|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
18-338 |
9.70e-77 |
|
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: 239.91 E-value: 9.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 18 GGAEKNIYDIVLNIDRARFTPYVFCLKG-GELVDDIRRKGIDSRIIDLDKIISLEGVRKgagLYKFLKSEKIDIVVTYHH 96
Cdd:cd03807 12 GGAETMLLRLLEHMDKSRFEHVVISLTGdGVLGEELLAAGVPVVCLGLSSGKDPGVLLR---LAKLIRKRNPDVVHTWMY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 97 DADIWGGAIAMLAGVPAVVSSRRDLGYQ--LEKKHVWAYRALNRFYTRIISVSDAVKREImRREWTPGGKIITVYNGVEI 174
Cdd:cd03807 89 HADLIGGLAAKLAGGVKVIWSVRSSNIPqrLTRLVRKLCLLLSKFSPATVANSSAVAEFH-QEQGYAKNKIVVIYNGIDL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 175 ERYRQGAKGQG---ASLGIGRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMVGykDTDYYREVKEEIERLGL 251
Cdd:cd03807 168 FKLSPDDASRArarRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVG--RGPERPNLERLLLELGL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 252 EDYFIFLGDRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEAVIDNeTGFLVPPADSHGLAGAIL 331
Cdd:cd03807 246 EDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPAGDPQALADAIR 324
|
....*..
gi 1084692519 332 RLLDDAE 338
Cdd:cd03807 325 ALLEDPE 331
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
6-339 |
1.36e-67 |
|
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: 216.25 E-value: 1.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 6 KILFLT-SLFGKMGGAEKNIYDIVLNIDRARFTPYVFCLKGGELVDDirrkgidsRIIDLDKIISLEGVRKGAGLYKFLK 84
Cdd:cd03801 1 KILLLSpELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPE--------ELEDGVIVPLLPSLAALLRARRLLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 85 SEKI-------DIVVTYHHDADIWGGAIAMLAGVPAVVSSRRDLGYQLEKKHVWAYRALNR------FYTRIISVSDAVK 151
Cdd:cd03801 73 ELRPllrlrkfDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLARaeallrRADAVIAVSEALR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 152 REIMRREWTPGGKIITVYNGVEIERYRQGAKgqgASLGIGRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMV 231
Cdd:cd03801 153 DELRALGGIPPEKIVVIPNGVDLERFSPPLR---RKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 232 GyKDTDYYREVKEEieRLGLEDYFIFLG--DRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEAV 309
Cdd:cd03801 230 G-GDGPLRAELEEL--ELGLGDRVRFLGfvPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV 306
|
330 340 350
....*....|....*....|....*....|
gi 1084692519 310 IDNETGFLVPPADSHGLAGAILRLLDDAEL 339
Cdd:cd03801 307 EDGEGGLVVPPDDVEALADALLRLLADPEL 336
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
6-341 |
1.90e-63 |
|
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: 205.28 E-value: 1.90e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 6 KILFLT-SLFGkmGGAEKNIYDIVLNIDRARFTPYVFCLKGGELVDDIRRKGIDSRIIDLDKIISLEGVRKGA--GLYKF 82
Cdd:cd03811 1 KILFVIpSLSG--GGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAilKLKRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 83 LKSEKIDIVVTYHHDADIWGGAIAmLAGVPAVVSSRRDLGYQL-EKKHVWAYRALNRFYTRIISVSDAVKREIMRREWTP 161
Cdd:cd03811 79 LKRAKPDVVISFLGFATYIVAKLA-AARSKVIAWIHSSLSKLYyLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 162 GGKIITVYNGVEIERYRQGAKGQgaSLGIGRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMVGykDTDYYRE 241
Cdd:cd03811 158 PEKIEVIYNPIDIDRIRALAKEP--ILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILG--DGPLREE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 242 VKEEIERLGLEDYFIFLGDRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEAVIDNETGFLVPPA 321
Cdd:cd03811 234 LEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDG 313
|
330 340
....*....|....*....|...
gi 1084692519 322 DS---HGLAGAILRLLDDAELGR 341
Cdd:cd03811 314 DAaalAGILAALLQKKLDAALRE 336
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
6-339 |
1.13e-53 |
|
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: 180.10 E-value: 1.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 6 KILFLTSlfgKMGGAEKNIYDIVLNIDRARFTPYVFCLKGGELVDDIRRKGIDSRIIDLDK--IISLEGVRKGAGLYKFL 83
Cdd:cd03808 1 KILFIVN---VDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKELGVKVIDIPILRrgINPLKDLKALFKLYKLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 84 KSEKIDIVVTYHHDADIWGGAIAMLAGVPAVVSSRRDLGY----QLEKKHVWA--YRALNRFYTRIISVSDAVKREIMRR 157
Cdd:cd03808 78 KKEKPDIVHCHTPKPGILGRLAARLAGVPKVIYTVHGLGFvfteGKLLRLLYLllEKLALLFTDKVIFVNEDDRDLAIKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 158 EWTPGGKIITVY-NGVEIERYRQgakgqgASLGIGRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMVGykDT 236
Cdd:cd03808 158 GIIKKKKTVLIPgSGVDLDRFQY------SPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVG--DG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 237 DYYREVKEEIERLGLEDYFIFLGDRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEAVIDNETGF 316
Cdd:cd03808 230 ELENPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGF 309
|
330 340
....*....|....*....|...
