|
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 ... |
17-407 |
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: 645.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 17 VLFLHPDMGIGGAERLVLDAALALQEYGCDVKIWTAHYDPNHCFIETRE--LSVQCAGDWLPRSLGwgGRGAAICSYVRM 94
Cdd:cd03805 3 VAFLHPDLGIGGAERLVVDAALALQSRGHEVTIYTSHHDPSHCFEETKDgtLPVRVRGDWLPRSIF--GRFHALCAYLRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 95 VFLALYVLFLSGEEFDVVVCDQVSACIPVFKLARRRKrVLFYCHFPDLLLTQRNSALKKFYRAPIDWIEEYTTGMADRIL 174
Cdd:cd03805 81 LYLALYLLLFSGEKYDVFIVDQVSACVPLLKLFRPSK-ILFYCHFPDQLLAQRKSLLKRLYRKPFDWLEEFTTGMADQIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 175 VNSQYTASVFKETFKTLSHRNPDVLYPSLNIGSFDLAIPEKID-DLVPKGKQFLFLSINRYERKKNLPLALRSLVQLRNR 253
Cdd:cd03805 160 VNSNFTAGVFKKTFPSLAKNPPEVLYPCVDTDSFDSTSEDPDPgDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 254 LPsqEWDKVHLFMAGGYDDRIPENVEHYKELKKMVQE-SDLERHVTFLRSFSDRQKISLLHGCLCVLYTPSNEHFGIVPL 332
Cdd:cd03805 240 LP--EFENVRLVIAGGYDPRVAENVEYLEELQRLAEElLNVEDQVLFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPL 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46395975 333 EAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVHFSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAFADQL 407
Cdd:cd03805 318 EAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAERL 392
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
17-409 |
1.19e-41 |
|
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: 150.77 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 17 VLFLHPDM--GIGGAERLVLDAALALQEYGCDVKIWTahYDPNHCFIETRELSVQCAGDWLPRSLGWGGRgaaicsyvrm 94
Cdd:cd03801 2 ILLLSPELppPVGGAERHVRELARALAARGHDVTVLT--PADPGEPPEELEDGVIVPLLPSLAALLRARR---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 95 vFLALYVLFLSGEEFDVVVC-DQVSACIPVFKLARRRKRVLFYCHFPDLLLTQRNSALKKFyrapidWIEE--YTTGMAD 171
Cdd:cd03801 70 -LLRELRPLLRLRKFDVVHAhGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERR------LLARaeALLRRAD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 172 RILVNSQYTASVFKETFKTLSHRnPDVLYPSLNIGSFDLAIPEKIDdlvPKGKQFLFLSINRYERKKNLPLALRSLVQLR 251
Cdd:cd03801 143 AVIAVSEALRDELRALGGIPPEK-IVVIPNGVDLERFSPPLRRKLG---IPPDRPVLLFVGRLSPRKGVDLLLEALAKLL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 252 NRLPsqewdKVHLFMAGGYDdripenvEHYKELKKMvqESDLERHVTFLRSFSDRQKISLLHGCLCVLYTPSNEHFGIVP 331
Cdd:cd03801 219 RRGP-----DVRLVIVGGDG-------PLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVV 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46395975 332 LEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVH-FSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAFADQLYQ 409
Cdd:cd03801 285 LEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEaLADALLRLLADPELRARLGRAARERVAERFSWERVAERLLD 363
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
224-393 |
1.68e-31 |
|
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: 117.38 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 224 KQFLFLSINRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLRSF 303
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNP-----NLKLVIAGDGEEE--------KRLKKLAEKLGLGDNVIFLGFV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 304 SDRQKISLLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSL 382
Cdd:pfam00534 68 SDEDLPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPnNAEALAEAIDKLLEDEEL 147
|
170
....*....|.
gi 46395975 383 KATMGLAGKAR 393
Cdd:pfam00534 148 RERLGENARKR 158
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
19-406 |
9.12e-29 |
|
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: 116.55 E-value: 9.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 19 FLHP--DMGiGGAERlVLDAAL-ALQEYGCDVK--IWTAHYDPNHCFI----ETR---ELSVQCAGDWLPRSLGW--GGR 84
Cdd:cd03806 5 FFHPycNAG-GGGER-VLWCAVkATQKAYPNNIcvIYTGDTDSSPEEIlekvESRfniDLDSPRIVFFLLKYRKLveAKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 85 -------GAAICSyvrmVFLALYVLFLSGEEfdvVVCDQV--SACIPVFKLARRRKrVLFYCHFP----DLL--LTQRN- 148
Cdd:cd03806 83 yprftllGQALGS----MILGFEALLKLVPD---VFIDTMgyPFTYPLVRLLGGCP-VVAYVHYPtistDMLnkVRSREa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 149 --------------SALKKFYRAPIDWIEEYTTGMADRILVNSQYTASVFKETFKtlSHRNPDVLYPSLNIGSFdLAIPE 214
Cdd:cd03806 155 synndstiarssvlSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWK--RNIKPSIVYPPCDTEEL-TKLPI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 215 KiddlvPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPSQEWDKVHLFMAGGYddRIPENVEHYKELKKMVQESDLE 294
Cdd:cd03806 232 D-----EKTRENQILSIAQFRPEKNHPLQLRAFAELLKRLPESIRSNPKLVLIGSC--RNEEDKERVEALKLLAKELILE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 295 RHVTFLRSFSDRQKISLLHGCLCVLYTPSNEHFGIVPLEamYMQCPVIAV--NNGGPLESIV----HKVTGFLCEpDPVH 368
Cdd:cd03806 305 DSVEFVVDAPYEELKELLSTASIGLHTMWNEHFGIGVVE--YMAAGLIPLahASAGPLLDIVvpwdGGPTGFLAS-TPEE 381
|
410 420 430
....*....|....*....|....*....|....*...
