|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
6-386 |
9.70e-36 |
|
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: 134.59 E-value: 9.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 6 KILLVHNHY-KIPGGEDTVVSNEKRLLEEHGHKVILYSRS-----NQEMQDFSVWQKLMLPFTSLFSLRTYRDVKALLKK 79
Cdd:cd03801 1 KILLLSPELpPPVGGAERHVRELARALAARGHDVTVLTPAdpgepPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 80 ERVDIVHVHNTLnlVSPSVYYAAFSLRVPVVQTLHNFRLlcpaatfvrdgricedcvkyglgcavrhgcYRNSRLQTLMS 159
Cdd:cd03801 81 RKFDVVHAHGLL--AALLAALLALLLGAPLVVTLHGAEP------------------------------GRLLLLLAAER 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 160 AAILKMYRLLGTYRRLfyICLTDFNKEKLLLLNQggrtiVREERVFVKSNFV----WRPQIREVERKEQ----YLYVGRL 231
Cdd:cd03801 129 RLLARAEALLRRADAV--IAVSEALRDELRALGG-----IPPEKIVVIPNGVdlerFSPPLRRKLGIPPdrpvLLFVGRL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 232 EDLKGVRFLVRTW----RDFPDRRLLLCGS-GPEEAWIRSYISENRmSQIELLGQVSHDEVMRLAAESRALIMPTMcYEG 306
Cdd:cd03801 202 SPRKGVDLLLEALakllRRGPDVRLVIVGGdGPLRAELEELELGLG-DRVRFLGFVPDEELPALYAAADVFVLPSR-YEG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 307 QGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAVRKF----EEAK--AWDTRPTYEKYYSPEKNYE 380
Cdd:cd03801 280 FGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLladpELRArlGRAARERVAERFSWERVAE 359
|
....*.
gi 1199425881 381 KLKEIY 386
Cdd:cd03801 360 RLLDLY 365
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
6-386 |
1.19e-32 |
|
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: 125.90 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 6 KILLVHNHY--KIPGGEDTVVSNEKRLLEEHGHKVILYSRSNQE-------------MQDFSVWQKLMLPFTSLFSLRTY 70
Cdd:cd03823 1 KILLVNSLYppQRVGGAEISVHDLAEALVAEGHEVAVLTAGVGPpgqatvarsvvryRRAPDETLPLALKRRGYELFETY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 71 -----RDVKALLKKERVDIVHVHNTLNLvSPSVYYAAFSLRVPVVQTLHNFRLLCPAATFVRDGRiceDCVkygLGcavr 145
Cdd:cd03823 81 npglrRLLARLLEDFRPDVVHTHNLSGL-GASLLDAARDLGIPVVHTLHDYWLLCPRQFLFKKGG---DAV---LA---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 146 hgcyrNSRlqtlmsaailkmyRLLGTYRRLFYicltdFNKEKLLLLNQggrtivreervfVKSNFVWRPQIREVERKEQY 225
Cdd:cd03823 150 -----PSR-------------FTANLHEANGL-----FSARISVIPNA------------VEPDLAPPPRRRPGTERLRF 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 226 LYVGRLEDLKGVRFLVRTWR--DFPDRRLLLCGSGPEEAwIRSYISEnrmSQIELLGQVSHDEVMRLAAESRALIMPTMC 303
Cdd:cd03823 195 GYIGRLTEEKGIDLLVEAFKrlPREDIELVIAGHGPLSD-ERQIEGG---RRIAFLGRVPTDDIKDFYEKIDVLVVPSIW 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 304 YEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAVRKFEEAKAWDTRptYEKYYSPEKNYEKLK 383
Cdd:cd03823 271 PEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLER--LRAGAEPPRSTESQA 348
|
...
gi 1199425881 384 EIY 386
Cdd:cd03823 349 EEY 351
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
222-359 |
9.56e-25 |
|
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 98.89 E-value: 9.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 222 KEQYLYVGRLEDLKGVRFLV----RTWRDFPDRRLLLCGSGPEEAWIRSYISENRMS-QIELLGQVSHDEVMRLAAESRA 296
Cdd:pfam00534 2 KKIILFVGRLEPEKGLDLLIkafaLLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGdNVIFLGFVSDEDLPELLKIADV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199425881 297 LIMPTMcYEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAVRKFEE 359
Cdd:pfam00534 82 FVLPSR-YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLE 143
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
7-355 |
9.81e-25 |
|
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: 103.59 E-value: 9.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 7 ILLVhNHYKIPGGEDTVVSNEKRLLEEHGHKVILYSRSNQEMQDFSVW-QKLMLPFTSLFS-LRTYRDVKALLKKERVDI 84
Cdd:cd03819 1 ILML-TPALEIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIgIGLPGLKVPLLRaLLGNVRLARLIRRERIDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 85 VHVHntLNLVSPSVYYAAFSLRVPVVQTLHNfrllcpaatfvrdgricedcvkyglgcavrhgCYRNSRLQTLMSAAILK 164
Cdd:cd03819 80 IHAH--SRAPAWLGWLASRLTGVPLVTTVHG--------------------------------SYLATYHPKDFALAVRA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 165 MYRllgtyrrlFYICLTDFNKEKLLllnqgGRTIVREERVFVKSN------FVWRP------QIREVERKEQYLYVGRLE 232
Cdd:cd03819 126 RGD--------RVIAVSELVRDHLI-----EALGVDPERIRVIPNgvdtdrFPPEAeaeeraQLGLPEGKPVVGYVGRLS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 233 DLKGVRFLVRT---WRDFPDRRLLLCGSGPEEAWIRSYISENRMSQ-IELLGqvSHDEVMRLAAESRALIMPTMcYEGQG 308
Cdd:cd03819 193 PEKGWLLLVDAaaeLKDEPDFRLLVAGDGPERDEIRRLVERLGLRDrVTFTG--FREDVPAALAASDVVVLPSL-HEEFG 269
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1199425881 309 LVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAVR 355
Cdd:cd03819 270 RVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALADAIR 316
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
6-383 |
2.45e-24 |
|
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: 102.67 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 6 KILLVHNHykiPGGEDTVVSNEKRLLEEHGHKVILYSRSNQEMQD------FSVWQKLML--PFTSLFSLRTYRDVKALL 77
Cdd:cd03808 1 KILFIVNV---DGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDelkelgVKVIDIPILrrGINPLKDLKALFKLYKLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 78 KKERVDIVHVHnTLNlvsPSVY--YAAFSLRVP-VVQTLHnfrllcpaatfvrdgricedcvkyGLGCAVrhgcYRNSRL 154
Cdd:cd03808 78 KKEKPDIVHCH-TPK---PGILgrLAARLAGVPkVIYTVH------------------------GLGFVF----TEGKLL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 155 QTLmsaaILKMYRLLGTYRRLfYICLTDFNKEklLLLNQGGRTIvrEERVFVKSNFV----WRPQIrEVERKEQY--LYV 228
Cdd:cd03808 126 RLL----YLLLEKLALLFTDK-VIFVNEDDRD--LAIKKGIIKK--KKTVLIPGSGVdldrFQYSP-ESLPSEKVvfLFV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 229 GRLEDLKGVRFLVRTWRD----FPDRRLLLCGSGPEE----AWIRSYISENRmsqIELLGQVShdEVMRLAAESRALIMP 300
Cdd:cd03808 196 ARLLKDKGIDELIEAAKIlkkkGPNVRFLLVGDGELEnpseILIEKLGLEGR---IEFLGFRS--DVPELLAESDVFVLP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 301 TMcYEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAVRKF-EEAKAWDT-----RPTYEKYYS 374
Cdd:cd03808 271 SY-REGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKLiEDPELRKEmgeaaRKRVEEKFD 349
|
....*....
