 248
Cdd:cd03801 154 ELRALgGIPPEKIVVIPNGVDLERFSPP--LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 249 -GELEEEVRAAIAasGLQNRIHLTSaFTGPQAVPAF----DLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDH 323
Cdd:cd03801 232 dGPLRAELEELEL--GLGDRVRFLG-FVPDEELPALyaaaDVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVED 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1549894312 324 GENGYIVPNsEDVSPLARAMI-AAADPE-MFRRLAGAAAARRDRFTLKRMLDETEEVY 379
Cdd:cd03801 309 GEGGLVVPP-DDVEALADALLrLLADPElRARLGRAARERVAERFSWERVAERLLDLY 365
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
23-351 |
1.32e-56 |
|
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: 190.11 E-value: 1.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 23 GGSGRHFLDLCRGMHVRGHHVEAIYSPVRAEDgfvRELKALGLPAIHAVGMRRAPGP-SDWSCLRAINRIIRTAGPfDVI 101
Cdd:cd03808 10 GGFQSFRLPLIKALVKKGYEVHVIAPDGDKLS---DELKELGVKVIDIPILRRGINPlKDLKALFKLYKLLKKEKP-DIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 102 HGHSSKAGALTRL--RLPGRHvPRVYTPHAFRTMDpTLGRGGRLIYGAIETLLARFfTDHLVAVSGDEFAHALSIGISGK 179
Cdd:cd03808 86 HCHTPKPGILGRLaaRLAGVP-KVIYTVHGLGFVF-TEGKLLRLLYLLLEKLALLF-TDKVIFVNEDDRDLAIKKGIIKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 180 GMSVIVNGVdtpSPDMAQTVRASFGIPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGSGELEEEVRAAI 259
Cdd:cd03808 163 KKTVLIPGS---GVDLDRFQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 260 AASGLQNRIHltsaFTGP-QAVPAF----DLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDHGENGYIVPnSE 334
Cdd:cd03808 240 EKLGLEGRIE----FLGFrSDVPELlaesDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVP-PG 314
|
330
....*....|....*...
gi 1549894312 335 DVSPLARAMIAAA-DPEM 351
Cdd:cd03808 315 DVEALADAIEKLIeDPEL 332
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
21-349 |
2.38e-46 |
|
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: 162.91 E-value: 2.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 21 GGGGSGRHFLDLCRGMHVRGHHVE-AIYSPVRAEDGFVRELKALGLPAIHAVgmrRAPGPSDWSCLRAINRIIRTAgPFD 99
Cdd:cd03811 10 SGGGAERVLLNLANALDKRGYDVTlVLLRDEGDLDKQLNGDVKLIRLLIRVL---KLIKLGLLKAILKLKRILKRA-KPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 100 VIHGHSSKAGALTRLrLPGRHVPRVYTPHafrtMDPTLGRGGRLIYGAIETLLARFftDHLVAVSGD--EFAHALSiGIS 177
Cdd:cd03811 86 VVISFLGFATYIVAK-LAAARSKVIAWIH----SSLSKLYYLKKKLLLKLKLYKKA--DKIVCVSKGikEDLIRLG-PSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 178 GKGMSVIVNGVDTPSPDMaQTVRASFGIPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGSGELEEEVRA 257
Cdd:cd03811 158 PEKIEVIYNPIDIDRIRA-LAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 258 AIAASGLQNRIHltsaFTGPQAVP-----AFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDHGENGYIVPN 332
Cdd:cd03811 237 LAKELGLAERVI----FLGFQSNPypylkKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPD 312
|
330
....*....|....*..
gi 1549894312 333 SeDVSPLARAMIAAADP 349
Cdd:cd03811 313 G-DAAALAGILAALLQK 328
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
23-379 |
1.63e-43 |
|
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: 155.55 E-value: 1.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 23 GGSGRHFLDLCRGMHVRGHHVEAIYspVRAEDGFVRELKALGLPaIHAVGMRraPGPSDWSCLRAInRIIRTAGPfDVIH 102
Cdd:cd03807 12 GGAETMLLRLLEHMDKSRFEHVVIS--LTGDGVLGEELLAAGVP-VVCLGLS--SGKDPGVLLRLA-KLIRKRNP-DVVH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 103 GHSSKAGALTRLRLPGRHVPRVYtpHAFRTMDpTLGRGGRLIYgAIETLLARFFTDhLVAVSGDEFAHALSIGISGKGMS 182
Cdd:cd03807 85 TWMYHADLIGGLAAKLAGGVKVI--WSVRSSN-IPQRLTRLVR-KLCLLLSKFSPA-TVANSSAVAEFHQEQGYAKNKIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 183 VIVNGVD----TPSPDMAQTVRASFGIPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGSGELEEEVRAA 258
Cdd:cd03807 160 VIYNGIDlfklSPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 259 IAASGLQNRIHltsaFTG-----PQAVPAFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDHGeNGYIVPNs 333
Cdd:cd03807 240 LLELGLEDRVH----LLGersdvPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPA- 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1549894312 334 EDVSPLARAMIAAAD--PEMFRRLAGAAAARRDRFTLKRMLDETEEVY 379
Cdd:cd03807 314 GDPQALADAIRALLEdpEKRARLGRAARERIANEFSIDAMVRRYETLY 361
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
12-348 |
2.43e-40 |
|
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: 146.73 E-value: 2.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 12 LRLLEVLEPGGGGsgRHFLDLCRGMHVRGHHVeaiyspVRAEDGF--VRELKALGLPaihaVGMRRAPGPSDWSCLRAIN 89
Cdd:cd03819 2 LMLTPALEIGGAE--TYILDLARALAERGHRV------LVVTAGGplLPRLRQIGIG----LPGLKVPLLRALLGNVRLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 90 RIIRTAGPfDVIHGHSSKAGALTRLRLPGRHVPRVYTPH--AFRTMDPTLGRggrliygaietLLARFFTDHLVAVSGDE 167
Cdd:cd03819 70 RLIRRERI-DLIHAHSRAPAWLGWLASRLTGVPLVTTVHgsYLATYHPKDFA-----------LAVRARGDRVIAVSELV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 168 FAHAL-SIGISGKGMSVIVNGVDTPSPDMAQTV--RASFGIPADAFVFGFIGRLSAQKAPERLLNAFGKAAsAVRNSHVV 244
Cdd:cd03819 138 RDHLIeALGVDPERIRVIPNGVDTDRFPPEAEAeeRAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELK-DEPDFRLL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 245 MVGSGELEEEVRAAIAASGLQNRIHltsaFTGP-QAVPAF----DLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGT 319
Cdd:cd03819 217 VAGDGPERDEIRRLVERLGLRDRVT----FTGFrEDVPAAlaasDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGARE 292
|
330 340
....*....|....*....|....*....