gi 46395975 369 FSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAFADQ 406
Cdd:cd03806 382 YAEAIEKILTLSEEERLQRREAARSSAERFSDEEFERD 419
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
26-407 |
2.75e-27 |
|
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: 111.15 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 26 IGGAERLVLDAALALQEYGCDVKIWTAHYDPNHCFIEtrELSVQCAG-DWLPRSLgwggrgaaicsYVRMVFLALYVL-- 102
Cdd:cd03808 9 DGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELK--ELGVKVIDiPILRRGI-----------NPLKDLKALFKLyk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 103 FLSGEEFDVVVCDQVSACI---PVFKLARRRKRVL----FYCHFPDllltqrNSALKKFYRapidWIEEYTTGMADRILV 175
Cdd:cd03808 76 LLKKEKPDIVHCHTPKPGIlgrLAARLAGVPKVIYtvhgLGFVFTE------GKLLRLLYL----LLEKLALLFTDKVIF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 176 NSQYTASVFKEtfKTLSHRNPDVLYPslNIGsFDLAIPEKIDDLVPKGKqFLFLSINRYERKKNLPLALRSLVQLRNRLP 255
Cdd:cd03808 146 VNEDDRDLAIK--KGIIKKKKTVLIP--GSG-VDLDRFQYSPESLPSEK-VVFLFVARLLKDKGIDELIEAAKILKKKGP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 256 sqewdKVHLFMAGGYDDRIPenvehykeLKKMVQESDLERHVTFLRSFSD-RQKISLLHgcLCVLytPSN-EHFGIVPLE 333
Cdd:cd03808 220 -----NVRFLLVGDGELENP--------SEILIEKLGLEGRIEFLGFRSDvPELLAESD--VFVL--PSYrEGLPRSLLE 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46395975 334 AMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAFADQL 407
Cdd:cd03808 283 AMAAGRPVITTDVPGCRELVIDGVNGFLVPPgDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKL 357
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
17-385 |
1.33e-25 |
|
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: 106.67 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 17 VLFLHPDMGIGGAERLVLDAALALQEYGCDVKIWTaHYDPNHCFIETRELSVQCAGDWLPRSLGWGGRGAAICSYVRmvf 96
Cdd:cd03811 2 ILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVL-LRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 97 lalyvlFLSGEEFDVVVCDQVSACIPVFKLARRRKRVLFYCH-FPDLLLTQRNSALKKFYRAPidwieeyttgMADRILV 175
Cdd:cd03811 78 ------ILKRAKPDVVISFLGFATYIVAKLAAARSKVIAWIHsSLSKLYYLKKKLLLKLKLYK----------KADKIVC 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 176 NSQYTASVFKETFKTLSHRNpDVLYpslNIGSFDLAIPE-KIDDLVPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRL 254
Cdd:cd03811 142 VSKGIKEDLIRLGPSPPEKI-EVIY---NPIDIDRIRALaKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 255 PsqewdKVHLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLrsfsDRQK--ISLLHGCLCVLYTPSNEHFGIVPL 332
Cdd:cd03811 218 P-----DVKLVILGDGPLR--------EELEKLAKELGLAERVIFL----GFQSnpYPYLKKADLFVLSSRYEGFPNVLL 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 46395975 333 EAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVHFSEAMEKFIHKPSLKAT 385
Cdd:cd03811 281 EAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQKKLDAA 333
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
311-415 |
7.06e-23 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 93.13 E-value: 7.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 311 LLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLA 389
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPgDPEALAEAILRLLEDPELRRRLGEA 96
|
90 100
....*....|....*....|....*.
gi 46395975 390 GKARVAEKFSADAFADQLYQYVTKLV 415
Cdd:COG0438 97 ARERAEERFSWEAIAERLLALYEELL 122
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
170-407 |
1.31e-21 |
|
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 95.12 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 170 ADRILVNSQYTASVFKETFKtLSHRNPDVLYPSLNIgSFDLAIPEKIDDLVPKGKQFLFLSINRYERKKNLPLALRSLVQ 249
Cdd:cd03809 139 ADAIITVSEATRDDIIKFYG-VPPEKIVVIPLGVDP-SFFPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFAL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 250 LRNRLPsqewdKVHLFMAGGYDDRipenvehYKELKKMVQESDLERHVTFLRSFSDRQKISLLHGCLCVLYtPS-NEHFG 328
Cdd:cd03809 217 LKKQGG-----DLKLVIVGGKGWE-------DEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVF-PSlYEGFG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 329 IVPLEAMYMQCPVIAVNNGgplesiVHK-VTG---FLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARvAEKFSADAF 403
Cdd:cd03809 284 LPVLEAMACGTPVIASNIS------VLPeVAGdaaLYFDPlDPESIADAILRLLEDPSLREELIRKGLER-AKKFSWEKT 356
|
....
