|
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 |
7.70e-60 |
|
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: 197.22 E-value: 7.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 80 PDVVHAHYATSYGLLGALSGF---HPYIISVWGSDVYDFPKGSYiKRKMVEYNLSKADIIMSTSKVMAEETSQYTT--KD 154
Cdd:cd03798 96 PDLIHAHFAYPAGFAAALLARlygVPYVVTEHGSDINVFPPRSL-LRKLLRWALRRAARVIAVSKALAEELVALGVprDR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 155 IEITPFGVNIDTFKPFADKYEKKEN-LVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELN 233
Cdd:cd03798 175 VDVIPNGVDPARFQPEDRGLGLPLDaFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 234 IRDHVKFLGFINQEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDEL 313
Cdd:cd03798 255 LGDRVTFTGRLPHEQVPAYYRACDVFVLPSR--HEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADAL 332
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 924281479 314 AEAIEKLIEDDNLRINMGKTGRRFVEdNFNIEDNFNNVDTIYKSI 358
Cdd:cd03798 333 AAALRRALAEPYLRELGEAARARVAE-RFSWVKAADRIAAAYRDV 376
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
11-356 |
7.90e-59 |
|
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: 194.29 E-value: 7.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 11 STHTKKWCRFFNNKGYDIDVISLNDGEIDGVAVHSFNKDLDKIRKGSSFNKISYIKYFSdikKIIEKIKPDVVHAHYATS 90
Cdd:cd03801 17 ERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELR---PLLRLRKFDVVHAHGLLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 91 --YGLLGALSGFHPYIISVWGSDVYDFPKGSYIKRKMV---EYNLSKADIIMSTSKVMAEETSQY---TTKDIEITPFGV 162
Cdd:cd03801 94 alLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLaraEALLRRADAVIAVSEALRDELRALggiPPEKIVVIPNGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 163 NIDTFKPF--ADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGV-GEQKDFLLSLcnELNIRDHVK 239
Cdd:cd03801 174 DLERFSPPlrRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGdGPLRAELEEL--ELGLGDRVR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 240 FLGFINQEKVIEAFNRFDIAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEK 319
Cdd:cd03801 252 FLGFVPDEELPALYAAADVFVLPS--RYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLR 329
|
330 340 350
....*....|....*....|....*....|....*..
gi 924281479 320 LIEDDNLRINMGKTGRRFVEDNFNIEDNFNNVDTIYK 356
Cdd:cd03801 330 LLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
2-345 |
3.52e-48 |
|
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: 166.23 E-value: 3.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 2 KICYLADANS---THTKKWCRFFNNKGYDIDVISLNDGEID------GVAVHSFNkdldkiRKGSSFNKISYIKYFSDIK 72
Cdd:cd03808 1 KILFIVNVDGgfqSFRLPLIKALVKKGYEVHVIAPDGDKLSdelkelGVKVIDIP------ILRRGINPLKDLKALFKLY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 73 KIIEKIKPDVVHAHyaTS----YGLLGALSGFHPYIISV---WGsdvYDFPKGSYIKR--KMVE-YNLSKADIIMSTSKV 142
Cdd:cd03808 75 KLLKKEKPDIVHCH--TPkpgiLGRLAARLAGVPKVIYTvhgLG---FVFTEGKLLRLlyLLLEkLALLFTDKVIFVNED 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 143 MAEETSQYTTKDIEITPF----GVNIDTFKPfADKYEKKENLVIGTV-KTLEPKyGIEYLVRAFAKVKQKHSNIKLEIAG 217
Cdd:cd03808 150 DRDLAIKKGIIKKKKTVLipgsGVDLDRFQY-SPESLPSEKVVFLFVaRLLKDK-GIDELIEAAKILKKKGPNVRFLLVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 218 VGEQKDFLLSLCNELNIRDHVKFLGFInqEKVIEAFNRFDIAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATS 297
Cdd:cd03808 228 DGELENPSEILIEKLGLEGRIEFLGFR--SDVPELLAESDVFVLPS--YREGLPRSLLEAMAAGRPVITTDVPGCRELVI 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 924281479 298 PNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIE 345
Cdd:cd03808 304 DGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEE 351
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
177-337 |
4.35e-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: 157.44 E-value: 4.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 177 KENLVIgTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRF 256
Cdd:pfam00534 1 KKKIIL-FVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 257 DIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRR 336
Cdd:pfam00534 80 DVFVLPSR--YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157
|
.
gi 924281479 337 F 337
Cdd:pfam00534 158 R 158
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
18-356 |
3.06e-45 |
|
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: 158.63 E-value: 3.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 18 CRFFNNKGYDIDVISL-NDGEI------DGVAVHSFNKDLDKirkgSSFNKISYIKYFSDIKkiiekikPDVVHAH--YA 88
Cdd:cd03807 22 LEHMDKSRFEHVVISLtGDGVLgeellaAGVPVVCLGLSSGK----DPGVLLRLAKLIRKRN-------PDVVHTWmyHA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 89 TSYGLLGA-LSGFHPYIISVWGSDvyDFPKGSYIKRKMvEYNLSKADI-IMSTSKVMAEETSQ--YTTKDIEITPFGVNI 164
Cdd:cd03807 91 DLIGGLAAkLAGGVKVIWSVRSSN--IPQRLTRLVRKL-CLLLSKFSPaTVANSSAVAEFHQEqgYAKNKIVVIYNGIDL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 165 DTFKP-FADKYEKKENL-------VIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRD 236
Cdd:cd03807 168 FKLSPdDASRARARRRLglaedrrVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERLLLELGLED 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 237 HVKFLGfiNQEKVIEAFNRFDIAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEaTSPNNSSLLVNKKNVDELAEA 316
Cdd:cd03807 248 RVHLLG--ERSDVPALLPAMDIFVLSS--RTEGFPNALLEAMACGLPVVATDVGGAAE-LVDDGTGFLVPAGDPQALADA 322
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 924281479 317 IEKLIEDDNLRINMGKTGRRFVEDNFNIEDNFNNVDTIYK 356
Cdd:cd03807 323 IRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
2-140 |
6.89e-39 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 135.14 E-value: 6.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 2 KICYLADANSTHTKKWCRFFNNKGYDIDVISLNDGEID-----GVAVHSFNKDldkiRKGssfnKISYIKYFSdIKKIIE 76
Cdd:pfam13477 1 KILLLANADSIHTLRWADALADRGYDVHVISSKGPAKDeliaeGIHVHRLKVP----RKG----PLGYLKAFR-LKKLIK 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 924281479 77 KIKPDVVHAHYATSYGLLGAL----SGFHPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMSTS 140
