|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
80-358 |
6.92e-59 |
|
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: 194.91 E-value: 6.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 80 PDVVHAHYATSYGLLGALSGF---HPYIISVWGSDVYDFPKGSYiKRKMVEYNLSKADIIMSTSKVMAEE-TNQYTTK-N 154
Cdd:cd03798 96 PDLIHAHFAYPAGFAAALLARlygVPYVVTEHGSDINVFPPRSL-LRKLLRWALRRAARVIAVSKALAEElVALGVPRdR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 155 IEITPFGVNIDTFKPCADKYEKKEN-LVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELN 233
Cdd:cd03798 175 VDVIPNGVDPARFQPEDRGLGLPLDaFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 234 IKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILVNKKSVDEL 313
Cdd:cd03798 255 LGDRVTFTGRLPHEQVPAYYRACDVFVLPSR--HEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADAL 332
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 920955171 314 AEAIEKLIkDDNLRINMGKTGRKFVEDNFNIEDNFNNVDIIYKSI 358
Cdd:cd03798 333 AAALRRAL-AEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
11-345 |
2.75e-58 |
|
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: 193.14 E-value: 2.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 11 STHTKKWCRFFKNKGYDIDVISLNDGDIDGVTVHSFNKDLDKIRKGSSFNKISYIRYFSdikKIIEKIKPDVVHAHYATS 90
Cdd:cd03801 17 ERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELR---PLLRLRKFDVVHAHGLLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 91 --YGLLGALSGFHPYIISVWGSDVYDFPKGSYIKRKMV---EYNLSKADIIMSTSKVMAEETNQY---TTKNIEITPFGV 162
Cdd:cd03801 94 alLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLaraEALLRRADAVIAVSEALRDELRALggiPPEKIVVIPNGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 163 NIDTFKPC--ADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGV-GDQKDFLLNLcnELNIKDHVK 239
Cdd:cd03801 174 DLERFSPPlrRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGdGPLRAELEEL--ELGLGDRVR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 240 FLGFINQEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILVNKKSVDELAEAIEK 319
Cdd:cd03801 252 FLGFVPDEELPALYAAADVFVLPS--RYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLR 329
|
330 340
....*....|....*....|....*.
gi 920955171 320 LIKDDNLRINMGKTGRKFVEDNFNIE 345
Cdd:cd03801 330 LLADPELRARLGRAARERVAERFSWE 355
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
177-337 |
2.05e-47 |
|
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: 158.21 E-value: 2.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 177 KENLVIgTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGFINQEKVIEAFNRF 256
Cdd:pfam00534 1 KKKIIL-FVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 257 DVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILVNKKSVDELAEAIEKLIKDDNLRINMGKTGRK 336
Cdd:pfam00534 80 DVFVLPSR--YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157
|
.
gi 920955171 337 F 337
Cdd:pfam00534 158 R 158
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
2-345 |
1.31e-46 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
Pssm-ID: 340837 [Multi-domain] Cd Length: 358 Bit Score: 162.38 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 2 KICYLADANS---THTKKWCRFFKNKGYDIDVISLNDGDID------GVTVHSFNkdldkiRKGSSFNKISYIRYFSDIK 72
Cdd:cd03808 1 KILFIVNVDGgfqSFRLPLIKALVKKGYEVHVIAPDGDKLSdelkelGVKVIDIP------ILRRGINPLKDLKALFKLY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 73 KIIEKIKPDVVHAHyaTS----YGLLGALSGFHPYIISV---WGsdvYDFPKGSYIKR--KMVE-YNLSKADIIMSTSKV 142
Cdd:cd03808 75 KLLKKEKPDIVHCH--TPkpgiLGRLAARLAGVPKVIYTvhgLG---FVFTEGKLLRLlyLLLEkLALLFTDKVIFVNED 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 143 MAEETNQY---TTKNIEITP-FGVNIDTFKPcADKYEKKENLVIGTV-KTLEPKyGIEYLVRAFAKVKQKHNNIKLEIAG 217
Cdd:cd03808 150 DRDLAIKKgiiKKKKTVLIPgSGVDLDRFQY-SPESLPSEKVVFLFVaRLLKDK-GIDELIEAAKILKKKGPNVRFLLVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 218 VGDQKDFLLNLCNELNIKDHVKFLGFInqEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATA 297
Cdd:cd03808 228 DGELENPSEILIEKLGLEGRIEFLGFR--SDVPELLAESDVFVLPS--YREGLPRSLLEAMAAGRPVITTDVPGCRELVI 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 920955171 298 PNNSSILVNKKSVDELAEAIEKLIKDDNLRINMGKTGRKFVEDNFNIE 345
Cdd:cd03808 304 DGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEE 351
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
18-346 |
8.98e-44 |
|
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: 154.78 E-value: 8.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 18 CRFFKNKGYDIDVISLNDGDI-------DGVTVHSFNKDLDKirkgSSFNKISYIRYFSDIKkiiekikPDVVHAH--YA 88
Cdd:cd03807 22 LEHMDKSRFEHVVISLTGDGVlgeellaAGVPVVCLGLSSGK----DPGVLLRLAKLIRKRN-------PDVVHTWmyHA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 89 TSYGLLGA-LSGFHPYIISVWGSDvyDFPKGSYIKRKMvEYNLSKADI-IMSTSKVMAEETNQ--YTTKNIEITPFGVNI 164
Cdd:cd03807 91 DLIGGLAAkLAGGVKVIWSVRSSN--IPQRLTRLVRKL-CLLLSKFSPaTVANSSAVAEFHQEqgYAKNKIVVIYNGIDL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 165 DTFKPCADK--------YEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKD 236
Cdd:cd03807 168 FKLSPDDASrararrrlGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERLLLELGLED 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 237 HVKFLGfiNQEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEaTAPNNSSILVNKKSVDELAEA 316
Cdd:cd03807 248 RVHLLG--ERSDVPALLPAMDIFVLSS--RTEGFPNALLEAMACGLPVVATDVGGAAE-LVDDGTGFLVPAGDPQALADA 322
|
330 340 350
....*....|....*....|....*....|
gi 920955171 317 IEKLIKDDNLRINMGKTGRKFVEDNFNIED 346
Cdd:cd03807 323 IRALLEDPEKRARLGRAARERIANEFSIDA 352
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
2-140 |
