|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
3-379 |
6.84e-66 |
|
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: 213.55 E-value: 6.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 3 RILYLHAGAEMY--GADKVLLELIKGLDHKEFEAHVILPNDGvlvevlrqvGAKVSVLDYPILRRKYFNPKGIADYIRSy 80
Cdd:cd03801 1 KILLLSPELPPPvgGAERHVRELARALAARGHDVTVLTPADP---------GEPPEELEDGVIVPLLPSLAALLRARRL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 81 nfyAKQIALYARQHSIDMVH-NNTAAVLEGIYLKRKLKLPLIWHVHEIIV---------KPKAISDFINMLmgRYADKIV 150
Cdd:cd03801 71 ---LRELRPLLRLRKFDVVHaHGLLAALLAALLALLLGAPLVVTLHGAEPgrlllllaaERRLLARAEALL--RRADAVI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 151 TVSQAVANHIEQSPFIKDSQVEVIYNGVDNAVYYPMdassIREKFDIAQDALVIGMIGRVNAIKGQNDFIEAVEPLLEKN 230
Cdd:cd03801 146 AVSEALRDELRALGGIPPEKIVVIPNGVDLERFSPP----LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 231 EKAVAFLAGGvfHGEEW-RLEELDNRIASssvvsQIHRIDY--YDKTSELYNMFDIFVLPSIkPDSLPTVVLEAMACSKP 307
Cdd:cd03801 222 PDVRLVIVGG--DGPLRaELEELELGLGD-----RVRFLGFvpDEELPALYAAADVFVLPSR-YEGFGLVVLEAMAAGLP 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48474171 308 VVGYNNGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQRELFSLESYIKNFSEFY 379
Cdd:cd03801 294 VVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
4-380 |
1.19e-46 |
|
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: 162.87 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 4 ILYLHAGaemyGADKVLLELIKGLDHKEFEAHVI-LPNDGVLVEVLRQVGAKVSVLDypilRRKYFNPKGIadyIRsynf 82
Cdd:cd03807 6 ITGLNVG----GAETMLLRLLEHMDKSRFEHVVIsLTGDGVLGEELLAAGVPVVCLG----LSSGKDPGVL---LR---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 83 YAKQIalyaRQHSIDMVH--NNTAAVLEGIYLKRKLKLPLIWHVHEIIVKPKA--ISDFINMLMGRYADKIVTVSQAVAN 158
Cdd:cd03807 71 LAKLI----RKRNPDVVHtwMYHADLIGGLAAKLAGGVKVIWSVRSSNIPQRLtrLVRKLCLLLSKFSPATVANSSAVAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 159 -HIEQSpfIKDSQVEVIYNGVDNAVYYPMDAS--SIREKFDIAQDALVIGMIGRVNAIKGQNDFIEAVEPLLEKNEKAVA 235
Cdd:cd03807 147 fHQEQG--YAKNKIVVIYNGIDLFKLSPDDASraRARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 236 FLAGGvfHGEEWRLEELdnrIASSSVVSQIHRIDYYDKTSELYNMFDIFVLPSiKPDSLPTVVLEAMACSKPVVGYNNGG 315
Cdd:cd03807 225 LLVGR--GPERPNLERL---LLELGLEDRVHLLGERSDVPALLPAMDIFVLSS-RTEGFPNALLEAMACGLPVVATDVGG 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48474171 316 IAEmVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQRELFSLESYIKNFSEFYD 380
Cdd:cd03807 299 AAE-LVDDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
3-373 |
6.51e-46 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
Pssm-ID: 340837 [Multi-domain] Cd Length: 358 Bit Score: 160.84 E-value: 6.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 3 RILYLHAGAEmyGADKVLLELIKGLDHKEFEAHVILPNDGVLVEVLRQVGAKVsvLDYPILRRkyfnpkGIADYirsYNF 82
Cdd:cd03808 1 KILFIVNVDG--GFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKELGVKV--IDIPILRR------GINPL---KDL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 83 YA-KQIALYARQHSIDMVHNNT--AAVLEGIYLKRKLKLPLIWHVH---EIIVKPKAISDFINML---MGRYADKIVTVS 153
Cdd:cd03808 68 KAlFKLYKLLKKEKPDIVHCHTpkPGILGRLAARLAGVPKVIYTVHglgFVFTEGKLLRLLYLLLeklALLFTDKVIFVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 154 QAVANHIEQSPFIKDSQVEVIY-NGVDNAVYYPMDASSIREKFdiaqdalVIGMIGRVNAIKGQNDFIEAVEPLLEKNEK 232
Cdd:cd03808 148 EDDRDLAIKKGIIKKKKTVLIPgSGVDLDRFQYSPESLPSEKV-------VFLFVARLLKDKGIDELIEAAKILKKKGPN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 233 AVAFLAGGvfhgeewrLEELDNRIASSSVVSQIHRIDYYDKTS---ELYNMFDIFVLPSIKpDSLPTVVLEAMACSKPVV 309
Cdd:cd03808 221 VRFLLVGD--------GELENPSEILIEKLGLEGRIEFLGFRSdvpELLAESDVFVLPSYR-EGLPRSLLEAMAAGRPVI 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48474171 310 GYNNGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQRELFSLESYIK 373
Cdd:cd03808 292 TTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVN 355
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
149-382 |
1.54e-45 |
|
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: 160.19 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 149 IVTVSQAVANHIEQSPFIKDSQVEVIYNGVDNAVYYPMDASSIREKFDIAQDALVIGMIGRVNAI--KGQNDFIEAVEpL 226
Cdd:cd03825 141 IVAPSRWLADMVRRSPLLKGLPVVVIPNGIDTEIFAPVDKAKARKRLGIPQDKKVILFGAESVTKprKGFDELIEALK-L 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 227 LEKNEKAVAFLAGGvfhgeewrleeLDNRIASSSVvsQIHRIDYYDKTSEL---YNMFDIFVLPSIKpDSLPTVVLEAMA 303
Cdd:cd03825 220 LATKDDLLLVVFGK-----------NDPQIVILPF--DIISLGYIDDDEQLvdiYSAADLFVHPSLA-DNLPNTLLEAMA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 304 CSKPVVGYNNGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGrvgyQRQREL----FSLESYIKNFSEFY 379
Cdd:cd03825 286 CGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLG----ERARALaenhFDQRVQAQRYLELY 361
|
...
gi 48474171 380 DNL 382
Cdd:cd03825 362 KDL 364
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
21-367 |
1.00e-39 |
|
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.
