|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-365 |
2.20e-70 |
|
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: 224.72 E-value: 2.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 2 RIGMICPYSFDVPGGVQSHVLQLAEVMRTRGHLVSVLAPASPHAALPDYfvsgGRAVPIPYNGSVARLRFGPATHRKVKK 81
Cdd:cd03801 1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEEL----EDGVIVPLLPSLAALLRARRLLRELRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 82 WLAHGDFDVLHLHEPNAPSLSMLALNIAEGPIVATFHTSTTKSLTLTVFQ--GILR---PMHEKIVGRIAVSDLARRWQM 156
Cdd:cd03801 77 LLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAerRLLAraeALLRRADAVIAVSEALRDELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 157 EALG---SDAVEIPNGVDVDSFASAARLD-GYPRQGKTVLFLGRYDePRKGMAVLLDALPKVVQRFPDVQLLIVGHGDA- 231
Cdd:cd03801 157 ALGGippEKIVVIPNGVDLERFSPPLRRKlGIPPDRPVLLFVGRLS-PRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 232 -DQLRGQAGRLAAHLRFLGQVDDAGKASAMRSADVYCAPNTGgESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHL 310
Cdd:cd03801 236 rAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRY-EGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489508612 311 VPVDPPDlqaaALADGLIAVLENDVLRERYVAAGNAAVR-RYDWSVVASQIMRVYE 365
Cdd:cd03801 315 VPPDDVE----ALADALLRLLADPELRARLGRAARERVAeRFSWERVAERLLDLYR 366
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
12-367 |
1.51e-42 |
|
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: 152.43 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 12 DVPGGVQShVLQLAEVMRTRGHLVSVLAPASPHAaLPDYFVSGGRAVPIPYNGSVARLRFGPATHrKVKKWLAHGDFDVL 91
Cdd:cd03817 12 QVNGVATS-VRNLARALEKRGHEVYVITPSDPGA-EDEEEVVRYRSFSIPIRKYHRQHIPFPFKK-AVIDRIKELGPDII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 92 HLHEPNapSLSMLALNIAEG---PIVATFHTSTTKSLTLTVFQGIL-RPMHEKIVGR--------IAVSDLARR-WQMEA 158
Cdd:cd03817 89 HTHTPF--SLGKLGLRIARKlkiPIVHTYHTMYEDYLHYIPKGKLLvKAVVRKLVRRfynhtdavIAPSEKIKDtLREYG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 159 LGSDAVEIPNGVDVDSFAS----AARLDGYPRQGKTVL-FLGRYDePRKGMAVLLDALPKVVQRfPDVQLLIVGHG-DAD 232
Cdd:cd03817 167 VKGPIEVIPNGIDLDKFEKplntEERRKLGLPPDEPILlYVGRLA-KEKNIDFLLRAFAELKKE-PNIKLVIVGDGpERE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 233 QLRGQAGRL--AAHLRFLGQVDDAGKASAMRSADVYCAPNTGgESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHL 310
Cdd:cd03817 245 ELKELARELglADKVIFTGFVPREELPEYYKAADLFVFASTT-ETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFL 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489508612 311 VPVDPPdlqaaALADGLIAVLENDVLRERYVAAGNAAVRRYDwsvVASQIMRVYETV 367
Cdd:cd03817 324 FEPNDE-----TLAEKLLHLRENLELLRKLSKNAEISAREFA---FAKSVEKLYEEV 372
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
15-351 |
2.40e-41 |
|
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: 148.66 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 15 GGVQSHVLQLAEVMRTRGHLVSVLApASPHAALPDYFVSGGRAVPIPYNGSVARLRFGPATHRKVKKWLAHGDFDVLHLH 94
Cdd:cd03811 12 GGAERVLLNLANALDKRGYDVTLVL-LRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRILKRAKPDVVISF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 95 EPNAPSLSMLaLNIAEGPIVATFHTSTTKSLTLTVFQGILRPMHEKIVGRIAVSDLARRWqMEALGSDAVE----IPNGV 170
Cdd:cd03811 91 LGFATYIVAK-LAAARSKVIAWIHSSLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKED-LIRLGPSPPEkievIYNPI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 171 DVDSFASAARLD--GYPRQGKTVLFLGRYDePRKGMAVLLDALPKVVQRFPDVQLLIVGHG-DADQLRGQAGRL--AAHL 245
Cdd:cd03811 169 DIDRIRALAKEPilNEPEDGPVILAVGRLD-PQKGHDLLIEAFAKLRKKYPDVKLVILGDGpLREELEKLAKELglAERV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 246 RFLGQVDDAgkASAMRSADVYCAPNTGgESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHLVPVDPPDLqAAALAD 325
Cdd:cd03811 248 IFLGFQSNP--YPYLKKADLFVLSSRY-EGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAA-LAGILA 323
|
330 340
....*....|....*....|....*.
gi 489508612 326 GLIAVLENDVLRERYVAAGNAAVRRY 351
Cdd:cd03811 324 ALLQKKLDAALRERLAKAQEAVFREY 349
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
12-367 |
5.27e-39 |
|
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: 142.90 E-value: 5.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 12 DVPGGVQSHVLQLAEVMRTRGHLVSVLAPASPHAAL---------PDYFVSGGRAVPIPYNGSVARLRFGPATHRKVKKW 82
Cdd:cd03798 11 ANSPGRGIFVRRQVRALSRRGVDVEVLAPAPWGPAAarllrkllgEAVPPRDGRRLLPLKPRLRLLAPLRAPSLAKLLKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 83 LAHGDFDVLHLHepNAPSLSMLALNIAE---GPIVATFHTSTTKSLTltvFQGILRPMHEKIVGR----IAVS-DLARRw 154
Cdd:cd03798 91 RRRGPPDLIHAH--FAYPAGFAAALLARlygVPYVVTEHGSDINVFP---PRSLLRKLLRWALRRaarvIAVSkALAEE- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 155 qMEALGSD---AVEIPNGVDVDSFASAARLDGYPRQGKTVLFLGRYdEPRKGMAVLLDALPKVVQRFPDVQLLIVGHG-D 230
Cdd:cd03798 165 -LVALGVPrdrVDVIPNGVDPARFQPEDRGLGLPLDAFVILFVGRL-IPRKGIDLLLEAFARLAKARPDVVLLIVGDGpL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 231 ADQLRGQAG--RLAAHLRFLGQVDDAGKASAMRSADVYCAPnTGGESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVG 308
Cdd:cd03798 243 REALRALAEdlGLGDRVTFTGRLPHEQVPAYYRACDVFVLP-SRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETG 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 489508612 309 HLVPvdPPDlqAAALADGLIAVLENDVLRERYVAAGNAAVRRYDWSVVASQIMRVYETV 367
Cdd:cd03798 322 LLVP--PGD--ADALAAALRRALAEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
188-333 |
3.86e-37 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 131.09 E-value: 3.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 188 GKTVLFLGRYDEPRKGMAVLLDALPKVVQRFPDVQLLIVGHGDADQLRGQAGRLAAHLRFLGQVDDagKASAMRSADVYC 267
Cdd:pfam13692 1 RPVILFVGRLHPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEELAAGLEDRVIFTGFVED--LAELLAAADVFV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489508612 268 APNTgGESFGIVLVEAMAAGTAVVASDLDAFRRVLrDGEVGHLVPVDPPDlqaaALADGLIAVLEN 333
Cdd:pfam13692 79 LPSL-YEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPE----ALAEAILRLLED 138
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
13-361 |
3.82e-35 |
|
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: 131.95 E-value: 3.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 13 VPGGVQSHVLQLAEVMRTRGHLVSVLAPASPhaALPDYFVSGG-RAVPIPYngsvarLRFGP------ATHRKVKKWLAH 85
Cdd:cd03808 8 VDGGFQSFRLPLIKALVKKGYEVHVIAPDGD--KLSDELKELGvKVIDIPI------LRRGInplkdlKALFKLYKLLKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 86 GDFDVLHLHEPNAPSLSMLALNIAEGP-IVATFHTSTTKSLTLTVFQGILRPMhEKIVGR-----IAVS----DLARRWQ 155
Cdd:cd03808 80 EKPDIVHCHTPKPGILGRLAARLAGVPkVIYTVHGLGFVFTEGKLLRLLYLLL-EKLALLftdkvIFVNeddrDLAIKKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 156 MEALGSDAVEIPNGVDVDSFAsaARLDGYPRQGKTVLFLGRYDEpRKGMAVLLDALPKVVQRFPDVQLLIVGHGDAD--- 232
