|
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 ... |
10-395 |
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: 605.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 10 MNIAIIHPDLGIGGAERLVVDAAVELASRGHKVHIFTAHHDKNRCFEETIAGIFPVTVYGSFLPRHIFYRLHALCAYLRC 89
Cdd:cd03805 1 LRVAFLHPDLGIGGAERLVVDAALALQSRGHEVTIYTSHHDPSHCFEETKDGTLPVRVRGDWLPRSIFGRFHALCAYLRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 90 LFVAFCVLFL-WPSFDVILADQVSVVIPILKLKRSTKVVFYCHFPDLLLAQHSTFLRRIYRKPIDYLEEITTGMADSILV 168
Cdd:cd03805 81 LYLALYLLLFsGEKYDVFIVDQVSACVPLLKLFRPSKILFYCHFPDQLLAQRKSLLKRLYRKPFDWLEEFTTGMADQIVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 169 NSNFTASTFANTFKHLDAKGIRpaVLYPAVNVDQF-----------NEPTSTKPNFLSINRFERKKNIQLAISAFAMLYS 237
Cdd:cd03805 161 NSNFTAGVFKKTFPSLAKNPPE--VLYPCVDTDSFdstsedpdpgdLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 238 pnrvlKHQAITNASLTVAGGFDKRLKENVEYLEELKDLAEK-EGVSDKIKFVTSCSTDERNALLSECLCVLYTPENEHFG 316
Cdd:cd03805 239 -----KLPEFENVRLVIAGGYDPRVAENVEYLEELQRLAEElLNVEDQVLFLRSISDSQKEQLLSSALALLYTPSNEHFG 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1379604785 317 IVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLCSPTPQEFSSAMANLINDPQEAEKMGNEARRHVVESFSTKTFGTHL 395
Cdd:cd03805 314 IVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAERL 392
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
11-387 |
1.44e-49 |
|
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: 171.57 E-value: 1.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 11 NIAIIHPDL--GIGGAERLVVDAAVELASRGHKVHIFTaHHDKNRCFEETIAGIFPVTVYGSFLPRHIFYRLHALCAYLR 88
Cdd:cd03801 1 KILLLSPELppPVGGAERHVRELARALAARGHDVTVLT-PADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 89 clfvafcvlflWPSFDVILA--DQVSVVIPILKLKRSTKVVFYCH-----FPDLLLAQHSTFLRRIYRKpidyleeitTG 161
Cdd:cd03801 80 -----------LRKFDVVHAhgLLAALLAALLALLLGAPLVVTLHgaepgRLLLLLAAERRLLARAEAL---------LR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 162 MADSILVNSNFTASTFANTFKHLDAKgirPAVLYPAVNVDQFNEPTSTKPN-------FLSINRFERKKNIQLAISAFAM 234
Cdd:cd03801 140 RADAVIAVSEALRDELRALGGIPPEK---IVVIPNGVDLERFSPPLRRKLGippdrpvLLFVGRLSPRKGVDLLLEALAK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 235 LyspnrvlkHQAITNASLTVAGGfdkrlkeNVEYLEELKDLaeKEGVSDKIKFVTSCSTDERNALLSECLCVLYTPENEH 314
Cdd:cd03801 217 L--------LRRGPDVRLVIVGG-------DGPLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEG 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1379604785 315 FGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLCSPT-PQEFSSAMANLINDPQEAEKMGNEARRHVVESFS 387
Cdd:cd03801 280 FGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDdVEALADALLRLLADPELRARLGRAARERVAERFS 353
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
12-394 |
6.66e-39 |
|
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: 144.29 E-value: 6.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 12 IAIIHP--DLGiGGAERlVVDAAVE---LASRGHKVHIFTAHHD----------KNRcFEetIAGIFPVTVYgsFLPRHI 76
Cdd:cd03806 3 VGFFHPycNAG-GGGER-VLWCAVKatqKAYPNNICVIYTGDTDsspeeilekvESR-FN--IDLDSPRIVF--FLLKYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 77 FYRLHALCAYLRCLFVAFCVLFLwpSFDVILADQVSVVI---------PILKLKRSTKVVFYCHFP-------------- 133
Cdd:cd03806 76 KLVEAKTYPRFTLLGQALGSMIL--GFEALLKLVPDVFIdtmgypftyPLVRLLGGCPVVAYVHYPtistdmlnkvrsre 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 134 -----DLLLAQHS--TFLRRIYRKPIDYLEEITTGMADSILVNSNFTastfantFKHLDA---KGIRPAVLYPAVNVDQF 203
Cdd:cd03806 154 asynnDSTIARSSvlSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWT-------YNHIRQlwkRNIKPSIVYPPCDTEEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 204 NE----PTSTKPNFLSINRFERKKNIQLAISAFAMLYSPnrvLKHQAITNASLTVAGGfdKRLKENVEYLEELKDLAEKE 279
Cdd:cd03806 227 TKlpidEKTRENQILSIAQFRPEKNHPLQLRAFAELLKR---LPESIRSNPKLVLIGS--CRNEEDKERVEALKLLAKEL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 280 GVSDKIKFVTSCSTDERNALLSECLCVLYTPENEHFGIVPLEAMAAYKVVIACNSGGPVESI----KNGVTGFLCSpTPQ 355
Cdd:cd03806 302 ILEDSVEFVVDAPYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIvvpwDGGPTGFLAS-TPE 380
|
410 420 430
....*....|....*....|....*....|....*....
gi 1379604785 356 EFSSAMANLINDPQEAEKMGNEARRHVVESFSTKTFGTH 394
Cdd:cd03806 381 EYAEAIEKILTLSEEERLQRREAARSSAERFSDEEFERD 419
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
11-391 |
1.50e-34 |
|
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: 130.94 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 11 NIAIIHPDLGIGGAERLVVDAAVELASRGHKVHIFTahHDKNRCFEETIAGIFPVTVYGSFLPRHIFYRLHALCAYLRcl 90
Cdd:cd03811 1 KILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVL--LRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 91 fvafcVLFLWPSFDVILA-DQVSVVIPILKLKRSTKVVFYCHFPdlllAQHSTFLRRIYRKPIDYLEeittgMADSILVN 169
Cdd:cd03811 77 -----RILKRAKPDVVISfLGFATYIVAKLAAARSKVIAWIHSS----LSKLYYLKKKLLLKLKLYK-----KADKIVCV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 170 SNFTASTFANTFKHLDAKgIRpaVLYPAVNVDQFNEPT--------STKPNFLSINRFERKKNIQLAISAFAMLyspnrv 241
Cdd:cd03811 143 SKGIKEDLIRLGPSPPEK-IE--VIYNPIDIDRIRALAkepilnepEDGPVILAVGRLDPQKGHDLLIEAFAKL------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 242 lkHQAITNASLTVAGGFDKRlkenveylEELKDLAEKEGVSDKIKFVTSCStderN--ALLSECLCVLYTPENEHFGIVP 319
Cdd:cd03811 214 --RKKYPDVKLVILGDGPLR--------EELEKLAKELGLAERVIFLGFQS----NpyPYLKKADLFVLSSRYEGFPNVL 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1379604785 320 LEAMAAYKVVIACNSGGPVESIKNGVTGFLCSPTPQEFSSAMANLINDPQEAEKMGNEARRHVVESFSTKTF 391
Cdd:cd03811 280 LEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEAVFREYTI 351
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
209-381 |
3.58e-33 |
|
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: 122.00 E-value: 3.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 209 TKPNFLSINRFERKKNIQLAISAFAMLYSPNRVLKhqaitnasLTVAGgfdkrlkeNVEYLEELKDLAEKEGVSDKIKFV 288
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLK--------LVIAG--------DGEEEKRLKKLAEKLGLGDNVIFL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 289 TSCSTDERNALLSECLCVLYTPENEHFGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLCSPT-PQEFSSAMANLIND 367
Cdd:pfam00534 65 GFVSDEDLPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNnAEALAEAIDKLLED 144
|
170
....*....|....
