|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
1-463 |
0e+00 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 945.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 1 MAIYFILYTLLTIIFAVSLSLFLSVINARKSRKRAVGFFHPYTNDGGGGERVLWCAVKAIQEENPDLDCVIFTGDHDSSS 80
Cdd:PLN02949 1 MAIWLILYHLLTSIVLLLVAIALSVLRARRSRKRAVGFFHPYTNDGGGGERVLWCAVRAIQEENPDLDCVIYTGDHDASP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 81 DSLARRAVDRFGVHLQSPPKVIHLNKRKWIEESTYPHFTMIGQSLGSVYLAWEALRMFTPLYFLDTSGYAFTYPLARIFG 160
Cdd:PLN02949 81 DSLAARARDRFGVELLSPPKVVHLRKRKWIEEETYPRFTMIGQSLGSVYLAWEALCKFTPLYFFDTSGYAFTYPLARLFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 161 CKVVCYTHYPTISLDMISRVRQRNSMYNNDASIAKSNWLSTCKLVYYRAFSWMYGMVGSCTHLAMVNSSWTKSHIEVLWR 240
Cdd:PLN02949 161 CKVVCYTHYPTISSDMISRVRDRSSMYNNDASIARSFWLSTCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 241 IPERITRVYPPCDTSGLQAFPLERSSDPPKIISVAQFRPEKAHMLQLEAFSLALEKLDADVPRPKLQFVGSCRNNSDEER 320
Cdd:PLN02949 241 IPERIKRVYPPCDTSGLQALPLERSEDPPYIISVAQFRPEKAHALQLEAFALALEKLDADVPRPKLQFVGSCRNKEDEER 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 321 LQKLKDRAVELKVDGDVQFYKNAMYRELVELLGNAVAGLHGMIDEHFGISVVEYMAAGAIPIAHNSAGPKMDIVLEEDGQ 400
Cdd:PLN02949 321 LQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVLDEDGQ 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42569790 401 KTGFLAETVEEYAEAILEIVKMNETERLKMAESARKRAARFSEQRFCEDFKTAIRPIFTGPLK 463
Cdd:PLN02949 401 QTGFLATTVEEYADAILEVLRMRETERLEIAAAARKRANRFSEQRFNEDFKDAIRPILNSASR 463
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
34-449 |
0e+00 |
|
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: 687.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 34 RAVGFFHPYTNDGGGGERVLWCAVKAIQEENPDLDCVIFTGDHDSSSDSLARRAVDRFGVHLQSPPKVIH-LNKRKWIEE 112
Cdd:cd03806 1 ITVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFlLKYRKLVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 113 STYPHFTMIGQSLGSVYLAWEALRMFTPLYFLDTSGYAFTYPLARIFG-CKVVCYTHYPTISLDMISRVRQRNSMYNNDA 191
Cdd:cd03806 81 KTYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGgCPVVAYVHYPTISTDMLNKVRSREASYNNDS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 192 SIAKSNWLSTCKLVYYRAFSWMYGMVGSCTHLAMVNSSWTKSHIEVLWRIPERITRVYPPCDTSGLQAFPLERSSDPPKI 271
Cdd:cd03806 161 TIARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPIDEKTRENQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 272 ISVAQFRPEKAHMLQLEAFSLALEKLDADVPR-PKLQFVGSCRNNSDEERLQKLKDRAVELKVDGDVQFYKNAMYRELVE 350
Cdd:cd03806 241 LSIAQFRPEKNHPLQLRAFAELLKRLPESIRSnPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDAPYEELKE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 351 LLGNAVAGLHGMIDEHFGISVVEYMAAGAIPIAHNSAGPKMDIVLEEDGQKTGFLAETVEEYAEAILEIVKMNETERLKM 430
Cdd:cd03806 321 LLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILTLSEEERLQR 400
|
410
....*....|....*....