5.23e-39 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 135.53 E-value: 5.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 2 KICYLADANSTHTKKWCRFFKNKGYDIDVISLNDGDID-----GVTVHSFNKDldkiRKGssfnKISYIRYFSdIKKIIE 76
Cdd:pfam13477 1 KILLLANADSIHTLRWADALADRGYDVHVISSKGPAKDeliaeGIHVHRLKVP----RKG----PLGYLKAFR-LKKLIK 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 920955171 77 KIKPDVVHAHYATSYGLLGAL----SGFHPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMSTS 140
Cdd:pfam13477 72 KIKPDVVHVHYAKPYGLLAGLaarlSGFPPVVLSAWGLDVYKFPNKSRLKKLLLKLNLKKATLIISTS 139
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-345 |
6.17e-37 |
|
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: 137.47 E-value: 6.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 2 KICYLAD-------ANSTHTKKWCRFFKNKGYDIDVI------------SLNDGDIDGVTVHSF-------NKDLDKIRK 55
Cdd:cd03794 1 KILLISQyypppkgAAAARVYELAKELVRRGHEVTVLtpspnyplgrifAGATETKDGIRVIRVklgpikkNGLIRRLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 56 GSSFNKISYIRYFsdikkiIEKIKPDVVHAH--YATSYGLLGALSGFH--PYIISV------WGSDVYDFPKGSYIK--R 123
Cdd:cd03794 81 YLSFALAALLKLL------VREERPDVIIAYspPITLGLAALLLKKLRgaPFILDVrdlwpeSLIALGVLKKGSLLKllK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 124 KMVEYNLSKADIIMSTSKVMAEETNQ--YTTKNIEITPFGVNIDTFKPCADKYEKKEN-----LVIGTVKTLEPKYGIEY 196
Cdd:cd03794 155 KLERKLYRLADAIIVLSPGLKEYLLRkgVPKEKIIVIPNWADLEEFKPPPKDELRKKLglddkFVVVYAGNIGKAQGLET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 197 LVRAFAKVKQkHNNIKLEIAGVGDQKDFLLNLCNELNIKDhVKFLGFINQEKVIEAFNRFDVAVFPstLDSESFGVAAV- 275
Cdd:cd03794 235 LLEAAERLKR-RPDIRFLFVGDGDEKERLKELAKARGLDN-VTFLGRVPKEEVPELLSAADVGLVP--LKDNPANRGSSp 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 920955171 276 ----EAQACGTPVIVSNVGGLPEATAPNNSSILVNKKSVDELAEAIEKLIKDDNLRINMGKTGRKFVEDNFNIE 345
Cdd:cd03794 311 sklfEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSRE 384
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
17-344 |
1.62e-36 |
|
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: 135.18 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 17 WCRFFKNKGYDIDVISLNDGDID------GVTVHSFNKDLDKIRKGSSFNKISYIRYFsdikkiIEKIKPDVVHAHYATS 90
Cdd:cd03811 21 LANALDKRGYDVTLVLLRDEGDLdkqlngDVKLIRLLIRVLKLIKLGLLKAILKLKRI------LKRAKPDVVISFLGFA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 91 YGLLGALSGFHPYIISVWGSDvYDFPKGSYIKRKMVEYNLSKADIIMSTSKVMAEE---TNQYTTKNIEITPFGVNIDTF 167
Cdd:cd03811 95 TYIVAKLAAARSKVIAWIHSS-LSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDlirLGPSPPEKIEVIYNPIDIDRI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 168 KPCADK---YEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGFi 244
Cdd:cd03811 174 RALAKEpilNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGLAERVIFLGF- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 245 nQEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILVNKKSVDELAE---AIEKLI 321
Cdd:cd03811 253 -QSNPYPYLKKADLFVLSS--RYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGilaALLQKK 329
|
330 340
....*....|....*....|...
gi 920955171 322 KDDNLRINMGKtGRKFVEDNFNI 344
Cdd:cd03811 330 LDAALRERLAK-AQEAVFREYTI 351
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
4-345 |
4.06e-36 |
|
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: 134.71 E-value: 4.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 4 CYLADAN--STHTKKWCRFFKNKGYDIDVISLNDGDidgvtvHSFNKDLDKIRKGSSFNKISYiRYF------SDIKKII 75
Cdd:cd03817 8 TYLPQVNgvATSVRNLARALEKRGHEVYVITPSDPG------AEDEEEVVRYRSFSIPIRKYH-RQHipfpfkKAVIDRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 76 EKIKPDVVHAHYATSYGLLGALSG----------FHpyiiSVWGSDVYDFPKGSYIKRKMVE------YNlsKADIIMST 139
Cdd:cd03817 81 KELGPDIIHTHTPFSLGKLGLRIArklkipivhtYH----TMYEDYLHYIPKGKLLVKAVVRklvrrfYN--HTDAVIAP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 140 SKVMAEETNQY-TTKNIEITPFGVNIDTFKPCADKYEKKENL------VIGTVKTLEPKYGIEYLVRAFAKVKQKhNNIK 212
Cdd:cd03817 155 SEKIKDTLREYgVKGPIEVIPNGIDLDKFEKPLNTEERRKLGlppdepILLYVGRLAKEKNIDFLLRAFAELKKE-PNIK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 213 LEIAGVGDQKDFLLNLCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGL 292
Cdd:cd03817 234 LVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFAST--TETQGLVYLEAMAAGLPVVAAKDPAA 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 920955171 293 PEATAPNNSSILVnKKSVDELAEAIEKLIKDDNLRINMGKTGRKFVEDNFNIE 345
Cdd:cd03817 312 SELVEDGENGFLF-EPNDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAK 363
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
11-345 |
6.44e-36 |
|
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: 134.03 E-value: 6.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 11 STHTKKWCRFFKNKGYDIDVISLNDGDIDGVTVHSFNKdLDKIRKGSSFNKISYIRYFSDIKKIIEKIKPDVVH-AHYAT 89
Cdd:cd03809 17 GRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYP-ELSLGVIKIKLWRELALLRWLQILLPKKDKPDLLHsPHNTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 90 SYGLLGAlsgfhPYIisVWgsdVYDF----------PKGSYIKRKMVEYNLSKADIIMSTSKVMAEETNQYT---TKNIE 156
Cdd:cd03809 96 PLLLKGC-----PQV--VT---IHDLiplrypeffpKRFRLYYRLLLPISLRRADAIITVSEATRDDIIKFYgvpPEKIV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 157 ITPFGVNIDTFKPCADKYEKKEN-------LVIGTvktLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDF-LLNL 228
Cdd:cd03809 166 VIPLGVDPSFFPPESAAVLIAKYllpepyfLYVGT---LEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEeLLDL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 229 CNELNIKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATAPnnSSILVNKK 308
Cdd:cd03809 243 VKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSL--YEGFGLPVLEAMACGTPVIASNISVLPEVAGD--AALYFDPL 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 920955171 309 SVDELAEAIEKLIKDDNLRINMGKTGRKFVEdNFNIE 345
