|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
8-356 |
3.79e-55 |
|
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: 185.05 E-value: 3.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 8 ILQLTHQGGPA--GSTQSIFDLGQHLARRGHRVLVGCRADVLLARLARDAGLPVVPLSFLPRGVLA----RALEDLLARE 81
Cdd:cd03801 2 ILLLSPELPPPvgGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRArrllRELRPLLRLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 82 RVDVVNSHATLDRRALTWMRWRGRLP-------QAFVVTRRTMPRTSPV--ELLPVGLTADRTIAVSEAVARALRRRLH- 151
Cdd:cd03801 82 KFDVVHAHGLLAALLAALLALLLGAPlvvtlhgAEPGRLLLLLAAERRLlaRAEALLRRADAVIAVSEALRDELRALGGi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 152 PGARLRVVPNGIALERvdappppaDLAAARAALGDPGGRPVVAMVSRL---KDQHVVLQALPLIQR---GVVVACVGTEP 225
Cdd:cd03801 162 PPEKIVVIPNGVDLER--------FSPPLRRKLGIPPDRPVLLFVGRLsprKGVDLLLEALAKLLRrgpDVRLVIVGGDG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 226 D--GRLGALAQALPDRHRVVFVPLSERALAFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGL 303
Cdd:cd03801 234 PlrAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGL 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1125431435 304 LVRPLDPAAWAEALERLLGDGALARRLAHAGRALVRREFTLERTAERTEAVYR 356
Cdd:cd03801 314 VVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
8-343 |
4.06e-39 |
|
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: 142.49 E-value: 4.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 8 ILQLTHQGGPAGSTQSIFDLGQHLARRGHRVLVGCRADVLLARLARDA-GLPVVPLSFLPRGVLARALEDLLARERVDVV 86
Cdd:cd03819 1 ILMLTPALEIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGiGLPGLKVPLLRALLGNVRLARLIRRERIDLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 87 NSHA-TLDRRALTWMRWRGrLPQAFVVTRRTMPRTSPVEL-LPVGLTADRTIAVSEAVARALRRRLHPG-ARLRVVPNGI 163
Cdd:cd03819 81 HAHSrAPAWLGWLASRLTG-VPLVTTVHGSYLATYHPKDFaLAVRARGDRVIAVSELVRDHLIEALGVDpERIRVIPNGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 164 ALERVDAPPPPADLAAAraalGDPGGRPVVAMVSRL---KDQHVVLQALPLIQRGVVVACV---GTEPDGRLGALAQALP 237
Cdd:cd03819 160 DTDRFPPEAEAEERAQL----GLPEGKPVVGYVGRLspeKGWLLLVDAAAELKDEPDFRLLvagDGPERDEIRRLVERLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 238 DRHRVVFVPLSERALAFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPLDPAAWAEAL 317
Cdd:cd03819 236 LRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALADAI 315
|
330 340
....*....|....*....|....*...
gi 1125431435 318 ERLLGDGALARRLAHAGRAL--VRREFT 343
Cdd:cd03819 316 RAAKLLPEAREKLQAAAALTeaVRELLL 343
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
24-352 |
1.61e-37 |
|
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: 138.50 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 24 IFDLGQHLARRGHRVLVGCRADVLLARLARDAGLPVVPLSFLPRGV-------LARALEDLLARERVDVVNSH------- 89
Cdd:cd03808 16 RLPLIKALVKKGYEVHVIAPDGDKLSDELKELGVKVIDIPILRRGInplkdlkALFKLYKLLKKEKPDIVHCHtpkpgil 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 90 ATLDRRALTWMRW----RGrLPQAFVVTRRTMPRTSPVELLpVGLTADRTIAVSEA-VARALRRRLHPGARLRVVP-NGI 163
Cdd:cd03808 96 GRLAARLAGVPKViytvHG-LGFVFTEGKLLRLLYLLLEKL-ALLFTDKVIFVNEDdRDLAIKKGIIKKKKTVLIPgSGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 164 ALERvdappppadlaAARAALGDPGGRPVVAMVSRL---KDQHVVLQALPLI-QRG--VVVACVG-TEPDGRLGALAQAL 236
Cdd:cd03808 174 DLDR-----------FQYSPESLPSEKVVFLFVARLlkdKGIDELIEAAKILkKKGpnVRFLLVGdGELENPSEILIEKL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 237 PDRHRVVFVPLSERALAFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPLDPAAWAEA 316
Cdd:cd03808 243 GLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADA 322
|
330 340 350
....*....|....*....|....*....|....*.