Pssm-ID: 340828 [Multi-domain] Cd Length: 376 Bit Score: 144.83 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 21 LELIKGLDHKEFEAHVILPNDGVLVEVLRQVGAKVSVLDYPILRRKYFNPKGIADYIRSYNFYAKQIALYARQHSIDMV- 99
Cdd:cd03798 21 RRQVRALSRRGVDVEVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAPSLAKLLKRRRRGPPDLIh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 100 -HNNTAAVLEGIYLKRKLKLPLIWHVHEiivkpkaiSDfINMLMG------------RYADKIVTVSQAVANHIEQSPFI 166
Cdd:cd03798 101 aHFAYPAGFAAALLARLYGVPYVVTEHG--------SD-INVFPPrsllrkllrwalRRAARVIAVSKALAEELVALGVP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 167 KDsQVEVIYNGVDNAVYYPMDassirEKFDIAQDALVIGMIGRVNAIKGQNDFIEAVEPLLEKNEKAVAFLAGgvfHGEE 246
Cdd:cd03798 172 RD-RVDVIPNGVDPARFQPED-----RGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVG---DGPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 247 wrLEELDNRIASSSVVSQIHRIDYYDKT--SELYNMFDIFVLPSIKpDSLPTVVLEAMACSKPVVGYNNGGIAEMVVDDK 324
Cdd:cd03798 243 --REALRALAEDLGLGDRVTFTGRLPHEqvPAYYRACDVFVLPSRH-EGFGLVLLEAMACGLPVVATDVGGIPEVVGDPE 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 48474171 325 SGYLVKPNRPQELSNAISLLLDSSEKREKfGRVGYQRQRELFS 367
Cdd:cd03798 320 TGLLVPPGDADALAAALRRALAEPYLREL-GEAARARVAERFS 361
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
3-366 |
2.04e-39 |
|
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: 143.65 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 3 RILYLHAGAEMYGADKVLLELIKGLDHKEFEAH-VILPNDGVLVEVLRQVGAKVSVLDYPILRRKYFNPKGIadyirsyn 81
Cdd:cd03811 1 KILFVIPSLSGGGAERVLLNLANALDKRGYDVTlVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAI-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 82 fyaKQIALYARQHSIDMVHNNTAAVLEGIYLKRKLKLPLIWHVH--EIIVKPKAISDFINMLMGRYADKIVTVSQAVANH 159
Cdd:cd03811 73 ---LKLKRILKRAKPDVVISFLGFATYIVAKLAAARSKVIAWIHssLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKED 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 160 IEQSPFIKDSQVEVIYNGVDNAvyyPMDASSIREKFDIAQDALVIGMIGRVNAIKGQNDFIEAVEPLLEKNEKAVAFLAG 239
Cdd:cd03811 150 LIRLGPSPPEKIEVIYNPIDID---RIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 240 gvfHGEEwrLEELDNRIASSSVVSQIHRIDYYDKTSELYNMFDIFVLPSIKpDSLPTVVLEAMACSKPVVGYNNGGIAEM 319
Cdd:cd03811 227 ---DGPL--REELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRY-EGFPNVLLEAMALGTPVVSTDCPGPREI 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 48474171 320 VVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQRELF 366
Cdd:cd03811 301 LDDGENGLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEAVFR 347
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
10-363 |
2.90e-38 |
|
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: 140.18 E-value: 2.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 10 GAEMYGADkvLLELIKGLDHKefeaHVILPNDGVLVEVLRQVGAKVSVLDYPILRRKYFNpkgiadyirsynfyaKQIAL 89
Cdd:cd03819 12 GAETYILD--LARALAERGHR----VLVVTAGGPLLPRLRQIGIGLPGLKVPLLRALLGN---------------VRLAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 90 YARQHSIDMVHNNT-AAVLEGIYLKRKLKLPLIWHVHEIIVKPKAISDFINMLMgRYADKIVTVSQAVANHIEQS-PFIK 167
Cdd:cd03819 71 LIRRERIDLIHAHSrAPAWLGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVR-ARGDRVIAVSELVRDHLIEAlGVDP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 168 DsQVEVIYNGVDNAVYYPMDASSIREKFDIAQDALVIGMIGRVNAIKGQNDFIEAVEpLLEKNEKAVAFLAGGvfhGEEw 247
Cdd:cd03819 150 E-RIRVIPNGVDTDRFPPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAA-ELKDEPDFRLLVAGD---GPE- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 248 rLEELDNRIASSSVVSQIHRIDYYDKTSELYNMFDIFVLPSIKPdSLPTVVLEAMACSKPVVGYNNGGIAEMVVDDKSGY 327
Cdd:cd03819 224 -RDEIRRLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHE-EFGRVALEAMACGTPVVATDVGGAREIVVHGRTGL 301
|
330 340 350
....*....|....*....|....*....|....*.
gi 48474171 328 LVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQR 363
Cdd:cd03819 302 LVPPGDAEALADAIRAAKLLPEAREKLQAAAALTEA 337
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
203-361 |
1.96e-30 |
|
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: 113.91 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 203 VIGMIGRVNAIKGQNDFIEAVEPLLEKNEKAVAFLAGGvfhGEEwrLEELDNRIASSSVVSQIH---RIDYYDKtSELYN 279
Cdd:pfam00534 4 IILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGD---GEE--EKRLKKLAEKLGLGDNVIflgFVSDEDL-PELLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 280 MFDIFVLPSIKpDSLPTVVLEAMACSKPVVGYNNGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGY 359
Cdd:pfam00534 78 IADVFVLPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENAR 156
|
..
gi 48474171 360 QR 361
Cdd:pfam00534 157 KR 158
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
3-375 |
1.44e-29 |
|
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
Pssm-ID: 340825 [Multi-domain] Cd Length: 391 Bit Score: 117.83 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 3 RILYLH--AGAEMYGADKVLLELIKGLDHKEFEAHVILPNDGVLvEVLRQVGAKVSVLDYPILRRKYFNPK--GIADYIR 78
Cdd:cd03794 1 KILLISqyYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYP-LGRIFAGATETKDGIRVIRVKLGPIKknGLIRRLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 79 SYNFYAKQIALYA--RQHSIDMVHNNTA---AVLEGIYLKRKLKLPLIWHVH----EIIVKPKAIS--------DFINML 141
Cdd:cd03794 80 NYLSFALAALLKLlvREERPDVIIAYSPpitLGLAALLLKKLRGAPFILDVRdlwpESLIALGVLKkgsllkllKKLERK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 142 MGRYADKIVTVSQAVANHIEQsPFIKDSQVEVIYNGVDNAVYYPMDASSIREKFdIAQDALVIGMIGrvNAIKGQN-DFI 220
Cdd:cd03794 160 LYRLADAIIVLSPGLKEYLLR-KGVPKEKIIVIPNWADLEEFKPPPKDELRKKL-GLDDKFVVVYAG--NIGKAQGlETL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 221 EAVEPLLEKNEKAVaFLAGGVFHGEEWRLEELDNRiaSSSVVSQIHRIDYyDKTSELYNMFDIFVLPsIKPD-----SLP 295
Cdd:cd03794 236 LEAAERLKRRPDIR-FLFVGDGDEKERLKELAKAR--GLDNVTFLGRVPK-EEVPELLSAADVGLVP-LKDNpanrgSSP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 296 TVVLEAMACSKPVVGYNNGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQRELFSLESYIKNF 375
Cdd:cd03794 311 SKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRL 390
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
9-373 |
4.25e-28 |
|