gi 1549894312 320 AVDHGENGYIVPNsEDVSPLARAMIAAAD 348
Cdd:cd03819 293 IVVHGRTGLLVPP-GDAEALADAIRAAKL 320
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
23-350 |
6.40e-33 |
|
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: 127.11 E-value: 6.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 23 GGSGRHFLDLCRGMHVRGH--HVEAIYSPVRAEDGFVRELKALGLP---AIHAVGMRRAPGPSDWSCLRAINRII--RTA 95
Cdd:cd03798 14 PGRGIFVRRQVRALSRRGVdvEVLAPAPWGPAAARLLRKLLGEAVPprdGRRLLPLKPRLRLLAPLRAPSLAKLLkrRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 96 GPFDVIHGH-SSKAGALTRL--RLPGrhVPRVYTPHAFRTMDPTLGRGGRLIYGAIetlLARFftDHLVAVSGDEFAHAL 172
Cdd:cd03798 94 GPPDLIHAHfAYPAGFAAALlaRLYG--VPYVVTEHGSDINVFPPRSLLRKLLRWA---LRRA--ARVIAVSKALAEELV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 173 SIGISGKGMSVIVNGVDtpsPDMAQTVRASFGIPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGSGELE 252
Cdd:cd03798 167 ALGVPRDRVDVIPNGVD---PARFQPEDRGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 253 EEVRAAIAASGLQNRIHLTSAFTgPQAVPAF----DLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDHGENGY 328
Cdd:cd03798 244 EALRALAEDLGLGDRVTFTGRLP-HEQVPAYyracDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGL 322
|
330 340
....*....|....*....|..
gi 1549894312 329 IVPnSEDVSPLARAMIAAADPE 350
Cdd:cd03798 323 LVP-PGDADALAAALRRALAEP 343
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
85-314 |
1.39e-26 |
|
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: 109.30 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 85 LRAINRIIRtAGPFDVIHGHSSKAGALTRLRLPGRHVP-RVYTPHAFRTMDptlGRGGRLIYGAIETLLARFFTDHLvAV 163
Cdd:cd03812 69 FIKLLKLIK-KEKYDIVHVHGSSSNGIILLLAAKAGVPvRIAHSHNTKDSS---IKLRKIRKNVLKKLIERLSTKYL-AC 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 164 SgDEFAHALSIGISGKGMSVIVNGVD----TPSPDMAQTVRASfGIPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVR 239
Cdd:cd03812 144 S-EDAGEWLFGEVENGKFKVIPNGIDiekyKFNKEKRRKRRKL-LILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 240 NSHVVMVGSGELEEEVRAAIAASGLQNRIHltsaFTG-----PQAVPAFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDV 314
Cdd:cd03812 222 NVKLVLVGEGELKEKIKEKVKELGLEDKVI----FLGfrndvSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDT 297
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
19-331 |
4.00e-26 |
|
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: 108.87 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 19 EPGG---GGSGRHFLDLCRGMHVRGHHVEAIYSPVRAEDGFVRELkalglpAIHAVGMRRAPGPSD-------WSCLRA- 87
Cdd:cd03800 14 QPGGadtGGQNVYVLELARALAELGYQVDIFTRRISPADPEVVEI------APGARVIRVPAGPPEylpkeelWPYLEEf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 88 ----INRIIRTAGPFDVIHGH---SSKAGALTRLRLpgrHVPRVYTPHAF-RTMDPTLGRGGR----LIYGAIETLLARf 155
Cdd:cd03800 88 adglLRFIAREGGRYDLIHSHywdSGLVGALLARRL---GVPLVHTFHSLgRVKYRHLGAQDTyhpsLRITAEEQILEA- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 156 fTDHLVAVSGDEFAHALS-IGISGKGMSVIVNGVDT----PSPDmAQTVRASFGIPADAFVFGFIGRLSAQKAPERLLNA 230
Cdd:cd03800 164 -ADRVIASTPQEADELISlYGADPSRINVVPPGVDLerffPVDR-AEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 231 FGKAASAVRNSHVVMVG-----SGELEEEVRAAIAAS-GLQNRIHlTSAFTGPQAVPAF----DLLVMPSRYEAMSYVML 300
Cdd:cd03800 242 FAQLPELRELANLVLVGgpsddPLSMDREELAELAEElGLIDRVR-FPGRVSRDDLPELyraaDVFVVPSLYEPFGLTAI 320
|
330 340 350
....*....|....*....|....*....|.
gi 1549894312 301 EAAAAGRPIIISDVGGAGTAVDHGENGYIVP 331
Cdd:cd03800 321 EAMACGTPVVATAVGGLQDIVRDGRTGLLVD 351
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
209-345 |
2.34e-25 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 100.28 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 209 AFVFGFIGRLSA-QKAPERLLNAFGKAASAVRNSHVVMVGSGElEEEVRAAIAasGLQNRIHltsaFTG-----PQAVPA 282
Cdd:pfam13692 1 RPVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGP-EEELEELAA--GLEDRVI----FTGfvedlAELLAA 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1549894312 283 FDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVdHGENGYIVPNsEDVSPLARAMIA 345
Cdd:pfam13692 74 ADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPP-GDPEALAEAILR 134
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
208-351 |
1.11e-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: 98.89 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 208 DAFVFGFIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGSGELEEEVRAAIAASGLQNRIHLTSaFTGPQAVPAF---- 283
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLG-FVSDEDLPELlkia 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1549894312 284 DLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDHGENGYIVPNsEDVSPLARAMIAA-ADPEM 351
Cdd:pfam00534 80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKP-NNAEALAEAIDKLlEDEEL 147
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
32-344 |
3.93e-24 |
|
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: 102.74 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 32 LCRGMHVRGHHVEAIYSPV----RAEDGFVRELKALGLPAIHAVGMRRAPGPsdwsclrAINRIIRTAGPfDVIHGHSSK 107
Cdd:cd03817 23 LARALEKRGHEVYVITPSDpgaeDEEEVVRYRSFSIPIRKYHRQHIPFPFKK-------AVIDRIKELGP-DIIHTHTPF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 108 AGALTRLRLPGR-HVPRVYTPHafrTMDP------TLGRGGRLIYgaIETLLARF--FTDHLVAVSGDEFAHALSIGISG 178
Cdd:cd03817 95 SLGKLGLRIARKlKIPIVHTYH---TMYEdylhyiPKGKLLVKAV--VRKLVRRFynHTDAVIAPSEKIKDTLREYGVKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 179 KgMSVIVNGVDT----PSPDMAQtvRASFGIPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVrNSHVVMVGSGELEEE 254
Cdd:cd03817 170 P-IEVIPNGIDLdkfeKPLNTEE--RRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEP-NIKLVIVGDGPEREE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 255 VRAAIAASGLQNRIHltsaFTG---PQAVPAF----DLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDHGENG 327
Cdd:cd03817 246 LKELARELGLADKVI----FTGfvpREELPEYykaaDLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENG 321
|
330
....*....|....*..