Cdd:pfam13477 72 KIKPDVVHVHYAKPYGLLAGLaarlSGFPPVVLSAWGLDVYKFPNKSRLKKLLLKLNLKKATLIISTS 139
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
80-343 |
3.57e-38 |
|
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: 140.84 E-value: 3.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 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 924281479 141 KVMAEETSQYTTKD--IEITPFGVNIDTFKPFADKYEKKENL-------VIGTVKTLEPKYGIEYLVRAFAKVKQKHSNI 211
Cdd:cd03800 173 QEADELISLYGADPsrINVVPPGVDLERFFPVDRAEARRARLllppdkpVVLALGRLDPRKGIDTLVRAFAQLPELRELA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 212 KLEIAGvGEQKD-------FLLSLCNELNIRDHVKFLGFINQEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPV 284
Cdd:cd03800 253 NLVLVG-GPSDDplsmdreELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSL--YEPFGLTAIEAMACGTPV 329
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 924281479 285 IVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFN 343
Cdd:cd03800 330 VATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYT 388
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
17-344 |
9.85e-37 |
|
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: 135.95 E-value: 9.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 17 WCRFFNNKGYDIDVISLNDG----EIDGVAVHSFNKDLDKIRKGSSFNKISYIKYFSdikkIIEKIKPDVVHAHYATSYG 92
Cdd:cd03811 21 LANALDKRGYDVTLVLLRDEgdldKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKR----ILKRAKPDVVISFLGFATY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 93 LLGALSGFHPYIISVWGSDvYDFPKGSYIKRKMVEYNLSKADIIMSTSKVMAEE---TSQYTTKDIEITPFGVNIDTFKP 169
Cdd:cd03811 97 IVAKLAAARSKVIAWIHSS-LSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDlirLGPSPPEKIEVIYNPIDIDRIRA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 170 FADK---YEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLGFinQ 246
Cdd:cd03811 176 LAKEpilNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGLAERVIFLGF--Q 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 247 EKVIEAFNRFDIAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAE---AIEKLIED 323
Cdd:cd03811 254 SNPYPYLKKADLFVLSS--RYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGilaALLQKKLD 331
|
330 340
....*....|....*....|.
gi 924281479 324 DNLRINMGKtGRRFVEDNFNI 344
Cdd:cd03811 332 AALRERLAK-AQEAVFREYTI 351
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
21-344 |
1.29e-36 |
|
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: 135.66 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 21 FNNKGYDIDVISLNDGeiDGVAVHSfnkDLDKIRKgSSFNKISYIKYFSDIKKIiekikpDVVHAHYatsyGLLGALSGF 100
Cdd:cd03799 24 LIDRGHEVDIYAVNPG--DLVKRHP---DVEKYNV-PSLNLLYAIVGLNKKGAY------DIIHCQF----GPLGALGAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 101 HPYIISVWGSDVYDFpKGSYIKRKMVEYN-------LSKADIIMSTSKVMAEETSQYTTKDIEITPFGVNIDTFK-PFAD 172
Cdd:cd03799 88 LRRLKVLKGKLVTSF-RGYDISMYVILEGnkvypqlFAQGDLFLPNCELFKHRLIALGCDEKKIIVHRSGIDCNKfRFKP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 173 KYEKKENLV-IGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLGFINQEKVIE 251
Cdd:cd03799 167 RYLPLDGKIrILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 252 AFNRFDIAVFPSTL----DSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLR 327
Cdd:cd03799 247 ILDEADIFIAPSVTaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIW 326
|
330
....*....|....*..
gi 924281479 328 INMGKTGRRFVEDNFNI 344
Cdd:cd03799 327 PEMGKAGRARVEEEYDI 343
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
23-345 |
2.53e-36 |
|
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: 134.67 E-value: 2.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 23 NKGYDIDVISLNDG------EIDGVAVHsfnKDLDKIRKGSSFNKISYIKYFSDIKKIIEKIKPDVVhahYATSYGLLGA 96
Cdd:cd03820 28 KKGYDVTIISLDSAekppfyELDDNIKI---KNLGDRKYSHFKLLLKYFKKVRRLRKYLKNNKPDVV---ISFRTSLLTF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 97 LSGF-HPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMSTSKVMAEETSQYTTKDIEITPfgvNIDTFKPFADKYE 175
Cdd:cd03820 102 LALIgLKSKLIVWEHNNYEAYNKGLRRLLLRRLLYKRADKIVVLTEADKLKKYKQPNSNVVVIP---NPLSFPSEEPSTN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 176 KKENLVIgTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLGFinQEKVIEAFNR 255
Cdd:cd03820 179 LKSKRIL-AVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLGP--TKNIAEEYAN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 256 FDIAVFPStlDSESFGVAAVEAQACGTPVIVSN-VGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTG 334
Cdd:cd03820 256 SSIFVLSS--RYEGFPMVLLEAMAYGLPIISFDcPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNA 333
|
330
....*....|.
gi 924281479 335 RRFVEDnFNIE 345
Cdd:cd03820 334 RKNAER-FSIE 343
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
23-345 |
3.41e-36 |
|
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: 135.19 E-value: 3.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 23 NKGYDIDVISLNDGEIDGVAVhsfnKDLDKIRKGSSFNKISYIK---------YFSDIKKIIEKIKPDVVHAHYATSYGL 93
Cdd:cd03821 29 ALGHEVTIVSTGDGYESLVVE----ENGRYIPPQDGFASIPLLRqgagrtdfsPGLPNWLRRNLREYDVVHIHGVWTYTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 94 LGAL---SGFH-PYIISVWGS-DVYDFPKgSYIKRKMVEY-----NLSKADIIMSTSKVMAEETS--QYTTKdIEITPFG 161
Cdd:cd03821 105 LAACklaRRRGiPYVVSPHGMlDPWALQQ-KHWKKRIALHlierrNLNNAALVHFTSEQEADELRrfGLEPP-IAVIPNG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 162 VNIDTFKPfADKYEKKENL-----VIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQK-DFLLSLCNELNIR 235
Cdd:cd03821 183 VDIPEFDP-GLRDRRKHNGledrrIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDGAyPAFLQLQSSLGLG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 236 DHVKFLGFINQEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSslLVNKKNVDELAE 315
Cdd:cd03821 262 DRVTFTGPLYGEAKWALYASADLFVLPSY--SENFGNVVAEALACGLPVVITDKCGLSELVEAGCG--VVVDPNVSSLAE 337
|
330 340 350
....*....|....*....|....*....|..