gi 1199425881 375 PEKNYEKLK 383
Cdd:cd03808 350 EEKVVNKLL 358
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
6-399 |
2.24e-22 |
|
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: 97.04 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 6 KILLVHNHYKIPGGEdTVVSNEKRLLEEHGHKVILYSRSN----------QEMQDFSVWQKLmlPFTSLFSLRTYRDVKA 75
Cdd:cd03811 1 KILFVIPSLSGGGAE-RVLLNLANALDKRGYDVTLVLLRDegdldkqlngDVKLIRLLIRVL--KLIKLGLLKAILKLKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 76 LLKKERVDIVHVHNTLnlvSPSVYYAAFSLRVPVVQTLHNFrllcpaatfvrdgricedcvkyglgcavrhgcYRNSRLQ 155
Cdd:cd03811 78 ILKRAKPDVVISFLGF---ATYIVAKLAAARSKVIAWIHSS--------------------------------LSKLYYL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 156 TLMSAAILKMYRLlGTYrrlfYICLTDFNKEKLLLLNqggrtIVREERVFVKSNFVWRPQIREVERKEQY---------L 226
Cdd:cd03811 123 KKKLLLKLKLYKK-ADK----IVCVSKGIKEDLIRLG-----PSPPEKIEVIYNPIDIDRIRALAKEPILnepedgpviL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 227 YVGRLEDLKGVRFLVRTWRDF----PDRRLLLCGSGPEEAWIRSYISENRMS-QIELLGQVShdEVMRLAAESRALIMPT 301
Cdd:cd03811 193 AVGRLDPQKGHDLLIEAFAKLrkkyPDVKLVILGDGPLREELEKLAKELGLAeRVIFLGFQS--NPYPYLKKADLFVLSS 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 302 McYEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAVRKFEEAkawdtrptyekyyspeKNYEK 381
Cdd:cd03811 271 R-YEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQK----------------KLDAA 333
|
410
....*....|....*...
gi 1199425881 382 LKEIYDRAEEILSREKRI 399
Cdd:cd03811 334 LRERLAKAQEAVFREYTI 351
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
65-389 |
2.63e-22 |
|
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: 97.45 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 65 FSLRTYRDVKALLKKERVDIVHVHNTLnlvsPSVYYA---AFSLRVPVVQTLHnfrllcpaatfvrdgriCEDCVKYglg 141
Cdd:cd03798 79 LRAPSLAKLLKRRRRGPPDLIHAHFAY----PAGFAAallARLYGVPYVVTEH-----------------GSDINVF--- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 142 cavrhgcyRNSRLQTLMSAAILKMYRLLgtyrrlfyICLTDFNKEKLLLLnqggrtIVREERVFVKSNFV----WRPQIR 217
Cdd:cd03798 135 --------PPRSLLRKLLRWALRRAARV--------IAVSKALAEELVAL------GVPRDRVDVIPNGVdparFQPEDR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 218 EVERKEQY---LYVGRLEDLKGVRFLV----RTWRDFPDRRLLLCGSGPEEAWIRSYISENRM-SQIELLGQVSHDEVMR 289
Cdd:cd03798 193 GLGLPLDAfviLFVGRLIPRKGIDLLLeafaRLAKARPDVVLLIVGDGPLREALRALAEDLGLgDRVTFTGRLPHEQVPA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 290 LAAESRALIMPTMcYEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAVRKfEEAKAWDT---- 365
Cdd:cd03798 273 YYRACDVFVLPSR-HEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRR-ALAEPYLRelge 350
|
330 340
....*....|....*....|....*.