gi 1379604785 368 PQEAEKMGNEARRH 381
Cdd:pfam00534 145 EELRERLGENARKR 158
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
22-387 |
3.70e-30 |
|
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: 120.04 E-value: 3.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 22 GGAERLVVDAAVELASRGHKVHIFTAHHDKNRcfeetiagifPVTVYGS--FLPRHI------FYRLHALCAYLrCLFVA 93
Cdd:cd03800 21 GGQNVYVLELARALAELGYQVDIFTRRISPAD----------PEVVEIApgARVIRVpagppeYLPKEELWPYL-EEFAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 94 FCVLFL-----WPsfDVI-----LADQVSvvipiLKLKRSTKVVFyCHFPdlllaqHStfLRRIYRK--PIDYLEEITTG 161
Cdd:cd03800 90 GLLRFIareggRY--DLIhshywDSGLVG-----ALLARRLGVPL-VHTF------HS--LGRVKYRhlGAQDTYHPSLR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 162 -MADSILV-NSNF-TASTF---ANTFKHLDAKGIRPAVLYPAVNVDQFNEPTST------------KPNFLSINRFERKK 223
Cdd:cd03800 154 iTAEEQILeAADRvIASTPqeaDELISLYGADPSRINVVPPGVDLERFFPVDRAearrarlllppdKPVVLALGRLDPRK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 224 NIQLAISAFAmlYSPNRVlkhqaiTNASLTVAGGFDKRLKENVEylEELKDLAEKEGVSDKIKFVTSCSTDERNALLSEC 303
Cdd:cd03800 234 GIDTLVRAFA--QLPELR------ELANLVLVGGPSDDPLSMDR--EELAELAEELGLIDRVRFPGRVSRDDLPELYRAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 304 -LCVLyTPENEHFGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLCSPT-PQEFSSAMANLINDPQEAEKMGNEARRH 381
Cdd:cd03800 304 dVFVV-PSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHdPEALAAALRRLLDDPALWQRLSRAGLER 382
|
....*.
gi 1379604785 382 VVESFS 387
Cdd:cd03800 383 ARAHYT 388
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
21-387 |
4.39e-26 |
|
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: 107.68 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 21 IGGAERLVVDAAVELASRGHKVHIFTAHHDKNRCFEETIaGIFPVTVYGSFLPRHIFYRLHALcAYLRCLFVAFcvlflw 100
Cdd:cd03808 9 DGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKEL-GVKVIDIPILRRGINPLKDLKAL-FKLYKLLKKE------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 101 pSFDVILAdqVS---VVIPIL--KLKRSTKVVFYCH-----FPDlllaqhSTFLRRIYRKpidyLEEITTGMADSILVNS 170
Cdd:cd03808 81 -KPDIVHC--HTpkpGILGRLaaRLAGVPKVIYTVHglgfvFTE------GKLLRLLYLL----LEKLALLFTDKVIFVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 171 NFTASTFANTFKHLDAKgirpAVLYP--AVNVDQF----NEPTSTKPNFLSINRFERKKNIQLAISAFamlyspnRVLKH 244
Cdd:cd03808 148 EDDRDLAIKKGIIKKKK----TVLIPgsGVDLDRFqyspESLPSEKVVFLFVARLLKDKGIDELIEAA-------KILKK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 245 QAItNASLTVAGGFDKRlkenveylEELKDLAEKEGVSDKIKFVTSCStdERNALLSECLCVLYTPENEHFGIVPLEAMA 324
Cdd:cd03808 217 KGP-NVRFLLVGDGELE--------NPSEILIEKLGLEGRIEFLGFRS--DVPELLAESDVFVLPSYREGLPRSLLEAMA 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1379604785 325 AYKVVIACNSGGPVESIKNGVTGFLCSP-TPQEFSSAMANLINDPQEAEKMGNEARRHVVESFS 387
Cdd:cd03808 286 AGRPVITTDVPGCRELVIDGVNGFLVPPgDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFD 349
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
12-390 |
1.12e-24 |
|
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: 103.86 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 12 IAIIHPDLG-IGGAERLVVDAAVELASRGHKVHIFTAHHDKNRCFEE-----TIAGIFPVTVYGSFLPRHIFYRLHALCA 85
Cdd:cd03820 2 IAIVIPSISnAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYElddniKIKNLGDRKYSHFKLLLKYFKKVRRLRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 86 YLRCLfvafcvlflwpSFDVILADQVSVVIPILKLKRSTKVVFYCHFPdlLLAQHSTFLRRIYRKpidyleeITTGMADS 165
Cdd:cd03820 82 YLKNN-----------KPDVVISFRTSLLTFLALIGLKSKLIVWEHNN--YEAYNKGLRRLLLRR-------LLYKRADK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 166 ILVNSNFTAstfantFKHLDAKGIRPAVLYPAVNVDQFNepTSTKPN---FLSINRFERKKNIQLAISAFAmlyspNRVL 242
Cdd:cd03820 142 IVVLTEADK------LKKYKQPNSNVVVIPNPLSFPSEE--PSTNLKskrILAVGRLTYQKGFDLLIEAWA-----LIAK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 243 KHQAITnasLTVAGGFDKRlkenveylEELKDLAEKEGVSDKIKFvtSCSTDERNALLSEC-LCVLyTPENEHFGIVPLE 321
Cdd:cd03820 209 KHPDWK---LRIYGDGPER--------EELEKLIDKLGLEDRVKL--LGPTKNIAEEYANSsIFVL-SSRYEGFPMVLLE 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1379604785 322 AMAAYKVVIA--CNSgGPVESIKNGVTGFLCSP-TPQEFSSAMANLINDPQEAEKMGNEArRHVVESFSTKT 390
Cdd:cd03820 275 AMAYGLPIISfdCPT-GPSEIIEDGENGLLVPNgDVDALAEALLRLMEDEELRKKMGKNA-RKNAERFSIEK 344
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
297-404 |
1.42e-22 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 91.98 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 297 NALLSECLCVLYTPENEHFGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLCSP-TPQEFSSAMANLINDPQEAEKMG 375
Cdd:COG0438 15 EALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPgDPEALAEAILRLLEDPELRRRLG 94
|
90 100
....*....|....*....|....*....