gi 1084692519 317 LVPPADSHGLAGAILRLLDDAEL 339
Cdd:cd03808 310 LVPPGDVEALADAIEKLIEDPEL 332
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
7-339 |
1.33e-52 |
|
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: 176.78 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 7 ILFLTSLFGkMGGAEKNIYDIVLNIDRARFTPYVFCLkGGELVDDIRRKGIDSRIIDLDKIISLEGVRKgagLYKFLKSE 86
Cdd:cd03819 1 ILMLTPALE-IGGAETYILDLARALAERGHRVLVVTA-GGPLLPRLRQIGIGLPGLKVPLLRALLGNVR---LARLIRRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 87 KIDIVvTYHHDADIWGGAIAM-LAGVPAVVSSRRDlgYQLEKKHVWAYRALNRFYTRIISVSDAVKREIMRREWTPGGKI 165
Cdd:cd03819 76 RIDLI-HAHSRAPAWLGWLASrLTGVPLVTTVHGS--YLATYHPKDFALAVRARGDRVIAVSELVRDHLIEALGVDPERI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 166 ITVYNGVEIERYR-QGAKGQGASLGIGRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRnKDFQIVMVGykDTDYYREVKE 244
Cdd:cd03819 153 RVIPNGVDTDRFPpEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDE-PDFRLLVAG--DGPERDEIRR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 245 EIERLGLEDYFIFLGDRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEAVIDNETGFLVPPADSH 324
Cdd:cd03819 230 LVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAE 309
|
330
....*....|....*
gi 1084692519 325 GLAGAILRLLDDAEL 339
Cdd:cd03819 310 ALADAIRAAKLLPEA 324
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
18-341 |
2.50e-46 |
|
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: 161.43 E-value: 2.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 18 GGAEKNIYDIVLNIDRARFTPYVFCLKG-GELVDDIRRKGIDsrIIDLDKiislegvRKGAG------LYKFLKSEKIDI 90
Cdd:TIGR03088 14 GGLENGLVNLINHLPADRYRHAVVALTEvSAFRKRIQRPDVA--FYALHK-------QPGKDvavypqLYRLLRQLRPDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 91 VVTyHHDADIWGGAIAMLAGVPAVVSSR--RDLgYQLEKKHvWAYRALNRFYTRIISVSDAVKREImrREW------TPG 162
Cdd:TIGR03088 85 VHT-RNLAALEAQLPAALAGVPARIHGEhgRDV-FDLDGSN-WKYRWLRRLYRPLIHHYVAVSRDL--EDWlrgpvkVPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 163 GKIITVYNGVEIERYRQGAKGQGASLG---IGRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQ----IVMVGykD 235
Cdd:TIGR03088 160 AKIHQIYNGVDTERFHPSRGDRSPILPpdfFADESVVVGTVGRLQAVKDQPTLVRAFALLVRQLPEGAerlrLVIVG--D 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 236 TDYYREVKEEIERLGLEDYFIFLGDRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEAVIDNETG 315
Cdd:TIGR03088 238 GPARGACEQMVRAAGLAHLVWLPGERDDVPALMQALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTG 317
|
330 340
....*....|....*....|....*.
gi 1084692519 316 FLVPPADSHGLAGAILRLLDDAELGR 341
Cdd:TIGR03088 318 ALVPPGDAVALARALQPYVSDPAARR 343
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
79-341 |
6.30e-45 |
|
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: 157.54 E-value: 6.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 79 LYKFLKSEKIDIVvtyHHDADIWGGAIAML----AGVPAVVSSRRDLGYQLEKKH------VWAYRalnRFyTRIISVSD 148
Cdd:cd03798 87 LLKRRRRGPPDLI---HAHFAYPAGFAAALlarlYGVPYVVTEHGSDINVFPPRSllrkllRWALR---RA-ARVIAVSK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 149 AVKREiMRREWTPGGKIITVYNGVEIERYRQGAKGQGASLGigrgKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQI 228
Cdd:cd03798 160 ALAEE-LVALGVPRDRVDVIPNGVDPARFQPEDRGLGLPLD----AFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 229 VMVGY-KDTDYYREVkeeIERLGLEDYFIFLG--DRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGN 305
Cdd:cd03798 235 LIVGDgPLREALRAL---AEDLGLGDRVTFTGrlPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGI 311
|
250 260 270
....*....|....*....|....*....|....*.
gi 1084692519 306 PEAVIDNETGFLVPPADSHGLAGAILRLLDDAELGR 341
Cdd:cd03798 312 PEVVGDPETGLLVPPGDADALAAALRRALAEPYLRE 347
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
194-336 |
2.85e-43 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 146.12 E-value: 2.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 194 KKVIGMLASLRP-VKGHIHLVRAVAEVVRRNKDFQIVMVGYKDTDYYREvkeeiERLGLEDYFIFLGDRKDVPETLSSFD 272
Cdd:pfam13692 1 RPVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEE-----LAAGLEDRVIFTGFVEDLAELLAAAD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084692519 273 MMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEaVIDNETGFLVPPADSHGLAGAILRLLDD 336
Cdd:pfam13692 76 VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPE-LVDGENGLLVPPGDPEALAEAILRLLED 138
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
193-339 |
1.73e-38 |
|
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 134.32 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 193 GKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMVGYKDtdYYREVKEEIERLGLEDYFIFLG--DRKDVPETLSS 270
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGE--EEKRLKKLAEKLGLGDNVIFLGfvSDEDLPELLKI 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084692519 271 FDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEAVIDNETGFLVPPADSHGLAGAILRLLDDAEL 339
Cdd:pfam00534 79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEEL 147
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
6-317 |
1.25e-37 |
|
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: 137.81 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 6 KIL-FLTSLFGkmGGAEKNIYDIV--LNIDRARFTPYVFCLKGGELVDDIRRKGIdsriidldKIISLEGVRKG-----A 77
Cdd:cd03812 1 KILhIVGGMNV--GGIETFLMNLYrkLDKSKIEFDFLATSDDKGEYDEELEELGG--------KIFYIPPKKKNiikyfI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 78 GLYKFLKSEKIDIVvtyHHDADIWGGAIAMLA---GVPAVVS---SRRDLGYQLEKKHVWAYRAL-NRFYTRIISVSDAV 150
Cdd:cd03812 71 KLLKLIKKEKYDIV---HVHGSSSNGIILLLAakaGVPVRIAhshNTKDSSIKLRKIRKNVLKKLiERLSTKYLACSEDA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 151 KREIMrrEWTPGGKIITVYNGVEIERYR--QGAKGQGASLGIGRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQI 228
Cdd:cd03812 148 GEWLF--GEVENGKFKVIPNGIDIEKYKfnKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 229 VMVGYKDTDYyrEVKEEIERLGLEDYFIFLGDRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNpEA 308
Cdd:cd03812 226 VLVGEGELKE--KIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITK-EC 302
|
....*....