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: 112.81 E-value: 4.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 9 AGAEMYGADkvLLELIKGLDHKE--FEAHVIlPNDGVLVEVLRQV--GAKVSVLDYPILRRKYFNpkgiadyIRSYNFY- 83
Cdd:cd03823 15 GGAEISVHD--LAEALVAEGHEVavLTAGVG-PPGQATVARSVVRyrRAPDETLPLALKRRGYEL-------FETYNPGl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 84 AKQIALYARQHSIDMVH-----NNTAAVLEGIylkRKLKLPLIWHVHEiivkPKAISDFINMlMGRYADKIVTVSQAVAN 158
Cdd:cd03823 85 RRLLARLLEDFRPDVVHthnlsGLGASLLDAA---RDLGIPVVHTLHD----YWLLCPRQFL-FKKGGDAVLAPSRFTAN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 159 -HIEQSPFikDSQVEVIYNGVDnavyyPMDASsiREKFDIAQDALVIGMIGRVNAIKGQNDFIEAVEPLLEknekavafl 237
Cdd:cd03823 157 lHEANGLF--SARISVIPNAVE-----PDLAP--PPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLPR--------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 238 aggvfhgEEWRL----EELDNRIASSSVVSQIHRIDYY--DKTSELYNMFDIFVLPSIKPDSLPTVVLEAMACSKPVVGY 311
Cdd:cd03823 219 -------EDIELviagHGPLSDERQIEGGRRIAFLGRVptDDIKDFYEKIDVLVVPSIWPEPFGLVVREAIAAGLPVIAS 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48474171 312 NNGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSE--KREKFGrvGYQRQRELFSLESYIK 373
Cdd:cd03823 292 DLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPAllERLRAG--AEPPRSTESQAEEYLK 353
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
64-382 |
3.27e-27 |
|
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: 110.83 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 64 RRKYFNPKGIADYIRSYNFYAKQIALYARQHSIDMVHNNTAAVLEGI--YLKRKLKLPLI--WH------VHEI-----I 128
Cdd:cd03817 53 YRSFSIPIRKYHRQHIPFPFKKAVIDRIKELGPDIIHTHTPFSLGKLglRIARKLKIPIVhtYHtmyedyLHYIpkgklL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 129 VKPKAISDFINMLmgRYADKIVTVSQAVANHIEQspFIKDSQVEVIYNGVDNAVYYPMDASSIREKFDIAQDALVIGMIG 208
Cdd:cd03817 133 VKAVVRKLVRRFY--NHTDAVIAPSEKIKDTLRE--YGVKGPIEVIPNGIDLDKFEKPLNTEERRKLGLPPDEPILLYVG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 209 RVNAIKGQNDFIEAVEPLLEKNEkavAFLaggVFHG---EEWRLEELDNRIASSSVVSQIHRIDYyDKTSELYNMFDIFV 285
Cdd:cd03817 209 RLAKEKNIDFLLRAFAELKKEPN---IKL---VIVGdgpEREELKELARELGLADKVIFTGFVPR-EELPEYYKAADLFV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 286 LPSiKPDSLPTVVLEAMACSKPVVGYNNGGIAEMVVDDKSGYLVKPNRPqELSNAISLLLDSSEKREKFGRVGYQRQREL 365
Cdd:cd03817 282 FAS-TTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDE-TLAEKLLHLRENLELLRKLSKNAEISAREF 359
|
330
....*....|....*..
gi 48474171 366 FSLESYIKnfseFYDNL 382
Cdd:cd03817 360 AFAKSVEK----LYEEV 372
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
277-382 |
5.13e-27 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 103.92 E-value: 5.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 277 LYNMFDIFVLPSIKpDSLPTVVLEAMACSKPVVGYNNGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGR 356
Cdd:COG0438 17 LLAAADVFVLPSRS-EGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGE 95
|
90 100
....*....|....*....|....*.
gi 48474171 357 VGYQRQRELFSLESYIKNFSEFYDNL 382
Cdd:COG0438 96 AARERAEERFSWEAIAERLLALYEEL 121
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
203-346 |
6.96e-27 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 103.75 E-value: 6.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 203 VIGMIGRVNA-IKGQNDFIEAVEPLLEKNEKAVAFLAGGvfhGEEWRLEELDNRIASssvvsQIHRIDYYDKTSELYNMF 281
Cdd:pfam13692 3 VILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGD---GPEEELEELAAGLED-----RVIFTGFVEDLAELLAAA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48474171 282 DIFVLPSIKpDSLPTVVLEAMACSKPVVGYNNGGIAEmVVDDKSGYLVKPNRPQELSNAISLLLD 346
Cdd:pfam13692 75 DVFVLPSLY-EGFGLKLLEAMAAGLPVVATDVGGIPE-LVDGENGLLVPPGDPEALAEAILRLLE 137
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
70-371 |
1.77e-26 |
|
sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
Pssm-ID: 340830 [Multi-domain] Cd Length: 398 Bit Score: 109.25 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 70 PKGIADYIRSYNFY------AKQIALYARQHSI--DMVHNNTA-AVLEGIYLKRKLKLPLIWHVHEI-IVKPKAISDF-- 137
Cdd:cd03800 68 PAGPPEYLPKEELWpyleefADGLLRFIAREGGryDLIHSHYWdSGLVGALLARRLGVPLVHTFHSLgRVKYRHLGAQdt 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 138 --------INMLMGRYADKIVTVSQAVA----NHIEQspfiKDSQVEVIYNGVDNAVYYPMD-ASSIREKFDIAQDALVI 204
Cdd:cd03800 148 yhpslritAEEQILEAADRVIASTPQEAdeliSLYGA----DPSRINVVPPGVDLERFFPVDrAEARRARLLLPPDKPVV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 205 GMIGRVNAIKGQNDFIEAVEPLLEKNEKAVAFLAGGVFHGEEWRLEELDNRIASssVVSQIHRIDYY-----DKTSELYN 279
Cdd:cd03800 224 LALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGGPSDDPLSMDREELAELAE--ELGLIDRVRFPgrvsrDDLPELYR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 280 MFDIFVLPSI-KPDSLptVVLEAMACSKPVVGYNNGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVG 358
Cdd:cd03800 302 AADVFVVPSLyEPFGL--TAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAG 379
|
330
....*....|...
gi 48474171 359 YQRQRELFSLESY 371
Cdd:cd03800 380 LERARAHYTWESV 392
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
109-380 |
4.94e-25 |
|
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: 105.88 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 109 GIYLK-RKLKLPL-IWHVHEIivKPKAISDF--INMLMGRYADKIVTVSQAvaNHIEQspfIKD----SQVEVIYNGVDN 180
Cdd:cd03813 206 GIYTReRKIEILQsTWIMGYI--KKLWIRFFerLGKLAYQQADKIISLYEG--NRRRQ---IRLgadpDKTRVIPNGIDI 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 181 AVYYPmdASSIREKfdiaQDALVIGMIGRVNAIKGQNDFIEAVEPLLEKNEKAVAFLAGGVFHGEEWRLEELdnRIASSS 260
Cdd:cd03813 279 QRFAP--AREERPE----KEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIGPEDEDPEYAQECK--RLVASL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 261 VVSQIHRIDYYDKTSELYNMFDIFVLPSIKpDSLPTVVLEAMACSKPVVGYNNGGIAEMV--VDDK---SGYLVKPNRPQ 335
Cdd:cd03813 351 GLENKVKFLGFQNIKEYYPKLGLLVLTSIS-EGQPLVILEAMASGVPVVATDVGSCRELIygADDAlgqAGLVVPPADPE 429
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 48474171 336 ELSNAISLLLDSSEKREKFGRVGYQRQRELFSLESYIKNFSEFYD 380
Cdd:cd03813 430 ALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
60-373 |
6.13e-25 |
|
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.