Cdd:cd03808 159 IIKKKKTVLIPGSGVDLDRFQ--YSPESLPSEKVVFLFVARLLK-DKGIDELIEAAKILKKKGPNVRFLLVGDGELEnps 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 233 QLRGQAGRLAAHLRFLGQVDDAgkASAMRSADVYCAPnTGGESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHLVP 312
Cdd:cd03808 236 EILIEKLGLEGRIEFLGFRSDV--PELLAESDVFVLP-SYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVP 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489508612 313 VDppdlQAAALADGLIAVLENDVLRERYVAAGNA-AVRRYDWSVVASQIM 361
Cdd:cd03808 313 PG----DVEALADAIEKLIEDPELRKEMGEAARKrVEEKFDEEKVVNKLL 358
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
2-361 |
1.28e-34 |
|
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: 130.95 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 2 RIGMICPYSFDVPGGVQSHVLQLAEVMRTRGHLVSVLAPasPHAALPDYFVSGGRAVPIPYNGSVaRLRFGPATHRKVKK 81
Cdd:cd03809 1 KILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAV--PPLPGELLRLLREYPELSLGVIKI-KLWRELALLRWLQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 82 WL-AHGDFDVLHLHEPNAPslsmlaLNIAEGPIVATFH---TSTTKSLTLTVFQGILRPMHeKIVGR-----IAVSDLAR 152
Cdd:cd03809 78 LLpKKDKPDLLHSPHNTAP------LLLKGCPQVVTIHdliPLRYPEFFPKRFRLYYRLLL-PISLRradaiITVSEATR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 153 RwQMEALGSDAVE----IPNGVDVDSF---ASAARLDGYPRQGKTVLFLGRYdEPRKGMAVLLDALPKVVQRFPDVQLLI 225
Cdd:cd03809 151 D-DIIKFYGVPPEkivvIPLGVDPSFFppeSAAVLIAKYLLPEPYFLYVGTL-EPRKNHERLLKAFALLKKQGGDLKLVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 226 VGHGDADQLRGQA----GRLAAHLRFLGQVDDAGKASAMRSADVYCAPNTGgESFGIVLVEAMAAGTAVVASDLDAFRRV 301
Cdd:cd03809 229 VGGKGWEDEELLDlvkkLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLY-EGFGLPVLEAMACGTPVIASNISVLPEV 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 302 LrdGEVGHLvpVDPPDlqAAALADGLIAVLENDVLRERYVAAGNAAVRRYDWSVVASQIM 361
Cdd:cd03809 308 A--GDAALY--FDPLD--PESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTL 361
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
189-344 |
1.07e-33 |
|
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: 122.77 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 189 KTVLFLGRYdEPRKGMAVLLDALPKVVQRFPDVQLLIVGHG-DADQLRGQAG--RLAAHLRFLGQVDDAGKASAMRSADV 265
Cdd:pfam00534 3 KIILFVGRL-EPEKGLDLLIKAFALLKEKNPNLKLVIAGDGeEEKRLKKLAEklGLGDNVIFLGFVSDEDLPELLKIADV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489508612 266 YCAPNTGgESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHLvpVDPPDlqAAALADGLIAVLENDVLRERYVAAG 344
Cdd:pfam00534 82 FVLPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFL--VKPNN--AEALAEAIDKLLEDEELRERLGENA 155
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
2-366 |
3.73e-31 |
|
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: 121.73 E-value: 3.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 2 RIGMICpYSFDVPGGVqSHVLQLAEVMRTRGHLVSVLAPASPHAALPDYFVSGGRAVPIPYNGSVARLRFGPATHRKVKK 81
Cdd:TIGR04047 1 RIALLT-YSTKPRGGV-VHTLELAEALTALGHDVTVWALAADGFGFFRDPPCAVRLVPVAPAPGDTDAMVEQRIARSIDH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 82 WLAHGD--FDVLHLHEpnAPSLSMLALNIAEGPI---VATFHTSTtksltltVFQG-ILRPMHEKIV----GRIAVSDLA 151
Cdd:TIGR04047 79 LRAHFArgFDVVHAQD--CISGNALATLRAEGLIpgfVRTVHHLD-------DFDDpRLAACQERAIveadAVLCVSAAW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 152 RRWQMEALGSDAVEIPNGVDVDSFASAARLDGYPRQGKTVLFLGRY------DEPRKGMAVLLDALPKVVQRFPDVQLLI 225
Cdd:TIGR04047 150 AAELRAEWGIDATVVPNGVDAARFSPAADAADAALRRRLGLRGGPYvlavggIEPRKNTIDLLEAFALLRARRPQAQLVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 226 VG------HGD-ADQLRGQA---GRLAAHLRFLGQVDDAGKASAMRSADVYCAPNTgGESFGIVLVEAMAAGTAVVASDL 295
Cdd:TIGR04047 230 AGgatlfdYDAyRREFRARAaelGVDPGPVVITGPVPDADLPALYRCADAFAFPSL-KEGFGLVVLEALASGIPVVASDI 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489508612 296 DAFRRVLRDGEVGHLVPVDPPDLqAAALADGLiavleNDVLRERYVAAGNAAVRRYDWSVVASQIMRVYET 366
Cdd:TIGR04047 309 APFTEYLGRFDAAWADPSDPDSI-ADALALAL-----DPARRPALRAAGPELAARYTWDASARAHLEFYRR 373
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
11-365 |
2.49e-29 |
|
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: 116.24 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 11 FDVPGGVQSHVLQLAEVMRTRGHLVSVLAPASPHAALPDYF-VSGGRAVPIPYNGSvarLRFGPATHRKVKKWLAHGDFD 89
Cdd:cd03814 10 HPQVNGVVRTLERLVDHLRRRGHEVRVVAPGPFDEAESAEGrVVSVPSFPLPFYPE---YRLALPLPRRVRRLIKEFQPD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 90 VLHLHEPNAPSLSMLALNIAEG-PIVATFH--------TSTTKSLTLTVFQGIL---RPMHEKIVGRIAVSDLARRWQME 157
Cdd:cd03814 87 IIHIATPGPLGLAALRAARRLGlPVVTSYHtdfpeylsYYTLGPLSWLAWAYLRwfhNPFDTTLVPSPSIARELEGHGFE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 158 algsDAVEIPNGVDVDSFASAARlDGYPRQG------KTVLFLGRYdEPRKGMAVLLDALPKVVQRFPdVQLLIVGHG-D 230
Cdd:cd03814 167 ----RVRLWPRGVDTELFHPSRR-DAALRRRlgppgrPLLLYVGRL-APEKNLEALLDADLPLAASPP-VRLVVVGDGpA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 231 ADQLrgQAGRLAAHlrFLGQVDDAGKASAMRSADVYCAPNTGgESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHL 310
Cdd:cd03814 240 RAEL--EARGPDVI--FTGFLTGEELARAYASADVFVFPSRT-ETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGAL 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489508612 311 VpvdpPDLQAAALADGLIAVLENDVLRERYVAAGNAAVRRYDWSVVASQIMRVYE 365
Cdd:cd03814 315 V----EPGDAAAFAAALRALLEDPELRRRMAARARAEAERYSWEAFLDNLLDYYA 365
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
13-350 |
3.72e-29 |
|
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: 115.53 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 13 VPGGVQSHVLQLAEVMRTRGHLVSVLAPASP------HAALPDYFVSGGRAVPIPYNGSVARLRfgpathrkvKKWlahg 86
Cdd:cd03819 9 EIGGAETYILDLARALAERGHRVLVVTAGGPllprlrQIGIGLPGLKVPLLRALLGNVRLARLI---------RRE---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 87 DFDVLHLHEPNAPSLSMLALNIAEGPIVATFHTSTTKSLTLTVFQGILRPMHEKIvgrIAVSDLARRWQMEALGSDAVE- 165
Cdd:cd03819 76 RIDLIHAHSRAPAWLGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVRARGDRV---IAVSELVRDHLIEALGVDPERi 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 166 --IPNGVDVDSF-----ASAARLDGYPRQGKTVLFLGRYDePRKGMAVLLDALPKVvQRFPDVQLLIVGHG-DADQLRGQ 237
Cdd:cd03819 153 rvIPNGVDTDRFppeaeAEERAQLGLPEGKPVVGYVGRLS-PEKGWLLLVDAAAEL-KDEPDFRLLVAGDGpERDEIRRL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 238 AGR--LAAHLRFLGQVDDAgkASAMRSADVYCAPNTGgESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHLVpvdp 315
Cdd:cd03819 231 VERlgLRDRVTFTGFREDV--PAALAASDVVVLPSLH-EEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLV---- 303
|
330 340 350
....*....|....*....|....*....|....*..