gi 1084692519 309 VIDNETGFL 317
Cdd:cd03812 303 DITNNVEFL 311
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
132-339 |
1.68e-34 |
|
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: 131.69 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 132 AYRALNRfytrIISVSDAvKREIMRREWTPGGKIITVYNGVEIERYRQGAKGQGASLGIgrgkkVIGMLASLRPVKGHIH 211
Cdd:cd03813 241 AYQQADK----IISLYEG-NRRRQIRLGADPDKTRVIPNGIDIQRFAPAREERPEKEPP-----VVGLVGRVVPIKDVKT 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 212 LVRAVAEVVRRNKDFQIVMVG--YKDTDYYREVKEEIERLGLEDYFIFLGdRKDVPETLSSFDMMVLPSLSEGFSNAALE 289
Cdd:cd03813 311 FIRAFKLVRRAMPDAEGWLIGpeDEDPEYAQECKRLVASLGLENKVKFLG-FQNIKEYYPKLGLLVLTSISEGQPLVILE 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1084692519 290 GMAAGKPVIATDCGGNPEAVID-----NETGFLVPPADSHGLAGAILRLLDDAEL 339
Cdd:cd03813 390 AMASGVPVVATDVGSCRELIYGaddalGQAGLVVPPADPEALAEALIKLLRDPEL 444
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
132-339 |
8.45e-34 |
|
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: 127.85 E-value: 8.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 132 AYRALNRF----YTRIISVSDAVKREImRREWTPGGKIITVYNGVEIERY-RQGAKGQGASLGIGRGKKVIGMLASLRPV 206
Cdd:cd04962 130 SLQPAVRFsinkSDRVTAVSSSLRQET-YELFDVDKDIEVIHNFIDEDVFkRKPAGALKRRLLAPPDEKVVIHVSNFRPV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 207 KGHIHLVRAVAEVVRRNKDfQIVMVGykDTDYYREVKEEIERLGLEDYFIFLGDRKDVPETLSSFDMMVLPSLSEGFSNA 286
Cdd:cd04962 209 KRIDDVVRVFARVRRKIPA-KLLLVG--DGPERVPAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLA 285
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1084692519 287 ALEGMAAGKPVIATDCGGNPEAVIDNETGFLVPPADSHGLAGAILRLLDDAEL 339
Cdd:cd04962 286 ALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDEL 338
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
76-341 |
4.89e-32 |
|
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: 123.50 E-value: 4.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 76 GAGLYKFLKSEKI--DIVVTYHHDADIWGGAIAMLAGVPAVVS-------SRRDLGYQlekkhvWAYRALNRFYT----- 141
Cdd:cd03800 88 ADGLLRFIAREGGryDLIHSHYWDSGLVGALLARRLGVPLVHTfhslgrvKYRHLGAQ------DTYHPSLRITAeeqil 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 142 ----RIISVSDAVKREIMRREWTPGGKIITVYNGVEIERYRQGAKGQG--ASLGIGRGKKVIGMLASLRPVKGHIHLVRA 215
Cdd:cd03800 162 eaadRVIASTPQEADELISLYGADPSRINVVPPGVDLERFFPVDRAEArrARLLLPPDKPVVLALGRLDPRKGIDTLVRA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 216 VAEVVRRNKDFQIVMVGYKDTDYYREVKEEI----ERLGLEDYFIFLG--DRKDVPETLSSFDMMVLPSLSEGFSNAALE 289
Cdd:cd03800 242 FAQLPELRELANLVLVGGPSDDPLSMDREELaelaEELGLIDRVRFPGrvSRDDLPELYRAADVFVVPSLYEPFGLTAIE 321
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1084692519 290 GMAAGKPVIATDCGGNPEAVIDNETGFLVPPADSHGLAGAILRLLDDAELGR 341
Cdd:cd03800 322 AMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQ 373
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
6-339 |
2.04e-31 |
|
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: 120.81 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 6 KILFLTSLFGKMGGAEK-----------NIYDI-VLNIDRARFTPYvFclkggELVDDIRRKGIDSRIIdLDKIISLEGV 73
Cdd:cd03820 1 KIAIVIPSISNAGGAERvainlanhlakKGYDVtIISLDSAEKPPF-Y-----ELDDNIKIKNLGDRKY-SHFKLLLKYF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 74 RKGAGLYKFLKSEKIDIVVTYHHDADIWggAIAMLAGVPAVVSSRRDLGYQLEKKHVWAYRALN-RFYTRIISVSdavKR 152
Cdd:cd03820 74 KKVRRLRKYLKNNKPDVVISFRTSLLTF--LALIGLKSKLIVWEHNNYEAYNKGLRRLLLRRLLyKRADKIVVLT---EA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 153 EIMRREWTPGGKIITVYNGVEIERYRQGAKgqgaslgigRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMVG 232
Cdd:cd03820 149 DKLKKYKQPNSNVVVIPNPLSFPSEEPSTN---------LKSKRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 233 ykDTDYYREVKEEIERLGLEDYFIFLGDRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDC-GGNPEAVID 311
Cdd:cd03820 220 --DGPEREELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCpTGPSEIIED 297
|
330 340
....*....|....*....|....*...
gi 1084692519 312 NETGFLVPPADSHGLAGAILRLLDDAEL 339
Cdd:cd03820 298 GENGLLVPNGDVDALAEALLRLMEDEEL 325
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
79-339 |
7.91e-30 |
|
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: 117.44 E-value: 7.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 79 LYKFLKSEKIDIVVTYHHDADIWGGA--IAMLAGVPAVV-------SSRRDLGYqLEKKHVwaYRALNRFY-------TR 142
Cdd:cd03794 90 LKLLVREERPDVIIAYSPPITLGLAAllLKKLRGAPFILdvrdlwpESLIALGV-LKKGSL--LKLLKKLErklyrlaDA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 143 IISVSDAVKREIMRREwTPGGKIITVYNGVEIERYRQGAKGQGASLGIGRGKKVIGMLASLrpvkGHIHLVR---AVAEV 219
Cdd:cd03794 167 IIVLSPGLKEYLLRKG-VPKEKIIVIPNWADLEEFKPPPKDELRKKLGLDDKFVVVYAGNI----GKAQGLEtllEAAER 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 220 VRRNKDFQIVMVGykDTDYYREVKEEIERLGLEDY-FIFLGDRKDVPETLSSFDMMVLPsLSEGFSNAA------LEGMA 292
Cdd:cd03794 242 LKRRPDIRFLFVG--DGDEKERLKELAKARGLDNVtFLGRVPKEEVPELLSAADVGLVP-LKDNPANRGsspsklFEYMA 318
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1084692519 293 AGKPVIATDCGGNPEAVIDNETGFLVPPADSHGLAGAILRLLDDAEL 339
Cdd:cd03794 319 AGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPEL 365
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
6-339 |
9.56e-30 |
|
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: 116.69 E-value: 9.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 6 KILF-LTSLFGKMGGAEKNIYDIV---LNIDRARFTPYVFCLKGGELVDDIRRKGIDSRIIDLDKIISLEGVRkgAGLYK 81
Cdd:cd03809 1 KILIdGRSLAQRLTGIGRYTRELLkalAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLR--WLQIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 82 FLKSEKIDIVVTYHHDADIWGGAIAMLAGV--------PAVVSSRRDLGYQlekkhvWAYRALNRFYTRIISVSDAVKRE 153
Cdd:cd03809 79 LPKKDKPDLLHSPHNTAPLLLKGCPQVVTIhdliplryPEFFPKRFRLYYR------LLLPISLRRADAIITVSEATRDD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 154 IMRREWTPGGKIITVYNGVEIERYRQGAKGQGASLGIGRGKKVIgMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMVGY 233
Cdd:cd03809 153 IIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLPEPYFL-YVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 234 KDtDYYREVKEEIERLGLEDYFIFLG--DRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEavID 311
Cdd:cd03809 232 KG-WEDEELLDLVKKLGLGGRVRFLGyvSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPE--VA 308
|
330 340
....*....|....*....|....*...
