|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-402 |
1.56e-108 |
|
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: 324.68 E-value: 1.56e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 2 KILIVADVYPPEVSSAANLMQELAQGLKKRGHQITVVTSYPRYYLTEAFKEKKFQIfsdeEGINVIRIKVLPHHKVNFII 81
Cdd:cd03794 1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGATETK----DGIRVIRVKLGPIKKNGLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 82 RGISQLTLPFLFFAKIKKFIKEIEAVIVYSPPLPLALVGGMIKRHYGVKFILNIQDIFPQNAIDLGILKGwkhKPAIWIF 161
Cdd:cd03794 77 RLLNYLSFALAALLKLLVREERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKK---GSLLKLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 162 EAIEKKVYKDADKITFHSEGGKKFLIKKKnILPEKIITLHNWIDITPYQNLTKNiSFRKQYGLEGKFIFLFAGIMGPAQG 241
Cdd:cd03794 154 KKLERKLYRLADAIIVLSPGLKEYLLRKG-VPKEKIIVIPNWADLEEFKPPPKD-ELRKKLGLDDKFVVVYAGNIGKAQG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 242 LEFLVEVASQIIDLKDVIFLLVGDGTEKEKIENKIKEYGLKNIIIKPLVPKEDYPYLVKDANVGLVCLSFNNKTPF-LPG 320
Cdd:cd03794 232 LETLLEAAERLKRRPDIRFLFVGDGDEKERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGsSPS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 321 KFLGYMAAAKPILVFLNKESDgfTLIQEAGCGYAVRSDNVEGAAQLVRKMYVERDSLSQFGKNGFIYAKQNFSLDVCLKK 400
Cdd:cd03794 312 KLFEYMAAGKPILASDDGGSD--LAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADR 389
|
..
gi 1277893519 401 IE 402
Cdd:cd03794 390 LL 391
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-405 |
2.00e-34 |
|
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: 131.12 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 2 KILIVADVYPPEVSSAANLMQELAQGLKKRGHQITVVTSYPRYYLTEAFKEKKFQIFSDEEGINVIRIKVLphhkvnfii 81
Cdd:cd03801 1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 82 rgisqltlpflffAKIKKFIKEIEAVIVYSPPLPLALVGGMIKRHYGVKFILNIQDIFPQNAIDLgilkGWKHKPAIwif 161
Cdd:cd03801 72 -------------RELRPLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLL----LAAERRLL--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 162 eAIEKKVYKDADKITFHSEGGKKFLIKKKNILPEKIITLHNWIDITPYQNLTKnisfRKQYGLEGKFIFLFAGIMGPAQG 241
Cdd:cd03801 132 -ARAEALLRRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSPPLR----RKLGIPPDRPVLLFVGRLSPRKG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 242 LEFLVEVASQIID-LKDVIFLLVG-DGTEKEKIENKIKEYGlKNIIIKPLVPKEDYPYLVKDANVgLVCLSFNnkTPFlP 319
Cdd:cd03801 207 VDLLLEALAKLLRrGPDVRLVIVGgDGPLRAELEELELGLG-DRVRFLGFVPDEELPALYAAADV-FVLPSRY--EGF-G 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 320 GKFLGYMAAAKPILVFlnkESDGFT-LIQEAGCGYAVRSDNVEGAAQLVRKMYVERDSLSQFGKNGFIYAKQNFSLDVCL 398
Cdd:cd03801 282 LVVLEAMAAGLPVVAT---DVGGLPeVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVA 358
|
....*..
gi 1277893519 399 KKIEKLL 405
Cdd:cd03801 359 ERLLDLY 365
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
1-403 |
9.19e-33 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 127.40 E-value: 9.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 1 MKILIVADVYPPEVSSAANLMQELAQGLKKRGHQITVVTS---YPRYYLTEAFKEKKFQIfSDEEGINVIR--------- 68
Cdd:PRK10307 1 MKILVYGINYAPELTGIGKYTGEMAEWLAARGHEVRVITAppyYPQWRVGEGYSAWRYRR-ESEGGVTVWRcplyvpkqp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 69 --IKVLPHHkVNFIirgisqLTLPFLFFAKIkkfIKEIEAVIVYSPPL---PLALvggMIKRHYGVKFILNIQDIFPQNA 143
Cdd:PRK10307 80 sgLKRLLHL-GSFA------LSSFFPLLAQR---RWRPDRVIGVVPTLfcaPGAR---LLARLSGARTWLHIQDYEVDAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 144 IDLGILK-GWKHKPAIWIfeaiEKKVYKDADKITFHSeggKKFLIK--KKNILPEKIITLHNWIDITPYQNLTKN--ISF 218
Cdd:PRK10307 147 FGLGLLKgGKVARLATAF----ERSLLRRFDNVSTIS---RSMMNKarEKGVAAEKVIFFPNWSEVARFQPVADAdvDAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 219 RKQYGL-EGKFIFLFAGIMGPAQGLEFLVEVASQIIDLKDVIFLLVGDGTEKEKIENKIKEYGLKNIIIKPLVPKEDYPY 297
Cdd:PRK10307 220 RAQLGLpDGKKIVLYSGNIGEKQGLELVIDAARRLRDRPDLIFVICGQGGGKARLEKMAQCRGLPNVHFLPLQPYDRLPA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 298 LVKDANVGLVCLSFNNKTPFLPGKFLGYMAAAKPILVFLNKESDGFTLIqeAGCGYAVRSDNVEGAAQLVRKMYVERDSL 377
Cdd:PRK10307 300 LLKMADCHLLPQKAGAADLVLPSKLTNMLASGRNVVATAEPGTELGQLV--EGIGVCVEPESVEALVAAIAALARQALLR 377
|
410 420
....*....|....*....|....*.
