|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
4-351 |
3.24e-103 |
|
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: 308.52 E-value: 3.24e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 4 KIACVIHSLDGGGAERVMAGLASRLADREHSVTLITLDDGKHDRHEVDPRVSRLSIDVLSTPGNTVSLWSRTLRLRSTIA 83
Cdd:cd03811 1 KILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRILK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 84 SGNFDVVLSFCD-ATNWLTLLATRGlgVPVVVSERSDPKHQSLGRAREFLRRQLYPKAYRVVCLSDDVAVTLQSQ---TR 159
Cdd:cd03811 81 RAKPDVVISFLGfATYIVAKLAAAR--SKVIAWIHSSLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLgpsPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 160 CHTLVIPSAIEVPKEFRTRLKPITERQSDPgqakCHLVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHGEGSQRDHL 239
Cdd:cd03811 159 EKIEVIYNPIDIDRIRALAKEPILNEPEDG----PVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 240 ESLASKLNLASRVKFPGWTRPIWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGAvREIIDHGRNGWLVTND 319
Cdd:cd03811 235 EKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGP-REILDDGENGLLVPDG 313
|
330 340 350
....*....|....*....|....*....|....*.
gi 32444551 320 DAALRAGLLHCL----TSTELRERFAAQAGEVTDRY 351
Cdd:cd03811 314 DAAALAGILAALlqkkLDAALRERLAKAQEAVFREY 349
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
4-362 |
1.60e-87 |
|
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: 268.34 E-value: 1.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 4 KIACVIHSLD-GGGAERVMAGLASRLADREHSVTLITLDDGKHD-RHEVDPRVSR--LSIDVLSTPGNTVSLWSRTLRLR 79
Cdd:cd03820 1 KIAIVIPSISnAGGAERVAINLANHLAKKGYDVTIISLDSAEKPpFYELDDNIKIknLGDRKYSHFKLLLKYFKKVRRLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 80 STIASGNFDVVLSFcdATNWLTLLATRGLGVPVVVSERSDPKHQSLGRAREFLRRQLYPKAYRVVCLSDDVAVTLQSQTR 159
Cdd:cd03820 81 KYLKNNKPDVVISF--RTSLLTFLALIGLKSKLIVWEHNNYEAYNKGLRRLLLRRLLYKRADKIVVLTEADKLKKYKQPN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 160 CHTLVIPSAIEVPKEfrtrlkpiteRQSDPGQAKChLVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHGEGSQRDHL 239
Cdd:cd03820 159 SNVVVIPNPLSFPSE----------EPSTNLKSKR-ILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 240 ESLASKLNLASRVKFPGWTRPIWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGAVREIIDHGRNGWLVTND 319
Cdd:cd03820 228 EKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCPTGPSEIIEDGENGLLVPNG 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 32444551 320 D-AALRAGLLHCLTSTELRERFAAQAGEVTDRYGWPAMVDAYEA 362
Cdd:cd03820 308 DvDALAEALLRLMEDEELRKKMGKNARKNAERFSIEKIIKQWEE 351
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
13-365 |
3.92e-62 |
|
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: 203.54 E-value: 3.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 13 DGGGAERVMAGLASRLADREHSVTLITLDDGKHDRHEVDPRVSRLSIDVLSTPGNTVSLWSRtlrLRSTIASGNFDVVLS 92
Cdd:cd03801 12 PVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRE---LRPLLRLRKFDVVHA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 93 FCDATNWLTLLATRGLGVPVVVSERSDPKHQSLGRA---REFLRRQLYPKAY--RVVCLSD---DVAVTLQSQTRCHTLV 164
Cdd:cd03801 89 HGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLaaeRRLLARAEALLRRadAVIAVSEalrDELRALGGIPPEKIVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 165 IPSAIEVpkefrTRLKPITERQSDPGQAKCHLVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHG-EGSQRDHLESLa 243
Cdd:cd03801 169 IPNGVDL-----ERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGgDGPLRAELEEL- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 244 sKLNLASRVKFPGWTRP--IWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGaVREIIDHGRNGWLVTNDD- 320
Cdd:cd03801 243 -ELGLGDRVRFLGFVPDeeLPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGG-LPEVVEDGEGGLVVPPDDv 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 32444551 321 AALRAGLLHCLTSTELRERFAAQAGE-VTDRYGWPAMVDAYEACLQ 365
Cdd:cd03801 321 EALADALLRLLADPELRARLGRAARErVAERFSWERVAERLLDLYR 366
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
4-364 |
1.58e-47 |
|
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: 165.18 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 4 KIACVIHSLDGGGAERVMAGLASRLADREHSVTLITL-DDGkhdrhEVDPRVSRLSIDVLSTPGNTVSLWSRTLRLRSTI 82
Cdd:cd03807 1 KVAHVITGLNVGGAETMLLRLLEHMDKSRFEHVVISLtGDG-----VLGEELLAAGVPVVCLGLSSGKDPGVLLRLAKLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 83 ASGNFDVVLSFCDATNWLTLLATRG-LGVPVVVSERS--DPKHQSLGRAREFLRRQLYPKAyrVVCLSDDVAVTLQSQTR 159
Cdd:cd03807 76 RKRNPDVVHTWMYHADLIGGLAAKLaGGVKVIWSVRSsnIPQRLTRLVRKLCLLLSKFSPA--TVANSSAVAEFHQEQGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 160 CH--TLVIPSAIEVPK-----EFRTRLKpitERQSDPGQAKcHLVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHGE 232
Cdd:cd03807 154 AKnkIVVIYNGIDLFKlspddASRARAR---RRLGLAEDRR-VIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 233 GSQRDHLESLASKLNLASRVKFPGwTRPIWP-VYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGAvREIIDHGr 311
Cdd:cd03807 230 GPERPNLERLLLELGLEDRVHLLG-ERSDVPaLLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGA-AELVDDG- 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 32444551 312 NGWLVTNDDA-----ALRAGLLHCLTSTELRERFAAQageVTDRYGWPAMVDAYEACL 364
Cdd:cd03807 307 TGFLVPAGDPqaladAIRALLEDPEKRARLGRAARER---IANEFSIDAMVRRYETLY 361
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
4-361 |
1.69e-46 |
|
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: 162.38 E-value: 1.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 4 KIACVIHSldGGGAERVMAGLASRLADREHSVTLITLDDGKHDRHEVDPRVSRLSIDVLSTPGNTVSLWSRTLRLRSTIA 83
