|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
9-389 |
0e+00 |
|
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: 637.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 9 MNIAIIHPDLGIGGAERLIVDAAVELASHGHKVHIFTSHHDKSRCFEETLSGIFQVTVYGSFLPRHIFYRLHAVCAYLRC 88
Cdd:cd03805 1 LRVAFLHPDLGIGGAERLVVDAALALQSRGHEVTIYTSHHDPSHCFEETKDGTLPVRVRGDWLPRSIFGRFHALCAYLRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 89 LFVALCVLLG-WSSFDVVLADQVSVVVPLLKLKRSSKVVFYCHFPDLLLAKHTTTLRRMYRKPIDFIEEQTTGMADMILV 167
Cdd:cd03805 81 LYLALYLLLFsGEKYDVFIVDQVSACVPLLKLFRPSKILFYCHFPDQLLAQRKSLLKRLYRKPFDWLEEFTTGMADQIVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 168 NSNFTASTFANTFKRLNAQGSRpaVLYPAVNIDQF-----------IEPHTYKLNFLSINRFERKKNIDLAVSAFAILCK 236
Cdd:cd03805 161 NSNFTAGVFKKTFPSLAKNPPE--VLYPCVDTDSFdstsedpdpgdLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 237 HKQNLSDVTLTVAGGYDERLKENVEYLEELRSLAEK-EGVSDRVNFITSCSTAERNELLSSCLCVLYTPTDEHFGIVPLE 315
Cdd:cd03805 239 KLPEFENVRLVIAGGYDPRVAENVEYLEELQRLAEElLNVEDQVLFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPLE 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22330726 316 AMAAYKPVIACNSGGPVETVKNGVTGYLCEPTPEDFSSAMARFIENPELANRMGAEARNHVVESFSVKTFGQKL 389
Cdd:cd03805 319 AMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAERL 392
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
10-381 |
5.69e-53 |
|
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: 180.43 E-value: 5.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 10 NIAIIHPDL--GIGGAERLIVDAAVELASHGHKVHIFTsHHDKSRCFEETLSGIFQVTVYGSFLPRHIFYRLHAVCAYLR 87
Cdd:cd03801 1 KILLLSPELppPVGGAERHVRELARALAARGHDVTVLT-PADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 88 clfvalcvllgWSSFDVVLA--DQVSVVVPLLKLKRSSKVVFYCH-FPDLLLAKHTTTLRRMYRKPIDFIEeqttgMADM 164
Cdd:cd03801 80 -----------LRKFDVVHAhgLLAALLAALLALLLGAPLVVTLHgAEPGRLLLLLAAERRLLARAEALLR-----RADA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 165 ILVNSNFTASTFANTFKRLNaqgSRPAVLYPAVNIDQFIEPHTYKLN-------FLSINRFERKKNIDLAVSAFAILckh 237
Cdd:cd03801 144 VIAVSEALRDELRALGGIPP---EKIVVIPNGVDLERFSPPLRRKLGippdrpvLLFVGRLSPRKGVDLLLEALAKL--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 238 KQNLSDVTLTVAGGYDErlkenveYLEELRSLaeKEGVSDRVNFITSCSTAERNELLSSCLCVLYTPTDEHFGIVPLEAM 317
Cdd:cd03801 218 LRRGPDVRLVIVGGDGP-------LRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAM 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22330726 318 AAYKPVIACNSGGPVETVKNGVTGYLCEPT-PEDFSSAMARFIENPELANRMGAEARNHVVESFS 381
Cdd:cd03801 289 AAGLPVVATDVGGLPEVVEDGEGGLVVPPDdVEALADALLRLLADPELRARLGRAARERVAERFS 353
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
212-375 |
1.38e-40 |
|
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: 141.26 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 212 FLSINRFERKKNIDLAVSAFAILCKhkqNLSDVTLTVAGgyderlkeNVEYLEELRSLAEKEGVSDRVNFITSCSTAERN 291
Cdd:pfam00534 5 ILFVGRLEPEKGLDLLIKAFALLKE---KNPNLKLVIAG--------DGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 292 ELLSSCLCVLYTPTDEHFGIVPLEAMAAYKPVIACNSGGPVETVKNGVTGYLCEPT-PEDFSSAMARFIENPELANRMGA 370
Cdd:pfam00534 74 ELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNnAEALAEAIDKLLEDEELRERLGE 153
|
....*
gi 22330726 371 EARNH 375
Cdd:pfam00534 154 NARKR 158
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
10-385 |
1.98e-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: 135.95 E-value: 1.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 10 NIAIIHPDLGIGGAERLIVDAAVELASHGHKVHIFTshHDKSRCFEETLSGIFQVTVYGSFLPRHIFYRLHAVCAYLRcl 89
Cdd:cd03811 1 KILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVL--LRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 90 fvalcVLLGWSSFDVVLA-DQVSVVVPLLKLKRSSKVVFYCH-FPDLLLAKHTTTL--RRMYRKpidfieeqttgmADMI 165
Cdd:cd03811 77 -----RILKRAKPDVVISfLGFATYIVAKLAAARSKVIAWIHsSLSKLYYLKKKLLlkLKLYKK------------ADKI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 166 LVNSNFTASTFAntfKRLNAQGSRPAVLYPAVNIDQFIEP--------HTYKLNFLSINRFERKKNIDLAVSAFAILckh 237
Cdd:cd03811 140 VCVSKGIKEDLI---RLGPSPPEKIEVIYNPIDIDRIRALakepilnePEDGPVILAVGRLDPQKGHDLLIEAFAKL--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 238 KQNLSDVTLTVAGGYDERlkenveylEELRSLAEKEGVSDRVNFITSCSTAerNELLSSCLCVLYTPTDEHFGIVPLEAM 317
Cdd:cd03811 214 RKKYPDVKLVILGDGPLR--------EELEKLAKELGLAERVIFLGFQSNP--YPYLKKADLFVLSSRYEGFPNVLLEAM 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22330726 318 AAYKPVIACNSGGPVETVKNGVTGYLCEPTPEDFSSAMARFIENPELANRMGAEARNHVVESFSVKTF 385
Cdd:cd03811 284 ALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEAVFREYTI 351
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
154-381 |
2.70e-36 |
|
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: 136.60 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 154 IEEQTTGMADMILVNsnfTASTFANTFKRLNAQGSRPAVLYPAVNIDQF--------------IEPHTYKLnfLSINRFE 219
Cdd:cd03800 156 AEEQILEAADRVIAS---TPQEADELISLYGADPSRINVVPPGVDLERFfpvdraearrarllLPPDKPVV--LALGRLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 220 RKKNIDLAVSAFAILCKHKQnlsDVTLTVAGGYDERLKENVEylEELRSLAEKEGVSDRVNFITSCSTAERNELLSSC-L 298
Cdd:cd03800 231 PRKGIDTLVRAFAQLPELRE---LANLVLVGGPSDDPLSMDR--EELAELAEELGLIDRVRFPGRVSRDDLPELYRAAdV 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 299 CVLyTPTDEHFGIVPLEAMAAYKPVIACNSGGPVETVKNGVTGYLCEPT-PEDFSSAMARFIENPELANRMGAEARNHVV 377
Cdd:cd03800 306 FVV-PSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHdPEALAAALRRLLDDPALWQRLSRAGLERAR 384
|
....