gi 42569790 431 AESARKRAARFSEQRFCED 449
Cdd:cd03806 401 REAARSSAERFSDEEFERD 419
|
|
| ALG11_N |
pfam15924 |
ALG11 mannosyltransferase N-terminus; |
33-239 |
1.69e-138 |
|
ALG11 mannosyltransferase N-terminus;
Pssm-ID: 464944 Cd Length: 209 Bit Score: 396.07 E-value: 1.69e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 33 KRAVGFFHPYTNDGGGGERVLWCAVKAIQEENPDLDCVIFTGDHDSSSDSLARRAVDRFGVHLQSPP-KVIHLNKRKWIE 111
Cdd:pfam15924 1 KGIVGFFHPYCNAGGGGERVLWCAVRATQRRYPNAICVVYTGDIDASKEEILAKVKSRFNIELDPSRiVFVYLRKRKLVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 112 ESTYPHFTMIGQSLGSVYLAWEALRMFTPLYFLDTSGYAFTYPLARIF-GCKVVCYTHYPTISLDMISRVRQRNSMYNND 190
Cdd:pfam15924 81 ASTYPRFTLLGQSLGSIILAWEALSKLVPDVFIDTMGYAFTYPLVRLLgGCPVGAYVHYPTISTDMLSRVSSREAGYNND 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 42569790 191 ASIAKSNWLSTCKLVYYRAFSWMYGMVGSCTHLAMVNSSWTKSHIEVLW 239
Cdd:pfam15924 161 SAIASSGLLSKAKLIYYRLFALLYGLVGSFADVVMVNSSWTQNHIRSLW 209
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
267-437 |
4.46e-28 |
|
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: 108.90 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 267 DPPKIISVAQFRPEKAHMLQLEAFslalEKLDADVPRPKLQFVGscrnnsDEERLQKLKDRAVELKVDGDVQFYKNAMYR 346
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAF----ALLKEKNPNLKLVIAG------DGEEEKRLKKLAEKLGLGDNVIFLGFVSDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 347 ELVELLGNAVAGLHGMIDEHFGISVVEYMAAGAIPIAHNSAGPkMDIVleEDGqKTGFLAET--VEEYAEAILEIVKMNE 424
Cdd:pfam00534 71 DLPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGP-PEVV--KDG-ETGFLVKPnnAEALAEAIDKLLEDEE 146
|
170
....*....|...
gi 42569790 425 TeRLKMAESARKR 437
Cdd:pfam00534 147 L-RERLGENARKR 158
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
154-450 |
9.30e-27 |
|
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: 111.14 E-value: 9.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 154 PLARIF-GCKVVCYTHYPTISLDmisrvrQRNSmynndasiaksnWLStcKLvyYRA-FSWM--YGMvgSCTHLAMVNSS 229
Cdd:cd03805 108 PLLKLFrPSKILFYCHFPDQLLA------QRKS------------LLK--RL--YRKpFDWLeeFTT--GMADQIVVNSN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 230 WTKS-HIEVLWRIPERITRV-YPPCDTS-------GLQAFPLERSSDPPKIISVAQFRPEKAHMLQLEAFSLALEKLdAD 300
Cdd:cd03805 164 FTAGvFKKTFPSLAKNPPEVlYPCVDTDsfdstseDPDPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQKL-PE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 301 VPRPKLQFVGSC--RNNSDEERLQKLKDRAVELK-VDGDVQFYKNAMYRELVELLGNAVAGLHGMIDEHFGISVVEYMAA 377
Cdd:cd03805 243 FENVRLVIAGGYdpRVAENVEYLEELQRLAEELLnVEDQVLFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPLEAMYA 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42569790 378 GAIPIAHNSAGPKMDIVleeDGQkTGFLAE-TVEEYAEAILEIVKMNEtERLKMAESARKRA-ARFSEQRFCEDF 450
Cdd:cd03805 323 GKPVIACNSGGPLETVV---EGV-TGFLCEpTPEAFAEAMLKLANDPD-LADRMGAAGRKRVkEKFSREAFAERL 392
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