gi 1549894312 328 YIVPNSEDvsPLARAMI 344
Cdd:cd03817 322 FLFEPNDE--TLAEKLL 336
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
12-346 |
4.13e-24 |
|
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: 102.83 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 12 LRLLEVLEPGGGGSGRHFLDLCRGMHVRGHHVEaIYSPVRAEDGFVRELKALGLPAI---HAVGMRRaPGPSDWS-CLRA 87
Cdd:cd03821 3 LHVTPSISPKAGGPVKVVLRLAAALAALGHEVT-IVSTGDGYESLVVEENGRYIPPQdgfASIPLLR-QGAGRTDfSPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 88 INRIIRTAGPFDVIHGH------SSKAGALTRlrlpGRHVPRVYTPHafrTMDPTLGRGGRLIYGAIETL------LARF 155
Cdd:cd03821 81 PNWLRRNLREYDVVHIHgvwtytSLAACKLAR----RRGIPYVVSPH---GMLDPWALQQKHWKKRIALHlierrnLNNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 156 FTDHLVAVsgDEFAHALSIGISGKgMSVIVNGVDTPSPDMAQTVRASFGIPADAFVFGFIGRLSAQKAPERLLNAFGKAA 235
Cdd:cd03821 154 ALVHFTSE--QEADELRRFGLEPP-IAVIPNGVDIPEFDPGLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 236 SAVRNSHVVMVGSGELEEEVRAA-IAASGLQNRIHLTSAFTG---PQAVPAFDLLVMPSRYEAMSYVMLEAAAAGRPIII 311
Cdd:cd03821 231 EQGRDWHLVIAGPDDGAYPAFLQlQSSLGLGDRVTFTGPLYGeakWALYASADLFVLPSYSENFGNVVAEALACGLPVVI 310
|
330 340 350
....*....|....*....|....*....|....*.
gi 1549894312 312 SD-VGGAGtAVDHGeNGYIVpnSEDVSPLARAMIAA 346
Cdd:cd03821 311 TDkCGLSE-LVEAG-CGVVV--DPNVSSLAEALAEA 342
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
22-351 |
1.10e-23 |
|
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: 101.25 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 22 GGGSGRHFLDLCRGMHVRGHHVEAIY-----SPVRAEDGFVRELKALGLPAIHAVGMRRAPGPS--DWSCLRAI-NRIIR 93
Cdd:cd03823 14 VGGAEISVHDLAEALVAEGHEVAVLTagvgpPGQATVARSVVRYRRAPDETLPLALKRRGYELFetYNPGLRRLlARLLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 94 TAGPfDVIHGHSSK---AGALTRLRLpgRHVPRVYTPHAFRTMDPtlgrGGRLIYGAIETLLA--RFFTDHLVAVsgdef 168
Cdd:cd03823 94 DFRP-DVVHTHNLSglgASLLDAARD--LGIPVVHTLHDYWLLCP----RQFLFKKGGDAVLApsRFTANLHEAN----- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 169 ahalsiGISGKGMSVIVNGVDTPSPDMAQTVRASfgipaDAFVFGFIGRLSAQKAPERLLNAFGKAASavRNSHVVMVGS 248
Cdd:cd03823 162 ------GLFSARISVIPNAVEPDLAPPPRRRPGT-----ERLRFGYIGRLTEEKGIDLLVEAFKRLPR--EDIELVIAGH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 249 GELEEEVRAAIAAsglqnRIHLTSAFTgPQAVPAF----DLLVMPSR-YEAMSYVMLEAAAAGRPIIISDVGGAGTAVDH 323
Cdd:cd03823 229 GPLSDERQIEGGR-----RIAFLGRVP-TDDIKDFyekiDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAELIQP 302
|
330 340
....*....|....*....|....*...
gi 1549894312 324 GENGYIVPnSEDVSPLARAMIAAADPEM 351
Cdd:cd03823 303 GVNGLLFA-PGDAEDLAAAMRRLLTDPA 329
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
181-350 |
2.34e-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: 97.31 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 181 MSVIVNGVDTPSPDMAQtvrasfgiPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGSGELEEEVRAAIA 260
Cdd:cd03820 161 VVVIPNPLSFPSEEPST--------NLKSKRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLID 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 261 ASGLQNRIHLTSAFTGPQAV-PAFDLLVMPSRYEAMSYVMLEAAAAGRPIIISD-VGGAGTAVDHGENGYIVPNsEDVSP 338
Cdd:cd03820 233 KLGLEDRVKLLGPTKNIAEEyANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDcPTGPSEIIEDGENGLLVPN-GDVDA 311
|
170
....*....|...
