|
Name |
Accession |
Description |
Interval |
E-value |
| GT33_ALG1-like |
cd03816 |
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ... |
6-442 |
0e+00 |
|
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.
Pssm-ID: 340843 [Multi-domain] Cd Length: 411 Bit Score: 672.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 6 PKKRNACVIVLGDIGRSPRMQYHAQSLLEENYHVDMIGYLETRPLEELTQHPRCRIHELTAVP-VTNLTPKLRLLFKAFW 84
Cdd:cd03816 1 PKKKRVCVLVLGDIGRSPRMQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPtKNKLPFLLFAPLKVLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 85 QTLSLLMALISIGRPSFLLVQNPPGIPTLIVCYLYCAVTRTKLAIDWHNYTYTVLALGMskGEQSPLIRLVRRLERYFGS 164
Cdd:cd03816 81 QALSLLWLLYELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKL--GENHPLVRLAKWYEKTFGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 165 KAHTHFCVTRAMQEDLQQ-NWGIGPVKVLYDRAPAQFHPIDLTHKHELYLKLAkdypqfqakdaeqsdvleataLTQKLA 243
Cdd:cd03816 159 MADAHLCVTKAMQRDLQQfENWNIRATVLYDRPPSHFRPIPLEEKHELFLELA---------------------LFRELA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 244 SGVVQYRPQRQAVLVSSTSWTPDEDFGILLKALQAYEETAQAEPLVYPSLLCIITGKGPQKEHYVAEIEKLQWQKVSVIT 323
Cdd:cd03816 218 EGAVSYKEGRPALLVSSTSWTPDEDFSILLDALKAYESSAATEPALLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 324 PWLEIEDYPTVLASADLGVCLHWSTSGLDLPMKVVDMFGSGLPVCAYDFKCLDELVKHGENGFVFGDHVQLAEQLRIWFE 403
Cdd:cd03816 298 PWLSAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLS 377
|
410 420 430
....*....|....*....|....*....|....*....
gi 24647789 404 NFPKNpSILETRAGFqrkiQEFQELRWRESWRLIAAPVL 442
Cdd:cd03816 378 DFDRG-KLNVLKKGA----QEESENRWDENWDRVAGPLF 411
|
|
| PLN02275 |
PLN02275 |
transferase, transferring glycosyl groups |
7-402 |
7.78e-157 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215155 [Multi-domain] Cd Length: 371 Bit Score: 448.35 E-value: 7.78e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 7 KKRNACVIVLGDIGRSPRMQYHAQSLLEE-NYHVDMIGYLETRPLEELTQHPRCRIHELTAVPVTNLTPK----LRLLFK 81
Cdd:PLN02275 3 RRGRAAVVVLGDFGRSPRMQYHALSLARQaSFQVDVVAYGGSEPIPALLNHPSIHIHLMVQPRLLQRLPRvlyaLALLLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 82 AFWQTLSLL-MALISIGRPSFLLVQNPPGIPTLIVCYLYCAVTRTKLAIDWHNYTYTVLALgmSKGEQSPLIRLVRRLER 160
Cdd:PLN02275 83 VAIQFLMLLwFLCVKIPRPDVFLVQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLAL--SLGRSHPLVRLYRWYER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 161 YFGSKAHTHFCVTRAMQEDLQQNWGIgPVKVLYDRAPAQFHPIDLThkhelylklakdypqfqakdaeqsdvleataltq 240
Cdd:PLN02275 161 HYGKMADGHLCVTKAMQHELDQNWGI-RATVLYDQPPEFFRPASLE---------------------------------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 241 klasgvVQYRPQRQAVLVSSTSWTPDEDFGILLKALQAY----------EETAQAEPLVYPSLLCIITGKGPQKEHYVAE 310
Cdd:PLN02275 206 ------IRLRPNRPALVVSSTSWTPDEDFGILLEAAVMYdrrvaarlneSDSASGKQSLYPRLLFIITGKGPQKAMYEEK 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 311 IEKLQWQKVSVITPWLEIEDYPTVLASADLGVCLHWSTSGLDLPMKVVDMFGSGLPVCAYDFKCLDELVKHGENGFVFGD 390
Cdd:PLN02275 280 ISRLNLRHVAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNGLLFSS 359
|
410
....*....|..
