|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
72-529 |
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: 603.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 72 KVFGFFHPYCNAGGGGEKVLWKAVDITLRKDAKNVIVIYSGDFVngenVTPENILNNVKAKFDYDLDSDRIFFISLKLRY 151
Cdd:cd03806 1 ITVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTD----SSPEEILEKVESRFNIDLDSPRIVFFLLKYRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 152 LVDSSTWKHFTLIGQAIGSMILAFESIIQCPPDIWIDTMGYPFSYPiIARFLRRIPIVTYTHYPIMSKDMLNKLFKMP-- 229
Cdd:cd03806 77 LVEAKTYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYP-LVRLLGGCPVVAYVHYPTISTDMLNKVRSREas 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 230 --------KKGIKVYGKILYWKVFMLIYQSIGSKIDIVITNSTWTNNHIKQIWQSNT-CKIIYPPCSTEKLVDWKQKfgt 300
Cdd:cd03806 156 ynndstiaRSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIkPSIVYPPCDTEELTKLPID--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 301 aKGERLNQAIVLAQFRPEKRHKLIIESFATFLKNLPDSV-SPIKLIMAGSTRSKQDENYVKSLQDwsENVLKIPKHLISF 379
Cdd:cd03806 233 -EKTRENQILSIAQFRPEKNHPLQLRAFAELLKRLPESIrSNPKLVLIGSCRNEEDKERVEALKL--LAKELILEDSVEF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 380 EKNLPFDKIEILLNKSTFGVNAMWNEHFGIAVVEYMASGLIPIVHASAGPLLDIVTPWdangnigkappqwelqkkyfak 459
Cdd:cd03806 310 VVDAPYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPW---------------------- 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 460 ledDGETTGFFFKEPSDPDYNttkdplrypnlsdlFLQITKLDYDcLRVMGARNQQYSLYKFSDLKFDKD 529
Cdd:cd03806 368 ---DGGPTGFLASTPEEYAEA--------------IEKILTLSEE-ERLQRREAARSSAERFSDEEFERD 419
|
|
| ALG11_N |
pfam15924 |
ALG11 mannosyltransferase N-terminus; |
72-274 |
3.89e-115 |
|
ALG11 mannosyltransferase N-terminus;
Pssm-ID: 464944 Cd Length: 209 Bit Score: 339.45 E-value: 3.89e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 72 KVFGFFHPYCNAGGGGEKVLWKAVDITLRKDAKNVIVIYSGDFvngeNVTPENILNNVKAKFDYDLDSDRIFFISLKLRY 151
Cdd:pfam15924 2 GIVGFFHPYCNAGGGGERVLWCAVRATQRRYPNAICVVYTGDI----DASKEEILAKVKSRFNIELDPSRIVFVYLRKRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 152 LVDSSTWKHFTLIGQAIGSMILAFESIIQCPPDIWIDTMGYPFSYPiIARFLRRIPIVTYTHYPIMSKDMLNKLFKMP-- 229
Cdd:pfam15924 78 LVEASTYPRFTLLGQSLGSIILAWEALSKLVPDVFIDTMGYAFTYP-LVRLLGGCPVGAYVHYPTISTDMLSRVSSREag 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1730730 230 --------KKGIKVYGKILYWKVFMLIYQSIGSKIDIVITNSTWTNNHIKQIW 274
Cdd:pfam15924 157 ynndsaiaSSGLLSKAKLIYYRLFALLYGLVGSFADVVMVNSSWTQNHIRSLW 209
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
73-469 |
1.31e-91 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 288.56 E-value: 1.31e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 73 VFGFFHPYCNAGGGGEKVLWKAVDITLRKDAKNVIVIYSGDfvngENVTPENILNNVKAKFDYDLDSDrIFFISLKLRYL 152
Cdd:PLN02949 35 AVGFFHPYTNDGGGGERVLWCAVRAIQEENPDLDCVIYTGD----HDASPDSLAARARDRFGVELLSP-PKVVHLRKRKW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 153 VDSSTWKHFTLIGQAIGSMILAFESIIQCPPDIWIDTMGYPFSYPIiARfLRRIPIVTYTHYPIMSKDMLNKLfkmpKKG 232
Cdd:PLN02949 110 IEEETYPRFTMIGQSLGSVYLAWEALCKFTPLYFFDTSGYAFTYPL-AR-LFGCKVVCYTHYPTISSDMISRV----RDR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 233 IKVY--------------GKILYWKVFMLIYQSIGSKIDIVITNSTWTNNHIKQIWQ-SNTCKIIYPPCSTEKLvdwkQK 297
Cdd:PLN02949 184 SSMYnndasiarsfwlstCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRiPERIKRVYPPCDTSGL----QA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 298 FGTAKGERLNQAIVLAQFRPEKRHKLIIESFATFLKNLPDSVSPIKLIMAGSTRSKQDENYVKSLQDWSENvLKIPKHlI 377
Cdd:PLN02949 260 LPLERSEDPPYIISVAQFRPEKAHALQLEAFALALEKLDADVPRPKLQFVGSCRNKEDEERLQKLKDRAKE-LGLDGD-V 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 378 SFEKNLPFDKIEILLNKSTFGVNAMWNEHFGIAVVEYMASGLIPIVHASAGPLLDIVtpwdangnigkappqwelqkkyf 457
Cdd:PLN02949 338 EFHKNVSYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIV----------------------- 394
|
410
....*....|..