36-455 |
1.17e-24 |
|
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: 104.93 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 36 VGFFHPYTN-DGGGGERVLWCAVKAIQEENPDLDCVIFTGDHDsssdslARRAVDRFGVHLQSPPKVIHLNKRKWIEEst 114
Cdd:cd03801 2 ILLLSPELPpPVGGAERHVRELARALAARGHDVTVLTPADPGE------PPEELEDGVIVPLLPSLAALLRARRLLRE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 115 yphftmigqslgsvYLAWEALRMFTPLYFLDTSGYAFTYPLARIFGCKVVCYTHYPTIsldmisrvrqrnsMYNNDASIA 194
Cdd:cd03801 74 --------------LRPLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEP-------------GRLLLLLAA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 195 KSNWLSTCKLVYYRAfswmygmvgsctHLAMVNSSWTKSHI-EVLWRIPERITRVYPPCDTSGLQAF---PLERSSDPPK 270
Cdd:cd03801 127 ERRLLARAEALLRRA------------DAVIAVSEALRDELrALGGIPPEKIVVIPNGVDLERFSPPlrrKLGIPPDRPV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 271 IISVAQFRPEKAHMLQLEAFSLALEKldadVPRPKLQFVGScrnnsDEERLQKLkdRAVELKVDGDVQFYKNAMYRELVE 350
Cdd:cd03801 195 LLFVGRLSPRKGVDLLLEALAKLLRR----GPDVRLVIVGG-----DGPLRAEL--EELELGLGDRVRFLGFVPDEELPA 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 351 LLGNAVAGLHGMIDEHFGISVVEYMAAGAIPIAHNSAGPkMDIVLEEDGqktGFLAE--TVEEYAEAILEIVKmNETERL 428
Cdd:cd03801 264 LYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGL-PEVVEDGEG---GLVVPpdDVEALADALLRLLA-DPELRA 338
|
410 420
....*....|....*....|....*...
gi 42569790 429 KMAESARKR-AARFSEQRFCEDFKTAIR 455
Cdd:cd03801 339 RLGRAARERvAERFSWERVAERLLDLYR 366
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
25-448 |
1.47e-17 |
|
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: 83.95 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 25 VINARksrkravGFFHPYTndggGGERVLWCAVKAIQEENPDlDCVIFTGDHDSSSDSLARRAvdrfgvhlqsPPKVIHL 104
Cdd:cd03809 3 LIDGR-------SLAQRLT----GIGRYTRELLKALAKNDPD-ESVLAVPPLPGELLRLLREY----------PELSLGV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 105 NKRKWIEESTYPHFtmigqslgsvYLAWEALRMFTPLYFldtsGYAFTYPLaRIFGCKVVCYTHyptislDMISrvrqrn 184
Cdd:cd03809 61 IKIKLWRELALLRW----------LQILLPKKDKPDLLH----SPHNTAPL-LLKGCPQVVTIH------DLIP------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 185 smynndasIAKSNWLSTCKLVYYRafsWMYGMVGSCTHLAMVNSSWTKSHIEVLWRIPERITRVYPPCdtSGLQAFPLER 264
Cdd:cd03809 114 --------LRYPEFFPKRFRLYYR---LLLPISLRRADAIITVSEATRDDIIKFYGVPPEKIVVIPLG--VDPSFFPPES 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 265 SS--------DPPKIISVAQFRPEKAHMLQLEAFSLalekLDADVPRPKLQFVGSCRNNSDEerlqkLKDRAVELKVDGD 336
Cdd:cd03809 181 AAvliakyllPEPYFLYVGTLEPRKNHERLLKAFAL----LKKQGGDLKLVIVGGKGWEDEE-----LLDLVKKLGLGGR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 337 VQFYKNAMYRELVELLGNAVAGLHGMIDEHFGISVVEYMAAGAIPIAHNSAgpkmdiVLEEDGQKTGFL--AETVEEYAE 414
Cdd:cd03809 252 VRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNIS------VLPEVAGDAALYfdPLDPESIAD 325
|
410 420 430
....*....|....*....|....*....|....