gi 489508612 316 PDLQAAALADGLIAVLENDVLRERYVAAG--NAAVRR 350
Cdd:cd03819 304 PPGDAEALADAIRAAKLLPEAREKLQAAAalTEAVRE 340
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
15-360 |
3.59e-27 |
|
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: 110.54 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 15 GGVQSHVLQLAEVMRTRGHLVSVLAPASPHAAL-------PDYFVSGGRAVPIPYNGSVA-RLRFGPATHRkvkkWLAHG 86
Cdd:cd03821 14 GGPVKVVLRLAAALAALGHEVTIVSTGDGYESLvveengrYIPPQDGFASIPLLRQGAGRtDFSPGLPNWL----RRNLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 87 DFDVLHLHEPNAPsLSMLALNIAEG---PIVATFHtsttksltltvfqGILRPM---HEKIVGRIAVSDLARRW------ 154
Cdd:cd03821 90 EYDVVHIHGVWTY-TSLAACKLARRrgiPYVVSPH-------------GMLDPWalqQKHWKKRIALHLIERRNlnnaal 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 155 -----QMEA-------LGSDAVEIPNGVDVDSFASAARLD---GYPRQGKTVLFLGRYDePRKGMAVLLDALPKVVQRFP 219
Cdd:cd03821 156 vhftsEQEAdelrrfgLEPPIAVIPNGVDIPEFDPGLRDRrkhNGLEDRRIILFLGRIH-PKKGLDLLIRAARKLAEQGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 220 DVQLLIVGHGD-----ADQLRGQAGrLAAHLRFLGQVDDAGKASAMRSADVYCAPnTGGESFGIVLVEAMAAGTAVVASD 294
Cdd:cd03821 235 DWHLVIAGPDDgaypaFLQLQSSLG-LGDRVTFTGPLYGEAKWALYASADLFVLP-SYSENFGNVVAEALACGLPVVITD 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489508612 295 LDAFRRVLRDGeVGHLVpvdppDLQAAALADGLIAVLENDVLRERYVAAGNAAVR---RYDWSVVASQI 360
Cdd:cd03821 313 KCGLSELVEAG-CGVVV-----DPNVSSLAEALAEALRDPADRKRLGEMARRARQveeNFSWEAVAGQL 375
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
15-362 |
1.16e-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: 109.64 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 15 GGVQSHVLQLAEVMRTRGHLVSVLAPASPhAALPDyfvsggrAVPIPYNGSVARLRFGPAThRKVKKWL----------- 83
Cdd:cd03800 21 GGQNVYVLELARALAELGYQVDIFTRRIS-PADPE-------VVEIAPGARVIRVPAGPPE-YLPKEELwpyleefadgl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 84 ------AHGDFDVLHLHEPNAPSLSMLALNIAEGPIVATFHT------STTKSLTLTVFQgiLRPMHEKIVGR-----IA 146
Cdd:cd03800 92 lrfiarEGGRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHSlgrvkyRHLGAQDTYHPS--LRITAEEQILEaadrvIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 147 VSDLARRWQMEALGSDAVE---IPNGVDVDSFASAARLD------GYPRQGKTVLFLGRYDePRKGMAVLLDALPKVVQR 217
Cdd:cd03800 170 STPQEADELISLYGADPSRinvVPPGVDLERFFPVDRAEarrarlLLPPDKPVVLALGRLD-PRKGIDTLVRAFAQLPEL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 218 FPDVQLLIVGHGDADQL---RGQAGRLAAHL------RFLGQVDDAGKASAMRSADVYCAPNTGgESFGIVLVEAMAAGT 288
Cdd:cd03800 249 RELANLVLVGGPSDDPLsmdREELAELAEELglidrvRFPGRVSRDDLPELYRAADVFVVPSLY-EPFGLTAIEAMACGT 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489508612 289 AVVASDLDAFRRVLRDGEVGHLVpvdpPDLQAAALADGLIAVLENDVLRERYVAAG-NAAVRRYDWSVVASQIMR 362
Cdd:cd03800 328 PVVATAVGGLQDIVRDGRTGLLV----DPHDPEALAAALRRLLDDPALWQRLSRAGlERARAHYTWESVADQLLT 398
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
166-367 |
2.60e-26 |
|
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: 108.19 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 166 IPNGVDVDSF-----ASAARLDGYPRQGKTVLFLG-RYDEPRKGMAVLLDALPKVVQRfPDVQLLIVGHGDAdqlrgQAG 239
Cdd:cd03825 166 IPNGIDTEIFapvdkAKARKRLGIPQDKKVILFGAeSVTKPRKGFDELIEALKLLATK-DDLLLVVFGKNDP-----QIV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 240 RLAAHLRFLGQVDDAGK-ASAMRSADVYCAPnTGGESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHLVPV-DPPD 317
Cdd:cd03825 240 ILPFDIISLGYIDDDEQlVDIYSAADLFVHP-SLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPgDVQA 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489508612 318 lqaaaLADGLIAVLENDVLRERY-VAAGNAAVRRYDWSVVASQIMRVYETV 367
Cdd:cd03825 319 -----LAEAIEWLLANPKERESLgERARALAENHFDQRVQAQRYLELYKDL 364
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
15-352 |
1.10e-25 |
|
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: 106.20 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 15 GGVQSHVLQLAEVMRTRGHLVSVLApASPHAALPDYFVSGGRAVPIPYNGSVARLRFGPA---THRKVKKWlahgdFDVL 91
Cdd:cd03795 14 GGIEQVIYDLAEGLKKKGIEVDVLC-FSKEKETPEKEENGIRIHRVKSFLNVASTPFSPSyikRFKKLAKE-----YDII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 92 HLHEPNaPSLSML-ALNIAEGPIVATFHtsttkslTLTVFQGILRPMHE-------KIVGRIAVSD---LARRWQMEALG 160
Cdd:cd03795 88 HYHFPN-PLADLLlFFSGAKKPVVVHWH-------SDIVKQKKLLKLYKplmtrflRRADRIIATSpnyVETSPTLREFK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 161 SDAVEIPNGVDVDSFASAARLDGYPRQ----GKTVLFLGRYdEPRKGMAVLLDALpkvvqRFPDVQLLIVGHGD-ADQLR 235
Cdd:cd03795 160 NKVRVIPLGIDKNVYNIPRVDFENIKRekkgKKIFLFIGRL-VYYKGLDYLIEAA-----QYLNYPIVIGGEGPlKPDLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 236 GQAgrlAAHL----RFLGQVDDAGKASAMRSADVYCAP-NTGGESFGIVLVEAMAAGTAVVASDLD-AFRRVLRDGEVGH 309
Cdd:cd03795 234 AQI---ELNLldnvKFLGRVDDEEKVIYLHLCDVFVFPsVLRSEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGL 310
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489508612 310 LVPvdPPDlqAAALADGLIAVLENDVLRERYvaaGNAAVRRYD 352
Cdd:cd03795 311 VVP--PKD--PDALAEAIDKLLSDEELRESY---GENAKKRFE 346
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