gi 1549894312 339 LARAMIA-AADPE 350
Cdd:cd03820 312 LAEALLRlMEDEE 324
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
21-379 |
2.57e-22 |
|
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: 97.13 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 21 GGGGSGRHFLDLCRGMHVRGHHVEAIYSpvraeDGFVRELKALGLPAIHAVGMRRAPgpsdWSCLRAINR---IIRTAGP 97
Cdd:cd04951 10 GLGGAEKQTVLLADQMFIRGHDVNIVYL-----TGEVEVKPLNNNIIIYNLGMDKNP----RSLLKALLKlkkIISAFKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 98 fDVIHGHSSKAGALTRL-RLPGRHVPRVYTPHAfrtmdptlgrggRLIYGAIETLLARFfTDHLVAVSGDEFAHALSIGI 176
Cdd:cd04951 81 -DVVHSHMFHANIFARFlRMLYPIPLLICTAHN------------KNEGGRIRMFIYRL-TDFLCDITTNVSREALDEFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 177 SGKGMS-----VIVNGVDTP----SPDMAQTVRASFGIPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVG 247
Cdd:cd04951 147 AKKAFSknksvPVYNGIDLNkfkkDINVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 248 SGELEEEVRAAIAASGLQNRIHLTSAFTG-PQAVPAFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDHGEn 326
Cdd:cd04951 227 DGPLRNELERLICNLNLVDRVILLGQISNiSEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHN- 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1549894312 327 gYIVPNSeDVSPLARAM--IAAADPEMFRRLAGAAAARRDRFTLKRMLDETEEVY 379
Cdd:cd04951 306 -YVVPVS-DPQLLAEKIkeIFDMSDEERDILGNKNEYIAKNFSINTIVNEWERLY 358
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
214-330 |
5.76e-21 |
|
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: 90.93 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 214 FIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGSGELEEEVRAAIAASGLQNRIHLTSAFTGPQAVPAF----DLLVMP 289
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLlaaaDVFVLP 194
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1549894312 290 SRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDHGENGYIV 330
Cdd:cd01635 195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
21-377 |
3.46e-19 |
|
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: 88.19 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 21 GGGGSGRHFLDLCRGMHVRGHHVeaIYSPVRAEDGFVRELKALGLPAIHAVGMRRAPGPSDWscLRAINRIIRTAGPFDV 100
Cdd:cd03809 12 RLTGIGRYTRELLKALAKNDPDE--SVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELAL--LRWLQILLPKKDKPDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 101 IHGHSSkagaltRLRLPGRHVPRVYTPH--AFRTMDPTLGRGGRLIYGAIETLLARFfTDHLVAVSgdEF-AHALS--IG 175
Cdd:cd03809 88 LHSPHN------TAPLLLKGCPQVVTIHdlIPLRYPEFFPKRFRLYYRLLLPISLRR-ADAIITVS--EAtRDDIIkfYG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 176 ISGKGMSVIVNGVDT-PSPDMAQTVRASFGIPADAFVFgFIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGSGELE-E 253
Cdd:cd03809 159 VPPEKIVVIPLGVDPsFFPPESAAVLIAKYLLPEPYFL-YVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEdE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 254 EVRAAIAASGLQNRIHltsaFTG--PQA-VPAF----DLLVMPSRYEAMSYVMLEAAAAGRPIIISD-------VGGAGT 319
Cdd:cd03809 238 ELLDLVKKLGLGGRVR----FLGyvSDEdLPALyrgaRAFVFPSLYEGFGLPVLEAMACGTPVIASNisvlpevAGDAAL 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1549894312 320 AVDhgengyivpnSEDVSPLARAMIAAA-DPEMFRRLAGAAAARRDRFTLKRMLDETEE 377
Cdd:cd03809 314 YFD----------PLDPESIADAILRLLeDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
177-343 |
4.63e-18 |
|
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: 85.08 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 177 SGKGMSVIVNGVDTP--SPDMAQTVRASFGIPADAFVFGFIgrlsAQKAPER-----LLNAFGKAASAVRNSHVVMVGSG 249
Cdd:cd03825 159 KGLPVVVIPNGIDTEifAPVDKAKARKRLGIPQDKKVILFG----AESVTKPrkgfdELIEALKLLATKDDLLLVVFGKN 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 250 ElEEEVRAAIAASGL---QNRIHLTSAFTgpqavpAFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDHGEN 326
Cdd:cd03825 235 D-PQIVILPFDIISLgyiDDDEQLVDIYS------AADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVT 307
|
170
....*....|....*..
gi 1549894312 327 GYIVPNsEDVSPLARAM 343
Cdd:cd03825 308 GYLVPP-GDVQALAEAI 323
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
282-379 |
1.87e-17 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 78.11 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 282 AFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDHGENGYIVPnSEDVSPLARAMI-AAADPEMFRRLAGAA- 359
Cdd:COG0438 20 AADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVP-PGDPEALAEAILrLLEDPELRRRLGEAAr 98
|
90 100
....*....|....*....|
gi 1549894312 360 AARRDRFTLKRMLDETEEVY 379
Cdd:COG0438 99 ERAEERFSWEAIAERLLALY 118
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
20-350 |
2.05e-16 |
|
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: 80.46 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 20 PGGGGSGRHFLDLCRGMHVRGHHVEAIYSPVRAEDGFVRELKALG----------LPAIHAVGMRRAPGPSDWSCLRAIN 89
Cdd:cd03794 11 PPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGATETkdgirvirvkLGPIKKNGLIRRLLNYLSFALAALL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 90 RIIRTAGPFDVIHGHSS-----KAGALTRLRlpgRHVPRVYTPHafrtmDP---TLGRGGRLIYGAIETLLARFF----- 156
Cdd:cd03794 91 KLLVREERPDVIIAYSPpitlgLAALLLKKL---RGAPFILDVR-----DLwpeSLIALGVLKKGSLLKLLKKLErklyr 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 157 -TDHLVAVSGDEFAHALSIGISGKGMSVIVNGVDTPSPD-MAQTVRASFGIPADAFVFGFIGRL-SAQkAPERLLNAFGK 233
Cdd:cd03794 163 lADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKpPPKDELRKKLGLDDKFVVVYAGNIgKAQ-GLETLLEAAER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 234 AASaVRNSHVVMVGSGELEEEVRAAIAASGLQNRIHLtsAFTGPQAVPAF----DLLVMPSRYEAMSYV-----MLEAAA 304
Cdd:cd03794 242 LKR-RPDIRFLFVGDGDEKERLKELAKARGLDNVTFL--GRVPKEEVPELlsaaDVGLVPLKDNPANRGsspskLFEYMA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1549894312 305 AGRPIIISDVGGAGTAVDHGENGYIVPNsEDVSPLARAMIAAADPE 350
Cdd:cd03794 319 AGKPILASDDGGSDLAVEINGCGLVVEP-GDPEALADAILELLDDP 363
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
23-190 |
2.48e-16 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 76.03 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 23 GGSGRHFLDLCRGMHVRGHHVEAIyspVRAEDGFVRELKALGLPAIHAVGMRRAPGPSDWSCLRAINRIIRTAGPfDVIH 102
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVV---TPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERP-DVVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 103 GHSSKAGALTRLRLP-GRHVPRVYTPHAFRTMDPTLGRGGRLIYGAIETLLARFF--TDHLVAVSGDEFAHALS-IGISG 178
Cdd:pfam13439 77 AHSPFPLGLAALAARlRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRRLERRLLrrADRVIAVSEAVADELRRlYGVPP 156
|
170
....*....|..