gi 1125431435 317 LERLLGDGALARRLAHAGRALVRREFTLERTAERTE 352
Cdd:cd03808 323 IEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
8-344 |
8.03e-36 |
|
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: 133.64 E-value: 8.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 8 ILQLTHQGGPAGSTQSIFDLGQHLARRGHRVLVGCRADVLLARLARDAG-------LPVVPLSFLPRGVLARALEDLLAR 80
Cdd:cd03811 2 ILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDvklirllIRVLKLIKLGLLKAILKLKRILKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 81 ERVDVVNSHATLDRRALTWMRwRGRLPqaFVVTRRTMPRTSPVELLPVGLT------ADRTIAVSEAVARALRRRLH-PG 153
Cdd:cd03811 82 AKPDVVISFLGFATYIVAKLA-AARSK--VIAWIHSSLSKLYYLKKKLLLKlklykkADKIVCVSKGIKEDLIRLGPsPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 154 ARLRVVPNGIALERVDAPPPPADLaaaraalGDPGGRPVVAMVSRL---KDQHVVLQALPLI---QRGVVVACVGT-EPD 226
Cdd:cd03811 159 EKIEVIYNPIDIDRIRALAKEPIL-------NEPEDGPVILAVGRLdpqKGHDLLIEAFAKLrkkYPDVKLVILGDgPLR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 227 GRLGALAQALPDRHRVVFVPLSERALAFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVR 306
Cdd:cd03811 232 EELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVP 311
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1125431435 307 PLDPAAWAEALERLLGDGALARRLAHAGRAL--VRREFTL 344
Cdd:cd03811 312 DGDAAALAGILAALLQKKLDAALRERLAKAQeaVFREYTI 351
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
253-360 |
2.43e-33 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 120.48 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 253 AFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPLDPAAWAEALERLLGDGALARRLAH 332
Cdd:COG0438 16 ALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGE 95
|
90 100
....*....|....*....|....*...
gi 1125431435 333 AGRALVRREFTLERTAERTEAVYREALA 360
Cdd:COG0438 96 AARERAEERFSWEAIAERLLALYEELLA 123
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
190-323 |
1.33e-31 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 116.46 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 190 RPVVAMVSRL----KDQHVVLQALPLIQR---GVVVACVGTEPDGRLGALAQALPDRhrVVFVPLSERALAFYHLATVAA 262
Cdd:pfam13692 1 RPVILFVGRLhpnvKGVDYLLEAVPLLRKrdnDVRLVIVGDGPEEELEELAAGLEDR--VIFTGFVEDLAELLAAADVFV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125431435 263 LPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRsGETGLLVRPLDPAAWAEALERLLGD 323
Cdd:pfam13692 79 LPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVD-GENGLLVPPGDPEALAEAILRLLED 138
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
189-335 |
2.41e-31 |
|
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 116.22 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 189 GRPVVAMVSRL---KDQHVVLQALPLIQRG-----VVVACVGTEPDgRLGALAQALPDRHRVVFVPLSERA--LAFYHLA 258
Cdd:pfam00534 1 KKKIILFVGRLepeKGLDLLIKAFALLKEKnpnlkLVIAGDGEEEK-RLKKLAEKLGLGDNVIFLGFVSDEdlPELLKIA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125431435 259 TVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGR 335
Cdd:pfam00534 80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENAR 156
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
19-358 |
4.90e-31 |
|
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: 121.23 E-value: 4.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 19 GSTQSIFDLGQHLARRGHRVLVGC--RADVLLARLARDAGLPVVPLSFLPRGVLAR----ALEDLLARERVDVVNSHATL 92
Cdd:cd03817 15 GVATSVRNLARALEKRGHEVYVITpsDPGAEDEEEVVRYRSFSIPIRKYHRQHIPFpfkkAVIDRIKELGPDIIHTHTPF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 93 dRRALTWMRWRGRLPQAFVVTRRTMPR-----TSPVELLPVGL----------TADRTIAVSEAVARALRRRLHpGARLR 157
Cdd:cd03817 95 -SLGKLGLRIARKLKIPIVHTYHTMYEdylhyIPKGKLLVKAVvrklvrrfynHTDAVIAPSEKIKDTLREYGV-KGPIE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 158 VVPNGIALERvdapPPPADLAAARAALGDPGGRPVVAMVSRL---KDQHVVLQALPLI--QRGVVVACVGTEPD-GRLGA 231
Cdd:cd03817 173 VIPNGIDLDK----FEKPLNTEERRKLGLPPDEPILLYVGRLakeKNIDFLLRAFAELkkEPNIKLVIVGDGPErEELKE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 232 LAQALPDRHRVVF---VPlSERALAFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPl 308
Cdd:cd03817 249 LARELGLADKVIFtgfVP-REELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEP- 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1125431435 309 DPAAWAEALERLLGDGALARRLAHAGRALVRReftlERTAERTEAVYREA 358
Cdd:cd03817 327 NDETLAEKLLHLRENLELLRKLSKNAEISARE----FAFAKSVEKLYEEV 372
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
17-356 |
5.13e-30 |
|
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: 118.19 E-value: 5.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 17 PAGSTQSIFDLGQHLARRGHRVLVGC--RADVLLARLaRDAGLPVVPL---SFLPRGVLARaLEDLLARERVDVVNSH-A 90
Cdd:cd03807 11 VGGAETMLLRLLEHMDKSRFEHVVISltGDGVLGEEL-LAAGVPVVCLglsSGKDPGVLLR-LAKLIRKRNPDVVHTWmY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 91 TLDRRALTWMRWRGRLPqaFVVTRRTM---PRTSPVEL---LPVGLTADRTIAVSEAVARALRRRLHPGARLRVVPNGIA 164
Cdd:cd03807 89 HADLIGGLAAKLAGGVK--VIWSVRSSnipQRLTRLVRklcLLLSKFSPATVANSSAVAEFHQEQGYAKNKIVVIYNGID 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 165 LERVDAPPPPADLAAARAalGDPGGRPVVAMVSRL---KDQHVVLQALPLIQRG---VVVACVGTEPDGR-LGALAQALP 237
Cdd:cd03807 167 LFKLSPDDASRARARRRL--GLAEDRRVIGIVGRLhpvKDHSDLLRAAALLVEThpdLRLLLVGRGPERPnLERLLLELG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 238 DRHRVVFVPLSERALAFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGeTGLLVRPLDPAAWAEAL 317
Cdd:cd03807 245 LEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPAGDPQALADAI 323
|
330 340 350
....*....|....*....|....*....|....*....