gi 1379604785 376 NEARRHVVESFSTKtfgTHLNRYLiDIYR 404
Cdd:COG0438 95 EAARERAEERFSWE---AIAERLL-ALYE 119
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
16-387 |
1.02e-20 |
|
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: 92.34 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 16 HPDlgIGGAERLVVDAAVELASRGHKVHIFTAHHDK-NRCFEETIAGIFPVTVYGS-----FLPrHIFYRLHALCAylrc 89
Cdd:cd03795 10 YPD--IGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKeTPEKEENGIRIHRVKSFLNvastpFSP-SYIKRFKKLAK---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 90 lfvafcvlflwpSFDVI-------LADQVSVVIpilKLKRSTkVVFYchfpdlllaqHSTFLRRIY-RKPIDYLEEITTG 161
Cdd:cd03795 83 ------------EYDIIhyhfpnpLADLLLFFS---GAKKPV-VVHW----------HSDIVKQKKlLKLYKPLMTRFLR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 162 MADSILVNSNFTASTFANTFKHLDAKGIRP----AVLYPAVNVDQFN--EPTSTKPNFLSINRFERKKNIQLAISAfaml 235
Cdd:cd03795 137 RADRIIATSPNYVETSPTLREFKNKVRVIPlgidKNVYNIPRVDFENikREKKGKKIFLFIGRLVYYKGLDYLIEA---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 236 yspnrvlkhQAITNASLTVAGgfdkrlkENVEYlEELKDLAEKeGVSDKIKFVTSCSTDERNALLSECLCVLYtP---EN 312
Cdd:cd03795 213 ---------AQYLNYPIVIGG-------EGPLK-PDLEAQIEL-NLLDNVKFLGRVDDEEKVIYLHLCDVFVF-PsvlRS 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1379604785 313 EHFGIVPLEAMAAYKVVIACNSGGPVESI-KNGVTGFLCSPT-PQEFSSAMANLINDPQEAEKMGNEARRHVVESFS 387
Cdd:cd03795 274 EAFGIVLLEAMMCGKPVISTNIGTGVPYVnNNGETGLVVPPKdPDALAEAIDKLLSDEELRESYGENAKKRFEELFT 350
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
12-395 |
1.19e-20 |
|
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: 92.44 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 12 IAIIHPDLGIGGAERLVVDAAVELASRGHKVHIFT--AHHDKNRCFEETIAGIFPVTVYGSFLprHIFYrlhaLCAYLRC 89
Cdd:cd03798 4 LTNIYPNANSPGRGIFVRRQVRALSRRGVDVEVLApaPWGPAAARLLRKLLGEAVPPRDGRRL--LPLK----PRLRLLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 90 LFVAFCVLFLW-----PSFDVILAdqvSVVIPIL----KLKRSTKV--VFYCHFPDLLLAQHSTFLRRIYRKpidyleei 158
Cdd:cd03798 78 PLRAPSLAKLLkrrrrGPPDLIHA---HFAYPAGfaaaLLARLYGVpyVVTEHGSDINVFPPRSLLRKLLRW-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 159 TTGMADSILVNSNFTASTFANtfkhLDAKGIRPAVLYPAVNVDQFNEPTST------KPNFLSINRFERKKNIQLAISAF 232
Cdd:cd03798 147 ALRRAARVIAVSKALAEELVA----LGVPRDRVDVIPNGVDPARFQPEDRGlglpldAFVILFVGRLIPRKGIDLLLEAF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 233 AMLYSPNRVLKhqaitnasLTVAGGFDKRlkenveylEELKDLAEKEGVSDKIKFVTSCSTDERNALLSECLCVLYTPEN 312
Cdd:cd03798 223 ARLAKARPDVV--------LLIVGDGPLR--------EALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 313 EHFGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLCSPT-PQEFSSAMANLINDPQEAEkMGNEARRHVVESFSTKTF 391
Cdd:cd03798 287 EGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGdADALAAALRRALAEPYLRE-LGEAARARVAERFSWVKA 365
|
....
gi 1379604785 392 GTHL 395
Cdd:cd03798 366 ADRI 369
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
11-404 |
4.08e-20 |
|
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: 90.42 E-value: 4.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 11 NIAIIHPDLG------IGGAERLVVDAAVELASRGHKVHIFTAHHDKNRCfeetiAGIFPVTVYGSFLPRHIFYRLHALc 84
Cdd:cd03802 1 RIAQVSPPRGpvppgkYGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSA-----PLVAVIPRALRLDPIPQESKLAEL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 85 aylrcLFVAFCVLFLWPsFDVILadqVSVVIPILKLKRSTKVVFYC--HFPDLLlaqhsTFLRRIYRKPidyleeittgm 162
Cdd:cd03802 75 -----LEALEVQLRASD-FDVIH---NHSYDWLPPFAPLIGTPFVTtlHGPSIP-----PSLAIYAAEP----------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 163 adsilvNSNFTASTFANTFKHLDAKgiRPAVLYPAVNVDQFNEPTSTKPNFLSINRFERKKNIQLAIsAFAmlyspnrvl 242
Cdd:cd03802 130 ------PVNYVSISDAQRAATPPID--YLTVVHNGLDPADYRFQPDPEDYLAFLGRIAPEKGLEDAI-RVA--------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 243 kHQAitNASLTVAGGfdKRLKENVEYLEELKDlaekegvSDKIKFVTSCSTDERNALLSECLCVLYTPE-NEHFGIVPLE 321
Cdd:cd03802 192 -RRA--GLPLKIAGK--VRDEDYFYYLQEPLP-------GPRIEFIGEVGHDEKQELLGGARALLFPINwDEPFGLVMIE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 322 AMAAYKVVIACNSGGPVESIKNGVTGFLCsPTPQEFSSAMANLindpqeaEKMGNEA-RRHVVESFSTKTFGthlNRYLi 400
Cdd:cd03802 260 AMACGTPVIAYRRGGLPEVIQHGETGFLV-DSVEEMAEAIANI-------DRIDRAAcRRYAEDRFSAARMA---DRYE- 327
|
....