gi 22330726 378 ESFS 381
Cdd:cd03800 385 AHYT 388
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
85-388 |
5.85e-34 |
|
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: 130.81 E-value: 5.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 85 YLRCLFVALC-VLLGWSSFDVVLADqvsVVV---------PLLKLKRSSKVVFYCHFP-------------------DLL 135
Cdd:cd03806 85 RFTLLGQALGsMILGFEALLKLVPD---VFIdtmgypftyPLVRLLGGCPVVAYVHYPtistdmlnkvrsreasynnDST 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 136 LAKH--TTTLRRMYRKPIDFIEEQTTGMADMILVNSNFTASTFANTFKRLNaqgsRPAVLYPAVNIDQF----IEPHTYK 209
Cdd:cd03806 162 IARSsvLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNI----KPSIVYPPCDTEELtklpIDEKTRE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 210 LNFLSINRFERKKNIDLAVSAFAILCK-HKQN-LSDVTLTVAGGYdeRLKENVEYLEELRSLAEKEGVSDRVNFITSCST 287
Cdd:cd03806 238 NQILSIAQFRPEKNHPLQLRAFAELLKrLPESiRSNPKLVLIGSC--RNEEDKERVEALKLLAKELILEDSVEFVVDAPY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 288 AERNELLSSCLCVLYTPTDEHFGIVPLEAMAAYKPVIACNSGGP----VETVKNGVTGYLCEpTPEDFSSAMARFIENPE 363
Cdd:cd03806 316 EELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPlldiVVPWDGGPTGFLAS-TPEEYAEAIEKILTLSE 394
|
330 340
....*....|....*....|....*
gi 22330726 364 LANRMGAEARNHVVESFSVKTFGQK 388
Cdd:cd03806 395 EERLQRREAARSSAERFSDEEFERD 419
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
11-384 |
8.15e-33 |
|
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: 126.20 E-value: 8.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 11 IAIIHPDLG-IGGAERLIVDAAVELASHGHKVHIFTSHHDKSRCFEE-----TLSGIFQVTVYGSFLPRHIFYRLHAVCA 84
Cdd:cd03820 2 IAIVIPSISnAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYElddniKIKNLGDRKYSHFKLLLKYFKKVRRLRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 85 YLRClfvalcvllgwSSFDVVLADQVSVVVPLLKLKRSSKVVFYCHFP---DLLLAKHTTTLRRMYRKpidfieeqttgm 161
Cdd:cd03820 82 YLKN-----------NKPDVVISFRTSLLTFLALIGLKSKLIVWEHNNyeaYNKGLRRLLLRRLLYKR------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 162 ADMILVNsnfTASTFANTFKRLNAQGsrpAVLYPAVNIDQFiePHTYKLN---FLSINRFERKKNIDLAVSAFAILCKhk 238
Cdd:cd03820 139 ADKIVVL---TEADKLKKYKQPNSNV---VVIPNPLSFPSE--EPSTNLKskrILAVGRLTYQKGFDLLIEAWALIAK-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 239 qNLSDVTLTVAGGYDERlkenveylEELRSLAEKEGVSDRVNFItsCSTAE-RNELLSSCLCVLyTPTDEHFGIVPLEAM 317
Cdd:cd03820 209 -KHPDWKLRIYGDGPER--------EELEKLIDKLGLEDRVKLL--GPTKNiAEEYANSSIFVL-SSRYEGFPMVLLEAM 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 318 AAYKPVIA--CNSgGPVETVKNGVTGYLCEP-TPEDFSSAMARFIENPELANRMGAEARnHVVESFSVKT 384
Cdd:cd03820 277 AYGLPIISfdCPT-GPSEIIEDGENGLLVPNgDVDALAEALLRLMEDEELRKKMGKNAR-KNAERFSIEK 344
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
20-383 |
1.71e-31 |
|
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: 122.70 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 20 IGGAERLIVDAAVELASHGHKVHIFTSHHDKSRCFEETLsgifQVTVYGSFLPRH---IFYRLHAVcAYLRCLFVALcvl 96
Cdd:cd03808 9 DGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKEL----GVKVIDIPILRRginPLKDLKAL-FKLYKLLKKE--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 97 lgwsSFDVVLAdqVS---VVVPLL--KLKRSSKVVFYCHfpdlllAKHTTTLRRMYRKPIDFIEEQTTG-MADMILVNSN 170
Cdd:cd03808 81 ----KPDIVHC--HTpkpGILGRLaaRLAGVPKVIYTVH------GLGFVFTEGKLLRLLYLLLEKLALlFTDKVIFVNE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 171 FTastfANTFKRLNAQGSRPAVLYP--AVNIDQF------IEPHTYKLNFLSinRFERKKNIDLAVSAFAILckhKQNLS 242
Cdd:cd03808 149 DD----RDLAIKKGIIKKKKTVLIPgsGVDLDRFqyspesLPSEKVVFLFVA--RLLKDKGIDELIEAAKIL---KKKGP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 243 DVTLTVAGGYDERlkenveylEELRSLAEKEGVSDRVNFITSCSTAErnELLSSC-LCVLytPTD-EHFGIVPLEAMAAY 320
Cdd:cd03808 220 NVRFLLVGDGELE--------NPSEILIEKLGLEGRIEFLGFRSDVP--ELLAESdVFVL--PSYrEGLPRSLLEAMAAG 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22330726 321 KPVIACNSGGPVETVKNGVTGYLCEP-TPEDFSSAMARFIENPELANRMGAEARNHVVESFSVK 383
Cdd:cd03808 288 RPVITTDVPGCRELVIDGVNGFLVPPgDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEE 351
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
293-398 |
1.01e-26 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 103.15 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 293 LLSSCLCVLYTPTDEHFGIVPLEAMAAYKPVIACNSGGPVETVKNGVTGYLCEP-TPEDFSSAMARFIENPELANRMGAE 371
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPgDPEALAEAILRLLEDPELRRRLGEA 96
|
90 100
....*....|....*....|....*..
gi 22330726 372 ARNHVVESFSVKTFGQKLNQYLVDVVS 398
Cdd:COG0438 97 ARERAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
11-389 |
2.80e-25 |
|
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: 105.44 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 11 IAIIHPDL-GIGGAERLIVdAAVELASHGHkvhIFTSHHDKSRCFEETLSGIFqvtVYGSFLPRHIFYRLHavcaYLRCL 89
Cdd:cd03804 2 VAIVHDWLvNYGGAERVLE-ALLELFPQAD---IYTLVDFLDKDDRLFIRGKK---VRTSFIQKLPKAKRK----YRKYL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 90 FvaLCVL----LGWSSFDVVLADQVSVVVPLLKlkRSSKV-VFYCHFP-----DL----------------LLAKHTTTL 143
Cdd:cd03804 71 P--LMPLaieqFDLSGYDLVISSSHAVAKGVLT--RPDQLhVCYVHSPiryawDLyhqylaesglgkgiksLLASLFLHY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 144 RRMYrkpiDFieeQTTGMADMILVNSNFTAstfantfKRLNAQGSRPA-VLYPAVNIDQFiEPHTYKLN-FLSINRFERK 221
Cdd:cd03804 147 LRLW----DV---RTAQRVDLFIANSQFVA-------RRIKKFYGREStVIYPPVDTDAF-APAADKEDyYLTASRLVPY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 222 KNIDLAVSAFAILCKHkqnlsdvtLTVAG-GYDerlkenveyLEELRSLAekegvSDRVNFITSCSTAERNELLSSCLCV 300
Cdd:cd03804 212 KRIDLAVEAFNELPKR--------LVVIGdGPD---------LDRLRAMA-----SPNVEFLGYQPDEVLKELLSKARAF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 301 LYtPTDEHFGIVPLEAMAAYKPVIACNSGGPVETVKNGVTGYL-CEPTPEDFSSAMARFIENPElanRMGAEA-RNHvVE 378
Cdd:cd03804 270 VF-AAEEDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILfGEQTVESLKAAVEEFEQNFD---RFKPQAiRAN-AE 344
|
410
....*....|.