Cdd:cd03809 319 DPESIADAILRLLEDPSLREELIRKGLERAK-KFSWE 354
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
80-343 |
1.08e-35 |
|
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: 133.90 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 80 PDVVHAHYATSyGLLGAL----SG------FH-------PYIIsvwGSDVYDFPKgsyikRKMVEYN-LSKAD-IIMSTS 140
Cdd:cd03800 102 YDLIHSHYWDS-GLVGALlarrLGvplvhtFHslgrvkyRHLG---AQDTYHPSL-----RITAEEQiLEAADrVIASTP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 141 KVMAEETNQYTTK--NIEITPFGVNIDTFKPCADKYEKKENL-------VIGTVKTLEPKYGIEYLVRAFAKVKQKHNNI 211
Cdd:cd03800 173 QEADELISLYGADpsRINVVPPGVDLERFFPVDRAEARRARLllppdkpVVLALGRLDPRKGIDTLVRAFAQLPELRELA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 212 KLEIAGvGDQKDFLLN-------LCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPV 284
Cdd:cd03800 253 NLVLVG-GPSDDPLSMdreelaeLAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSL--YEPFGLTAIEAMACGTPV 329
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 920955171 285 IVSNVGGLPEATAPNNSSILVNKKSVDELAEAIEKLIKDDNLRINMGKTGRKFVEDNFN 343
Cdd:cd03800 330 VATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYT 388
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
13-345 |
4.23e-35 |
|
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: 132.11 E-value: 4.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 13 HTKKWCRFFK---NKGYDIDVISLNDGDIDGVTV--HSFNKDLDKIRK----GSSFNKISYiRYFSDIKKIIEKIKPDVV 83
Cdd:cd03821 16 PVKVVLRLAAalaALGHEVTIVSTGDGYESLVVEenGRYIPPQDGFASipllRQGAGRTDF-SPGLPNWLRRNLREYDVV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 84 HAHYATSYGLLGAL---SGFH-PYIISVWGS-DVYDFPKgSYIKRKMVEY-----NLSKADIIMSTSKVMAEETN--QYT 151
Cdd:cd03821 95 HIHGVWTYTSLAACklaRRRGiPYVVSPHGMlDPWALQQ-KHWKKRIALHlierrNLNNAALVHFTSEQEADELRrfGLE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 152 TKnIEITPFGVNIDTFKPcADKYEKKENL-----VIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQK-DFL 225
Cdd:cd03821 174 PP-IAVIPNGVDIPEFDP-GLRDRRKHNGledrrIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDGAyPAF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 226 LNLCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSsiLV 305
Cdd:cd03821 252 LQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSY--SENFGNVVAEALACGLPVVITDKCGLSELVEAGCG--VV 327
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 920955171 306 NKKSVDELAEAIEKLIKDDNLRINMGKTGRKFV--EDNFNIE 345
Cdd:cd03821 328 VDPNVSSLAEALAEALRDPADRKRLGEMARRARqvEENFSWE 369
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
181-323 |
6.21e-35 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 124.93 E-value: 6.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 181 VIGTVKTLEPKY-GIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDfLLNLCNELNikDHVKFLGFINQekVIEAFNRFDVA 259
Cdd:pfam13692 3 VILFVGRLHPNVkGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEE-LEELAAGLE--DRVIFTGFVED--LAELLAAADVF 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 920955171 260 VFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEAtAPNNSSILVNKKSVDELAEAIEKLIKD 323
Cdd:pfam13692 78 VLPSL--YEGFGLKLLEAMAAGLPVVATDVGGIPEL-VDGENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
21-344 |
7.38e-35 |
|
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: 131.03 E-value: 7.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 21 FKNKGYDIDVISLNDGDIDgvTVHSfnkDLDKIRKgSSFNKISYIRYFSDIKKIiekikpDVVHAHYATSyGLLGAL--- 97
Cdd:cd03799 24 LIDRGHEVDIYAVNPGDLV--KRHP---DVEKYNV-PSLNLLYAIVGLNKKGAY------DIIHCQFGPL-GALGALlrr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 98 ---------SGFHPYIISVW----GSDVYD--FPKGS-------YIKRKMVEYNLSKADIIMSTSKVmaeETNQYTtkni 155
Cdd:cd03799 91 lkvlkgklvTSFRGYDISMYvileGNKVYPqlFAQGDlflpnceLFKHRLIALGCDEKKIIVHRSGI---DCNKFR---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 156 eitpfgvnidtFKPCADKYEKKenLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIK 235
Cdd:cd03799 164 -----------FKPRYLPLDGK--IRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 236 DHVKFLGFINQEKVIEAFNRFDVAVFPSTL----DSESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILVNKKSVD 311
Cdd:cd03799 231 DCVKLLGWKPQEEIIEILDEADIFIAPSVTaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAE 310
|
330 340 350
....*....|....*....|....*....|...
gi 920955171 312 ELAEAIEKLIKDDNLRINMGKTGRKFVEDNFNI 344
Cdd:cd03799 311 AIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDI 343
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
23-345 |
7.79e-35 |
|
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: 130.82 E-value: 7.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 23 NKGYDIDVISLNDGDI-------DGVTVhsfnKDLDKIRKGSSFNKISYIRYFSDIKKIIEKIKPDVVhahYATSYGLLG 95
Cdd:cd03820 28 KKGYDVTIISLDSAEKppfyeldDNIKI----KNLGDRKYSHFKLLLKYFKKVRRLRKYLKNNKPDVV---ISFRTSLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 96 ALSGF-HPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMSTSKVMAEETNQYTTKNIEITPfgvNIDTFKPCADKY 174
Cdd:cd03820 101 FLALIgLKSKLIVWEHNNYEAYNKGLRRLLLRRLLYKRADKIVVLTEADKLKKYKQPNSNVVVIP---NPLSFPSEEPST 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 175 EKKENLVIgTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGFinQEKVIEAFN 254
Cdd:cd03820 178 NLKSKRIL-AVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLGP--TKNIAEEYA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 255 RFDVAVFPStlDSESFGVAAVEAQACGTPVIVSN-VGGLPEATAPNNSSILVNKKSVDELAEAIEKLIKDDNLRINMGKT 333
Cdd:cd03820 255 NSSIFVLSS--RYEGFPMVLLEAMAYGLPIISFDcPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKN 332
|
330
....*....|..