gi 1084692519 312 NETGFLVPPADSHGLAGAILRLLDDAEL 339
Cdd:cd03809 309 GDAALYFDPLDPESIADAILRLLEDPSL 336
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
117-336 |
1.66e-28 |
|
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: 113.20 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 117 SRRDLGYQLEKKHVWAYRALNRFytrIISVSDAVKREIMRREWTPGGKIITVYNGVEIERYRQGAKGQG-ASLGIGRGKK 195
Cdd:cd03825 118 AKKDLSRQLFRRKREALAKKRLT---IVAPSRWLADMVRRSPLLKGLPVVVIPNGIDTEIFAPVDKAKArKRLGIPQDKK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 196 VIGMLAS--LRPVKGHIHLVRAVAEVVRrNKDFQIVMVGYKDtdyyrevkEEIERLGLE-DYFIFLGDRKDVPETLSSFD 272
Cdd:cd03825 195 VILFGAEsvTKPRKGFDELIEALKLLAT-KDDLLLVVFGKND--------PQIVILPFDiISLGYIDDDEQLVDIYSAAD 265
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084692519 273 MMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEAVIDNETGFLVPPADSHGLAGAILRLLDD 336
Cdd:cd03825 266 LFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLAN 329
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
155-318 |
5.51e-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: 103.64 E-value: 5.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 155 MRREWTPGGKIITVYNGVEIERYRQGAKGQGASLGIGRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMVGYK 234
Cdd:cd01635 71 LLAARLLGIPIVVTVHGPDSLESTRSELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 235 DTDYYREVKEEIERLGLEDYFIFLGDRKDVPETLS-SFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEAVIDNE 313
Cdd:cd01635 151 GEREEEEALAAALGLLERVVIIGGLVDDEVLELLLaAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGE 230
|
....*
gi 1084692519 314 TGFLV 318
Cdd:cd01635 231 NGLLV 235
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
6-336 |
4.26e-25 |
|
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: 103.68 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 6 KILFLTSLFGkMGGAEKNIYDIVLNIDRARFTPYVFCLKGGELVDDIrrkgidsriIDLDKIISLEGVRKGAGLY----- 80
Cdd:cd04951 1 KILYVITGLG-LGGAEKQTVLLADQMFIRGHDVNIVYLTGEVEVKPL---------NNNIIIYNLGMDKNPRSLLkallk 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 81 --KFLKSEKIDIVVTYHHDADIWGGAIAMLAGVPAVVSS--RRDLGYQLEKKhvwAYRALNRFYTRIISVSDAVKREIMR 156
Cdd:cd04951 71 lkKIISAFKPDVVHSHMFHANIFARFLRMLYPIPLLICTahNKNEGGRIRMF---IYRLTDFLCDITTNVSREALDEFIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 157 REWTPGGKIITVYNGVEIERY------RQGAKGQgasLGIGRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVM 230
Cdd:cd04951 148 KKAFSKNKSVPVYNGIDLNKFkkdinvRLKIRNK---LNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 231 VGykDTDYYREVKEEIERLGLEDYFIFLGDRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEAVI 310
Cdd:cd04951 225 AG--DGPLRNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVG 302
|
330 340
....*....|....*....|....*.
gi 1084692519 311 DNEtgFLVPPADSHGLAGAILRLLDD 336
Cdd:cd04951 303 DHN--YVVPVSDPQLLAEKIKEIFDM 326
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
79-341 |
4.68e-25 |
|
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: 104.00 E-value: 4.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 79 LYKFLKSEKIDIVVTYHHDAdIWGGAIA-------MLAGVP--AVVSSRRDLGYQLEKKHVWAYRaLNRFYTRIISVSDA 149
Cdd:cd03822 67 LLDHLNFKKPDVVHIQHEFG-IFGGKYGlyalgllLHLRIPviTTLHTVLDLSDPGKQALKVLFR-IATLSERVVVMAPI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 150 VKREIMRREWTPGGKIITVYNGVeIERYRQGAKGQGASLGIgRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIV 229
Cdd:cd03822 145 SRFLLVRIKLIPAVNIEVIPHGV-PEVPQDPTTALKRLLLP-EGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 230 MVG-----YKDTDYYREVKEEIERLGLEDYfIFLGDRK----DVPETLSSFDMMVLPSLSEGFSN--AALEGMAAGKPVI 298
Cdd:cd03822 223 IAGelhpsLARYEGERYRKAAIEELGLQDH-VDFHNNFlpeeEVPRYISAADVVVLPYLNTEQSSsgTLSYAIACGKPVI 301
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1084692519 299 ATDCGGNPEAVIDNEtGFLVPPADSHGLAGAILRLLDDAELGR 341
Cdd:cd03822 302 STPLRHAEELLADGR-GVLVPFDDPSAIAEAILRLLEDDERRQ 343
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
6-336 |
1.37e-24 |
|
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.
Pssm-ID: 340848 [Multi-domain] Cd Length: 377 Bit Score: 102.83 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 6 KILFLTSLF-GKMGGAEKNIYDIVLNIDRARFTPYVFCLKGGElvDDIRRKGIDSRIIDLDKIISLEGVRKGAGLYKFlk 84
Cdd:cd03821 1 KILHVTPSIsPKAGGPVKVVLRLAAALAALGHEVTIVSTGDGY--ESLVVEENGRYIPPQDGFASIPLLRQGAGRTDF-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 85 SEKIDIVVTYH-------HDADIWG------GAIAMLAGVPAVVSSRRDLG-YQLEKKHVWAYRALNRFYTRIISVSDAV 150
Cdd:cd03821 77 SPGLPNWLRRNlreydvvHIHGVWTytslaaCKLARRRGIPYVVSPHGMLDpWALQQKHWKKRIALHLIERRNLNNAALV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 151 KREI-MRREWT----PGGKIITVYNGVEIERYrQGAKGQGASLGIGRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKD 225
Cdd:cd03821 157 HFTSeQEADELrrfgLEPPIAVIPNGVDIPEF-DPGLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 226 FQIVMVGYKDTDYYREVKEeIERLGLEDYFIFLG--DRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATD-C 302
Cdd:cd03821 236 WHLVIAGPDDGAYPAFLQL-QSSLGLGDRVTFTGplYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDkC 314
|
330 340 350
....*....|....*....|....*....|....