2-359 |
2.38e-25 |
|
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: 105.01 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 2 RIGMICPySFDVPGGVQSHVLQLAEVMRTRGHLVSVLAPASPhAALPDYFVSGG---RAVPIPYNGSVARLRFGPATHRK 78
Cdd:cd03820 1 KIAIVIP-SISNAGGAERVAINLANHLAKKGYDVTIISLDSA-EKPPFYELDDNikiKNLGDRKYSHFKLLLKYFKKVRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 79 VKKWLAHGDFDVLHLHEPNAPS-LSMLALNIaegPIVATFHTSTTKSLTLTVFQGILR---PMHEKIVgriAVSDLARRW 154
Cdd:cd03820 79 LRKYLKNNKPDVVISFRTSLLTfLALIGLKS---KLIVWEHNNYEAYNKGLRRLLLRRllyKRADKIV---VLTEADKLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 155 QMEALGSDAVEIPNGVDVDSFASAarldgYPRQGKTVLFLGRYdEPRKGMAVLLDALPKVVQRFPDVQLLIVGHG-DADQ 233
Cdd:cd03820 153 KYKQPNSNVVVIPNPLSFPSEEPS-----TNLKSKRILAVGRL-TYQKGFDLLIEAWALIAKKHPDWKLRIYGDGpEREE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 234 LRGQA--GRLAAHLRFLGQVDDAgkASAMRSADVYCAPNTGgESFGIVLVEAMAAGTAVVASDLDAFRR-VLRDGEVGHL 310
Cdd:cd03820 227 LEKLIdkLGLEDRVKLLGPTKNI--AEEYANSSIFVLSSRY-EGFPMVLLEAMAYGLPIISFDCPTGPSeIIEDGENGLL 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 489508612 311 VPVDppdlQAAALADGLIAVLENDVLRERYVAAGNAAVRRYDWSVVASQ 359
Cdd:cd03820 304 VPNG----DVDALAEALLRLMEDEELRKKMGKNARKNAERFSIEKIIKQ 348
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
2-367 |
4.08e-24 |
|
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: 101.21 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 2 RIGMICPYSFDVP----GGVQSHVLQLAEVMRTRGHLVSVLAPASPHAALPDYFVSGG--RAVPIPYNGSVARLRFgpat 75
Cdd:cd03802 1 RIAQVSPPRGPVPpgkyGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSAPLVAVIPRalRLDPIPQESKLAELLE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 76 hrKVKKWLAHGDFDVLHLHEPNAPSLSMLALNiaeGPIVATFHTSTTKSLTLTVFQgilrpmhEKIVGRIAVSDLARRwQ 155
Cdd:cd03802 77 --ALEVQLRASDFDVIHNHSYDWLPPFAPLIG---TPFVTTLHGPSIPPSLAIYAA-------EPPVNYVSISDAQRA-A 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 156 MEALGSDAVeIPNGVDVDSFASAarldgyPRQGKTVLFLGRYdEPRKGmavLLDALpKVVQRfPDVQLLIVGhGDADQLR 235
Cdd:cd03802 144 TPPIDYLTV-VHNGLDPADYRFQ------PDPEDYLAFLGRI-APEKG---LEDAI-RVARR-AGLPLKIAG-KVRDEDY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 236 G---QAGRLAAHLRFLGQVDDAGKASAMRSADVYCAPNTGGESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHLVp 312
Cdd:cd03802 210 FyylQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLV- 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489508612 313 vdpPDLQAAALADGLIAVLENDVLRERyvaagnaAVRRYDWSVVASQIMRVYETV 367
Cdd:cd03802 289 ---DSVEEMAEAIANIDRIDRAACRRY-------AEDRFSAARMADRYEALYRKV 333
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
15-355 |
6.38e-24 |
|
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: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 15 GGVQSHVLQLAEVMRTRGHLVSVLAPASPHAALPDYFVSGGRAVPIPYNGSVARLRFG---------PATHRKVKKWLAH 85
Cdd:cd03823 15 GGAEISVHDLAEALVAEGHEVAVLTAGVGPPGQATVARSVVRYRRAPDETLPLALKRRgyelfetynPGLRRLLARLLED 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 86 GDFDVLHLHepNAPSLSMLALNIAEG---PIVATFHTsttksltltVFQGILR--PMHEKIVGRIAVS-DLARRWQMEAL 159
Cdd:cd03823 95 FRPDVVHTH--NLSGLGASLLDAARDlgiPVVHTLHD---------YWLLCPRqfLFKKGGDAVLAPSrFTANLHEANGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 160 GSDAVE-IPNGVDVDSFASAARLDGYPRqgKTVLFLGRyDEPRKGMAVLLDALPKVvqRFPDVQLLIVGHGDADQLRGQA 238
Cdd:cd03823 164 FSARISvIPNAVEPDLAPPPRRRPGTER--LRFGYIGR-LTEEKGIDLLVEAFKRL--PREDIELVIAGHGPLSDERQIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 239 GRLAahLRFLGQVDDAGKASAMRSADVYCAPNTGGESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHLVPVDppdl 318
Cdd:cd03823 239 GGRR--IAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPG---- 312
|
330 340 350
....*....|....*....|....*....|....*..
gi 489508612 319 QAAALADGLIAVLENDVLRERYvAAGNAAVRRYDWSV 355
Cdd:cd03823 313 DAEDLAAAMRRLLTDPALLERL-RAGAEPPRSTESQA 348
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
14-347 |
2.74e-23 |
|
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: 99.70 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 14 PGGVQSHVLQLAEVMRTRGHLVSVLApasphAALPDYFVSGGRAVPIPYNGSVARLRFGPATHRKVKKWLAHGDFDVLHL 93
Cdd:cd03807 11 VGGAETMLLRLLEHMDKSRFEHVVIS-----LTGDGVLGEELLAAGVPVVCLGLSSGKDPGVLLRLAKLIRKRNPDVVHT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 94 HEPNAPSLSMLALNIAEG-PIVATFHTSTTKSLTLTVFQGILRPMHEKIVGRIAVSDLARRwQMEALGSDA---VEIPNG 169
Cdd:cd03807 86 WMYHADLIGGLAAKLAGGvKVIWSVRSSNIPQRLTRLVRKLCLLLSKFSPATVANSSAVAE-FHQEQGYAKnkiVVIYNG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 170 VDVDSF-------ASAARLDGYPRQGKTVLFLGRYdEPRKGMAVLLDALPKVVQRFPDVQLLIVGHG----DADQLRGQA 238
Cdd:cd03807 165 IDLFKLspddasrARARRRLGLAEDRRVIGIVGRL-HPVKDHSDLLRAAALLVETHPDLRLLLVGRGperpNLERLLLEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 239 GrLAAHLRFLGQVDDAgkASAMRSADVYCAPNTGgESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGeVGHLVPVDPPDl 318
Cdd:cd03807 244 G-LEDRVHLLGERSDV--PALLPAMDIFVLSSRT-EGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPAGDPQ- 317
|
330 340
....*....|....*....|....*....