gi 1199425881 366 --RPTYEKYYSPEKNYEKLKEIYDRA 389
Cdd:cd03798 351 aaRARVAERFSWVKAADRIAAAYRDV 376
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
226-356 |
1.24e-21 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 89.88 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 226 LYVGRL-EDLKGVRFLVRTW----RDFPDRRLLLCGSGPEEaWIRSYISENRmSQIELLGQVshDEVMRLAAESRALIMP 300
Cdd:pfam13692 5 LFVGRLhPNVKGVDYLLEAVpllrKRDNDVRLVIVGDGPEE-ELEELAAGLE-DRVIFTGFV--EDLAELLAAADVFVLP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199425881 301 TMcYEGQGLVLLESYAVGTPVLASALGNVGNIVIpNVTGLRFAAGDAEALKEAVRK 356
Cdd:pfam13692 81 SL-YEGFGLKLLEAMAAGLPVVATDVGGIPELVD-GENGLLVPPGDPEALAEAILR 134
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
220-360 |
6.27e-21 |
|
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: 93.12 E-value: 6.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 220 ERKEQYLYVGRLEDLKGVRFLVRTWRDFPdRRLLLCGSGPEEAWIRSYISENrmsqIELLGQVSHDEVMRLAAESRALIM 299
Cdd:cd03804 197 DKEDYYLTASRLVPYKRIDLAVEAFNELP-KRLVVIGDGPDLDRLRAMASPN----VEFLGYQPDEVLKELLSKARAFVF 271
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199425881 300 PTMcyEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAVRKFEEA 360
Cdd:cd03804 272 AAE--EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEFEQN 330
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
177-354 |
5.41e-20 |
|
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: 90.59 E-value: 5.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 177 YICLTDFNKEKLLllnQGGrtiVREERVFVK------SNFVWRPqirEVERKEQYLYVGRLEDLKGVRFLVRTWRDF--- 247
Cdd:cd05844 147 FVAVSGFIRDRLL---ARG---LPAERIHVHyigidpAKFAPRD---PAERAPTILFVGRLVEKKGCDVLIEAFRRLaar 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 248 -PDRRLLLCGSGPEEAWIRSYISenRMSQIELLGQVSHDEVMRLAAESRALIMPTMC-----YEGQGLVLLESYAVGTPV 321
Cdd:cd05844 218 hPTARLVIAGDGPLRPALQALAA--ALGRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdSEGLGIVLLEAAACGVPV 295
|
170 180 190
....*....|....*....|....*....|...
gi 1199425881 322 LASALGNVGNIVIPNVTGLRFAAGDAEALKEAV 354
Cdd:cd05844 296 VSSRHGGIPEAILDGETGFLVPEGDVDALADAL 328
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
6-357 |
3.60e-18 |
|
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: 84.98 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 6 KILLVHNHYKIPGGEDTVVSNEKRLLEEHGHKVILYSRSNQEMQDF-----SV-WQKLMLPFTSLFS-----LRTYRDVK 74
Cdd:cd03820 1 KIAIVIPSISNAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFyelddNIkIKNLGDRKYSHFKlllkyFKKVRRLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 75 ALLKKERVDIVHVHNTLNLVSPsvyyAAFSLRVPVVQTLHNfrllCPAATFVRDGRIcedcvkyglgcAVRHGCYRN-SR 153
Cdd:cd03820 81 KYLKNNKPDVVISFRTSLLTFL----ALIGLKSKLIVWEHN----NYEAYNKGLRRL-----------LLRRLLYKRaDK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 154 LQTLMSAAILKMYRLLGTyrrlfyicltdfnkekllllnqggrtivreeRVFVKSNFV---WRPQIREVERKeQYLYVGR 230
Cdd:cd03820 142 IVVLTEADKLKKYKQPNS-------------------------------NVVVIPNPLsfpSEEPSTNLKSK-RILAVGR 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 231 LEDLKGVRFLVRTWR----DFPDRRLLLCGSGPEEAWIRSYISENRMSQ-IELLGQVSH-DEVMRlaaESRALIMPTMcY 304
Cdd:cd03820 190 LTYQKGFDLLIEAWAliakKHPDWKLRIYGDGPEREELEKLIDKLGLEDrVKLLGPTKNiAEEYA---NSSIFVLSSR-Y 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1199425881 305 EGQGLVLLESYAVGTPVLASALgNVG--NIVIPNVTGLRFAAGDAEALKEAVRKF 357
Cdd:cd03820 266 EGFPMVLLEAMAYGLPIISFDC-PTGpsEIIEDGENGLLVPNGDVDALAEALLRL 319
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
6-397 |
4.16e-17 |
|
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
Pssm-ID: 340825 [Multi-domain] Cd Length: 391 Bit Score: 82.39 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 6 KILLVHNHYKIP-GGEDTVVSNEKRLLEEHGHKVILYSRSNQEMQDFS------------VWQKLMLPFT---------- 62
Cdd:cd03794 1 KILLISQYYPPPkGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIfagatetkdgirVIRVKLGPIKknglirrlln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 63 -SLFSLRTYRdvKALLKKERVDIVHVHNTLNLVSPSVYYAAFSLRVPVVqtlHNFRLLCPaatfvrdgricedcvkyglg 141
Cdd:cd03794 81 yLSFALAALL--KLLVREERPDVIIAYSPPITLGLAALLLKKLRGAPFI---LDVRDLWP-------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 142 cavrhgcyrnsrlQTLMSAAILK---MYRLLGTYRRLFY------ICLTDFNKEKLLllnqggRTIVREERVFVKSNFV- 211
Cdd:cd03794 136 -------------ESLIALGVLKkgsLLKLLKKLERKLYrladaiIVLSPGLKEYLL------RKGVPKEKIIVIPNWAd 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 212 ---WRPQIREVERKEQ-------YLYVGRLEDLKGVRFLVRTW---RDFPDRRLLLCGSGPEEAWIRSYISENRMSQIEL 278
Cdd:cd03794 197 leeFKPPPKDELRKKLglddkfvVVYAGNIGKAQGLETLLEAAerlKRRPDIRFLFVGDGDEKERLKELAKARGLDNVTF 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 279 LGQVSHDEVMRLAAESRALIMPTMCYEGQGLV----LLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAV 354
Cdd:cd03794 277 LGRVPKEEVPELLSAADVGLVPLKDNPANRGSspskLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAI 356
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1199425881 355 rkfeeakawdtrptyEKYYSPEKNYEKLKE-IYDRAEEILSREK 397
Cdd:cd03794 357 ---------------LELLDDPELRRAMGEnGRELAEEKFSREK 385
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
217-397 |
1.36e-16 |
|
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: 80.40 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 217 REVERKEQYLYVGRLEDLKGVRFLVRTWR--DFPdrrLLLCGSGPEEAWIRSYISENRMSQIELLGQVSHDEVMRLAAES 294
Cdd:cd03795 186 REKKGKKIFLFIGRLVYYKGLDYLIEAAQylNYP---IVIGGEGPLKPDLEAQIELNLLDNVKFLGRVDDEEKVIYLHLC 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 295 RALIMPTMC-YEGQGLVLLESYAVGTPVLASALGNVGN-IVIPNVTGLRFAAGDAEALKEAVRKFEEakawDTrptyEKY 372
Cdd:cd03795 263 DVFVFPSVLrSEAFGIVLLEAMMCGKPVISTNIGTGVPyVNNNGETGLVVPPKDPDALAEAIDKLLS----DE----ELR 334
|
170 180
....*....|....*....|....*
gi 1199425881 373 YSPEKNYEKlkeiydRAEEILSREK 397
Cdd:cd03795 335 ESYGENAKK------RFEELFTAEK 353
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
199-356 |
2.24e-15 |
|
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: 76.63 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 199 VREERVFVKSNFV---WRPQIREVERKEQY-------LYVGRLEDLKGVRFLVRTWRDFPDRR-----LLLCGSGPE-EA 262
Cdd:cd03809 159 VPPEKIVVIPLGVdpsFFPPESAAVLIAKYllpepyfLYVGTLEPRKNHERLLKAFALLKKQGgdlklVIVGGKGWEdEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 263 WIRSYISENRMSQIELLGQVSHDEVMRLAAESRALIMPTMcYEGQGLVLLESYAVGTPVLASalgnvgNI-VIPNVTG-- 339
Cdd:cd03809 239 LLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSL-YEGFGLPVLEAMACGTPVIAS------NIsVLPEVAGda 311
|
170
....*....|....*...