gi 42569790 415 AILEIVkMNETERLKMAESARKRAARFSEQRFCE 448
Cdd:cd03809 326 AILRLL-EDPSLREELIRKGLERAKKFSWEKTAE 358
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
232-450 |
6.10e-14 |
|
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: 73.08 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 232 KSHIEVlwrIPERI--TRVYPPCDTSGLQAFPLerSSDPPKIISVAQFRPEKAHMLQLEAFSLALEKLDAdvprpKLQFV 309
Cdd:cd03817 168 KGPIEV---IPNGIdlDKFEKPLNTEERRKLGL--PPDEPILLYVGRLAKEKNIDFLLRAFAELKKEPNI-----KLVIV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 310 GscrnnsDEERLQKLKDRAVELKVDGDVQFYKNAMYRELVELLGNAVAGLHGMIDEHFGISVVEYMAAGaIPIAHNSAGP 389
Cdd:cd03817 238 G------DGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAG-LPVVAAKDPA 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42569790 390 KMDIVleEDGqKTGFL-AETVEEYAEAILEIVKMNETERlKMAESARKRAARFSEQRFCEDF 450
Cdd:cd03817 311 ASELV--EDG-ENGFLfEPNDETLAEKLLHLRENLELLR-KLSKNAEISAREFAFAKSVEKL 368
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
238-442 |
4.72e-13 |
|
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: 70.49 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 238 LWRIPERITRVYPPCDTSGLQAFP--LERSSDPPKIISVAQFRPEKAHMLQLEAFslalEKLDADVPRPKLQFVGscrnn 315
Cdd:cd03798 168 LGVPRDRVDVIPNGVDPARFQPEDrgLGLPLDAFVILFVGRLIPRKGIDLLLEAF----ARLAKARPDVVLLIVG----- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 316 sDEERLQKLKDRAVELKVDGDVQFyknamyreLVELLGNAVAGLHGMID--------EHFGISVVEYMAAGAIPIAHNSA 387
Cdd:cd03798 239 -DGPLREALRALAEDLGLGDRVTF--------TGRLPHEQVPAYYRACDvfvlpsrhEGFGLVLLEAMACGLPVVATDVG 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 42569790 388 GPkMDIVleeDGQKTGFLAET--VEEYAEAILEIVkMNETERLKMAESARKRAARFS 442
Cdd:cd03798 310 GI-PEVV---GDPETGLLVPPgdADALAAALRRAL-AEPYLRELGEAARARVAERFS 361
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
250-445 |
5.74e-13 |
|
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: 70.04 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 250 PPCDTSGLQAFPLERSSdpPKIISVAQFRPEKAHMLQLEAFSLALEKldadvpRPKLQFV----GSCRNNSDEERLQK-L 324
Cdd:cd03807 174 DASRARARRRLGLAEDR--RVIGIVGRLHPVKDHSDLLRAAALLVET------HPDLRLLlvgrGPERPNLERLLLELgL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 325 KDRAVELKVDGDVQFYKNAMYrelVELLGNAVAGlhgmidehFGISVVEYMAAGaIPIAHNSAGPKMDIVLEedgqKTGF 404
Cdd:cd03807 246 EDRVHLLGERSDVPALLPAMD---IFVLSSRTEG--------FPNALLEAMACG-LPVVATDVGGAAELVDD----GTGF 309
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 42569790 405 L--AETVEEYAEAILEIVKMNETeRLKMAESARKR-AARFSEQR 445
Cdd:cd03807 310 LvpAGDPQALADAIRALLEDPEK-RARLGRAARERiANEFSIDA 352
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
265-443 |
1.28e-12 |
|
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: 68.48 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 265 SSDPPKIISVAQFRPEKAHMLQLEAFSLALEKldadVPRPKLQFVGscrnnSDEERlQKLKDRAVELKVDGDVQFYKNAm 344
Cdd:cd04949 157 ERKSNKIITISRLAPEKQLDHLIEAVAKAVKK----VPEITLDIYG-----YGEER-EKLKKLIEELHLEDNVFLKGYH- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 345 yRELVELLGNAVAGLHGMIDEHFGISVVEYMAAGAIPIAHN-SAGPKmDIVleEDGqKTGFLAET--VEEYAEAILEIVK 421
Cdd:cd04949 226 -SNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDvKYGPS-ELI--EDG-ENGYLIEKnnIDALADKIIELLN 300
|
170 180
....*....|....*....|..