gi 1277893519 378 SQFGKNGFIYAKQNFSLDVCLKKIEK 403
Cdd:PRK10307 378 PKLGTVAREYAERTLDKENVLRQFIA 403
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
2-406 |
2.63e-24 |
|
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.
Pssm-ID: 340844 [Multi-domain] Cd Length: 372 Bit Score: 103.13 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 2 KILIVADVYPPEVSSAANLMQELAQGLKKRGHQITVVT-SYPRYylteafkekkfqifSDEEGINVIRIKVLPHHKVNFI 80
Cdd:cd03817 1 KIAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITpSDPGA--------------EDEEEVVRYRSFSIPIRKYHRQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 81 IrgisqltLPFLFFAKIKKFIKEIEAVIVYS-PPLPLALVGGMIKRHYGVKFI----LNIQDIFPqNAIDLGILKGWKHK 155
Cdd:cd03817 67 H-------IPFPFKKAVIDRIKELGPDIIHThTPFSLGKLGLRIARKLKIPIVhtyhTMYEDYLH-YIPKGKLLVKAVVR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 156 PaiwifeaIEKKVYKDADKITFHSEGGKKFLIKKKNILPEKIITlhNWIDITPYQNLtKNISFRKQYGL-EGKFIFLFAG 234
Cdd:cd03817 139 K-------LVRRFYNHTDAVIAPSEKIKDTLREYGVKGPIEVIP--NGIDLDKFEKP-LNTEERRKLGLpPDEPILLYVG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 235 IMGPAQGLEFLVEVASQIIDLKDVIFLLVGDGTEKEKIENKIKEYGL-KNIIIKPLVPKEDYPYLVKDANV--------- 304
Cdd:cd03817 209 RLAKEKNIDFLLRAFAELKKEPNIKLVIVGDGPEREELKELARELGLaDKVIFTGFVPREELPEYYKAADLfvfasttet 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 305 -GLVCLSfnnktpflpgkflgYMAAAKPILVflnKESDGFT-LIQEAGCGYAVRSDNVEGAAQLVRkMYVERDSLSQFGK 382
Cdd:cd03817 289 qGLVYLE--------------AMAAGLPVVA---AKDPAASeLVEDGENGFLFEPNDETLAEKLLH-LRENLELLRKLSK 350
|
410 420
....*....|....*....|....
gi 1277893519 383 NGFIYAKQnFSLDvclKKIEKLLD 406
Cdd:cd03817 351 NAEISARE-FAFA---KSVEKLYE 370
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
2-402 |
1.28e-18 |
|
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: 86.50 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 2 KILIVADVyppeVSSAANLMQELAQGLKKRGHQITVVTSYpryylteafkEKKFQIFSDEEGINVIRIKVLphhkvnfiI 81
Cdd:cd03808 1 KILFIVNV----DGGFQSFRLPLIKALVKKGYEVHVIAPD----------GDKLSDELKELGVKVIDIPIL--------R 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 82 RGISqltlPFLFFA---KIKKFIKEIE--AVIVYSP-PlplALVGGMIKRHYGVKFILNiqdifpqNAIDLGILKGwKHK 155
Cdd:cd03808 59 RGIN----PLKDLKalfKLYKLLKKEKpdIVHCHTPkP---GILGRLAARLAGVPKVIY-------TVHGLGFVFT-EGK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 156 PAIWIFEAIEKKVYKDADKITFHSEGGKKFLIKKKNILPEKIITL-HNWIDITPYQNLTKNISfrkqyglEGKFIFLFAG 234
Cdd:cd03808 124 LLRLLYLLLEKLALLFTDKVIFVNEDDRDLAIKKGIIKKKKTVLIpGSGVDLDRFQYSPESLP-------SEKVVFLFVA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 235 IMGPAQGLEFLVEVASQIIDLK-DVIFLLVGDGTEKEKIENKIKEYGLKNIIIkPLVPKEDYPYLVKDANVGLvclsfnn 313
Cdd:cd03808 197 RLLKDKGIDELIEAAKILKKKGpNVRFLLVGDGELENPSEILIEKLGLEGRIE-FLGFRSDVPELLAESDVFV------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 314 ktpfLPGKFLG-------YMAAAKPILVFL---NKES--DGFTliqeagcGYAVRSDNVEGAAQLVRKMYVERDSLSQFG 381
Cdd:cd03808 269 ----LPSYREGlprslleAMAAGRPVITTDvpgCRELviDGVN-------GFLVPPGDVEALADAIEKLIEDPELRKEMG 337
|
410 420
....*....|....*....|.