gi 1549894312 179 KGMSVIVNGVDT 190
Cdd:pfam13439 157 EKIRVIPNGVDL 168
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
20-350 |
2.53e-16 |
|
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: 79.65 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 20 PGGGGSGRHFLDLCRGMHVRGHHVEaIYSPvraeDGFVRELKALGlpAIHAVGMRRAPGPSD----WSCLRAINRIIRTA 95
Cdd:cd03814 11 PQVNGVVRTLERLVDHLRRRGHEVR-VVAP----GPFDEAESAEG--RVVSVPSFPLPFYPEyrlaLPLPRRVRRLIKEF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 96 GPfDVIH-------GHsskAGALTRLRLpgrHVPRVYTPH-------AFRTMDPTLG---RGGRLIYGAIETLLARfftd 158
Cdd:cd03814 84 QP-DIIHiatpgplGL---AALRAARRL---GLPVVTSYHtdfpeylSYYTLGPLSWlawAYLRWFHNPFDTTLVP---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 159 hlvavSGDEFAHALSIGISGkgMSVIVNGVDTP--SPDMA-QTVRASFGIPaDAFVFGFIGRLSAQKAPERLLNAFGKAA 235
Cdd:cd03814 153 -----SPSIARELEGHGFER--VRLWPRGVDTElfHPSRRdAALRRRLGPP-GRPLLLYVGRLAPEKNLEALLDADLPLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 236 SAVRnSHVVMVGSGELeeevRAAIAASGLQnrIHLTSAFTGP---QAVPAFDLLVMPSRYEAMSYVMLEAAAAGRPIIIS 312
Cdd:cd03814 225 ASPP-VRLVVVGDGPA----RAELEARGPD--VIFTGFLTGEelaRAYASADVFVFPSRTETFGLVVLEAMASGLPVVAA 297
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1549894312 313 DVGGAGTAVDHGENGYIVP--NSEDVSPLARAMiaAADPE 350
Cdd:cd03814 298 DAGGPRDIVRPGGTGALVEpgDAAAFAAALRAL--LEDPE 335
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
99-379 |
2.92e-15 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340841 [Multi-domain] Cd Length: 474 Bit Score: 77.38 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 99 DVIHGHS----SKAGALTRLRlpgRHVPRVYTPHAFRTMDPTLG-RGGRLIYGAIETLLARFFtDHL---------VAVS 164
Cdd:cd03813 175 DLYHSVStgyaGLLGALARHR---RGIPFLLTEHGIYTRERKIEiLQSTWIMGYIKKLWIRFF-ERLgklayqqadKIIS 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 165 GDEFAHALSI--GISGKGMSVIVNGVDTPSPDMAQTVRAsfgiPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVRNSH 242
Cdd:cd03813 251 LYEGNRRRQIrlGADPDKTRVIPNGIDIQRFAPAREERP----EKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 243 VVMVGsGELEEEVRAA-----IAASGLQNRIhltsAFTGPQ----AVPAFDLLVMPSRYEAMSYVMLEAAAAGRPIIISD 313
Cdd:cd03813 327 GWLIG-PEDEDPEYAQeckrlVASLGLENKV----KFLGFQnikeYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATD 401
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1549894312 314 VGGA-----GTAVDHGENGYIVPnSEDVSPLARAMIAA-ADPE-MFRRLAGAAAARRDRFTLKRMLDETEEVY 379
Cdd:cd03813 402 VGSCreliyGADDALGQAGLVVP-PADPEALAEALIKLlRDPElRQAFGEAGRKRVEKYYTLEGMIDSYRKLY 473
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
210-343 |
6.82e-15 |
|
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: 75.39 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 210 FVFgFIGRLSAQKAPERLLNAfgkaaSAVRNSHVVMVGSGELEEEVRAAIAAsGLQNRIHLTSAFTGPQAV---PAFDLL 286
Cdd:cd03795 193 IFL-FIGRLVYYKGLDYLIEA-----AQYLNYPIVIGGEGPLKPDLEAQIEL-NLLDNVKFLGRVDDEEKViylHLCDVF 265
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 287 VMPS--RYEAMSYVMLEAAAAGRPIIISDVGGAGTAVD-HGENGYIVPNsEDVSPLARAM 343
Cdd:cd03795 266 VFPSvlRSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNnNGETGLVVPP-KDPDALAEAI 324
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
20-379 |
7.24e-15 |
|
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: 75.47 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 20 PGGGGSGRHFLDLCRGMHVRGHHVEAIYS--PVRaedgfvrelkaLGLPA----IHAVGMRRAP----GPSDWSCLRAIN 89
Cdd:cd04962 9 PSYGGSGVVATELGLELAERGHEVHFISSaiPFR-----------LNLYSgnifFHEVEVPNYPlfeyPPYTLALASKIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 90 RIIRTAGpFDVIHGH----SSKAGALTRlRLPGRHVPRVYTPHAfrtMDPTLGRGGRLIYGAIETLLARffTDHLVAVSG 165
Cdd:cd04962 78 EVAKEHK-LDVLHAHyaipHASCAYLAR-EILGEKIPIVTTLHG---TDITLVGYDPSLQPAVRFSINK--SDRVTAVSS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 166 DEFAHALSIGISGKGMSVIVNGVDTP--SPDMAQTVRASFGIPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVrNSHV 243
Cdd:cd04962 151 SLRQETYELFDVDKDIEVIHNFIDEDvfKRKPAGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKI-PAKL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 244 VMVGSGELEEEVRAAIAASGLQNRIHLTSAFTGPQAV-PAFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVD 322
Cdd:cd04962 230 LLVGDGPERVPAEELARELGVEDRVLFLGKQDDVEELlSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVK 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1549894312 323 HGENGYIVPNSEDVSPLARAMIAAADPEMFRR-LAGAAAARRDRFTLKRMLDETEEVY 379
Cdd:cd04962 310 HGETGFLSDVGDVDAMAKSALSILEDDELYNRmGRAARKRAAERFDPERIVPQYEAYY 367
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
23-187 |
1.06e-14 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 71.28 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 23 GGSGRHFLDLCRGMHVRGHHVEAIyspVRAEDGFVRELKALGLPAIHAVGMRRAPGPSDWSCLRAINRIIRtAGPFDVIH 102
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVV---TPGGPPGRPELVGDGVRVHRLPVPPRPSPLADLAALRRLRRLLR-AERPDVVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 103 GHSSKAGALTRLRLPGRHVPRVYTPHAFRTmDPTLGRGGRLiYGAIETLLARFFtDHLVAVSGDEFAHALSIGISGKGMS 182
Cdd:pfam13579 77 AHSPTAGLAARLARRRRGVPLVVTVHGLAL-DYGSGWKRRL-ARALERRLLRRA-DAVVVVSEAEAELLRALGVPAARVV 153
|
....*
gi 1549894312 183 VIVNG 187
Cdd:pfam13579 154 VVPNG 158
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
205-344 |
1.20e-13 |
|