gi 42569790 422 mNETERLKMAESARKRAARFSE 443
Cdd:cd04949 301 -DPEKLQQFSEESYKIAEKYST 321
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
340-457 |
2.32e-12 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 63.86 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 340 YKNamYRELVE-LLGNAVAGLHGMIDEHFGISVVEYMAAGAIPIAHNSAGPKmDIVLEEDgqkTGFL--AETVEEYAEAI 416
Cdd:COG0438 7 RKG--LDLLLEaLLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLP-EVIEDGE---TGLLvpPGDPEALAEAI 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 42569790 417 LEIVKmNETERLKMAESARKRAA-RFSEQRFCEDFKTAIRPI 457
Cdd:COG0438 81 LRLLE-DPELRRRLGEAARERAEeRFSWEAIAERLLALYEEL 121
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
239-452 |
1.06e-11 |
|
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: 66.11 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 239 WRIPERITRVYPPCDtsglqaFPLERSSDPPK---IISVAQFRPEKAHMLQLEAFSLALEKldadvpRP--KLQFVGSCr 313
Cdd:cd03820 155 KQPNSNVVVIPNPLS------FPSEEPSTNLKskrILAVGRLTYQKGFDLLIEAWALIAKK------HPdwKLRIYGDG- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 314 nnSDEERLQKLkdrAVELKVdgdvqfyknamyRELVELLGNAVAglhgmIDEH---------------FGISVVEYMAAG 378
Cdd:cd03820 222 --PEREELEKL---IDKLGL------------EDRVKLLGPTKN-----IAEEyanssifvlssryegFPMVLLEAMAYG 279
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42569790 379 AIPIAHNS-AGPKmDIVleEDGqKTGFLAET--VEEYAEAILEIVKmNETERLKMAESARKRAARFSEQRFCEDFKT 452
Cdd:cd03820 280 LPIISFDCpTGPS-EII--EDG-ENGLLVPNgdVDALAEALLRLME-DEELRKKMGKNARKNAERFSIEKIIKQWEE 351
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
265-449 |
5.19e-11 |
|
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: 63.77 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 265 SSDPPKIISVAQFRPEKAHMLQLEAFslalEKLDADVPRPKLQFVGSC-RNNSDEERLQKLKDravelkvDGDVQFYKna 343
Cdd:cd03808 186 PSEKVVFLFVARLLKDKGIDELIEAA----KILKKKGPNVRFLLVGDGeLENPSEILIEKLGL-------EGRIEFLG-- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 344 mYRELV-ELLGNAVAGLHGMIDEHFGISVVEYMAAGaIP-IAHNSAGPKmDIVleEDGQkTGFLAET--VEEYAEAILEI 419
Cdd:cd03808 253 -FRSDVpELLAESDVFVLPSYREGLPRSLLEAMAAG-RPvITTDVPGCR-ELV--IDGV-NGFLVPPgdVEALADAIEKL 326
|
170 180 190
....*....|....*....|....*....|
gi 42569790 420 VkMNETERLKMAESARKRAarfsEQRFCED 449
Cdd:cd03808 327 I-EDPELRKEMGEAARKRV----EEKFDEE 351
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
272-399 |
1.98e-09 |
|
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: 57.80 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 272 ISVAQFRPEKAHMLQLEAFSLALEKLdadvPRPKLQFVGscrnnsDEERLQKLKDRAVELKVDGDVQFYKNAMYRELVEL 351
Cdd:cd01635 114 VSVGRLVPEKGIDLLLEALALLKARL----PDLVLVLVG------GGGEREEEEALAAALGLLERVVIIGGLVDDEVLEL 183
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 42569790 352 LGNAV-AGLHGMIDEHFGISVVEYMAAGAIPIAHNSAGPKMDIVLEEDG 399
Cdd:cd01635 184 LLAAAdVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENG 232
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
329-457 |
5.09e-09 |
|