gi 1084692519 303 GGnpEAVIDNETGFLVPPADsHGLAGAILRLLDD 336
Cdd:cd03821 315 GL--SELVEAGCGVVVDPNV-SSLAEALAEALRD 345
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
258-341 |
1.45e-24 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 96.60 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 258 LGDRKDVPETL----SSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEAVIDNETGFLVPPADSHGLAGAILRL 333
Cdd:COG0438 4 LVPRKGLDLLLeallAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRL 83
|
....*...
gi 1084692519 334 LDDAELGR 341
Cdd:COG0438 84 LEDPELRR 91
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
6-339 |
7.72e-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: 100.48 E-value: 7.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 6 KILFLTSLF--GKMGGAEKNIYDIVLNIDRARFTPYVFCL--------KGGELVDDIRRKGIDSRIIDLDKIISLEGVRK 75
Cdd:cd03823 1 KILLVNSLYppQRVGGAEISVHDLAEALVAEGHEVAVLTAgvgppgqaTVARSVVRYRRAPDETLPLALKRRGYELFETY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 76 GAGLY----KFLKSEKIDIVVTYH---HDADIWggAIAMLAGVPAVVSSRrDlgYQLEKKHVWAYRALNRfytRIISVSD 148
Cdd:cd03823 81 NPGLRrllaRLLEDFRPDVVHTHNlsgLGASLL--DAARDLGIPVVHTLH-D--YWLLCPRQFLFKKGGD---AVLAPSR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 149 AVKReIMRREWTPGGKIITVYNGVEIERYRQGAKGQGaslgigRGKKVIGMLASLRPVKGhIHLVRavaEVVRRNKDFQI 228
Cdd:cd03823 153 FTAN-LHEANGLFSARISVIPNAVEPDLAPPPRRRPG------TERLRFGYIGRLTEEKG-IDLLV---EAFKRLPREDI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 229 --VMVGYKDtdyyrevKEEIERLGLEDYFIFLG--DRKDVPETLSSFDMMVLPSL-SEGFSNAALEGMAAGKPVIATDCG 303
Cdd:cd03823 222 elVIAGHGP-------LSDERQIEGGRRIAFLGrvPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLG 294
|
330 340 350
....*....|....*....|....*....|....*.
gi 1084692519 304 GNPEAVIDNETGFLVPPADSHGLAGAILRLLDDAEL 339
Cdd:cd03823 295 GIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPAL 330
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
79-341 |
8.77e-22 |
|
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: 94.65 E-value: 8.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 79 LYKFLKSEKIDIVVTYHH-DADIWGGAIAMLAGVPAVVSS----RRDLGY-----QLEKKHV-WAYRALNRFYTRIISVS 147
Cdd:cd03817 76 VIDRIKELGPDIIHTHTPfSLGKLGLRIARKLKIPIVHTYhtmyEDYLHYipkgkLLVKAVVrKLVRRFYNHTDAVIAPS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 148 DAVKREImrREWTPGGKIITVYNGVEIERY-RQGAKGQGASLGIGRGKKVIGMLASLRPVKGHIHLVRAVAEVvRRNKDF 226
Cdd:cd03817 156 EKIKDTL--REYGVKGPIEVIPNGIDLDKFeKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAEL-KKEPNI 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 227 QIVMVGykDTDYYREVKEEIERLGLEDYFIFLG--DRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGG 304
Cdd:cd03817 233 KLVIVG--DGPEREELKELARELGLADKVIFTGfvPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPA 310
|
250 260 270
....*....|....*....|....*....|....*..
gi 1084692519 305 NPEAVIDNETGFLVPPaDSHGLAGAILRLLDDAELGR 341
Cdd:cd03817 311 ASELVEDGENGFLFEP-NDETLAEKLLHLRENLELLR 346
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
166-339 |
3.93e-20 |
|
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: 89.64 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 166 ITVYNG--VEIERYRQGAKGQGASLGIGRgkkvigmlasLRPVKGHIHLVRAVAEVvrrnkDFQIVMVGykDTDYYREVK 243
Cdd:cd03795 171 KNVYNIprVDFENIKREKKGKKIFLFIGR----------LVYYKGLDYLIEAAQYL-----NYPIVIGG--EGPLKPDLE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 244 EEIERLGLEDYFiFLG--DRKDVPETLSSFDMMVLPSL--SEGFSNAALEGMAAGKPVIATDCG-GNPEAVIDNETGFLV 318
Cdd:cd03795 234 AQIELNLLDNVK-FLGrvDDEEKVIYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVV 312
|
170 180
....*....|....*....|.
gi 1084692519 319 PPADSHGLAGAILRLLDDAEL 339
Cdd:cd03795 313 PPKDPDALAEAIDKLLSDEEL 333
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
157-339 |
5.20e-20 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 89.85 E-value: 5.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 157 REWTPGGKIITVYNGVEIERY-RQGAKGQGASLGIGRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMVG--- 232
Cdd:PRK15484 155 EERLPNADISIVPNGFCLETYqSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGdpt 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 233 ----YKDTDYYREVKEEIERLGleDYFIFLGDRKdvPETLSSF----DMMVLPS-LSEGFSNAALEGMAAGKPVIATDCG 303
Cdd:PRK15484 235 asskGEKAAYQKKVLEAAKRIG--DRCIMLGGQP--PEKMHNYyplaDLVVVPSqVEEAFCMVAVEAMAAGKPVLASTKG 310
|
170 180 190
....*....|....*....|....*....|....*..
gi 1084692519 304 GNPEAVIDNETGF-LVPPADSHGLAGAILRLLDDAEL 339
Cdd:PRK15484 311 GITEFVLEGITGYhLAEPMTSDSIISDINRTLADPEL 347
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
186-339 |
6.04e-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: 88.90 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 186 ASLGIGRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMVGYKDTDYyrEVKEEIERLGLEDYFIFLGDRKDVP 265
Cdd:cd04949 152 AESNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEERE--KLKKLIEELHLEDNVFLKGYHSNLD 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084692519 266 ETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCG-GNPEAVIDNETGFLVPPADSHGLAGAILRLLDDAEL 339
Cdd:cd04949 230 QEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEK 304
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
81-333 |
8.10e-20 |
|
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.