gi 22330726 379 SFSVKTFGQKL 389
Cdd:cd03804 345 RFSRARFRQEI 355
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
11-396 |
3.03e-25 |
|
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: 105.54 E-value: 3.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 11 IAIIHPDLGIGGAERLIVDAAVELASHGHKVHIFT--SHHDKSRCFEETLSGIFQVTVYGSFLprHIFY-----RLHAVC 83
Cdd:cd03798 4 LTNIYPNANSPGRGIFVRRQVRALSRRGVDVEVLApaPWGPAAARLLRKLLGEAVPPRDGRRL--LPLKprlrlLAPLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 84 AYLRCLfvaLCVLLGWSsFDVVLADQVSVVVPL-LKLKRSSKV--VFYCHFPDLLLAKHTTTLRRMYRkpidFIEEQTTG 160
Cdd:cd03798 82 PSLAKL---LKRRRRGP-PDLIHAHFAYPAGFAaALLARLYGVpyVVTEHGSDINVFPPRSLLRKLLR----WALRRAAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 161 MAdmilvnsnFTASTFANTFKRLNAQGSRPAVLYPAVNIDQF-------IEPHTYKLnFLSINRFERKKNIDLAVSAFAI 233
Cdd:cd03798 154 VI--------AVSKALAEELVALGVPRDRVDVIPNGVDPARFqpedrglGLPLDAFV-ILFVGRLIPRKGIDLLLEAFAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 234 LCKHKQnlsDVTLTVAGGYDERlkenveylEELRSLAEKEGVSDRVNFITSCSTAERNELLSSCLC-VLytPT-DEHFGI 311
Cdd:cd03798 225 LAKARP---DVVLLIVGDGPLR--------EALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVfVL--PSrHEGFGL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 312 VPLEAMAAYKPVIACNSGGPVETVKNGVTGYLCEPT-PEDFSSAMARFIENPELaNRMGAEARNHVVESFSVKTFGQKLN 390
Cdd:cd03798 292 VLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGdADALAAALRRALAEPYL-RELGEAARARVAERFSWVKAADRIA 370
|
....*.
gi 22330726 391 QYLVDV 396
Cdd:cd03798 371 AAYRDV 376
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
10-389 |
2.87e-24 |
|
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: 103.19 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 10 NIAIIHPD--LGIGGAERLIVDAAVELASHGHKVHIFTS--HHDKSRCF---EETLSGI-FQVTVYGSFLPRHIFYR-LH 80
Cdd:cd03794 1 KILLISQYypPPKGAAAARVYELAKELVRRGHEVTVLTPspNYPLGRIFagaTETKDGIrVIRVKLGPIKKNGLIRRlLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 81 AVCAYLRCLFVALcvlLGWSSFDVVLAdqVS------VVVPLLKLKRSSKVVFYCH--FPDLLLAKHTTTLRRMYRKpID 152
Cdd:cd03794 81 YLSFALAALLKLL---VREERPDVIIA--YSppitlgLAALLLKKLRGAPFILDVRdlWPESLIALGVLKKGSLLKL-LK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 153 FIEEQTTGMADMILVNSNftasTFANTFKRLNAQGSRPAVLYPAVNIDQFIEPHTYKLNFLSINR----------FERKK 222
Cdd:cd03794 155 KLERKLYRLADAIIVLSP----GLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPKDELRKKLGLDdkfvvvyagnIGKAQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 223 NIDLAVSAFAILckhkQNLSDVTLTVAGGYDErlKENVEYLEELRSLaekegvsDRVNFITSCSTAERNELLSSC--LCV 300
Cdd:cd03794 231 GLETLLEAAERL----KRRPDIRFLFVGDGDE--KERLKELAKARGL-------DNVTFLGRVPKEEVPELLSAAdvGLV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 301 LYTPTDEHFGIVP---LEAMAAYKPVIACNSGGPVETVKNGVTGYLCEPT-PEDFSSAMARFIENPELANRMGAEARNHV 376
Cdd:cd03794 298 PLKDNPANRGSSPsklFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGdPEALADAILELLDDPELRRAMGENGRELA 377
|
410
....*....|...
gi 22330726 377 VESFSVKTFGQKL 389
Cdd:cd03794 378 EEKFSREKLADRL 390
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
10-396 |
1.37e-23 |
|
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: 100.44 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 10 NIAIIHPDLG------IGGAERLIVDAAVELASHGHKVHIFTSHHDKSRCfeeTLsgifqVTVYGSFLPRHIFYRLHAVC 83
Cdd:cd03802 1 RIAQVSPPRGpvppgkYGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSA---PL-----VAVIPRALRLDPIPQESKLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 84 aylrCLFVALCVLLGWSSFDVVLadqVSVVVPLLKLKRSSKVVFYC--HFPDLLlakhtTTLRRMYRKPidfieeqttgm 161
Cdd:cd03802 73 ----ELLEALEVQLRASDFDVIH---NHSYDWLPPFAPLIGTPFVTtlHGPSIP-----PSLAIYAAEP----------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 162 admilvNSNFTASTFANtfKRLNAQGSRPAVLYPAVNIDQFIEPHTYKLNFLSINRFERKKNIDLAVsAFAILCKHKqnl 241
Cdd:cd03802 130 ------PVNYVSISDAQ--RAATPPIDYLTVVHNGLDPADYRFQPDPEDYLAFLGRIAPEKGLEDAI-RVARRAGLP--- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 242 sdvtLTVAGGYDERLKEnvEYLEELRslaekegVSDRVNFITSCSTAERNELLSSCLCVLYTPT-DEHFGIVPLEAMAAY 320
Cdd:cd03802 198 ----LKIAGKVRDEDYF--YYLQEPL-------PGPRIEFIGEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACG 264
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22330726 321 KPVIACNSGGPVETVKNGVTGYLCEPTpedfsSAMARFIENPELANRmgAEARNHVVESFSVKTFGQKLNQYLVDV 396
Cdd:cd03802 265 TPVIAYRRGGLPEVIQHGETGFLVDSV-----EEMAEAIANIDRIDR--AACRRYAEDRFSAARMADRYEALYRKV 333
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
16-381 |
4.42e-23 |
|
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: 98.97 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 16 PDLGIGGAERLIVDAAVELASHGHKVHIFTSHHDKSRCFEETLSGIFQVTVYGSFLPRHIFYR-----------LHAvca 84
Cdd:cd03819 6 PALEIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGIGLPGLKVPLLRALLGNVRLarlirreridlIHA--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 85 ylRCLFVALCVLLGWSSFDVVLADQVSVVVPLlklkrsskvvfYCHFPDLLLAKHTTTLRRmyrkpidfieeqttgmadm 164
Cdd:cd03819 83 --HSRAPAWLGWLASRLTGVPLVTTVHGSYLA-----------TYHPKDFALAVRARGDRV------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 165 ILVnSNFTASTfanTFKRLNAQGSRPAVLYPAVNIDQFIEPHTYKLN-----------FLSINRFERKKNIDLAVSAFAI 233