gi 24647789 391 HVQLAEQLRIWF 402
Cdd:PLN02275 360 SSELADQLLELL 371
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
272-404 |
1.39e-08 |
|
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: 53.82 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 272 LLKALQAYEETaqaeplvYPSLLCIITGKGPQKEHYVAEIEKLQWQKVSVITPWLEIEDYPTVLASADLGVClhwsTSGL 351
Cdd:pfam00534 20 LIKAFALLKEK-------NPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVL----PSRY 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 24647789 352 D-LPMKVVDMFGSGLPVCAYDFKCLDELVKHGENGFVF--GDHVQLAEQLRIWFEN 404
Cdd:pfam00534 89 EgFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVkpNNAEALAEAIDKLLED 144
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
335-445 |
2.62e-08 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 51.91 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 335 LASADLGVCLHWSTSgldLPMKVVDMFGSGLPVCAYDFKCLDELVKHGENGFVF--GDHVQLAEQLRIWFENFpknpsil 412
Cdd:COG0438 18 LAAADVFVLPSRSEG---FGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVppGDPEALAEAILRLLEDP------- 87
|
90 100 110
....*....|....*....|....*....|...
gi 24647789 413 ETRAGFQRKIQEFQELRWreSWRLIAAPVLEAF 445
Cdd:COG0438 88 ELRRRLGEAARERAEERF--SWEAIAERLLALY 118
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GT33_ALG1-like |
cd03816 |
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ... |
6-442 |
0e+00 |
|
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.
Pssm-ID: 340843 [Multi-domain] Cd Length: 411 Bit Score: 672.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 6 PKKRNACVIVLGDIGRSPRMQYHAQSLLEENYHVDMIGYLETRPLEELTQHPRCRIHELTAVP-VTNLTPKLRLLFKAFW 84
Cdd:cd03816 1 PKKKRVCVLVLGDIGRSPRMQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPtKNKLPFLLFAPLKVLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 85 QTLSLLMALISIGRPSFLLVQNPPGIPTLIVCYLYCAVTRTKLAIDWHNYTYTVLALGMskGEQSPLIRLVRRLERYFGS 164
Cdd:cd03816 81 QALSLLWLLYELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKL--GENHPLVRLAKWYEKTFGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 165 KAHTHFCVTRAMQEDLQQ-NWGIGPVKVLYDRAPAQFHPIDLTHKHELYLKLAkdypqfqakdaeqsdvleataLTQKLA 243
Cdd:cd03816 159 MADAHLCVTKAMQRDLQQfENWNIRATVLYDRPPSHFRPIPLEEKHELFLELA---------------------LFRELA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 244 SGVVQYRPQRQAVLVSSTSWTPDEDFGILLKALQAYEETAQAEPLVYPSLLCIITGKGPQKEHYVAEIEKLQWQKVSVIT 323
Cdd:cd03816 218 EGAVSYKEGRPALLVSSTSWTPDEDFSILLDALKAYESSAATEPALLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 324 PWLEIEDYPTVLASADLGVCLHWSTSGLDLPMKVVDMFGSGLPVCAYDFKCLDELVKHGENGFVFGDHVQLAEQLRIWFE 403
Cdd:cd03816 298 PWLSAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLS 377
|
410 420 430
....*....|....*....|....*....|....*....