Cdd:cd03808 1 KILFIVNV--DGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKELGVKVIDIPILRRGINPLKDLKALFKLYKLLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 84 SGNFDVVLSFCDATNWLTLLATRGLGVPVVV-------SERSDPKHQSLGRARefLRRQLYPKAYRVVCLSD---DVAVT 153
Cdd:cd03808 79 KEKPDIVHCHTPKPGILGRLAARLAGVPKVIytvhglgFVFTEGKLLRLLYLL--LEKLALLFTDKVIFVNEddrDLAIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 154 LQSQTRCHTLVIPSAIEVPKEFRTRLKPIteRQSDPgqakcHLVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHGEG 233
Cdd:cd03808 157 KGIIKKKKTVLIPGSGVDLDRFQYSPESL--PSEKV-----VFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 234 SQRDHLESLASKLNLASRVKFPGWTRPIWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGAvREIIDHGRNG 313
Cdd:cd03808 230 ELENPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGC-RELVIDGVNG 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 32444551 314 WLVTNDDAALRAGLLHCL-TSTELRERFAAQAGE-VTDRYGWPAMVDAYE 361
Cdd:cd03808 309 FLVPPGDVEALADAIEKLiEDPELRKEMGEAARKrVEEKFDEEKVVNKLL 358
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
8-346 |
2.12e-45 |
|
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: 159.06 E-value: 2.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 8 VIHSLDGGGAERVMAGLASRLADREHSVTLITLDDgkhdrhevdPRVSRLSIDVLSTPGNTVSLWSRTL---RLRSTIAS 84
Cdd:cd03819 4 LTPALEIGGAETYILDLARALAERGHRVLVVTAGG---------PLLPRLRQIGIGLPGLKVPLLRALLgnvRLARLIRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 85 GNFDVVLSFCDATNWLTLLATRGLGVPVVVSersdpKHQSLGRAREFLRRQLYPKAY--RVVCLSDDVAVTLQ-----SQ 157
Cdd:cd03819 75 ERIDLIHAHSRAPAWLGWLASRLTGVPLVTT-----VHGSYLATYHPKDFALAVRARgdRVIAVSELVRDHLIealgvDP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 158 TRCHtlVIPSAIEvPKEFRTRLKPITERQSDPGQAKCHLVAVGRLEREKGFDRLIRSLGDLpDDAPDWELTIHGEGSQRD 237
Cdd:cd03819 150 ERIR--VIPNGVD-TDRFPPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAGDGPERD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 238 HLESLASKLNLASRVKFPGWTRPIWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGAvREIIDHGRNGWLVT 317
Cdd:cd03819 226 EIRRLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGA-REIVVHGRTGLLVP 304
|
330 340 350
....*....|....*....|....*....|
gi 32444551 318 -NDDAALRAGLLHCLTSTELRERFAAQAGE 346
Cdd:cd03819 305 pGDAEALADAIRAAKLLPEAREKLQAAAAL 334
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
24-362 |
2.76e-41 |
|
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: 148.97 E-value: 2.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 24 LASRLADREHSVTLITLDDGKHDRhEVDPRVSRLSIDVLSTPGNTVSLWSRTLRLRSTIASGNFDVVLSFCD-ATNWLTL 102
Cdd:cd03817 23 LARALEKRGHEVYVITPSDPGAED-EEEVVRYRSFSIPIRKYHRQHIPFPFKKAVIDRIKELGPDIIHTHTPfSLGKLGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 103 LATRGLGVPVVVS----------ERSDPKHQSLGRAREFLRRqLYPKAYRVVCLSDDVAVTLQS---QTRCHtlVIPSAI 169
Cdd:cd03817 102 RIARKLKIPIVHTyhtmyedylhYIPKGKLLVKAVVRKLVRR-FYNHTDAVIAPSEKIKDTLREygvKGPIE--VIPNGI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 170 EvPKEFRTRLKPITERQSDPGQAKCHLVAVGRLEREKGFDRLIRSLGDLPDdAPDWELTIHGEGSQRDHLESLASKLNLA 249
Cdd:cd03817 179 D-LDKFEKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKK-EPNIKLVIVGDGPEREELKELARELGLA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 250 SRVKFPGWTRP--IWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGaVREIIDHGRNGWLVTNDDAALRAGL 327
Cdd:cd03817 257 DKVIFTGFVPReeLPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPA-ASELVEDGENGFLFEPNDETLAEKL 335
|
330 340 350
....*....|....*....|....*....|....*
gi 32444551 328 LHCLTSTELRERFAAQAGEVTDRYGWPAMVDAYEA 362
Cdd:cd03817 336 LHLRENLELLRKLSKNAEISAREFAFAKSVEKLYE 370
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
196-344 |
5.68e-41 |
|
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: 141.64 E-value: 5.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 196 LVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHGEGSQRDHLESLASKLNLASRVKFPG--WTRPIWPVYQSADCFVL 273
Cdd:pfam00534 5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGfvSDEDLPELLKIADVFVL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32444551 274 PSRYEGFPSALLEAMACSTAVLTVDAGGaVREIIDHGRNGWLV-TNDDAALRAGLLHCLTSTELRERFAAQA 344
Cdd:pfam00534 85 PSRYEGFGIVLLEAMACGLPVIASDVGG-PPEVVKDGETGFLVkPNNAEALAEAIDKLLEDEELRERLGENA 155
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
28-367 |
6.38e-40 |
|
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: 145.22 E-value: 6.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 28 LADREHSVTLITLDDGKH------DRHEVDPRVSRLSIDVLSTPGNTVSLW----SRTLRLRSTIASGNFDVVL-SFCDA 96
Cdd:cd03798 27 LSRRGVDVEVLAPAPWGPaaarllRKLLGEAVPPRDGRRLLPLKPRLRLLAplraPSLAKLLKRRRRGPPDLIHaHFAYP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 97 TNWLTLLATRGLGVPVVVSE-RSDPKHQSLGRAREFLRRQLYPKAYRVVCLSDDVAVTLQSQT--RCHTLVIPSAIevpk 173
Cdd:cd03798 107 AGFAAALLARLYGVPYVVTEhGSDINVFPPRSLLRKLLRWALRRAARVIAVSKALAEELVALGvpRDRVDVIPNGV---- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 174 eFRTRLKPITERQSDPGQAKChLVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHGEGSQRDHLESLASKLNLASRVK 253
Cdd:cd03798 183 -DPARFQPEDRGLGLPLDAFV-ILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 254 FPGWtRP---IWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGaVREIIDHGRNGWLVTNDDA-ALRAGLLH 329
Cdd:cd03798 261 FTGR-LPheqVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGG-IPEVVGDPETGLLVPPGDAdALAAALRR 338
|
330 340 350
....*....|....*....|....*....|....*...