gi 46395975 404 ADQL 407
Cdd:cd03809 357 AEKT 360
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
19-404 |
1.57e-21 |
|
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: 95.03 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 19 FLHPDmgIGGAERLVLDAALALQEYGCDVKIWTAHYDPNHCFIETRELSVQCAGDWlprslgwggrgaaiCSYVRMVFLA 98
Cdd:cd03795 8 FYYPD--IGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIRIHRVKSF--------------LNVASTPFSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 99 LYVLFLSG--EEFDVVV--CDQVSACIPVFKLARRRKRVLFYcHfPDLLltqRNSALKKFYRAPIDWieeyTTGMADRIL 174
Cdd:cd03795 72 SYIKRFKKlaKEYDIIHyhFPNPLADLLLFFSGAKKPVVVHW-H-SDIV---KQKKLLKLYKPLMTR----FLRRADRII 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 175 VnsqyTASVFKETFKTL-SHRNPDVLYP-SLNIGSFDLAI--PEKIDDLVPKGKQFLFLSINRYerKKNLPLALRSLVQL 250
Cdd:cd03795 143 A----TSPNYVETSPTLrEFKNKVRVIPlGIDKNVYNIPRvdFENIKREKKGKKIFLFIGRLVY--YKGLDYLIEAAQYL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 251 rnrlpsqewdKVHLFMAGgyddripENVEhYKELKKMVQESDLERhVTFLRSFSDRQKISLLHGCLCVLYtPS---NEHF 327
Cdd:cd03795 217 ----------NYPIVIGG-------EGPL-KPDLEAQIELNLLDN-VKFLGRVDDEEKVIYLHLCDVFVF-PSvlrSEAF 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46395975 328 GIVPLEAMYMQCPVIAVNNGGPLESIV-HKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAFA 404
Cdd:cd03795 277 GIVLLEAMMCGKPVISTNIGTGVPYVNnNGETGLVVPPkDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEKMK 355
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
221-407 |
4.32e-21 |
|
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: 94.23 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 221 PKGKQFLFLSinRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAGGYDDRIPENVEhyKELKKMVQESDLERHVTFL 300
Cdd:cd03800 218 PDKPVVLALG--RLDPRKGIDTLVRAFAQLPELRE-----LANLVLVGGPSDDPLSMDR--EELAELAEELGLIDRVRFP 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 301 rSFSDRQKISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIH 378
Cdd:cd03800 289 -GRVSRDDLPELYRAADVFVVPSlYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPhDPEALAAALRRLLD 367
|
170 180
....*....|....*....|....*....
gi 46395975 379 KPSLKATMGLAGKARVAEKFSADAFADQL 407
Cdd:cd03800 368 DPALWQRLSRAGLERARAHYTWESVADQL 396
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
16-407 |
5.65e-20 |
|
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: 90.86 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 16 SVLFLHPD--MGIGGAERLVLDAALALQEYGCDVKIWTAhyDPNHCFIETRELSVQCAGD------WLPRS--LGWGGRG 85
Cdd:cd03794 1 KILLISQYypPPKGAAAARVYELAKELVRRGHEVTVLTP--SPNYPLGRIFAGATETKDGirvirvKLGPIkkNGLIRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 86 AAICSYVRMVFLALyvlFLSGEEFDVVVC--DQVSACIPVFKLARR-RKRVLFYCH--FPDLLLTQRNSALKKFYRApID 160
Cdd:cd03794 79 LNYLSFALAALLKL---LVREERPDVIIAysPPITLGLAALLLKKLrGAPFILDVRdlWPESLIALGVLKKGSLLKL-LK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 161 WIEEYTTGMADRILVNSQYTASVFKEtfKTLSHRNPDVLYPSLNIGSFDLAIPEKIDDLVPKGKQFLFLSINryerkkNL 240
Cdd:cd03794 155 KLERKLYRLADAIIVLSPGLKEYLLR--KGVPKEKIIVIPNWADLEEFKPPPKDELRKKLGLDDKFVVVYAG------NI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 241 PLA--LRSLVQLRNRLPSQewDKVHLFMAGGYDDRipenvehyKELKKMVQESDLERhVTFLRSFSDRQKISLLHGC--L 316
Cdd:cd03794 227 GKAqgLETLLEAAERLKRR--PDIRFLFVGDGDEK--------ERLKELAKARGLDN-VTFLGRVPKEEVPELLSAAdvG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 317 CVLYTPSNEHFGIVP---LEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKA 392
Cdd:cd03794 296 LVPLKDNPANRGSSPsklFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPgDPEALADAILELLDDPELRRAMGENGRE 375
|
410
....*....|....*
gi 46395975 393 RVAEKFSADAFADQL 407
Cdd:cd03794 376 LAEEKFSREKLADRL 390
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
212-411 |
6.77e-20 |
|
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: 90.42 E-value: 6.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 212 IPEKIDDLVPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPsqewdkVHLFMAGGYDDRipenvehyKELKKMVQES 291
Cdd:cd03817 188 NTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEPN------IKLVIVGDGPER--------EELKELAREL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 292 DLERHVTFLrSFSDRQKISLLHGCLCVLYTPSN-EHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVHFS 370
Cdd:cd03817 254 GLADKVIFT-GFVPREELPEYYKAADLFVFASTtETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDETLA 332
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46395975 371 EAMEKFIHKPSLKATMGLAGKARvAEKFSADAFADQLYQYV 411
Cdd:cd03817 333 EKLLHLRENLELLRKLSKNAEIS-AREFAFAKSVEKLYEEV 372
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
221-411 |
2.07e-19 |
|
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: 88.50 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 221 PKGKQFLFLSinRYERKKNLPLALRSLVQLrnrlpsqewdKVHLFMAGGYDDRipenvEHYKELkkmvQESDLERHVTFL 300
Cdd:cd03802 167 DPEDYLAFLG--RIAPEKGLEDAIRVARRA----------GLPLKIAGKVRDE-----DYFYYL----QEPLPGPRIEFI 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 301 RSFSDRQKISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPdpvhfSEAMEKFIHK 379
Cdd:cd03802 226 GEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDS-----VEEMAEAIAN 300
|
170 180 190
....*....|....*....|....*....|....*.