gi 1277893519 382 KNGFIYAKQNFSLDVCLKKIE 402
Cdd:cd03808 338 EAARKRVEEKFDEEKVVNKLL 358
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
23-286 |
2.55e-15 |
|
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: 76.63 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 23 ELAQGLKKRGHQIT-VVTSYPRYYLTEAFKEKKfqifsdeegINVIRIKVLPHHKVNFiirgisqltlpFLFFAKIKKFI 101
Cdd:cd03811 20 NLANALDKRGYDVTlVLLRDEGDLDKQLNGDVK---------LIRLLIRVLKLIKLGL-----------LKAILKLKRIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 102 KE--IEAVIVYSPPLPLALvggMIKRHYGVKFILNIQDIFPqnaidlgilkgwkHKPAIWIFEAIEKKVYKDADKITFHS 179
Cdd:cd03811 80 KRakPDVVISFLGFATYIV---AKLAAARSKVIAWIHSSLS-------------KLYYLKKKLLLKLKLYKKADKIVCVS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 180 EGGKKFLIKKKNILPEKIITLHNWIDItpyQNLTKNISFRKQYGLEGKFIFLFAGIMGPAQGLEFLVEVASQIID-LKDV 258
Cdd:cd03811 144 KGIKEDLIRLGPSPPEKIEVIYNPIDI---DRIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKkYPDV 220
|
250 260
....*....|....*....|....*...
gi 1277893519 259 IFLLVGDGTEKEKIENKIKEYGLKNIII 286
Cdd:cd03811 221 KLVILGDGPLREELEKLAKELGLAERVI 248
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
24-286 |
4.47e-14 |
|
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: 72.66 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 24 LAQGLKKRGHQITVVTSYPRYylteafKEKKFQIFSDeeginvIRIKVLPHHKVNFIIRGISQLTLpflfFAKIKKFIKE 103
Cdd:cd03820 22 LANHLAKKGYDVTIISLDSAE------KPPFYELDDN------IKIKNLGDRKYSHFKLLLKYFKK----VRRLRKYLKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 104 IEA--VIVYSPPLPLALvggmikrhygvkfilniqdifpqNAIDLGILK-GWKH-----KPAIWIFEAIEKKVYKDADKI 175
Cdd:cd03820 86 NKPdvVISFRTSLLTFL-----------------------ALIGLKSKLiVWEHnnyeaYNKGLRRLLLRRLLYKRADKI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 176 TFHSEGGKkflIKKKNILPEKIITLHNWIDITPYQNLTKNISFRkqyglegkfiFLFAGIMGPAQGLEFLVEVASQIID- 254
Cdd:cd03820 143 VVLTEADK---LKKYKQPNSNVVVIPNPLSFPSEEPSTNLKSKR----------ILAVGRLTYQKGFDLLIEAWALIAKk 209
|
250 260 270
....*....|....*....|....*....|..
gi 1277893519 255 LKDVIFLLVGDGTEKEKIENKIKEYGLKNIII 286
Cdd:cd03820 210 HPDWKLRIYGDGPEREELEKLIDKLGLEDRVK 241
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
2-390 |
4.98e-14 |
|
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: 72.71 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 2 KILIVADVYPPEVSSAANLMQELAQGLKKRGHQITVVTSYPRYylteafkekkfqiFSDEEGINVIRIKVLPhhkvnfiI 81
Cdd:cd03814 1 RIALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVAPGPFD-------------EAESAEGRVVSVPSFP-------L 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 82 RGISQLTLPFLFFAKIKKFIKEIEAVIVY-SPPLPLALVGGMIKRHYGVKFILNIQDIFPQnaidlgILKGWKHKPAIWI 160
Cdd:cd03814 61 PFYPEYRLALPLPRRVRRLIKEFQPDIIHiATPGPLGLAALRAARRLGLPVVTSYHTDFPE------YLSYYTLGPLSWL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 161 FEAIEKKVYKDADKITFHSEGGKKFLIkkkNILPEKIITLHNWIDITPYQNLTKNISFRKQYGLEGKFIFLFAGIMGPAQ 240
Cdd:cd03814 135 AWAYLRWFHNPFDTTLVPSPSIARELE---GHGFERVRLWPRGVDTELFHPSRRDAALRRRLGPPGRPLLLYVGRLAPEK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 241 GLEFLVEVASQIIDLKDVIFLLVGDGTEKEKIENKikeygLKNIIIKPLVPKEDYPYLVKDANV----------GLVCLS 310
Cdd:cd03814 212 NLEALLDADLPLAASPPVRLVVVGDGPARAELEAR-----GPDVIFTGFLTGEELARAYASADVfvfpsrtetfGLVVLE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 311 fnnktpflpgkflgYMAAAKPILVFlnkESDGFT-LIQEAGCGYAVRSDNVEGAAQLVRKMYVERDSLSQFGKNGFIYAK 389
Cdd:cd03814 287 --------------AMASGLPVVAA---DAGGPRdIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAE 349
|
.