Cdd:cd03819 131 IAV-SELVRDH---LIEALGVDPERIRVIPNGVDTDRFPPEAEAEERaqlglpegkpvVGYVGRLSPEKGWLLLVDAAAE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 234 LCKHKqnlsDVTLTVAGGYDERlkenveylEELRSLAEKEGVSDRVNFITSCSTAERneLLSSCLCVLYTPTDEHFGIVP 313
Cdd:cd03819 207 LKDEP----DFRLLVAGDGPER--------DEIRRLVERLGLRDRVTFTGFREDVPA--ALAASDVVVLPSLHEEFGRVA 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22330726 314 LEAMAAYKPVIACNSGGPVETVKNGVTGYLCEP-TPEDFSSAMARFIENPELANRMGAEARN--HVVESFS 381
Cdd:cd03819 273 LEAMACGTPVVATDVGGAREIVVHGRTGLLVPPgDAEALADAIRAAKLLPEAREKLQAAAALteAVRELLL 343
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
33-374 |
6.78e-22 |
|
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: 96.19 E-value: 6.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 33 ELASHGHKVHIFTSHHDKSRCFEEtlsgifqvtVYGSFLPRHIFYRLHAVCAYLRCLFVALCVLLGWSsFDVVLA-DQVS 111
Cdd:cd03817 26 ALEKRGHEVYVITPSDPGAEDEEE---------VVRYRSFSIPIRKYHRQHIPFPFKKAVIDRIKELG-PDIIHThTPFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 112 VVVPLLKLKRSSKV-------------VFYCHFPDLLL-AKHTTTLRRMYRKpidfieeqttgmADMILVNSNFTAstfa 177
Cdd:cd03817 96 LGKLGLRIARKLKIpivhtyhtmyedyLHYIPKGKLLVkAVVRKLVRRFYNH------------TDAVIAPSEKIK---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 178 NTFKRLNaqGSRPA-VLYPAVNIDQFIEPHTYKLN-----------FLSINRFERKKNIDLAVSAFAILcKHKQNlsdVT 245
Cdd:cd03817 160 DTLREYG--VKGPIeVIPNGIDLDKFEKPLNTEERrklglppdepiLLYVGRLAKEKNIDFLLRAFAEL-KKEPN---IK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 246 LTVAG-GYDErlkenveylEELRSLAEKEGVSDRVNFITSCSTAERNELLSSCLCVLYTPTDEHFGIVPLEAMAAYKPVI 324
Cdd:cd03817 234 LVIVGdGPER---------EELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVV 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 22330726 325 ACNSGGPVETVKNGVTGYLCEPTPEDFSSAMARFIENPELANRMGAEARN 374
Cdd:cd03817 305 AAKDPAASELVEDGENGFLFEPNDETLAEKLLHLRENLELLRKLSKNAEI 354
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
9-393 |
1.43e-21 |
|
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: 95.11 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 9 MNIAII-HPdlGIGGAERLIVDAAVELASHGHKVHIFTS--------HHDKSRC----------FEE-----TL-SGIFQ 63
Cdd:cd04962 1 MKIGIVcYP--SYGGSGVVATELGLELAERGHEVHFISSaipfrlnlYSGNIFFhevevpnyplFEYppytlALaSKIVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 64 VTVYGSFLPRHIFYRL-HAVCAYL------RCLFVaLCVLLGwssFDVVLADQVSVVVPLLKL--KRSSKVVFYCHFpdl 134
Cdd:cd04962 79 VAKEHKLDVLHAHYAIpHASCAYLareilgEKIPI-VTTLHG---TDITLVGYDPSLQPAVRFsiNKSDRVTAVSSS--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 135 lLAKHTttlRRMY--RKPIDFIEeqttgmadmilvnsNFTAStfaNTFKRLNAQGSRPAVLYPAvniDQFIEPHtyklnf 212
Cdd:cd04962 152 -LRQET---YELFdvDKDIEVIH--------------NFIDE---DVFKRKPAGALKRRLLAPP---DEKVVIH------ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 213 lsINRFERKKNIDLAVSAFAILckhkQNLSDVTLTVAGGYDERlkenveylEELRSLAEKEGVSDRVNFITSCSTAErnE 292
Cdd:cd04962 202 --VSNFRPVKRIDDVVRVFARV----RRKIPAKLLLVGDGPER--------VPAEELARELGVEDRVLFLGKQDDVE--E 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 293 LLSSCLCVLYTPTDEHFGIVPLEAMAAYKPVIACNSGGPVETVKNGVTGYLCEPTP-EDFSSAMARFIENPELANRMGAE 371
Cdd:cd04962 266 LLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDvDAMAKSALSILEDDELYNRMGRA 345
|
410 420
....*....|....*....|..
gi 22330726 372 ARNHVVESFSVKtfgQKLNQYL 393
Cdd:cd04962 346 ARKRAAERFDPE---RIVPQYE 364
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
104-380 |
1.23e-20 |
|
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: 92.38 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 104 VVLADQVSVVVPLLKLKRSSKVVFYCHFpDLllakhTTTLRRMYRKPIDFIEeQTTGMADMILvnsnFTASTFAntfkrl 183
Cdd:cd03792 91 VVIHDPQPALLPKIKKKRDRKWIWRCHI-DI-----STPLTEPQPRVWDFLW-NYIEGYDLFV----FHPPEFV------ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 184 naqgsRPAVLYPAVNIDQFIEPHTYK---LN--------------------FLSINRFERKKNIDLAVSAFAILCKHKqn 240
Cdd:cd03792 154 -----PPQVPPPKFYIPPSIDPLSGKnkdLSpadiryylekpfvidperpyILQVARFDPSKDPLGVIDAYKLFKRRA-- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 241 lSDVTLTVAGGYDERLKENVEYLEELRslaEKEGVSDRVNFITSC-STAERNELLSSCLCVLYTPTDEHFGIVPLEAMAA 319
Cdd:cd03792 227 -EEPQLVICGHGAVDDPEGSVVYEEVM---EYAGDDHDIHVLRLPpSDQEINALQRAATVVLQLSTREGFGLTVSEALWK 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22330726 320 YKPVIACNSGGPVETVKNGVTGYLCePTPEDFSSAMARFIENPELANRMGAEARNHVVESF 380
Cdd:cd03792 303 GKPVIATPAGGIPLQVIDGETGFLV-NSVEGAAVRILRLLTDPELRRKMGLAAREHVRDNF 362
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
115-368 |
1.81e-20 |
|
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: 91.66 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 115 PLLKLKRssKVVFYCH--FPDLLLAKHTTTLRRMYRKPIDFIEEQttgmADMILVNSNFTASTFAntfKRLNAQGSRPAV 192
Cdd:cd03809 96 PLLLKGC--PQVVTIHdlIPLRYPEFFPKRFRLYYRLLLPISLRR----ADAIITVSEATRDDII---KFYGVPPEKIVV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 193 LYPAVNIDQFIEPHTYKLN---------FLSINRFERKKNIDLAVSAFAILckhKQNLSDVTLTVAGGYDErlkenveYL 263
Cdd:cd03809 167 IPLGVDPSFFPPESAAVLIakyllpepyFLYVGTLEPRKNHERLLKAFALL---KKQGGDLKLVIVGGKGW-------ED 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 264 EELRSLAEKEGVSDRVNFITSCSTAERNELLSSCLCVLYTPTDEHFGIVPLEAMAAYKPVIACNsGGPVETVkNGVTGYL 343
Cdd:cd03809 237 EELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASN-ISVLPEV-AGDAALY 314
|
250 260
....*....|....*....|....*.