gi 46395975 380 -PSLKatmGLAGKARVAEKFSADAFADQ---LYQYV 411
Cdd:cd03802 301 iDRID---RAACRRYAEDRFSAARMADRyeaLYRKV 333
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
16-406 |
7.69e-19 |
|
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: 86.91 E-value: 7.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 16 SVLFLHPDMG-IGGAERLVLDAALALQEYGCDVKIWTAHYDPNHCFIEtrelsvqcagdwLPRSLGWGGRGAAICSYVRM 94
Cdd:cd03820 1 KIAIVIPSISnAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYE------------LDDNIKIKNLGDRKYSHFKL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 95 VFLALYVL-----FLSGEEFDVVVCDQVS--ACIPVFKLARRrkrvlfychfpdLLLTQRNSALKKFYRAPIDWIEEYTT 167
Cdd:cd03820 69 LLKYFKKVrrlrkYLKNNKPDVVISFRTSllTFLALIGLKSK------------LIVWEHNNYEAYNKGLRRLLLRRLLY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 168 GMADRILVNSQYTasvfKETFKTLSHRNPDVLYpslNIGSFDLaiPEKIDDLvpkgKQFLFLSINRYERKKNLPLALRSL 247
Cdd:cd03820 137 KRADKIVVLTEAD----KLKKYKQPNSNVVVIP---NPLSFPS--EEPSTNL----KSKRILAVGRLTYQKGFDLLIEAW 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 248 VQLRNRLPsqEWDkvhLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLRSFSDRQKISLLHGCLCVlyTPSNEHF 327
Cdd:cd03820 204 ALIAKKHP--DWK---LRIYGDGPER--------EELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVL--SSRYEGF 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 328 GIVPLEAMYMQCPVIAVN-NGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARvAEKFSADAFAD 405
Cdd:cd03820 269 PMVLLEAMAYGLPIISFDcPTGPSEIIEDGENGLLVPNgDVDALAEALLRLMEDEELRKKMGKNARKN-AERFSIEKIIK 347
|
.
gi 46395975 406 Q 406
Cdd:cd03820 348 Q 348
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
20-409 |
1.15e-18 |
|
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: 87.05 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 20 LHPDMGIggaerLVLDAALALQEYGCDVKIWTahydPNHCFIETRELSVQCAGDWLP-----RSLGWGGRGAAICSYVRM 94
Cdd:cd03798 12 NSPGRGI-----FVRRQVRALSRRGVDVEVLA----PAPWGPAAARLLRKLLGEAVPprdgrRLLPLKPRLRLLAPLRAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 95 VFLALYvLFLSGEEFDVVVCDQVSACIPVFKLARRR--KRVLFYCHFPDLLLTQRNSALKKFYRapidwieeYTTGMADR 172
Cdd:cd03798 83 SLAKLL-KRRRRGPPDLIHAHFAYPAGFAAALLARLygVPYVVTEHGSDINVFPPRSLLRKLLR--------WALRRAAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 173 ILVNSQYTASVFKETFktLSHRNPDVLYpslNigSFDLAIPEKIDD-LVPKGKQFLFLSINRYERKKNLPLALRSLVQLR 251
Cdd:cd03798 154 VIAVSKALAEELVALG--VPRDRVDVIP---N--GVDPARFQPEDRgLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 252 NRLPSqewdkVHLFMAGGYDDRIPenvehykeLKKMVQESDLERHVTFLRSFSdRQKISLLHGCLCVLYTPS-NEHFGIV 330
Cdd:cd03798 227 KARPD-----VVLLIVGDGPLREA--------LRALAEDLGLGDRVTFTGRLP-HEQVPAYYRACDVFVLPSrHEGFGLV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 331 PLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPsLKATMGLAGKARVAEKFSADAFADQLYQ 409
Cdd:cd03798 293 LLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPgDADALAAALRRALAEP-YLRELGEAARARVAERFSWVKAADRIAA 371
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
17-390 |
3.87e-17 |
|
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: 82.02 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 17 VLFLHPDMGIGGAERLVLDAALALQEYGCDVKIWTAHyDPNHCFietrelsVQCAGDWLP-RSLGWGGRGAAICSYVRMv 95
Cdd:cd03819 1 ILMLTPALEIGGAETYILDLARALAERGHRVLVVTAG-GPLLPR-------LRQIGIGLPgLKVPLLRALLGNVRLARL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 96 flalyvlfLSGEEFDVVVCdQVSACIPVFKLARRRKRVlfychfpDLLLTQRNSALkkFYRAPIDWIEEYTTgMADRILV 175
Cdd:cd03819 72 --------IRRERIDLIHA-HSRAPAWLGWLASRLTGV-------PLVTTVHGSYL--ATYHPKDFALAVRA-RGDRVIA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 176 NSQYTASVFKETFKTLSHRnPDVLYPSLNIGSFDLAI-PEKIDDLVPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRL 254
Cdd:cd03819 133 VSELVRDHLIEALGVDPER-IRVIPNGVDTDRFPPEAeAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 255 PsqewdkVHLFMAGgyDDRIPENVEHYKElkkmvqESDLERHVTFLrSFSDRQKiSLLHGCLCVLYTPSNEHFGIVPLEA 334
Cdd:cd03819 212 D------FRLLVAG--DGPERDEIRRLVE------RLGLRDRVTFT-GFREDVP-AALAASDVVVLPSLHEEFGRVALEA 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 46395975 335 MYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAG 390
Cdd:cd03819 276 MACGTPVVATDVGGAREIVVHGRTGLLVPPgDAEALADAIRAAKLLPEAREKLQAAA 332
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
231-415 |
2.35e-15 |
|
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: 77.01 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 231 INRYERKKNLPLALRSLVQLRNRLPSQewdkvhLFMAGGYDDRIPenvehykeLKKMVQESDLERHVTFLRSFSDRQKIs 310
Cdd:cd04962 202 VSNFRPVKRIDDVVRVFARVRRKIPAK------LLLVGDGPERVP--------AEELARELGVEDRVLFLGKQDDVEEL- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 311 lLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVH-FSEAMEKFIHKPSLKATMGLA 389
Cdd:cd04962 267 -LSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDaMAKSALSILEDDELYNRMGRA 345
|
170 180
....*....|....*....|....*.