gi 1199425881 340 -LRFAAGDAEALKEAVRK 356
Cdd:cd03809 312 aLYFDPLDPESIADAILR 329
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
17-382 |
8.47e-15 |
|
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.
Pssm-ID: 340832 [Multi-domain] Cd Length: 333 Bit Score: 74.63 E-value: 8.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 17 PGGEDTVVSNEKRLLEEHGHKVILYSRSNQEMQ--DFSVWQKLMLPFTSLFSLRTYRDVKALLKKER---VDIVHVHntl 91
Cdd:cd03802 17 YGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSapLVAVIPRALRLDPIPQESKLAELLEALEVQLRasdFDVIHNH--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 92 nLVSPSVYYAAFsLRVPVVQTLHNFrllcpaatfvrdgricedcvkyglgcavrhgcyrnsrlqtlmsaAILKMYRLLGT 171
Cdd:cd03802 94 -SYDWLPPFAPL-IGTPFVTTLHGP--------------------------------------------SIPPSLAIYAA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 172 YRRLFYICLTDFNKEKLLLLNQGGrtivreervFVKSNFVWRPQIREVERKEQYLYVGRLEDLKGVRFLVRTWRDfPDRR 251
Cdd:cd03802 128 EPPVNYVSISDAQRAATPPIDYLT---------VVHNGLDPADYRFQPDPEDYLAFLGRIAPEKGLEDAIRVARR-AGLP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 252 LLLCGSGPEEAWIRSYISENRMSQIELLGQVSHDEVMRLAAESRALIMPTMCYEGQGLVLLESYAVGTPVLASALGNVGN 331
Cdd:cd03802 198 LKIAGKVRDEDYFYYLQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPE 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1199425881 332 IVIPNVTGlrFAAGDAEALKEAVRKFEEAKAWDTRPTYEKYYSPE---KNYEKL 382
Cdd:cd03802 278 VIQHGETG--FLVDSVEEMAEAIANIDRIDRAACRRYAEDRFSAArmaDRYEAL 329
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
284-389 |
9.79e-15 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 70.02 E-value: 9.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 284 HDEVMRLA-AESRALIMPTmCYEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAVRKF-EEAK 361
Cdd:COG0438 10 LDLLLEALlAAADVFVLPS-RSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLlEDPE 88
|
90 100 110
....*....|....*....|....*....|...
gi 1199425881 362 AWDT-----RPTYEKYYSPEKNYEKLKEIYDRA 389
Cdd:COG0438 89 LRRRlgeaaRERAEERFSWEAIAERLLALYEEL 121
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
17-357 |
3.65e-14 |
|
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: 73.12 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 17 PGGEDTVVsneKRLLEE-----HGHKVILYSRS---NQEMQDFSVwQKLMLPFTSLFSLRTYRDVKALLKKERVDIVHVH 88
Cdd:cd03807 11 VGGAETML---LRLLEHmdksrFEHVVISLTGDgvlGEELLAAGV-PVVCLGLSSGKDPGVLLRLAKLIRKRNPDVVHTW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 89 NtlnlvspsvYYAAFSLR--------VPVVQTLHN----------FRLLCPAATFVRDGRICEdcvkyglgcavrhgcyr 150
Cdd:cd03807 87 M---------YHADLIGGlaaklaggVKVIWSVRSsnipqrltrlVRKLCLLLSKFSPATVAN----------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 151 nsrlqtlmSAAILKMYRLLGTYRRLFYICLTDFNKEKLLLlNQGGRTIVREERVFVKSNFVwrpqireverkeqYLYVGR 230
Cdd:cd03807 141 --------SSAVAEFHQEQGYAKNKIVVIYNGIDLFKLSP-DDASRARARRRLGLAEDRRV-------------IGIVGR 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 231 LEDLKGVRFLVRTWR----DFPDRRLLLCGSGPE----EAWIRSYISENRmsqIELLGQVSHdeVMRLAAESRALIMPTm 302
Cdd:cd03807 199 LHPVKDHSDLLRAAAllveTHPDLRLLLVGRGPErpnlERLLLELGLEDR---VHLLGERSD--VPALLPAMDIFVLSS- 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1199425881 303 CYEGQGLVLLESYAVGTPVLASALGNVGNIVIPNvTGLRFAAGDAEALKEAVRKF 357
Cdd:cd03807 273 RTEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPAGDPQALADAIRAL 326
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
17-365 |
3.43e-13 |
|
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: 70.35 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 17 PGGEDT------VVSNEKRLLEEhGHKVILYSRSNQEMQDFSV------------------WQKLMLP-----FTSlFSL 67
Cdd:cd03800 15 PGGADTggqnvyVLELARALAEL-GYQVDIFTRRISPADPEVVeiapgarvirvpagppeyLPKEELWpyleeFAD-GLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 68 RTYRDVKAllkkeRVDIVHVHNTL-NLVSpsvYYAAFSLRVPVVQTLHNF-----RLLCPAATFVRDGRI-CEDCVkygl 140
Cdd:cd03800 93 RFIAREGG-----RYDLIHSHYWDsGLVG---ALLARRLGVPLVHTFHSLgrvkyRHLGAQDTYHPSLRItAEEQI---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 141 gcavrhgcYRNS-RLQTLMSAAILKMYRLLGTYRRLFYI--CLTDFNkekllLLNQGGRTIVREERvfvksnFVWRPQIR 217
Cdd:cd03800 161 --------LEAAdRVIASTPQEADELISLYGADPSRINVvpPGVDLE-----RFFPVDRAEARRAR------LLLPPDKP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 218 EVerkeqyLYVGRLEDLKGVRFLVRTWRDFPDRR----LLLCG-------SGPEEAwIRSYISENRMS-QIELLGQVSHD 285
Cdd:cd03800 222 VV------LALGRLDPRKGIDTLVRAFAQLPELRelanLVLVGgpsddplSMDREE-LAELAEELGLIdRVRFPGRVSRD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 286 EVMRLAAESRALIMPTMcYEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAVRK-FEEAKAWD 364
Cdd:cd03800 295 DLPELYRAADVFVVPSL-YEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRlLDDPALWQ 373
|
.