Pssm-ID: 340847 [Multi-domain] Cd Length: 351 Bit Score: 104.24 E-value: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 60 YPI---LRRKYFNPKGIADYIRSYNFYAKQIAL--YARQHSIDMV---HNNTAAVLegIYLKRKLKLPLIWHVHEIIVKP 131
Cdd:cd03820 47 YELddnIKIKNLGDRKYSHFKLLLKYFKKVRRLrkYLKNNKPDVVisfRTSLLTFL--ALIGLKSKLIVWEHNNYEAYNK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 132 KAISDFINMLMGRYADKIVTVSQAVANHIEQSPFIKdsqVEVIYNgvdnavyyPMDASSIREKFDIAQDalVIGMIGRVN 211
Cdd:cd03820 125 GLRRLLLRRLLYKRADKIVVLTEADKLKKYKQPNSN---VVVIPN--------PLSFPSEEPSTNLKSK--RILAVGRLT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 212 AIKGQNDFIEAVEPLLEKNEkavaflaggvfhgeEWRL---------EELDNRIASSSVVSQIHRIDYYDKTSELYNMFD 282
Cdd:cd03820 192 YQKGFDLLIEAWALIAKKHP--------------DWKLriygdgperEELEKLIDKLGLEDRVKLLGPTKNIAEEYANSS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 283 IFVLPSiKPDSLPTVVLEAMACSKPVVGYN-NGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQR 361
Cdd:cd03820 258 IFVLSS-RYEGFPMVLLEAMAYGLPIISFDcPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKN 336
|
330
....*....|..
gi 48474171 362 qRELFSLESYIK 373
Cdd:cd03820 337 -AERFSIEKIIK 347
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
92-382 |
1.73e-23 |
|
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.
Pssm-ID: 132132 [Multi-domain] Cd Length: 374 Bit Score: 100.18 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 92 RQHSIDMVHNNTAAVLEGIYLKRKLKLPLI------WHVHEI---IVKPKAISDFINMLMGRYadkiVTVSQAVANHIEQ 162
Cdd:TIGR03088 78 RQLRPDIVHTRNLAALEAQLPAALAGVPARihgehgRDVFDLdgsNWKYRWLRRLYRPLIHHY----VAVSRDLEDWLRG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 163 SPFIKDSQVEVIYNGVDNAVYYPMDA--SSIREKFDIAQDALVIGMIGRVNAIKGQ----NDFIEAVEPLLEKNEKAVAF 236
Cdd:TIGR03088 154 PVKVPPAKIHQIYNGVDTERFHPSRGdrSPILPPDFFADESVVVGTVGRLQAVKDQptlvRAFALLVRQLPEGAERLRLV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 237 LAG-GVFHGEewrLEELdnrIASSSVVSQIHRIDYYDKTSELYNMFDIFVLPSiKPDSLPTVVLEAMACSKPVVGYNNGG 315
Cdd:TIGR03088 234 IVGdGPARGA---CEQM---VRAAGLAHLVWLPGERDDVPALMQALDLFVLPS-LAEGISNTILEAMASGLPVIATAVGG 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 48474171 316 IAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQRELFSLESYIKNFSEFYDNL 382
Cdd:TIGR03088 307 NPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSINAMVAAYAGLYDQL 373
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
15-372 |
1.98e-23 |
|
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340826 [Multi-domain] Cd Length: 355 Bit Score: 100.04 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 15 GADKVLLELIKGLDHKEFEAHVILPNDgvlvevlRQVGAKVSVLDYPILRRKYFnpKGIADYIRSYNFYAKQIALYArqh 94
Cdd:cd03795 15 GIEQVIYDLAEGLKKKGIEVDVLCFSK-------EKETPEKEENGIRIHRVKSF--LNVASTPFSPSYIKRFKKLAK--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 95 SIDMVHN---NTAAVLegIYLKRKLKLPLIWHVHEIIVKPKAISDFINMLMGRY---ADKIVTVSqavANHIEQSPFIKD 168
Cdd:cd03795 83 EYDIIHYhfpNPLADL--LLFFSGAKKPVVVHWHSDIVKQKKLLKLYKPLMTRFlrrADRIIATS---PNYVETSPTLRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 169 SQ--VEVIYNGVDNAVYYPMDASSIREKFDIAQDALVIgMIGRVNAIKGQNDFIEAVEPLlekneKAVAFLAGgvfhgeE 246
Cdd:cd03795 158 FKnkVRVIPLGIDKNVYNIPRVDFENIKREKKGKKIFL-FIGRLVYYKGLDYLIEAAQYL-----NYPIVIGG------E 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 247 WRL-EELDNRIA--SSSVVSQIHRIDYYDKTSeLYNMFDIFVLPSI-KPDSLPTVVLEAMACSKPVVGYN-NGGIAEMVV 321
Cdd:cd03795 226 GPLkPDLEAQIElnLLDNVKFLGRVDDEEKVI-YLHLCDVFVFPSVlRSEAFGIVLLEAMMCGKPVISTNiGTGVPYVNN 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 48474171 322 DDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQRELFSLESYI 372
Cdd:cd03795 305 NGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEKMK 355
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
79-379 |
3.36e-22 |
|
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: 96.65 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 79 SYNFY----AKQIALYARQHSIDMVH------NNTAAVLEGIYLKRKLKLPLIWHVHEIIV--KPKAISDFINMLMGRyA 146
Cdd:cd04962 64 EYPPYtlalASKIVEVAKEHKLDVLHahyaipHASCAYLAREILGEKIPIVTTLHGTDITLvgYDPSLQPAVRFSINK-S 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 147 DKIVTVSQAVANHIeQSPFIKDSQVEVIYNGVDNAVYYPMDASSIREKFDIAQDALVIGMIGRVNAIKGQNDFIEAVEpL 226
Cdd:cd04962 143 DRVTAVSSSLRQET-YELFDVDKDIEVIHNFIDEDVFKRKPAGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFA-R 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 227 LEKNEKAVAFLAGgvfHGEEwrLEELDNRIASSSVVSQIHRIDYYDKTSELYNMFDIFVLPSIKpDSLPTVVLEAMACSK 306
Cdd:cd04962 221 VRRKIPAKLLLVG---DGPE--RVPAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEK-ESFGLAALEAMACGV 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48474171 307 PVVGYNNGGIAEMVVDDKSGYLVKPNRPQELS-NAISLLLDsSEKREKFGRVGYQRQRELFSLESYIKNFSEFY 379
Cdd:cd04962 295 PVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAkSALSILED-DELYNRMGRAARKRAAERFDPERIVPQYEAYY 367
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
19-373 |
4.27e-21 |
|
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: 93.20 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 19 VLLELIKGLdHKEFEAHVILPNDGVLVEVLRqvgakvsVLDYPILRRKYFNPKGIADYIRSYNFYAKQIALYARQHSIDM 98
Cdd:cd03809 19 YTRELLKAL-AKNDPDESVLAVPPLPGELLR-------LLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKPDLLHS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 99 VHNNTAAVLEGI-----------YLKRKLKLPLIWHVHEIIVKpkaisdfinmLMGRYADKIVTVSQAVANHIEQSPFIK 167
Cdd:cd03809 91 PHNTAPLLLKGCpqvvtihdlipLRYPEFFPKRFRLYYRLLLP----------ISLRRADAIITVSEATRDDIIKFYGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 168 DSQVEVIYNGVDnAVYYPMDASSIREKFDIAQDALVIgMIGRVNAIKGQNDFIEAVEPLLEKNEKAVAFLAGgvfhGEEW 247
Cdd:cd03809 161 PEKIVVIPLGVD-PSFFPPESAAVLIAKYLLPEPYFL-YVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVG----GKGW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 248 RLEELDNRIASSSVVSQIHRIDY--YDKTSELYNMFDIFVLPSI-KPDSLPtvVLEAMACSKPVVGYNNGGIAEmvVDDK 324
Cdd:cd03809 235 EDEELLDLVKKLGLGGRVRFLGYvsDEDLPALYRGARAFVFPSLyEGFGLP--VLEAMACGTPVIASNISVLPE--VAGD 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 48474171 325 SGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQReLFSLESYIK 373
Cdd:cd03809 311 AALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAK-KFSWEKTAE 358
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
82-379 |
1.54e-19 |
|