gi 1277893519 390 Q 390
Cdd:cd03814 350 R 350
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
17-206 |
1.71e-13 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 67.94 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 17 AANLMQELAQGLKKRGHQITVVTsyPRYYLTEAfkekkfqifsdEEGINVIRIKVLPHHKVNFIIRGisqltlpFLFFAK 96
Cdd:pfam13439 3 VERYVLELARALARRGHEVTVVT--PGGPGPLA-----------EEVVRVVRVPRVPLPLPPRLLRS-------LAFLRR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 97 IKKFIKEIEAVIVYSP-PLPLALVGGMIKRHYGVKFILNIQDIFPQNAIdlgilKGWKHKPAIWIFEAIEKKVYKDADKI 175
Cdd:pfam13439 63 LRRLLRRERPDVVHAHsPFPLGLAALAARLRLGIPLVVTYHGLFPDYKR-----LGARLSPLRRLLRRLERRLLRRADRV 137
|
170 180 190
....*....|....*....|....*....|.
gi 1277893519 176 TFHSEGGKKFLIKKKNILPEKIITLHNWIDI 206
Cdd:pfam13439 138 IAVSEAVADELRRLYGVPPEKIRVIPNGVDL 168
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
2-396 |
2.36e-13 |
|
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: 70.77 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 2 KILIVADVYPPEVSSAANLMQELAQGLKKRGHQITVVTsypryylteaFKEKKFQIFSDEEGINVIRIKVlphhkvnfiI 81
Cdd:cd03795 1 KVLHVFKFYYPDIGGIEQVIYDLAEGLKKKGIEVDVLC----------FSKEKETPEKEENGIRIHRVKS---------F 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 82 RGISQLTLPFLFFAKIKKFIKEIEaVIVYSPPLPLA-LVGGMIKRHygVKFILNIQ-DIFpqnaidlgilkgwKHKPAIW 159
Cdd:cd03795 62 LNVASTPFSPSYIKRFKKLAKEYD-IIHYHFPNPLAdLLLFFSGAK--KPVVVHWHsDIV-------------KQKKLLK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 160 IFEAIEKKVYKDADKITFHSEGGK---KFLI---KKKNILPEKIitlhNWIDITPYQNLTKNIsfRKQYglEGKFIFLFA 233
Cdd:cd03795 126 LYKPLMTRFLRRADRIIATSPNYVetsPTLRefkNKVRVIPLGI----DKNVYNIPRVDFENI--KREK--KGKKIFLFI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 234 GIMGPAQGLEFLVEvASQIIDLKDVIfllVGDGTEKEKIENKIKEYGLKNIIIKPLVPKEDYPYLVKDANVglVCLSFNN 313
Cdd:cd03795 198 GRLVYYKGLDYLIE-AAQYLNYPIVI---GGEGPLKPDLEAQIELNLLDNVKFLGRVDDEEKVIYLHLCDV--FVFPSVL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 314 KTPFLPGKFLGYMAAAKPIL--------VFLNKesDGFTliqeagcGYAVRSDNVEGAAQLVRKMYVERDSLSQFGKNGF 385
Cdd:cd03795 272 RSEAFGIVLLEAMMCGKPVIstnigtgvPYVNN--NGET-------GLVVPPKDPDALAEAIDKLLSDEELRESYGENAK 342
|
410
....*....|.