gi 1199425881 365 T 365
Cdd:cd03800 374 R 374
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
226-355 |
3.73e-13 |
|
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: 70.02 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 226 LYVGRLEDLKGVRFLVRTWRDFPDR---RLLLCGSGPEEAWIRSyisenRMSQIELLGQVSHDEVMRLAAESRALIMP-- 300
Cdd:cd03814 202 LYVGRLAPEKNLEALLDADLPLAASppvRLVVVGDGPARAELEA-----RGPDVIFTGFLTGEELARAYASADVFVFPsr 276
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1199425881 301 TmcyEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAVR 355
Cdd:cd03814 277 T---ETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALR 328
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
6-394 |
7.21e-13 |
|
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: 69.23 E-value: 7.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 6 KILLVHNHYK-IPGGEDTVVSNEKRLLEEHGHKV---------------ILYSRSNQEMQDFSVWQKLMLPFTSLfslrt 69
Cdd:cd03817 1 KIAIFTDTYLpQVNGVATSVRNLARALEKRGHEVyvitpsdpgaedeeeVVRYRSFSIPIRKYHRQHIPFPFKKA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 70 yrdVKALLKKERVDIVHVHNTLNLVSPSVYYAAfSLRVPVVQTLHnfrllcpaaTFVrdgricEDCVKYGLGcavrhgcy 149
Cdd:cd03817 76 ---VIDRIKELGPDIIHTHTPFSLGKLGLRIAR-KLKIPIVHTYH---------TMY------EDYLHYIPK-------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 150 rnsrLQTLMSAAILKMYRLLGTYRRLFyICLTDFNKEKLLLLNQGGRtivreerVFVKSN----FVWRPQIREVERKEQY 225
Cdd:cd03817 129 ----GKLLVKAVVRKLVRRFYNHTDAV-IAPSEKIKDTLREYGVKGP-------IEVIPNgidlDKFEKPLNTEERRKLG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 226 --------LYVGRLEDLKGVRFLVRTWRDF---PDRRLLLCGSGPEEAWIRSYISENRMS-QIELLGQVSHDEVMRLAAE 293
Cdd:cd03817 197 lppdepilLYVGRLAKEKNIDFLLRAFAELkkePNIKLVIVGDGPEREELKELARELGLAdKVIFTGFVPREELPEYYKA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 294 SRALIMPTMcYEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAealkEAVRKFEEAKAwdtrpTYEKYY 373
Cdd:cd03817 277 ADLFVFAST-TETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDE----TLAEKLLHLRE-----NLELLR 346
|
410 420
....*....|....*....|.
gi 1199425881 374 SPEKNYEKLKEIYDRAEEILS 394
Cdd:cd03817 347 KLSKNAEISAREFAFAKSVEK 367
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
208-342 |
1.10e-11 |
|
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: 64.35 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 208 SNFVWRPQIREVERKEQYLYVGRLEDLKGVRFLVRTWR----DFPDRRLLLCGSGPEEAWIRSYISENR-MSQIELLGQV 282
Cdd:cd01635 96 SELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALAllkaRLPDLVLVLVGGGGEREEEEALAAALGlLERVVIIGGL 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199425881 283 SHDEVMR-LAAESRALIMPTMcYEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRF 342
Cdd:cd01635 176 VDDEVLElLLAAADVFVLPSR-SEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
66-388 |
7.96e-11 |
|
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: 63.12 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 66 SLRTYRDVKALLKK---ERVDIVHVHNtlnLVSPSVYYAA---FSLRVPVVQTLHNFRLLCpaatfvrdGRiC---EDCV 136
Cdd:cd03825 33 STMLVGRKKNLISKpefIEADIIHLHW---IHGGYLSLKAlfkLLRRKPVVWTLHDMWPFT--------GG-ChypMECE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 137 KYGLGCAVRHGCYRNSRLQTLMSAAILKMYRLLGTYRRLFYICLTDFNKEKLLllnqgGRTIVREERVFVKSNFV----W 212
Cdd:cd03825 101 GWKTGCGNCPNLNSYPPAKKDLSRQLFRRKREALAKKRLTIVAPSRWLADMVR-----RSPLLKGLPVVVIPNGIdteiF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 213 RPQIREVERK----EQYLYVG-----RLEDL-KGVRFLVRTWRDFPDRR---LLLCGSGPEEAWIRSyisenrmSQIELL 279
Cdd:cd03825 176 APVDKAKARKrlgiPQDKKVIlfgaeSVTKPrKGFDELIEALKLLATKDdllLVVFGKNDPQIVILP-------FDIISL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 280 GQVSHDEVMRLA-AESRALIMPTMcYEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAVRKF- 357
Cdd:cd03825 249 GYIDDDEQLVDIySAADLFVHPSL-ADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLl 327
|
330 340 350
....*....|....*....|....*....|....*...