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: 89.04 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 82 FYAKQIALYARQHSI--DMVHNNTAAVLEGIYLKrklKLPLIWHVHEiivkpKAISDFINMLMGRY----ADKIVTVSQ- 154
Cdd:cd04951 69 LKLKKIISAFKPDVVhsHMFHANIFARFLRMLYP---IPLLICTAHN-----KNEGGRIRMFIYRLtdflCDITTNVSRe 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 155 AVANHIEQSPFIKDSQVEViYNGVDNAV--YYPMDASSIREKFDIAQDALVIGMIGRVNAIKGQNDFIEAVEPLLEKNEK 232
Cdd:cd04951 141 ALDEFIAKKAFSKNKSVPV-YNGIDLNKfkKDINVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKND 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 233 AVAFLAGgvfHGEewRLEELDNRIASSSVVSQIHRIDYYDKTSELYNMFDIFVLPSiKPDSLPTVVLEAMACSKPVVGYN 312
Cdd:cd04951 220 FKLLIAG---DGP--LRNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSS-EWEGFGLVVAEAMACERPVVATD 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48474171 313 NGGIAEmVVDDkSGYLVKPNRPQELSNAIS-LLLDSSEKREKFGRVGYQRQRElFSLESYIKNFSEFY 379
Cdd:cd04951 294 AGGVAE-VVGD-HNYVVPVSDPQLLAEKIKeIFDMSDEERDILGNKNEYIAKN-FSINTIVNEWERLY 358
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
3-309 |
1.94e-19 |
|
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: 88.50 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 3 RILYLHAGAEMYGADKVLLELIKGLDHKEFEAHVILPND--GVLVEVLRQVGAKVSVLDYpilRRKYFnpkgIADYIRSY 80
Cdd:cd03812 1 KILHIVGGMNVGGIETFLMNLYRKLDKSKIEFDFLATSDdkGEYDEELEELGGKIFYIPP---KKKNI----IKYFIKLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 81 NFYAKqialyarqHSIDMVHNNTAAVLEGIYLK-RKLKLP-LIWHVH----EIIVKPKAISDFINMLMGRYADKIVTVSQ 154
Cdd:cd03812 74 KLIKK--------EKYDIVHVHGSSSNGIILLLaAKAGVPvRIAHSHntkdSSIKLRKIRKNVLKKLIERLSTKYLACSE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 155 AVANHIEQSPFIKdsQVEVIYNGVDNAVY-YPMDASSIREKFDIAQDALVIGMIGRVNAIKGQNDFIEAVEPLLEKNEKA 233
Cdd:cd03812 146 DAGEWLFGEVENG--KFKVIPNGIDIEKYkFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNV 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 48474171 234 VAFLAGgvfHGEEwrLEELDNRIASSSVVSQIHRIDYYDKTSELYNMFDIFVLPSiKPDSLPTVVLEAMACSKPVV 309
Cdd:cd03812 224 KLVLVG---EGEL--KEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPS-LYEGLPLVAVEAQASGLPCL 293
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
146-380 |
5.71e-17 |
|
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: 81.19 E-value: 5.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 146 ADKIVTVSQAVANHIEQSPFikdSQVEVIYNGVDNAVYYPMDAS-SIREKFDIAQDALVIgMIGRVNAIKGQNDFIEAVE 224
Cdd:cd03814 146 FDTTLVPSPSIARELEGHGF---ERVRLWPRGVDTELFHPSRRDaALRRRLGPPGRPLLL-YVGRLAPEKNLEALLDADL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 225 PLLEKNEKAVAFLAGG-------------VFHGEEWRlEELDNRIASSsvvsqihridyydktselynmfDIFVLPSIKp 291
Cdd:cd03814 222 PLAASPPVRLVVVGDGparaeleargpdvIFTGFLTG-EELARAYASA----------------------DVFVFPSRT- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 292 DSLPTVVLEAMACSKPVVGYNNGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQRElFSLESY 371
Cdd:cd03814 278 ETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAER-YSWEAF 356
|
....*....
gi 48474171 372 IKNFSEFYD 380
Cdd:cd03814 357 LDNLLDYYA 365
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
15-179 |
9.82e-17 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 77.19 E-value: 9.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 15 GADKVLLELIKGLDHKEFEAHVILPNDGVLVEVLRQVGAKVSVLDYPILRRKYFNPkgiadyirsynFYAKQIALYARQH 94
Cdd:pfam13439 2 GVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSL-----------AFLRRLRRLLRRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 95 SIDMVHNNT--AAVLEGIYLKRKLKLPLIWHVHEII-------VKPKAISDFINMLM---GRYADKIVTVSQAVANHIEQ 162
Cdd:pfam13439 71 RPDVVHAHSpfPLGLAALAARLRLGIPLVVTYHGLFpdykrlgARLSPLRRLLRRLErrlLRRADRVIAVSEAVADELRR 150
|
170
....*....|....*..
gi 48474171 163 SPFIKDSQVEVIYNGVD 179
Cdd:pfam13439 151 LYGVPPEKIRVIPNGVD 167
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
206-329 |
1.61e-16 |
|
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: 78.21 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 206 MIGRVNAIKGQNDFIEAVEPLLEKNEKAVAFLAGGVFHGEEWRLEELDNRIASSsvVSQIHRIDYYDKTSELYNMFDIFV 285
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLER--VVIIGGLVDDEVLELLLAAADVFV 192
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 48474171 286 LPSIkPDSLPTVVLEAMACSKPVVGYNNGGIAEMVVDDKSGYLV 329
Cdd:cd01635 193 LPSR-SEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
97-356 |
5.33e-16 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 78.98 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 97 DMVHNNT--AAVLEGIYLKRKLKLPLI--WHVHEIIVKP--------KAISDFINMLMgRYADKIVTVSQAVANHIEQSP 164
Cdd:PLN02871 146 DLIHASSpgIMVFGALFYAKLLCVPLVmsYHTHVPVYIPrytfswlvKPMWDIIRFLH-RAADLTLVTSPALGKELEAAG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 165 FIKDSQVEVIYNGVDNAVYYPMDAS-SIREKF-DIAQDALVIGMIGRVNAIKGqndfIEAVEPLLEKNEKA-VAFLAGGV 241
Cdd:PLN02871 225 VTAANRIRVWNKGVDSESFHPRFRSeEMRARLsGGEPEKPLIVYVGRLGAEKN----LDFLKRVMERLPGArLAFVGDGP 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 242 FHgeewrlEELDNRIASSSVV--SQIHRidyyDKTSELYNMFDIFVLPSiKPDSLPTVVLEAMACSKPVVGYNNGGIAEM 319
Cdd:PLN02871 301 YR------EELEKMFAGTPTVftGMLQG----DELSQAYASGDVFVMPS-ESETLGFVVLEAMASGVPVVAARAGGIPDI 369
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 48474171 320 VVDD---KSGYLVKPNRPQELSNAISLLLDSSEKREKFGR 356
Cdd:PLN02871 370 IPPDqegKTGFLYTPGDVDDCVEKLETLLADPELRERMGA 409
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
161-369 |
1.39e-15 |
|
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: 77.41 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 161 EQSPFIKDSQVEVIYNGVDNAVYYPmdASSIREKFDIAQDALVIGMIGRVNAIKGQNDFIEAVEPLLEKNEKAVAFLAGG 240
Cdd:cd03821 166 ELRRFGLEPPIAVIPNGVDIPEFDP--GLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 241 VFHGEEWRLEEldnrIASSSVVSQIHRID--YYDKTSELYNMFDIFVLPSIKpDSLPTVVLEAMACSKPVVGYNNGGIAE 318
Cdd:cd03821 244 DDGAYPAFLQL----QSSLGLGDRVTFTGplYGEAKWALYASADLFVLPSYS-ENFGNVVAEALACGLPVVITDKCGLSE 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 48474171 319 MVVDDkSGYLVKPNrPQELSNAISLLLDSSEKREKFGRVG--YQRQRELFSLE 369
Cdd:cd03821 319 LVEAG-CGVVVDPN-VSSLAEALAEALRDPADRKRLGEMArrARQVEENFSWE 369
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
142-369 |
8.33e-15 |
|
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.