gi 1379604785 401 DIYR 404
Cdd:cd03802 328 ALYR 331
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
105-404 |
1.03e-19 |
|
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: 90.07 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 105 VILADQVSVVIPILKLKRSTKVVFYCHFpdlllaQHSTFLRRIYRKPIDYLEEITTGmADSILvnsnFTASTFAntfkhl 184
Cdd:cd03792 91 VVIHDPQPALLPKIKKKRDRKWIWRCHI------DISTPLTEPQPRVWDFLWNYIEG-YDLFV----FHPPEFV------ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 185 dAKGIRPAVLYPAVNVDQ---FN---EPTST-------------KPNFLSINRFERKKNIQLAISAFAMLyspnrvlkHQ 245
Cdd:cd03792 154 -PPQVPPPKFYIPPSIDPlsgKNkdlSPADIryylekpfvidpeRPYILQVARFDPSKDPLGVIDAYKLF--------KR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 246 AITNASLTVAGGFDKRLKENVEYLEELKdlaEKEGVSDKIKFVTSCSTD-ERNALLSECLCVLYTPENEHFGIVPLEAMA 324
Cdd:cd03792 225 RAEEPQLVICGHGAVDDPEGSVVYEEVM---EYAGDDHDIHVLRLPPSDqEINALQRAATVVLQLSTREGFGLTVSEALW 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 325 AYKVVIACNSGGPVESIKNGVTGFLcSPTPQEFSSAMANLINDPQEAEKMGNEARRHVVESFSTKtfgTHLNRYLIDIYR 404
Cdd:cd03792 302 KGKPVIATPAGGIPLQVIDGETGFL-VNSVEGAAVRILRLLTDPELRRKMGLAAREHVRDNFLIT---GNLRAWLYLIAK 377
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
34-382 |
2.69e-19 |
|
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: 88.57 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 34 ELASRGHKVHIFTAHHDKNRCFEETIAGIFPVTVYGSFLPRHIFYRLHALCAYLRCLFVafcvlflwpsFDVILadqvSV 113
Cdd:cd03809 26 ALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDK----------PDLLH----SP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 114 VIPILKLKRSTKVVFYCH----------FPDLLLAQHSTFLRRIYRKpidyleeittgmADSILVNSNFTASTFAntfKH 183
Cdd:cd03809 92 HNTAPLLLKGCPQVVTIHdliplrypefFPKRFRLYYRLLLPISLRR------------ADAIITVSEATRDDII---KF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 184 LDAKGIRPAVLYPAVNVDQFNEPTS---------TKPNFLSINRFERKKNIQLAISAFAMLysPNRVLKHQaitnasLTV 254
Cdd:cd03809 157 YGVPPEKIVVIPLGVDPSFFPPESAavliakyllPEPYFLYVGTLEPRKNHERLLKAFALL--KKQGGDLK------LVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 255 AGGFDkrlkenvEYLEELKDLAEKEGVSDKIKFVTSCSTDERNALLSECLCVLYTPENEHFGIVPLEAMAAYKVVIACNs 334
Cdd:cd03809 229 VGGKG-------WEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASN- 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1379604785 335 GGPVESIkNGVTGFLCSPT-PQEFSSAMANLINDPQEAEKMGNEARRHV 382
Cdd:cd03809 301 ISVLPEV-AGDAALYFDPLdPESIADAILRLLEDPSLREELIRKGLERA 348
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
163-380 |
3.98e-19 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 89.03 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 163 ADSILVNSNFTAStfantfkHLDA--KGI-RPAVLYPAVNVDQFN----EPTSTKPNFLSINRFERKKNIQLAISAFAML 235
Cdd:PLN02949 221 AHLAMVNSSWTKS-------HIEAlwRIPeRIKRVYPPCDTSGLQalplERSEDPPYIISVAQFRPEKAHALQLEAFALA 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 236 YspnRVLKHQaITNASLTVAGGFdkRLKENVEYLEELKDLAEKEGVSDKIKFVTSCSTDERNALLSECLCVLYTPENEHF 315
Cdd:PLN02949 294 L---EKLDAD-VPRPKLQFVGSC--RNKEDEERLQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGGAVAGLHSMIDEHF 367
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 316 GIVPLEAMAAYKVVIACNSGGPVESI----KNGVTGFLCSpTPQEFSSAMANLINDPQ-EAEKMGNEARR 380
Cdd:PLN02949 368 GISVVEYMAAGAVPIAHNSAGPKMDIvldeDGQQTGFLAT-TVEEYADAILEVLRMREtERLEIAAAARK 436
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
10-389 |
4.52e-19 |
|
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: 87.79 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 10 MNIAII-HPdlGIGGAERLVVDAAVELASRGHKVHIFT-------AHHDKNRCFEETIAGIFPVTVY-------GSFLPR 74
Cdd:cd04962 1 MKIGIVcYP--SYGGSGVVATELGLELAERGHEVHFISsaipfrlNLYSGNIFFHEVEVPNYPLFEYppytlalASKIVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 75 ----------HIFYRL-HALCAYLrclfvafcvlflwpsfdvilADQVsvvipilkLKRSTKVVFYCHFPDLLLAQHSTF 143
Cdd:cd04962 79 vakehkldvlHAHYAIpHASCAYL--------------------AREI--------LGEKIPIVTTLHGTDITLVGYDPS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 144 LRRIYRKPIDYLEEITTgmadsilvNSNFTAstfANTFKHLDAkgirpavlypavnvdqfNEPTSTKPNFLSINRFERKK 223
Cdd:cd04962 131 LQPAVRFSINKSDRVTA--------VSSSLR---QETYELFDV-----------------DKDIEVIHNFIDEDVFKRKP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 224 NIQLAISAFA-------MLYSPNRVLKH-----------QAITNASLTVAG-GFDKrlkenveylEELKDLAEKEGVSDK 284
Cdd:cd04962 183 AGALKRRLLAppdekvvIHVSNFRPVKRiddvvrvfarvRRKIPAKLLLVGdGPER---------VPAEELARELGVEDR 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 285 IKFVTScsTDERNALLSECLCVLYTPENEHFGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLCSPTPQE-FSSAMAN 363
Cdd:cd04962 254 VLFLGK--QDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDaMAKSALS 331
|
410 420
....*....|....*....|....*.