gi 489508612 319 qaaALADGLIAVLEndvLRERYVAAGNAA 347
Cdd:cd03807 318 ---ALADAIRALLE---DPEKRARLGRAA 340
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
83-365 |
2.76e-22 |
|
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: 96.69 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 83 LAHGDFDVLHL-HE-----PNAPSLSMLALNIAEGPIVATFHTSTTKS----LTLTVFQGILRPMHEKIVGRIAVSDLAR 152
Cdd:cd03822 71 LNFKKPDVVHIqHEfgifgGKYGLYALGLLLHLRIPVITTLHTVLDLSdpgkQALKVLFRIATLSERVVVMAPISRFLLV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 153 RwqMEALGSDAVE-IPNGV-DVDSFASAARLDGYPRQGKTVL----FLGRYdeprKGMAVLLDALPKVVQRFPDVQLLIV 226
Cdd:cd03822 151 R--IKLIPAVNIEvIPHGVpEVPQDPTTALKRLLLPEGKKVIltfgFIGPG----KGLEILLEALPELKAEFPDVRLVIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 227 GHGDADQLRGQAGR-LAAHLRFLGQVDDA-------GKASAMR---SADVYCAP--NTGGESFGiVLVEAMAAGTAVVAS 293
Cdd:cd03822 225 GELHPSLARYEGERyRKAAIEELGLQDHVdfhnnflPEEEVPRyisAADVVVLPylNTEQSSSG-TLSYAIACGKPVIST 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489508612 294 DLDAFRRVLRDGEvGHLVPVDPPdlqaAALADGLIAVLENDVLRERYVAAGNAAVRRYDWSVVASQIMRVYE 365
Cdd:cd03822 304 PLRHAEELLADGR-GVLVPFDDP----SAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADRYLRLFN 370
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
259-367 |
1.38e-21 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 88.89 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 259 AMRSADVYCAPNTGgESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHLVPVDppdlQAAALADGLIAVLENDVLRE 338
Cdd:COG0438 17 LLAAADVFVLPSRS-EGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPG----DPEALAEAILRLLEDPELRR 91
|
90 100 110
....*....|....*....|....*....|
gi 489508612 339 RYVAAGNAAVR-RYDWSVVASQIMRVYETV 367
Cdd:COG0438 92 RLGEAARERAEeRFSWEAIAERLLALYEEL 121
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
104-350 |
1.96e-21 |
|
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340860 [Multi-domain] Cd Length: 365 Bit Score: 94.44 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 104 LALNIAEG---PIVATFH---------TSTTKSLTLTVFQGILRPMHEKIVGRIAVSDLARRwQMEALGSDA---VEIPN 168
Cdd:cd05844 95 YALPLARAlgvPLVVTFHgfdittsraWLAASPGWPSQFQRHRRALQRPAALFVAVSGFIRD-RLLARGLPAeriHVHYI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 169 GVDVDSFASAARldgyPRQGKTVLFLGRYDEpRKGMAVLLDALPKVVQRFPDVQLLIVGHG-DADQLRGQAGRLaAHLRF 247
Cdd:cd05844 174 GIDPAKFAPRDP----AERAPTILFVGRLVE-KKGCDVLIEAFRRLAARHPTARLVIAGDGpLRPALQALAAAL-GRVRF 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 248 LGQVDDAGKASAMRSADVYC-----APNTGGESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHLVPVDPPDlqaaA 322
Cdd:cd05844 248 LGALPHAEVQDWMRRAEIFClpsvtAASGDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVD----A 323
|
250 260
....*....|....*....|....*...
gi 489508612 323 LADGLIAVLENDVLRERYVAAGNAAVRR 350
Cdd:cd05844 324 LADALQALLADRALADRMGGAARAFVCE 351
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
15-173 |
2.18e-20 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 87.20 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 15 GGVQSHVLQLAEVMRTRGHLVSVLAPASPHAalPDYFVSGGRAVPIPYNGSVARLRFGPATHRKVKKWLAHGDFDVLHLH 94
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGP--LAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 95 EPNAPSLSMLALNIAEG-PIVATFHTSTTKSLTLTVFQGILRPMHEKIVGR--------IAVSDLARRWQMEALGSDAVE 165
Cdd:pfam13439 79 SPFPLGLAALAARLRLGiPLVVTYHGLFPDYKRLGARLSPLRRLLRRLERRllrradrvIAVSEAVADELRRLYGVPPEK 158
|
170
....*....|.
gi 489508612 166 ---IPNGVDVD 173
Cdd:pfam13439 159 irvIPNGVDLE 169
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
3-311 |
5.70e-20 |
|
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: 87.84 E-value: 5.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 3 IGMICPYSFDVPGGVQSHVLQLAEVMRTRGHLVSVLAPASPHaalpdyfvsggravpipyngsvarlrfgpatHRKVKKW 82
Cdd:cd01635 1 ILLVTGEYPPLRGGLELHVRALARALAALGHEVTVLALLLLA-------------------------------LRRILKK 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 83 LAHGDFDVLHLHEPNAPSLS-MLALNIAEGPIVATFHtsttksltltvfqgilrpmhekivgriaVSDLARRWQMEALGS 161
Cdd:cd01635 50 LLELKPDVVHAHSPHAAALAaLLAARLLGIPIVVTVH----------------------------GPDSLESTRSELLAL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 162 DAVEIPngvdvdsfasaarldgypRQGKTVLFLGRYDePRKGMAVLLDALPKVVQRFPDVQLLIVGHGDAD----QLRGQ 237
Cdd:cd01635 102 ARLLVS------------------LPLADKVSVGRLV-PEKGIDLLLEALALLKARLPDLVLVLVGGGGEReeeeALAAA 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489508612 238 AGRLAAHLRFLGQVDDAGKASAMRSADVYCAPnTGGESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHLV 311
Cdd:cd01635 163 LGLLERVVIIGGLVDDEVLELLLAAADVFVLP-SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
145-351 |
4.82e-19 |
|
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: 88.16 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 145 IAVSDLARRWQmEALGSDAVE---IPNGVDVDSFASAaRLDGYPRQGKTVLFLGRYDePRKGMAVLLDALPKVVQRFPDV 221
Cdd:cd03813 249 ISLYEGNRRRQ-IRLGADPDKtrvIPNGIDIQRFAPA-REERPEKEPPVVGLVGRVV-PIKDVKTFIRAFKLVRRAMPDA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 222 QLLIVGHGDADQLRGQAGR-LAAHLRFLGQVDDAGKasaMRSADVYcaPNTG-------GESFGIVLVEAMAAGTAVVAS 293