gi 46395975 390 GKARVAEKFSADAFADQlYQYVTKLV 415
Cdd:cd04962 346 ARKRAAERFDPERIVPQ-YEAYYRRL 370
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
20-407 |
3.65e-15 |
|
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: 76.21 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 20 LHPDMGIGGAERLVLDAALALQEYGCDVKIWTAHydpNHC-FIETRELSV----QCAGDWLPRSLGWGGRGAAICSYVRM 94
Cdd:cd03823 8 LYPPQRVGGAEISVHDLAEALVAEGHEVAVLTAG---VGPpGQATVARSVvryrRAPDETLPLALKRRGYELFETYNPGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 95 VflALYVLFLSGEEFDVVV--CDQVSACIPVFKLARRRKRVLFYCHfpDLLLTQRNSALKKfyrapidwieeyttGMADR 172
Cdd:cd03823 85 R--RLLARLLEDFRPDVVHthNLSGLGASLLDAARDLGIPVVHTLH--DYWLLCPRQFLFK--------------KGGDA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 173 ILVNSQYTASVFKETFKTLSHRNpdVLYPSLnigSFDLAIPEKIddlVPKGKQFLFLSINRYERKKNLPLALRSLvqlrN 252
Cdd:cd03823 147 VLAPSRFTANLHEANGLFSARIS--VIPNAV---EPDLAPPPRR---RPGTERLRFGYIGRLTEEKGIDLLVEAF----K 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 253 RLPSQEWdkvHLFMAGGYDDRIPEnvehykelkkmvqESDLERHVTFLrSFSDRQKISLLHGCLCVLYTPS--NEHFGIV 330
Cdd:cd03823 215 RLPREDI---ELVIAGHGPLSDER-------------QIEGGRRIAFL-GRVPTDDIKDFYEKIDVLVVPSiwPEPFGLV 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46395975 331 PLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAFADQL 407
Cdd:cd03823 278 VREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPgDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEEYLKLY 355
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
223-409 |
3.97e-15 |
|
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: 76.30 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 223 GKQFLFLSINRYERKKNLPLALRSLVQLRNRLPSQEwDKVHLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLrs 302
Cdd:TIGR03088 192 DESVVVGTVGRLQAVKDQPTLVRAFALLVRQLPEGA-ERLRLVIVGDGPAR--------GACEQMVRAAGLAHLVWLP-- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 303 fSDRQKISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKP 380
Cdd:TIGR03088 261 -GERDDVPALMQALDLFVLPSlAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPgDAVALARALQPYVSDP 339
|
170 180 190
....*....|....*....|....*....|..
gi 46395975 381 SLKATMGLAGKARVAEKFSADAFADQ---LYQ 409
Cdd:TIGR03088 340 AARRAHGAAGRARAEQQFSINAMVAAyagLYD 371
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
104-398 |
6.64e-15 |
|
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: 75.82 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 104 LSGEEFDVVVC-DQVSACIPVFKLARRRKrVLFYCHFpDLlltqRNSALKKFYRApIDWIEEYTtgmadrilvnSQYTAS 182
Cdd:cd03792 83 LLDGDADVVVIhDPQPALLPKIKKKRDRK-WIWRCHI-DI----STPLTEPQPRV-WDFLWNYI----------EGYDLF 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 183 VF--KETFKtlshrnPDVLYPSLnigsfdlAIPEKIDDLVPKGKQF--------------------LFLSINRYERKKNL 240
Cdd:cd03792 146 VFhpPEFVP------PQVPPPKF-------YIPPSIDPLSGKNKDLspadiryylekpfvidperpYILQVARFDPSKDP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 241 PLALRSLVQLRNRLPSqewdkVHLFMAGGYDDRIPENVEHYKELKKMvqeSDLERHVTFLR-SFSDRQKISLLHGCLCVL 319
Cdd:cd03792 213 LGVIDAYKLFKRRAEE-----PQLVICGHGAVDDPEGSVVYEEVMEY---AGDDHDIHVLRlPPSDQEINALQRAATVVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 320 YTPSNEHFGIVPLEAMYMQCPVIAVNNGG-PLEsIVHKVTGFLC---EPDPVHFseamEKFIHKPSLKATMGLAGKARVA 395
Cdd:cd03792 285 QLSTREGFGLTVSEALWKGKPVIATPAGGiPLQ-VIDGETGFLVnsvEGAAVRI----LRLLTDPELRRKMGLAAREHVR 359
|
...