gi 1125431435 318 ERLLGDGALARRLAHAGRALVRREFTLERTAERTEAVYR 356
Cdd:cd03807 324 RALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
24-353 |
2.06e-29 |
|
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: 117.34 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 24 IFDLGQHLARRGHRVLVGCRAD-------VLLARLARDAGLPVVPLSFLPRGVLARALE----DLLARERV-----DVVN 87
Cdd:cd03800 27 VLELARALAELGYQVDIFTRRIspadpevVEIAPGARVIRVPAGPPEYLPKEELWPYLEefadGLLRFIAReggryDLIH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 88 SHATLDRRAltWMRWRGRLPQAFVVTRRTMPRTSPVELLP---------------VGLTADRTIAVSEAVARALRRRL-H 151
Cdd:cd03800 107 SHYWDSGLV--GALLARRLGVPLVHTFHSLGRVKYRHLGAqdtyhpslritaeeqILEAADRVIASTPQEADELISLYgA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 152 PGARLRVVPNGIALERVdapPPPADLAAARAALGDPGGRPVVAMVSRL---KDQHVVLQAL----PLIQRGVVVACVGTE 224
Cdd:cd03800 185 DPSRINVVPPGVDLERF---FPVDRAEARRARLLLPPDKPVVLALGRLdprKGIDTLVRAFaqlpELRELANLVLVGGPS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 225 PDGRLGA--LAQALPDRHRVV-----FVPLSERALA-FYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMV 296
Cdd:cd03800 262 DDPLSMDreELAELAEELGLIdrvrfPGRVSRDDLPeLYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIV 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1125431435 297 RSGETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRALVRREFTLERTAERTEA 353
Cdd:cd03800 342 RDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQLLT 398
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
23-358 |
1.55e-28 |
|
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: 114.40 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 23 SIFDLGQHLARRGHRVLVGCRADVLLARLARDAGLPVVPLSFLPR--------------GVLARALEDLLA---RERVDV 85
Cdd:cd03798 19 FVRRQVRALSRRGVDVEVLAPAPWGPAAARLLRKLLGEAVPPRDGrrllplkprlrllaPLRAPSLAKLLKrrrRGPPDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 86 VNSH-ATLDRRALTWMRWRGRLPqaFVVTRRT------MPRTSPVELLPVGLT-ADRTIAVSEAVARALRRRLHPGARLR 157
Cdd:cd03798 99 IHAHfAYPAGFAAALLARLYGVP--YVVTEHGsdinvfPPRSLLRKLLRWALRrAARVIAVSKALAEELVALGVPRDRVD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 158 VVPNGIALERvdappppadLAAARAALGDPGGRPVVAMVSRL---KDQHVVLQALPLIQRG---VVVACVGTEPDG-RLG 230
Cdd:cd03798 177 VIPNGVDPAR---------FQPEDRGLGLPLDAFVILFVGRLiprKGIDLLLEAFARLAKArpdVVLLIVGDGPLReALR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 231 ALAQAL---PDRHRVVFVPLSErALAFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRP 307
Cdd:cd03798 248 ALAEDLglgDRVTFTGRLPHEQ-VPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPP 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1125431435 308 LDPAAWAEALERLLgDGALARRLAHAGRALVRREFTLERTAERTEAVYREA 358
Cdd:cd03798 327 GDADALAAALRRAL-AEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
136-359 |
8.43e-26 |
|
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.
Pssm-ID: 132132 [Multi-domain] Cd Length: 374 Bit Score: 106.73 E-value: 8.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 136 IAVSEAVARALRRRLH-PGARLRVVPNGIALERVDAPPPPADLAAARAALGDpggRPVVAM-VSRL---KDQHVVLQA-- 208
Cdd:TIGR03088 141 VAVSRDLEDWLRGPVKvPPAKIHQIYNGVDTERFHPSRGDRSPILPPDFFAD---ESVVVGtVGRLqavKDQPTLVRAfa 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 209 -----LPLIQRGVVVACVGTEPD-GRLGALAQALPDRHRVVFVPLSERALAFYHLATVAALPSRMEGLSQALLEAMALGL 282
Cdd:TIGR03088 218 llvrqLPEGAERLRLVIVGDGPArGACEQMVRAAGLAHLVWLPGERDDVPALMQALDLFVLPSLAEGISNTILEAMASGL 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125431435 283 PVVASDAGGNPEMVRSGETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRALVRREFTLERTAERTEAVYREAL 359
Cdd:TIGR03088 298 PVIATAVGGNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSINAMVAAYAGLYDQLL 374
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
132-353 |
3.45e-25 |
|
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: 104.75 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 132 ADRTIAVSEAVARALRRRLH-PGARLRVVPNGIALERVDAPPPPADLAAARAAlgdpggRPVVAMVSRL---KDQHVVLQ 207
Cdd:cd03809 139 ADAIITVSEATRDDIIKFYGvPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLP------EPYFLYVGTLeprKNHERLLK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 208 ALPLI--QRGV---VVACVGTEPDGRLGALAQALPDRHRVVF---VPLSERAlAFYHLATVAALPSRMEGLSQALLEAMA 279
Cdd:cd03809 213 AFALLkkQGGDlklVIVGGKGWEDEELLDLVKKLGLGGRVRFlgyVSDEDLP-ALYRGARAFVFPSLYEGFGLPVLEAMA 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125431435 280 LGLPVVASDAGGNPEMVrsGETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRALVRReFTLERTAERTEA 353
Cdd:cd03809 292 CGTPVIASNISVLPEVA--GDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKK-FSWEKTAEKTLE 362
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
133-358 |
3.22e-24 |
|
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: 102.04 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 133 DRTIAVSEAVARALRRRLHPGARLRVVPNGIALERVDAPPPPADLAAAraalGDPGGRPVVAMVS---RLKDQHVVLQAL 209
Cdd:cd04962 143 DRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKPAGALKRRL----LAPPDEKVVIHVSnfrPVKRIDDVVRVF 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 210 PLIQRGVVVAC--VGTEPD-GRLGALAQALPDRHRVVFVPLSERALAFYHLATVAALPSRMEGLSQALLEAMALGLPVVA 286
Cdd:cd04962 219 ARVRRKIPAKLllVGDGPErVPAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVS 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125431435 287 SDAGGNPEMVRSGETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRALVRREFTLERTAERTEAVYREA 358
Cdd:cd04962 299 SNAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
136-357 |
3.74e-23 |
|
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.