gi 24647789 404 NFPKNpSILETRAGFqrkiQEFQELRWRESWRLIAAPVL 442
Cdd:cd03816 378 DFDRG-KLNVLKKGA----QEESENRWDENWDRVAGPLF 411
|
|
| PLN02275 |
PLN02275 |
transferase, transferring glycosyl groups |
7-402 |
7.78e-157 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215155 [Multi-domain] Cd Length: 371 Bit Score: 448.35 E-value: 7.78e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 7 KKRNACVIVLGDIGRSPRMQYHAQSLLEE-NYHVDMIGYLETRPLEELTQHPRCRIHELTAVPVTNLTPK----LRLLFK 81
Cdd:PLN02275 3 RRGRAAVVVLGDFGRSPRMQYHALSLARQaSFQVDVVAYGGSEPIPALLNHPSIHIHLMVQPRLLQRLPRvlyaLALLLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 82 AFWQTLSLL-MALISIGRPSFLLVQNPPGIPTLIVCYLYCAVTRTKLAIDWHNYTYTVLALgmSKGEQSPLIRLVRRLER 160
Cdd:PLN02275 83 VAIQFLMLLwFLCVKIPRPDVFLVQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLAL--SLGRSHPLVRLYRWYER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 161 YFGSKAHTHFCVTRAMQEDLQQNWGIgPVKVLYDRAPAQFHPIDLThkhelylklakdypqfqakdaeqsdvleataltq 240
Cdd:PLN02275 161 HYGKMADGHLCVTKAMQHELDQNWGI-RATVLYDQPPEFFRPASLE---------------------------------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 241 klasgvVQYRPQRQAVLVSSTSWTPDEDFGILLKALQAY----------EETAQAEPLVYPSLLCIITGKGPQKEHYVAE 310
Cdd:PLN02275 206 ------IRLRPNRPALVVSSTSWTPDEDFGILLEAAVMYdrrvaarlneSDSASGKQSLYPRLLFIITGKGPQKAMYEEK 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 311 IEKLQWQKVSVITPWLEIEDYPTVLASADLGVCLHWSTSGLDLPMKVVDMFGSGLPVCAYDFKCLDELVKHGENGFVFGD 390
Cdd:PLN02275 280 ISRLNLRHVAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNGLLFSS 359
|
410
....*....|..
gi 24647789 391 HVQLAEQLRIWF 402
Cdd:PLN02275 360 SSELADQLLELL 371
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
17-425 |
2.54e-15 |
|
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: 77.38 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 17 GDIGRSPRMQYHAQSLLEENYHVDMIGYLETRPLEELTQHPRC-----RIHElTAVPVTNLTPKLRLLFKAFWQTL-SLL 90
Cdd:cd03794 12 PKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGATEtkdgiRVIR-VKLGPIKKNGLIRRLLNYLSFALaALL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 91 MALISIGRPSFLLVQNPPGIPTLIVcYLYCAVTRTKLAID----WHNytyTVLALGMSKGeqSPLIRLVRRLERYFGSKA 166
Cdd:cd03794 91 KLLVREERPDVIIAYSPPITLGLAA-LLLKKLRGAPFILDvrdlWPE---SLIALGVLKK--GSLLKLLKKLERKLYRLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 167 HTHFCVTRAMQEDLQQNwGIGPVKVLYDRAPAQFHPIDLTHKHELYLKLAKDypqfqakdaeqsDVLeataltqklasgV 246
Cdd:cd03794 165 DAIIVLSPGLKEYLLRK-GVPKEKIIVIPNWADLEEFKPPPKDELRKKLGLD------------DKF------------V 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 247 VQYrpqrqavlvsSTSWTPDEDFGILLKALQAYEETAQAEplvypsLLCIitGKGPQKEHYVAEIEKLQWQKVSVItPWL 326
Cdd:cd03794 220 VVY----------AGNIGKAQGLETLLEAAERLKRRPDIR------FLFV--GDGDEKERLKELAKARGLDNVTFL-GRV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 327 EIEDYPTVLASADLG-VCLH-WSTSGLDLPMKVVDMFGSGLPVCAYDFKCLDELVKHGENGFVF--GDHVQLAEQLriwf 402
Cdd:cd03794 281 PKEEVPELLSAADVGlVPLKdNPANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVepGDPEALADAI---- 356
|
410 420
....*....|....*....|....*
gi 24647789 403 ENFPKNPSILET--RAGFQRKIQEF 425
Cdd:cd03794 357 LELLDDPELRRAmgENGRELAEEKF 381
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
20-445 |
8.75e-12 |
|
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: 66.41 E-value: 8.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 20 GRSPRMQYHAQSLLEENYHVDMIGYleTRPLEELTQHPRCRIHELTAVpvtnltpklRLLFKAFWQTLSLLMALISIGRP 99