Cdd:cd03813 326 EGWLIGPEDEDPEYAQECKrLVASLGLENKVKFLGF---QNIKEYY--PKLGllvltsiSEGQPLVILEAMASGVPVVAT 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489508612 294 DLDAFRRVLRD-----GEVGHLVPVDPPDlqaaALADGLIAVLENDVLRERYVAAGNAAVRRY 351
Cdd:cd03813 401 DVGSCRELIYGaddalGQAGLVVPPADPE----ALAEALIKLLRDPELRQAFGEAGRKRVEKY 459
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
5-360 |
2.37e-17 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 83.22 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 5 MICPYSFDVPGGVQSHVLQLAEVMRTRGHLVSVLapaSPHAALPDYF----VSGGRAVPIPYNGSVArLRFgpATHRKVK 80
Cdd:PLN02871 64 FVEPSPFSYVSGYKNRFQNFIRYLREMGDEVLVV---TTDEGVPQEFhgakVIGSWSFPCPFYQKVP-LSL--ALSPRII 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 81 KWLAHGDFDVLHLHEPNApslsML--ALNIAEG---PIVATFHTSTTKSLTLTVFQGILRPMHEKIVGRIAVSDL----- 150
Cdd:PLN02871 138 SEVARFKPDLIHASSPGI----MVfgALFYAKLlcvPLVMSYHTHVPVYIPRYTFSWLVKPMWDIIRFLHRAADLtlvts 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 151 -ARRWQMEALGSDAVE----IPNGVDVDSF-------ASAARLDGYPRQGKTVLFLGRYdeprkGMAVLLDALPKVVQRF 218
Cdd:PLN02871 214 pALGKELEAAGVTAANrirvWNKGVDSESFhprfrseEMRARLSGGEPEKPLIVYVGRL-----GAEKNLDFLKRVMERL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 219 PDVQLLIVGHGDADQlrgqagRLAAHLR-----FLGQVDDAGKASAMRSADVYCAPNTGgESFGIVLVEAMAAGTAVVAS 293
Cdd:PLN02871 289 PGARLAFVGDGPYRE------ELEKMFAgtptvFTGMLQGDELSQAYASGDVFVMPSES-ETLGFVVLEAMASGVPVVAA 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489508612 294 DLDAFRRVLRD---GEVGHLVPvdPPDLQAAAladGLI-AVLENDVLRERYVAAGNAAVRRYDWSVVASQI 360
Cdd:PLN02871 362 RAGGIPDIIPPdqeGKTGFLYT--PGDVDDCV---EKLeTLLADPELRERMGAAAREEVEKWDWRAATRKL 427
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-361 |
4.20e-17 |
|
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
Pssm-ID: 340825 [Multi-domain] Cd Length: 391 Bit Score: 82.00 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 2 RIGMICPYSFDVPGGVQSHVLQLAEVMRTRGHLVSVLAPaSPHAALPDYFVSGGRA--------VPIPY---NGSVAR-- 68
Cdd:cd03794 1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTP-SPNYPLGRIFAGATETkdgirvirVKLGPikkNGLIRRll 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 69 --LRFGpathRKVKKWL--AHGDFDVLHLHEPNAPS--LSMLALNIAEGPIVATFH------TSTTKSLTLTVFQGILRP 136
Cdd:cd03794 80 nyLSFA----LAALLKLlvREERPDVIIAYSPPITLglAALLLKKLRGAPFILDVRdlwpesLIALGVLKKGSLLKLLKK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 137 MHEKIVGR----IAVSDLARRwQMEALGSDA---VEIPNGVDVDSFAS----AARLDGYPRQGKTVLFLGRYDEPRkGMA 205
Cdd:cd03794 156 LERKLYRLadaiIVLSPGLKE-YLLRKGVPKekiIVIPNWADLEEFKPppkdELRKKLGLDDKFVVVYAGNIGKAQ-GLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 206 VLLDALpKVVQRFPDVQLLIVGHGD--ADQLRGQAGRLAAHLRFLGQVDDAGKASAMRSADVYCAPNTGGESFGIV---- 279
Cdd:cd03794 234 TLLEAA-ERLKRRPDIRFLFVGDGDekERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGSspsk 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 280 LVEAMAAGTAVVASDLDAFRRVLRDGEVGhlVPVDPPDlqAAALADGLIAVLENDVLRERYVAAGNAAV-RRYDWSVVAS 358
Cdd:cd03794 313 LFEYMAAGKPILASDDGGSDLAVEINGCG--LVVEPGD--PEALADAILELLDDPELRRAMGENGRELAeEKFSREKLAD 388
|
...
gi 489508612 359 QIM 361
Cdd:cd03794 389 RLL 391
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
166-358 |
6.21e-16 |
|
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: 78.56 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 166 IPNGVDVDSFA--SAARLD-----GYPRQGKTVLFLGRYDEPRKGMAVLLDALPKVVQRFPDVQLLIVG---------HG 229
Cdd:cd03818 184 IHDGVDTDRLApdPAARLRllngtELKAGDPVITYVARNLEPYRGFHVFMRALPRIQARRPDARVVVVGgdgvsygspPP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 230 DADQLRGQAGR-LAAHLR---FLGQVDDAGKASAMRSADVYCAPN-TGGESFGivLVEAMAAGTAVVASDLDAFRRVLRD 304
Cdd:cd03818 264 DGGSWKQKMLAeLGVDLErvhFVGKVPYDQYVRLLQLSDAHVYLTyPFVLSWS--LLEAMACGCPVIGSDTAPVREVIRD 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489508612 305 GEVGHLVPVDPPDlqaaALADGLIAVLENDVLRERY-VAAGNAAVRRYDWSVVAS 358
Cdd:cd03818 342 GRNGLLVDFFDPD----ALAAAVLELLEDPDRAAALrRAARRTVERSDSLDVCLA 392
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
1-367 |
1.53e-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: 77.01 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 1 MRIGMICPYSFDVPGGVQSHV-LQLAEvmrtRGHLVSVLAPASP-----HAALPDYFVSGGRAVPI----PYNGSVARlr 70
Cdd:cd04962 1 MKIGIVCYPSYGGSGVVATELgLELAE----RGHEVHFISSAIPfrlnlYSGNIFFHEVEVPNYPLfeypPYTLALAS-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 71 fgpathrKVKKWLAHGDFDVLHLHE--PNApSLSMLALNIAEG--PIVATFHTS-TTKSLTLTVFQGILRPMHEKIVGRI 145
Cdd:cd04962 75 -------KIVEVAKEHKLDVLHAHYaiPHA-SCAYLAREILGEkiPIVTTLHGTdITLVGYDPSLQPAVRFSINKSDRVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 146 AVSDLARRWQMEALGSDA-VE-IPNGVDVDSF-----ASAARLDGYPRQGKTVLFLGRYdEPRKGMAVLLDALPKVVQRF 218
Cdd:cd04962 147 AVSSSLRQETYELFDVDKdIEvIHNFIDEDVFkrkpaGALKRRLLAPPDEKVVIHVSNF-RPVKRIDDVVRVFARVRRKI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 219 PdVQLLIVGHG-DADQLRGQAGRLAA--HLRFLGQVDDAgkASAMRSADVYCAPnTGGESFGIVLVEAMAAGTAVVASDL 295
Cdd:cd04962 226 P-AKLLLVGDGpERVPAEELARELGVedRVLFLGKQDDV--EELLSIADLFLLP-SEKESFGLAALEAMACGVPVVSSNA 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489508612 296 DAFRRVLRDGEVGHLVPVDPPDlqaaALADGLIAVLENDVLRERYVAAG-NAAVRRYDWSVVASQIMRVYETV 367