gi 1379604785 364 LINDPQEAEKMGNEARRHVVESFSTK 389
Cdd:cd04962 332 ILEDDELYNRMGRAARKRAAERFDPE 357
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
11-389 |
6.96e-19 |
|
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: 87.78 E-value: 6.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 11 NIAIIHPD--LGIGGAERLVVDAAVELASRGHKVHIFT--AHHDKNRCF---EETIAGI----FPVTVYGSFLPRHIFyr 79
Cdd:cd03794 1 KILLISQYypPPKGAAAARVYELAKELVRRGHEVTVLTpsPNYPLGRIFagaTETKDGIrvirVKLGPIKKNGLIRRL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 80 LHALCAYLRCLFVAfcvLFLWPSFDVILA--DQVSVVIPILKLKR--STKVVFYCH--FPDLLLAqHSTFLRRIYRKPID 153
Cdd:cd03794 79 LNYLSFALAALLKL---LVREERPDVIIAysPPITLGLAALLLKKlrGAPFILDVRdlWPESLIA-LGVLKKGSLLKLLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 154 YLEEITTGMADSILVNSNFTAstfantfKHLDAKGIRP---AVLYPAVNVDQFNEPTSTKPNFLSINR----------FE 220
Cdd:cd03794 155 KLERKLYRLADAIIVLSPGLK-------EYLLRKGVPKekiIVIPNWADLEEFKPPPKDELRKKLGLDdkfvvvyagnIG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 221 RKKNIQLAISAFAMLyspnrvlkhQAITNASLTVAGGFDKRlkenveylEELKDLAEKEGvSDKIKFVTSCSTDERNALL 300
Cdd:cd03794 228 KAQGLETLLEAAERL---------KRRPDIRFLFVGDGDEK--------ERLKELAKARG-LDNVTFLGRVPKEEVPELL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 301 SEC--LCVLYTPENEHFGIVP---LEAMAAYKVVIACNSGGPVESIKNGVTGFLCSPT-PQEFSSAMANLINDPQEAEKM 374
Cdd:cd03794 290 SAAdvGLVPLKDNPANRGSSPsklFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGdPEALADAILELLDDPELRRAM 369
|
410
....*....|....*
gi 1379604785 375 GNEARRHVVESFSTK 389
Cdd:cd03794 370 GENGRELAEEKFSRE 384
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
34-379 |
5.80e-18 |
|
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: 84.64 E-value: 5.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 34 ELASRGHKVHIFTAHHDkNRCFEETIAGIFPVTVYGSFLPRHIFYRLHALCAYLRclfvafcvLFLWpSFDVILA-DQVS 112
Cdd:cd03817 26 ALEKRGHEVYVITPSDP-GAEDEEEVVRYRSFSIPIRKYHRQHIPFPFKKAVIDR--------IKEL-GPDIIHThTPFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 113 VVIPILKLKRSTKV-------------VFYCHFPDLLL-AQHSTFLRRIYRKpidyleeittgmADSILVNSNFTASTFA 178
Cdd:cd03817 96 LGKLGLRIARKLKIpivhtyhtmyedyLHYIPKGKLLVkAVVRKLVRRFYNH------------TDAVIAPSEKIKDTLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 179 N----TFKHLDAKGIRPAVLYPAVNVDQFNE--PTSTKPNFLSINRFERKKNIQLAISAFAMLYSPNrvlkhqaitNASL 252
Cdd:cd03817 164 EygvkGPIEVIPNGIDLDKFEKPLNTEERRKlgLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEP---------NIKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 253 TVAGGFDkrlkenveYLEELKDLAEKEGVSDKIKFVTSCSTDERNALLSECLCVLYTPENEHFGIVPLEAMAAYKVVIAC 332
Cdd:cd03817 235 VIVGDGP--------EREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAA 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1379604785 333 NSGGPVESIKNGVTGFLCSPTPQEFSSAMANLINDPQEAEKMGNEAR 379
Cdd:cd03817 307 KDPAASELVEDGENGFLFEPNDETLAEKLLHLRENLELLRKLSKNAE 353
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
11-405 |
1.65e-17 |
|
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: 83.15 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 11 NIAII---HPDLGIGGAERLVVDAAVELASRGHKVHIFTAHhdkNRCFEETIAGIFPVTVYGSFLPRH---IFYRLHALC 84
Cdd:cd03823 1 KILLVnslYPPQRVGGAEISVHDLAEALVAEGHEVAVLTAG---VGPPGQATVARSVVRYRRAPDETLplaLKRRGYELF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 85 AY----LRCLFVAFCVLFlwpSFDVILADQVSV----VIPILKlKRSTKVVFYCHFPDLLLAQHSTFLRRIyrkpidyle 156
Cdd:cd03823 78 ETynpgLRRLLARLLEDF---RPDVVHTHNLSGlgasLLDAAR-DLGIPVVHTLHDYWLLCPRQFLFKKGG--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 157 eittgmaDSILVNSNFTASTFANTFkhldAKGIRPAVLYPAVNVD----QFNEPTSTKPNFLSINRFERKKNIQLAISAF 232
Cdd:cd03823 145 -------DAVLAPSRFTANLHEANG----LFSARISVIPNAVEPDlappPRRRPGTERLRFGYIGRLTEEKGIDLLVEAF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 233 AMLYSPNrvlkhqaitnASLTVAGGFDkrlkenveyleeLKDLAEKEGvSDKIKFVTSCSTDERNALLSECLCVLYT--- 309
Cdd:cd03823 214 KRLPRED----------IELVIAGHGP------------LSDERQIEG-GRRIAFLGRVPTDDIKDFYEKIDVLVVPsiw 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 310 PENehFGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLCSPT-PQEFSSAMANLINDPQEAEKMGNEARRHvvesfst 388
Cdd:cd03823 271 PEP--FGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGdAEDLAAAMRRLLTDPALLERLRAGAEPP------- 341
|
410
....*....|....*..
gi 1379604785 389 kTFGTHLNRYLIDIYRG 405
Cdd:cd03823 342 -RSTESQAEEYLKLYRD 357
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
17-388 |
1.24e-15 |
|
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: 77.40 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 17 PDLGIGGAERLVVDAAVELASRGHKVHIftahhdknrcfeetiagifpVTVYGSFLPRHIFYRLHalcayLRCLFVAFcV 96
Cdd:cd03819 6 PALEIGGAETYILDLARALAERGHRVLV--------------------VTAGGPLLPRLRQIGIG-----LPGLKVPL-L 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 97 LFLWPSF---DVILADQVSVV---------IPILkLKRSTKVvfychfPdLLLAQHStfLRRIYRKPIDYLEEITTgMAD 164
Cdd:cd03819 60 RALLGNVrlaRLIRRERIDLIhahsrapawLGWL-ASRLTGV------P-LVTTVHG--SYLATYHPKDFALAVRA-RGD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 165 SILVNSNFTASTfanTFKHLDAKGIRPAVLYPAVNVDQF-----------NEPTSTKPNFLSINRFERKKNIQLAISAFA 233
Cdd:cd03819 129 RVIAVSELVRDH---LIEALGVDPERIRVIPNGVDTDRFppeaeaeeraqLGLPEGKPVVGYVGRLSPEKGWLLLVDAAA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 234 mlyspnrVLKHQaiTNASLTVAGgfDKRLKENVEyleelkDLAEKEGVSDKIKFVTSCstDERNALLSECLCVLYTPENE 313
Cdd:cd03819 206 -------ELKDE--PDFRLLVAG--DGPERDEIR------RLVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSLHE 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1379604785 314 HFGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLCSP-TPQEFSSAMANLINDPQEAEKMGNEAR--RHVVESFST 388
Cdd:cd03819 267 EFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPgDAEALADAIRAAKLLPEAREKLQAAAAltEAVRELLLR 344
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
210-367 |
1.94e-15 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 72.54 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 210 KPNFLSINRF-ERKKNIQLAISAFAMLyspnrvlkHQAITNASLTVAGGFDkrlkenveyLEELKDLAEkeGVSDKIKFV 288
Cdd:pfam13692 1 RPVILFVGRLhPNVKGVDYLLEAVPLL--------RKRDNDVRLVIVGDGP---------EEELEELAA--GLEDRVIFT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 289 TScsTDERNALLSECLCVLYTPENEHFGIVPLEAMAAYKVVIACNSGGPVESIkNGVTGFLCSP-TPQEFSSAMANLIND 367
Cdd:pfam13692 62 GF--VEDLAELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPgDPEALAEAILRLLED 138
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
164-349 |
7.46e-15 |
|
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: 75.40 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 164 DSILVNSNFTASTFANTFKhldakgiRPA-VLYPAVNVDQFnEPTSTKPN-FLSINRFERKKNIQLAISAFAMLysPNRv 241
Cdd:cd03804 159 DLFIANSQFVARRIKKFYG-------REStVIYPPVDTDAF-APAADKEDyYLTASRLVPYKRIDLAVEAFNEL--PKR- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 242 lkhqaitnasLTVAG-GFDkrlkenveyLEELKDLAekegvSDKIKFVTSCSTDERNALLSECLCVLYtPENEHFGIVPL 320
Cdd:cd03804 228 ----------LVVIGdGPD---------LDRLRAMA-----SPNVEFLGYQPDEVLKELLSKARAFVF-AAEEDFGIVPV 282
|
170 180
....*....|....*....|....*....