gi 1277893519 386 IYAKQNFSLDV 396
Cdd:cd03795 343 KRFEELFTAEK 353
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
22-334 |
1.06e-12 |
|
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: 68.54 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 22 QELAQGLKKRGHQITVVTSYPRyylteafKEKKFQIFSDEeginvirikvLPHHKVNFIIRGISQLTLpflffakiKKFI 101
Cdd:cd03819 18 LDLARALAERGHRVLVVTAGGP-------LLPRLRQIGIG----------LPGLKVPLLRALLGNVRL--------ARLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 102 KEIEAVIVYSPPLPLALVGGMIKRHYGVKFILNIQDifpqnaidLGILKGWKHKPAiwifeaieKKVYKDADKITFHSEG 181
Cdd:cd03819 73 RRERIDLIHAHSRAPAWLGWLASRLTGVPLVTTVHG--------SYLATYHPKDFA--------LAVRARGDRVIAVSEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 182 GKKFLIKKKNILPEKIITLHNWIDITPYQNLTKNISFRKQYGLEGKFIFLFAGIMGPAQGLEFLVEVASQIIDLKDVIFL 261
Cdd:cd03819 137 VRDHLIEALGVDPERIRVIPNGVDTDRFPPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFRLL 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277893519 262 LVGDGTEKEKIENKIKEYGLKNIIIkpLV-PKEDYPYLVKDANVgLVCLSFNnktPFLPGKFLGYMAAAKPILV 334
Cdd:cd03819 217 VAGDGPERDEIRRLVERLGLRDRVT--FTgFREDVPAALAASDV-VVLPSLH---EEFGRVALEAMACGTPVVA 284
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
83-406 |
1.22e-12 |
|
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: 68.50 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 83 GISQLTLPFLFFaKIKKFIKEIEAVIV----YSPPLPLALVGGMIKrhyGVKFILNIQDI-FPQNaidlgiLKGWKHKPA 157
Cdd:cd03807 58 GLSSGKDPGVLL-RLAKLIRKRNPDVVhtwmYHADLIGGLAAKLAG---GVKVIWSVRSSnIPQR------LTRLVRKLC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 158 IWIFEAIEKKVYKDADKITFHSEGGKKflikkknilPEKIITLHNWIDITPYQN-LTKNISFRKQYGL-EGKFIFLFAGI 235
Cdd:cd03807 128 LLLSKFSPATVANSSAVAEFHQEQGYA---------KNKIVVIYNGIDLFKLSPdDASRARARRRLGLaEDRRVIGIVGR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 236 MGPAQGLEFLVEVASQIID-LKDVIFLLVGDGTEKEKIENKIKEYGLKNIIIKpLVPKEDYPYLVKDANVGlvCLSfnNK 314
Cdd:cd03807 199 LHPVKDHSDLLRAAALLVEtHPDLRLLLVGRGPERPNLERLLLELGLEDRVHL-LGERSDVPALLPAMDIF--VLS--SR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 315 TPFLPGKFLGYMAAAKPILVflnkeSD--GFTLIQEAGCGYAVRSDNVEGAAQLVRKMYVERDSLSQFGKNGFIYAKQNF 392
Cdd:cd03807 274 TEGFPNALLEAMACGLPVVA-----TDvgGAAELVDDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEF 348
|
330
....*....|....
gi 1277893519 393 SLDVCLKKIEKLLD 406
Cdd:cd03807 349 SIDAMVRRYETLYY 362
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
55-403 |
2.54e-12 |
|
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: 67.77 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 55 FQIFSDEEGINVIRIKVLPHHKVNFIIRGISQLTLPFLFFAKIKKFIKEIEAVIVYSPPLPLalvggmikRHYGVKFILN 134
Cdd:cd03809 36 VLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKPDLLHSPHNTAPL--------LLKGCPQVVT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 135 IQDIFPQnaidlgILKGWKHKPAIWIFEAIEKKVYKDADKITFHSEGGKKFLIKKKNILPEKIITLHNWIDItPYQNLTK 214
Cdd:cd03809 108 IHDLIPL------RYPEFFPKRFRLYYRLLLPISLRRADAIITVSEATRDDIIKFYGVPPEKIVVIPLGVDP-SFFPPES 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 215 NISFRKQYGLEGKFiFLFAGIMGPAQGLEFLVEVASQIIDLKDVIFLLV--GDGTEKEKIENKIKEYGL-KNIIIKPLVP 291
Cdd:cd03809 181 AAVLIAKYLLPEPY-FLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIvgGKGWEDEELLDLVKKLGLgGRVRFLGYVS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 292 KEDYPYLVKDAnvglVCLSFnnktpflPGKFLGY-------MAAAKPILVflnkeSDGFTLIQEAG-CGYAVRSDNVEGA 363
Cdd:cd03809 260 DEDLPALYRGA----RAFVF-------PSLYEGFglpvleaMACGTPVIA-----SNISVLPEVAGdAALYFDPLDPESI 323
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1277893519 364 AQLVRKMYVERDSLSQFGKNGFIYAKQnFSLDVCLKKIEK 403
Cdd:cd03809 324 ADAILRLLEDPSLREELIRKGLERAKK-FSWEKTAEKTLE 362
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
2-393 |
4.45e-12 |
|
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: 67.01 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 2 KILIVADVYPPEVSSAANLMQELAQGLKKRGHQITVVTsypryylTEAFKEKkfqifSDEEGINVIRIKVLPHHKVNFII 81
Cdd:cd03821 1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVS-------TGDGYES-----LVVEENGRYIPPQDGFASIPLLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 82 RGISQLTLPFLFFAKIKKFIKEIEAVIVYSPPLPLALVGGMIKRHYGVKFILNIQDIFPQNAIDLgilKGWKHKpaiWIF 161
Cdd:cd03821 69 QGAGRTDFSPGLPNWLRRNLREYDVVHIHGVWTYTSLAACKLARRRGIPYVVSPHGMLDPWALQQ---KHWKKR---IAL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 162 EAIEKKVYKDADKITFHSEGGKKFLIKKknILPEKIITLHNWIDITPYQnltKNISFRKQ-YGLEGKFIFLFAGIMGPAQ 240
Cdd:cd03821 143 HLIERRNLNNAALVHFTSEQEADELRRF--GLEPPIAVIPNGVDIPEFD---PGLRDRRKhNGLEDRRIILFLGRIHPKK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 241 GLEFLVEVASQIID-LKDVIFLLVG-DGTEKEKIENKIKEYGLKNIIIKP-LVPKEDYPYLVKDANvgLVCL-----SFN 312
Cdd:cd03821 218 GLDLLIRAARKLAEqGRDWHLVIAGpDDGAYPAFLQLQSSLGLGDRVTFTgPLYGEAKWALYASAD--LFVLpsyseNFG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 313 NKTpflpgkfLGYMAAAKPILVflnKESDGFTLIQEAGCGYAVRsDNVEGAAQLVRKM---YVERDSLSQFGKnGFIYAK 389
Cdd:cd03821 296 NVV-------AEALACGLPVVI---TDKCGLSELVEAGCGVVVD-PNVSSLAEALAEAlrdPADRKRLGEMAR-RARQVE 363
|
....