Pssm-ID: 340851 [Multi-domain] Cd Length: 364 Bit Score: 98.94 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 136 IAVSEAVARALRR-RLHPGARLRVVPNGIALERvdapPPPADLAAARAALGDPGGRPVVAMVS-----RLKDQHVVLQAL 209
Cdd:cd03825 142 VAPSRWLADMVRRsPLLKGLPVVVIPNGIDTEI----FAPVDKAKARKRLGIPQDKKVILFGAesvtkPRKGFDELIEAL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 210 PLI--QRGVVVACVG--TEPDGRLGalaqalpdrHRVVFVPL--SERALA-FYHLATVAALPSRMEGLSQALLEAMALGL 282
Cdd:cd03825 218 KLLatKDDLLLVVFGknDPQIVILP---------FDIISLGYidDDEQLVdIYSAADLFVHPSLADNLPNTLLEAMACGT 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125431435 283 PVVASDAGGNPEMVRSGETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRALVRREFTLERTAERTEAVYRE 357
Cdd:cd03825 289 PVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYKD 363
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
8-346 |
1.08e-22 |
|
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: 97.69 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 8 ILQLTHQGGPAGSTQ-SIFDLGQHLARRGHRVLV----GCRAD--------VLLARLARDAGLPVVPLSFLPRGVlaRAL 74
Cdd:cd03820 2 IAIVIPSISNAGGAErVAINLANHLAKKGYDVTIisldSAEKPpfyelddnIKIKNLGDRKYSHFKLLLKYFKKV--RRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 75 EDLLARERVDVVNSHATLDRRALTWMRWRGRLpqafVVTRRTMPRTSPVELLPVGL------TADRTIAVSEAVARALRR 148
Cdd:cd03820 80 RKYLKNNKPDVVISFRTSLLTFLALIGLKSKL----IVWEHNNYEAYNKGLRRLLLrrllykRADKIVVLTEADKLKKYK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 149 RLHPgaRLRVVPNGIALERVDAPPPPadlaaaraalgdpgGRPVVAMVSRL---KDQHVVLQALPLIQRG-----VVVAC 220
Cdd:cd03820 156 QPNS--NVVVIPNPLSFPSEEPSTNL--------------KSKRILAVGRLtyqKGFDLLIEAWALIAKKhpdwkLRIYG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 221 VGTEpDGRLGALAQALPDRHRVVFVPLSERALAFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDA-GGNPEMVRSG 299
Cdd:cd03820 220 DGPE-REELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCpTGPSEIIEDG 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1125431435 300 ETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRAlVRREFTLER 346
Cdd:cd03820 299 ENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARK-NAERFSIEK 344
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
131-356 |
3.91e-21 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340841 [Multi-domain] Cd Length: 474 Bit Score: 94.32 E-value: 3.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 131 TADRTIAVSEavaRALRRRLHPGA---RLRVVPNGIALERVDAPPPPAdlaaaraalgDPGGRPVVAMVSR---LKDQHV 204
Cdd:cd03813 244 QADKIISLYE---GNRRRQIRLGAdpdKTRVIPNGIDIQRFAPAREER----------PEKEPPVVGLVGRvvpIKDVKT 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 205 VLQALPLIQR---GVVVACVGTEPDGRLGA-----LAQALPDRHRVVFVPLSERALAFYHLATVAaLPSRMEGLSQALLE 276
Cdd:cd03813 311 FIRAFKLVRRampDAEGWLIGPEDEDPEYAqeckrLVASLGLENKVKFLGFQNIKEYYPKLGLLV-LTSISEGQPLVILE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 277 AMALGLPVVASDAGGNPEMV-----RSGETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRALVRREFTLERTAERT 351
Cdd:cd03813 390 AMASGVPVVATDVGSCRELIygaddALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSY 469
|
....*
gi 1125431435 352 EAVYR 356
Cdd:cd03813 470 RKLYL 474
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
7-352 |
7.46e-21 |
|
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: 92.79 E-value: 7.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 7 TILQLTHQGGP--AGSTQSIFDLGQHLARRGHRVLVGC-RADVLLARLARDA-----GLPVVPLSFLPR---GVLARALE 75