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: 57.68 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 329 VELKVDGDVQFYKNAMYRELVELLGNAVAGLHgMI--DEHFGISVVEYMAAGAIPIAHNSAGPKmDIVleEDGqKTGFLA 406
Cdd:cd03802 214 QEPLPGPRIEFIGEVGHDEKQELLGGARALLF-PInwDEPFGLVMIEAMACGTPVIAYRRGGLP-EVI--QHG-ETGFLV 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 42569790 407 ETVEEYAEAILEIVKMNeteRLKMAESARKraaRFSEQRFCEDFKTAIRPI 457
Cdd:cd03802 289 DSVEEMAEAIANIDRID---RAACRRYAED---RFSAARMADRYEALYRKV 333
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
225-451 |
8.48e-09 |
|
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: 56.91 E-value: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 225 MVNSSWTKSHIEVLWRIPERItrVYPPCDTSGLQafPLERSSDppKIISVAQFRPEKAHMLQLEAFslalekldADVPRP 304
Cdd:cd03804 162 IANSQFVARRIKKFYGRESTV--IYPPVDTDAFA--PAADKED--YYLTASRLVPYKRIDLAVEAF--------NELPKR 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 305 kLQFVGscrnnsDEERLQKLKDRAvelkvDGDVQFYKNAMYRELVELLGNAVAGLHgMIDEHFGISVVEYMAAGAIPIAH 384
Cdd:cd03804 228 -LVVIG------DGPDLDRLRAMA-----SPNVEFLGYQPDEVLKELLSKARAFVF-AAEEDFGIVPVEAQACGTPVIAF 294
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 385 NSAGPKmDIVLeedGQKTGFLAEtvEEYAEAILEIVkmNETERLKMA---ESARKRAARFSEQRFCEDFK 451
Cdd:cd03804 295 GKGGAL-ETVR---PGPTGILFG--EQTVESLKAAV--EEFEQNFDRfkpQAIRANAERFSRARFRQEIR 356
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
226-446 |
8.63e-09 |
|
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: 56.98 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 226 VNSSWTKSH-IEVLWRIPERITRVYPPCDTSGLQAFPLERSS----DPPKIISVAQFRPEKAHMLQLEAFslalEKLDAD 300
Cdd:cd03811 141 CVSKGIKEDlIRLGPSPPEKIEVIYNPIDIDRIRALAKEPILnepeDGPVILAVGRLDPQKGHDLLIEAF----AKLRKK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 301 VPRPKLQFVGscrNNSDEERLQKLkdrAVELKVDGDVQFY---KNAmyrelVELLGNAVAGLHGMIDEHFGISVVEYMAA 377
Cdd:cd03811 217 YPDVKLVILG---DGPLREELEKL---AKELGLAERVIFLgfqSNP-----YPYLKKADLFVLSSRYEGFPNVLLEAMAL 285
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 378 GAIPIAHNSAGPKmDIVleeDGQKTGFLAETV-EEYAEAILEIVKMNETERLKMAESARKRAARFSEQRF 446
Cdd:cd03811 286 GTPVVSTDCPGPR-EIL---DDGENGLLVPDGdAAALAGILAALLQKKLDAALRERLAKAQEAVFREYTI 351
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
268-421 |
1.12e-08 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 53.67 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 268 PPKIISVAQFRPE-KAHMLQLEAFSLALEKlDADVprpKLQFVGSCRNNSDEERLQKLKDRaVELKvdGDVQfyknamyr 346
Cdd:pfam13692 1 RPVILFVGRLHPNvKGVDYLLEAVPLLRKR-DNDV---RLVIVGDGPEEELEELAAGLEDR-VIFT--GFVE-------- 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42569790 347 ELVELLGNAVAGLHGMIDEHFGISVVEYMAAGAIPIAHNSAGPKmDIVLEEdgqkTGFLAET--VEEYAEAILEIVK 421
Cdd:pfam13692 66 DLAELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIP-ELVDGE----NGLLVPPgdPEALAEAILRLLE 137
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
233-448 |
2.47e-08 |
|
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: 55.71 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 233 SHIEVlwrIPE--RITRVYPPcDTSGLQAFPLERSSDPPKIISVAQFRPEKAHMLQLEAFSlALEKLDadvPRPKLQFVG 310