gi 1730730 458 akLEDDGETTGF 469
Cdd:PLN02949 395 --LDEDGQQTGF 404
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
307-466 |
1.75e-22 |
|
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: 93.88 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 307 NQAIVLAQFRPEKRHKLIIESFATFLKNLPDsvspIKLIMAGstrskqDENYVKSLQDWSENVLKIPKHLISFEKNLPfD 386
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPN----LKLVIAG------DGEEEKRLKKLAEKLGLGDNVIFLGFVSDE-D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 387 KIEILLNKSTFGVNAMWnEHFGIAVVEYMASGLIPIVHAsAGPLLDIVTPWDaNGNIGKaPPQWELQKKYFAKLEDDGET 466
Cdd:pfam00534 72 LPELLKIADVFVLPSRY-EGFGIVLLEAMACGLPVIASD-VGGPPEVVKDGE-TGFLVK-PNNAEALAEAIDKLLEDEEL 147
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
177-436 |
1.65e-16 |
|
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: 81.43 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 177 SIIQCPPDIWIDTMGYPFSYPIIARFLRRIPIVTYTHYPImsKDMLNKLFKMPKKGIKVYGKILywkvfmliyqsigSKI 256
Cdd:cd03801 77 LLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAE--PGRLLLLLAAERRLLARAEALL-------------RRA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 257 DIVITNSTWTNNHIKQIWQSNTCKI--IYPPCSTEKL-VDWKQKFGTAKGERLnqAIVLAQFRPEKRHKLIIESFAtflk 333
Cdd:cd03801 142 DAVIAVSEALRDELRALGGIPPEKIvvIPNGVDLERFsPPLRRKLGIPPDRPV--LLFVGRLSPRKGVDLLLEALA---- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 334 NLPDSVSPIKLIMAGStrskqDENYVKSLQDWSenvLKIPKHlISFEKNLPFDKIEILLNKSTFGVNAMWNEHFGIAVVE 413
Cdd:cd03801 216 KLLRRGPDVRLVIVGG-----DGPLRAELEELE---LGLGDR-VRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLE 286
|
250 260
....*....|....*....|...
gi 1730730 414 YMASGLiPIVHASAGPLLDIVTP 436
Cdd:cd03801 287 AMAAGL-PVVATDVGGLPEVVED 308
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
201-435 |
4.49e-15 |
|
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: 77.24 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 201 RFLRRIPIVTYTHYPimskDMLnkLfkMPKKGIKvygKILYWKVFMLIYQSIGSKIDIVITNSTWTNNHIKQIWQS---N 277
Cdd:cd03805 111 KLFRPSKILFYCHFP----DQL--L--AQRKSLL---KRLYRKPFDWLEEFTTGMADQIVVNSNFTAGVFKKTFPSlakN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 278 TCKIIYPPCSTEKLVDWKQKFGTAKGERLNQAIV---LAQFRPEKRHKLIIESFATFLKNLPDSvSPIKLIMAGSTRSKQ 354
Cdd:cd03805 180 PPEVLYPCVDTDSFDSTSEDPDPGDLIAKSNKKFflsINRFERKKNIALAIEAFAKLKQKLPEF-ENVRLVIAGGYDPRV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 355 DEN--YVKSLQDWSENvLKIPKHLISFEKNLPFDKIEILLNKSTFGVNAMWNEHFGIAVVEYMASGLIPIVHASAGPLLD 432
Cdd:cd03805 259 AENveYLEELQRLAEE-LLNVEDQVLFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLET 337
|
...