Cdd:cd03794 1 KILLISQYYPPpkGAAAARVYELAKELVRRGHEVTVLTpSPNYPLGRIFAGAtetkdGIRVIRVKLGPIkknGLIRRLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 76 DLL-----------ARERVDVVNSHAT--LDRRALTWMRWRGRLPqAFVVTRRTMPRtSPVEL------LPVGL------ 130
Cdd:cd03794 81 YLSfalaallkllvREERPDVIIAYSPpiTLGLAALLLKKLRGAP-FILDVRDLWPE-SLIALgvlkkgSLLKLlkkler 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 131 ----TADRTIAVSEAVARALRRRLHPGARLRVVPNGIALERVDAPPPPADLAAARaalgdPGGRPVVAMV---SRLKDQH 203
Cdd:cd03794 159 klyrLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPKDELRKKLG-----LDDKFVVVYAgniGKAQGLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 204 VVLQALPLIQR--GVVVACVGTEPD-GRLGALAQALpDRHRVVFVPLSERALAFYHLATV--------------AALPSR 266
Cdd:cd03794 234 TLLEAAERLKRrpDIRFLFVGDGDEkERLKELAKAR-GLDNVTFLGRVPKEEVPELLSAAdvglvplkdnpanrGSSPSK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 267 meglsqaLLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRALVRREFTLER 346
Cdd:cd03794 313 -------LFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREK 385
|
....*.
gi 1125431435 347 TAERTE 352
Cdd:cd03794 386 LADRLL 391
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
18-345 |
2.37e-20 |
|
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).
Pssm-ID: 340850 [Multi-domain] Cd Length: 357 Bit Score: 90.85 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 18 AGSTQSIFDLGQHLARRGHRVLV-----GCRADVLLARLARDAGLPVVPLSFLP------------RGVLARALEDLLAR 80
Cdd:cd03823 15 GGAEISVHDLAEALVAEGHEVAVltagvGPPGQATVARSVVRYRRAPDETLPLAlkrrgyelfetyNPGLRRLLARLLED 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 81 ERVDVVNSHATLDRRALTWMRWRGRLPQAfVVTRRTMPRTSPVELLpVGLTADRTIAVSEAVARALRRRLHPGARLRVVP 160
Cdd:cd03823 95 FRPDVVHTHNLSGLGASLLDAARDLGIPV-VHTLHDYWLLCPRQFL-FKKGGDAVLAPSRFTANLHEANGLFSARISVIP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 161 NGIALERvdappppadlaAARAALGDPGGRPVVAMVSRL---KDQHVVLQA-LPLIQRGVVVACVGTEPDGRLgALAQAL 236
Cdd:cd03823 173 NAVEPDL-----------APPPRRRPGTERLRFGYIGRLteeKGIDLLVEAfKRLPREDIELVIAGHGPLSDE-RQIEGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 237 PDRHRVVFVPlSERALAFYHLATVAALPSR-MEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPLDPAAWAE 315
Cdd:cd03823 241 RRIAFLGRVP-TDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAA 319
|
330 340 350
....*....|....*....|....*....|
gi 1125431435 316 ALERLLGDGALARRLAHAGRALVRREFTLE 345
Cdd:cd03823 320 AMRRLLTDPALLERLRAGAEPPRSTESQAE 349
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
19-340 |
1.60e-19 |
|
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: 88.89 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 19 GSTQSIFDLGQHLARRGHRVLV-----GCRADVLLARLARDAGLPV-----VPLSFLPRGVLARaledLLARERVDVVNS 88
Cdd:cd03814 15 GVVRTLERLVDHLRRRGHEVRVvapgpFDEAESAEGRVVSVPSFPLpfypeYRLALPLPRRVRR----LIKEFQPDIIHI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 89 hATLDRRALTWMRWRGRLPQAFVVTRRT-----MPRTSPVELLPVGLT--------ADRTIAVSEAVARALRRrlHPGAR 155
Cdd:cd03814 91 -ATPGPLGLAALRAARRLGLPVVTSYHTdfpeyLSYYTLGPLSWLAWAylrwfhnpFDTTLVPSPSIARELEG--HGFER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 156 LRVVPNGIALERVDAPPPPADLAAARaalgDPGGRPVVAMVSRL---KDQHVVLQA-LPLIQR-GVVVACVGTEPDgrLG 230
Cdd:cd03814 168 VRLWPRGVDTELFHPSRRDAALRRRL----GPPGRPLLLYVGRLapeKNLEALLDAdLPLAASpPVRLVVVGDGPA--RA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 231 ALAQALPDrhrVVFV-PLSERALAFYHL-ATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPL 308
Cdd:cd03814 242 ELEARGPD---VIFTgFLTGEELARAYAsADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPG 318
|
330 340 350
....*....|....*....|....*....|..