gi 924281479 316 AIEKLIEDDNLRINMGKTGRRFV--EDNFNIE 345
Cdd:cd03821 338 ALAEALRDPADRKRLGEMARRARqvEENFSWE 369
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
81-345 |
3.72e-36 |
|
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: 134.79 E-value: 3.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 81 DVVHAHYATSYgllgALSGFH---------PYIISVWGSDV----YDFPKGSYIKrkmveYNLSKADIIMSTSKVMAEET 147
Cdd:cd04962 86 DVLHAHYAIPH----ASCAYLareilgekiPIVTTLHGTDItlvgYDPSLQPAVR-----FSINKSDRVTAVSSSLRQET 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 148 SQY--TTKDIEITPFGVNIDTFKPFADKYEKKENL------VIGTVKTLEPKYGIEYLVRAFAKVkQKHSNIKLEIAGVG 219
Cdd:cd04962 157 YELfdVDKDIEVIHNFIDEDVFKRKPAGALKRRLLappdekVVIHVSNFRPVKRIDDVVRVFARV-RRKIPAKLLLVGDG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 220 EQKDFLLSLCNELNIRDHVKFLGfiNQEKVIEAFNRFDIAVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPN 299
Cdd:cd04962 236 PERVPAEELARELGVEDRVLFLG--KQDDVEELLSIADLFLLPS--EKESFGLAALEAMACGVPVVSSNAGGIPEVVKHG 311
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 924281479 300 NSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIE 345
Cdd:cd04962 312 ETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPE 357
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-345 |
7.27e-36 |
|
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: 134.39 E-value: 7.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 2 KICYLAD-------ANSTHTKKWCRFFNNKGYDIDVI------------SLNDGEIDGVAVHSF-------NKDLDKIRK 55
Cdd:cd03794 1 KILLISQyypppkgAAAARVYELAKELVRRGHEVTVLtpspnyplgrifAGATETKDGIRVIRVklgpikkNGLIRRLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 56 GSSFNKISYIKYFsdikkiIEKIKPDVVHAH--YATSYGLLGALSGFH--PYIISV------WGSDVYDFPKGSYIK--R 123
Cdd:cd03794 81 YLSFALAALLKLL------VREERPDVIIAYspPITLGLAALLLKKLRgaPFILDVrdlwpeSLIALGVLKKGSLLKllK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 124 KMVEYNLSKADIIMSTSKVMAEETSQYTTKD--IEITPFGVNIDTFKPFADKYEKKEN-----LVIGTVKTLEPKYGIEY 196
Cdd:cd03794 155 KLERKLYRLADAIIVLSPGLKEYLLRKGVPKekIIVIPNWADLEEFKPPPKDELRKKLglddkFVVVYAGNIGKAQGLET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 197 LVRAFAKVKQkHSNIKLEIAGVGEQKDFLLSLCNELNIrDHVKFLGFINQEKVIEAFNRFDIAVFPstLDSESFGVAAV- 275
Cdd:cd03794 235 LLEAAERLKR-RPDIRFLFVGDGDEKERLKELAKARGL-DNVTFLGRVPKEEVPELLSAADVGLVP--LKDNPANRGSSp 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 924281479 276 ----EAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIE 345
Cdd:cd03794 311 sklfEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSRE 384
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
18-345 |
1.66e-35 |
|
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: 132.78 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 18 CRFFNNKGYDIDVISLN------DGEIDGVAVHSFNKDLDKIRKGSSFnkiSYIKYFsdikkIIEKIKPDVVHAHYATSY 91
Cdd:cd03795 24 AEGLKKKGIEVDVLCFSkeketpEKEENGIRIHRVKSFLNVASTPFSP---SYIKRF-----KKLAKEYDIIHYHFPNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 92 G-LLGALSGFH-PYIISvWGSDVydfpkgsyIKRKMVE--YN------LSKADIIMSTSKVMAEET---SQYTTKdIEIT 158
Cdd:cd03795 96 AdLLLFFSGAKkPVVVH-WHSDI--------VKQKKLLklYKplmtrfLRRADRIIATSPNYVETSptlREFKNK-VRVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 159 PFGVNIDTFKPFADKYEKKENLVIGT-----VKTLEPKYGIEYLVRAfakvkQKHSNIKLEIAGVGEQKDFLLSLCnELN 233
Cdd:cd03795 166 PLGIDKNVYNIPRVDFENIKREKKGKkiflfIGRLVYYKGLDYLIEA-----AQYLNYPIVIGGEGPLKPDLEAQI-ELN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 234 IRDHVKFLGFINQEKVIEAFNRFDIAVFPSTLDSESFGVAAVEAQACGTPVIVSNVGGlpeATSPNN----SSLLVNKKN 309
Cdd:cd03795 240 LLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTNIGT---GVPYVNnngeTGLVVPPKD 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 924281479 310 VDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIE 345
Cdd:cd03795 317 PDALAEAIDKLLSDEELRESYGENAKKRFEELFTAE 352
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
121-345 |
3.68e-35 |
|
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: 132.10 E-value: 3.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 121 IKRKMVEYNLSKADIIMSTSKVMAEETSQYT---TKDIEITPFGVNIDTFKPFADKYEKKEN-------LVIGTvktLEP 190
Cdd:cd03809 127 YYRLLLPISLRRADAIITVSEATRDDIIKFYgvpPEKIVVIPLGVDPSFFPPESAAVLIAKYllpepyfLYVGT---LEP 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 191 KYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDF-LLSLCNELNIRDHVKFLGFINQEKVIEAFNRFDIAVFPSTldSES 269
Cdd:cd03809 204 RKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEeLLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSL--YEG 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 924281479 270 FGVAAVEAQACGTPVIVSNVGGLPEATSPnnSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEdNFNIE 345
Cdd:cd03809 282 FGLPVLEAMACGTPVIASNISVLPEVAGD--AALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAK-KFSWE 354
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
181-323 |
4.07e-35 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 125.32 E-value: 4.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 181 VIGTVKTLEPKY-GIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDfLLSLCNELNirDHVKFLGFINQekVIEAFNRFDIA 259
Cdd:pfam13692 3 VILFVGRLHPNVkGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEE-LEELAAGLE--DRVIFTGFVED--LAELLAAADVF 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 924281479 260 VFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNsSLLVNKKNVDELAEAIEKLIED 323
Cdd:pfam13692 78 VLPSL--YEGFGLKLLEAMAAGLPVVATDVGGIPELVDGEN-GLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
4-358 |
3.01e-34 |
|
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: 129.71 E-value: 3.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 4 CYLADAN--STHTKKWCRFFNNKGYDIDVISLNDGEidgvavHSFNKDLDKIRKGSSFNKISY-----IKYFSDIKKIIE 76
Cdd:cd03817 8 TYLPQVNgvATSVRNLARALEKRGHEVYVITPSDPG------AEDEEEVVRYRSFSIPIRKYHrqhipFPFKKAVIDRIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 77 KIKPDVVHAHYATSYGLLGALSG----------FHpyiiSVWGSDVYDFPKGSYIKRKMVE------YNlsKADIIMSTS 140