gi 22330726 344 CEPT-PEDFSSAMARFIENPELANRM 368
Cdd:cd03809 315 FDPLdPESIADAILRLLEDPSLREEL 340
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
10-376 |
2.58e-20 |
|
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: 91.24 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 10 NIAII---HPDLGIGGAERLIVDAAVELASHGHKVHIFTSHhdkSRCFEETLSGIFQVTVYGSFLPRH---IFYRLHAVC 83
Cdd:cd03823 1 KILLVnslYPPQRVGGAEISVHDLAEALVAEGHEVAVLTAG---VGPPGQATVARSVVRYRRAPDETLplaLKRRGYELF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 84 AY----LRCLFVALCVLLgwsSFDVVLADQVSV----VVPLLKlKRSSKVVFYCHFPDLLLAKHTttlrrMYRKPIdfie 155
Cdd:cd03823 78 ETynpgLRRLLARLLEDF---RPDVVHTHNLSGlgasLLDAAR-DLGIPVVHTLHDYWLLCPRQF-----LFKKGG---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 156 eqttgmaDMILVNSNFTastfANTFKRLNAQGSRPAVLYPAVNID----QFIEPHTYKLNFLSINRFERKKNIDLAVSAF 231
Cdd:cd03823 145 -------DAVLAPSRFT----ANLHEANGLFSARISVIPNAVEPDlappPRRRPGTERLRFGYIGRLTEEKGIDLLVEAF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 232 AiLCKHKqnlsDVTLTVAGGYDErlkenveyLEELRSLAEkegvsDRVNFITSCSTAERNELLSScLCVLYTPT--DEHF 309
Cdd:cd03823 214 K-RLPRE----DIELVIAGHGPL--------SDERQIEGG-----RRIAFLGRVPTDDIKDFYEK-IDVLVVPSiwPEPF 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22330726 310 GIVPLEAMAAYKPVIACNSGGPVETVKNGVTGYLCEPT-PEDFSSAMARFIENPELANRMGAEARNHV 376
Cdd:cd03823 275 GLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGdAEDLAAAMRRLLTDPALLERLRAGAEPPR 342
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
212-361 |
6.54e-20 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 85.26 E-value: 6.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 212 FLSINRF-ERKKNIDLAVSAFAILCKHKQnlsDVTLTVAGGYDERlkenveyleELRSLAEkeGVSDRVNFITScsTAER 290
Cdd:pfam13692 4 ILFVGRLhPNVKGVDYLLEAVPLLRKRDN---DVRLVIVGDGPEE---------ELEELAA--GLEDRVIFTGF--VEDL 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22330726 291 NELLSSCLCVLYTPTDEHFGIVPLEAMAAYKPVIACNSGGPVETVkNGVTGYLCEP-TPEDFSSAMARFIEN 361
Cdd:pfam13692 68 AELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPgDPEALAEAILRLLED 138
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
15-382 |
4.08e-19 |
|
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: 87.71 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 15 HPDlgIGGAERLIVDAAVELASHGHKVHIFTSHHDKSRCFEETLSgifqvtvygsflprHIFYRLHAVCAYLRCLFvalc 94
Cdd:cd03795 10 YPD--IGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENG--------------IRIHRVKSFLNVASTPF---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 95 vllgwsSFdvvladqvSVVVPLLKLKRSSKVVFYcHFP----DLLLAK-----------HTTTLR-RMYRKPIDFIEEQT 158
Cdd:cd03795 70 ------SP--------SYIKRFKKLAKEYDIIHY-HFPnplaDLLLFFsgakkpvvvhwHSDIVKqKKLLKLYKPLMTRF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 159 TGMADMILVNSN--FTASTFANTFKR--------LNAQGsrpavlYPAVNIDQFIEPHTYKLN--FLSINRFERKKNIDL 226
Cdd:cd03795 135 LRRADRIIATSPnyVETSPTLREFKNkvrviplgIDKNV------YNIPRVDFENIKREKKGKkiFLFIGRLVYYKGLDY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 227 AVSAFAILckhkqnlsDVTLTVAGGYDERlkenveylEELRSLAEKeGVSDRVNFITSCSTAERNELLSSCLCVL---YT 303
Cdd:cd03795 209 LIEAAQYL--------NYPIVIGGEGPLK--------PDLEAQIEL-NLLDNVKFLGRVDDEEKVIYLHLCDVFVfpsVL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 304 PTdEHFGIVPLEAMAAYKPVIACN-SGGPVETVKNGVTGYLCEPT-PEDFSSAMARFIENPELANRMGAEARNHVVESFS 381
Cdd:cd03795 272 RS-EAFGIVLLEAMMCGKPVISTNiGTGVPYVNNNGETGLVVPPKdPDALAEAIDKLLSDEELRESYGENAKKRFEELFT 350
|
.
gi 22330726 382 V 382
Cdd:cd03795 351 A 351
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
162-373 |
3.69e-17 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 82.86 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 162 ADMILVNSNFTASTFANTFKrlnaQGSRPAVLYPAVNIDQF----IEPHTYKLNFLSINRFERKKNIDLAVSAFAILckh 237
Cdd:PLN02949 221 AHLAMVNSSWTKSHIEALWR----IPERIKRVYPPCDTSGLqalpLERSEDPPYIISVAQFRPEKAHALQLEAFALA--- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 238 KQNLSDVT----LTVAGGYdeRLKENVEYLEELRSLAEKEGVSDRVNFITSCSTAERNELLSSCLCVLYTPTDEHFGIVP 313
Cdd:PLN02949 294 LEKLDADVprpkLQFVGSC--RNKEDEERLQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGGAVAGLHSMIDEHFGISV 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22330726 314 LEAMAAYKPVIACNSGGP----VETVKNGVTGYLCEpTPEDFSSAMARFIENPELAN-RMGAEAR 373
Cdd:PLN02949 372 VEYMAAGAVPIAHNSAGPkmdiVLDEDGQQTGFLAT-TVEEYADAILEVLRMRETERlEIAAAAR 435
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
21-391 |
3.98e-17 |
|
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: 82.03 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 21 GGAERLIVDAAVELASHGHKVHIFTSHhDKSRCFEETLSGIFQVTVYGsflprhiFYRLHAVCA----YLRCLFVALCVL 96
Cdd:cd03821 14 GGPVKVVLRLAAALAALGHEVTIVSTG-DGYESLVVEENGRYIPPQDG-------FASIPLLRQgagrTDFSPGLPNWLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 97 LGWSSFDVV----LADQVSVVVplLKLKRSSKVVfYCHFP----DLLLAKHTTTLRRMYRKpidFIEEQTTGMADMIlvn 168
Cdd:cd03821 86 RNLREYDVVhihgVWTYTSLAA--CKLARRRGIP-YVVSPhgmlDPWALQQKHWKKRIALH---LIERRNLNNAALV--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 169 sNFTASTFANTFKRLNAQGsRPAVLYPAVNIDQFIEPH--TYKLN---------FLSinRFERKKNIDLAVSAFAILCKH 237
Cdd:cd03821 157 -HFTSEQEADELRRFGLEP-PIAVIPNGVDIPEFDPGLrdRRKHNgledrriilFLG--RIHPKKGLDLLIRAARKLAEQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 238 KQnlsDVTLTVAGgYDERlkenvEYLEELRSLAEKeGVSDRVNFITSCSTAERNELLSSCLCVLYTPTDEHFGIVPLEAM 317
Cdd:cd03821 233 GR---DWHLVIAG-PDDG-----AYPAFLQLQSSL-GLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEAL 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22330726 318 AAYKPV-IACNSGGPVETVKNGvtGYLCEPTPEDFSSAMARFIENPELANRMGAEARN--HVVESFSVKTFGQKLNQ 391
Cdd:cd03821 303 ACGLPVvITDKCGLSELVEAGC--GVVVDPNVSSLAEALAEALRDPADRKRLGEMARRarQVEENFSWEAVAGQLGE 377
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
211-344 |
2.39e-15 |
|
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: 74.75 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 211 NFLSINRFERKKNIDLAVSAFAILckhKQNLSDVTLTVAGGYDERLKENVEyleelrsLAEKEGVSDRVNFITSCSTAER 290
Cdd:cd01635 112 DKVSVGRLVPEKGIDLLLEALALL---KARLPDLVLVLVGGGGEREEEEAL-------AAALGLLERVVIIGGLVDDEVL 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 22330726 291 NELLSSCLCVLYTPTDEHFGIVPLEAMAAYKPVIACNSGGPVETVKNGVTGYLC 344
Cdd:cd01635 182 ELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
11-378 |
2.41e-15 |
|
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: 76.56 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 11 IAII----HPDlgIGGAERLIVDAAVELASHGHKVHIFTSHHdksrcFEETLSGIFQVTVYGSF-LPRHIFYRLHAVcay 85
Cdd:cd03814 2 IALVtdtyHPQ--VNGVVRTLERLVDHLRRRGHEVRVVAPGP-----FDEAESAEGRVVSVPSFpLPFYPEYRLALP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 86 lrcLFVALCVLLGWSSFDVV-LADQVSVVVPLLKLKRSSK--VVFYCH----------FPDLLLAKHTTTLRRMYRkpid 152
Cdd:cd03814 72 ---LPRRVRRLIKEFQPDIIhIATPGPLGLAALRAARRLGlpVVTSYHtdfpeylsyyTLGPLSWLAWAYLRWFHN---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 153 fieeqttgMADMILVNSNFTAstfantfKRLNAQGSRPAVLYP-AVNIDQF-------------IEPHTYKLNFLSinRF 218
Cdd:cd03814 145 --------PFDTTLVPSPSIA-------RELEGHGFERVRLWPrGVDTELFhpsrrdaalrrrlGPPGRPLLLYVG--RL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 219 ERKKNIDLAVSAFAILCKHKqnlsDVTLTVAGGYDERlkenvEYLEElrslaekegVSDRVNFITSCSTAERNELLSSCL 298
Cdd:cd03814 208 APEKNLEALLDADLPLAASP----PVRLVVVGDGPAR-----AELEA---------RGPDVIFTGFLTGEELARAYASAD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 299 CVLYTPTDEHFGIVPLEAMAAYKPVIACNSGGPVETVKNGVTGYLCEP-TPEDFSSAMARFIENPELANRMGAEARNHVV 377
Cdd:cd03814 270 VFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPgDAAAFAAALRALLEDPELRRRMAARARAEAE 349
|
.