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: 71.56 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 205 IPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGSGELEEEVRAAIAASGLQNRIHLTSAFTGPQAV-PAF 283
Cdd:cd04949 156 HERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQEyQDA 235
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1549894312 284 DLLVMPSRYEAMSYVMLEAAAAGRPIIISDVG-GAGTAVDHGENGYIVPNsEDVSPLARAMI 344
Cdd:cd04949 236 YLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEK-NNIDALADKII 296
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
99-345 |
4.73e-13 |
|
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340860 [Multi-domain] Cd Length: 365 Bit Score: 69.79 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 99 DVIHGHSSKAGALTrlrLPGRH---VPRVYTPHAFrtmDPTL-------GRGGRLIYGAIETLLARFfTDHLVAVSGDEF 168
Cdd:cd05844 83 ALVHAHFGRDGVYA---LPLARalgVPLVVTFHGF---DITTsrawlaaSPGWPSQFQRHRRALQRP-AALFVAVSGFIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 169 AHALSIGISGKGMSVIVNGVDTpspdmAQTVRASFGIPADAFVFgfIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGS 248
Cdd:cd05844 156 DRLLARGLPAERIHVHYIGIDP-----AKFAPRDPAERAPTILF--VGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 249 GELEEEVRAAIAASGlqnRIHLTSAFTGPQAVPAFD---LLVMPSRY------EAMSYVMLEAAAAGRPIIISDVGGAGT 319
Cdd:cd05844 229 GPLRPALQALAAALG---RVRFLGALPHAEVQDWMRraeIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPE 305
|
250 260
....*....|....*....|....*.
gi 1549894312 320 AVDHGENGYIVPnSEDVSPLARAMIA 345
Cdd:cd05844 306 AILDGETGFLVP-EGDVDALADALQA 330
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
181-328 |
7.23e-12 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 66.35 E-value: 7.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 181 MSVIVNGVD--TPSPDMAQTVRASFGIPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVG---------SG 249
Cdd:PRK15484 163 ISIVPNGFCleTYQSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGdptasskgeKA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 250 ELEEEVRAaiAASGLQNRIHLTSAfTGPQAVPAF----DLLVMPSRY-EAMSYVMLEAAAAGRPIIISDVGGAGTAVDHG 324
Cdd:PRK15484 243 AYQKKVLE--AAKRIGDRCIMLGG-QPPEKMHNYyplaDLVVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGITEFVLEG 319
|
....
gi 1549894312 325 ENGY 328
Cdd:PRK15484 320 ITGY 323
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
97-348 |
2.13e-11 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 65.83 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 97 PFDVIH---GHSSKAGALTRLrLPGrhVPRVYTphAFRTMDPTLGRGG-RLIYGAIETLLARFFTDHLVAVSgDEFAHAL 172
Cdd:PRK15179 400 VPSVVHiwqDGSIFACALAAL-LAG--VPRIVL--SVRTMPPVDRPDRyRVEYDIIYSELLKMRGVALSSNS-QFAAHRY 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 173 S--IGISGKGMSVIVNGV-------DTPSPDMAQTVRASfgiPADA-FVFGFIGRLSAQKAPERLLNAFGKAASAVRNSH 242
Cdd:PRK15179 474 AdwLGVDERRIPVVYNGLaplksvqDDACTAMMAQFDAR---TSDArFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVR 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 243 VVMVGSGELEEEVRAAIAASGLQNRIHLT--SAFTGpQAVPAFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTA 320
Cdd:PRK15179 551 FIMVGGGPLLESVREFAQRLGMGERILFTglSRRVG-YWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEA 629
|
250 260
....*....|....*....|....*....
gi 1549894312 321 VDHGENGYIVPNSEDVSP-LARAMIAAAD 348
Cdd:PRK15179 630 VQEGVTGLTLPADTVTAPdVAEALARIHD 658
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
184-352 |
4.15e-10 |
|
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: 61.43 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 184 IVNGVDT----PSPD-----------------MAQTVRASFGIP--ADAFVFGFIGRLSAQK-------APERLLNAFGK 233
Cdd:cd03791 246 ILNGIDYdewnPATDklipanysandlegkaeNKAALQKELGLPvdPDAPLFGFVGRLTEQKgvdlildALPELLEEGGQ 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 234 aasavrnshVVMVGSGELEEEVRAAIAASGLQNRIHLTSAFTGPQAVPAF---DLLVMPSRYEAMSYVMLEAAAAGRPII 310
Cdd:cd03791 326 ---------LVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYagaDFFLMPSRFEPCGLVQMYAMRYGTLPI 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1549894312 311 ISDVGG-AGTAVDHGE-----NGYIVpNSEDVSPLARAMIAA----ADPEMF 352
Cdd:cd03791 397 VRRTGGlADTVFDYDPetgegTGFVF-EDYDAEALLAALRRAlalyRNPELW 447
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
17-343 |
5.03e-10 |
|
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: 60.38 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 17 VLEPGGGGSGRHFLDLCRGMHVRGHHVEAIY---SPVRAEdgfvrelkalgLPAIHAVGMRRAPGPSDWS--CLRAINRI 91
Cdd:cd03802 12 VPPGKYGGTELVVSALTEGLVRRGHEVTLFApgdSHTSAP-----------LVAVIPRALRLDPIPQESKlaELLEALEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 92 IRTAGPFDVIHGHSskaGALTRLRLPGRHVPRVYTPHafrtmdptlgrgGRLIYGAIETLLARFFTdHLVAVSgdefAHA 171
Cdd:cd03802 81 QLRASDFDVIHNHS---YDWLPPFAPLIGTPFVTTLH------------GPSIPPSLAIYAAEPPV-NYVSIS----DAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 172 LSIGISGKGMSVIVNGVDTpspdmaqtvrASFG-IPADAFVFGFIGRLSAQKAPERLLnafgKAASAVrNSHVVMVGSGE 250
Cdd:cd03802 141 RAATPPIDYLTVVHNGLDP----------ADYRfQPDPEDYLAFLGRIAPEKGLEDAI----RVARRA-GLPLKIAGKVR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 251 LEEEVRAaIAASGLQNRIHLTSAFTGPQAVPAFD----LLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDHGEN 326
Cdd:cd03802 206 DEDYFYY-LQEPLPGPRIEFIGEVGHDEKQELLGgaraLLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGET 284
|
330
....*....|....*..