Cdd:cd03817 82 ELGPDIIHTHTPFSLGKLGLRIArklkipivhtYH----TMYEDYLHYIPKGKLLVKAVVRklvrrfYN--HTDAVIAPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 141 KVMAEETSQY-TTKDIEITPFGVNIDTFKPFADKYEKKENL------VIGTVKTLEPKYGIEYLVRAFAKVKQKhSNIKL 213
Cdd:cd03817 156 EKIKDTLREYgVKGPIEVIPNGIDLDKFEKPLNTEERRKLGlppdepILLYVGRLAKEKNIDFLLRAFAELKKE-PNIKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 214 EIAGVGEQKDFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLP 293
Cdd:cd03817 235 VIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFAST--TETQGLVYLEAMAAGLPVVAAKDPAAS 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 924281479 294 EATSPNNSSLLVnKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIEDnfnnVDTIYKSI 358
Cdd:cd03817 313 ELVEDGENGFLF-EPNDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAKS----VEKLYEEV 372
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
80-339 |
2.66e-31 |
|
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: 120.92 E-value: 2.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 80 PDVVHAHyATSYGLLGAL---SGFHPYIISVWGSD-VYDFPKGSYI-KRKMVEYnlskaDIIMSTSKVMAEETSQYTTKD 154
Cdd:cd03819 77 IDLIHAH-SRAPAWLGWLasrLTGVPLVTTVHGSYlATYHPKDFALaVRARGDR-----VIAVSELVRDHLIEALGVDPE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 155 -IEITPFGVNIDTFKPFADKYEKKENL------VIGTVKTLEPKYGIEYLVRAFAKVKqKHSNIKLEIAGVGEQKDFLLS 227
Cdd:cd03819 151 rIRVIPNGVDTDRFPPEAEAEERAQLGlpegkpVVGYVGRLSPEKGWLLLVDAAAELK-DEPDFRLLVAGDGPERDEIRR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 228 LCNELNIRDHVKFLGFInqEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNK 307
Cdd:cd03819 230 LVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSL--HEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPP 305
|
250 260 270
....*....|....*....|....*....|..
gi 924281479 308 KNVDELAEAIEKLIEDDNLRinmGKTGRRFVE 339
Cdd:cd03819 306 GDAEALADAIRAAKLLPEAR---EKLQAAAAL 334
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
245-359 |
1.86e-30 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 112.78 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 245 NQEKVIEAF-NRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIED 323
Cdd:COG0438 9 GLDLLLEALlAAADVFVLPSR--SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLED 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 924281479 324 DNLRINMGKTGRRFVEDNFNIEDNFNNVDTIYKSII 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 |
1.26e-29 |
|
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: 118.59 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 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 924281479 140 SkvmaEETSQYTTKD------IEITPFGVNIDTFKPFADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKL 213
Cdd:cd03813 252 Y----EGNRRRQIRLgadpdkTRVIPNGIDIQRFAPAREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEG 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 214 EIAG-VGEQKDFL---LSLCNELNIRDHVKFLGFINqekVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNV 289
Cdd:cd03813 328 WLIGpEDEDPEYAqecKRLVASLGLENKVKFLGFQN---IKEYYPKLGLLVLTSI--SEGQPLVILEAMASGVPVVATDV 402
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 924281479 290 GGLPEA-----TSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIEDNFNNVDTIYK 356
Cdd:cd03813 403 GSCRELiygadDALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
|
|
| mycothiol_MshA |
TIGR03449 |
D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively ... |
133-331 |
1.90e-29 |
|
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: 117.15 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 133 ADI-IMSTSKVMAEETSQY--TTKDIEITPFGVNIDTFKPfADKYEKKENL-------VIGTVKTLEPKYGIEYLVRAFA 202
Cdd:TIGR03449 164 ADRlIANTDEEARDLVRHYdaDPDRIDVVAPGADLERFRP-GDRATERARLglpldtkVVAFVGRIQPLKAPDVLLRAVA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 203 KVKQKHSNIKLEIAGVG-------EQKDFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRFDIAVFPSTldSESFGVAAV 275
Cdd:TIGR03449 243 ELLDRDPDRNLRVIVVGgpsgsglATPDALIELAAELGIADRVRFLPPRPPEELVHVYRAADVVAVPSY--NESFGLVAM 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 924281479 276 EAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMG 331
Cdd:TIGR03449 321 EAQACGTPVVAARVGGLPVAVADGETGLLVDGHDPADWADALARLLDDPRTRIRMG 376
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
155-344 |
6.22e-29 |
|
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: 115.24 E-value: 6.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 155 IEITPFGVNIDtfkPFADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELni 234
Cdd:cd05844 168 IHVHYIGIDPA---KFAPRDPAERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAAL-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 235 rDHVKFLGFINQEKVIEAFNRFDIAVFPSTL----DSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNV 310
Cdd:cd05844 243 -GRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDV 321
|
170 180 190
....*....|....*....|....*....|....
gi 924281479 311 DELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNI 344
Cdd:cd05844 322 DALADALQALLADRALADRMGGAARAFVCEQFDI 355
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
130-358 |
2.70e-26 |
|
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: 107.80 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 130 LSKADI-IMSTSKVMAEETSQ---YTTKDIEITPFGVNIDTFKPFADKY-------EKKENLVI-GTVKTLEPKYGIEYL 197
Cdd:cd03825 134 LAKKRLtIVAPSRWLADMVRRsplLKGLPVVVIPNGIDTEIFAPVDKAKarkrlgiPQDKKVILfGAESVTKPRKGFDEL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 198 VRAfakVKQKHSNIKLEIAGVGEQKDFLLSLcnELNIRDhvkfLGFI-NQEKVIEAFNRFDIAVFPSTLDSesFGVAAVE 276
Cdd:cd03825 214 IEA---LKLLATKDDLLLVVFGKNDPQIVIL--PFDIIS----LGYIdDDEQLVDIYSAADLFVHPSLADN--LPNTLLE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 277 AQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFN----IEDNFNnvd 352
Cdd:cd03825 283 AMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDqrvqAQRYLE--- 359
|
....*.