gi 1277893519 390 QNFS 393
Cdd:cd03821 364 ENFS 367
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
226-384 |
2.52e-10 |
|
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: 58.82 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 226 GKFIFLFAGIMGPAQGLEFLVEVASQIIDLKDVIFL-LVGDGTEKEKIENKIKEYGLK-NIIIKPLVPKEDYPYLVKDAN 303
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLvIAGDGEEEKRLKKLAEKLGLGdNVIFLGFVSDEDLPELLKIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 304 VgLVCLSFNNktPFlPGKFLGYMAAAKPILVflnkeSDGFT---LIQEAGCGYAVRSDNVEGAAQLVRKMYVERDSLSQF 380
Cdd:pfam00534 81 V-FVLPSRYE--GF-GIVLLEAMACGLPVIA-----SDVGGppeVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERL 151
|
....
gi 1277893519 381 GKNG 384
Cdd:pfam00534 152 GENA 155
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
2-369 |
1.08e-09 |
|
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: 59.71 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 2 KILIVADvYPPEVSSAANLMQELAQGLKKRGHQ-ITVVTSYPrYYLTEAFKEKKFQIFSDEEGINVIRikVLPHhkVNFI 80
Cdd:cd03822 1 KIAVLGT-LPPRKCGIATYTDDLVEGLRKGGPVvIVVIVSPQ-DEILKDDDFEVPNEIKSWNSNEYFR--LLDH--LNFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 81 IRGISQLTLPFLFFAKikkfiKEIEAVIVYSpplplalvggmikRHYGVKFILNIQDIFPqnAIDLGilkgwkHKPAIWI 160
Cdd:cd03822 75 KPDVVHIQHEFGIFGG-----KYGLYALGLL-------------LHLRIPVITTLHTVLD--LSDPG------KQALKVL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 161 FEAIEKKvykdaDKITFHSEGGKKFLIKKKNILPEKIITLHNWIDITPYQNLTKNisfRKQYGLEGKFIFLFAGIMGPAQ 240
Cdd:cd03822 129 FRIATLS-----ERVVVMAPISRFLLVRIKLIPAVNIEVIPHGVPEVPQDPTTAL---KRLLLPEGKKVILTFGFIGPGK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 241 GLEFLVEVASQIID-LKDVIFLLVG---DGTEKEKIENK----IKEYGLKNIIIKPL--VPKEDYPYLVKDANVglVCLS 310
Cdd:cd03822 201 GLEILLEALPELKAeFPDVRLVIAGelhPSLARYEGERYrkaaIEELGLQDHVDFHNnfLPEEEVPRYISAADV--VVLP 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277893519 311 FNNKTPFLPGKFLGYMAAAKPILVflnkeSD--GFTLIQEAGCGYAVRSDNVEGAAQLVRK 369
Cdd:cd03822 279 YLNTEQSSSGTLSYAIACGKPVIS-----TPlrHAEELLADGRGVLVPFDDPSAIAEAILR 334
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
22-203 |
4.35e-09 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 55.10 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 22 QELAQGLKKRGHQITVVTsyPRYYLTEAfkekkfqiFSDEEGINVIRIKVLPHHkvnfiiRGISQLTLPFLFFAKIKKFi 101
Cdd:pfam13579 8 LELARALAALGHEVRVVT--PGGPPGRP--------ELVGDGVRVHRLPVPPRP------SPLADLAALRRLRRLLRAE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 102 kEIEAVIVYSPPLPLALVggMIKRHYGVKFILNIQDifpqNAIDLGilKGWKHkpaiWIFEAIEKKVYKDADKITFHSEG 181
Cdd:pfam13579 71 -RPDVVHAHSPTAGLAAR--LARRRRGVPLVVTVHG----LALDYG--SGWKR----RLARALERRLLRRADAVVVVSEA 137
|
170 180
....*....|....*....|..