gi 32444551 330 CLTSTELRERFAAQAGEVTDRYGWPAMVDAYEACLQDA 367
Cdd:cd03798 339 ALAEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
4-361 |
1.09e-38 |
|
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: 142.12 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 4 KIACVIHSLDG--GGAERVMAGLASRLADREHSVTLITLDDGkhDRHEVDPRVSRLSIDVLST-------PGNTVSLWSR 74
Cdd:cd03821 1 KILHVTPSISPkaGGPVKVVLRLAAALAALGHEVTIVSTGDG--YESLVVEENGRYIPPQDGFasipllrQGAGRTDFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 75 TLRLRSTIASGNFDVV--------LSFCDATnwltllATRGLGVPVVVSERSDPKHQSLGRARE--------FLRRQLYP 138
Cdd:cd03821 79 GLPNWLRRNLREYDVVhihgvwtyTSLAACK------LARRRGIPYVVSPHGMLDPWALQQKHWkkrialhlIERRNLNN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 139 KAYRVVCLSDDVAVTLQSQTRCHTLVIPSAIEVPkEFRTRLKPIteRQSDPGQAKCHLVAVGRLEREKGFDRLIRSLGDL 218
Cdd:cd03821 153 AALVHFTSEQEADELRRFGLEPPIAVIPNGVDIP-EFDPGLRDR--RKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 219 PDDAPDWELTIHGEGSQ-RDHLESLASKLNLASRVKFPGWTRP--IWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVL 295
Cdd:cd03821 230 AEQGRDWHLVIAGPDDGaYPAFLQLQSSLGLGDRVTFTGPLYGeaKWALYASADLFVLPSYSENFGNVVAEALACGLPVV 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32444551 296 TVDAGGaVREIIDHGrNGWLVTNDDAALRAGLLHCLTSTELRERFAAQAGEVTD---RYGWPAMVDAYE 361
Cdd:cd03821 310 ITDKCG-LSELVEAG-CGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRARQveeNFSWEAVAGQLG 376
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
196-332 |
5.49e-34 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 122.62 E-value: 5.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 196 LVAVGRL-EREKGFDRLIRSLGDLPDDAPDWELTIHGEGSQRdHLESLASklNLASRVKFPGWTRPIWPVYQSADCFVLP 274
Cdd:pfam13692 4 ILFVGRLhPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEE-ELEELAA--GLEDRVIFTGFVEDLAELLAAADVFVLP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 32444551 275 SRYEGFPSALLEAMACSTAVLTVDAGGaVREIIdHGRNGWLVTNDDA-ALRAGLLHCLT 332
Cdd:pfam13692 81 SLYEGFGLKLLEAMAAGLPVVATDVGG-IPELV-DGENGLLVPPGDPeALAEAILRLLE 137
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
5-362 |
2.33e-32 |
|
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.
Pssm-ID: 132132 [Multi-domain] Cd Length: 374 Bit Score: 124.84 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 5 IACVIHSLDGGGAERVMAGLASRL-ADR-EHSVTLITlDDGKHDRHEVDPRVSRLSIDvlSTPGNTVSLWSRTLRLRSTI 82
Cdd:TIGR03088 4 IVHVVYRFDVGGLENGLVNLINHLpADRyRHAVVALT-EVSAFRKRIQRPDVAFYALH--KQPGKDVAVYPQLYRLLRQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 83 ASgnfDVVLSfCDATNWLTLLATRGLGVPVVV-SERSDPKHQSLGRAR--EFLRRQLYPKAYRVVCLSDDVAVTLQ---- 155
Cdd:TIGR03088 81 RP---DIVHT-RNLAALEAQLPAALAGVPARIhGEHGRDVFDLDGSNWkyRWLRRLYRPLIHHYVAVSRDLEDWLRgpvk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 156 -SQTRCHTlvIPSAIEvPKEFRTRLKPITERQSDPGQAKCHLVA--VGRLEREKGFDRLIRSLGDL----PDDAPDWELT 228
Cdd:TIGR03088 157 vPPAKIHQ--IYNGVD-TERFHPSRGDRSPILPPDFFADESVVVgtVGRLQAVKDQPTLVRAFALLvrqlPEGAERLRLV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 229 IHGEGSQRDHLESLASKLNLASRVKFPGWTRPIWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGAVrEIID 308
Cdd:TIGR03088 234 IVGDGPARGACEQMVRAAGLAHLVWLPGERDDVPALMQALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNP-ELVQ 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 32444551 309 HGRNGWLVTNDDA-ALRAGLLHCLTSTELRERFAAQA-GEVTDRYGWPAMVDAYEA 362
Cdd:TIGR03088 313 HGVTGALVPPGDAvALARALQPYVSDPAARRAHGAAGrARAEQQFSINAMVAAYAG 368
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
13-362 |
2.64e-29 |
|
sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
Pssm-ID: 340830 [Multi-domain] Cd Length: 398 Bit Score: 116.96 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 13 DGGGAERVMAGLASRLADREHSVTLIT--LDDGKHDRHEVDPRVsrLSIDVLSTPGNTVS---LW----------SRTLR 77
Cdd:cd03800 19 DTGGQNVYVLELARALAELGYQVDIFTrrISPADPEVVEIAPGA--RVIRVPAGPPEYLPkeeLWpyleefadglLRFIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 78 LRStiasGNFDVVLS-FCDAtNWLTLLATRGLGVPVVVS----ERSDPKHQSLGRAREFLRR-----QLYPKAYRVVCLS 147
Cdd:cd03800 97 REG----GRYDLIHShYWDS-GLVGALLARRLGVPLVHTfhslGRVKYRHLGAQDTYHPSLRitaeeQILEAADRVIAST 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 148 DDVAV---TLQSQTRCHTLVIPSAIEvPKEFRtrlkPITERQSDP-----GQAKCHLVAVGRLEREKGFDRLIRSLGDLP 219
Cdd:cd03800 172 PQEADeliSLYGADPSRINVVPPGVD-LERFF----PVDRAEARRarlllPPDKPVVLALGRLDPRKGIDTLVRAFAQLP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 220 DDAPDWELTIHGeGSQRD-------HLESLASKLNLASRVKFPGWTRP--IWPVYQSADCFVLPSRYEGFPSALLEAMAC 290
Cdd:cd03800 247 ELRELANLVLVG-GPSDDplsmdreELAELAEELGLIDRVRFPGRVSRddLPELYRAADVFVVPSLYEPFGLTAIEAMAC 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32444551 291 STAVLTVDAGGAvREIIDHGRNGWLVT-NDDAALRAGLLHCLTSTELRERFAAQAGE-VTDRYGWPAMVDAYEA 362
Cdd:cd03800 326 GTPVVATAVGGL-QDIVRDGRTGLLVDpHDPEALAAALRRLLDDPALWQRLSRAGLErARAHYTWESVADQLLT 398
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
4-325 |
1.55e-28 |
|
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: 114.08 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 4 KIACVIHSLDGGGAERVMAGLASRLADREHSVTLITLddgkHDRHEVDPRVSRLSIDVLSTPGNTVSLWSRTLRLRSTIA 83
Cdd:cd04951 1 KILYVITGLGLGGAEKQTVLLADQMFIRGHDVNIVYL----TGEVEVKPLNNNIIIYNLGMDKNPRSLLKALLKLKKIIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 84 SGNFDVVLSFCDATNWLTLLATRGLGVPVVVSERSDPKHQslGRAREFLRRQ---LYPKAYRVVCLSDDVAVTLQSQTRC 160
Cdd:cd04951 77 AFKPDVVHSHMFHANIFARFLRMLYPIPLLICTAHNKNEG--GRIRMFIYRLtdfLCDITTNVSREALDEFIAKKAFSKN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 161 HTLVIPSAIEVPK-EFRTRLKPITERQSDPGQAKCHLVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHGEGSQRDHL 239
Cdd:cd04951 155 KSVPVYNGIDLNKfKKDINVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPLRNEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 240 ESLASKLNLASRVKFPGWTRPIWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGaVREIIDHGRngWLVTND 319
Cdd:cd04951 235 ERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGG-VAEVVGDHN--YVVPVS 311
|
....*.