gi 1125431435 309 DPAAWAEALERLLGDGALARRLAHAGRALVRR 340
Cdd:cd03814 319 DAAAFAAALRALLEDPELRRRMAARARAEAER 350
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
8-352 |
2.54e-17 |
|
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: 82.42 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 8 ILQLT-----HQGGPAgstQSIFDLGQHLARRGHRVLVGCRADVLLARLARDAGLPVVPLSFLPRGVLARA--------- 73
Cdd:cd03821 2 ILHVTpsispKAGGPV---KVVLRLAAALAALGHEVTIVSTGDGYESLVVEENGRYIPPQDGFASIPLLRQgagrtdfsp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 74 -LEDLLARE--RVDVVNSHATLDR---RALTWMRWRGRlpqAFVVTRRTM------PRTSPVELLPVGLTADR------- 134
Cdd:cd03821 79 gLPNWLRRNlrEYDVVHIHGVWTYtslAACKLARRRGI---PYVVSPHGMldpwalQQKHWKKRIALHLIERRnlnnaal 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 135 TIAVSEAVARALRRrLHPGARLRVVPNGIALERVDAPPPPADLAaaraalGDPGGRPVVAMVSRL---KDQHVVLQALPL 211
Cdd:cd03821 156 VHFTSEQEADELRR-FGLEPPIAVIPNGVDIPEFDPGLRDRRKH------NGLEDRRIILFLGRIhpkKGLDLLIRAARK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 212 IQ---RGVVVACVGTEPDGRLGALAQ--ALPDRHRVVFV-PLSERAL-AFYHLATVAALPSRMEGLSQALLEAMALGLPV 284
Cdd:cd03821 229 LAeqgRDWHLVIAGPDDGAYPAFLQLqsSLGLGDRVTFTgPLYGEAKwALYASADLFVLPSYSENFGNVVAEALACGLPV 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 285 VASDAGGNPEMVRSGeTGLLVRPlDPAAWAEALERLLGDGALARRLAHAGRALVRRE--FTLERTAERTE 352
Cdd:cd03821 309 VITDKCGLSELVEAG-CGVVVDP-NVSSLAEALAEALRDPADRKRLGEMARRARQVEenFSWEAVAGQLG 376
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
188-346 |
6.14e-17 |
|
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340826 [Multi-domain] Cd Length: 355 Bit Score: 81.17 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 188 GGRPVVAMVSRL---KDQHVVLQALPLIQRGVVVACVGTEPDgRLGALAqALPDRHRVVFV-PLSERALA-FYHLATVAA 262
Cdd:cd03795 189 KGKKIFLFIGRLvyyKGLDYLIEAAQYLNYPIVIGGEGPLKP-DLEAQI-ELNLLDNVKFLgRVDDEEKViYLHLCDVFV 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 263 LPS--RMEGLSQALLEAMALGLPVVASD-AGGNPEMVRSGETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRALVR 339
Cdd:cd03795 267 FPSvlRSEAFGIVLLEAMMCGKPVISTNiGTGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFE 346
|
....*..
gi 1125431435 340 REFTLER 346
Cdd:cd03795 347 ELFTAEK 353
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
136-354 |
7.80e-17 |
|
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340860 [Multi-domain] Cd Length: 365 Bit Score: 80.96 E-value: 7.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 136 IAVSEAVARALRRRLHPGARLRVVPNGIALERVDAppppadlaaaraalGDPGGR-PVVAMVSRL---KDQHVVLQALPL 211
Cdd:cd05844 148 VAVSGFIRDRLLARGLPAERIHVHYIGIDPAKFAP--------------RDPAERaPTILFVGRLvekKGCDVLIEAFRR 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 212 IQRGVVVACVGTEPDGRLGALAQALPDR-HRVVF---------VPLSERALAFYhLATVAALPSRMEGLSQALLEAMALG 281
Cdd:cd05844 214 LAARHPTARLVIAGDGPLRPALQALAAAlGRVRFlgalphaevQDWMRRAEIFC-LPSVTAASGDSEGLGIVLLEAAACG 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125431435 282 LPVVASDAGGNPEMVRSGETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRALVRREFTLERTAERTEAV 354
Cdd:cd05844 293 VPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFDIRVQTAKLEAI 365
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
186-348 |
1.06e-14 |
|
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: 74.66 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 186 DPGgRPVVAMVSR---LKDQHVVLQALPLIQRGVV----VACVGTEPDGRLGAL----AQALPDRHRVVFV---PLSERA 251
Cdd:cd03792 194 DPE-RPYILQVARfdpSKDPLGVIDAYKLFKRRAEepqlVICGHGAVDDPEGSVvyeeVMEYAGDDHDIHVlrlPPSDQE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 252 L-AFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPLDPAawAEALERLLGDGALARRL 330
Cdd:cd03792 273 InALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGA--AVRILRLLTDPELRRKM 350
|
170
....*....|....*...