gi 1730730 433 IVT 435
Cdd:cd03805 338 VVE 340
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
221-440 |
1.19e-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: 70.51 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 221 MLNKLFKMPKKGIKVYGKILYwKVFMLIYQSIGSKIDIVITNSTW--TNNHIKQIWQSNTcKIIY----PPCSTEKLVDW 294
Cdd:cd01635 21 ALARALAALGHEVTVLALLLL-ALRRILKKLLELKPDVVHAHSPHaaALAALLAARLLGI-PIVVtvhgPDSLESTRSEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 295 KQKFGTAKGERLNQAIVLAQFRPEKRHKLIIESFATFLKNLPDsvspIKLIMAGSTRSKQDENYVKSLQDWSENVLKIpk 374
Cdd:cd01635 99 LALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALLKARLPD----LVLVLVGGGGEREEEEALAAALGLLERVVII-- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730730 375 hlisfEKNLPFDKIEILLNKSTFGVNAMWNEHFGIAVVEYMASGLIPIVHASAGPLLDIVTPWDAN 440
Cdd:cd01635 173 -----GGLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
209-436 |
1.03e-07 |
|
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: 54.21 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 209 VTYTHYPI----------MSKDMLNKLFKMPKKGIkVYGKILYWKVfmliyqSIGSKIDIVITNSTWTNNHIKQIWQsNT 278
Cdd:cd03804 108 VCYVHSPIryawdlyhqyLAESGLGKGIKSLLASL-FLHYLRLWDV------RTAQRVDLFIANSQFVARRIKKFYG-RE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 279 CKIIYPPCSTEKLvdwkqkfgTAKGERLNQAIVLAQFRPEKRHKLIIESFATflknlpdsvSPIKLIMAGStrsKQDENY 358
Cdd:cd03804 180 STVIYPPVDTDAF--------APAADKEDYYLTASRLVPYKRIDLAVEAFNE---------LPKRLVVIGD---GPDLDR 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730730 359 VKSLQdwSENVLKIPKhlisfeknLPFDKIEILLNKSTFGVnAMWNEHFGIAVVEYMASGlIPIVHASAGPLLDIVTP 436
Cdd:cd03804 240 LRAMA--SPNVEFLGY--------QPDEVLKELLSKARAFV-FAAEEDFGIVPVEAQACG-TPVIAFGKGGALETVRP 305
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
137-439 |
1.31e-06 |
|
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: 50.82 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 137 LDSDRIFFISLKLR--YLVDSSTWKHFTLIGQAIGSMILAFESIIQCPPDIWIDTMGYPFSYPIIA-RFLRRIPIVTYTH 213
Cdd:cd03809 30 NDPDESVLAVPPLPgeLLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKPDLLHSPHNTApLLLKGCPQVVTIH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 214 ypimskDMLnkLFKMPKKGIKVYGKILYWKVFMLIYQSigskiDIVITNSTWTNNHIKQI--WQSNTCKIIYPPCSTEKL 291
Cdd:cd03809 110 ------DLI--PLRYPEFFPKRFRLYYRLLLPISLRRA-----DAIITVSEATRDDIIKFygVPPEKIVVIPLGVDPSFF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 292 VDWKQKFGTAKGERLNQ-AIVLAQFRPEKRHKLIIESFatflKNLPDSVSPIKLIMAGStRSKQDENYVKSLQDWsenvl 370
Cdd:cd03809 177 PPESAAVLIAKYLLPEPyFLYVGTLEPRKNHERLLKAF----ALLKKQGGDLKLVIVGG-KGWEDEELLDLVKKL----- 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730730 371 KIPKHLIsFEKNLPFDKIEILLNKSTFGVNAMWNEHFGIAVVEYMASGLiPIVhASAGPLLDIVTPWDA 439
Cdd:cd03809 247 GLGGRVR-FLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGT-PVI-ASNISVLPEVAGDAA 312
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
388-534 |
2.23e-05 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 43.83 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 388 IEILLNKSTFGVNAMWNEHFGIAVVEYMASGLiPIVHASAGPLLDIVTpwdangnigkappqwelqkkyfakledDGEtT 467
Cdd:COG0438 14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGL-PVIATDVGGLPEVIE---------------------------DGE-T 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730730 468 GFFFkEPSDPDynttkdplrypnlsDLFLQITKL--DYDCLRVMGARNQQYSLYKFSdlkfdkdWENFV 534
Cdd:COG0438 65 GLLV-PPGDPE--------------ALAEAILRLleDPELRRRLGEAARERAEERFS-------WEAIA 111
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
183-434 |
1.03e-04 |
|
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: 44.62 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 183 PDIWIDTMGYPFSYPIIARFLRRIPIVtythypIMSKDMLNKLFKMPKKGIKVYGKILYWKVFmLIYQSIGSKIDivitn 262
Cdd:cd03807 80 PDVVHTWMYHADLIGGLAAKLAGGVKV------IWSVRSSNIPQRLTRLVRKLCLLLSKFSPA-TVANSSAVAEF----- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 263 stwtnnHIKQIWQSNTCKIIY-----------PPCSTEKlvdwKQKFGTAKGERLnqAIVLAQFRPEKRHKLIIESFATF 331
Cdd:cd03807 148 ------HQEQGYAKNKIVVIYngidlfklspdDASRARA----RRRLGLAEDRRV--IGIVGRLHPVKDHSDLLRAAALL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 332 LKNLPDsvspIKLIMAGSTRSKQD---ENYVKSLQDwseNVlkipkHLISFEKNLPfdkieILLNKSTFGVNAMWNEHFG 408
Cdd:cd03807 216 VETHPD----LRLLLVGRGPERPNlerLLLELGLED---RV-----HLLGERSDVP-----ALLPAMDIFVLSSRTEGFP 278
|
250 260
....*....|....*....|....*.