gi 32444551 320 DAALRA 325
Cdd:cd04951 312 DPQLLA 317
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
265-369 |
4.05e-27 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 103.92 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 265 YQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGaVREIIDHGRNGWLVTNDDA-ALRAGLLHCLTSTELRERFAAQ 343
Cdd:COG0438 18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGG-LPEVIEDGETGLLVPPGDPeALAEAILRLLEDPELRRRLGEA 96
|
90 100
....*....|....*....|....*..
gi 32444551 344 AGE-VTDRYGWPAMVDAYEACLQDACK 369
Cdd:COG0438 97 ARErAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
4-344 |
2.92e-26 |
|
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: 107.80 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 4 KIACVIHSLD---GGGAERVMAGLASRLADREHSVTLITLDDG----KHDRHEVDPRVSRLSIDVLSTPGNTVSLWSRTL 76
Cdd:cd03823 1 KILLVNSLYPpqrVGGAEISVHDLAEALVAEGHEVAVLTAGVGppgqATVARSVVRYRRAPDETLPLALKRRGYELFETY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 77 R------LRSTIASGNFDVVLSFCDATNWLTLL-ATRGLGVPVVVSERSDPkhqsLGRAREFLRRqlyPKAYRVVCLSDD 149
Cdd:cd03823 81 NpglrrlLARLLEDFRPDVVHTHNLSGLGASLLdAARDLGIPVVHTLHDYW----LLCPRQFLFK---KGGDAVLAPSRF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 150 VAVTLQ----SQTRCHtlVIPSAIEVPKEFRTRLKPITERqsdpgqakchLVA--VGRLEREKGFDRLIRSLGDLPddAP 223
Cdd:cd03823 154 TANLHEanglFSARIS--VIPNAVEPDLAPPPRRRPGTER----------LRFgyIGRLTEEKGIDLLVEAFKRLP--RE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 224 DWELTIHGEGSQRDhleslASKLNLASRVKFPGW--TRPIWPVYQSADCFVLPSR-YEGFPSALLEAMACSTAVLTVDAG 300
Cdd:cd03823 220 DIELVIAGHGPLSD-----ERQIEGGRRIAFLGRvpTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLG 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 32444551 301 GAVrEIIDHGRNGWLVT-NDDAALRAGLLHCLTSTELRERFAAQA 344
Cdd:cd03823 295 GIA-ELIQPGVNGLLFApGDAEDLAAAMRRLLTDPALLERLRAGA 338
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
13-358 |
3.93e-26 |
|
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: 107.38 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 13 DGGGAERVMAGLASRLADREHSVTLITLDDGKHDRHEVDPRVSRLSIDVLSTPGNTVSLwSRTLRLRSTIASGNFDVV-L 91
Cdd:cd03814 12 QVNGVVRTLERLVDHLRRRGHEVRVVAPGPFDEAESAEGRVVSVPSFPLPFYPEYRLAL-PLPRRVRRLIKEFQPDIIhI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 92 SFCDATNWLTLLATRGLGVPVVVS------ERSDPKHQSLGRAR--EFLRRqLYPKAYRVVCLSDDVAVTLQSQTRCHTL 163
Cdd:cd03814 91 ATPGPLGLAALRAARRLGLPVVTSyhtdfpEYLSYYTLGPLSWLawAYLRW-FHNPFDTTLVPSPSIARELEGHGFERVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 164 VIPSAIEVpKEFRTRLKPITERQSDPGQAKCHLVAVGRLEREKGFDRLIRSLGDLPDDAPdWELTIHGEGSQRdhlESLA 243
Cdd:cd03814 170 LWPRGVDT-ELFHPSRRDAALRRRLGPPGRPLLLYVGRLAPEKNLEALLDADLPLAASPP-VRLVVVGDGPAR---AELE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 244 SKLnlaSRVKFPGWTRP--IWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGAvREIIDHGRNGWLVTNDDA 321
Cdd:cd03814 245 ARG---PDVIFTGFLTGeeLARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGP-RDIVRPGGTGALVEPGDA 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 32444551 322 ALRAGLLHCLT-STELRERFAAQAGEVTDRYGWPAMVD 358
Cdd:cd03814 321 AAFAAALRALLeDPELRRRMAARARAEAERYSWEAFLD 358
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
5-361 |
6.54e-26 |
|
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: 107.43 E-value: 6.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 5 IACVIHSLDGGGAERVMAGLASRLADREHSVTLIT----------LDDGKHDRHEVDP-RVSRLSIDVLSTPGNTVSLWS 73
Cdd:cd03794 4 LISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTpspnyplgriFAGATETKDGIRViRVKLGPIKKNGLIRRLLNYLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 74 --RTLRLRSTIASGNFDVVL--SFCDATNWLTLLATRGLGVPVVVsERSDP-----------KHQSLGRAREFLRRQLYP 138
Cdd:cd03794 84 faLAALLKLLVREERPDVIIaySPPITLGLAALLLKKLRGAPFIL-DVRDLwpeslialgvlKKGSLLKLLKKLERKLYR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 139 KAYRVVCLSDDVA--VTLQSQTRCHTLVIPSAIEVpkEFRTRLKPITERQSDPGQAKCHLVAVGRLEREKGFDRLIRSLG 216
Cdd:cd03794 163 LADAIIVLSPGLKeyLLRKGVPKEKIIVIPNWADL--EEFKPPPKDELRKKLGLDDKFVVVYAGNIGKAQGLETLLEAAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 217 DLPDDaPDWELTIHGEGSQRDHLESLASKLNLaSRVKFPGWTRP--IWPVYQSADCFVLP-----SRYEGFPSALLEAMA 289
Cdd:cd03794 241 RLKRR-PDIRFLFVGDGDEKERLKELAKARGL-DNVTFLGRVPKeeVPELLSAADVGLVPlkdnpANRGSSPSKLFEYMA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32444551 290 CSTAVLTVDAGGAVREIIDhGRNGWLVTNDD-AALRAGLLHCLTSTELRERFAAQAGEVTD-RYGWPAMVDAYE 361
Cdd:cd03794 319 AGKPILASDDGGSDLAVEI-NGCGLVVEPGDpEALADAILELLDDPELRRAMGENGRELAEeKFSREKLADRLL 391
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
5-316 |
8.40e-26 |
|
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: 104.02 E-value: 8.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 5 IACVIHSLD--GGGAERVMAGLASRLADREHSVTLITLddgkhdrhevdprvsrlsidvlstpgntvsLWSRTLRLRSTI 82
Cdd:cd01635 1 ILLVTGEYPplRGGLELHVRALARALAALGHEVTVLAL------------------------------LLLALRRILKKL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 83 ASGNFDVVLS-FCDATNWLTLLATRGLGVPVVVsersdpkhqslgrareflrrqlypkayrvvclsddvavtlqsqtRCH 161
Cdd:cd01635 51 LELKPDVVHAhSPHAAALAALLAARLLGIPIVV--------------------------------------------TVH 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 162 TLVIPSAIEVPKEFRTRLKPITErqsdpgqaKCHLVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHGEGSQRDHLES 241
Cdd:cd01635 87 GPDSLESTRSELLALARLLVSLP--------LADKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEA 158
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32444551 242 LASKLNLASRVKFPGWTRP---IWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGaVREIIDHGRNGWLV 316
Cdd:cd01635 159 LAAALGLLERVVIIGGLVDdevLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGG-IPEFVVDGENGLLV 235
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
4-362 |
1.96e-25 |
|