gi 920955171 334 GRKFVEDnFNIE 345
Cdd:cd03820 333 ARKNAER-FSIE 343
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
81-345 |
3.79e-34 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340859 [Multi-domain] Cd Length: 370 Bit Score: 129.39 E-value: 3.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 81 DVVHAHYATSYgllgALSGFH---------PYIISVWGSDV----YDFPKGSYIKrkmveYNLSKADIIMSTSKVMAEET 147
Cdd:cd04962 86 DVLHAHYAIPH----ASCAYLareilgekiPIVTTLHGTDItlvgYDPSLQPAVR-----FSINKSDRVTAVSSSLRQET 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 148 NQY--TTKNIEITPFGVNIDTFKPCADKYEKKENL------VIGTVKTLEPKYGIEYLVRAFAKVkQKHNNIKLEIAGVG 219
Cdd:cd04962 157 YELfdVDKDIEVIHNFIDEDVFKRKPAGALKRRLLappdekVVIHVSNFRPVKRIDDVVRVFARV-RRKIPAKLLLVGDG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 220 DQKDFLLNLCNELNIKDHVKFLGfiNQEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATAPN 299
Cdd:cd04962 236 PERVPAEELARELGVEDRVLFLG--KQDDVEELLSIADLFLLPS--EKESFGLAALEAMACGVPVVSSNAGGIPEVVKHG 311
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 920955171 300 NSSILVNKKSVDELAEAIEKLIKDDNLRINMGKTGRKFVEDNFNIE 345
Cdd:cd04962 312 ETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPE 357
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
18-345 |
4.96e-34 |
|
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: 128.55 E-value: 4.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 18 CRFFKNKGYDIDVISLNDgDIDGVTVHSFNkdlDKIRKGSSFNKI-------SYIRYFsdikkIIEKIKPDVVHAHYATS 90
Cdd:cd03795 24 AEGLKKKGIEVDVLCFSK-EKETPEKEENG---IRIHRVKSFLNVastpfspSYIKRF-----KKLAKEYDIIHYHFPNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 91 YG-LLGALSGFH-PYIISvWGSDVydfpkgsyIKRKMVE--YN------LSKADIIMSTSKVMAEETNQYT--TKNIEIT 158
Cdd:cd03795 95 LAdLLLFFSGAKkPVVVH-WHSDI--------VKQKKLLklYKplmtrfLRRADRIIATSPNYVETSPTLRefKNKVRVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 159 PFGVNIDTFKPCADKYEKKENLVIGT-----VKTLEPKYGIEYLVRAfakvkQKHNNIKLEIAGVGDQKDFLLNLCnELN 233
Cdd:cd03795 166 PLGIDKNVYNIPRVDFENIKREKKGKkiflfIGRLVYYKGLDYLIEA-----AQYLNYPIVIGGEGPLKPDLEAQI-ELN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 234 IKDHVKFLGFINQEKVIEAFNRFDVAVFPSTLDSESFGVAAVEAQACGTPVIVSNVGGlpeATAPNN----SSILVNKKS 309
Cdd:cd03795 240 LLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTNIGT---GVPYVNnngeTGLVVPPKD 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 920955171 310 VDELAEAIEKLIKDDNLRINMGKTGRKFVEDNFNIE 345
Cdd:cd03795 317 PDALAEAIDKLLSDEELRESYGENAKKRFEELFTAE 352
|
|
| mycothiol_MshA |
TIGR03449 |
D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively ... |
133-331 |
6.49e-30 |
|
D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively in the Actinobacteria, are MshA, the glycosyltransferase of mycothiol biosynthesis. Mycothiol replaces glutathione in these species.
Pssm-ID: 132490 [Multi-domain] Cd Length: 405 Bit Score: 118.30 E-value: 6.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 133 ADI-IMSTSKVMAEETNQY--TTKNIEITPFGVNIDTFKPcADKYEKKENL-------VIGTVKTLEPKYGIEYLVRAFA 202
Cdd:TIGR03449 164 ADRlIANTDEEARDLVRHYdaDPDRIDVVAPGADLERFRP-GDRATERARLglpldtkVVAFVGRIQPLKAPDVLLRAVA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 203 KVKQKHNNIKLEIAGVG-------DQKDFLLNLCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVFPSTldSESFGVAAV 275
Cdd:TIGR03449 243 ELLDRDPDRNLRVIVVGgpsgsglATPDALIELAAELGIADRVRFLPPRPPEELVHVYRAADVVAVPSY--NESFGLVAM 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 920955171 276 EAQACGTPVIVSNVGGLPEATAPNNSSILVNKKSVDELAEAIEKLIKDDNLRINMG 331
Cdd:TIGR03449 321 EAQACGTPVVAARVGGLPVAVADGETGLLVDGHDPADWADALARLLDDPRTRIRMG 376
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
245-359 |
2.19e-29 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 109.69 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 245 NQEKVIEAF-NRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILVNKKSVDELAEAIEKLIKD 323
Cdd:COG0438 9 GLDLLLEALlAAADVFVLPSR--SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLED 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 920955171 324 DNLRINMGKTGRKFVEDNFNIEDNFNNVDIIYKSII 359
Cdd:COG0438 87 PELRRRLGEAARERAEERFSWEAIAERLLALYEELL 122
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
81-356 |
2.10e-28 |
|
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: 115.12 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 81 DVVHAHyATSY-GLLGALSGFH---PYIISVWGsdVY------DFPKGS----YIKRKMVEY--NLSK-----ADIIMST 139
Cdd:cd03813 175 DLYHSV-STGYaGLLGALARHRrgiPFLLTEHG--IYtrerkiEILQSTwimgYIKKLWIRFfeRLGKlayqqADKIISL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 140 SkvmaEETNQYTTK------NIEITPFGVNIDTFKPCADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKL 213
Cdd:cd03813 252 Y----EGNRRRQIRlgadpdKTRVIPNGIDIQRFAPAREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEG 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 214 EIAGVGDQKDFLLNLCNEL----NIKDHVKFLGFINqekVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNV 289
Cdd:cd03813 328 WLIGPEDEDPEYAQECKRLvaslGLENKVKFLGFQN---IKEYYPKLGLLVLTSI--SEGQPLVILEAMASGVPVVATDV 402
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920955171 290 GGLPEA-----TAPNNSSILVNKKSVDELAEAIEKLIKDDNLRINMGKTGRKFVEDNFNIEDNFNNVDIIYK 356
Cdd:cd03813 403 GSCRELiygadDALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
80-327 |
2.99e-28 |
|
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: 112.83 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 80 PDVVHAHyATSYGLLGAL---SGFHPYIISVWGSD-VYDFPKGSYI-KRKMVEYnlskaDIIMSTSKVMAEETNQYTTKN 154
Cdd:cd03819 77 IDLIHAH-SRAPAWLGWLasrLTGVPLVTTVHGSYlATYHPKDFALaVRARGDR-----VIAVSELVRDHLIEALGVDPE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 155 -IEITPFGVNIDTFKP-----CADKYEKKEN-LVIGTVKTLEPKYGIEYLVRAFAKVKqKHNNIKLEIAGVGDQKDFLLN 227
Cdd:cd03819 151 rIRVIPNGVDTDRFPPeaeaeERAQLGLPEGkPVVGYVGRLSPEKGWLLLVDAAAELK-DEPDFRLLVAGDGPERDEIRR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 228 LCNELNIKDHVKFLGFInqEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILVNK 307
Cdd:cd03819 230 LVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSL--HEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPP 305
|
250 260
....*....|....*....|
gi 920955171 308 KSVDELAEAIEKLIKDDNLR 327
Cdd:cd03819 306 GDAEALADAIRAAKLLPEAR 325
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
155-344 |
4.25e-28 |
|
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: 112.93 E-value: 4.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 155 IEITPFGVNIDTFKPcadKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELni 234
Cdd:cd05844 168 IHVHYIGIDPAKFAP---RDPAERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAAL-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 235 kDHVKFLGFINQEKVIEAFNRFDVAVFPSTL----DSESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILVNKKSV 310
Cdd:cd05844 243 -GRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDV 321
|
170 180 190
....*....|....*....|....*....|....