gi 1277893519 182 GKKFLIkKKNILPEKIITLHNW 203
Cdd:pfam13579 138 EAELLR-ALGVPAARVVVVPNG 158
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
289-406 |
6.78e-09 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 53.46 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 289 LVPKEDYPYLVK----DANVGLVCLSFNNktpfLPGKFLGYMAAAKPILVFlnkESDGF-TLIQEAGCGYAVRSDNVEGA 363
Cdd:COG0438 4 LVPRKGLDLLLEallaAADVFVLPSRSEG----FGLVLLEAMAAGLPVIAT---DVGGLpEVIEDGETGLLVPPGDPEAL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1277893519 364 AQLVRKMYVERDSLSQFGKNGFIYAKQNFSLDVCLKKIEKLLD 406
Cdd:COG0438 77 AEAILRLLEDPELRRRLGEAARERAEERFSWEAIAERLLALYE 119
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
165-286 |
1.08e-08 |
|
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: 56.53 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 165 EKKVYKDADKITFHSEGGKKFLIKKKNIlpEKIITLHNWIDITPYQ-NLTKNISFRKQYGLEGKFIFLFAGIMGPAQGLE 243
Cdd:cd03812 130 KKLIERLSTKYLACSEDAGEWLFGEVEN--GKFKVIPNGIDIEKYKfNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHS 207
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1277893519 244 FLVEVASQIIDL-KDVIFLLVGDGTEKEKIENKIKEYGLKNIII 286
Cdd:cd03812 208 FLIDIFEELKKKnPNVKLVLVGEGELKEKIKEKVKELGLEDKVI 251
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
197-335 |
1.18e-07 |
|
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: 52.41 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 197 IITLHNWIDITPYQNLTKNISFRKQYGleGKFIFLFAGIMGPAQGLEFLVEVASQII-DLKDVIFLLVGDGTEKEKIENK 275
Cdd:cd01635 82 VVTVHGPDSLESTRSELLALARLLVSL--PLADKVSVGRLVPEKGIDLLLEALALLKaRLPDLVLVLVGGGGEREEEEAL 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277893519 276 IKEYGLK--NIIIKPLVPKEDYPYLVKDANVgLVCLSFNnkTPFlPGKFLGYMAAAKPILVF 335
Cdd:cd01635 160 AAALGLLerVVIIGGLVDDEVLELLLAAADV-FVLPSRS--EGF-GLVLLEAMAAGKPVIAT 217
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
117-404 |
3.72e-06 |
|
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: 48.87 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 117 ALVGGMIKRHYGVKFILNIQDIFP-QNAIDlgILKGWKHKPAI---WI--FEAIEKKVYKDADKITFHSEGGKKFLIKkk 190
Cdd:cd03813 186 GLLGALARHRRGIPFLLTEHGIYTrERKIE--ILQSTWIMGYIkklWIrfFERLGKLAYQQADKIISLYEGNRRRQIR-- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 191 niL---PEKIITLHNWIDITPYQNLtknisfRKQYGLEGKFIFLFAGIMGPAQGLEFLVEVASQII-DLKDVIFLLVGDG 266
Cdd:cd03813 262 --LgadPDKTRVIPNGIDIQRFAPA------REERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRrAMPDAEGWLIGPE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 267 TEKEK-------------IENKIKEYGLKNIiikplvpKEDYPYLvkdanvGLVCLSfnNKTPFLPGKFLGYMAAAKPIL 333
Cdd:cd03813 334 DEDPEyaqeckrlvaslgLENKVKFLGFQNI-------KEYYPKL------GLLVLT--SISEGQPLVILEAMASGVPVV 398
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277893519 334 ---VFLNKESDGFTLIQEAGCGYAVRSDNVEGAAQLVRKMYVERDSLSQFGKNGFIYAKQNFSLDVCLKKIEKL 404
Cdd:cd03813 399 atdVGSCRELIYGADDALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKL 472
|
|
| GT33_ALG1-like |
cd03816 |
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ... |
21-309 |
9.43e-06 |
|
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.