Cdd:cd03801 15 GAERHVRELARALAARGHDVTVLTP--ADPGEPPEELEDGVIVPLLPS---------LAALLRARRLLRELRPLLRLRKF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 100 SFLLVQNPPgipTLIVCYLYCAVTRTKLAIDWHNYTYTVLALGMSKGEqspliRLVRRLErYFGSKAHTHFCVTRAMQED 179
Cdd:cd03801 84 DVVHAHGLL---AALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAER-----RLLARAE-ALLRRADAVIAVSEALRDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 180 LQQNWGIGP--VKVLYdrapaqfHPIDLTHKHelyLKLAKDYPqfqakdaeqsdvleataltqklasgvvqyRPQRQAVL 257
Cdd:cd03801 155 LRALGGIPPekIVVIP-------NGVDLERFS---PPLRRKLG-----------------------------IPPDRPVL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 258 VSSTSWTPDEDFGILLKALqayeetAQAEPLVYPSLLCIITGKGPQKEHYVAEIEKLQwQKVsVITPWLEIEDYPTVLAS 337
Cdd:cd03801 196 LFVGRLSPRKGVDLLLEAL------AKLLRRGPDVRLVIVGGDGPLRAELEELELGLG-DRV-RFLGFVPDEELPALYAA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 338 ADLGVCLHWSTSgldLPMKVVDMFGSGLPVCAYDFKCLDELVKHGENGFVF--GDHVQLAEQLRIWFenfpKNPSILET- 414
Cdd:cd03801 268 ADVFVLPSRYEG---FGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVppDDVEALADALLRLL----ADPELRARl 340
|
410 420 430
....*....|....*....|....*....|..
gi 24647789 415 -RAGFQRKIQEFqelrwreSWRLIAAPVLEAF 445
Cdd:cd03801 341 gRAARERVAERF-------SWERVAERLLDLY 365
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
258-388 |
9.91e-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: 55.87 E-value: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 258 VSSTSWTPDEDFGILLKALqayeetAQAEPLVYPSLLCIITGKGPQKEHYVAEIEKLQWQKVSVITPWLEIEDYPTVLAS 337
Cdd:cd01635 114 VSVGRLVPEKGIDLLLEAL------ALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAA 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 24647789 338 ADLGVCLHWSTSgldLPMKVVDMFGSGLPVCAYDFKCLDELVKHGENGFVF 388
Cdd:cd01635 188 ADVFVLPSRSEG---FGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
272-404 |
1.39e-08 |
|
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: 53.82 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 272 LLKALQAYEETaqaeplvYPSLLCIITGKGPQKEHYVAEIEKLQWQKVSVITPWLEIEDYPTVLASADLGVClhwsTSGL 351
Cdd:pfam00534 20 LIKAFALLKEK-------NPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVL----PSRY 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 24647789 352 D-LPMKVVDMFGSGLPVCAYDFKCLDELVKHGENGFVF--GDHVQLAEQLRIWFEN 404
Cdd:pfam00534 89 EgFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVkpNNAEALAEAIDKLLED 144
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
83-425 |
1.99e-08 |
|
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: 55.68 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 83 FWQTLSLLMALISIGRPSFLLVQNP-PGIPTLIVCYLycavTRTKLAIdwhnytYTVLALGMSKGEQSPLIRLVRRLERY 161
Cdd:cd03808 66 DLKALFKLYKLLKKEKPDIVHCHTPkPGILGRLAARL----AGVPKVI------YTVHGLGFVFTEGKLLRLLYLLLEKL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 162 FGSKAHTHFCVTRAMQEDLQQNWGIGPVKVLYdrapaqfHP---IDLTHKHELYLKLAKDYPQFqakdaeqsdVLEATAL 238
Cdd:cd03808 136 ALLFTDKVIFVNEDDRDLAIKKGIIKKKKTVL-------IPgsgVDLDRFQYSPESLPSEKVVF---------LFVARLL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 239 TQKlasgvvqyrpqrqavlvsstswtpdeDFGILLKAlqayeetAQAEPLVYPSLLCIITGKGPQKEHYVAEIEklQWQK 318
Cdd:cd03808 200 KDK--------------------------GIDELIEA-------AKILKKKGPNVRFLLVGDGELENPSEILIE--KLGL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 319 VSVITPWLEIEDYPTVLASADLgVCL--HWStsGLdlPMKVVDMFGSGLPVCAYDFKCLDELVKHGENGFVF--GDHVQL 394
Cdd:cd03808 245 EGRIEFLGFRSDVPELLAESDV-FVLpsYRE--GL--PRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVppGDVEAL 319
|
330 340 350
....*....|....*....|....*....|...