Cdd:cd04962 302 GGIPEVVKHGETGFLSDVGDVD----AMAKSALSILEDDELYNRMGRAArKRAAERFDPERIVPQYEAYYRRL 370
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
14-294 |
4.82e-14 |
|
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: 72.71 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 14 PGGVQSHVLQLAEVMRTRGHLVSVLAPASPHAALPDYFVS-GGRAVPIPYNGSVARLRFgpathRKVKKWLAHGDFDVLH 92
Cdd:cd03812 11 VGGIETFLMNLYRKLDKSKIEFDFLATSDDKGEYDEELEElGGKIFYIPPKKKNIIKYF-----IKLLKLIKKEKYDIVH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 93 LHEPNAPSLSMLALNIAEGPI-VATFHT-STTKSLTLTVFQGILRPMHEKIV-GRIAVSDLARRW--QMEALGSDAVeIP 167
Cdd:cd03812 86 VHGSSSNGIILLLAAKAGVPVrIAHSHNtKDSSIKLRKIRKNVLKKLIERLStKYLACSEDAGEWlfGEVENGKFKV-IP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 168 NGVDVDSF-----ASAARLDGYPRQGKTVL-FLGRYDEpRKGMAVLLDALPKVVQRFPDVQLLIVGHGdadQLRGQAGRL 241
Cdd:cd03812 165 NGIDIEKYkfnkeKRRKRRKLLILEDKLVLgHVGRFNE-QKNHSFLIDIFEELKKKNPNVKLVLVGEG---ELKEKIKEK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 489508612 242 AAHLR------FLGQVDDAgkASAMRSADVYCAPNTGgESFGIVLVEAMAAGTAVVASD 294
Cdd:cd03812 241 VKELGledkviFLGFRNDV--SEILSAMDVFLFPSLY-EGLPLVAVEAQASGLPCLLSD 296
|
|
| thiol_BshA |
TIGR03999 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, ... |
87-365 |
1.20e-13 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, a glycosyltransferase required for bacillithiol biosynthesis. This enzyme combines UDP-GlcNAc and L-malate to form N-acetyl-alpha-D-glucosaminyl L-malate synthase. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
Pssm-ID: 274914 [Multi-domain] Cd Length: 374 Bit Score: 71.48 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 87 DFDVLHLHE--PNAPSlSMLALNIAEG-----PIVATFHTS-TTKSLTLTVFQGILRPMHEKIVGRIAVSDLARR--WQM 156
Cdd:TIGR03999 84 KLDLLHVHYaiPHAIA-AYLARQMLGKegidiPIVTTLHGTdITLVGADPSFKPAVRFSIEKSDGVTAVSESLKEetYEL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 157 EALGSDAVEIPNGVDVDSfasaarldgYPRQGKTVL---FLGRYDEP--------RKgmavlLDALPKVVQRFPDVQ--- 222
Cdd:TIGR03999 163 FDIDKPIEVIPNFVDTDR---------YRRKNDPALkrkLGAPEDEKvlihisnfRP-----VKRVEDVIEVFARVQqev 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 223 ---LLIVGHGDAdqlRGQAGRLAAHL------RFLGQVDDAGKASAMrsADVYCAPnTGGESFGIVLVEAMAAGTAVVAS 293
Cdd:TIGR03999 229 pakLLLVGDGPE---RSPAEQLVRELgltdrvLFLGKQDDVAELLSI--SDLFLLP-SEKESFGLAALEAMACGVPVIAS 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489508612 294 DLDAFRRVLRDGEVGHLVPVDppDLQAAalADGLIAVLENDVLRERYVAAG-NAAVRRYDwsvvASQIMRVYE 365
Cdd:TIGR03999 303 NAGGIPEVVEHGVTGFLCDVG--DVETM--AEYAISLLEDEELLQRFSAAArERAKERFD----SEKIVPQYE 367
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
2-368 |
1.74e-12 |
|
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: 68.03 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 2 RIGMICPYSFDVPGGVQSHVLQLAEVMRTRGHLVSVLApaspHAALPDY---FVSGGRAV---PIP--YNGSVARLRFGp 73
Cdd:cd03796 1 RICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVIT----HAYGNRVgvrYLTNGLKVyylPFKvfYNQSTLPTLFS- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 74 aTHRKVKKWLAHGDFDVLHLHEpnapSLSMLALniaEGPIVA---------TFHTSTTKSLTLTVFQGILRPMHEKIVGR 144
Cdd:cd03796 76 -TFPLLRNILIRERIQIVHGHQ----AFSSLAH---EALFHArtlglktvfTDHSLFGFADASSILTNKLLRFSLADIDH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 145 -IAVSDLAR-----RWQMEAlgSDAVEIPNGVDVDSFASAArlDGYPRQGKTVLFLGRYdEPRKGMAVLLDALPKVVQRF 218
Cdd:cd03796 148 vICVSHTSKentvlRASLDP--RIVSVIPNAVDSSDFTPDP--SKPDPNKITIVVISRL-VYRKGIDLLVGIIPRICKKH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 219 PDVQLLIVGHG----DADQLRgQAGRLAAHLRFLGQVDDAGKASAMRSADVYCapNTG-GESFGIVLVEAMAAGTAVVAS 293
Cdd:cd03796 223 PNVRFIIGGDGpkriELEEMR-EKYQLQDRVELLGAVPHEEVRDVLVQGHIFL--NTSlTEAFCIAIVEAASCGLLVVST 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489508612 294 DLDAFRRVLRDGEVGHLVPvDPPDLQAAAladgLIAVlenDVLRERYVA---AGNAAVRRYDWSVVASQIMRVYETVA 368
Cdd:cd03796 300 RVGGIPEVLPPDMILLAEP-DPEDIVRKL----EEAI---SILRTGKHDpwsFHNRVKKMYSWEDVARRTEKVYDRIL 369
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
86-352 |
9.66e-12 |
|
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: 65.55 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 86 GDFDVLHLH--EPNAPSLSMLALNIAEGPIVATFHTSTTKSLtltvfqgiLRPMHEKIVGRI-AVSDL----ARRWQMEA 158
Cdd:cd03799 69 GAYDIIHCQfgPLGALGALLRRLKVLKGKLVTSFRGYDISMY--------VILEGNKVYPQLfAQGDLflpnCELFKHRL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 159 --LGSDAVEI---PNGVDVDSFASAARLDgyPRQGKT-VLFLGRYDEpRKGMAVLLDALPKVVQRFPDVQLLIVGHGDad 232
Cdd:cd03799 141 iaLGCDEKKIivhRSGIDCNKFRFKPRYL--PLDGKIrILTVGRLTE-KKGLEYAIEAVAKLAQKYPNIEYQIIGDGD-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 233 qLRGQAGRLAAHL------RFLGQVDDAGKASAMRSADVYCAPNT---GGESFGIV--LVEAMAAGTAVVASDLDAFRRV 301
Cdd:cd03799 216 -LKEQLQQLIQELnigdcvKLLGWKPQEEIIEILDEADIFIAPSVtaaDGDQDGPPntLKEAMAMGLPVISTEHGGIPEL 294
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489508612 302 LRDGEVGHLVpvdpPDLQAAALADGLIAVLENDVLRERYVAAGNAAVR-RYD 352
Cdd:cd03799 295 VEDGVSGFLV----PERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEeEYD 342
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
161-364 |
2.33e-11 |
|
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.