gi 1379604785 321 EAMAAYKVVIACNSGGPVESIKNGVTGFL 349
Cdd:cd03804 283 EAQACGTPVIAFGKGGALETVRPGPTGIL 311
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
22-201 |
8.21e-15 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 71.79 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 22 GGAERLVVDAAVELASRGHKVHIFTAHHDKNRCFEETIAGIFPVTVYGSF-LPRHIFYRLHALCAYLRCLfvafcvlflw 100
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPpRLLRSLAFLRRLRRLLRRE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 101 pSFDVILADQ---VSVVIPILKLKRSTKVVFYCHFPDLLLAQHStFLRRIYRKPIDYLEEITTGMADSILVNSNFTASTF 177
Cdd:pfam13439 71 -RPDVVHAHSpfpLGLAALAARLRLGIPLVVTYHGLFPDYKRLG-ARLSPLRRLLRRLERRLLRRADRVIAVSEAVADEL 148
|
170 180
....*....|....*....|....
gi 1379604785 178 ANTFkHLDAKGIRpaVLYPAVNVD 201
Cdd:pfam13439 149 RRLY-GVPPEKIR--VIPNGVDLE 169
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
22-390 |
2.08e-13 |
|
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: 70.86 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 22 GGAERLVVDAAVELASRGHKVHI-FTAHHDKNRCFEETIAGIFPVTVYGSFL-----PRHIFYRLH---ALCAYLRClfv 92
Cdd:cd03821 14 GGPVKVVLRLAAALAALGHEVTIvSTGDGYESLVVEENGRYIPPQDGFASIPllrqgAGRTDFSPGlpnWLRRNLRE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 93 afcvlflwpsFDVI----LADQVSvvIPILKLKRSTKVVfYCHFP----DLLLAQHSTFLRRIYRkpIDYLEEITTGMAD 164
Cdd:cd03821 91 ----------YDVVhihgVWTYTS--LAACKLARRRGIP-YVVSPhgmlDPWALQQKHWKKRIAL--HLIERRNLNNAAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 165 SIlvnsnFTASTFAntfKHLDAKGIRP--AVLYPAVNVDQFnEPTST----------KPNFLSINRFERKKNIQLAISAF 232
Cdd:cd03821 156 VH-----FTSEQEA---DELRRFGLEPpiAVIPNGVDIPEF-DPGLRdrrkhngledRRIILFLGRIHPKKGLDLLIRAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 233 AMLYSPNRvlkhqaitNASLTVAGGFDKrlkenvEYLEELKDLAEKeGVSDKIKFVTSCSTDERNALLSECLCVLYTPEN 312
Cdd:cd03821 227 RKLAEQGR--------DWHLVIAGPDDG------AYPAFLQLQSSL-GLGDRVTFTGPLYGEAKWALYASADLFVLPSYS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 313 EHFGIVPLEAMAA-YKVVIACNSGGPvesikNGVT---GFLCSPTPQEFSSAMANLINDPQEAEKMGNEARR--HVVESF 386
Cdd:cd03821 292 ENFGNVVAEALACgLPVVITDKCGLS-----ELVEagcGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRarQVEENF 366
|
....
gi 1379604785 387 STKT 390
Cdd:cd03821 367 SWEA 370
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
182-405 |
3.67e-13 |
|
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: 70.83 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 182 KHLDAKGIRPAVLYPAVNVDQFNE-----PTSTKPNFLSINRFERKKNIQLAISAFAMLYSpnrvlkhqAITNASLTVAG 256
Cdd:cd03813 260 IRLGADPDKTRVIPNGIDIQRFAPareerPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRR--------AMPDAEGWLIG 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 257 GFDkrlkENVEYLEELKDLAEKEGVSDKIKFVTSCSTDErnALLSECLCVLyTPENEHFGIVPLEAMAAYKVVIACNSGG 336
Cdd:cd03813 332 PED----EDPEYAQECKRLVASLGLENKVKFLGFQNIKE--YYPKLGLLVL-TSISEGQPLVILEAMASGVPVVATDVGS 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1379604785 337 PVESI-----KNGVTGFLCSPT-PQEFSSAMANLINDPQEAEKMGNEARRHVVESFSTKTFgthlnrylIDIYRG 405
Cdd:cd03813 405 CRELIygaddALGQAGLVVPPAdPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGM--------IDSYRK 471
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
12-404 |
5.89e-13 |
|
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: 69.63 E-value: 5.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 12 IAII----HPDlgIGGAERLVVDAAVELASRGHKVHIFTAHHdknrcFEETIAGIFPVTVYGSF-LPRHIFYRLhALCAY 86
Cdd:cd03814 2 IALVtdtyHPQ--VNGVVRTLERLVDHLRRRGHEVRVVAPGP-----FDEAESAEGRVVSVPSFpLPFYPEYRL-ALPLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 87 LRclfvafcVLFLWPSF--DVIladQVSVVIPI------LKLKRSTKVVFYCH----------FPDLLLAQHSTFLRRIY 148
Cdd:cd03814 74 RR-------VRRLIKEFqpDII---HIATPGPLglaalrAARRLGLPVVTSYHtdfpeylsyyTLGPLSWLAWAYLRWFH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 149 RkpidyleeittgMADSILVNSNFTAstfantfKHLDAKGIRPAVLYP-AVNVDQFN----------EPTST-KPNFLSI 216
Cdd:cd03814 144 N------------PFDTTLVPSPSIA-------RELEGHGFERVRLWPrGVDTELFHpsrrdaalrrRLGPPgRPLLLYV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 217 NRFERKKNIQLAISAFAMLyspnrvlkhQAITNASLTVAGG--FDKRLKE---NVEYLEELK--DLAEKEGVSDKikFVT 289
Cdd:cd03814 205 GRLAPEKNLEALLDADLPL---------AASPPVRLVVVGDgpARAELEArgpDVIFTGFLTgeELARAYASADV--FVF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 290 SCSTdernallseclcvlytpenEHFGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLCSP-TPQEFSSAMANLINDP 368
Cdd:cd03814 274 PSRT-------------------ETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPgDAAAFAAALRALLEDP 334
|
410 420 430
....*....|....*....|....*....|....*.