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: 105.52 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 4 KIACVIHSLDG--GGAERVMAGLASRLADREHSVTLITLDDGKHDRHEVDPRVSRLSIDVLSTPGNTVSLWSRTLRLRST 81
Cdd:cd03809 1 KILIDGRSLAQrlTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 82 IAsGNFDVVLSFCDatnwltLLATRGLGVPVVV-----SERSDPKHQSLGRA---REFLRRQLyPKAYRVVCLSDDVAVT 153
Cdd:cd03809 81 KK-DKPDLLHSPHN------TAPLLLKGCPQVVtihdlIPLRYPEFFPKRFRlyyRLLLPISL-RRADAIITVSEATRDD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 154 LQSQTRC---HTLVIPSAIEVPKEFRTRLKPITERQSDPGQakcHLVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIH 230
Cdd:cd03809 153 IIKFYGVppeKIVVIPLGVDPSFFPPESAAVLIAKYLLPEP---YFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 231 GE-GSQRDHLESLASKLNLASRVKFPGW--TRPIWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDaGGAVREII 307
Cdd:cd03809 230 GGkGWEDEELLDLVKKLGLGGRVRFLGYvsDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASN-ISVLPEVA 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 32444551 308 dhGRNGWLVTNDDA-ALRAGLLHCLTSTELRERFAAQAGEVTDRYGWPAMVDAYEA 362
Cdd:cd03809 309 --GDAALYFDPLDPeSIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
4-298 |
1.28e-23 |
|
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: 100.44 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 4 KIACVIHSLDGGGAERVMAGLASRLADREHSVTLITLDDGKHDRHEvdpRVSRLSIDVLSTPGNTVSLWSRTLRLRSTIA 83
Cdd:cd03812 1 KILHIVGGMNVGGIETFLMNLYRKLDKSKIEFDFLATSDDKGEYDE---ELEELGGKIFYIPPKKKNIIKYFIKLLKLIK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 84 SGNFDVVLSFCDATNWLTLLATRGLGVPVVV--SERSDPKHQSLGRAREFLRRQLYPKAYRVVC-LSDDVAVTLQSQTRC 160
Cdd:cd03812 78 KEKYDIVHVHGSSSNGIILLLAAKAGVPVRIahSHNTKDSSIKLRKIRKNVLKKLIERLSTKYLaCSEDAGEWLFGEVEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 161 HT-LVIPSAIEV-----PKEFRTRLKpiTERQSDPGQAKCHlvaVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHGEGS 234
Cdd:cd03812 158 GKfKVIPNGIDIekykfNKEKRRKRR--KLLILEDKLVLGH---VGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32444551 235 QRDHLESLASKLNLASRVKFPGWTRPIWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVD 298
Cdd:cd03812 233 LKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSD 296
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
153-344 |
1.85e-23 |
|
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: 100.10 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 153 TLQSQTRCHtlVIPSAIEVPkEFRTRLKPITERQSD-PGQAKCHL-VAVGRLEREKGFDRLIRSLGDLPDDaPDWELTIH 230
Cdd:cd03825 156 PLLKGLPVV--VIPNGIDTE-IFAPVDKAKARKRLGiPQDKKVILfGAESVTKPRKGFDELIEALKLLATK-DDLLLVVF 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 231 GEGSQRD--------HLESLASKLNLASrvkfpgwtrpiwpVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGa 302
Cdd:cd03825 232 GKNDPQIvilpfdiiSLGYIDDDEQLVD-------------IYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGG- 297
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 32444551 303 VREIIDHGRNGWLVTNDDA-ALRAGLLHCLTSTELRERFAAQA 344
Cdd:cd03825 298 SPEIVQHGVTGYLVPPGDVqALAEAIEWLLANPKERESLGERA 340
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
15-344 |
2.85e-23 |
|
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: 99.27 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 15 GGAERVMAGLASRLADREHSVTLITLDDGKHDRHEV--DPRVSR--LSIDVLSTPGN-TVSLWSRTLRLRSTIASGNF-- 87
Cdd:cd03795 14 GGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEenGIRIHRvkSFLNVASTPFSpSYIKRFKKLAKEYDIIHYHFpn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 88 ---DVVLSFCDATNwltllatrglgvPVVVSERSD-PKHQSLGRA-REFLRRQLYpKAYRVVCLSDDVAVTlqSQT---- 158
Cdd:cd03795 94 plaDLLLFFSGAKK------------PVVVHWHSDiVKQKKLLKLyKPLMTRFLR-RADRIIATSPNYVET--SPTlref 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 159 RCHTLVIPSAIE-----VPKEFRTRLKPITERQSDpgqakchLVAVGRLEREKGFDRLIRSLGDLpddapDWELTIHGEG 233
Cdd:cd03795 159 KNKVRVIPLGIDknvynIPRVDFENIKREKKGKKI-------FLFIGRLVYYKGLDYLIEAAQYL-----NYPIVIGGEG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 234 SQRDHLESLAsKLNLASRVKFPGWT----RPIWpvYQSADCFVLPS--RYEGFPSALLEAMACSTAVLTVDAGGAVREII 307
Cdd:cd03795 227 PLKPDLEAQI-ELNLLDNVKFLGRVddeeKVIY--LHLCDVFVFPSvlRSEAFGIVLLEAMMCGKPVISTNIGTGVPYVN 303
|
330 340 350
....*....|....*....|....*....|....*...
gi 32444551 308 DHGRNGWLVTNDDA-ALRAGLLHCLTSTELRERFAAQA 344
Cdd:cd03795 304 NNGETGLVVPPKDPdALAEAIDKLLSDEELRESYGENA 341
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
164-367 |
1.34e-21 |
|
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: 94.73 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 164 VIPSAIEVpKEFRTRLKPITERQ--SDPGQAKchLVAVGRLEREKGFDRLIRSLGDLPDDAPDwELTIHGEGSQRDHLES 241
Cdd:cd04962 168 VIHNFIDE-DVFKRKPAGALKRRllAPPDEKV--VIHVSNFRPVKRIDDVVRVFARVRRKIPA-KLLLVGDGPERVPAEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 242 LASKLNLASRVKFPGWTRPIWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGaVREIIDHGRNGWLVTNDDA 321
Cdd:cd04962 244 LARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGG-IPEVVKHGETGFLSDVGDV 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 32444551 322 -ALRAGLLHCLTSTELRERFAAQAGE-VTDRYGWPAMVDAYEACLQDA 367
Cdd:cd04962 323 dAMAKSALSILEDDELYNRMGRAARKrAAERFDPERIVPQYEAYYRRL 370
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
179-351 |
3.29e-20 |
|
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: 90.05 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 179 LKPITERQSDPGQAKCHLVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHGEGSQRDHLESLASKLNLASRVKFPGWT 258
Cdd:cd04949 146 VDQLDTAESNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYH 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 259 RPIWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGAVREIIDHGRNGWLVTNDDA-ALRAGLLHCLTSTELR 337
Cdd:cd04949 226 SNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKYGPSELIEDGENGYLIEKNNIdALADKIIELLNDPEKL 305
|
170
....*....|....