gi 920955171 311 DELAEAIEKLIKDDNLRINMGKTGRKFVEDNFNI 344
Cdd:cd05844 322 DALADALQALLADRALADRMGGAARAFVCEQFDI 355
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
130-358 |
2.21e-25 |
|
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: 105.11 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 130 LSKADI-IMSTSKVMAEETNQ---YTTKNIEITPFGVNIDTFKPCADKY-------EKKENLVI-GTVKTLEPKYGIEYL 197
Cdd:cd03825 134 LAKKRLtIVAPSRWLADMVRRsplLKGLPVVVIPNGIDTEIFAPVDKAKarkrlgiPQDKKVILfGAESVTKPRKGFDEL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 198 VRAFAKVkQKHNNIKLEIAGVGDQKDFLLNLcnelnikDHVKFlGFI-NQEKVIEAFNRFDVAVFPSTLDSesFGVAAVE 276
Cdd:cd03825 214 IEALKLL-ATKDDLLLVVFGKNDPQIVILPF-------DIISL-GYIdDDEQLVDIYSAADLFVHPSLADN--LPNTLLE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 277 AQACGTPVIVSNVGGLPEATAPNNSSILVNKKSVDELAEAIEKLIKDDNLRINMGKTGRKFVEDNFN----IEDNFNnvd 352
Cdd:cd03825 283 AMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDqrvqAQRYLE--- 359
|
....*.
gi 920955171 353 iIYKSI 358
Cdd:cd03825 360 -LYKDL 364
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
134-326 |
4.51e-24 |
|
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).
Pssm-ID: 340850 [Multi-domain] Cd Length: 357 Bit Score: 101.25 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 134 DIIMSTSKVMAE--ETNQYTTKNIEITPFGVNIDTfKPCADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKhnNI 211
Cdd:cd03823 145 DAVLAPSRFTANlhEANGLFSARISVIPNAVEPDL-APPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLPRE--DI 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 212 KLEIAGVGDQKDfllnlCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVFPSTLDsESFGVAAVEAQACGTPVIVSNVGG 291
Cdd:cd03823 222 ELVIAGHGPLSD-----ERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWP-EPFGLVVREAIAAGLPVIASDLGG 295
|
170 180 190
....*....|....*....|....*....|....*
gi 920955171 292 LPEATAPNNSSILVNKKSVDELAEAIEKLIKDDNL 326
Cdd:cd03823 296 IAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPAL 330
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
80-305 |
1.18e-22 |
|
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: 95.16 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 80 PDVVHAHYATSYGLLGALSGF---HPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMstskvmaeetnqyttknie 156
Cdd:cd01635 55 PDVVHAHSPHAAALAALLAARllgIPIVVTVHGPDSLESTRSELLALARLLVSLPLADKVS------------------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 157 itpfgvnidtfkpcadkyekkenlvigtVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKD 236
Cdd:cd01635 116 ----------------------------VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 237 HVKFLGFINQEKVIEAFNR-FDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILV 305
Cdd:cd01635 168 RVVIIGGLVDDEVLELLLAaADVFVLPSR--SEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
24-328 |
1.24e-22 |
|
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: 97.36 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 24 KGYDIDVISLNDGDIDgvtvhsfnKDLDKIRKGS-----SFNKISYIRYFSDIKKIIEKIKPDVVHAHYATSYG--LLGA 96
Cdd:cd03812 28 SKIEFDFLATSDDKGE--------YDEELEELGGkifyiPPKKKNIIKYFIKLLKLIKKEKYDIVHVHGSSSNGiiLLLA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 97 LSGFHPYIISVWGSDVYDfpkgSYIKRKMVEYNLSKADIIMST-----SKVMAEET-NQYTTKNIEITPFGVNIDTF--- 167
Cdd:cd03812 100 AKAGVPVRIAHSHNTKDS----SIKLRKIRKNVLKKLIERLSTkylacSEDAGEWLfGEVENGKFKVIPNGIDIEKYkfn 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 168 KPCADKYEKKEN----LVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGF 243
Cdd:cd03812 176 KEKRRKRRKLLIledkLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLEDKVIFLGF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 244 INQekVIEAFNRFDVAVFPSTLdsESFGVAAVEAQACGTPVIVSNVGGlPEATAPNNSSILVNKKSVDELAEAIEKLIKD 323
Cdd:cd03812 256 RND--VSEILSAMDVFLFPSLY--EGLPLVAVEAQASGLPCLLSDTIT-KECDITNNVEFLPLNETPSTWAEKILKLIKR 330
|
....*
gi 920955171 324 DNLRI 328
Cdd:cd03812 331 KRRIN 335
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
133-340 |
5.67e-22 |
|
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: 95.44 E-value: 5.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 133 ADIIMSTSKVMAEETNQYTTKNIEITPFGVNIDTFKPCA------DKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQ 206
Cdd:cd03814 146 FDTTLVPSPSIARELEGHGFERVRLWPRGVDTELFHPSRrdaalrRRLGPPGRPLLLYVGRLAPEKNLEALLDADLPLAA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 207 kHNNIKLEIAGVGDQKDfllnlcnELNIKD-HVKFLGFINQEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQACGTPVI 285
Cdd:cd03814 226 -SPPVRLVVVGDGPARA-------ELEARGpDVIFTGFLTGEELARAYASADVFVFPS--RTETFGLVVLEAMASGLPVV 295
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 920955171 286 VSNVGGLPEATAPNNSSILVNKKSVDELAEAIEKLIKDDNLRINMGKTGRKFVED 340
Cdd:cd03814 296 AADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAER 350
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
129-341 |
8.19e-21 |
|
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: 91.59 E-value: 8.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 129 NLSKAD-IIMSTSK---VMAEETNQYttKNIEITPFGVnIDTFKPCADKYEKKENLVIgTVKTLEPKYGIEYLVRAFAKV 204
Cdd:cd04949 110 NLNKYDaIIVSTEQqkqDLSERFNKY--PPIFTIPVGY-VDQLDTAESNHERKSNKII-TISRLAPEKQLDHLIEAVAKA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 205 KQKHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGFINQEKVIeaFNRFDVAVFPSTldSESFGVAAVEAQACGTPV 284
Cdd:cd04949 186 VKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQE--YQDAYLSLLTSQ--MEGFGLTLMEAIGHGLPV 261
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 920955171 285 IVSNVG-GLPEATAPNNSSILVNKKSVDELAEAIEKLIKDDNLRINMGKTGRKFVEDN 341
Cdd:cd04949 262 VSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAEKY 319
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
81-321 |
7.11e-19 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 86.91 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 81 DVVHAHYATSY----GLLGA-LSGFHPYII--SVWG-SDVydfpkGSYIKRKMVEYNLSKADIIMSTSKVMAEET---NQ 149
Cdd:cd03796 90 QIVHGHQAFSSlaheALFHArTLGLKTVFTdhSLFGfADA-----SSILTNKLLRFSLADIDHVICVSHTSKENTvlrAS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 150 YTTKNIEITPFGVNIDTFKPCADKYEKKEnLVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLC 229
Cdd:cd03796 165 LDPRIVSVIPNAVDSSDFTPDPSKPDPNK-ITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMR 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 230 NELNIKDHVKFLGFINQEKVIEAFNRFDVavFPSTLDSESFGVAAVEAQACGTPVIVSNVGGLPEATAPNnsSILVNKKS 309
Cdd:cd03796 244 EKYQLQDRVELLGAVPHEEVRDVLVQGHI--FLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPD--MILLAEPD 319
|
250
....*....|..