gi 1379604785 369 QEAEKMGNEARRHVVEsfstKTFgTHLNRYLIDIYR 404
Cdd:cd03814 335 ELRRRMAARARAEAER----YSW-EAFLDNLLDYYA 365
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
11-387 |
3.92e-11 |
|
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: 63.88 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 11 NIAIIHPDLGIGGAERLVVDAAVELASRGHKVHIFTAHHDKNRcFEETIAgiFPVTVYgsFLPRHIFYRLHALCAYLRcL 90
Cdd:cd03807 1 KVAHVITGLNVGGAETMLLRLLEHMDKSRFEHVVISLTGDGVL-GEELLA--AGVPVV--CLGLSSGKDPGVLLRLAK-L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 91 FVAFCVlflwpsfDVIL-----ADQVSvvIPILKLKRSTKVVFYCHfpDLLLAQHST-FLRRIYRKpidyleeiTTGMAD 164
Cdd:cd03807 75 IRKRNP-------DVVHtwmyhADLIG--GLAAKLAGGVKVIWSVR--SSNIPQRLTrLVRKLCLL--------LSKFSP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 165 SILVNSNFTA-STFANtfkHLDAKGIRpaVLYPAVNVDQFNEP-------------TSTKPNFLSINRFERKKNIQLAIS 230
Cdd:cd03807 136 ATVANSSAVAeFHQEQ---GYAKNKIV--VIYNGIDLFKLSPDdasrararrrlglAEDRRVIGIVGRLHPVKDHSDLLR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 231 AFAMLYSpnrvlkhqAITNASLTVAGGFDKRlKENVEYLEELkdlaekeGVSDKIKFvtscsTDERNALlSECLCVLY-- 308
Cdd:cd03807 211 AAALLVE--------THPDLRLLLVGRGPER-PNLERLLLEL-------GLEDRVHL-----LGERSDV-PALLPAMDif 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 309 --TPENEHFGIVPLEAMAAYKVVIACNSGGPVESIKNGvTGFLCSP-TPQEFSSAMANLINDPQEAEKMGNEARRHVVES 385
Cdd:cd03807 269 vlSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPAgDPQALADAIRALLEDPEKRARLGRAARERIANE 347
|
..
gi 1379604785 386 FS 387
Cdd:cd03807 348 FS 349
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
65-350 |
7.12e-11 |
|
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: 62.04 E-value: 7.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 65 VTVYGSFLPRHIFYRLHALCAYLRCLFVAFCVLFLWPSFDVILADQVSVVIPIlklkrstkvVFYCHFPDLLlAQHSTFL 144
Cdd:cd01635 4 VTGEYPPLRGGLELHVRALARALAALGHEVTVLALLLLALRRILKKLLELKPD---------VVHAHSPHAA-ALAALLA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 145 RRIYRKPIdyleeittgmadsilvnsNFTASTFANTFKHLDAKGIRPAVLYPAVNVDQfneptstkpnfLSINRFERKKN 224
Cdd:cd01635 74 ARLLGIPI------------------VVTVHGPDSLESTRSELLALARLLVSLPLADK-----------VSVGRLVPEKG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 225 IQLAISAFAMLYspnrvlkhQAITNASLTVAGGFDKRlkenveylEELKDLAEKEGVSDKIKFVTSCSTDERNALLSECL 304
Cdd:cd01635 125 IDLLLEALALLK--------ARLPDLVLVLVGGGGER--------EEEEALAAALGLLERVVIIGGLVDDEVLELLLAAA 188
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1379604785 305 -CVLYTPENEHFGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLC 350
Cdd:cd01635 189 dVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
188-386 |
7.94e-10 |
|
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: 60.16 E-value: 7.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 188 GIRPAVLYPAvnvdqfnEPTSTKPNFLSINRFERKKNIQLAISAFamlyspnRVLKHQAITnASLTVAGgfDKRLkenve 267
Cdd:cd05844 174 GIDPAKFAPR-------DPAERAPTILFVGRLVEKKGCDVLIEAF-------RRLAARHPT-ARLVIAG--DGPL----- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 268 yLEELKDLAEKEGvsdKIKFVTSCSTDERNALL--SECLCV-LYTPEN---EHFGIVPLEAMAAYKVVIACNSGGPVESI 341
Cdd:cd05844 232 -RPALQALAAALG---RVRFLGALPHAEVQDWMrrAEIFCLpSVTAASgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAI 307
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1379604785 342 KNGVTGFLCSP-TPQEFSSAMANLINDPQEAEKMGNEARRHVVESF 386
Cdd:cd05844 308 LDGETGFLVPEgDVDALADALQALLADRALADRMGGAARAFVCEQF 353
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
22-192 |
1.02e-09 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 57.03 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 22 GGAERLVVDAAVELASRGHKVHIFTAHHDkNRCFEETIAGifpVTVYGSFLPRH--IFYRLHALCAYLRclfvafcvLFL 99
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGP-PGRPELVGDG---VRVHRLPVPPRpsPLADLAALRRLRR--------LLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 100 WPSFDVILAD--QVSVVIPILKLKRSTKVVFYCHfpDLLLAQHSTFLRRIYRkpidYLEEITTGMADSILVNSNFTASTF 177
Cdd:pfam13579 69 AERPDVVHAHspTAGLAARLARRRRGVPLVVTVH--GLALDYGSGWKRRLAR----ALERRLLRRADAVVVVSEAEAELL 142
|
170
....*....|....*
gi 1379604785 178 AntfkhldAKGIRPA 192
Cdd:pfam13579 143 R-------ALGVPAA 150
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
313-404 |
3.37e-09 |
|
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: 58.11 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 313 EHFGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLCSP-TPQEFSSAMANLINDPQEAEKMGNEARRHVVESFSTKtf 391
Cdd:cd03825 274 DNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPgDVQALAEAIEWLLANPKERESLGERARALAENHFDQR-- 351
|
90
....*....|...
gi 1379604785 392 gTHLNRYlIDIYR 404
Cdd:cd03825 352 -VQAQRY-LELYK 362
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
210-395 |
1.17e-08 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 57.30 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 210 KPNFLSINRFERKKNIqlaiSAFAMLYSPNRVLKHQAitnaSLTVAGGFDKRLK----ENVEYLEELKDLAEKEGVSDKI 285
Cdd:PLN00142 573 KPIIFSMARLDRVKNL----TGLVEWYGKNKRLRELV----NLVVVGGFIDPSKskdrEEIAEIKKMHSLIEKYNLKGQF 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 286 KFVTSCSTDERNALLSECLC---------VLYtpenEHFGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLCSP-TPQ 355
Cdd:PLN00142 645 RWIAAQTNRVRNGELYRYIAdtkgafvqpALY----EAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPyHGD 720
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1379604785 356 EFSSAMANLI----NDPQEAEKMGNEARRHVVESFSTKTFGTHL 395
Cdd:PLN00142 721 EAANKIADFFekckEDPSYWNKISDAGLQRIYECYTWKIYAERL 764
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
320-387 |
2.07e-07 |
|
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).