Cdd:cd03800 187 SRINV---VPPgvDLERFFPV-DRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFA-QLPELR---ELANLVLVG 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 311 SCRNNSDEERLQKLKDRAVELKVDGDVQFYKNAMYRELVELLgnAVAGLHGM--IDEHFGISVVEYMAAGAIPIAHNSAG 388
Cdd:cd03800 259 GPSDDPLSMDREELAELAEELGLIDRVRFPGRVSRDDLPELY--RAADVFVVpsLYEPFGLTAIEAMACGTPVVATAVGG 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42569790 389 PKmDIVleEDGQkTGFLAE--TVEEYAEAILEIVKMNETERlKMAESARKRA-ARFSEQRFCE 448
Cdd:cd03800 337 LQ-DIV--RDGR-TGLLVDphDPEALAAALRRLLDDPALWQ-RLSRAGLERArAHYTWESVAD 394
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
287-451 |
6.60e-08 |
|
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: 54.27 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 287 LEAFSLALEKLDAdvprpKLQFVGSCRnnsDEERLQKLkdraVELKVDGDVQFYKNAMYRELVELLGNAVAGLHGMIDEH 366
Cdd:cd03794 236 LEAAERLKRRPDI-----RFLFVGDGD---EKERLKEL----AKARGLDNVTFLGRVPKEEVPELLSAADVGLVPLKDNP 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 367 FGISVV-----EYMAAGaIPIAhNSAGPKMDIVLEEDGqkTGFLAET--VEEYAEAILEIvKMNETERLKMAESARKRAA 439
Cdd:cd03794 304 ANRGSSpsklfEYMAAG-KPIL-ASDDGGSDLAVEING--CGLVVEPgdPEALADAILEL-LDDPELRRAMGENGRELAE 378
|
170
....*....|...
gi 42569790 440 -RFSEQRFCEDFK 451
Cdd:cd03794 379 eKFSREKLADRLL 391
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
271-445 |
1.37e-07 |
|
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: 53.51 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 271 IISVAQFRPEKAHMLQLEAFSLALEKLDAdvprpKLQFVGSCRNNSDEERLqklkdrAVELKVDGDVQFYKNamYRELVE 350
Cdd:cd04962 199 VIHVSNFRPVKRIDDVVRVFARVRRKIPA-----KLLLVGDGPERVPAEEL------ARELGVEDRVLFLGK--QDDVEE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 351 LLGNAVAGLHGMIDEHFGISVVEYMAAGAIPIAHNSAGPKMDIVleeDGQkTGFL-----AETVEEYAEAILEivkmNET 425
Cdd:cd04962 266 LLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVK---HGE-TGFLsdvgdVDAMAKSALSILE----DDE 337
|
170 180
....*....|....*....|.
gi 42569790 426 ERLKMAESARKRAA-RFSEQR 445
Cdd:cd04962 338 LYNRMGRAARKRAAeRFDPER 358
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
207-450 |
3.26e-07 |
|
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: 52.30 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 207 YRAFSWMYGMVgsctHLAMVNSSWTKSHIEvlWRIPERITRVYPPCDTsglQAF-PLERSSDP---------PKIISVAQ 276
Cdd:cd03814 136 WAYLRWFHNPF----DTTLVPSPSIARELE--GHGFERVRLWPRGVDT---ELFhPSRRDAALrrrlgppgrPLLLYVGR 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 277 FRPEKahmlQLEAFSLALEKLdADVPRPKLQFVGScrnNSDEERLQklkdravelkvdgdvQFYKNAMY------RELVE 350
Cdd:cd03814 207 LAPEK----NLEALLDADLPL-AASPPVRLVVVGD---GPARAELE---------------ARGPDVIFtgfltgEELAR 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 351 LLGNAVAGLHGMIDEHFGISVVEYMAAGAIPIAHNSAGPKmDIVleeDGQKTGFLAE--TVEEYAEAILEIVkMNETERL 428
Cdd:cd03814 264 AYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPR-DIV---RPGGTGALVEpgDAAAFAAALRALL-EDPELRR 338
|
250 260
....*....|....*....|..