Pssm-ID: 340857 [Multi-domain] Cd Length: 360 Bit Score: 64.39 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 161 SDAVEIPNGVDVDSF--ASAARL---DGYPRQGKTVLFL--GRYDEPrKGMAVLLDALPKVVQRFPDVQLLIVGHGdadQ 233
Cdd:cd04951 154 NKSVPVYNGIDLNKFkkDINVRLkirNKLNLKNDEFVILnvGRLTEA-KDYPNLLLAISELILSKNDFKLLIAGDG---P 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 234 LRGQAGRLAAHLR------FLGQVDDAgkASAMRSADVYCAPNTGgESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEv 307
Cdd:cd04951 230 LRNELERLICNLNlvdrviLLGQISNI--SEYYNAADLFVLSSEW-EGFGLVVAEAMACERPVVATDAGGVAEVVGDHN- 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489508612 308 gHLVPVDPPDLQAAALADGLIAVLEndvLRERYVAAGNAAVRRYDWSVVASQIMRVY 364
Cdd:cd04951 306 -YVVPVSDPQLLAEKIKEIFDMSDE---ERDILGNKNEYIAKNFSINTIVNEWERLY 358
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
145-308 |
1.29e-10 |
|
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: 62.30 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 145 IAVSD-LARRWQmEALGSDAVEIPNGVDVDSFASAARLDGYprqgktVLFLGRYdEPRKGMAVLLDA---LPKvvqrfpd 220
Cdd:cd03804 162 IANSQfVARRIK-KFYGRESTVIYPPVDTDAFAPAADKEDY------YLTASRL-VPYKRIDLAVEAfneLPK------- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 221 vQLLIVGHG-DADQLRGQAGRlaaHLRFLGQVDDAGKASAMRSADVYCAPntGGESFGIVLVEAMAAGTAVVASDLDAFR 299
Cdd:cd03804 227 -RLVVIGDGpDLDRLRAMASP---NVEFLGYQPDEVLKELLSKARAFVFA--AEEDFGIVPVEAQACGTPVIAFGKGGAL 300
|
....*....
gi 489508612 300 RVLRDGEVG 308
Cdd:cd03804 301 ETVRPGPTG 309
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
139-357 |
2.34e-10 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 61.34 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 139 EKIVGRIAVSDLARRWQMEALGSDAVEI-PNGVDVDSFASAARLD-----GYPRQGKTVLFLGRYdEPRKGMAVLLDALP 212
Cdd:PRK15484 138 DKNAKIIVPSQFLKKFYEERLPNADISIvPNGFCLETYQSNPQPNlrqqlNISPDETVLLYAGRI-SPDKGILLLMQAFE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 213 KVVQRFPDVQLLIVG------HGDA----DQLRGQAGRLAAHLRFLGQVDDAGKASAMRSADVYCAPNTGGESFGIVLVE 282
Cdd:PRK15484 217 KLATAHSNLKLVVVGdptassKGEKaayqKKVLEAAKRIGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVEEAFCMVAVE 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489508612 283 AMAAGTAVVASDLDAFRRVLRDGEVG-HLVPVDPPDlqaaALADGLIAVLENDVLRERYVAAGNAAVRRYDWSVVA 357
Cdd:PRK15484 297 AMAAGKPVLASTKGGITEFVLEGITGyHLAEPMTSD----SIISDINRTLADPELTQIAEQAKDFVFSKYSWEGVT 368
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
166-351 |
7.94e-09 |
|
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: 56.86 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 166 IPNGVDVDSFAS--AARLDGYPrqgKTVLFLGRYdEPRKGMAVLLDALPKVVQRFPDVQLLIVGHGDADQLRGQAGR--- 240
Cdd:NF038011 285 IPNGIDLPRLAPlrAQRPAGIP---PVVGLIGRV-VPIKDIKTFIRAMRTVVRAMPEAEGWIVGPEEEDPAYAAECRslv 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 241 ----LAAHLRFLG--QVDDagkasamrsadvyCAPNTG-------GESFGIVLVEAMAAGTAVVASDLDAFRRVL----- 302
Cdd:NF038011 361 aslgLQDKVKFLGfqKIDD-------------LLPQVGlmvlssiSEALPLVVLEAFAAGVPVVTTDVGSCRQLIeglde 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489508612 303 --RD-GEVGHLVPV-DPpdlqaAALADGLIAVLENDVLRERYVAAGNAAVRRY 351
Cdd:NF038011 428 edRAlGAAGEVVAIaDP-----QALARAALDLLRDPQRWQAAQAAGLARVERY 475
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
170-344 |
1.64e-08 |
|
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: 55.67 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 170 VDVDSFASA-ARLDGY--PRQGKTVLFLG--RYdEPRKGMAVLLDALPKVVQR---FPDVQLLIVGHGD---------AD 232
Cdd:cd03805 188 VDTDSFDSTsEDPDPGdlIAKSNKKFFLSinRF-ERKKNIALAIEAFAKLKQKlpeFENVRLVIAGGYDprvaenveyLE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 233 QLRGQAGRL---AAHLRFLGQVDDAGKASAMRSAD--VYCAPNtggESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEV 307
Cdd:cd03805 267 ELQRLAEELlnvEDQVLFLRSISDSQKEQLLSSALalLYTPSN---EHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVT 343
|
170 180 190
....*....|....*....|....*....|....*..
gi 489508612 308 GHLVPVDPpdlqaAALADGLIAVLENDVLRERYVAAG 344
Cdd:cd03805 344 GFLCEPTP-----EAFAEAMLKLANDPDLADRMGAAG 375
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
15-169 |
4.83e-08 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 52.02 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 15 GGVQSHVLQLAEVMRTRGHLVSVLAPAsPHAALPDYFVSGGRAVPIPYnGSVARLRFGPATHRKVKKWLAHGDFDVLHLH 94
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPG-GPPGRPELVGDGVRVHRLPV-PPRPSPLADLAALRRLRRLLRAERPDVVHAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 95 EPNAPSLSMLALNIAEGPIVATFHTSTTKSLTLTVfQGILRPMHEKIVGR----IAVSDLARRwQMEALGSDAVE---IP 167
Cdd:pfam13579 79 SPTAGLAARLARRRRGVPLVVTVHGLALDYGSGWK-RRLARALERRLLRRadavVVVSEAEAE-LLRALGVPAARvvvVP 156
|
..
gi 489508612 168 NG 169
Cdd:pfam13579 157 NG 158
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
166-351 |
7.62e-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: 53.46 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 166 IPNG-VDVDSFASAARldgyPRQGKTVLFLGRYdEPRKGMAVLLDALPKVVQRFPDVQLLIVGHGDADQ---LRGQAGRL 241
Cdd:cd04949 141 IPVGyVDQLDTAESNH----ERKSNKIITISRL-APEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREklkKLIEELHL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 242 AAHLRFLGQVDDAGKASAmrSADVYCAPNTgGESFGIVLVEAMAAGTAVVASDLD-AFRRVLRDGEVGHLVPVDppDLQa 320
Cdd:cd04949 216 EDNVFLKGYHSNLDQEYQ--DAYLSLLTSQ-MEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKN--NID- 289
|
170 180 190
....*....|....*....|....*....|.
gi 489508612 321 aALADGLIAVLENDVLRERYVAAGNAAVRRY 351
Cdd:cd04949 290 -ALADKIIELLNDPEKLQQFSEESYKIAEKY 319
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
268-362 |
1.44e-05 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 43.36 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508612 268 APNTGGESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEvgHLVPVDPPDlqaaALADGLIAVLENDVLRERYVAAGNAA 347
Cdd:pfam13524 4 NPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGE--EILLYRDPE----ELAEKIRYLLEHPEERRAIAAAGRER 77
|
90
....*....|....*.
gi 489508612 348 V-RRYDWSVVASQIMR 362
Cdd:pfam13524 78 VlAEHTYAHRAEQLLD 93
|
|
| |