gi 924281479 353 tIYKSI 358
Cdd:cd03825 360 -LYKDL 364
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
133-340 |
5.18e-25 |
|
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: 104.30 E-value: 5.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 133 ADIIMSTSKVMAEETSQYTTKDIEITPFGVNIDTFKP------FADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQ 206
Cdd:cd03814 146 FDTTLVPSPSIARELEGHGFERVRLWPRGVDTELFHPsrrdaaLRRRLGPPGRPLLLYVGRLAPEKNLEALLDADLPLAA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 207 kHSNIKLEIAGVGEQKDfllslcnELNIRD-HVKFLGFINQEKVIEAFNRFDIAVFPStlDSESFGVAAVEAQACGTPVI 285
Cdd:cd03814 226 -SPPVRLVVVGDGPARA-------ELEARGpDVIFTGFLTGEELARAYASADVFVFPS--RTETFGLVVLEAMASGLPVV 295
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 924281479 286 VSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVED 340
Cdd:cd03814 296 AADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAER 350
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
178-357 |
4.83e-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: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 178 ENLVIGTVKTLEPKYGIEYLVRAFAKVKQKhsNIKLEIAGvgeqkDFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRFD 257
Cdd:cd03823 190 ERLRFGYIGRLTEEKGIDLLVEAFKRLPRE--DIELVIAG-----HGPLSDERQIEGGRRIAFLGRVPTDDIKDFYEKID 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 258 IAVFPSTLDsESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTgrrf 337
Cdd:cd03823 263 VLVVPSIWP-EPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAG---- 337
|
170 180
....*....|....*....|
gi 924281479 338 VEDNFNIEDNFNNVDTIYKS 357
Cdd:cd03823 338 AEPPRSTESQAEEYLKLYRD 357
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
19-328 |
3.02e-23 |
|
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: 98.90 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 19 RFFNNKGYDIDVISLNDGEIDgvavhsfnKDLDKIRKGS-----SFNKISYIKYFSDIKKIIEKIKPDVVHAHYATSYG- 92
Cdd:cd03812 23 RKLDKSKIEFDFLATSDDKGE--------YDEELEELGGkifyiPPKKKNIIKYFIKLLKLIKKEKYDIVHVHGSSSNGi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 93 -LLGALSGFHPYIISVWGSDVYDfpkgSYIKRKMVEYNLSKADIIMST-----SKVMAEET-SQYTTKDIEITPFGVNID 165
Cdd:cd03812 95 iLLLAAKAGVPVRIAHSHNTKDS----SIKLRKIRKNVLKKLIERLSTkylacSEDAGEWLfGEVENGKFKVIPNGIDIE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 166 TF---KPFADKYEKKEN----LVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHV 238
Cdd:cd03812 171 KYkfnKEKRRKRRKLLIledkLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLEDKV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 239 KFLGFINQekVIEAFNRFDIAVFPSTLdsESFGVAAVEAQACGTPVIVSNVGGlPEATSPNNSSLLVNKKNVDELAEAIE 318
Cdd:cd03812 251 IFLGFRND--VSEILSAMDVFLFPSLY--EGLPLVAVEAQASGLPCLLSDTIT-KECDITNNVEFLPLNETPSTWAEKIL 325
|
330
....*....|
gi 924281479 319 KLIEDDNLRI 328
Cdd:cd03812 326 KLIKRKRRIN 335
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
80-305 |
1.47e-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: 94.78 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 80 PDVVHAHYATSYGLLGALSGF---HPYIISVWGSDVYDFPKGSYIKRKMVEYNLSKADIIMstskvmaeetsqyttkdie 156
Cdd:cd01635 55 PDVVHAHSPHAAALAALLAARllgIPIVVTVHGPDSLESTRSELLALARLLVSLPLADKVS------------------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 157 itpfgvnidtfkpfadkyekkenlvigtVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRD 236
Cdd:cd01635 116 ----------------------------VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 237 HVKFLGFINQEKVIEAFNR-FDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLV 305
Cdd:cd01635 168 RVVIIGGLVDDEVLELLLAaADVFVLPSR--SEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
129-332 |
5.87e-20 |
|
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.
Pssm-ID: 340855 [Multi-domain] Cd Length: 328 Bit Score: 89.28 E-value: 5.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 129 NLSKAD-IIMSTSK---VMAEETSQYTTkdIEITPFGVnIDTFKPFADKYEKKENLVIgTVKTLEPKYGIEYLVRAFAKV 204
Cdd:cd04949 110 NLNKYDaIIVSTEQqkqDLSERFNKYPP--IFTIPVGY-VDQLDTAESNHERKSNKII-TISRLAPEKQLDHLIEAVAKA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 205 KQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLGFINQEKVIeaFNRFDIAVFPSTldSESFGVAAVEAQACGTPV 284
Cdd:cd04949 186 VKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQE--YQDAYLSLLTSQ--MEGFGLTLMEAIGHGLPV 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 924281479 285 IVSNVG-GLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGK 332
Cdd:cd04949 262 VSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSE 310
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
81-322 |
1.45e-18 |
|
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: 86.14 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 81 DVVHAHYATSY----GLLGA-LSGFHPYII--SVWG-SDVydfpkGSYIKRKMVEYNLSKADIIMSTSKVMAEET---SQ 149
Cdd:cd03796 90 QIVHGHQAFSSlaheALFHArTLGLKTVFTdhSLFGfADA-----SSILTNKLLRFSLADIDHVICVSHTSKENTvlrAS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 150 YTTKDIEITPFGVNIDTFKPfADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLC 229
Cdd:cd03796 165 LDPRIVSVIPNAVDSSDFTP-DPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMR 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 230 NELNIRDHVKFLGFINQEKVIEAFNRFDIavFPSTLDSESFGVAAVEAQACGTPVIVSNVGGLPEATsPNNSSLLVNKKN 309
Cdd:cd03796 244 EKYQLQDRVELLGAVPHEEVRDVLVQGHI--FLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVL-PPDMILLAEPDP 320
|
250
....*....|....*.