gi 1549894312 327 GYIVPNSEDvspLARAM 343
Cdd:cd03802 285 GFLVDSVEE---MAEAI 298
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
89-348 |
5.34e-10 |
|
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: 60.48 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 89 NRIIRTAGPfDVIH--------GHSSKAGALTRLRLPGRhvPRVYTPHAFRTMdPTLGRGGRLIYGAIETLLARFFTDHl 160
Cdd:cd03822 68 LDHLNFKKP-DVVHiqhefgifGGKYGLYALGLLLHLRI--PVITTLHTVLDL-SDPGKQALKVLFRIATLSERVVVMA- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 161 vaVSGDEFAHAlSIGISGKGMSVIVNGV-DTPSPDmaQTVRASFGIPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVR 239
Cdd:cd03822 143 --PISRFLLVR-IKLIPAVNIEVIPHGVpEVPQDP--TTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFP 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 240 NSHVVMVGS-------GELEEEVRAAIAASGLQNRIHLTSAFTGPQAVP----AFDLLVMP--SRYEAMSYVMLEAAAAG 306
Cdd:cd03822 218 DVRLVIAGElhpslarYEGERYRKAAIEELGLQDHVDFHNNFLPEEEVPryisAADVVVLPylNTEQSSSGTLSYAIACG 297
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1549894312 307 RPIIISDVGGAGTAVdHGENGYIVPnSEDVSPLARAMIAAAD 348
Cdd:cd03822 298 KPVISTPLRHAEELL-ADGRGVLVP-FDDPSAIAEAILRLLE 337
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
99-297 |
3.42e-09 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 58.59 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 99 DVIHGHSSKAG---AL--TRLRLPGRHVPRVYTPH--AF-----RTMDPTLGRG-------GRLIYGAIETLLAR-FFTD 158
Cdd:PRK00654 120 DIVHAHDWHTGlipALlkEKYWRGYPDIKTVFTIHnlAYqglfpAEILGELGLPaeafhleGLEFYGQISFLKAGlYYAD 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 159 HLVAVS--------GDEFAHALS---IGISGKgMSVIVNGVDT----PSPD-----------------MAQTVRASFGIP 206
Cdd:PRK00654 200 RVTTVSptyareitTPEFGYGLEgllRARSGK-LSGILNGIDYdiwnPETDpllaanysaddlegkaeNKRALQERFGLP 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 207 -ADAFVFGFIGRLSAQKAPERLLNAFGKAASavRNSHVVMVGSGE--LEEEVRAaiAASGLQNRIHLTSAFTGPQA---V 280
Cdd:PRK00654 279 dDDAPLFAMVSRLTEQKGLDLVLEALPELLE--QGGQLVLLGTGDpeLEEAFRA--LAARYPGKVGVQIGYDEALAhriY 354
|
250 260
....*....|....*....|....*
gi 1549894312 281 PAFDLLVMPSRYE--------AMSY 297
Cdd:PRK00654 355 AGADMFLMPSRFEpcgltqlyALRY 379
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
99-347 |
7.83e-09 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 57.42 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 99 DVIHGHSSKAG-ALTRLRLPGRHVPR-VYTPH--AF-----RTMDPTLGR-------GGRLIYGAIETLLARF-FTDHLV 161
Cdd:PRK14099 135 DIVHAHDWQAGlAPAYLHYSGRPAPGtVFTIHnlAFqgqfpRELLGALGLppsafslDGVEYYGGIGYLKAGLqLADRIT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 162 AVSGdefAHALSIGISGKGM-------------SVIVNGVDT----PSPDMA-----------------QTVRASFGIPA 207
Cdd:PRK14099 215 TVSP---TYALEIQGPEAGMgldgllrqradrlSGILNGIDTavwnPATDELiaatydvetlaaraankAALQARFGLDP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 208 D--AFVFGFIGRLSAQKAPERLLNAFGKAASAvrNSHVVMVGSGELEEEVRAAIAASGLQNRI-----------HLTSAf 274
Cdd:PRK14099 292 DpdALLLGVISRLSWQKGLDLLLEALPTLLGE--GAQLALLGSGDAELEARFRAAAQAYPGQIgvvigydealaHLIQA- 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1549894312 275 tgpqavpAFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGG-AGTAVDHGENGYIVPNSEDV--SPLARAMIAAA 347
Cdd:PRK14099 369 -------GADALLVPSRFEPCGLTQLCALRYGAVPVVARVGGlADTVVDANEMAIATGVATGVqfSPVTADALAAA 437
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
159-329 |
3.28e-07 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 52.02 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 159 HLVAVSGDEfAHALSIGISGKGMSVIVNGVDTPSPDMAQTVRasfGIPAdafVFGFIGRLSA--QKAPERLLNAFGKAAS 236
Cdd:PRK09922 137 HLAISSGIK-EQMMARGISAQRISVIYNPVEIKTIIIPPPER---DKPA---VFLYVGRLKFegQKNVKELFDGLSQTTG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 237 avrNSHVVMVGSGELEEEVRAAIAASGLQNRIHLTSAFTGP-----QAVPAFDLLVMPSRYEAMSYVMLEAAAAGRPIII 311
Cdd:PRK09922 210 ---EWQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQPwevvqQKIKNVSALLLTSKFEGFPMTLLEAMSYGIPCIS 286
|
170
....*....|....*....
gi 1549894312 312 SD-VGGAGTAVDHGENGYI 329
Cdd:PRK09922 287 SDcMSGPRDIIKPGLNGEL 305
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
137-351 |
4.41e-07 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 51.52 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 137 LGRGGRL--IYGAIE-TLLARFftDHLVAVSGDEFAHALSIGISGKGMSVIVNGVDT------PSPDmAQTVRASFGIPA 207
Cdd:PRK10307 151 LLKGGKVarLATAFErSLLRRF--DNVSTISRSMMNKAREKGVAAEKVIFFPNWSEVarfqpvADAD-VDALRAQLGLPD 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 208 DAFVFGFIGRLSAQKAPERLLNAfGKAASAVRNSHVVMVGSGELEEEVRAAIAASGLQN-------------------RI 268
Cdd:PRK10307 228 GKKIVLYSGNIGEKQGLELVIDA-ARRLRDRPDLIFVICGQGGGKARLEKMAQCRGLPNvhflplqpydrlpallkmaDC 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 269 HLTsaftgPQAVPAFDLlVMPSRYEAMsyvmleaAAAGRPIIISDVGGAGTAVDHGENGYIVPnSEDVSPLARAMIA-AA 347
Cdd:PRK10307 307 HLL-----PQKAGAADL-VLPSKLTNM-------LASGRNVVATAEPGTELGQLVEGIGVCVE-PESVEALVAAIAAlAR 372
|
....
gi 1549894312 348 DPEM 351
Cdd:PRK10307 373 QALL 376
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
215-344 |
1.47e-06 |
|
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.