Pssm-ID: 340834 [Multi-domain] Cd Length: 392 Bit Score: 75.32 E-value: 8.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 142 MGrYADKIVTVSQAVANHIEQS-PFIKDSQVEVIYNGVDNAVYYPMDASSIREKFDIAQDALVIGMIGRVNAIKGQNDFI 220
Cdd:cd03805 152 TG-MADQIVVNSNFTAGVFKKTfPSLAKNPPEVLYPCVDTDSFDSTSEDPDPGDLIAKSNKKFFLSINRFERKKNIALAI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 221 EAVEPLLEKNEKAVAF---LAGGVfhgeewrleelDNRIASSsvvsqihrIDYY----DKTSELYNM-FDIFVLPSIkPD 292
Cdd:cd03805 231 EAFAKLKQKLPEFENVrlvIAGGY-----------DPRVAEN--------VEYLeelqRLAEELLNVeDQVLFLRSI-SD 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 293 SL--------------PT------VVLEAMACSKPVVGYNNGGIAEMVVDDKSGYLVKPNrPQELSNAISLLLDSSEKRE 352
Cdd:cd03805 291 SQkeqllssalallytPSnehfgiVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEPT-PEAFAEAMLKLANDPDLAD 369
|
250
....*....|....*..
gi 48474171 353 KFGRVGYQRQRELFSLE 369
Cdd:cd03805 370 RMGAAGRKRVKEKFSRE 386
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
53-365 |
1.47e-14 |
|
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: 74.34 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 53 AKVSVLDYPILRRKYFNPKGIADYIRSYNFYAkQIALYARqhSIDMVH-------NNTAAVLEGIYLKRKLKLPLIWHVH 125
Cdd:cd03822 36 VIVSPQDEILKDDDFEVPNEIKSWNSNEYFRL-LDHLNFK--KPDVVHiqhefgiFGGKYGLYALGLLLHLRIPVITTLH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 126 EII--VKPKAISDFINMLMGRYADKIVTVSQAVANHIEQSPFIKDSQVEVIYNGVDNavyYPMDASSIREKFDIAQDALV 203
Cdd:cd03822 113 TVLdlSDPGKQALKVLFRIATLSERVVVMAPISRFLLVRIKLIPAVNIEVIPHGVPE---VPQDPTTALKRLLLPEGKKV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 204 IGMIGRVNAIKGQNDFIEAVEPLLEKNEKAVAFLAGGVfHGEEWRLE---ELDNRIASSSVVSQIHRIDYYDKTSELY-- 278
Cdd:cd03822 190 ILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGEL-HPSLARYEgerYRKAAIEELGLQDHVDFHNNFLPEEEVPry 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 279 -NMFDIFVLPSikPDSLPT---VVLEAMACSKPVVGYNNGGIAEMVVDDkSGYLVKPNRPQELSNAISLLLDSSEKREKF 354
Cdd:cd03822 269 iSAADVVVLPY--LNTEQSssgTLSYAIACGKPVISTPLRHAEELLADG-RGVLVPFDDPSAIAEAILRLLEDDERRQAI 345
|
330
....*....|.
gi 48474171 355 GRVGYQRQREL 365
Cdd:cd03822 346 AERAYAYARAM 356
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
91-368 |
3.19e-14 |
|
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: 73.26 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 91 ARQHSIDMVHNNTAavLEGIY---LKRKLKLPLI--WHVHEIIVKPKAISDFINMLMGRYADKIVTVSQAvANHIEQSPF 165
Cdd:cd05844 77 AAGLAPALVHAHFG--RDGVYalpLARALGVPLVvtFHGFDITTSRAWLAASPGWPSQFQRHRRALQRPA-ALFVAVSGF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 166 IKDS---------QVEVIYNGVDNAVYYPMDAssirekfdiAQDALVIGMIGRVNAIKGQNDFIEAVEPLLEKNEKAVAF 236
Cdd:cd05844 154 IRDRllarglpaeRIHVHYIGIDPAKFAPRDP---------AERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 237 LAGGvfhGEEwrLEELDNRIASSSVVSQIHRIDYyDKTSELYNMFDIFVLPSIKPDS-----LPTVVLEAMACSKPVVGY 311
Cdd:cd05844 225 IAGD---GPL--RPALQALAAALGRVRFLGALPH-AEVQDWMRRAEIFCLPSVTAASgdsegLGIVLLEAAACGVPVVSS 298
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 48474171 312 NNGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQRELFSL 368
Cdd:cd05844 299 RHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFDI 355
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
148-352 |
7.00e-12 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 66.35 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 148 KIVTVSQAVANHIEQspFIKDSQVEVIYNGVDNAVYYPMDASSIREKFDIAQDALVIGMIGRVNAIKGQNDFIEAVEPLL 227
Cdd:PRK15484 142 KIIVPSQFLKKFYEE--RLPNADISIVPNGFCLETYQSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 228 EKNEKAVAFLAGGVFHGEEWRLEELDNRI--ASSSVVSQIHRIDYY--DKTSELYNMFDIFVLPSIKPDSLPTVVLEAMA 303
Cdd:PRK15484 220 TAHSNLKLVVVGDPTASSKGEKAAYQKKVleAAKRIGDRCIMLGGQppEKMHNYYPLADLVVVPSQVEEAFCMVAVEAMA 299
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 48474171 304 CSKPVVGYNNGGIAEMVVDDKSGY-LVKPNRPQELSNAISLLLDSSEKRE 352
Cdd:PRK15484 300 AGKPVLASTKGGITEFVLEGITGYhLAEPMTSDSIISDINRTLADPELTQ 349
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
87-382 |
1.11e-11 |
|
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: 65.39 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 87 IALYARQHSIDMVHNNtaavlegiylkrkLKLPLIWHVHEIIVKpkaisdFINMLMGRYADKIVTVSQAVAN-------H 159
Cdd:cd03802 78 LEVQLRASDFDVIHNH-------------SYDWLPPFAPLIGTP------FVTTLHGPSIPPSLAIYAAEPPvnyvsisD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 160 IEQSPFIKDSQVEVIYNGVDNAVYYPMDAssirekfdiAQDALviGMIGRVNAIKGQNDFIEAVE----PLleknekava 235
Cdd:cd03802 139 AQRAATPPIDYLTVVHNGLDPADYRFQPD---------PEDYL--AFLGRIAPEKGLEDAIRVARraglPL--------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 236 FLAGGVFHGEEWRLEeldNRIASSSVVSQIHRIDYYDKTSELYN----MFdifvlPSIKPDSLPTVVLEAMACSKPVVGY 311
Cdd:cd03802 199 KIAGKVRDEDYFYYL---QEPLPGPRIEFIGEVGHDEKQELLGGaralLF-----PINWDEPFGLVMIEAMACGTPVIAY 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48474171 312 NNGGIAEMVVDDKSGYLVKPnrPQELSNAIsllldssEKREKFGRVGYQRQ-RELFSLESYIKNFSEFYDNL 382
Cdd:cd03802 271 RRGGLPEVIQHGETGFLVDS--VEEMAEAI-------ANIDRIDRAACRRYaEDRFSAARMADRYEALYRKV 333
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
204-374 |
2.10e-11 |
|
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: 64.24 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 204 IGMIGRVNAIKGQNDFIEAVEPLLEKNEKAVAFLAGgvfHGEEwrLEELDNRIASSSVVSQIHRIDYYDKTSELYNMFDI 283
Cdd:cd04949 163 IITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYG---YGEE--REKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 284 FVLPSIKpDSLPTVVLEAMACSKPVVGYN-NGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQ 362
Cdd:cd04949 238 SLLTSQM-EGFGLTLMEAIGHGLPVVSYDvKYGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIA 316
|
170
....*....|..