gi 22330726 378 E 378
Cdd:cd03814 350 R 350
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
217-381 |
1.68e-14 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 74.44 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 217 RFERKKNIDLAVSAFAILCKHKQNLSdvtLTVAGGYDERLK-ENVEYLEELRSLAEKEGvsDRVNFITSCSTAERNELLS 295
Cdd:PRK15484 201 RISPDKGILLLMQAFEKLATAHSNLK---LVVVGDPTASSKgEKAAYQKKVLEAAKRIG--DRCIMLGGQPPEKMHNYYP 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 296 -SCLCVLYTPTDEHFGIVPLEAMAAYKPVIACNSGGPVETVKNGVTGY-LCEP-TPEDFSSAMARFIENPELANrMGAEA 372
Cdd:PRK15484 276 lADLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYhLAEPmTSDSIISDINRTLADPELTQ-IAEQA 354
|
....*....
gi 22330726 373 RNHVVESFS 381
Cdd:PRK15484 355 KDFVFSKYS 363
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
10-381 |
3.27e-14 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 73.51 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 10 NIAIIHPDLGIGGAERLIVDAAVELASHGHKVHIFTSHHDksrcfeetlsgifqvtvyGSFLPRHIFYRLHAVCaylrcl 89
Cdd:cd03807 1 KVAHVITGLNVGGAETMLLRLLEHMDKSRFEHVVISLTGD------------------GVLGEELLAAGVPVVC------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 90 fvalcvlLGWSSFDVVLadqvsVVVPLLKLKRSSKV-VFYCHFPDLLL-----------AKHTTTLRRM---YRKP--ID 152
Cdd:cd03807 57 -------LGLSSGKDPG-----VLLRLAKLIRKRNPdVVHTWMYHADLigglaaklaggVKVIWSVRSSnipQRLTrlVR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 153 FIEEQTTGMADMILVNSNFTAstfantfKRLNAQGSRPA---VLYPAVNIDQF-IEPHTYKLNFLSIN------------ 216
Cdd:cd03807 125 KLCLLLSKFSPATVANSSAVA-------EFHQEQGYAKNkivVIYNGIDLFKLsPDDASRARARRRLGlaedrrvigivg 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 217 RFERKKNIDLAVSAFAILCKHKqnlSDVTLTVAGGYDERlkenveylEELRSLAEKEGVSDRVNFitscsTAERN---EL 293
Cdd:cd03807 198 RLHPVKDHSDLLRAAALLVETH---PDLRLLLVGRGPER--------PNLERLLLELGLEDRVHL-----LGERSdvpAL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 294 LSS----CLCVLYtptdEHFGIVPLEAMAAYKPVIACNSGGPVETVKNGvTGYLCEP-TPEDFSSAMARFIENPELANRM 368
Cdd:cd03807 262 LPAmdifVLSSRT----EGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPAgDPQALADAIRALLEDPEKRARL 336
|
410
....*....|...
gi 22330726 369 GAEARNHVVESFS 381
Cdd:cd03807 337 GRAARERIANEFS 349
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
181-392 |
6.37e-14 |
|
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: 73.14 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 181 KRLNAQGSRPAVLYPAVNIDQFIEPHTYK-----LNFLSINRFERKKNIDLAVSAFAILckhKQNLSDVTLTVAGGYDEr 255
Cdd:cd03813 260 IRLGADPDKTRVIPNGIDIQRFAPAREERpekepPVVGLVGRVVPIKDVKTFIRAFKLV---RRAMPDAEGWLIGPEDE- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 256 lkeNVEYLEELRSLAEKEGVSDRVNFItscSTAERNELLSSCLCVLYTPTDEHFGIVPLEAMAAYKPVIACNSGGPVETV 335
Cdd:cd03813 336 ---DPEYAQECKRLVASLGLENKVKFL---GFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELI 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22330726 336 -----KNGVTGYLCEPT-PEDFSSAMARFIENPELANRMGAEARNHVVESFSVKTFgqkLNQY 392
Cdd:cd03813 410 ygaddALGQAGLVVPPAdPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGM---IDSY 469
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
21-200 |
2.66e-13 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 67.56 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 21 GGAERLIVDAAVELASHGHKVHIFTSHHDKSrcFEETLSGIFQVTVYGSFLPRHIFYRLHAVCAYLRclfvalcvLLGWS 100
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGP--LAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRR--------LLRRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 101 SFDVVLADQ---VSVVVPLLKLKRSSKVVFYCHFPDLLLAKHtTTLRRMYRKPIDFIEEQTTGMADMILVNSNFTASTFA 177
Cdd:pfam13439 71 RPDVVHAHSpfpLGLAALAARLRLGIPLVVTYHGLFPDYKRL-GARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELR 149
|
170 180
....*....|....*....|...
gi 22330726 178 ntfKRLNAQGSRPAVLYPAVNID 200
Cdd:pfam13439 150 ---RLYGVPPEKIRVIPNGVDLE 169
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
212-392 |
3.07e-11 |
|
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: 64.40 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 212 FLSINRFERKKNIDLAVSAFAILckhKQNLSDVTLTVAGGYDERlkenveylEELRSLAEKEGvsdRVNFITSCSTAERN 291
Cdd:cd05844 192 ILFVGRLVEKKGCDVLIEAFRRL---AARHPTARLVIAGDGPLR--------PALQALAAALG---RVRFLGALPHAEVQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 292 ELL--SSCLCV-LYTPTD---EHFGIVPLEAMAAYKPVIACNSGGPVETVKNGVTGYLC-EPTPEDFSSAMARFIENPEL 364
Cdd:cd05844 258 DWMrrAEIFCLpSVTAASgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVpEGDVDALADALQALLADRAL 337
|
170 180
....*....|....*....|....*...