gi 24647789 395 AEQLRIWFEnfpkNPSILET--RAGFQRKIQEF 425
Cdd:cd03808 320 ADAIEKLIE----DPELRKEmgEAARKRVEEKF 348
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
335-445 |
2.62e-08 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 51.91 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 335 LASADLGVCLHWSTSgldLPMKVVDMFGSGLPVCAYDFKCLDELVKHGENGFVF--GDHVQLAEQLRIWFENFpknpsil 412
Cdd:COG0438 18 LAAADVFVLPSRSEG---FGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVppGDPEALAEAILRLLEDP------- 87
|
90 100 110
....*....|....*....|....*....|...
gi 24647789 413 ETRAGFQRKIQEFQELRWreSWRLIAAPVLEAF 445
Cdd:COG0438 88 ELRRRLGEAARERAEERF--SWEAIAERLLALY 118
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
29-425 |
3.53e-08 |
|
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: 55.06 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 29 AQSLLEENYHVDMIGYLETRPLEeltqHPRCRIHELTAVPVTNLTPKLRLLFKAFWQtlslLMALISIGRPSFLLVQNpp 108
Cdd:cd03811 22 ANALDKRGYDVTLVLLRDEGDLD----KQLNGDVKLIRLLIRVLKLIKLGLLKAILK----LKRILKRAKPDVVISFL-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 109 GIPTLIVCYLYCAvtRTKLAIDWHNYtytvlalgMSKGEQSPLIRLvrrLERYFGSKAHTHFCVTRAMQEDLQQNWGIGP 188
Cdd:cd03811 92 GFATYIVAKLAAA--RSKVIAWIHSS--------LSKLYYLKKKLL---LKLKLYKKADKIVCVSKGIKEDLIRLGPSPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 189 --VKVLYDrapaqfhPIDLthkhelylklakdyPQFQAKDAEQSDVLEATALtqklasgvvqyrpqrqaVLVSSTSWTPD 266
Cdd:cd03811 159 ekIEVIYN-------PIDI--------------DRIRALAKEPILNEPEDGP-----------------VILAVGRLDPQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 267 EDFGILLKALQAYEETaqaeplvYPSLLCIITGKGPQKEHYVAEIEKLQWQKvSVITP-WleIED-YPtVLASADLGVCl 344
Cdd:cd03811 201 KGHDLLIEAFAKLRKK-------YPDVKLVILGDGPLREELEKLAKELGLAE-RVIFLgF--QSNpYP-YLKKADLFVL- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 345 hwsTS---GLdlPMKVVDMFGSGLPVCAYDFKCLDELVKHGENGFVF--GDHVQLAEQLRIWFENFPKNPSILETRAGFQ 419
Cdd:cd03811 269 ---SSryeGF--PNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVpdGDAAALAGILAALLQKKLDAALRERLAKAQE 343
|
....*.