gi 1730730 409 IAVVEYMASGLiPIVHASAGPLLDIV 434
Cdd:cd03807 279 NALLEAMACGL-PVVATDVGGAAELV 303
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
299-436 |
1.52e-04 |
|
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: 44.29 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 299 GTAKGERLNQAIVL--AQFRPEKRHKLIIESFATFLKNLPDsvspIKLIMAGSTRSKQdenyvkSLQDWSENVLKIPKhl 376
Cdd:cd03798 191 DRGLGLPLDAFVILfvGRLIPRKGIDLLLEAFARLAKARPD----VVLLIVGDGPLRE------ALRALAEDLGLGDR-- 258
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 377 ISFEKNLPFDKIEILLNKSTFGVNAMWNEHFGIAVVEYMASGLiPIVHASAGPLLDIVTP 436
Cdd:cd03798 259 VTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGL-PVVATDVGGIPEVVGD 317
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
84-438 |
2.20e-04 |
|
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: 43.50 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 84 GGGGEKVLwKAVDITLRKDAKNV-IVIYSGDFVNGENVTPENILNNVKAKFDYDLdSDRIFFISLKLRYLvdsstwkhft 162
Cdd:cd03811 11 GGGAERVL-LNLANALDKRGYDVtLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLI-KLGLLKAILKLKRI---------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 163 ligqaigsmilafesIIQCPPDIWIDTMGypfSYPIIARFL--RRIPIVTYTHYPIMSKDMLNKLFKMPKKGIKvygkil 240
Cdd:cd03811 79 ---------------LKRAKPDVVISFLG---FATYIVAKLaaARSKVIAWIHSSLSKLYYLKKKLLLKLKLYK------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 241 ywkvfmliyqsigsKIDIVITNSTWTNNHIKQIWQSNTCKI--IYPPcsteklVDWKQKFGTAK----GERLNQAIVLAQ 314
Cdd:cd03811 135 --------------KADKIVCVSKGIKEDLIRLGPSPPEKIevIYNP------IDIDRIRALAKepilNEPEDGPVILAV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 315 FR--PEKRHKLIIESFATFLKNLPDsvspIKLIMAGSTRSKQD-ENYVKSLqDWSENVlkipkHLISFEKNlPFDkieiL 391
Cdd:cd03811 195 GRldPQKGHDLLIEAFAKLRKKYPD----VKLVILGDGPLREElEKLAKEL-GLAERV-----IFLGFQSN-PYP----Y 259
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1730730 392 LNKSTFGVNAMWNEHFGIAVVEYMASGlIPIVHASAGPLLDIVTPWD 438
Cdd:cd03811 260 LKKADLFVLSSRYEGFPNVLLEAMALG-TPVVSTDCPGPREILDDGE 305
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
135-423 |
2.93e-04 |
|
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: 43.38 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 135 YDLDsDRIFFISLKLRYLVDSSTWKHFTLIGQAIgSMILAFESiiqcpPDIWIDTMGYPFSypIIARFLRRIPIVTYTHY 214
Cdd:cd03820 47 YELD-DNIKIKNLGDRKYSHFKLLLKYFKKVRRL-RKYLKNNK-----PDVVISFRTSLLT--FLALIGLKSKLIVWEHN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 215 PImskdmlnklfkmpkkgiKVYGKILYWK-VFMLIYQsigsKIDIVITNSTWTNNHIKQIWQSNTCKI--IYPPCSTEKL 291
Cdd:cd03820 118 NY-----------------EAYNKGLRRLlLRRLLYK----RADKIVVLTEADKLKKYKQPNSNVVVIpnPLSFPSEEPS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 292 VDWKQKfgtakgerlnqaIVLAQFR--PEKRHKLIIESFATFLKNLPDsvspIKLIMAGS--TRSKQdENYVKSLQdWSE 367