gi 42569790 429 KMAESARKRAARFSEQRFCEDF 450
Cdd:cd03814 339 RMAARARAEAERYSWEAFLDNL 360
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
247-437 |
3.74e-06 |
|
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: 48.86 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 247 RVYPPCDTSGLQAFPLERSSDPPKIISVAQFRPEKAHMLQLEAFSLALEKLDAdvprPKLQFVGScrNNSDEERLQKLKD 326
Cdd:cd03792 176 KDLSPADIRYYLEKPFVIDPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEE----PQLVICGH--GAVDDPEGSVVYE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 327 RAVELK-VDGDVQFYK-NAMYRELVELLGNAVAGLHGMIDEHFGISVVEYMAAGAIPIAHNSAGPKMDIvleEDGqKTGF 404
Cdd:cd03792 250 EVMEYAgDDHDIHVLRlPPSDQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQV---IDG-ETGF 325
|
170 180 190
....*....|....*....|....*....|...
gi 42569790 405 LAETVEEYAEAILEIVKmNETERLKMAESARKR 437
Cdd:cd03792 326 LVNSVEGAAVRILRLLT-DPELRRKMGLAAREH 357
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
231-439 |
1.98e-05 |
|
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: 46.58 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 231 TKSHIEVLW-RIPERITRVYPPCDTSGLQAFPLER-------SSDPPKIISVAQFRPEKAHmlqlEAFSLALEKLDaDVP 302
Cdd:cd03819 137 VRDHLIEALgVDPERIRVIPNGVDTDRFPPEAEAEeraqlglPEGKPVVGYVGRLSPEKGW----LLLVDAAAELK-DEP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 303 RPKLQFVGscrnnsDEERLQKLKDRAVELKVDGDVQFyknAMYRELV-ELLGNAVAGLHGMIDEHFGISVVEYMAAGAIP 381
Cdd:cd03819 212 DFRLLVAG------DGPERDEIRRLVERLGLRDRVTF---TGFREDVpAALAASDVVVLPSLHEEFGRVALEAMACGTPV 282
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 382 IAHNSAGPkMDIVLEEdgqKTGFLAE--TVEEYAEAILEIVKMNEtERLKMAESARKRAA 439
Cdd:cd03819 283 VATDVGGA-REIVVHG---RTGLLVPpgDAEALADAIRAAKLLPE-AREKLQAAAALTEA 337
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
365-442 |
4.81e-04 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 42.39 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 365 EHFGISVVEYMAAGaIPIAHNSAGPKMDIVLEEDGQKTGFLAET--VEEYAEAILEIVKmNETERLKMAESARKRAARFS 442
Cdd:PLN02871 342 ETLGFVVLEAMASG-VPVVAARAGGIPDIIPPDQEGKTGFLYTPgdVDDCVEKLETLLA-DPELRERMGAAAREEVEKWD 419
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
365-450 |
1.89e-03 |
|
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: 40.43 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569790 365 EHFGISVVEYMAAGaIPIAHNSAGPKMDIVLEEDGQKTgflAETVEEYAEAILEIVKmNETERLKMAESARKraARFSEQ 444
Cdd:cd03821 292 ENFGNVVAEALACG-LPVVITDKCGLSELVEAGCGVVV---DPNVSSLAEALAEALR-DPADRKRLGEMARR--ARQVEE 364
|
....*.
gi 42569790 445 RFCEDF 450
Cdd:cd03821 365 NFSWEA 370
|
|
| |