gi 1199425881 358 -------EEAKAwdTRPTYEKYYSPEKNYEKLKEIYDR 388
Cdd:cd03825 328 anpkereSLGER--ARALAENHFDQRVQAQRYLELYKD 363
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
226-359 |
1.17e-09 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 59.72 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 226 LYVGRLEDLKGVRFLVRTWRDFPDRRLLLCGSGPEEAWIRSYISENRMSqieLLGQVSHDEVMRLAAESRALIMPTMCyE 305
Cdd:PLN02871 267 VYVGRLGAEKNLDFLKRVMERLPGARLAFVGDGPYREELEKMFAGTPTV---FTGMLQGDELSQAYASGDVFVMPSES-E 342
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199425881 306 GQGLVLLESYAVGTPVLASALGNVGNIVIP---NVTGLRFAAGDAEalkEAVRKFEE 359
Cdd:PLN02871 343 TLGFVVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGDVD---DCVEKLET 396
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
78-389 |
1.57e-09 |
|
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: 58.90 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 78 KKERVDIVHVHNTLNLVSpSVYYAA--FSLRVPVVQTLHNFRLlcpaaTFVRDGRICEDcvkyglgcAVRHGCYRNSRLQ 155
Cdd:cd04962 81 KEHKLDVLHAHYAIPHAS-CAYLAReiLGEKIPIVTTLHGTDI-----TLVGYDPSLQP--------AVRFSINKSDRVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 156 TLMSAAILKMYRLLGTYRRLFYI-CLTDFNKEKLLLlnqgGRTIVR------EERVFVK-SNFvwRPqireverkeqyly 227
Cdd:cd04962 147 AVSSSLRQETYELFDVDKDIEVIhNFIDEDVFKRKP----AGALKRrllappDEKVVIHvSNF--RP------------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 228 VGRLEDLkgVRFLVRTWRDFPDRrLLLCGSGPE----EAWIRSYISENRmsqIELLGQVshDEVMRLAAESRALIMPTMc 303
Cdd:cd04962 208 VKRIDDV--VRVFARVRRKIPAK-LLLVGDGPErvpaEELARELGVEDR---VLFLGKQ--DDVEELLSIADLFLLPSE- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 304 YEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEAL-KEAVRKFEEAKAWD-----TRPTYEKYYSPEK 377
Cdd:cd04962 279 KESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMaKSALSILEDDELYNrmgraARKRAAERFDPER 358
|
330
....*....|..
gi 1199425881 378 NYEKLKEIYDRA 389
Cdd:cd04962 359 IVPQYEAYYRRL 370
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
59-324 |
4.62e-09 |
|
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: 57.68 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 59 LPFTSLFSLRTYRDVKALLKKERVDIVHVHNTLNLVSpsVYYAAFSLRVPVvqtlhnfrllcpaatfvrdgRICedcvky 138
Cdd:cd03812 58 IPPKKKNIIKYFIKLLKLIKKEKYDIVHVHGSSSNGI--ILLLAAKAGVPV--------------------RIA------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 139 glgcavrHgcyrnSRLQTLMSAAILKMyrLLGTYRRLFYI-------CLTDFNKEkLLLLNQGGRTIVREERVFVKsNFV 211
Cdd:cd03812 110 -------H-----SHNTKDSSIKLRKI--RKNVLKKLIERlstkylaCSEDAGEW-LFGEVENGKFKVIPNGIDIE-KYK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 212 WRPQIREVERKEQYL-------YVGRLEDLKGVRFLVRTWRDFPDR----RLLLCGSGPEEAWIRSYISENRMSQ-IELL 279
Cdd:cd03812 174 FNKEKRRKRRKLLILedklvlgHVGRFNEQKNHSFLIDIFEELKKKnpnvKLVLVGEGELKEKIKEKVKELGLEDkVIFL 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1199425881 280 GQVShdEVMRLAAESRALIMPTMcYEGQGLVLLESYAVGTPVLAS 324
Cdd:cd03812 254 GFRN--DVSEILSAMDVFLFPSL-YEGLPLVAVEAQASGLPCLLS 295
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
213-362 |
1.54e-08 |
|
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: 55.84 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 213 RPQIREVERKEQYLYVGRLEDLKGVRFLVRTWRD----FPDRRLLLCGSGP--EEAWIRSYISENRMSQIELLGQVSHDE 286
Cdd:cd03821 195 RRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKlaeqGRDWHLVIAGPDDgaYPAFLQLQSSLGLGDRVTFTGPLYGEA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 287 VMRLAAESRALIMPTMcYEGQGLVLLESYAVGTPVLAS------ALGNVGN--IVIPNVTGLrfaagdAEALKEAVRKFE 358
Cdd:cd03821 275 KWALYASADLFVLPSY-SENFGNVVAEALACGLPVVITdkcglsELVEAGCgvVVDPNVSSL------AEALAEALRDPA 347
|
....
gi 1199425881 359 EAKA 362
Cdd:cd03821 348 DRKR 351
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
172-352 |
1.75e-08 |
|
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: 55.53 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 172 YRRLF-----YICLTDFNKEKLLLLNQGGRTIVREERVFVKSNFVWRPQIREVERKEQYLYVGRLEDLKGVRFLVRTWRD 246
Cdd:cd03799 119 YPQLFaqgdlFLPNCELFKHRLIALGCDEKKIIVHRSGIDCNKFRFKPRYLPLDGKIRILTVGRLTEKKGLEYAIEAVAK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 247 ----FPDRRLLLCGSGPEEAWIRSYISE-NRMSQIELLGQVSHDEVMRLAAESRALIMPTMC-----YEGQGLVLLESYA 316
Cdd:cd03799 199 laqkYPNIEYQIIGDGDLKEQLQQLIQElNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTaadgdQDGPPNTLKEAMA 278
|
170 180 190
....*....|....*....|....*....|....*.