Pssm-ID: 340832 [Multi-domain] Cd Length: 333 Bit Score: 88.50 E-value: 8.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 81 KFLKSEKIDIVvtyHHDADIWGGAIAMLAGVPAVVSSRrdlGYQLEKKHVwayRALNRFYTRIISVSDAvkreiMRREWT 160
Cdd:cd03802 80 VQLRASDFDVI---HNHSYDWLPPFAPLIGTPFVTTLH---GPSIPPSLA---IYAAEPPVNYVSISDA-----QRAATP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 161 PGGKIITVYNGVEIERYRQGAKGQGASLGIGRgkkvigmlasLRPVKGhIHLVRAVAEVVRRnkdfQIVMVG-YKDTDYY 239
Cdd:cd03802 146 PIDYLTVVHNGLDPADYRFQPDPEDYLAFLGR----------IAPEKG-LEDAIRVARRAGL----PLKIAGkVRDEDYF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 240 REVKEEIERLGLEDYFIFLGDRKdvPETLSSFDMMVLPSL-SEGFSNAALEGMAAGKPVIATDCGGNPEAVIDNETGFLV 318
Cdd:cd03802 211 YYLQEPLPGPRIEFIGEVGHDEK--QELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLV 288
|
250
....*....|....*
gi 1084692519 319 PPADshGLAGAILRL 333
Cdd:cd03802 289 DSVE--EMAEAIANI 301
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
78-341 |
7.04e-19 |
|
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: 86.35 E-value: 7.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 78 GLYKFLKSEKIDI--VVTYHhdadiwGGAIAMlagVPAVVSSRRDLGYQLEKKHvwayRALNRFYTRIISVSDAVKREIM 155
Cdd:cd05844 93 GVYALPLARALGVplVVTFH------GFDITT---SRAWLAASPGWPSQFQRHR----RALQRPAALFVAVSGFIRDRLL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 156 RREWtPGGKIITVYNGVEIERYRQGAKGQGAslgigrgkKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMVGykD 235
Cdd:cd05844 160 ARGL-PAERIHVHYIGIDPAKFAPRDPAERA--------PTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAG--D 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 236 TDYYREVKEEIERLGledYFIFLG--DRKDVPETLSSFDMMVLPSL------SEGFSNAALEGMAAGKPVIATDCGGNPE 307
Cdd:cd05844 229 GPLRPALQALAAALG---RVRFLGalPHAEVQDWMRRAEIFCLPSVtaasgdSEGLGIVLLEAAACGVPVVSSRHGGIPE 305
|
250 260 270
....*....|....*....|....*....|....
gi 1084692519 308 AVIDNETGFLVPPADSHGLAGAILRLLDDAELGR 341
Cdd:cd05844 306 AILDGETGFLVPEGDVDALADALQALLADRALAD 339
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
68-341 |
2.90e-18 |
|
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: 84.65 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 68 ISLEGVRKGAGLyKFLKSEKIDIVVTYHHDadiwggaiamlagVPAVVSSRrdlGYQLEKKHVWAY-RALNRFYTRIISV 146
Cdd:cd03814 90 IATPGPLGLAAL-RAARRLGLPVVTSYHTD-------------FPEYLSYY---TLGPLSWLAWAYlRWFHNPFDTTLVP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 147 SDAVKREimrREWTPGGKIITVYNGVEIERYRQGAKGQG--ASLGIGrGKKVIGMLASLRPVKgHIHLVRAVAEVVRRNK 224
Cdd:cd03814 153 SPSIARE---LEGHGFERVRLWPRGVDTELFHPSRRDAAlrRRLGPP-GRPLLLYVGRLAPEK-NLEALLDADLPLAASP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 225 DFQIVMVGykDTDYyrevKEEIERLGLEdyFIFLG--DRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDC 302
Cdd:cd03814 228 PVRLVVVG--DGPA----RAELEARGPD--VIFTGflTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADA 299
|
250 260 270
....*....|....*....|....*....|....*....
gi 1084692519 303 GGNPEAVIDNETGFLVPPADSHGLAGAILRLLDDAELGR 341
Cdd:cd03814 300 GGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRR 338
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
164-339 |
4.15e-15 |
|
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: 75.18 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 164 KIITVYNGVEIERYRQGAKGQGASlgigrGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMVGykDTDYYREVK 243
Cdd:cd03799 149 KIIVHRSGIDCNKFRFKPRYLPLD-----GKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIG--DGDLKEQLQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 244 EEIERLGLEDYFIFLG--DRKDVPETLSSFDMMVLPSLS------EGFSNAALEGMAAGKPVIATDCGGNPEAVIDNETG 315
Cdd:cd03799 222 QLIQELNIGDCVKLLGwkPQEEIIEILDEADIFIAPSVTaadgdqDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSG 301
|
170 180
....*....|....*....|....
gi 1084692519 316 FLVPPADSHGLAGAILRLLDDAEL 339
Cdd:cd03799 302 FLVPERDAEAIAEKLTYLIEHPAI 325
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
71-335 |
4.88e-15 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 76.23 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 71 EGVRKgagLYKFLKSEKIDIVVTYHhDADIWGGAIA-MLAGVPAVVSSRRDLG-------YQLEKKHVwaYRALNRFyTR 142
Cdd:PRK15179 387 EGTTK---LTDVMRSSVPSVVHIWQ-DGSIFACALAaLLAGVPRIVLSVRTMPpvdrpdrYRVEYDII--YSELLKM-RG 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 143 IISVSDAVKREIMRREW--TPGGKIITVYNGVEIERYRQ--GAKGQGASL--GIGRGKKVIGMLASLRPVKGHIHLVRAV 216
Cdd:PRK15179 460 VALSSNSQFAAHRYADWlgVDERRIPVVYNGLAPLKSVQddACTAMMAQFdaRTSDARFTVGTVMRVDDNKRPFLWVEAA 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 217 AEVVRRNKDFQIVMVGykDTDYYREVKEEIERLGLEDYFIFLGDRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKP 296
Cdd:PRK15179 540 QRFAASHPKVRFIMVG--GGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVP 617
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1084692519 297 VIATDCGGNPEAVIDNETGFLVPPAD--SHGLAGAILRLLD 335
Cdd:PRK15179 618 VVTTLAGGAGEAVQEGVTGLTLPADTvtAPDVAEALARIHD 658
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
156-338 |
7.52e-15 |
|
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: 74.97 E-value: 7.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 156 RREWTPGG---KIITVYNGVEIERYRQGAKGQGASLgigrgKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMVG 232
Cdd:NF038011 270 LRQIADGAppeRTRVIPNGIDLPRLAPLRAQRPAGI-----PPVVGLIGRVVPIKDIKTFIRAMRTVVRAMPEAEGWIVG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 233 YKDTD--YYREVKEEIERLGLEDYFIFLGDRKdVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATD---C----- 302
Cdd:NF038011 345 PEEEDpaYAAECRSLVASLGLQDKVKFLGFQK-IDDLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDvgsCrqlie 423
|
170 180 190
....*....|....*....|....*....|....*.