gi 1125431435 331 AHAGRALVRREFTLERTA 348
Cdd:cd03792 351 GLAAREHVRDNFLITGNL 368
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
11-357 |
1.44e-14 |
|
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274943 [Multi-domain] Cd Length: 373 Bit Score: 74.36 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 11 LTHQGGPAGSTQSIFDLGQHLARRGHRVLVGCRADVLLARlARDAGLPV--VPLSFLPRGVLA----------RALEDLL 78
Cdd:TIGR04047 5 LTYSTKPRGGVVHTLELAEALTALGHDVTVWALAADGFGF-FRDPPCAVrlVPVAPAPGDTDAmveqriarsiDHLRAHF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 79 AReRVDVVNSHATLDRRALTWMRWRGRLPQaFVVTRRTMPRTSPVELLPVG----LTADRTIAVSEAVARALRRRLhpGA 154
Cdd:TIGR04047 84 AR-GFDVVHAQDCISGNALATLRAEGLIPG-FVRTVHHLDDFDDPRLAACQeraiVEADAVLCVSAAWAAELRAEW--GI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 155 RLRVVPNGIALERVDAPPPPADLAAARAAlGDPGGRPVVAM---------VSRLKDQHVVLQALPLIQrgVVVACVGTEP 225
Cdd:TIGR04047 160 DATVVPNGVDAARFSPAADAADAALRRRL-GLRGGPYVLAVggieprkntIDLLEAFALLRARRPQAQ--LVIAGGATLF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 226 D-----GRLGALAQALPDRHRVVFV--PLSERAL-AFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVR 297
Cdd:TIGR04047 237 DydayrREFRARAAELGVDPGPVVItgPVPDADLpALYRCADAFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYLG 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 298 sGETGLLVRPLDPAAWAEALERLLgDGALARRLAHAGRALVRReFTLERTAERTEAVYRE 357
Cdd:TIGR04047 317 -RFDAAWADPSDPDSIADALALAL-DPARRPALRAAGPELAAR-YTWDASARAHLEFYRR 373
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
148-350 |
1.83e-14 |
|
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).
Pssm-ID: 340845 [Multi-domain] Cd Length: 396 Bit Score: 73.94 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 148 RRLHPGA---RLRVVPNGIALERVDAPPPPADLAAARAALgdPGGRPVVAMVSR----LKDQHVVLQALPLIQR---GVV 217
Cdd:cd03818 170 RSLFPAAyrdRISVIHDGVDTDRLAPDPAARLRLLNGTEL--KAGDPVITYVARnlepYRGFHVFMRALPRIQArrpDAR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 218 VACVGTE--------PDG---RLGALAQALPDRHRVVFVPLSERA--LAFYHLATVAALPSRMEGLSQALLEAMALGLPV 284
Cdd:cd03818 248 VVVVGGDgvsygsppPDGgswKQKMLAELGVDLERVHFVGKVPYDqyVRLLQLSDAHVYLTYPFVLSWSLLEAMACGCPV 327
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1125431435 285 VASDAGGNPEMVRSGETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRALVRREFTLERTAER 350
Cdd:cd03818 328 IGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCLAR 393
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
275-350 |
3.27e-14 |
|
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: 73.39 E-value: 3.27e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1125431435 275 LEAMALGLPVVASDAGGNPEMVRSGETGLLVRPlDPAAWAEALERLLGDGALARRLAHAGRALVRREFTLERTAER 350
Cdd:cd03805 317 LEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAER 391
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
195-305 |
6.19e-14 |
|
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: 6.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 195 MVSRL---KDQHVVLQALPLI----QRGVVVACVGTEPDGRLGALAQALPDRHRVVFV---PLSERALAFYHLATVAALP 264
Cdd:cd01635 115 SVGRLvpeKGIDLLLEALALLkarlPDLVLVLVGGGGEREEEEALAAALGLLERVVIIgglVDDEVLELLLAAADVFVLP 194
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1125431435 265 SRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLV 305
Cdd:cd01635 195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
190-357 |
6.67e-13 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 69.51 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 190 RPVVAMVSRLKDQ---HVVLQALP-LIQRGVVVACVGT---EPDGRLGALAQALPDRHRVVFVPlSEralAFYHLATVAA 262
Cdd:cd03791 294 APLFGFVGRLTEQkgvDLILDALPeLLEEGGQLVVLGSgdpEYEQAFRELAERYPGKVAVVIGF-DE---ALAHRIYAGA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 263 ----LPSRME--GLSQalLEAMALGLPVVASDAGGNPEMVRSGE------TGLLVRPLDPAAWAEALERLLgdgALARRL 330
Cdd:cd03791 370 dfflMPSRFEpcGLVQ--MYAMRYGTLPIVRRTGGLADTVFDYDpetgegTGFVFEDYDAEALLAALRRAL---ALYRNP 444
|
170 180 190
....*....|....*....|....*....|.
gi 1125431435 331 AHAgRALVRR----EFTLERTAERTEAVYRE 357
Cdd:cd03791 445 ELW-RKLQKNamkqDFSWDKSAKEYLELYRS 474
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
19-166 |
3.86e-12 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 64.09 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 19 GSTQSIFDLGQHLARRGHRVLVGCRAD--VLLARLARDAGLPVVPLSFLPRGVL----ARALEDLLARERVDVVNSH-AT 91
Cdd:pfam13439 2 GVERYVLELARALARRGHEVTVVTPGGpgPLAEEVVRVVRVPRVPLPLPPRLLRslafLRRLRRLLRRERPDVVHAHsPF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 92 LDRRALTWMRWRGRLPqaFVVTR-RTMPRTSPVELLPVGLT-------------ADRTIAVSEAVARALRRRLH-PGARL 156
Cdd:pfam13439 82 PLGLAALAARLRLGIP--LVVTYhGLFPDYKRLGARLSPLRrllrrlerrllrrADRVIAVSEAVADELRRLYGvPPEKI 159
|
170
....*....|
gi 1125431435 157 RVVPNGIALE 166
Cdd:pfam13439 160 RVIPNGVDLE 169
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
131-340 |
6.92e-12 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 66.27 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 131 TADRTIAVSEAVARALRR-RLHPGARLRVVPNGIALERVDAPPPPADLAAARAAlGDPGgRPVVAMVSR------LKDQH 203
Cdd:PLN02871 205 AADLTLVTSPALGKELEAaGVTAANRIRVWNKGVDSESFHPRFRSEEMRARLSG-GEPE-KPLIVYVGRlgaeknLDFLK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 204 VVLQALPliqrGVVVACVGTEP-DGRLGALAQALPdrhrVVFVPL--SERALAFYHLATVAALPSRMEGLSQALLEAMAL 280
Cdd:PLN02871 283 RVMERLP----GARLAFVGDGPyREELEKMFAGTP----TVFTGMlqGDELSQAYASGDVFVMPSESETLGFVVLEAMAS 354
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125431435 281 GLPVVASDAGGNPEMV---RSGETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRALVRR 340
Cdd:PLN02871 355 GVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEK 417
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
257-342 |
2.30e-11 |
|
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.