gi 32444551 338 ERFAAQAGEVTDRY 351
Cdd:cd04949 306 QQFSEESYKIAEKY 319
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
14-365 |
2.57e-19 |
|
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: 87.73 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 14 GGGAERVMAGLASRLADREHSVTLITLDDGKHDR--HEVDPRVSRlsidvLSTPGNTVSLWSRTLRLRSTIASGNFDVVL 91
Cdd:cd03802 17 YGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSAplVAVIPRALR-----LDPIPQESKLAELLEALEVQLRASDFDVIH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 92 SFCDatnWLTLLATRGLGVPVVVSersdpKHQSLgRAREFLRRQLYPKAyRVVCLSDDvavtlqsqTRCHTLVIPSAIEV 171
Cdd:cd03802 92 NHSY---DWLPPFAPLIGTPFVTT-----LHGPS-IPPSLAIYAAEPPV-NYVSISDA--------QRAATPPIDYLTVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 172 PKEFRtrlkPITERQSDPGQAkcHLVAVGRLEREKGFDRLI---RSLGdlpddapdWELTIHGEGSQRDHLESLaSKLNL 248
Cdd:cd03802 154 HNGLD----PADYRFQPDPED--YLAFLGRIAPEKGLEDAIrvaRRAG--------LPLKIAGKVRDEDYFYYL-QEPLP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 249 ASRVKFPGwtrPIWP-----VYQSADCFVLPSRY-EGFPSALLEAMACSTAVLTVdAGGAVREIIDHGRNGWLVTNDDAA 322
Cdd:cd03802 219 GPRIEFIG---EVGHdekqeLLGGARALLFPINWdEPFGLVMIEAMACGTPVIAY-RRGGLPEVIQHGETGFLVDSVEEM 294
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 32444551 323 LRAgllhCLTSTELRERFAAQAGEvtDRYGWPAMVDAYEACLQ 365
Cdd:cd03802 295 AEA----IANIDRIDRAACRRYAE--DRFSAARMADRYEALYR 331
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
176-359 |
2.87e-17 |
|
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: 82.11 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 176 RTRLKPITerqsDPGQAKCHLVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHGEGSQRDHLESLASKLNLASRVKFP 255
Cdd:cd03799 161 KFRFKPRY----LPLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 256 GWTR--PIWPVYQSADCFVLPS------RYEGFPSALLEAMACSTAVLTVDAGGaVREIIDHGRNGWLVTNDDA-ALRAG 326
Cdd:cd03799 237 GWKPqeEIIEILDEADIFIAPSvtaadgDQDGPPNTLKEAMAMGLPVISTEHGG-IPELVEDGVSGFLVPERDAeAIAEK 315
|
170 180 190
....*....|....*....|....*....|...
gi 32444551 327 LLHCLTSTELrerfaaqagevtdrygWPAMVDA 359
Cdd:cd03799 316 LTYLIEHPAI----------------WPEMGKA 332
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
172-317 |
3.55e-17 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 81.68 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 172 PKEFRTRLKPITERQSdpgqaKCHLVAVGRL--EREKGFDRLIRSLGDLpddAPDWELTIHGEGSQRDHLESLASKLNLA 249
Cdd:PRK09922 164 PVEIKTIIIPPPERDK-----PAVFLYVGRLkfEGQKNVKELFDGLSQT---TGEWQLHIIGDGSDFEKCKAYSRELGIE 235
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32444551 250 SRVKFPGWTRPIWPVYQ----SADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGAVREIIDHGRNGWLVT 317
Cdd:PRK09922 236 QRIIWHGWQSQPWEVVQqkikNVSALLLTSKFEGFPMTLLEAMSYGIPCISSDCMSGPRDIIKPGLNGELYT 307
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
15-151 |
4.55e-16 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 74.74 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 15 GGAERVMAGLASRLADREHSVTLITLDDGKHDRHEVDPRVSRLSIDVLSTPGnTVSLWSRTLRLRSTIASGNFDVVLSFC 94
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPVPPRPS-PLADLAALRRLRRLLRAERPDVVHAHS 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 95 DATNWLTLLATRGLGVPVVVSERS---DPKHQSLGRAREFLRRQLYPKAYRVVCLSDDVA 151
Cdd:pfam13579 80 PTAGLAARLARRRRGVPLVVTVHGlalDYGSGWKRRLARALERRLLRRADAVVVVSEAEA 139
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
106-346 |
1.33e-15 |
|
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: 77.11 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 106 RGLGVPVVV----SERSDPKHQSLGRAREF-----LRRQLYPKAYRVVCLSDDV-----AVTLQSQtRCHtlVIPSAIEV 171
Cdd:cd05844 101 RALGVPLVVtfhgFDITTSRAWLAASPGWPsqfqrHRRALQRPAALFVAVSGFIrdrllARGLPAE-RIH--VHYIGIDP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 172 pkefrTRLKPITERQSDPgqakcHLVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHGEGSQRDHLESLASKLnlaSR 251
Cdd:cd05844 178 -----AKFAPRDPAERAP-----TILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAAL---GR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 252 VKFPGW-TRP-IWPVYQSADCFVLPSRY------EGFPSALLEAMACSTAVLTVDAGGaVREIIDHGRNGWLVTNDD-AA 322
Cdd:cd05844 245 VRFLGAlPHAeVQDWMRRAEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGG-IPEAILDGETGFLVPEGDvDA 323
|
250 260
....*....|....*....|....