Pssm-ID: 340829 [Multi-domain] Cd Length: 350 Bit Score: 49.76 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 215 IGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGSGELEEEVRAAIAASGLQNRIHLTSAFTGPQAVPAFD---LLVMPS- 290
Cdd:cd03799 180 VGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIEILDeadIFIAPSv 259
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1549894312 291 -----RYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDHGENGYIVPnSEDVSPLARAMI 344
Cdd:cd03799 260 taadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVP-ERDAEAIAEKLT 317
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
184-297 |
1.85e-06 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 49.71 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 184 IVNGVDT----PSPDMA-----------------QTVRASFGIP--ADAFVFGFIGRLSAQKAPERLLNAFGKAASavRN 240
Cdd:COG0297 247 ILNGIDYdvwnPATDPYlpanysaddlegkaankAALQEELGLPvdPDAPLIGMVSRLTEQKGLDLLLEALDELLE--ED 324
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1549894312 241 SHVVMVGSGE--LEEEVRAaiAASGLQNRIHLTSAFTGP-----QAvpAFDLLVMPSRYE--------AMSY 297
Cdd:COG0297 325 VQLVVLGSGDpeYEEAFRE--LAARYPGRVAVYIGYDEAlahriYA--GADFFLMPSRFEpcglnqmyALRY 392
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
180-350 |
6.09e-06 |
|
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: 48.13 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 180 GMSVIVNGVDTP--SPDMAQTVRASFG--IPADAFVFGFIGR-LSAQKAPERLLNAFGKAASAVRNSHVVMVGSGELEEE 254
Cdd:cd03818 180 RISVIHDGVDTDrlAPDPAARLRLLNGteLKAGDPVITYVARnLEPYRGFHVFMRALPRIQARRPDARVVVVGGDGVSYG 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 255 VRAAIAASGLQ----------NRIHltsaFTGP-------QAVPAFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGA 317
Cdd:cd03818 260 SPPPDGGSWKQkmlaelgvdlERVH----FVGKvpydqyvRLLQLSDAHVYLTYPFVLSWSLLEAMACGCPVIGSDTAPV 335
|
170 180 190
....*....|....*....|....*....|....
gi 1549894312 318 GTAVDHGENGYIVPnSEDVSPLARAMIAA-ADPE 350
Cdd:cd03818 336 REVIRDGRNGLLVD-FFDPDALAAAVLELlEDPD 368
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
187-316 |
1.11e-05 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 47.40 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 187 GVDTPS--P---DMAQTVRASFGIPaDAFVFGFIGRLSAQKAperlLNAFGKAASAVRNSHVVMVGSGELEEEVRAAIAA 261
Cdd:PLN02871 237 GVDSESfhPrfrSEEMRARLSGGEP-EKPLIVYVGRLGAEKN----LDFLKRVMERLPGARLAFVGDGPYREELEKMFAG 311
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1549894312 262 SglqnRIHLTSAFTG---PQAVPAFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGG 316
Cdd:PLN02871 312 T----PTVFTGMLQGdelSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGG 365
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
183-315 |
1.93e-05 |
|
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: 46.46 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 183 VIVNGVDTPSPDMAQTVRASfGIPAdafVFGFIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGSGELE----EEVRAA 258
Cdd:NF038011 284 VIPNGIDLPRLAPLRAQRPA-GIPP---VVGLIGRVVPIKDIKTFIRAMRTVVRAMPEAEGWIVGPEEEDpayaAECRSL 359
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1549894312 259 IAASGLQNRIHltsaFTGPQAV----PAFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVG 315
Cdd:NF038011 360 VASLGLQDKVK----FLGFQKIddllPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVG 416
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
176-337 |
2.40e-05 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 46.62 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 176 ISGKGMSVIVNGV----DTPSPDMAQTVRASFGIP---ADAFVFGfIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGS 248
Cdd:PRK15490 359 LEAKHFQVVYNGVlppsTEPSSEVPHKIWQQFTQKtqdADTTIGG-VFRFVGDKNPFAWIDFAARYLQHHPATRFVLVGD 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 249 GELEEEVRAAIAASGLQNRIhltsAFTGPQA-----VPAFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDH 323
Cdd:PRK15490 438 GDLRAEAQKRAEQLGILERI----LFVGASRdvgywLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGSAECFIE 513
|
170
....*....|....
gi 1549894312 324 GENGYIVPNSEDVS 337
Cdd:PRK15490 514 GVSGFILDDAQTVN 527
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
246-338 |
1.72e-04 |
|
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.
Pssm-ID: 340854 [Multi-domain] Cd Length: 401 Bit Score: 43.60 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 246 VGSGELEEEVRAaIAASGLQN-RIHLTSAFTGPQAVP-----AFDLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGT 319
Cdd:cd04946 263 IGGGPLKERLEK-LAENKLENvKVNFTGEVSNKEVKQlykenDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTRE 341
|
90
....*....|....*....
gi 1549894312 320 AVDHGENGYIVpnSEDVSP 338
Cdd:cd04946 342 IVENETNGLLL--DKDPTP 358
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
194-337 |
8.28e-04 |
|
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: 41.15 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549894312 194 DMAQTVRASFGIPADAFVFGFIGRLSAQKAPERLLNAFGKAASAVRNSHVVMVGSG--------ELEEEVRAAiaaSGLQ 265
Cdd:cd03792 182 DIRYYLEKPFVIDPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGavddpegsVVYEEVMEY---AGDD 258
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1549894312 266 NRIHLTSAFTGPQAVPAF----DLLVMPSRYEAMSYVMLEAAAAGRPIIISDVGGAGTAVDHGENGYIVPNSEDVS 337
Cdd:cd03792 259 HDIHVLRLPPSDQEINALqraaTVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAA 334
|
|
|