gi 924281479 310 VD---ELAEAIEKLIE 322
Cdd:cd03796 321 EDivrKLEEAISILRT 336
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
80-355 |
5.38e-18 |
|
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: 84.03 E-value: 5.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 80 PDVVHAHYatsygllgalsgFHPYIISVWGSDVYDFPK----------GSYIKRKMVEYNLSKADIIMSTSKVMAEE-TS 148
Cdd:cd04951 80 PDVVHSHM------------FHANIFARFLRMLYPIPLlictahnkneGGRIRMFIYRLTDFLCDITTNVSREALDEfIA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 149 QYTTKDIEITPF--GVNIDTFKPFADKYEKKEN--------LVIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGV 218
Cdd:cd04951 148 KKAFSKNKSVPVynGIDLNKFKKDINVRLKIRNklnlkndeFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 219 GEQKDFLLSLCNELNIRDHVKFLGFINQekVIEAFNRFDIAVFPSTLdsESFGVAAVEAQACGTPVIVSNVGGLPEATSP 298
Cdd:cd04951 228 GPLRNELERLICNLNLVDRVILLGQISN--ISEYYNAADLFVLSSEW--EGFGLVVAEAMACERPVVATDAGGVAEVVGD 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 924281479 299 NNssLLVNKKNVDELAEAI-EKLIEDDNLRINMGKTgRRFVEDNFNIEDNFNNVDTIY 355
Cdd:cd04951 304 HN--YVVPVSDPQLLAEKIkEIFDMSDEERDILGNK-NEYIAKNFSINTIVNEWERLY 358
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
80-344 |
1.56e-17 |
|
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: 82.85 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 80 PDVVHAH--YATSYGLLGALSGFHPYIISVWGSDVYDfPKGSYIKrkmveYNLSKADI--IMSTSKVMAEETSQYTTKDI 155
Cdd:TIGR03088 82 PDIVHTRnlAALEAQLPAALAGVPARIHGEHGRDVFD-LDGSNWK-----YRWLRRLYrpLIHHYVAVSRDLEDWLRGPV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 156 EITPF-------GVNIDTFKP--------FADKYEKKENLVIGTVKTLEPKYGIEYLVRAFAKVKQKHS----NIKLEIA 216
Cdd:TIGR03088 156 KVPPAkihqiynGVDTERFHPsrgdrspiLPPDFFADESVVVGTVGRLQAVKDQPTLVRAFALLVRQLPegaeRLRLVIV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 217 GVGEQKDFLLSLCNELNIRDHVKFLGfiNQEKVIEAFNRFDIAVFPSTldSESFGVAAVEAQACGTPVIVSNVGGLPEAT 296
Cdd:TIGR03088 236 GDGPARGACEQMVRAAGLAHLVWLPG--ERDDVPALMQALDLFVLPSL--AEGISNTILEAMASGLPVIATAVGGNPELV 311
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 924281479 297 SPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNI 344
Cdd:TIGR03088 312 QHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSI 359
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
159-345 |
1.85e-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: 82.34 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 159 PFGVNIDTFkPFADKyeKKENLV-IGTVKtlePKYGIEYLVRAFAKvkqkhSNIKLEIAGVGEQKDFLLSLcNELNIRDH 237
Cdd:cd03802 154 HNGLDPADY-RFQPD--PEDYLAfLGRIA---PEKGLEDAIRVARR-----AGLPLKIAGKVRDEDYFYYL-QEPLPGPR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 238 VKFLGFINQEKVIEAFNRFDIAVFPSTLDsESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNkkNVDELAEAI 317
Cdd:cd03802 222 IEFIGEVGHDEKQELLGGARALLFPINWD-EPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVD--SVEEMAEAI 298
|
170 180
....*....|....*....|....*...
gi 924281479 318 EKLIEDDNLRInmgktgRRFVEDNFNIE 345
Cdd:cd03802 299 ANIDRIDRAAC------RRYAEDRFSAA 320
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
131-339 |
6.42e-17 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 81.68 E-value: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 131 SKADIIMSTSKVMAEE--TSQYTT-KDIEITPFGVNIDTFKPFADKYEKKENL--------VIGTVKTLepkyGIEYLVR 199
Cdd:PLN02871 204 RAADLTLVTSPALGKEleAAGVTAaNRIRVWNKGVDSESFHPRFRSEEMRARLsggepekpLIVYVGRL----GAEKNLD 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 200 AFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNirdhVKFLGFINQEKVIEAFNRFDIAVFPStlDSESFGVAAVEAQA 279
Cdd:PLN02871 280 FLKRVMERLPGARLAFVGDGPYREELEKMFAGTP----TVFTGMLQGDELSQAYASGDVFVMPS--ESETLGFVVLEAMA 353
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 924281479 280 CGTPVIVSNVGGLPE---ATSPNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVE 339
Cdd:PLN02871 354 SGVPVVAARAGGIPDiipPDQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVE 416
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
116-345 |
7.98e-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: 7.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 116 PKGSYIKR-------KMVEYNLSKADIIMSTSKVMAEETSQyTTKDIEITPFGV-----NIDTFKPFADKYEKKENLVIG 183
Cdd:cd03805 131 QRKSLLKRlyrkpfdWLEEFTTGMADQIVVNSNFTAGVFKK-TFPSLAKNPPEVlypcvDTDSFDSTSEDPDPGDLIAKS 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 184 TVKTL------EPKYGIEYLVRAFAKVKQKH---SNIKLEIAG-----VGEQKDF---LLSLCNEL-NIRDHVKFLGFIN 245
Cdd:cd03805 210 NKKFFlsinrfERKKNIALAIEAFAKLKQKLpefENVRLVIAGgydprVAENVEYleeLQRLAEELlNVEDQVLFLRSIS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 246 QEKVIEAFNRFDIAVFpsTLDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNkKNVDELAEAIEKLIEDDN 325
Cdd:cd03805 290 DSQKEQLLSSALALLY--TPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCE-PTPEAFAEAMLKLANDPD 366
|
250 260
....*....|....*....|
gi 924281479 326 LRINMGKTGRRFVEDNFNIE 345
Cdd:cd03805 367 LADRMGAAGRKRVKEKFSRE 386
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
162-318 |
9.82e-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: 77.33 E-value: 9.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 162 VNIDTFKPfadKYEKKENLVigTVKTLEPKYGIEYLVRAFAKvkqkhSNIKLEIAGVGEQKDFLLSLCnelniRDHVKFL 241
Cdd:cd03804 187 VDTDAFAP---AADKEDYYL--TASRLVPYKRIDLAVEAFNE-----LPKRLVVIGDGPDLDRLRAMA-----SPNVEFL 251
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 924281479 242 GFINQEKVIEAFNRFDIAVFPSTldsESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIE 318
Cdd:cd03804 252 GYQPDEVLKELLSKARAFVFAAE---EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVE 325
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
190-344 |
1.22e-13 |
|
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: 71.20 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 190 PKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKD----FLLS--LCNELNIRD-HVKFLGFINQEkvIEAFNRF-DIAVF 261
Cdd:cd03792 208 PSKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDDpegsVVYEevMEYAGDDHDiHVLRLPPSDQE--INALQRAaTVVLQ 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 262 PSTldSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKknVDELAEAIEKLIEDDNLRINMGKTGRRFVEDN 341
Cdd:cd03792 286 LST--REGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNS--VEGAAVRILRLLTDPELRRKMGLAAREHVRDN 361
|
...