gi 48474171 363 RElFSLESYIKN 374
Cdd:cd04949 317 EK-YSTENVMEK 327
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
15-177 |
3.73e-09 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 55.10 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 15 GADKVLLELIKGLDHKEFEAHVILPNDGVLVEVLRQVGAKVSVLdyPILRRkyfnPKGIADYIRSYNFYAkqialYARQH 94
Cdd:pfam13579 2 GIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRL--PVPPR----PSPLADLAALRRLRR-----LLRAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 95 SIDMVH--NNTAAVLeGIYLKRKLKLPLIWHVHEIIVKP-----KAISDFINMLMGRYADKIVTVSQAVANHIEQSpFIK 167
Cdd:pfam13579 71 RPDVVHahSPTAGLA-ARLARRRRGVPLVVTVHGLALDYgsgwkRRLARALERRLLRRADAVVVVSEAEAELLRAL-GVP 148
|
170
....*....|
gi 48474171 168 DSQVEVIYNG 177
Cdd:pfam13579 149 AARVVVVPNG 158
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
164-377 |
8.94e-09 |
|
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: 56.60 E-value: 8.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 164 PFIKDsQVEVIYNGVDNAVYYPMDASSIREKFD--IAQDALVIGMIGR-VNAIKGQNDFIEAVEPLLEKNEKAVAFLAGG 240
Cdd:cd03818 175 AAYRD-RISVIHDGVDTDRLAPDPAARLRLLNGteLKAGDPVITYVARnLEPYRGFHVFMRALPRIQARRPDARVVVVGG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 241 --------VFHGEEWR---LEELD---NRIASSSVVSqihridyYDKTSELYNMFDIFVLPSiKPDSLPTVVLEAMACSK 306
Cdd:cd03818 254 dgvsygspPPDGGSWKqkmLAELGvdlERVHFVGKVP-------YDQYVRLLQLSDAHVYLT-YPFVLSWSLLEAMACGC 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 48474171 307 PVVGYNNGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQRELFSLESYIKNFSE 377
Cdd:cd03818 326 PVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCLARYLA 396
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
7-357 |
9.38e-08 |
|
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: 53.72 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 7 LHAGAEMYGADK------VLLELIKGLDHKEFEAHVILP-------------------------NDGVLVEVLRQVGAKV 55
Cdd:cd03791 3 LFVTSEVAPFAKtgglgdVAGALPKALAKLGHDVRVILPrygqipdeldgylrvlglevkvggrGEEVGVFELPVDGVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 56 SVLDYPIL-RRKYFNPKGIADYI---RSYNFYAKQIALYARQHSI--DMVHNN---TAAVLegIYLKRK----------- 115
Cdd:cd03791 83 YFLDNPEFfDRPGLPGPPGYDYPdnaERFAFFSRAALELLRRLGFqpDIIHANdwhTALVP--AYLKTRyrgpgfkkikt 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 116 --------------------LKLPLIWHVHEIIVKPkaisDFINMLMG--RYADKIVTVSQAVANHIEQSPF-------- 165
Cdd:cd03791 161 vftihnlayqglfpldtlaeLGLPPELFHIDGLEFY----GQINFLKAgiVYADRVTTVSPTYAKEILTPEYgegldgvl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 166 -IKDSQVEVIYNGVDNAVYYPM---------DASSIREK------------FDIAQDALVIGMIGRVNAIKGQNDFIEAV 223
Cdd:cd03791 237 rARAGKLSGILNGIDYDEWNPAtdklipanySANDLEGKaenkaalqkelgLPVDPDAPLFGFVGRLTEQKGVDLILDAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 224 EPLLEKNEKaVAFLAGGvfhgeEWRLEELDNRIAsssvvSQIH-----RIDYYDKTS-ELYNMFDIFVLPSI-KPDSLpt 296
Cdd:cd03791 317 PELLEEGGQ-LVVLGSG-----DPEYEQAFRELA-----ERYPgkvavVIGFDEALAhRIYAGADFFLMPSRfEPCGL-- 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 48474171 297 VVLEAMACSKPVVGYNNGGIAEMVVD------DKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRV 357
Cdd:cd03791 384 VQMYAMRYGTLPIVRRTGGLADTVFDydpetgEGTGFVFEDYDAEALLAALRRALALYRNPELWRKL 450
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
141-375 |
2.48e-07 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 52.29 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 141 LMGRYaDKIVTVSQAVANHIEQSPfIKDSQVEVIYNGVDNAVYYPM---DASSIREKFDIAQDALVIGMIGRVNAIKGQN 217
Cdd:PRK10307 168 LLRRF-DNVSTISRSMMNKAREKG-VAAEKVIFFPNWSEVARFQPVadaDVDALRAQLGLPDGKKIVLYSGNIGEKQGLE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 218 DFIEAVEPLLEKNEKAVAFLAGGVFHGeewRLEELdnriASSSVVSQIHRIDY--YDKTSELYNMFDIFVLPSIK--PDS 293
Cdd:PRK10307 246 LVIDAARRLRDRPDLIFVICGQGGGKA---RLEKM----AQCRGLPNVHFLPLqpYDRLPALLKMADCHLLPQKAgaADL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 294 -LPTVVLEAMACSKPVVGYNNGG--IAEMVvdDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGRVGYQRQRELFSLES 370
Cdd:PRK10307 319 vLPSKLTNMLASGRNVVATAEPGteLGQLV--EGIGVCVEPESVEALVAAIAALARQALLRPKLGTVAREYAERTLDKEN 396
|
....*
gi 48474171 371 YIKNF 375
Cdd:PRK10307 397 VLRQF 401
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
144-358 |
2.53e-07 |
|
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274943 [Multi-domain] Cd Length: 373 Bit Score: 52.01 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 144 RYADKIVTVSQAVANHIEQSPFIKDSqveVIYNGVDNAVYYPM---DASSIREKFDIAQDALVIGmIGRVNAIKGQNDFI 220
Cdd:TIGR04047 137 VEADAVLCVSAAWAAELRAEWGIDAT---VVPNGVDAARFSPAadaADAALRRRLGLRGGPYVLA-VGGIEPRKNTIDLL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 221 EAVEPLLEKNEKAVAFLAGG--VFHGEEWRlEELDNRIASSSV-VSQIH---RIDYYDKTSeLYNMFDIFVLPSIKpDSL 294
Cdd:TIGR04047 213 EAFALLRARRPQAQLVIAGGatLFDYDAYR-REFRARAAELGVdPGPVVitgPVPDADLPA-LYRCADAFAFPSLK-EGF 289
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48474171 295 PTVVLEAMACSKPVVGYNNGGIAEMvVDDKSGYLVKPNRPQELSNAISLLLDSSeKREKFGRVG 358
Cdd:TIGR04047 290 GLVVLEALASGIPVVASDIAPFTEY-LGRFDAAWADPSDPDSIADALALALDPA-RRPALRAAG 351
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
282-366 |
6.67e-07 |
|