gi 32444551 323 LRAGLLHCLTSTELRERFAAQAGE 346
Cdd:cd05844 324 LADALQALLADRALADRMGGAARA 347
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
8-355 |
1.67e-15 |
|
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274943 [Multi-domain] Cd Length: 373 Bit Score: 77.05 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 8 VIHSLDgggaervmagLASRLADREHSVTLITLDDGKHDRhEVDPRVSRLSIDVLSTPGNTVSL-WSRTLRLRSTIASG- 85
Cdd:TIGR04047 15 VVHTLE----------LAEALTALGHDVTVWALAADGFGF-FRDPPCAVRLVPVAPAPGDTDAMvEQRIARSIDHLRAHf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 86 --NFDVVLSF-CDATNWLTLLATRGLGVPVV-----VSERSDPKHQSLGRaREFLRrqlypkAYRVVCLSDDVAVTLQSQ 157
Cdd:TIGR04047 84 arGFDVVHAQdCISGNALATLRAEGLIPGFVrtvhhLDDFDDPRLAACQE-RAIVE------ADAVLCVSAAWAAELRAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 158 TRCHTLVIPSAIEVpkefrTRLKPITERQsdPGQAKCHL--------VAVGRLEREKGFDRLIRSLGDLPDDAPDWELTI 229
Cdd:TIGR04047 157 WGIDATVVPNGVDA-----ARFSPAADAA--DAALRRRLglrggpyvLAVGGIEPRKNTIDLLEAFALLRARRPQAQLVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 230 HGEGSQRDH------LESLASKLNLAsrvkfPGWTRPIWPV--------YQSADCFVLPSRYEGFPSALLEAMACSTAVL 295
Cdd:TIGR04047 230 AGGATLFDYdayrreFRARAAELGVD-----PGPVVITGPVpdadlpalYRCADAFAFPSLKEGFGLVVLEALASGIPVV 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 296 TVDAgGAVREIIDHGRNGWLVTNDDAALRAGLLHCLtSTELRERFAAQAGEVTDRYGWPA 355
Cdd:TIGR04047 305 ASDI-APFTEYLGRFDAAWADPSDPDSIADALALAL-DPARRPALRAAGPELAARYTWDA 362
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
130-360 |
7.39e-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: 75.45 E-value: 7.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 130 EFLRRQLYPKAYRVVCLSDDvavTLQSQTRC-----HTLVIPSAIEVpkefrTRLKPITERQSDPgqAKCHLVAVGRLER 204
Cdd:cd03813 235 ERLGKLAYQQADKIISLYEG---NRRRQIRLgadpdKTRVIPNGIDI-----QRFAPAREERPEK--EPPVVGLVGRVVP 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 205 EKGFDRLIRSLGDLPDDAPDWELTIHGeGSQRD-----HLESLASKLNLASRVKFPGWTRpIWPVYQSADCFVLPSRYEG 279
Cdd:cd03813 305 IKDVKTFIRAFKLVRRAMPDAEGWLIG-PEDEDpeyaqECKRLVASLGLENKVKFLGFQN-IKEYYPKLGLLVLTSISEG 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 280 FPSALLEAMACSTAVLTVDAgGAVREII-----DHGRNGWLVTNDDA-ALRAGLLHCLTSTELRERFAAQAGE-VTDRYG 352
Cdd:cd03813 383 QPLVILEAMASGVPVVATDV-GSCRELIygaddALGQAGLVVPPADPeALAEALIKLLRDPELRQAFGEAGRKrVEKYYT 461
|
....*...
gi 32444551 353 WPAMVDAY 360
Cdd:cd03813 462 LEGMIDSY 469
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
196-355 |
8.42e-15 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 75.52 E-value: 8.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 196 LVAVGRLEREKGFDRLIRSLGDLPDDapdwELTIHGEGSQRDHLESLASKLNlasrVKFPGWTR--PIWPVYQSADCFVL 273
Cdd:PLN02871 266 IVYVGRLGAEKNLDFLKRVMERLPGA----RLAFVGDGPYREELEKMFAGTP----TVFTGMLQgdELSQAYASGDVFVM 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 274 PSRYEGFPSALLEAMACSTAVLTVDAGGaVREII---DHGRNGWLVTNDDAALRAGLLHCL-TSTELRERFAAQAGEVTD 349
Cdd:PLN02871 338 PSESETLGFVVLEAMASGVPVVAARAGG-IPDIIppdQEGKTGFLYTPGDVDDCVEKLETLlADPELRERMGAAAREEVE 416
|
....*.
gi 32444551 350 RYGWPA 355
Cdd:PLN02871 417 KWDWRA 422
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
15-171 |
1.86e-14 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 70.64 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 15 GGAERVMAGLASRLADREHSVTLITLDDGKHDRHEVDPRVSRLSIDVLSTPGNTVSLWSRtLRLRSTIASGNFDVVLSFC 94
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFL-RRLRRLLRRERPDVVHAHS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 95 DATNWLTLLATR-GLGVPVVVS--------ERSDPKHQSLGRAREFLRRQLYPKAYRVVCLSDDVAVTLQSQ---TRCHT 162
Cdd:pfam13439 80 PFPLGLAALAARlRLGIPLVVTyhglfpdyKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLygvPPEKI 159
|
....*....
gi 32444551 163 LVIPSAIEV 171
Cdd:pfam13439 160 RVIPNGVDL 168
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
199-344 |
4.27e-11 |
|
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: 63.92 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 199 VGR-LEREKGFDRLIRSLGDLPDDAPDWELTIHGE------------GSQRDH-LESLASKLnlaSRVKFPGwTRP---I 261
Cdd:cd03818 219 VARnLEPYRGFHVFMRALPRIQARRPDARVVVVGGdgvsygspppdgGSWKQKmLAELGVDL---ERVHFVG-KVPydqY 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 262 WPVYQSADCFVLPSrYEGFPS-ALLEAMACSTAVLTVDAGGaVREIIDHGRNGWLVTNDDA-ALRAGLLHCLTSTELRER 339
Cdd:cd03818 295 VRLLQLSDAHVYLT-YPFVLSwSLLEAMACGCPVIGSDTAP-VREVIRDGRNGLLVDFFDPdALAAAVLELLEDPDRAAA 372
|
....*
gi 32444551 340 FAAQA 344
Cdd:cd03818 373 LRRAA 377
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
75-365 |
1.28e-10 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 62.74 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 75 TLRLRSTIASGNFDVVLSFCDATNWLTLLATRGLGVP-VVVSERSDPKHQSLGRAREflrrqLYPKAYRVVCLSDDVAVT 153
Cdd:PRK15179 389 TTKLTDVMRSSVPSVVHIWQDGSIFACALAALLAGVPrIVLSVRTMPPVDRPDRYRV-----EYDIIYSELLKMRGVALS 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 154 LQSQ--------------TRCHTL---VIPSAIEVPKEFRTRLKPITERQSDpgqAKCHLVAVGRLEREKGFDRLIRSLG 216
Cdd:PRK15179 464 SNSQfaahryadwlgvdeRRIPVVyngLAPLKSVQDDACTAMMAQFDARTSD---ARFTVGTVMRVDDNKRPFLWVEAAQ 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 217 DLPDDAPDWELTIHGEGSQRDHLESLASKLNLASRVKFPGWTRPIWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLT 296
Cdd:PRK15179 541 RFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVT 620
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32444551 297 VDAGGAvREIIDHGRNGWLVTNDDA-------ALRAGLLHCLTSTELRERFAAQAgevTDRYGWPAMVDAYEACLQ 365
Cdd:PRK15179 621 TLAGGA-GEAVQEGVTGLTLPADTVtapdvaeALARIHDMCAADPGIARKAADWA---SARFSLNQMIASTVRCYQ 692
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
197-315 |
2.67e-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: 61.15 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 197 VAVGRLEREKGFDRLIRSLGDLPDdapdwELTIHGEGSQRDHLESLASKlnlasRVKFPGWTRP--IWPVYQSADCFVLP 274
Cdd:cd03804 203 LTASRLVPYKRIDLAVEAFNELPK-----RLVVIGDGPDLDRLRAMASP-----NVEFLGYQPDevLKELLSKARAFVFA 272
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 32444551 275 SRyEGFPSALLEAMACSTAVLTVDAGGAvREIIDHGRNGWL 315
Cdd:cd03804 273 AE-EDFGIVPVEAQACGTPVIAFGKGGA-LETVRPGPTGIL 311
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
132-319 |
8.56e-09 |
|
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: 56.70 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 132 LRRQLYPKAYRVVCLSDDVAVTLQSQtrchtlvIPSAIEvpKEFRTRLK-PITERQSDPG-QAKCHLVAVGRLEREKGFD 209
Cdd:cd04946 170 LREYLVSYLDAVFLISKEGKDYLQKC-------YPAYKE--KIFVSRLGvSDKEQYSKVKkEGDLRLVSCSSIVPVKRID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 210 RLIRSLGDLPDDAPD--WELTIHGEGSQRDHLESLASKLNLASRVKFPGW--TRPIWPVYQ--SADCFVLPSRYEGFPSA 283
Cdd:cd04946 241 LIIETLNSLCVAHPSicISWTHIGGGPLKERLEKLAENKLENVKVNFTGEvsNKEVKQLYKenDVDVFVNVSESEGIPVS 320
|
170 180 190
....*....|....*....|....*....|....*.