gi 1199425881 317 VGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKE 352
Cdd:cd03799 279 MGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAE 314
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
18-115 |
3.72e-08 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 52.53 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 18 GGEDTVVSNEKRLLEEHGHKVILYSRSNQEMQDFSVW-------QKLMLPFTSLFSLRTYRDVKALLKKERVDIVHVHnT 90
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVrvvrvprVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAH-S 79
|
90 100
....*....|....*....|....*
gi 1199425881 91 LNLVSPSVYYAAFSLRVPVVQTLHN 115
Cdd:pfam13439 80 PFPLGLAALAARLRLGIPLVVTYHG 104
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
228-387 |
2.46e-07 |
|
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: 52.34 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 228 VGRLEDLKGVRFLVRTW----RDFPDRRLLLCGSGPEEAwirSYISENRM--SQIELLGQVSHDEVMRLAAESR--ALIM 299
Cdd:cd03813 299 VGRVVPIKDVKTFIRAFklvrRAMPDAEGWLIGPEDEDP---EYAQECKRlvASLGLENKVKFLGFQNIKEYYPklGLLV 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 300 PTMCYEGQGLVLLESYAVGTPVLASALGNVGNIV-----IPNVTGLRFAAGDAEALKEAVRKFEEAKA-WDT-----RPT 368
Cdd:cd03813 376 LTSISEGQPLVILEAMASGVPVVATDVGSCRELIygaddALGQAGLVVPPADPEALAEALIKLLRDPElRQAfgeagRKR 455
|
170
....*....|....*....
gi 1199425881 369 YEKYYSPEKNYEKLKEIYD 387
Cdd:cd03813 456 VEKYYTLEGMIDSYRKLYL 474
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
228-354 |
4.38e-06 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 48.88 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 228 VGRLEDLKGVRFLVRTWRDF----PDRRLLLCGSGPEEAWIRSYISENRMSQIELLGQVSHDEVMRLAAESRALIMPTmc 303
Cdd:PRK15179 523 VMRVDDNKRPFLWVEAAQRFaashPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSR-- 600
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1199425881 304 YEGQGLVLLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEA--LKEAV 354
Cdd:PRK15179 601 FEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTApdVAEAL 653
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
199-392 |
1.37e-05 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 46.63 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 199 VREERVFV-------KSNFVWRPqirEVERKEQYLYVGRL---------EDLKGVRFLVRTWRdfpdrrLLLCGSGPEEA 262
Cdd:PRK09922 153 ISAQRISViynpveiKTIIIPPP---ERDKPAVFLYVGRLkfegqknvkELFDGLSQTTGEWQ------LHIIGDGSDFE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 263 WIRSYISENRMSQ-IELLGQVSH--DEVMRLAAESRALIMpTMCYEGQGLVLLESYAVGTPVLAS-ALGNVGNIVIPNVT 338
Cdd:PRK09922 224 KCKAYSRELGIEQrIIWHGWQSQpwEVVQQKIKNVSALLL-TSKFEGFPMTLLEAMSYGIPCISSdCMSGPRDIIKPGLN 302
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199425881 339 GLRFAAGDAEALKEAVRKFEEAKAW----DTRPTYEKYYSpEKNYEKLKEIYDRAEEI 392
Cdd:PRK09922 303 GELYTPGNIDEFVGKLNKVISGEVKyqhdAIPNSIERFYE-VLYFKNLNNALFSKLQK 359
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
18-118 |
2.69e-05 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 43.93 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 18 GGEDTVVSNEKRLLEEHGHKVILYSRSNQEMQDFSVWQKLM-----LPFTS--LFSLRTYRDVKALLKKERVDIVHVHNT 90
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRvhrlpVPPRPspLADLAALRRLRRLLRAERPDVVHAHSP 80
|
90 100
....*....|....*....|....*...
gi 1199425881 91 LNlvSPSVYYAAFSLRVPVVQTLHNFRL 118
Cdd:pfam13579 81 TA--GLAARLARRRRGVPLVVTVHGLAL 106
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
6-114 |
9.85e-05 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 41.92 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 6 KILLVHNHykiPGGEDTVVSNEkrlLEEHGHKVILYSRSNQEMQ----DFSVWQKLMLPFTSLFSLRTYRDVKALLKKER 81
Cdd:pfam13477 1 KILLLANA---DSIHTLRWADA---LADRGYDVHVISSKGPAKDeliaEGIHVHRLKVPRKGPLGYLKAFRLKKLIKKIK 74
|
90 100 110
....*....|....*....|....*....|....*..