gi 920955171 310 VDELAEAIEKLI 321
Cdd:cd03796 320 PEDIVRKLEEAI 331
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
131-339 |
3.31e-17 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 82.45 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 131 SKADIIMSTSKVMAEE--TNQYTT-KNIEITPFGVNIDTFKPCADKYEKKENL--------VIGTVKTLepkyGIEYLVR 199
Cdd:PLN02871 204 RAADLTLVTSPALGKEleAAGVTAaNRIRVWNKGVDSESFHPRFRSEEMRARLsggepekpLIVYVGRL----GAEKNLD 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 200 AFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNikdhVKFLGFINQEKVIEAFNRFDVAVFPStlDSESFGVAAVEAQA 279
Cdd:PLN02871 280 FLKRVMERLPGARLAFVGDGPYREELEKMFAGTP----TVFTGMLQGDELSQAYASGDVFVMPS--ESETLGFVVLEAMA 353
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 920955171 280 CGTPVIVSNVGGLPEATAP---NNSSILVNKKSVDELAEAIEKLIKDDNLRINMGKTGRKFVE 339
Cdd:PLN02871 354 SGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVE 416
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
80-355 |
3.80e-17 |
|
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: 81.72 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 80 PDVVHAHYatsygllgalsgFHPYIISVWGSDVYDFPK----------GSYIKRKMVEYNLSKADIIMSTSKVMAEE--T 147
Cdd:cd04951 80 PDVVHSHM------------FHANIFARFLRMLYPIPLlictahnkneGGRIRMFIYRLTDFLCDITTNVSREALDEfiA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 148 NQYTTKNIEIT-PFGVNIDTFKPCADKYEKKEN--------LVIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGV 218
Cdd:cd04951 148 KKAFSKNKSVPvYNGIDLNKFKKDINVRLKIRNklnlkndeFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 219 GDQKDFLLNLCNELNIKDHVKFLGFINQekVIEAFNRFDVAVFPSTLdsESFGVAAVEAQACGTPVIVSNVGGLPEATAP 298
Cdd:cd04951 228 GPLRNELERLICNLNLVDRVILLGQISN--ISEYYNAADLFVLSSEW--EGFGLVVAEAMACERPVVATDAGGVAEVVGD 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 920955171 299 NNSSILVNKKSvdELAEAIEKLIK-DDNLRINMGKTgRKFVEDNFNIEDNFNNVDIIY 355
Cdd:cd04951 304 HNYVVPVSDPQ--LLAEKIKEIFDmSDEERDILGNK-NEYIAKNFSINTIVNEWERLY 358
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
159-345 |
6.28e-17 |
|
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: 80.79 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 159 PFGVNIDTFKPCadkYEKKENLV-IGTVKtlePKYGIEYLVRAFAKVkqkhnNIKLEIAGVGDQKD---FLlnlcNELNI 234
Cdd:cd03802 154 HNGLDPADYRFQ---PDPEDYLAfLGRIA---PEKGLEDAIRVARRA-----GLPLKIAGKVRDEDyfyYL----QEPLP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 235 KDHVKFLGFINQEKVIEAFNRFDVAVFPSTLDsESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILVNkkSVDELA 314
Cdd:cd03802 219 GPRIEFIGEVGHDEKQELLGGARALLFPINWD-EPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVD--SVEEMA 295
|
170 180 190
....*....|....*....|....*....|.
gi 920955171 315 EAIEKLIKDDNLRInmgktgRKFVEDNFNIE 345
Cdd:cd03802 296 EAIANIDRIDRAAC------RRYAEDRFSAA 320
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
116-345 |
6.63e-16 |
|
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: 78.01 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 116 PKGSYIKR-------KMVEYNLSKADIIMSTSKVMAEETNQyTTKNIEITPFGV-----NIDTFKPCADKYEKKENLVIG 183
Cdd:cd03805 131 QRKSLLKRlyrkpfdWLEEFTTGMADQIVVNSNFTAGVFKK-TFPSLAKNPPEVlypcvDTDSFDSTSEDPDPGDLIAKS 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 184 TVKTL------EPKYGIEYLVRAFAKVKQKHN---NIKLEIAGVGDQK--------DFLLNLCNEL-NIKDHVKFLGFIN 245
Cdd:cd03805 210 NKKFFlsinrfERKKNIALAIEAFAKLKQKLPefeNVRLVIAGGYDPRvaenveylEELQRLAEELlNVEDQVLFLRSIS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 246 QEKVIEAFNRFDVAVFpsTLDSESFGVAAVEAQACGTPVIVSNVGGlPEATAPNNSSILVNKKSVDELAEAIEKLIKDDN 325
Cdd:cd03805 290 DSQKEQLLSSALALLY--TPSNEHFGIVPLEAMYAGKPVIACNSGG-PLETVVEGVTGFLCEPTPEAFAEAMLKLANDPD 366
|
250 260
....*....|....*....|
gi 920955171 326 LRINMGKTGRKFVEDNFNIE 345
Cdd:cd03805 367 LADRMGAAGRKRVKEKFSRE 386
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
80-344 |
7.74e-16 |
|
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: 77.84 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 80 PDVVHAH--YATSYGLLGALSGFHPYIISVWGSDVYDfPKGSYIKrkmveYNLSKADI--IMSTSKVMAEETNQYTTKNI 155
Cdd:TIGR03088 82 PDIVHTRnlAALEAQLPAALAGVPARIHGEHGRDVFD-LDGSNWK-----YRWLRRLYrpLIHHYVAVSRDLEDWLRGPV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 156 EITPF-------GVNIDTFKP--------CADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQK----HNNIKLEIA 216
Cdd:TIGR03088 156 KVPPAkihqiynGVDTERFHPsrgdrspiLPPDFFADESVVVGTVGRLQAVKDQPTLVRAFALLVRQlpegAERLRLVIV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 217 GVGDQKDFLLNLCNELNIKDHVKFLGfiNQEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEAT 296
Cdd:TIGR03088 236 GDGPARGACEQMVRAAGLAHLVWLPG--ERDDVPALMQALDLFVLPSL--AEGISNTILEAMASGLPVIATAVGGNPELV 311
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 920955171 297 APNNSSILVNKKSVDELAEAIEKLIKDDNLRINMGKTGRKFVEDNFNI 344
Cdd:TIGR03088 312 QHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSI 359
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
162-318 |
8.14e-16 |
|
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: 77.71 E-value: 8.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 162 VNIDTFKPCADKyekKENLVigTVKTLEPKYGIEYLVRAFAKVkqkhnNIKLEIAGVGDQKDFLLNLCnelniKDHVKFL 241
Cdd:cd03804 187 VDTDAFAPAADK---EDYYL--TASRLVPYKRIDLAVEAFNEL-----PKRLVVIGDGPDLDRLRAMA-----SPNVEFL 251
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 920955171 242 GFINQEKVIEAFNRFDVAVFPSTldsESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILVNKKSVDELAEAIE 318
Cdd:cd03804 252 GYQPDEVLKELLSKARAFVFAAE---EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVE 325
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
190-344 |
2.58e-14 |
|
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.