gi 24647789 420 RKIQEF 425
Cdd:cd03811 344 AVFREY 349
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
296-427 |
1.24e-06 |
|
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: 50.36 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 296 IITGKGPQKEHYVAEIEKLQWQKVSVITPWLEIEDYPTVLASADLGVclHWSTSGLdLPMKVVDMFGSGLPVCAYDFKCL 375
Cdd:cd03817 235 VIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFV--FASTTET-QGLVYLEAMAAGLPVVAAKDPAA 311
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24647789 376 DELVKHGENGFVF-GDHVQLAEqlriWFENFPKNPSILE----------TRAGFQRKIQEFQE 427
Cdd:cd03817 312 SELVEDGENGFLFePNDETLAE----KLLHLRENLELLRklsknaeisaREFAFAKSVEKLYE 370
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
297-404 |
2.33e-06 |
|
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: 49.54 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 297 ITGKGPQKEHYVAEIEKLQWQKVSVI-TPWLEIEDYptvLASADLGVClhwsTS---GLdlPMKVVDMFGSGLPVCAYDF 372
Cdd:cd03820 217 IYGDGPEREELEKLIDKLGLEDRVKLlGPTKNIAEE---YANSSIFVL----SSryeGF--PMVLLEAMAYGLPIISFDC 287
|
90 100 110
....*....|....*....|....*....|....*
gi 24647789 373 KC-LDELVKHGENGFVF--GDHVQLAEQLRIWFEN 404
Cdd:cd03820 288 PTgPSEIIEDGENGLLVpnGDVDALAEALLRLMED 322
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
296-404 |
1.69e-05 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 44.42 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 296 IITGKGPQKEhYVAEIEKLQwQKVsVITPWleIEDYPTVLASADLGVC-LHWSTsgldLPMKVVDMFGSGLPVCAYDFKC 374
Cdd:pfam13692 37 VIVGDGPEEE-LEELAAGLE-DRV-IFTGF--VEDLAELLAAADVFVLpSLYEG----FGLKLLEAMAAGLPVVATDVGG 107
|
90 100 110
....*....|....*....|....*....|..
gi 24647789 375 LDELVkHGENGFVF--GDHVQLAEQLRIWFEN 404
Cdd:pfam13692 108 IPELV-DGENGLLVppGDPEALAEAILRLLED 138
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
29-191 |
1.83e-05 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 44.83 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 29 AQSLLEENYHVDMIgyleTRPLEELTQHPRCRIHELTAVPvtnltPKLRLLFKAFWQTLSLLMALISIGRPSFLLVQNPp 108
Cdd:pfam13439 11 ARALARRGHEVTVV----TPGGPGPLAEEVVRVVRVPRVP-----LPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 109 gIPTLIVCYLYCAVTRTKLAIDWHNytyTVLALGMSKGEQSPLIRLVRRLERYFGSKAHTHFCVTRAMQEDLQQNWGIGP 188
Cdd:pfam13439 81 -FPLGLAALAARLRLGIPLVVTYHG---LFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVPP 156
|
...
gi 24647789 189 VKV 191
Cdd:pfam13439 157 EKI 159
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
29-191 |
1.96e-05 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 44.70 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 29 AQSLLEENYHVDMIGYLETRPLEELtQHPRCRIHELTAVPVTNLTPKLRLLFkAFWQTLSLlmalisiGRPSFLLVQNPP 108
Cdd:pfam13579 11 ARALAALGHEVRVVTPGGPPGRPEL-VGDGVRVHRLPVPPRPSPLADLAALR-RLRRLLRA-------ERPDVVHAHSPT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647789 109 gipTLIVCYLYCAVTRTKLAIDWHNYTYTvlalgmskGEQSPLIRLVRRLERYFGSKAHTHFCVTRAMQEDLQQnWGIGP 188
Cdd:pfam13579 82 ---AGLAARLARRRRGVPLVVTVHGLALD--------YGSGWKRRLARALERRLLRRADAVVVVSEAEAELLRA-LGVPA 149
|
...
gi 24647789 189 VKV 191
Cdd:pfam13579 150 ARV 152
|
|
| |