gi 32444551 284 LLEAMACSTAVLTVDAGGaVREIIDHGRNGWLVTND 319
Cdd:cd04946 321 IMEAISFGIPVIATNVGG-TREIVENETNGLLLDKD 355
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
200-360 |
2.90e-08 |
|
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: 55.08 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 200 GRLEREKGFDRLIRSLGDLPDDAPDWELTIHGE--GSQRDH-----LESLASKLNLASRVKFPGWTRPIWPVY---QSAD 269
Cdd:cd03822 194 GFIGPGKGLEILLEALPELKAEFPDVRLVIAGElhPSLARYegeryRKAAIEELGLQDHVDFHNNFLPEEEVPryiSAAD 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 270 CFVLPSRYEGFPS--ALLEAMACSTAVLTVDAGGAvREIIDHGRNGWLVTNDDAALRAGLLHCLTSTELRERFAAQAGEV 347
Cdd:cd03822 274 VVVLPYLNTEQSSsgTLSYAIACGKPVISTPLRHA-EELLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAY 352
|
170
....*....|...
gi 32444551 348 TDRYGWPAMVDAY 360
Cdd:cd03822 353 ARAMTWESIADRY 365
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
223-321 |
7.59e-08 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 53.94 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 223 PDWELTIHGEGSQRDHLESLASKLNLASRVKFPGWTRPIWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGGA 302
Cdd:PRK15490 428 PATRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGS 507
|
90
....*....|....*....
gi 32444551 303 VREIIDhGRNGWLVtnDDA 321
Cdd:PRK15490 508 AECFIE-GVSGFIL--DDA 523
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
3-356 |
9.08e-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: 53.36 E-value: 9.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 3 MKIAcVIH-SLDGGGAERVMAGLASRLADREHSVTLIT-LDDGKHDRHEVdpRVSRLSIDVLstpGNTV--SLWSR---- 74
Cdd:cd03805 1 LRVA-FLHpDLGIGGAERLVVDAALALQSRGHEVTIYTsHHDPSHCFEET--KDGTLPVRVR---GDWLprSIFGRfhal 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 75 --TLR-LRSTIA-----SGNFDVVlsFCD---ATNWLTLLATRglgvpvvvsersdPK-----H---QSLGRAREFLRRq 135
Cdd:cd03805 75 caYLRmLYLALYlllfsGEKYDVF--IVDqvsACVPLLKLFRP-------------SKilfycHfpdQLLAQRKSLLKR- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 136 lypkAYRVVC---------LSDDVAV--------------TLQSQTR------CHTLVIPSAIEVPKEfrtrlkpiteRQ 186
Cdd:cd03805 139 ----LYRKPFdwleefttgMADQIVVnsnftagvfkktfpSLAKNPPevlypcVDTDSFDSTSEDPDP----------GD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 187 SDPGQAKCHLVAVGRLEREKGFDRLIRSLGDLPDDAPDWE---LTIHGEGSQR--------DHLESLA-SKLNLASRVKF 254
Cdd:cd03805 205 LIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQKLPEFEnvrLVIAGGYDPRvaenveylEELQRLAeELLNVEDQVLF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 255 pgwTRPI-----WPVYQSADCfVL--PSRyEGFPSALLEAMACSTAVLTVDAGGAVrEIIDHGRNGWLVTNDDAALRAGL 327
Cdd:cd03805 285 ---LRSIsdsqkEQLLSSALA-LLytPSN-EHFGIVPLEAMYAGKPVIACNSGGPL-ETVVEGVTGFLCEPTPEAFAEAM 358
|
410 420 430
....*....|....*....|....*....|
gi 32444551 328 LHCLTSTELRERFAAQAGE-VTDRYGWPAM 356
Cdd:cd03805 359 LKLANDPDLADRMGAAGRKrVKEKFSREAF 388
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
164-301 |
5.89e-07 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 51.08 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 164 VIPSAIE----VPKEFRTRLKPITerqsdpgqakchLVAVGRLEREKGFDRLIRSLGDLPDDAPDWELTIHGEGSQRDHL 239
Cdd:cd03796 172 VIPNAVDssdfTPDPSKPDPNKIT------------IVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIEL 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32444551 240 ESLASKLNLASRVKFPGWTRP--IWPVYQSADCFVLPSRYEGFPSALLEAMACSTAVLTVDAGG 301
Cdd:cd03796 240 EEMREKYQLQDRVELLGAVPHeeVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGG 303
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
262-360 |
4.34e-06 |
|
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: 48.09 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32444551 262 WPVYQSADCFVLP-SRYEGFPSALLEAMACSTAVLTVDAGGAVREIIdHGRNGWLVT-NDDAALRagLLHCLTSTELRER 339
Cdd:cd03792 273 INALQRAATVVLQlSTREGFGLTVSEALWKGKPVIATPAGGIPLQVI-DGETGFLVNsVEGAAVR--ILRLLTDPELRRK 349
|
90 100
....*....|....*....|..
gi 32444551 340 FAAQAGE-VTDRYGWPAMVDAY 360
Cdd:cd03792 350 MGLAAREhVRDNFLITGNLRAW 371
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
274-351 |
8.69e-03 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 35.27 E-value: 8.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32444551 274 PSRYEGFPSA-LLEAMACSTAVLTvDAGGAVREIIDHGRNGwLVTNDDAALRAGLLHCLTSTELRERFAAQAGEVTDRY 351
Cdd:pfam13524 5 PSRRPDSPNMrVFEAAACGAPLLT-DRTPGLEELFEPGEEI-LLYRDPEELAEKIRYLLEHPEERRAIAAAGRERVLAE 81
|
|
| |