Cdd:cd03820 177 TNLKSK------------RILAVGRltYQKGFDLLIEAWALIAKKHPD----WKLRIYGDgpEREEL-EKLIDKLG-LED 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1730730 368 NVlkipkHLISFEKNLpfdkIEILLNKSTFGVNAMWnEHFGIAVVEYMASGLIPIV 423
Cdd:cd03820 239 RV-----KLLGPTKNI----AEEYANSSIFVLSSRY-EGFPMVLLEAMAYGLPIIS 284
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
183-463 |
3.71e-04 |
|
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: 43.04 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 183 PDIwIDTMGyPFSYPIIARFLRR---IPIVT--------YTHYpimskdmLNKLFKMPKKGIKVYGKILYwkvfmliyqs 251
Cdd:cd03817 85 PDI-IHTHT-PFSLGKLGLRIARklkIPIVHtyhtmyedYLHY-------IPKGKLLVKAVVRKLVRRFY---------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 252 igSKIDIVITNSTWTNNHIKQIWQSNTCKIIY---PPCSTEKLV--DWKQKFGTAKGERLnqAIVLAQFRPEKRHKLIIE 326
Cdd:cd03817 146 --NHTDAVIAPSEKIKDTLREYGVKGPIEVIPngiDLDKFEKPLntEERRKLGLPPDEPI--LLYVGRLAKEKNIDFLLR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 327 SFATFLKNlpdsvSPIKLIMAGstrskqDENYVKSLQDWSENvLKIPKHLIsFEKNLPFDKIEILLNKSTFGVNAMWNEH 406
Cdd:cd03817 222 AFAELKKE-----PNIKLVIVG------DGPEREELKELARE-LGLADKVI-FTGFVPREELPEYYKAADLFVFASTTET 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1730730 407 FGIAVVEYMASGLiPIVHASAGPLLDIVtpwdANGNIGKA-PPQWELQKKYFAKLEDD 463
Cdd:cd03817 289 QGLVYLEAMAAGL-PVVAAKDPAASELV----EDGENGFLfEPNDETLAEKLLHLREN 341
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
316-434 |
1.95e-03 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 38.65 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 316 RPEKRHKLIIESFATFLKNLPDsvspIKLIMAGSTRSKQDENYVKSLQDwseNVlkipkHLISFEKNLPfdkieILLNKS 395
Cdd:pfam13692 12 PNVKGVDYLLEAVPLLRKRDND----VRLVIVGDGPEEELEELAAGLED---RV-----IFTGFVEDLA-----ELLAAA 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 1730730 396 TFGVNAMWNEHFGIAVVEYMASGLiPIVHASAGPLLDIV 434
Cdd:pfam13692 75 DVFVLPSLYEGFGLKLLEAMAAGL-PVVATDVGGIPELV 112
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
129-236 |
2.42e-03 |
|
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.
Pssm-ID: 427107 [Multi-domain] Cd Length: 139 Bit Score: 38.42 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730730 129 VKAKFDYDL-DSDRIFFISLKLRYLVDSSTWKHFTLIGQAIGSMILAFESIIQCPPDIWIDTMGYPFSYPIIARFLRRIP 207
Cdd:pfam03033 34 TKRGFEEFLvEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKAFRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIP 113
|
90 100
....*....|....*....|....*....
gi 1730730 208 IVTYTHYPIMSKdmLNKLfkMPKKGIKVY 236
Cdd:pfam03033 114 IIIHEQNGIPGL--TNKT--LPRTATKVA 138
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
405-444 |
6.41e-03 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 39.31 E-value: 6.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1730730 405 EHFGIAVVEYMASGlIPIVHASAGPLLDIVTPwDANGNIG 444
Cdd:PLN02871 342 ETLGFVVLEAMASG-VPVVAARAGGIPDIIPP-DQEGKTG 379
|
|
| |