gi 22330726 365 ANRMGAEARNHVVESFSVKTFGQKLNQY 392
Cdd:cd05844 338 ADRMGGAARAFVCEQFDIRVQTAKLEAI 365
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
161-388 |
1.10e-10 |
|
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: 62.73 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 161 MADMILVNSNFTastfantfkrlnaqGSRPAVLYPAVNIDQF-------------IEPHTYKLNFLSINRFERKKNIDLA 227
Cdd:cd03825 148 LADMVRRSPLLK--------------GLPVVVIPNGIDTEIFapvdkakarkrlgIPQDKKVILFGAESVTKPRKGFDEL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 228 VSAFAILCKHKqnlsDVTLTVAGGYDERLKE------NVEYLEELRSLAEkegvsdrvnfitscstaerneLLSSC-LCV 300
Cdd:cd03825 214 IEALKLLATKD----DLLLVVFGKNDPQIVIlpfdiiSLGYIDDDEQLVD---------------------IYSAAdLFV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 301 LytPT-DEHFGIVPLEAMAAYKPVIACNSGGPVETVKNGVTGYLCEP-TPEDFSSAMARFIENPELANRMGAEARNHVVE 378
Cdd:cd03825 269 H--PSlADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPgDVQALAEAIEWLLANPKERESLGERARALAEN 346
|
250
....*....|
gi 22330726 379 SFSVKTFGQK 388
Cdd:cd03825 347 HFDQRVQAQR 356
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
10-388 |
1.91e-10 |
|
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: 61.69 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 10 NIAIIHPDLGIGGAERLIVDAAVELASHGHKVHIFTshhdksrcfeetLSGIFQVTvygSFLPRHIFYRLH---AVCAYL 86
Cdd:cd04951 1 KILYVITGLGLGGAEKQTVLLADQMFIRGHDVNIVY------------LTGEVEVK---PLNNNIIIYNLGmdkNPRSLL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 87 RCLFVALCVLLGWSSfDVVLADQV--SVVVPLLKlkrsskvvFYCHFPDLLLAKHTTTLR---RM--YRKpIDFIEEQTT 159
Cdd:cd04951 66 KALLKLKKIISAFKP-DVVHSHMFhaNIFARFLR--------MLYPIPLLICTAHNKNEGgriRMfiYRL-TDFLCDITT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 160 gmadmilvNSNFTASTFANTFKRLNAQGSRPavLYPAVNIDQFIEPHTYKLN-------------FLSINRFERKKNIDL 226
Cdd:cd04951 136 --------NVSREALDEFIAKKAFSKNKSVP--VYNGIDLNKFKKDINVRLKirnklnlkndefvILNVGRLTEAKDYPN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 227 AVSAFAILCKHKqnlSDVTLTVAGgyDERLKENVE-YLEELrslaekeGVSDRVNFITSCSTAErnELLSSCLCVLYTPT 305
Cdd:cd04951 206 LLLAISELILSK---NDFKLLIAG--DGPLRNELErLICNL-------NLVDRVILLGQISNIS--EYYNAADLFVLSSE 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 306 DEHFGIVPLEAMAAYKPVIACNSGGPVETVKNgvTGYLCePT--PEDFSSAMARFIENPELANRMGAEARNHVVESFSVK 383
Cdd:cd04951 272 WEGFGLVVAEAMACERPVVATDAGGVAEVVGD--HNYVV-PVsdPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFSIN 348
|
....*
gi 22330726 384 TFGQK 388
Cdd:cd04951 349 TIVNE 353
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
214-389 |
8.07e-10 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 60.76 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 214 SINRFERKKNIDLAVSAFAilcKHKQNLSDVTLTVAGGYDERLK----ENVEYLEELRSLAEKEGVSDRVNFITSCSTAE 289
Cdd:PLN00142 578 SMARLDRVKNLTGLVEWYG---KNKRLRELVNLVVVGGFIDPSKskdrEEIAEIKKMHSLIEKYNLKGQFRWIAAQTNRV 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 290 RNELLSSCLC---------VLYtptdEHFGIVPLEAMAAYKPVIACNSGGPVETVKNGVTGYLCEP-TPEDFSSAMARFI 359
Cdd:PLN00142 655 RNGELYRYIAdtkgafvqpALY----EAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPyHGDEAANKIADFF 730
|
170 180 190
....*....|....*....|....*....|....
gi 22330726 360 E----NPELANRMGAEARNHVVESFSVKTFGQKL 389
Cdd:PLN00142 731 EkckeDPSYWNKISDAGLQRIYECYTWKIYAERL 764
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
314-382 |
9.74e-10 |
|
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: 59.74 E-value: 9.74e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 314 LEAMAAYKPVIACNSGGPVETVKNGVTGYLCEPT-PEDFSSAMARFIENPELANRMGAEARNHVVESFSV 382
Cdd:TIGR03088 290 LEAMASGLPVIATAVGGNPELVQHGVTGALVPPGdAVALARALQPYVSDPAARRAHGAAGRARAEQQFSI 359
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
266-382 |
5.33e-09 |
|
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).
Pssm-ID: 340845 [Multi-domain] Cd Length: 396 Bit Score: 57.37 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 266 LRSLAEKEGVSDRVNFITSCSTAERNELL--SSCLCVLYTPTDEHFGIvpLEAMAAYKPVIACNSGGPVETVKNGVTGYL 343
Cdd:cd03818 270 QKMLAELGVDLERVHFVGKVPYDQYVRLLqlSDAHVYLTYPFVLSWSL--LEAMACGCPVIGSDTAPVREVIRDGRNGLL 347
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 22330726 344 CE-PTPEDFSSAMARFIENPELANRMGAEARNHVVESFSV 382
Cdd:cd03818 348 VDfFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSL 387
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
209-393 |
4.19e-08 |
|
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.
Pssm-ID: 340829 [Multi-domain] Cd Length: 350 Bit Score: 54.38 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 209 KLNFLSINRFERKKNIDLAVSAFAILckhKQNLSDVTLTVAGgyDERLKENveyleeLRSLAEKEGVSDRVNFITSCSTA 288
Cdd:cd03799 174 KIRILTVGRLTEKKGLEYAIEAVAKL---AQKYPNIEYQIIG--DGDLKEQ------LQQLIQELNIGDCVKLLGWKPQE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 289 ERNELLSSCLCVLYTPT-----DEHFGIVPL-EAMAAYKPVIACNSGGPVETVKNGVTGYLcepTPEDFSSAMA----RF 358
Cdd:cd03799 243 EIIEILDEADIFIAPSVtaadgDQDGPPNTLkEAMAMGLPVISTEHGGIPELVEDGVSGFL---VPERDAEAIAekltYL 319
|
170 180 190
....*....|....*....|....*....|....*
gi 22330726 359 IENPELANRMGAEARNHVVESFSVktfgQKLNQYL 393
Cdd:cd03799 320 IEHPAIWPEMGKAGRARVEEEYDI----NKLNDEL 350
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
300-376 |
1.20e-07 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 53.56 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 300 VLYTPTD-EHFGIVPLEAMAAYKPVIACNSGG-P--VETVKNGVTGYLCEPTP-EDFSSAMARFIENPELANRMGAEARN 374
Cdd:PLN02871 334 VFVMPSEsETLGFVVLEAMASGVPVVAARAGGiPdiIPPDQEGKTGFLYTPGDvDDCVEKLETLLADPELRERMGAAARE 413
|
..