Pssm-ID: 340823 [Multi-domain] Cd Length: 378 Bit Score: 73.51 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 190 PKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKD----FLLN--LCNELNIKD-HVKFLGFINQEkvIEAFNRF-DVAVF 261
Cdd:cd03792 208 PSKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDDpegsVVYEevMEYAGDDHDiHVLRLPPSDQE--INALQRAaTVVLQ 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 262 PSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILVNkkSVDELAEAIEKLIKDDNLRINMGKTGRKFVEDN 341
Cdd:cd03792 286 LST--REGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVN--SVEGAAVRILRLLTDPELRRKMGLAAREHVRDN 361
|
...
gi 920955171 342 FNI 344
Cdd:cd03792 362 FLI 364
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
49-349 |
3.01e-13 |
|
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: 70.18 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 49 DLDKIRKGSSFNK--------ISYIRYFSDIKKIIEKIKPDVVHAH--YATSYGL-LGALSGFHPYIIS-VWGSDVYDFP 116
Cdd:cd04946 83 IKDKPRSGSFLLLyyfliasfLSKHRVLALLQFVSIFGQGTVVYSYwlNHTALGLgLLKDEYYRDVVISrAHRYDLYEDQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 117 KGSYI---KRKMVEYnLSKADIIMSTSKVMAEETNQYTTKNIEITPFGVNIDTFKpcaDKYEKKENLVIGTVKTLEPKYG 193
Cdd:cd04946 163 YGSYYlplREYLVSY-LDAVFLISKEGKDYLQKCYPAYKEKIFVSRLGVSDKEQY---SKVKKEGDLRLVSCSSIVPVKR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 194 IEYLVRAFAKVKQKHNNIKLE---IAGVGDQKDFLLNLCNELNIKDhVKFLGFINQEKVIEAFNRFDVAVFPSTLDSESF 270
Cdd:cd04946 239 IDLIIETLNSLCVAHPSICISwthIGGGPLKERLEKLAENKLENVK-VNFTGEVSNKEVKQLYKENDVDVFVNVSESEGI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 271 GVAAVEAQACGTPVIVSNVGGLPEATapNNSS---ILVNKKSVDELAEAIEKLIKDDNLRINMGKTGRKFVEDNFNIEDN 347
Cdd:cd04946 318 PVSIMEAISFGIPVIATNVGGTREIV--ENETnglLLDKDPTPNEIVSSIMKFYLDGGDYKTMKISARECWEERFNAEVN 395
|
..
gi 920955171 348 FN 349
Cdd:cd04946 396 YS 397
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
154-345 |
3.12e-13 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 70.20 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 154 NIEITPFGVNIDTFKPCADKyEKKENLVIGTVKT-------LEPKYGIEYLVRAFAKVKQKHNNIKLEIAG------VGD 220
Cdd:PRK15484 162 DISIVPNGFCLETYQSNPQP-NLRQQLNISPDETvllyagrISPDKGILLLMQAFEKLATAHSNLKLVVVGdptassKGE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 221 QKDFLLNLCNELN-IKDHVKFLGFINQEKVIEAFNRFDVAVFPSTLDsESFGVAAVEAQACGTPVIVSNVGGLPEATAPN 299
Cdd:PRK15484 241 KAAYQKKVLEAAKrIGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVE-EAFCMVAVEAMAAGKPVLASTKGGITEFVLEG 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 920955171 300 NSSI-LVNKKSVDELAEAIEKLIKDDNlRINMGKTGRKFVEDNFNIE 345
Cdd:PRK15484 320 ITGYhLAEPMTSDSIISDINRTLADPE-LTQIAEQAKDFVFSKYSWE 365
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
154-327 |
9.82e-10 |
|
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: 59.32 E-value: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 154 NIEITPFGVNIDTFKPcaDKYEKKENL-----VIGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAG--VGDQKD--- 223
Cdd:cd03822 159 NIEVIPHGVPEVPQDP--TTALKRLLLpegkkVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGelHPSLARyeg 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 224 --FLLNLCNELNIKDHVKF-LGFINQEKVIEAFNRFDVAVFP--STLDSESfGVAAVeAQACGTPVIVSNVGGLPEATAp 298
Cdd:cd03822 237 erYRKAAIEELGLQDHVDFhNNFLPEEEVPRYISAADVVVLPylNTEQSSS-GTLSY-AIACGKPVISTPLRHAEELLA- 313
|
170 180
....*....|....*....|....*....
gi 920955171 299 NNSSILVNKKSVDELAEAIEKLIKDDNLR 327
Cdd:cd03822 314 DGRGVLVPFDDPSAIAEAILRLLEDDERR 342
|
|
| COG4641 |
COG4641 |
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]; |
129-338 |
5.11e-09 |
|
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443679 [Multi-domain] Cd Length: 303 Bit Score: 56.86 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 129 NLSKADIIMSTSKVMAEETNQYTTKNIEITPFGVNIDTFKPCADKYEKKENLV-IGTvktlepkyGIEYLVRAFAKVKQK 207
Cdd:COG4641 89 LLPLYDLVFTFDGDCVEEYRALGARRVFYLPFAADPELHRPVPPEARFRYDVAfVGN--------YYPDRRARLEELLLA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 208 HNNIKLEIAGVGDQKDFLLnlcnelnikDHVKFLGFINQEKVIEAFNRFDVAV-FPSTLDSE-SFGVAAVEAQACGTPVI 285
Cdd:COG4641 161 PAGLRLKIYGPGWPKLALP---------ANVRRGGHLPGEEHPAAYASSKITLnVNRMAASPdSPTRRTFEAAACGAFLL 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 920955171 286 VSNVGGLPEATAPNNSSILVNkkSVDELAEAIEKLIKDDNLRINMGKTGRKFV 338
Cdd:COG4641 232 SDPWEGLEELFEPGEEVLVFR--DGEELAEKLRYLLADPEERRAIAEAGRRRV 282
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
198-343 |
1.53e-08 |
|
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.