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: 50.53 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 282 DIFVLPSIKP-----DSLPTVVLEAMACSKPVVGYNNGGIAEMVVDDKSGYLVKPNRPQELSNAISLLLDSSEKREKFGR 356
Cdd:cd03799 252 DIFIAPSVTAadgdqDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGK 331
|
90
....*....|
gi 48474171 357 VGYQRQRELF 366
Cdd:cd03799 332 AGRARVEEEY 341
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
166-380 |
1.52e-06 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 50.03 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 166 IKDSQVEVIYNGV----------DNAVYYPMDASSIREKFdiaqdalVIGMIGRVNAIKGQNDFIEAVEPLLEKNEKA-V 234
Cdd:PRK15179 479 VDERRIPVVYNGLaplksvqddaCTAMMAQFDARTSDARF-------TVGTVMRVDDNKRPFLWVEAAQRFAASHPKVrF 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 235 AFLAGGVFHGEewrLEELDNRIASSS---VVSQIHRIDYYdktselYNMFDIFVLPSiKPDSLPTVVLEAMACSKPVVGY 311
Cdd:PRK15179 552 IMVGGGPLLES---VREFAQRLGMGErilFTGLSRRVGYW------LTQFNAFLLLS-RFEGLPNVLIEAQFSGVPVVTT 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 48474171 312 NNGGIAEMVVDDKSGYLVKPNRPQ--ELSNAISLLLDSSEKREKFGRVGYQRQRELFSLESYIKNFSEFYD 380
Cdd:PRK15179 622 LAGGAGEAVQEGVTGLTLPADTVTapDVAEALARIHDMCAADPGIARKAADWASARFSLNQMIASTVRCYQ 692
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
258-375 |
3.20e-06 |
|
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.
Pssm-ID: 340823 [Multi-domain] Cd Length: 378 Bit Score: 48.86 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 258 SSSVVSQIHRIDYYDKtselynmfDIFVLPSIKPDSL--------------------PTVVLEAMACSKPVVGYNNGGIA 317
Cdd:cd03792 244 GSVVYEEVMEYAGDDH--------DIHVLRLPPSDQEinalqraatvvlqlstregfGLTVSEALWKGKPVIATPAGGIP 315
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 48474171 318 EMVVDDKSGYLVkpNRPQELSNAISLLLDSSEKREKFGRVGYQRQRELFSLESYIKNF 375
Cdd:cd03792 316 LQVIDGETGFLV--NSVEGAAVRILRLLTDPELRRKMGLAAREHVRDNFLITGNLRAW 371
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
283-361 |
5.19e-06 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 44.52 E-value: 5.19e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48474171 283 IFVLPSIKPDSLPTVVLEAMACSKPVVGYNNGGIAEMVVDDKSGYLVKpnRPQELSNAISLLLDSSEKREKFGRVGYQR 361
Cdd:pfam13524 1 IVLNPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRER 77
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
298-341 |
6.47e-06 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 48.05 E-value: 6.47e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 48474171 298 VLEAMACSKPVVGYNNGGIAEMVVDDKSGYLVKPNRPQELSNAI 341
Cdd:PLN00142 683 VVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDEAANKI 726
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
276-379 |
1.65e-05 |
|
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.
Pssm-ID: 340854 [Multi-domain] Cd Length: 401 Bit Score: 46.68 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 276 ELY--NMFDIFVLPSiKPDSLPTVVLEAMACSKPVVGYNNGGIAEMVVDDKSGYL-VKPNRPQELSNAISLLLDSSEKRE 352
Cdd:cd04946 298 QLYkeNDVDVFVNVS-ESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLLlDKDPTPNEIVSSIMKFYLDGGDYK 376
|
90 100
....*....|....*....|....*..
gi 48474171 353 KFGRVGYQRQRELFSLEsyiKNFSEFY 379
Cdd:cd04946 377 TMKISARECWEERFNAE---VNYSKFA 400
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
297-376 |
2.35e-04 |
|
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: 42.66 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 297 VVLEAMACSKPVVGYNNGGIAEMVVDDKSGYLVKPNRPQELSNAISLLldsSEKREKFGRVGYQRQRELFSLESYIKNFS 376
Cdd:cd03804 280 VPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEF---EQNFDRFKPQAIRANAERFSRARFRQEIR 356
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
145-240 |
1.14e-03 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 40.86 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 145 YADKIVTVSQAVANHIeQSP----------FIKDSQVEVIYNGVDNAVYYPMDASSIREKFDIAQ--------------- 199
Cdd:PRK14099 209 LADRITTVSPTYALEI-QGPeagmgldgllRQRADRLSGILNGIDTAVWNPATDELIAATYDVETlaaraankaalqarf 287
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 48474171 200 ------DALVIGMIGRVNAIKGQNDFIEAVePLLEKNEKAVAFLAGG 240
Cdd:PRK14099 288 gldpdpDALLLGVISRLSWQKGLDLLLEAL-PTLLGEGAQLALLGSG 333
|
|
| PRK05749 |
PRK05749 |
3-deoxy-D-manno-octulosonic-acid transferase; Reviewed |
299-372 |
6.60e-03 |
|
3-deoxy-D-manno-octulosonic-acid transferase; Reviewed
Pssm-ID: 235589 [Multi-domain] Cd Length: 425 Bit Score: 38.28 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 299 LEAMACSKPVV-G---YNNGGIAEMVVDDKSGYLVKPnrPQELSNAISLLLDSSEKREKFGRVGYQR--------QRELF 366
Cdd:PRK05749 338 LEPAAFGVPVIsGphtFNFKEIFERLLQAGAAIQVED--AEDLAKAVTYLLTDPDARQAYGEAGVAFlkqnqgalQRTLQ 415
|
....*.
gi 48474171 367 SLESYI 372
Cdd:PRK05749 416 LLEPYL 421
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
138-230 |
9.67e-03 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 37.76 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48474171 138 INMLMG--RYADKIVTVSQAVANHIeQSPFI----------KDSQVEVIYNGVDNAVYYPM---------DASSIREK-- 194
Cdd:COG0297 200 INFLKAgiVYADRVTTVSPTYAREI-QTPEFgegldgllraRSGKLSGILNGIDYDVWNPAtdpylpanySADDLEGKaa 278
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 48474171 195 ----------FDIAQDALVIGMIGRVNAIKGQnDFI-EAVEPLLEKN 230
Cdd:COG0297 279 nkaalqeelgLPVDPDAPLIGMVSRLTEQKGL-DLLlEALDELLEED 324
|
|
| |