gi 1084692519 303 GGNPEAVIDNETGFLVPPADSHGLAGAILRLLDDAE 338
Cdd:NF038011 424 GLDEEDRALGAAGEVVAIADPQALARAALDLLRDPQ 459
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
173-341 |
1.81e-14 |
|
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: 73.51 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 173 EIERYRQgakgqgASLGIGRGKKVIGMLASLRPVKGHIHLVRAVAEVVRRNKDFQIVMVGYKDTD------YYREVKEeI 246
Cdd:cd03792 182 DIRYYLE------KPFVIDPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDdpegsvVYEEVME-Y 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 247 ERLGLEDYFIFLGDRKDVPETLSSFDMMVLP-SLSEGFSNAALEGMAAGKPVIATDCGGNPEAVIDNETGFLVPPADshG 325
Cdd:cd03792 255 AGDDHDIHVLRLPPSDQEINALQRAATVVLQlSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVE--G 332
|
170
....*....|....*.
gi 1084692519 326 LAGAILRLLDDAELGR 341
Cdd:cd03792 333 AAVRILRLLTDPELRR 348
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
163-341 |
9.14e-14 |
|
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).
Pssm-ID: 340845 [Multi-domain] Cd Length: 396 Bit Score: 71.63 E-value: 9.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 163 GKIITVYNGVEIERYRQGAKGQGASLGIGR---GKKVIGMLA-SLRPVKGHIHLVRAVAEVVRRNKDFQIVMVGYKDTDY 238
Cdd:cd03818 179 DRISVIHDGVDTDRLAPDPAARLRLLNGTElkaGDPVITYVArNLEPYRGFHVFMRALPRIQARRPDARVVVVGGDGVSY 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 239 YREVK-------EEIERLGLED-YFIFLG--DRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEA 308
Cdd:cd03818 259 GSPPPdggswkqKMLAELGVDLeRVHFVGkvPYDQYVRLLQLSDAHVYLTYPFVLSWSLLEAMACGCPVIGSDTAPVREV 338
|
170 180 190
....*....|....*....|....*....|....*..
gi 1084692519 309 VIDNETGFLVPPADSHGLAGAILRLLDD----AELGR 341
Cdd:cd03818 339 IRDGRNGLLVDFFDPDALAAAVLELLEDpdraAALRR 375
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
18-175 |
1.88e-13 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 67.56 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 18 GGAEKNIYDIVLNIDRARFTPYVFCLKGG----ELVDDIRRKGIDSRIIDLDKIISLEGVRKgagLYKFLKSEKIDIVVT 93
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPgplaEEVVRVVRVPRVPLPLPPRLLRSLAFLRR---LRRLLRRERPDVVHA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 94 YHHDADIWGG-AIAMLAGVPAVVS------SRRDLGYQLEKKHVWAYRALNRFY---TRIISVSDAVKREIMRREWTPGG 163
Cdd:pfam13439 78 HSPFPLGLAAlAARLRLGIPLVVTyhglfpDYKRLGARLSPLRRLLRRLERRLLrraDRVIAVSEAVADELRRLYGVPPE 157
|
170
....*....|..
gi 1084692519 164 KIITVYNGVEIE 175
Cdd:pfam13439 158 KIRVIPNGVDLE 169
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
225-339 |
5.24e-11 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 63.58 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 225 DFQIVMVGY----KDTDYYREVKEEI------------ERLGLEDYF-----IFLG--DRKDVPETLSSFDMMVLPSLSE 281
Cdd:PLN02871 263 KPLIVYVGRlgaeKNLDFLKRVMERLpgarlafvgdgpYREELEKMFagtptVFTGmlQGDELSQAYASGDVFVMPSESE 342
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084692519 282 GFSNAALEGMAAGKPVIATDCGGNPEAVID---NETGFLVPPADSHGLAGAILRLLDDAEL 339
Cdd:PLN02871 343 TLGFVVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGDVDDCVEKLETLLADPEL 403
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
213-341 |
6.93e-10 |
|
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: 59.91 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 213 VRAVAEVVRRNKDFQIVMV----GYkDT------DYYREVKEEIERL-GLEDYFIFLGDRKD-VPETLSSFDMMVL--PS 278
Cdd:cd03805 230 IEAFAKLKQKLPEFENVRLviagGY-DPrvaenvEYLEELQRLAEELlNVEDQVLFLRSISDsQKEQLLSSALALLytPS 308
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084692519 279 lSEGFSNAALEGMAAGKPVIATDCGGNPEAVIDNETGFLVPPaDSHGLAGAILRLLDDAELGR 341
Cdd:cd03805 309 -NEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFAEAMLKLANDPDLAD 369
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
227-329 |
2.72e-09 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 58.17 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 227 QIVMVGykDTDYYREVKEEIERLGLEDYFIFLGDRKDVPETLSSFDMMVLPSLSEGFSNAALEGMAAGKPVIATDCGGNP 306
Cdd:PRK15490 431 RFVLVG--DGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGSA 508
|
90 100
....*....|....*....|...
gi 1084692519 307 EAVIDNETGFLVPPADSHGLAGA 329
Cdd:PRK15490 509 ECFIEGVSGFILDDAQTVNLDQA 531
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
18-171 |
2.76e-07 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 49.71 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 18 GGAEKNIYDIVLNIDRARFTPYVFCLKGGELVDDIRRKGIDSRIIDL-DKIISLEGVRKGAGLYKFLKSEKIDIVVTYHH 96
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPVpPRPSPLADLAALRRLRRLLRAERPDVVHAHSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084692519 97 DADIWGGAIAMLAGVPAVVSSRRDLGYQLEKKHVWAYRALNRF----YTRIISVSDAVkREIMRREWTPGGKIITVYNG 171
Cdd:pfam13579 81 TAGLAARLARRRRGVPLVVTVHGLALDYGSGWKRRLARALERRllrrADAVVVVSEAE-AELLRALGVPAARVVVVPNG 158
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
200-322 |
2.59e-06 |
|
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: 48.61 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 200 LASLRPVKgHIH-LVRAVAEVVRRNKDFQIVMVGYKDTDYYREVKEEIERLGLEDYFIFLG--DRKDVPE--TLSSFDMM 274
Cdd:cd04946 230 CSSIVPVK-RIDlIIETLNSLCVAHPSICISWTHIGGGPLKERLEKLAENKLENVKVNFTGevSNKEVKQlyKENDVDVF 308
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1084692519 275 VLPSLSEGFSNAALEGMAAGKPVIATDCGGNPEaVIDNETGFLVPPAD 322
Cdd:cd04946 309 VNVSESEGIPVSIMEAISFGIPVIATNVGGTRE-IVENETNGLLLDKD 355
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
130-338 |
1.24e-05 |
|
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.