gi 924281479 342 FNI 344
Cdd:cd03792 362 FLI 364
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
154-345 |
2.02e-13 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 70.59 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 154 DIEITPFGVNIDTFKPFADKyEKKENLVIGTVKT-------LEPKYGIEYLVRAFAKVKQKHSNIKLEIAG------VGE 220
Cdd:PRK15484 162 DISIVPNGFCLETYQSNPQP-NLRQQLNISPDETvllyagrISPDKGILLLMQAFEKLATAHSNLKLVVVGdptassKGE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 221 QKDF---LLSLCNElnIRDHVKFLGFINQEKVIEAFNRFDIAVFPSTLDsESFGVAAVEAQACGTPVIVSNVGGLPEATS 297
Cdd:PRK15484 241 KAAYqkkVLEAAKR--IGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVE-EAFCMVAVEAMAAGKPVLASTKGGITEFVL 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 924281479 298 PNNSSL-LVNKKNVDELAEAIEKLIEDDNlRINMGKTGRRFVEDNFNIE 345
Cdd:PRK15484 318 EGITGYhLAEPMTSDSIISDINRTLADPE-LTQIAEQAKDFVFSKYSWE 365
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
49-349 |
4.58e-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: 69.80 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 49 DLDKIRKGSSFNK--------ISYIKYFSDIKKIIEKIKPDVVHAH--YATSYGL-LGALSGFHPYIIS-VWGSDVYDFP 116
Cdd:cd04946 83 IKDKPRSGSFLLLyyfliasfLSKHRVLALLQFVSIFGQGTVVYSYwlNHTALGLgLLKDEYYRDVVISrAHRYDLYEDQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 117 KGSYI---KRKMVEYnLSKADIIMSTSKVMAEETSQYTTKDIEITPFGVNIDTFKpfaDKYEKKENLVIGTVKTLEPKYG 193
Cdd:cd04946 163 YGSYYlplREYLVSY-LDAVFLISKEGKDYLQKCYPAYKEKIFVSRLGVSDKEQY---SKVKKEGDLRLVSCSSIVPVKR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 194 IEYLVRAFAKVKQKHSNIKLEIA--GVGEQKDFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRFDIAVFPSTLDSESFG 271
Cdd:cd04946 239 IDLIIETLNSLCVAHPSICISWThiGGGPLKERLEKLAENKLENVKVNFTGEVSNKEVKQLYKENDVDVFVNVSESEGIP 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 924281479 272 VAAVEAQACGTPVIVSNVGGLPEATS-PNNSSLLVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNFNIEDNFN 349
Cdd:cd04946 319 VSIMEAISFGIPVIATNVGGTREIVEnETNGLLLDKDPTPNEIVSSIMKFYLDGGDYKTMKISARECWEERFNAEVNYS 397
|
|
| COG4641 |
COG4641 |
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]; |
129-338 |
1.24e-09 |
|
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443679 [Multi-domain] Cd Length: 303 Bit Score: 58.79 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 129 NLSKADIIMSTSKVMAEETSQYTTKDIEITPFGVNIDTFKPFADKYEKKENLV-IGTvktlepkyGIEYLVRAFAKVKQK 207
Cdd:COG4641 89 LLPLYDLVFTFDGDCVEEYRALGARRVFYLPFAADPELHRPVPPEARFRYDVAfVGN--------YYPDRRARLEELLLA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 208 HSNIKLEIAGVGeqkdFllslcNELNIRDHVKFLGFINQEKVIEAFNRFDIAV-FPSTLDSE-SFGVAAVEAQACGTPVI 285
Cdd:COG4641 161 PAGLRLKIYGPG----W-----PKLALPANVRRGGHLPGEEHPAAYASSKITLnVNRMAASPdSPTRRTFEAAACGAFLL 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 924281479 286 VSNVGGLPEATSPNNSSLLVNkkNVDELAEAIEKLIEDDNLRINMGKTGRRFV 338
Cdd:COG4641 232 SDPWEGLEELFEPGEEVLVFR--DGEELAEKLRYLLADPEERRAIAEAGRRRV 282
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
155-327 |
1.69e-09 |
|
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.
Pssm-ID: 340849 [Multi-domain] Cd Length: 370 Bit Score: 58.55 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 155 IEITPFGVNIdtfKPFADKYEKKENL------VIGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAG--VGEQKD--- 223
Cdd:cd03822 160 IEVIPHGVPE---VPQDPTTALKRLLlpegkkVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGelHPSLARyeg 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 224 --FLLSLCNELNIRDHVKF-LGFINQEKVIEAFNRFDIAVFP--STLDSESfGVAAVeAQACGTPVIVSNVGGLpEATSP 298
Cdd:cd03822 237 erYRKAAIEELGLQDHVDFhNNFLPEEEVPRYISAADVVVLPylNTEQSSS-GTLSY-AIACGKPVISTPLRHA-EELLA 313
|
170 180
....*....|....*....|....*....
gi 924281479 299 NNSSLLVNKKNVDELAEAIEKLIEDDNLR 327
Cdd:cd03822 314 DGRGVLVPFDDPSAIAEAILRLLEDDERR 342
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
176-346 |
2.12e-08 |
|
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: 55.45 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 176 KKENLVIGTV-KTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAG------------VGEQKDFLLSlcnELNI-RDHVKFL 241
Cdd:cd03818 210 KAGDPVITYVaRNLEPYRGFHVFMRALPRIQARRPDARVVVVGgdgvsygspppdGGSWKQKMLA---ELGVdLERVHFV 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 242 GFINQEKVIEAFNRFDIAVFPSTLDSESFGVaaVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLI 321
Cdd:cd03818 287 GKVPYDQYVRLLQLSDAHVYLTYPFVLSWSL--LEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELL 364
|
170 180
....*....|....*....|....*
gi 924281479 322 EDDNLRINMGKTGRRFVEDNFNIED 346
Cdd:cd03818 365 EDPDRAAALRRAARRTVERSDSLDV 389
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
162-342 |
4.20e-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: 54.54 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 162 VNIDTFKPFADKYEKKENLVIgTVKTLEPKYGIEYLVRAFAKVKQKH-----SNIKLEIAG-VGEQKD-----FLLSLCN 230
Cdd:cd03806 221 CDTEELTKLPIDEKTRENQIL-SIAQFRPEKNHPLQLRAFAELLKRLpesirSNPKLVLIGsCRNEEDkerveALKLLAK 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 231 ELNIRDHVKFLGFINQEKVIEAFNRFDIAVfpSTLDSESFGVAAVEAQACGTPVIVSNVGGlPE-----ATSPNNSSLLV 305
Cdd:cd03806 300 ELILEDSVEFVVDAPYEELKELLSTASIGL--HTMWNEHFGIGVVEYMAAGLIPLAHASAG-PLldivvPWDGGPTGFLA 376
|
170 180 190
....*....|....*....|....*....|....*..