Pssm-ID: 340843 [Multi-domain] Cd Length: 411 Bit Score: 47.27 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 21 MQELAQGLKKRGHQITVVtsypRYYLTEAFKEkkfqIFSDEEgINVIRIKVLPH-HKVNFIIRGISQLTLPF--LFFAKI 97
Cdd:cd03816 20 MQYHALSLARHGWRVDLI----GYLESPPHDE----LLSHPN-ITIHALPPPPTkNKLPFLLFAPLKVLLQAlsLLWLLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 98 KkfIKEIEAVIVYSPP-LPLALVGGMIKRHYGVKFIlniqdifpqnaID--------LGILKGWKHkPAIWIFEAIEKKV 168
Cdd:cd03816 91 E--LRPADYILVQNPPsIPTLAIAWLYCRLRRTKLI-----------IDwhnfgytiLALKLGENH-PLVRLAKWYEKTF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 169 YKDADKITFHSEGGKKFLIKKKNIlPEKIITLHN---------WIDITpYQNLTKNISFRKQYG-----LEGKFIFLFA- 233
Cdd:cd03816 157 GRMADAHLCVTKAMQRDLQQFENW-NIRATVLYDrppshfrpiPLEEK-HELFLELALFRELAEgavsyKEGRPALLVSs 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 234 ---------GIMgpaqgLEFLVEVASQIID----LKDVIFLLVGDGTEKEKIENKIKEYGLKNIIIK-PLVPKEDYPYLV 299
Cdd:cd03816 235 tswtpdedfSIL-----LDALKAYESSAATepalLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRtPWLSAEDYPRLL 309
|
330
....*....|
gi 1277893519 300 KDANVGlVCL 309
Cdd:cd03816 310 ASADLG-VCL 318
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
227-371 |
2.26e-05 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 44.04 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 227 KFIFLFAGIMGPAQ-GLEFLVEVASQIID-LKDVIFLLVGDGTEKEkIENKIKEYGlKNIIIKPLVpkEDYPYLVKDANV 304
Cdd:pfam13692 1 RPVILFVGRLHPNVkGVDYLLEAVPLLRKrDNDVRLVIVGDGPEEE-LEELAAGLE-DRVIFTGFV--EDLAELLAAADV 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277893519 305 GLVCLSFNNktpfLPGKFLGYMAAAKPILVFlnkESDGFTLIQEAGCGYAVRSDNVEGAAQLVRKMY 371
Cdd:pfam13692 77 FVLPSLYEG----FGLKLLEAMAAGLPVVAT---DVGGIPELVDGENGLLVPPGDPEALAEAILRLL 136
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
172-286 |
4.50e-05 |
|
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: 45.13 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 172 ADKITFHSEGGKKFLIKKKNILPEKIITLHNWIDITPYQ-NLTKNISFRKQYGLE-GKFIFLFAGIMGPAQGLEFLVEVA 249
Cdd:cd04951 131 CDITTNVSREALDEFIAKKAFSKNKSVPVYNGIDLNKFKkDINVRLKIRNKLNLKnDEFVILNVGRLTEAKDYPNLLLAI 210
|
90 100 110
....*....|....*....|....*....|....*...
gi 1277893519 250 SQIIDLK-DVIFLLVGDGTEKEKIENKIKEYGLKNIII 286
Cdd:cd04951 211 SELILSKnDFKLLIAGDGPLRNELERLICNLNLVDRVI 248
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
195-368 |
5.31e-05 |
|
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: 45.04 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 195 EKIITLHNWIDITPYQNLTKNISFRKQYGLEGKFIFL----FAGIMGPAQGLEFLVEVASQIidlkDVIFLLVGDGTEKE 270
Cdd:cd04962 164 KDIEVIHNFIDEDVFKRKPAGALKRRLLAPPDEKVVIhvsnFRPVKRIDDVVRVFARVRRKI----PAKLLLVGDGPERV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 271 KIENKIKEYGLKNIIIkplvpkedypylvkdanvglvclsfnnktpflpgkFLGYMAAAKPIL----VFL---NKESDGF 343
Cdd:cd04962 240 PAEELARELGVEDRVL-----------------------------------FLGKQDDVEELLsiadLFLlpsEKESFGL 284
|
170 180
....*....|....*....|....*
gi 1277893519 344 TLIQEAGCGYAVRSDNVEGAAQLVR 368
Cdd:cd04962 285 AALEAMACGVPVVSSNAGGIPEVVK 309
|
|
| PLN02275 |
PLN02275 |
transferase, transferring glycosyl groups |
257-309 |
2.39e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215155 [Multi-domain] Cd Length: 371 Bit Score: 43.12 E-value: 2.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1277893519 257 DVIFLLVGDGTEKEKIENKIKEYGLKNIIIKPL-VPKEDYPYLVKDANVGlVCL 309
Cdd:PLN02275 261 RLLFIITGKGPQKAMYEEKISRLNLRHVAFRTMwLEAEDYPLLLGSADLG-VSL 313
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
2-179 |
3.06e-04 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 40.77 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 2 KILIVADVypPEVssaanLMQELAQGLKKRGHQITVVTSYPRYylteafkeKKFQIfsdEEGINVIRIKVlphhkvnfii 81
Cdd:pfam13477 1 KILLLANA--DSI-----HTLRWADALADRGYDVHVISSKGPA--------KDELI---AEGIHVHRLKV---------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893519 82 rgISQLTLPFLFFAKIKKFIKEI--EAVIVYSPPlPLALVGGMIKRHYGV-KFILNI--QDIFpqnaidlgilkgwKHKP 156
Cdd:pfam13477 53 --PRKGPLGYLKAFRLKKLIKKIkpDVVHVHYAK-PYGLLAGLAARLSGFpPVVLSAwgLDVY-------------KFPN 116
|
170 180
....*....|....*....|...
gi 1277893519 157 AIWIFEAIEKKVYKDADKITFHS 179
Cdd:pfam13477 117 KSRLKKLLLKLNLKKATLIISTS 139
|
|
| |