gi 1199425881 82 VDIVHVHNTlnlvSPSVYYAAFSLR----VPVVQTLH 114
Cdd:pfam13477 75 PDVVHVHYA----KPYGLLAGLAARlsgfPPVVLSAW 107
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
18-333 |
1.18e-04 |
|
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: 43.97 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 18 GGEDTVVSNEKRLLEEHGHKV-ILYSRSNQE---MQDFSVWQKLMLPFTSLFSLRTYRDVKALLKKERVDIVHVHntlnl 93
Cdd:cd04951 12 GGAEKQTVLLADQMFIRGHDVnIVYLTGEVEvkpLNNNIIIYNLGMDKNPRSLLKALLKLKKIISAFKPDVVHSH----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 94 vspsVYYAAFSLRVPVVqTLHNFRLLCPAATFVRDGRIcedcvkyglgcavRHGCYRnsrLQTLMSAAILKMYRLLGTYr 173
Cdd:cd04951 87 ----MFHANIFARFLRM-LYPIPLLICTAHNKNEGGRI-------------RMFIYR---LTDFLCDITTNVSREALDE- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 174 rlfYICLTDFNKEKLLLLNQGGRTIVREERVFVKSNFvwRPQIREVERKEQYLYVGRLEDLKGVRFLVRTWRDF----PD 249
Cdd:cd04951 145 ---FIAKKAFSKNKSVPVYNGIDLNKFKKDINVRLKI--RNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELilskND 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 250 RRLLLCGSGPEEAWIRSYISENRMSQ-IELLGQVSHDEVMRLAAEsraLIMPTMCYEGQGLVLLESYAVGTPVLASALGN 328
Cdd:cd04951 220 FKLLIAGDGPLRNELERLICNLNLVDrVILLGQISNISEYYNAAD---LFVLSSEWEGFGLVVAEAMACERPVVATDAGG 296
|
....*
gi 1199425881 329 VGNIV 333
Cdd:cd04951 297 VAEVV 301
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
227-354 |
5.59e-04 |
|
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: 41.96 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 227 YVGR-LEDLKG----VRFLVRTWRDFPDRRLLLCGS-----GPE----EAWIRSYISENRM--SQIELLGQVSHDEVMRL 290
Cdd:cd03818 218 YVARnLEPYRGfhvfMRALPRIQARRPDARVVVVGGdgvsyGSPppdgGSWKQKMLAELGVdlERVHFVGKVPYDQYVRL 297
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199425881 291 AAESRALIMPTMCYegqglV----LLESYAVGTPVLASALGNVGNIVIPNVTGLRFAAGDAEALKEAV 354
Cdd:cd03818 298 LQLSDAHVYLTYPF-----VlswsLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAV 360
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
227-386 |
5.60e-04 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 41.78 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 227 YVGRLEDLKGVRFLVRTWRDFPDR--RLLLCGSGPE--EAWIRSYISE--NRMSqiellGQVSHDEVM--RLAAESRALI 298
Cdd:cd03791 299 FVGRLTEQKGVDLILDALPELLEEggQLVVLGSGDPeyEQAFRELAERypGKVA-----VVIGFDEALahRIYAGADFFL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 299 MPTMcYEGQGLVLLESYAVGTPVLASALGNVGNIVIPNV------TGLRFAAGDAEALKEAVRKFeeAKAWDTRPTYEKY 372
Cdd:cd03791 374 MPSR-FEPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYDpetgegTGFVFEDYDAEALLAALRRA--LALYRNPELWRKL 450
|
170 180
....*....|....*....|..
gi 1199425881 373 --------YSPEKNYEKLKEIY 386
Cdd:cd03791 451 qknamkqdFSWDKSAKEYLELY 472
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
155-381 |
3.12e-03 |
|
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: 39.21 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 155 QTLMSAAILKMYR--LLGTYRRLFYICLTDfnKEKLLLLNQGGRTI-VREERVFVKSNFVwrPQIREVERKE-QYLYVGR 230
Cdd:cd04949 93 DDPEHSLIKNFYKyvFENLNKYDAIIVSTE--QQKQDLSERFNKYPpIFTIPVGYVDQLD--TAESNHERKSnKIITISR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 231 LEDLKGVRFLVRTW----RDFPDRRLLLCGSGPEEAWIRSYISENRMS-QIELLGqvSHDEVMRLAAESRALIMpTMCYE 305
Cdd:cd04949 169 LAPEKQLDHLIEAVakavKKVPEITLDIYGYGEEREKLKKLIEELHLEdNVFLKG--YHSNLDQEYQDAYLSLL-TSQME 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 306 GQGLVLLESYAVGTPVLASALgNVGN--IVIPNVTGLRFAAGDAEALKEAVRK-FEEAKAWDT--RPTYE--KYYSPEKN 378
Cdd:cd04949 246 GFGLTLMEAIGHGLPVVSYDV-KYGPseLIEDGENGYLIEKNNIDALADKIIElLNDPEKLQQfsEESYKiaEKYSTENV 324
|
...
gi 1199425881 379 YEK 381
Cdd:cd04949 325 MEK 327
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
31-399 |
6.16e-03 |
|
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: 38.37 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 31 LEEHGHKVILYSRSNQE----------MQDFSVWQKLMLP---FTSLFSLRTYrdVKALLKKERVDIVHVHNTLNLVSPS 97
Cdd:cd03796 27 LIKRGHKVIVITHAYGNrvgvryltngLKVYYLPFKVFYNqstLPTLFSTFPL--LRNILIRERIQIVHGHQAFSSLAHE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 98 VYYAAFSLRVPVVQTLHNFRLLCPAATFVRDgriceDCVKYGLGCaVRHgcyrnsrlqtlmsaailkmyrllgtyrrlfY 177
Cdd:cd03796 105 ALFHARTLGLKTVFTDHSLFGFADASSILTN-----KLLRFSLAD-IDH------------------------------V 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 178 ICLTDFNKEKLLLlnqggRTIVREERVFVKSN------FVWRPQIREVErKEQYLYVGRLEDLKGVRFLV----RTWRDF 247
Cdd:cd03796 149 ICVSHTSKENTVL-----RASLDPRIVSVIPNavdssdFTPDPSKPDPN-KITIVVISRLVYRKGIDLLVgiipRICKKH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 248 PDRRLLLCGSGPEEAWIRSYISENRM-SQIELLGQVSHDEVMRLAAESRALIMPTMCyEGQGLVLLESYAVGTPVLASal 326
Cdd:cd03796 223 PNVRFIIGGDGPKRIELEEMREKYQLqDRVELLGAVPHEEVRDVLVQGHIFLNTSLT-EAFCIAIVEAASCGLLVVST-- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199425881 327 gNVGNI--VIPNvTGLRFAAGDAEALkeaVRKFEEA------KAWDTRPTYE---KYYSPEKNYEKLKEIYDRAEE---- 391
Cdd:cd03796 300 -RVGGIpeVLPP-DMILLAEPDPEDI---VRKLEEAisilrtGKHDPWSFHNrvkKMYSWEDVARRTEKVYDRILStpnr 374
|
....*....
gi 1199425881 392 -ILSREKRI 399
Cdd:cd03796 375 pFLERLKRY 383
|
|
| |