Pssm-ID: 340845 [Multi-domain] Cd Length: 396 Bit Score: 52.75 E-value: 2.07e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1379604785 320 LEAMAAYKVVIACNSGGPVESIKNGVTGFLCS-PTPQEFSSAMANLINDPQEAEKMGNEARRHVVESFS 387
Cdd:cd03818 318 LEAMACGCPVIGSDTAPVREVIRDGRNGLLVDfFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDS 386
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
141-387 |
3.60e-07 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 51.71 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 141 STFLRRIYRKPIDYleeittgmADSILVNSNFTASTFANTFKHLDAKgirpavlypavnvdQFNEPTSTKPNFLSiNRFE 220
Cdd:PRK15484 147 SQFLKKFYEERLPN--------ADISIVPNGFCLETYQSNPQPNLRQ--------------QLNISPDETVLLYA-GRIS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 221 RKKNIQLAISAFamlyspNRVLKHQaiTNASLTVAGG-FDKRLKENVEYLEELKDLAEKEGvsDKIKFVTSCSTDERNAL 299
Cdd:PRK15484 204 PDKGILLLMQAF------EKLATAH--SNLKLVVVGDpTASSKGEKAAYQKKVLEAAKRIG--DRCIMLGGQPPEKMHNY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 300 LSEC-LCVLYTPENEHFGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGF-LCSP-TPQEFSSAMANLINDPQEAEkMGN 376
Cdd:PRK15484 274 YPLAdLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYhLAEPmTSDSIISDINRTLADPELTQ-IAE 352
|
250
....*....|.
gi 1379604785 377 EARRHVVESFS 387
Cdd:PRK15484 353 QAKDFVFSKYS 363
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
11-392 |
4.53e-07 |
|
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: 51.29 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 11 NIAIIHPDLGIGGAERLVVDAAVELASRGHKVHIFTAHHDKNrcfeetiagifpvtvYGSFLPRHIFYRLH---ALCAYL 87
Cdd:cd04951 1 KILYVITGLGLGGAEKQTVLLADQMFIRGHDVNIVYLTGEVE---------------VKPLNNNIIIYNLGmdkNPRSLL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 88 RCLFVAFCVL-FLWPsfDVILADQVSVVIpILKLKRstkvvFYCHFPDLLLAQHST----FLR-RIYRKpIDYLEEITTG 161
Cdd:cd04951 66 KALLKLKKIIsAFKP--DVVHSHMFHANI-FARFLR-----MLYPIPLLICTAHNKneggRIRmFIYRL-TDFLCDITTN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 162 MadsilvnSNFTASTFANTFKHLDAKgirpavlypavnvdqfnepTSTKPNFLSINRFERKKNIQLAI--------SAFA 233
Cdd:cd04951 137 V-------SREALDEFIAKKAFSKNK-------------------SVPVYNGIDLNKFKKDINVRLKIrnklnlknDEFV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 234 MLYS---------PNRVLK----HQAITNASLTVAGgfDKRLKENVEyleelkDLAEKEGVSDKIKFVTSCSTDERnaLL 300
Cdd:cd04951 191 ILNVgrlteakdyPNLLLAiselILSKNDFKLLIAG--DGPLRNELE------RLICNLNLVDRVILLGQISNISE--YY 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 301 SECLCVLYTPENEHFGIVPLEAMAAYKVVIACNSGGPVESIKNgvTGFLCS-PTPQEFSSAMANLINDPQEAEKMGNEAR 379
Cdd:cd04951 261 NAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGD--HNYVVPvSDPQLLAEKIKEIFDMSDEERDILGNKN 338
|
410
....*....|...
gi 1379604785 380 RHVVESFSTKTFG 392
Cdd:cd04951 339 EYIAKNFSINTIV 351
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
196-389 |
9.96e-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: 50.38 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 196 PAVNVDQFNEPTSTKPN----FLSINRFERKKNIQLAISAFAMLyspnrvlkHQAITNASLTVAG-GFDKrlkenveylE 270
Cdd:cd04949 142 PVGYVDQLDTAESNHERksnkIITISRLAPEKQLDHLIEAVAKA--------VKKVPEITLDIYGyGEER---------E 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 271 ELKDLAEKEGVSDKIKFvtSCSTDERNALLSECLCVLYTPENEHFGIVPLEAMAAYKVVIACNSG-GPVESIKNGVTGFL 349
Cdd:cd04949 205 KLKKLIEELHLEDNVFL--KGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYL 282
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1379604785 350 cspTPQE----FSSAMANLINDPQEAEKMGNEARRHvVESFSTK 389
Cdd:cd04949 283 ---IEKNnidaLADKIIELLNDPEKLQQFSEESYKI-AEKYSTE 322
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
311-382 |
1.46e-05 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 47.01 E-value: 1.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1379604785 311 ENEHFGIVPLEAMAAYKVVIACNSGGPVESI---KNGVTGFLCSPTP-QEFSSAMANLINDPQEAEKMGNEARRHV 382
Cdd:PLN02871 340 ESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDvDDCVEKLETLLADPELRERMGAAAREEV 415
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
204-386 |
3.57e-05 |
|
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: 45.52 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 204 NEPTSTKPNFLSINRFERKKNIQLAISAFAMLYspnrvlkhQAITNASLTVAGgfDKRLKENveyleeLKDLAEKEGVSD 283
Cdd:cd03799 168 YLPLDGKIRILTVGRLTEKKGLEYAIEAVAKLA--------QKYPNIEYQIIG--DGDLKEQ------LQQLIQELNIGD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 284 KIKFVTSCSTDERNALLSECLCVLYTP------ENEHFGIVPLEAMAAYKVVIACNSGGPVESIKNGVTGFLcspTPQEF 357
Cdd:cd03799 232 CVKLLGWKPQEEIIEILDEADIFIAPSvtaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFL---VPERD 308
|
170 180 190
....*....|....*....|....*....|...
gi 1379604785 358 SSAMAN----LINDPQEAEKMGNEARRHVVESF 386
Cdd:cd03799 309 AEAIAEkltyLIEHPAIWPEMGKAGRARVEEEY 341
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
32-160 |
4.20e-04 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 42.15 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 32 AVELASRGHKVHIFTAHHDknrcFEETI--AGIFPVTVYGSFLPRHIFYRLHALCAYLRCLFVAFCV------------L 97
Cdd:cd03784 21 AKALAARGHEVTVATPPFN----FADLVeaAGLTFVPVGDDPDELELDSETNLGPDSLLELLRRLLKaadellddllaaL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1379604785 98 FLWPSFDVILADQVSVVIPILKLKRSTKVVFYCHFPDLLLAQHSTFLRRIYRKPIDYLEEITT 160
Cdd:cd03784 97 RSSWKPDLVIADPFAYAGPLVAEELGIPSVRLFTGPATLLSAYLHPFGVLNLLLSSLLEPELF 159
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
269-389 |
7.68e-04 |
|
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: 41.29 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379604785 269 LEELKDLAEKEGVSDKIKFVTSCSTDERNALLSECLCVLYTPENEHFGIvP---LEAMAAYKVVIACNSGGPVESIKNGV 345
Cdd:cd04946 269 KERLEKLAENKLENVKVNFTGEVSNKEVKQLYKENDVDVFVNVSESEGI-PvsiMEAISFGIPVIATNVGGTREIVENET 347
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1379604785 346 TGFLCS--PTPQEFSSAMANLINDPQEAEKMGNEARRHVVESFSTK 389
Cdd:cd04946 348 NGLLLDkdPTPNEIVSSIMKFYLDGGDYKTMKISARECWEERFNAE 393
|
|
| |