gi 46395975 396 EKF 398
Cdd:cd03792 360 DNF 362
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
125-408 |
9.41e-15 |
|
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: 75.05 E-value: 9.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 125 KLARRRKRVLFYCHFPDLLLTQRNSAL-----KKFYRAPIDWIEEYTTGMadRILVN------SQYTASVFKETFKtlSH 193
Cdd:cd03807 73 KLIRKRNPDVVHTWMYHADLIGGLAAKlaggvKVIWSVRSSNIPQRLTRL--VRKLClllskfSPATVANSSAVAE--FH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 194 RN----PDVLYPSLN-IGSFDLAIPEKIDD-----LVPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPsqewdKVH 263
Cdd:cd03807 149 QEqgyaKNKIVVIYNgIDLFKLSPDDASRArarrrLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHP-----DLR 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 264 LFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLrsfSDRQKISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVI 342
Cdd:cd03807 224 LLLVGRGPER--------PNLERLLLELGLEDRVHLL---GERSDVPALLPAMDIFVLSSrTEGFPNALLEAMACGLPVV 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 343 AVNNGGPLEsIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAFA---DQLY 408
Cdd:cd03807 293 ATDVGGAAE-LVDDGTGFLVPAgDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVrryETLY 361
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
171-403 |
1.82e-14 |
|
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: 74.24 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 171 DRILVNSQYTASVFKETFktlsHRNPDVLYPSLNIGSFDLAiPEKIDDlvpkgkqflFLSINRYERKKNLPLALRSLvql 250
Cdd:cd03804 159 DLFIANSQFVARRIKKFY----GRESTVIYPPVDTDAFAPA-ADKEDY---------YLTASRLVPYKRIDLAVEAF--- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 251 rNRLPSQewdkvhLFMAGGYDDRipenvehyKELKKMVQesdleRHVTFLRSFSDRQKISLLHGCLCVLYtPSNEHFGIV 330
Cdd:cd03804 222 -NELPKR------LVVIGDGPDL--------DRLRAMAS-----PNVEFLGYQPDEVLKELLSKARAFVF-AAEEDFGIV 280
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46395975 331 PLEAMYMQCPVIAVNNGGPLESIVHKVTGFL-CEPDPVHFSEAMEKFIHKPSL---KATMglagkaRVAEKFSADAF 403
Cdd:cd03804 281 PVEAQACGTPVIAFGKGGALETVRPGPTGILfGEQTVESLKAAVEEFEQNFDRfkpQAIR------ANAERFSRARF 351
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
223-378 |
3.96e-14 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 69.08 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 223 GKQFLFLSiNRYERKKNLPLALRSLVQLRNRLpsqewDKVHLFMAGGYDDRipenvehykELKKMVQesDLERHVTFLRS 302
Cdd:pfam13692 1 RPVILFVG-RLHPNVKGVDYLLEAVPLLRKRD-----NDVRLVIVGDGPEE---------ELEELAA--GLEDRVIFTGF 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46395975 303 FSDrqKISLLHGC-LCVLytPSN-EHFGIVPLEAMYMQCPVIAVNNGGPLEsIVHKVTGFLCEP-DPVHFSEAMEKFIH 378
Cdd:pfam13692 64 VED--LAELLAAAdVFVL--PSLyEGFGLKLLEAMAAGLPVVATDVGGIPE-LVDGENGLLVPPgDPEALAEAILRLLE 137
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
27-407 |
4.32e-14 |
|
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: 73.17 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 27 GGAERLVLDAALALQEYGCDVKIWTahYDPNHcfietRELSVQCAGDWLPRSLGWG-------GRGAAICSYVRMVFLAL 99
Cdd:cd03821 14 GGPVKVVLRLAAALAALGHEVTIVS--TGDGY-----ESLVVEENGRYIPPQDGFAsipllrqGAGRTDFSPGLPNWLRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 100 YVLflsgeEFDVV----VCDQVSAciPVFKLARRRKRVlfYCHFP----DLLLTQRNSALKKFYRapiDWIEEYTTGMAD 171
Cdd:cd03821 87 NLR-----EYDVVhihgVWTYTSL--AACKLARRRGIP--YVVSPhgmlDPWALQQKHWKKRIAL---HLIERRNLNNAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 172 RILVNSQYTAsvfkETFKTLSHRNPDVLYP-SLNIGSFD--LAIPEKIDDLvPKGKQFLFLSinRYERKKNLPLALRSLV 248
Cdd:cd03821 155 LVHFTSEQEA----DELRRFGLEPPIAVIPnGVDIPEFDpgLRDRRKHNGL-EDRRIILFLG--RIHPKKGLDLLIRAAR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 249 QLRNRLPsqewdKVHLFMAGgYDDRipenvEHYKELKKMvQESDLERHVTFLRSFSDRQKISLLHGCLC-VLytPS-NEH 326
Cdd:cd03821 228 KLAEQGR-----DWHLVIAG-PDDG-----AYPAFLQLQ-SSLGLGDRVTFTGPLYGEAKWALYASADLfVL--PSySEN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 327 FGIVPLEAMYMQCPVIaVNNGGPLESIVHKVTGFLCEPDPVHFSEAMEKFIHKPSLKATMGLAGKARVA--EKFSADAFA 404
Cdd:cd03821 294 FGNVVAEALACGLPVV-ITDKCGLSELVEAGCGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRARQveENFSWEAVA 372
|
...
gi 46395975 405 DQL 407
Cdd:cd03821 373 GQL 375
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
227-410 |
5.47e-14 |
|
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: 72.71 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 227 LFLSINRYERKKNLPlALRSLVQlrnRLPSQewDKVHLFMAGGYDDRipenvehykelkkmvqeSDLER---HVTFLRsF 303
Cdd:cd03814 200 LLLYVGRLAPEKNLE-ALLDADL---PLAAS--PPVRLVVVGDGPAR-----------------AELEArgpDVIFTG-F 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 304 SDRQKISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPS 381
Cdd:cd03814 256 LTGEELARAYASADVFVFPSrTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPgDAAAFAAALRALLEDPE 335
|
170 180
....*....|....*....|....*....