Pssm-ID: 340835 [Multi-domain] Cd Length: 419 Bit Score: 46.83 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 130 VWAYRALNRFYTRIISVSDAV------KREIMRREWTPGGKIITVYNGVEIERYRQGAKGQGASlgigrgKKVIGMLASL 203
Cdd:cd03806 173 LLYYRLFAFLYGLAGSFADVVmvnstwTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPIDEKTR------ENQILSIAQF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 204 RPVKGHIHLVRAVAEVVRRNKDFQ-----IVMVG----YKDTDYYREVKEEIERLGLEDYFIFlgdRKDVP-ETL----- 268
Cdd:cd03806 247 RPEKNHPLQLRAFAELLKRLPESIrsnpkLVLIGscrnEEDKERVEALKLLAKELILEDSVEF---VVDAPyEELkells 323
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084692519 269 -SSF--DMMVlpslSEGFSNAALEGMAAGKPVIATDCGGnPE-----AVIDNETGFLVPPADSHGLAGAILRLLDDAE 338
Cdd:cd03806 324 tASIglHTMW----NEHFGIGVVEYMAAGLIPLAHASAG-PLldivvPWDGGPTGFLASTPEEYAEAIEKILTLSEEE 396
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
128-339 |
6.46e-05 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 44.58 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 128 KHVWAYRALNRFYTRIISVSDAVK---REIMRREWTPGG---KIITVYNGVEIERYRQGAKGQG----ASLGIGRGKKVI 197
Cdd:PRK10307 153 KGGKVARLATAFERSLLRRFDNVStisRSMMNKAREKGVaaeKVIFFPNWSEVARFQPVADADVdalrAQLGLPDGKKIV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 198 ---GMLASlrpvKGHIHLVRAVAEVVRRNKDFQIVMVGykdTDYYREVKEEIER-LGLED-YFIFLGDRKDVPETLSSFD 272
Cdd:PRK10307 233 lysGNIGE----KQGLELVIDAARRLRDRPDLIFVICG---QGGGKARLEKMAQcRGLPNvHFLPLQPYDRLPALLKMAD 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084692519 273 MMVLPSLSegfsNAA-------LEGM-AAGKPVIATdcgGNPEAVIDNET---GFLVPPADSHGLAGAILRLLDDAEL 339
Cdd:PRK10307 306 CHLLPQKA----GAAdlvlpskLTNMlASGRNVVAT---AEPGTELGQLVegiGVCVEPESVEALVAAIAALARQALL 376
|
|
| GT4_TuaH-like |
cd04950 |
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this ... |
162-300 |
7.14e-05 |
|
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. 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.
Pssm-ID: 340856 [Multi-domain] Cd Length: 373 Bit Score: 44.28 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 162 GGKIITVYNGVEIERYRQgAKGQGASLGIGRGKKvigmlaslRPVKGHI-----HL-VRAVAEVVRRNKDFQIVMVGykd 235
Cdd:cd04950 172 HENVHPIPNGVDVEHFAA-ARQPLDDPIDLREIP--------GPVLGFFgaideKLdFDLIEELAKARPQWNFVFIG--- 239
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084692519 236 tdyyREVKEEIERLGLEDYFIFLGDR--KDVPETLSSFDMMVLPSLSEGFSNAA-----LEGMAAGKPVIAT 300
Cdd:cd04950 240 ----PVVKIDPSSLPRAPNIHWLGPKpyKELPAYLAGFDVALLPFALNEYTRFIsplklFEYLAAGKPVVAT 307
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
123-317 |
9.57e-05 |
|
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: 43.81 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 123 YQLEKKHVWAYRALNRFyTRIISVSDAVKREI---MRREwtpggkIITVYNGVEIERYRQGAKGQGASLGIGRgkkvigm 199
Cdd:cd03804 142 LFLHYLRLWDVRTAQRV-DLFIANSQFVARRIkkfYGRE------STVIYPPVDTDAFAPAADKEDYYLTASR------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 200 lasLRPVKGhIHL-VRAVAEVVRRnkdfqIVMVGY-KDTDYYREV-KEEIERLGledyfiFLGDRKdVPETLSSFDMMVL 276
Cdd:cd03804 208 ---LVPYKR-IDLaVEAFNELPKR-----LVVIGDgPDLDRLRAMaSPNVEFLG------YQPDEV-LKELLSKARAFVF 271
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1084692519 277 PSlSEGFSNAALEGMAAGKPVIATDCGGNPEAVIDNETGFL 317
Cdd:cd03804 272 AA-EEDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGIL 311
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
212-335 |
8.62e-04 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 40.85 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 212 LVRAVAEVvrrNKDFQIVMVGykDTDYYREVKEEIERLGLEDYFIFLGDRKD----VPETLSSFDMMVLPSLSEGFSNAA 287
Cdd:PRK09922 200 LFDGLSQT---TGEWQLHIIG--DGSDFEKCKAYSRELGIEQRIIWHGWQSQpwevVQQKIKNVSALLLTSKFEGFPMTL 274
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1084692519 288 LEGMAAGKPVIATDCGGNPEAVI-DNETGFLVPPADSHGLAGAILRLLD 335
Cdd:PRK09922 275 LEAMSYGIPCISSDCMSGPRDIIkPGLNGELYTPGNIDEFVGKLNKVIS 323
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
39-147 |
5.54e-03 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 36.53 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692519 39 YVFCLKGGElVDDIRRKGIDSRIIDLDKIISLEGVrKGAGLYKFLKSEKIDIV-VTYHHDADIWGGAIAMLAGVPAVVSS 117
Cdd:pfam13477 28 HVISSKGPA-KDELIAEGIHVHRLKVPRKGPLGYL-KAFRLKKLIKKIKPDVVhVHYAKPYGLLAGLAARLSGFPPVVLS 105
|
90 100 110
....*....|....*....|....*....|....
gi 1084692519 118 RRDLG-YQLEKKHVW---AYRALNRFYTRIISVS 147
Cdd:pfam13477 106 AWGLDvYKFPNKSRLkklLLKLNLKKATLIISTS 139
|
|
| |