Pssm-ID: 340835 [Multi-domain] Cd Length: 419 Bit Score: 55.69 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 198 VRAFAKVKQKH-----NNIKLEIAG----VGDQK--DFLLNLCNELNIKDHVKFLGFINQEKVIEAFNRFDVAVfpSTLD 266
Cdd:cd03806 256 LRAFAELLKRLpesirSNPKLVLIGscrnEEDKErvEALKLLAKELILEDSVEFVVDAPYEELKELLSTASIGL--HTMW 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 267 SESFGVAAVEAQACGTPVIVSNVGGlPEAtapnnsSILVNK---------KSVDELAEAIEKLIKDDNL-RINMGKTGR- 335
Cdd:cd03806 334 NEHFGIGVVEYMAAGLIPLAHASAG-PLL------DIVVPWdggptgflaSTPEEYAEAIEKILTLSEEeRLQRREAARs 406
|
170
....*....|.
gi 920955171 336 ---KFVEDNFN 343
Cdd:cd03806 407 saeRFSDEEFE 417
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
264-343 |
2.13e-07 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 48.37 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 264 TLDSESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILVnkKSVDELAEAIEKLIKDDNLRINMGKTGRKFVEDNFN 343
Cdd:pfam13524 6 SRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLY--RDPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHT 83
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
176-346 |
4.04e-07 |
|
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: 51.59 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 176 KKENLVIGTV-KTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGvGDQ-------------KDFLLNlcnELNIKDH-VKF 240
Cdd:cd03818 210 KAGDPVITYVaRNLEPYRGFHVFMRALPRIQARRPDARVVVVG-GDGvsygspppdggswKQKMLA---ELGVDLErVHF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 241 LGFINQEKVIEAFNRFDVAVFPSTLDSESFGVaaVEAQACGTPVIVSNVGGLPEATAPNNSSILVNKKSVDELAEAIEKL 320
Cdd:cd03818 286 VGKVPYDQYVRLLQLSDAHVYLTYPFVLSWSL--LEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLEL 363
|
170 180
....*....|....*....|....*.
gi 920955171 321 IKDDNLRINMGKTGRKFVEDNFNIED 346
Cdd:cd03818 364 LEDPDRAAALRRAARRTVERSDSLDV 389
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
198-343 |
2.47e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 48.97 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 198 VRAFAKVKQKHN----NIKLEIAGV----GDQK--DFLLNLCNELNIKDHVKFLGFINQEKVIEAFNRfDVAVFPSTLDs 267
Cdd:PLN02949 287 LEAFALALEKLDadvpRPKLQFVGScrnkEDEErlQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGG-AVAGLHSMID- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 268 ESFGVAAVEAQACGTPVIVSNVGG------LPEATAPnnSSILVNkkSVDELAEAIEKLIK-DDNLRINMGKTGRK---- 336
Cdd:PLN02949 365 EHFGISVVEYMAAGAVPIAHNSAGpkmdivLDEDGQQ--TGFLAT--TVEEYADAILEVLRmRETERLEIAAAARKranr 440
|
....*..
gi 920955171 337 FVEDNFN 343
Cdd:PLN02949 441 FSEQRFN 447
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
182-331 |
1.30e-05 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 46.95 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 182 IGTVKTLEPKYGIEYLVRAFAKVKQKHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGFINqeKVIEAFNRFDVAVF 261
Cdd:PRK15179 520 VGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSR--RVGYWLTQFNAFLL 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920955171 262 PSTLdsESFGVAAVEAQACGTPVIVSNVGGLPEATAPNNSSILVNKKSVD--ELAEAIEKLIkdDNLRINMG 331
Cdd:PRK15179 598 LSRF--EGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTapDVAEALARIH--DMCAADPG 665
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
25-146 |
9.28e-05 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 42.39 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 25 GYDIDVISLNDG------DIDGVTVHSfnkdLDKIRKGSSFNKISYIRYFSDIKKIIEkikPDVVHAHYATS--YGLLGA 96
Cdd:pfam13579 18 GHEVRVVTPGGPpgrpelVGDGVRVHR----LPVPPRPSPLADLAALRRLRRLLRAER---PDVVHAHSPTAglAARLAR 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 920955171 97 LSGFHPYIISVWGSDV--YDFPKGSYIkRKMVEYNLSKADIIMSTSKVMAEE 146
Cdd:pfam13579 91 RRRGVPLVVTVHGLALdyGSGWKRRLA-RALERRLLRRADAVVVVSEAEAEL 141
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
11-165 |
1.14e-04 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 42.13 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 11 STHTKKWCRFFKNKGYDIDVISLNDGD------IDGVTVHSFNKDLDKIRKGSSFNKISYIRYFSDIKkiiekikPDVVH 84
Cdd:pfam13439 4 ERYVLELARALARRGHEVTVVTPGGPGplaeevVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRER-------PDVVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 85 AHYATS--YGLLGALSGFH-PYIISV-----WGSDVYDFPKGSYIKRKMVEYNL-SKADIIMSTSKVMAEETNQY---TT 152
Cdd:pfam13439 77 AHSPFPlgLAALAARLRLGiPLVVTYhglfpDYKRLGARLSPLRRLLRRLERRLlRRADRVIAVSEAVADELRRLygvPP 156
|
170
....*....|...
gi 920955171 153 KNIEITPFGVNID 165
Cdd:pfam13439 157 EKIRVIPNGVDLE 169
|
|
| PRK05749 |
PRK05749 |
3-deoxy-D-manno-octulosonic-acid transferase; Reviewed |
276-341 |
2.00e-04 |
|
3-deoxy-D-manno-octulosonic-acid transferase; Reviewed
Pssm-ID: 235589 [Multi-domain] Cd Length: 425 Bit Score: 42.90 E-value: 2.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 920955171 276 EAQACGTPVI----VSNvggLPEATAP-NNSSILVNKKSVDELAEAIEKLIKDDNLRINMGKTGRKFVEDN 341
Cdd:PRK05749 339 EPAAFGVPVIsgphTFN---FKEIFERlLQAGAAIQVEDAEDLAKAVTYLLTDPDARQAYGEAGVAFLKQN 406
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
169-351 |
2.47e-03 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 39.31 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 169 PCADKYEKKENLVIGTVKtLEPKYGIEYLVRAFAKVkqkHNNIKLEIAGVGDQKDFLLNLCNELNIKDHVKFLGFINQEK 248
Cdd:PRK09922 173 PPPERDKPAVFLYVGRLK-FEGQKNVKELFDGLSQT---TGEWQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQPW 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920955171 249 VIEAFNRFDVAVFPSTLDSESFGVAAVEAQACGTPVIVSN-VGGLPEATAPNNSSILVNKKSVDELAEAIEKLIKDDNLR 327
Cdd:PRK09922 249 EVVQQKIKNVSALLLTSKFEGFPMTLLEAMSYGIPCISSDcMSGPRDIIKPGLNGELYTPGNIDEFVGKLNKVISGEVKY 328
|
170 180
....*....|....*....|....*...
gi 920955171 328 ----INMgkTGRKFVEDNFniEDNFNNV 351
Cdd:PRK09922 329 qhdaIPN--SIERFYEVLY--FKNLNNA 352
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
227-290 |
7.93e-03 |
|
GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.
Pssm-ID: 411604 [Multi-domain] Cd Length: 489 Bit Score: 37.99 E-value: 7.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 920955171 227 NLCNELNIKDHVKFLGFinqEKVIEAFNRFDVAVFPSTldSESFGVAAVEAQACGTPVIVSNVG 290
Cdd:NF038011 358 SLVASLGLQDKVKFLGF---QKIDDLLPQVGLMVLSSI--SEALPLVVLEAFAAGVPVVTTDVG 416
|
|
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