gi 46395975 382 LKATMGLAGKARvAEKFSADAFADQLYQY 410
Cdd:cd03814 336 LRRRMAARARAE-AERYSWEAFLDNLLDY 363
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
228-362 |
1.18e-13 |
|
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: 70.13 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 228 FLSINRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLRSFSDRQ 307
Cdd:cd01635 113 KVSVGRLVPEKGIDLLLEALALLKARLP-----DLVLVLVGGGGER--------EEEEALAAALGLLERVVIIGGLVDDE 179
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 46395975 308 KISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLC 362
Cdd:cd01635 180 VLELLLAAADVFVLPSrSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
149-415 |
2.80e-12 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 68.23 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 149 SALKKFYRAPIDWIEEYTTGMADRILVNSQYTASVFKETFKTLSHrnPDVLYPSLNIGSFDlAIPEKIDDLVPKgkqflF 228
Cdd:PLN02949 200 STCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPER--IKRVYPPCDTSGLQ-ALPLERSEDPPY-----I 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 229 LSINRYERKKNLPLALRSLVQLRNRLPSQEwDKVHLFMAGGYddRIPENVEHYKELKKMVQESDLERHVTFLRSFSDRQK 308
Cdd:PLN02949 272 ISVAQFRPEKAHALQLEAFALALEKLDADV-PRPKLQFVGSC--RNKEDEERLQKLKDRAKELGLDGDVEFHKNVSYRDL 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 309 ISLLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIV-----HKvTGFLCEPDPvHFSEAMEKFIHKPSlK 383
Cdd:PLN02949 349 VRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVldedgQQ-TGFLATTVE-EYADAILEVLRMRE-T 425
|
250 260 270
....*....|....*....|....*....|...
gi 46395975 384 ATMGLAGKARV-AEKFSADAFADQLYQYVTKLV 415
Cdd:PLN02949 426 ERLEIAAAARKrANRFSEQRFNEDFKDAIRPIL 458
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
214-414 |
2.03e-11 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 65.77 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 214 EKIDDLVPKGKQFLFlSINRYERKKNLPlalrSLVQL--RN-RLPsqewDKVHLFMAGGYDDRIPEN-VEHYKELKKM-- 287
Cdd:PLN00142 563 EHIGYLKDRKKPIIF-SMARLDRVKNLT----GLVEWygKNkRLR----ELVNLVVVGGFIDPSKSKdREEIAEIKKMhs 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 288 -VQESDLERHVTFLRSFSDRQKISLLHGCLC---------VLYtpsnEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKV 357
Cdd:PLN00142 634 lIEKYNLKGQFRWIAAQTNRVRNGELYRYIAdtkgafvqpALY----EAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGV 709
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46395975 358 TGFLCepDPVHFSEAMEK---FIHK----PSLKATMGLAGKARVAEKFSADAFADQL---------YQYVTKL 414
Cdd:PLN00142 710 SGFHI--DPYHGDEAANKiadFFEKckedPSYWNKISDAGLQRIYECYTWKIYAERLltlggvygfWKYVSKL 780
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
27-188 |
5.83e-11 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 60.62 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 27 GGAERLVLDAALALQEYGCDVKIWTAHYDPNHCFIETRELSVQCAGDWLPRSLGWggrgaaicsyvRMVFLALYVLFLSG 106
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLR-----------SLAFLRRLRRLLRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 107 EEFDVVVCDQVSACIPVFKLARR--RKRVLFYCHFPDlLLTQRNSALKKFYRAPIDWIEEYTTGMADRILVNSQYTASVF 184
Cdd:pfam13439 70 ERPDVVHAHSPFPLGLAALAARLrlGIPLVVTYHGLF-PDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADEL 148
|
....
gi 46395975 185 KETF 188
Cdd:pfam13439 149 RRLY 152
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
228-407 |
8.60e-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: 62.86 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 228 FLSINRYERKKNLPLALRSLVQLRNRLPSqewdkVHLFMAGGYDDRipenvehyKELKKMVqeSDLERhVTFLRSFSDRQ 307
Cdd:cd05844 192 ILFVGRLVEKKGCDVLIEAFRRLAARHPT-----ARLVIAGDGPLR--------PALQALA--AALGR-VRFLGALPHAE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 308 KISLLHG----CLCVLYTPSN--EHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLC-EPDPVHFSEAMEKFIHKP 380
Cdd:cd05844 256 VQDWMRRaeifCLPSVTAASGdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVpEGDVDALADALQALLADR 335
|
170 180
....*....|....*....|....*..
gi 46395975 381 SLKATMGLAGKARVAEKFSADAFADQL 407
Cdd:cd05844 336 ALADRMGGAARAFVCEQFDIRVQTAKL 362
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
198-406 |
1.19e-10 |
|
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: 63.12 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 198 VLYPSLNIGSFDLAIPEKiddlvPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAGGYDdripEN 277
Cdd:cd03813 271 VIPNGIDIQRFAPAREER-----PEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMP-----DAEGWLIGPED----ED 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 278 VEHYKELKKMVQESDLERHVTFLrsfsDRQKIS--LLHGCLCVLyTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVH 355
Cdd:cd03813 337 PEYAQECKRLVASLGLENKVKFL----GFQNIKeyYPKLGLLVL-TSISEGQPLVILEAMASGVPVVATDVGSCRELIYG 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46395975 356 KV-----TGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAFADQ 406
Cdd:cd03813 412 ADdalgqAGLVVPPaDPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDS 468
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
221-407 |
1.74e-09 |
|
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: 59.00 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 221 PKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPSQEWDKVhlfmagGYDDRipenvehYKELKKMVQESDLERHVTFL 300
Cdd:cd03799 170 PLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQII------GDGDL-------KEQLQQLIQELNIGDCVKLL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 301 RSFSDRQKISLLHGCLcVLYTPS------NEHFGIVPL-EAMYMQCPVIAVNNGGPLESIVHKVTGFLC-EPDPVHFSEA 372
Cdd:cd03799 237 GWKPQEEIIEILDEAD-IFIAPSvtaadgDQDGPPNTLkEAMAMGLPVISTEHGGIPELVEDGVSGFLVpERDAEAIAEK 315
|
170 180 190
....*....|....*....|....*....|....*
gi 46395975 373 MEKFIHKPSLKATMGLAGKARVAEKFSADAFADQL 407
Cdd:cd03799 316 LTYLIEHPAIWPEMGKAGRARVEEEYDINKLNDEL 350
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
27-181 |
5.12e-09 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 55.10 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 27 GGAERLVLDAALALQEYGCDVKIWTAHYDPNHCFIETRELSVQCAgdWLPRSLGWGGRGAAICSYVRMvflalyvlfLSG 106
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRL--PVPPRPSPLADLAALRRLRRL---------LRA 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46395975 107 EEFDVVVCDQVSACIPVfKLARRRKRVLFYCHFPDLLLTQRNSALKKFYRapidWIEEYTTGMADRILVNSQYTA 181
Cdd:pfam13579 70 ERPDVVHAHSPTAGLAA-RLARRRRGVPLVVTVHGLALDYGSGWKRRLAR----ALERRLLRRADAVVVVSEAEA 139
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
224-399 |
1.05e-08 |
|
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: 56.54 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 224 KQFLFLSINRYERKKNLPLALRSLVQLRNRLPSQewdKVHLFmagGYDDripenvEHYKeLKKMVQESDLERHVT---FL 300
Cdd:cd04949 159 KSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEI---TLDIY---GYGE------EREK-LKKLIEELHLEDNVFlkgYH 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 301 RSFSDRQKISLLhgclcVLYTPSNEHFGIVPLEAMYMQCPVIAVN-NGGPLESIVHKVTGFLCEPDPVH-FSEAMEKFIH 378
Cdd:cd04949 226 SNLDQEYQDAYL-----SLLTSQMEGFGLTLMEAIGHGLPVVSYDvKYGPSELIEDGENGYLIEKNNIDaLADKIIELLN 300
|
170 180
....*....|....*....|.