gi 924281479 306 nkKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDNF 342
Cdd:cd03806 377 --STPEEYAEAIEKILTLSEEERLQRREAARSSAERF 411
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
258-343 |
4.34e-08 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 50.30 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 258 IAVFPStLDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVnkKNVDELAEAIEKLIEDDNLRINMGKTGRRF 337
Cdd:pfam13524 1 IVLNPS-RRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLY--RDPEELAEKIRYLLEHPEERRAIAAAGRER 77
|
....*.
gi 924281479 338 VEDNFN 343
Cdd:pfam13524 78 VLAEHT 83
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
198-343 |
1.43e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 49.74 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 198 VRAFAKVKQKHS----NIKLEIAGVGEQK------DFLLSLCNELNIRDHVKFLGFINQEKVIEAFNRfDIAVFPSTLDs 267
Cdd:PLN02949 287 LEAFALALEKLDadvpRPKLQFVGSCRNKedeerlQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGG-AVAGLHSMID- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 268 ESFGVAAVEAQACGTPVIVSNVGG------LPEATSPnnSSLLVNkkNVDELAEAIEKLIE-DDNLRINMGKTGR----R 336
Cdd:PLN02949 365 EHFGISVVEYMAAGAVPIAHNSAGpkmdivLDEDGQQ--TGFLAT--TVEEYADAILEVLRmRETERLEIAAAARkranR 440
|
....*..
gi 924281479 337 FVEDNFN 343
Cdd:PLN02949 441 FSEQRFN 447
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
182-331 |
3.33e-06 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 48.88 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 182 IGTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLGFINqeKVIEAFNRFDIAVF 261
Cdd:PRK15179 520 VGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSR--RVGYWLTQFNAFLL 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 924281479 262 PSTLdsESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVD--ELAEAIEKLIedDNLRINMG 331
Cdd:PRK15179 598 LSRF--EGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTapDVAEALARIH--DMCAADPG 665
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
11-165 |
3.44e-04 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 40.98 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 11 STHTKKWCRFFNNKGYDIDVISLNDG------EIDGVAVHSFNKDLDKIRKGSSFNKISYIKYFSDIKkiiekikPDVVH 84
Cdd:pfam13439 4 ERYVLELARALARRGHEVTVVTPGGPgplaeeVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRER-------PDVVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 85 AHYATS--YGLLGALSGFH-PYIISV-----WGSDVYDFPKGSYIKRKMVEYNL-SKADIIMSTSKVMAEETSQY---TT 152
Cdd:pfam13439 77 AHSPFPlgLAALAARLRLGiPLVVTYhglfpDYKRLGARLSPLRRLLRRLERRLlRRADRVIAVSEAVADELRRLygvPP 156
|
170
....*....|...
gi 924281479 153 KDIEITPFGVNID 165
Cdd:pfam13439 157 EKIRVIPNGVDLE 169
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
25-146 |
1.10e-03 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 39.31 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 25 GYDIDVISLNDGEI------DGVAVHSfnkdLDKIRKGSSFNKISYIKYFSDIKKIIEkikPDVVHAHYATS--YGLLGA 96
Cdd:pfam13579 18 GHEVRVVTPGGPPGrpelvgDGVRVHR----LPVPPRPSPLADLAALRRLRRLLRAER---PDVVHAHSPTAglAARLAR 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 924281479 97 LSGFHPYIISVWGSDV--YDFPKGSYIkRKMVEYNLSKADIIMSTSKVMAEE 146
Cdd:pfam13579 91 RRRGVPLVVTVHGLALdyGSGWKRRLA-RALERRLLRRADAVVVVSEAEAEL 141
|
|
| PRK05749 |
PRK05749 |
3-deoxy-D-manno-octulosonic-acid transferase; Reviewed |
276-341 |
1.12e-03 |
|
3-deoxy-D-manno-octulosonic-acid transferase; Reviewed
Pssm-ID: 235589 [Multi-domain] Cd Length: 425 Bit Score: 40.59 E-value: 1.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 924281479 276 EAQACGTPVIvsnvgglpeaTSP---NNSSL---------LVNKKNVDELAEAIEKLIEDDNLRINMGKTGRRFVEDN 341
Cdd:PRK05749 339 EPAAFGVPVI----------SGPhtfNFKEIferllqagaAIQVEDAEDLAKAVTYLLTDPDARQAYGEAGVAFLKQN 406
|
|
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
268-329 |
2.96e-03 |
|
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.
Pssm-ID: 274147 [Multi-domain] Cd Length: 1050 Bit Score: 39.76 E-value: 2.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 924281479 268 ESFGVAAVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKKNVDELAEAIEKLIEDDNL----RIN 329
Cdd:TIGR02468 582 EPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKLVADKQLwaecRQN 647
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
167-358 |
4.24e-03 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 38.91 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 167 FKPFADKYEKKENLVIGTVKTLEPKYGIEYLVRAfAKVKQKHSNIKLEIAGVGEQKDFLLSLCNELNIRDHVKFLG---- 242
Cdd:PRK15490 387 WQQFTQKTQDADTTIGGVFRFVGDKNPFAWIDFA-ARYLQHHPATRFVLVGDGDLRAEAQKRAEQLGILERILFVGasrd 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 243 ---FINQEKVIEAFNRFDiaVFPSTLdsesfgvaaVEAQACGTPVIVSNVGGLPEATSPNNSSLLVNKK---NVDELAEA 316
Cdd:PRK15490 466 vgyWLQKMNVFILFSRYE--GLPNVL---------IEAQMVGVPVISTPAGGSAECFIEGVSGFILDDAqtvNLDQACRY 534
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 924281479 317 IEKLIEDDNLRINMGKTGRRFVEDNFNIEdnfNNVDTIYKSI 358
Cdd:PRK15490 535 AEKLVNLWRSRTGICQQTQSFLQERFTVE---HMVGTFVKTI 573
|
|
| PHA01633 |
PHA01633 |
putative glycosyl transferase group 1 |
183-315 |
6.98e-03 |
|
putative glycosyl transferase group 1
Pssm-ID: 107050 [Multi-domain] Cd Length: 335 Bit Score: 38.04 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924281479 183 GTVKTLEPKYGIEYLVRAFAKVKQKHSNIKLEIAG-VGEQKDFllslcNELNIRDHVKFL---GFINQEKVIEAFNRFDI 258
Cdd:PHA01633 152 GIVSGLTKRKNMDLMLQVFNELNTKYPDIAKKIHFfVISHKQF-----TQLEVPANVHFVaefGHNSREYIFAFYGAMDF 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 924281479 259 AVFPStlDSESFGVAAVEAQACGTPVIVSNVGGLPEATSPnNSSLLVNKKNVDELAE 315
Cdd:PHA01633 227 TIVPS--GTEGFGMPVLESMAMGTPVIHQLMPPLDEFTSW-QWNLLIKSSKVEEYYD 280
|
|
|