gi 22330726 375 HV 376
Cdd:PLN02871 414 EV 415
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
187-381 |
2.68e-07 |
|
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: 51.92 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 187 GSRPAVLYPAVNIDQfiEPHTyklnFLSINRFERKKNIDLAVSAFAILckhKQNLSDVTLTVAGGYDERlkenveylEEL 266
Cdd:cd04949 144 GYVDQLDTAESNHER--KSNK----IITISRLAPEKQLDHLIEAVAKA---VKKVPEITLDIYGYGEER--------EKL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 267 RSLAEKEGVSDRVNFitSCSTAERNELLSSCLCVLYTPTDEHFGIVPLEAMAAYKPVIACNSG-GPVETVKNGVTGYLCE 345
Cdd:cd04949 207 KKLIEELHLEDNVFL--KGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIE 284
|
170 180 190
....*....|....*....|....*....|....*..
gi 22330726 346 P-TPEDFSSAMARFIENPELANRMGAEARNHvVESFS 381
Cdd:cd04949 285 KnNIDALADKIIELLNDPEKLQQFSEESYKI-AEKYS 320
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
21-196 |
2.06e-06 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 47.40 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 21 GGAERLIVDAAVELASHGHKVHIFTSHHDkSRCFEETLSGifqVTVYGSFLPRH--IFYRLHAVCAYLRclfvalcvLLG 98
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGP-PGRPELVGDG---VRVHRLPVPPRpsPLADLAALRRLRR--------LLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 99 WSSFDVVLAD--QVSVVVPLLKLKRSSKVVFYCHfpDLLLAKHTTTLRRMYRkpidFIEEQTTGMADMILVNSNFTASTF 176
Cdd:pfam13579 69 AERPDVVHAHspTAGLAARLARRRRGVPLVVTVH--GLALDYGSGWKRRLAR----ALERRLLRRADAVVVVSEAEAELL 142
|
170 180
....*....|....*....|
gi 22330726 177 AntfkRLNAQGSRPAVLYPA 196
Cdd:pfam13579 143 R----ALGVPAARVVVVPNG 158
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
19-355 |
4.92e-06 |
|
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: 48.39 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 19 GIGGAERLIVDAAVELASHGHKVHIFTsHHDKSRCFEETLSGIFQV---------------TVYGSF-LPRHIFYR---- 78
Cdd:cd03796 12 NLGGVETHIYQLSQCLIKRGHKVIVIT-HAYGNRVGVRYLTNGLKVyylpfkvfynqstlpTLFSTFpLLRNILIReriq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 79 -LHavcaylrclfvalcvllGWSSFDVvLADQVSVVVPLLKLKrsskVVFYCH----FPDLLlAKHTTTLRRMYRKPIDf 153
Cdd:cd03796 91 iVH-----------------GHQAFSS-LAHEALFHARTLGLK----TVFTDHslfgFADAS-SILTNKLLRFSLADID- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 154 ieeqttgmaDMILVnSNFTAStfaNTFKRLNAQGSRPAVLYPAVNIDQFI----EPHTYKLNFLSINRFERKKNIDLAVS 229
Cdd:cd03796 147 ---------HVICV-SHTSKE---NTVLRASLDPRIVSVIPNAVDSSDFTpdpsKPDPNKITIVVISRLVYRKGIDLLVG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 230 AFAILCKhkqNLSDVTLTVAGGYDERLKenveyLEELRslaEKEGVSDRVNFITSCSTAERNELLSSCLCVLYTPTDEHF 309
Cdd:cd03796 214 IIPRICK---KHPNVRFIIGGDGPKRIE-----LEEMR---EKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAF 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 22330726 310 GIVPLEAMAAYKPVIACNSGGPVETVKNGVTgYLCEPTPEDFSSAM 355
Cdd:cd03796 283 CIAIVEAASCGLLVVSTRVGGIPEVLPPDMI-LLAEPDPEDIVRKL 327
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
263-383 |
6.26e-06 |
|
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: 47.84 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 263 LEELRSLAEKEGVSDRVNFItscstaerNELLSSCLCVLYTPTDEHFGI-------VP---LEAMAAYKPVIACNSGGPV 332
Cdd:cd04946 269 KERLEKLAENKLENVKVNFT--------GEVSNKEVKQLYKENDVDVFVnvsesegIPvsiMEAISFGIPVIATNVGGTR 340
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 22330726 333 ETVKNGVTGYLC--EPTPEDFSSAMARFIENPELANRMGAEARNHVVESFSVK 383
Cdd:cd04946 341 EIVENETNGLLLdkDPTPNEIVSSIMKFYLDGGDYKTMKISARECWEERFNAE 393
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
192-366 |
5.82e-05 |
|
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: 44.97 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 192 VLYPAVNIDQFIEPHTY-----KLNFLS-------INRFERKKNIDLAVSAFAILckHKQNlSDVTLTVAGgyderlkeN 259
Cdd:cd03812 162 VIPNGIDIEKYKFNKEKrrkrrKLLILEdklvlghVGRFNEQKNHSFLIDIFEEL--KKKN-PNVKLVLVG--------E 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 260 VEYLEELRSLAEKEGVSDRVNFITSCSTAerNELLSScLCVLYTPTD-EHFGIVPLEAMAAYKPVIACNSGGPVETVKNG 338
Cdd:cd03812 231 GELKEKIKEKVKELGLEDKVIFLGFRNDV--SEILSA-MDVFLFPSLyEGLPLVAVEAQASGLPCLLSDTITKECDITNN 307
|
170 180
....*....|....*....|....*...
gi 22330726 339 VTGYLCEPTPEDFSSAMARFIENPELAN 366
Cdd:cd03812 308 VEFLPLNETPSTWAEKILKLIKRKRRIN 335
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
220-368 |
9.69e-05 |
|
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: 44.30 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 220 RKKNIDLAVSAFAILCKHKQnlsDVTLTVAGGYDERLKENVEYLEELRSLAEKeGVSDRVNFIT-SCSTAERNELLSSC- 297
Cdd:cd03822 198 PGKGLEILLEALPELKAEFP---DVRLVIAGELHPSLARYEGERYRKAAIEEL-GLQDHVDFHNnFLPEEEVPRYISAAd 273
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22330726 298 LCVL-YTPTDEHFGIVPLEAMAAYKPVIACNSGGPVETVKNGvTGYLCEP-TPEDFSSAMARFIENPELANRM 368
Cdd:cd03822 274 VVVLpYLNTEQSSSGTLSYAIACGKPVISTPLRHAEELLADG-RGVLVPFdDPSAIAEAILRLLEDDERRQAI 345
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
309-381 |
3.13e-04 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 39.51 E-value: 3.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22330726 309 FGIVPLEAMAAYKPVIACNSGGPVETVKNGVTGYLCEpTPEDFSSAMARFIENPELANRMGAEARNHVVESFS 381
Cdd:pfam13524 12 PNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR-DPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHT 83
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
188-360 |
2.67e-03 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 39.69 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 188 SRPAVLYPAVNIDQFIEP---HTYKLNFLSINR--FERKKNIDLAVSAFAilckhkQNLSDVTLTVAGGYDErlkenvey 262
Cdd:PRK09922 156 QRISVIYNPVEIKTIIIPppeRDKPAVFLYVGRlkFEGQKNVKELFDGLS------QTTGEWQLHIIGDGSD-------- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330726 263 LEELRSLAEKEGVSDRVNFI--TSCSTAERNELLSSCLCVLYTPTDEHFGIVPLEAMAAYKPVIA--CNSGgPVETVKNG 338
Cdd:PRK09922 222 FEKCKAYSRELGIEQRIIWHgwQSQPWEVVQQKIKNVSALLLTSKFEGFPMTLLEAMSYGIPCISsdCMSG-PRDIIKPG 300
|
170 180
....*....|....*....|...
gi 22330726 339 VTGYLCEP-TPEDFSSAMARFIE 360
Cdd:PRK09922 301 LNGELYTPgNIDEFVGKLNKVIS 323
|
|
| |