gi 46395975 379 KPSLKATMGlAGKARVAEKFS 399
Cdd:cd04949 301 DPEKLQQFS-EESYKIAEKYS 320
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
225-409 |
9.94e-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: 50.52 E-value: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 225 QFLFLSINRYERKK---NLPLALRSLVQLRNRlpsqewdkVHLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLR 301
Cdd:cd04951 188 EFVILNVGRLTEAKdypNLLLAISELILSKND--------FKLLIAGDGPLR--------NELERLICNLNLVDRVILLG 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 302 SFSDrqkISLLHgCLCVLYTPSN--EHFGIVPLEAMYMQCPVIAVNNGGPLEsIVHKVTGFLCEPDPVHFSEAM-EKFIH 378
Cdd:cd04951 252 QISN---ISEYY-NAADLFVLSSewEGFGLVVAEAMACERPVVATDAGGVAE-VVGDHNYVVPVSDPQLLAEKIkEIFDM 326
|
170 180 190
....*....|....*....|....*....|.
gi 46395975 379 KPSLKATMGLAGKARvAEKFSADAFADQLYQ 409
Cdd:cd04951 327 SDEERDILGNKNEYI-AKNFSINTIVNEWER 356
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
325-409 |
1.13e-05 |
|
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: 46.94 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 325 EHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAF 403
Cdd:cd03825 274 DNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPgDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQ 353
|
....*....
gi 46395975 404 ADQ---LYQ 409
Cdd:cd03825 354 AQRyleLYK 362
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
318-399 |
2.36e-05 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 46.24 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 318 VLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGpLESIVHK----VTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGK 391
Cdd:PLN02871 334 VFVMPSeSETLGFVVLEAMASGVPVVAARAGG-IPDIIPPdqegKTGFLYTPgDVDDCVEKLETLLADPELRERMGAAAR 412
|
....*...
gi 46395975 392 ARVaEKFS 399
Cdd:PLN02871 413 EEV-EKWD 419
|
|
| PHA01633 |
PHA01633 |
putative glycosyl transferase group 1 |
209-342 |
6.38e-04 |
|
putative glycosyl transferase group 1
Pssm-ID: 107050 [Multi-domain] Cd Length: 335 Bit Score: 41.50 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 209 DLAIPEKIDDLVPKGKQFL---------FLSINRYERKKNLPLALRSLVQLRNRLPSQEwDKVHLFMAGGYD---DRIPE 276
Cdd:PHA01633 123 NFKIVENAEKLVPQLKQKLdkdfpdtikFGIVSGLTKRKNMDLMLQVFNELNTKYPDIA-KKIHFFVISHKQftqLEVPA 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46395975 277 NVEHYKELkkmvqesdlerhvtflrSFSDRQKISLLHGCLCVLYTPSN-EHFGIVPLEAMYMQCPVI 342
Cdd:PHA01633 202 NVHFVAEF-----------------GHNSREYIFAFYGAMDFTIVPSGtEGFGMPVLESMAMGTPVI 251
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
226-379 |
1.27e-03 |
|
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: 40.74 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395975 226 FLFLSINRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAGgyddripeNVEHYKELKKMVQESDLERHVTFLRSFSD 305
Cdd:cd03812 192 LVLGHVGRFNEQKNHSFLIDIFEELKKKNP-----NVKLVLVG--------EGELKEKIKEKVKELGLEDKVIFLGFRND 258
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46395975 306 RQKIsLLHgcLCVLYTPSN-EHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVHFSEAMEKFIHK 379
Cdd:cd03812 259 VSEI-LSA--MDVFLFPSLyEGLPLVAVEAQASGLPCLLSDTITKECDITNNVEFLPLNETPSTWAEKILKLIKR 330
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
332-404 |
2.36e-03 |
|
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: 40.04 E-value: 2.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46395975 332 LEAMYMQCPVIAVNNGGPLESIVHKVTGFLCE-PDPVHFSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAFA 404
Cdd:cd03818 318 LEAMACGCPVIGSDTAPVREVIRDGRNGLLVDfFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCL 391
|
|
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