Pssm-ID: 340829 [Multi-domain] Cd Length: 350 Bit Score: 64.39 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 257 LATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRA 336
Cdd:cd03799 256 APSVTAADGDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRA 335
|
....*.
gi 1125431435 337 LVRREF 342
Cdd:cd03799 336 RVEEEY 341
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
27-357 |
9.00e-11 |
|
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: 62.31 E-value: 9.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 27 LGQHLARRGHRVLVGCRAD-VLLARLARDAGLPVVPLSFLPRGVLARALEDLLARER---VDVVNSHAtldrraLTWMRW 102
Cdd:cd03802 27 LTEGLVRRGHEVTLFAPGDsHTSAPLVAVIPRALRLDPIPQESKLAELLEALEVQLRasdFDVIHNHS------YDWLPP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 103 RGRLPQAFVVTRRTMPRTSPVELLPVGLTADRTIAVSeavaRALRRRLHPGARLRVVPNGIALERVDAPpppadlaaara 182
Cdd:cd03802 101 FAPLIGTPFVTTLHGPSIPPSLAIYAAEPPVNYVSIS----DAQRAATPPIDYLTVVHNGLDPADYRFQ----------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 183 algdPGGRPVVAMVSRL---KDQHVVLQALPLIQRGVVVACVGTEPDG--RLGALAqALPDRHRVVFVPLSERAlafYHL 257
Cdd:cd03802 166 ----PDPEDYLAFLGRIapeKGLEDAIRVARRAGLPLKIAGKVRDEDYfyYLQEPL-PGPRIEFIGEVGHDEKQ---ELL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 258 ATVAAL--PSRME---GLsqALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPldpaaWAEALERLLGDGALARRlah 332
Cdd:cd03802 238 GGARALlfPINWDepfGL--VMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDS-----VEEMAEAIANIDRIDRA--- 307
|
330 340
....*....|....*....|....*
gi 1125431435 333 AGRALVRREFTLERTAERTEAVYRE 357
Cdd:cd03802 308 ACRRYAEDRFSAARMADRYEALYRK 332
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
190-361 |
1.03e-10 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 62.83 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 190 RPVVAMVSRLKDQ---HVVLQALP-LIQRGVVVACVGT-EPD--GRLGALAQALPDRHRVV--FvplSErALAfyHL--- 257
Cdd:PRK00654 282 APLFAMVSRLTEQkglDLVLEALPeLLEQGGQLVLLGTgDPEleEAFRALAARYPGKVGVQigY---DE-ALA--HRiya 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 258 -ATVAALPSRME--GLSQalLEAMALG-LPVVASDAG-------GNPEMvRSGeTGLLVRPLDPAAWAEALERLL---GD 323
Cdd:PRK00654 356 gADMFLMPSRFEpcGLTQ--LYALRYGtLPIVRRTGGladtvidYNPED-GEA-TGFVFDDFNAEDLLRALRRALelyRQ 431
|
170 180 190
....*....|....*....|....*....|....*...
gi 1125431435 324 GALARRLAHAGralVRREFTLERTAERTEAVYREALAR 361
Cdd:PRK00654 432 PPLWRALQRQA---MAQDFSWDKSAEEYLELYRRLLGK 466
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
262-350 |
1.09e-10 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 57.61 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 262 ALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRplDPAAWAEALERLLGDGALARRLAHAGRALVRRE 341
Cdd:pfam13524 4 NPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERVLAE 81
|
....*....
gi 1125431435 342 FTLERTAER 350
Cdd:pfam13524 82 HTYAHRAEQ 90
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
103-354 |
2.09e-10 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 61.73 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 103 RGRLPQAFVVtrrtMPRTSPVEllPVGLTADRTIAVSEAVARALRRRLHPGARLRVVPNGIALERVDAPPPPADLAAARA 182
Cdd:PRK15484 116 RERAPQAKLV----MHMHNAFE--PELLDKNAKIIVPSQFLKKFYEERLPNADISIVPNGFCLETYQSNPQPNLRQQLNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 183 ALGDP----GGRpvvamVSRLKDQHVVLQALPLIQRG------VVVACVGTEPDGRLGA-------LAQALPDR-HRVVF 244
Cdd:PRK15484 190 SPDETvllyAGR-----ISPDKGILLLMQAFEKLATAhsnlklVVVGDPTASSKGEKAAyqkkvleAAKRIGDRcIMLGG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 245 VPlSERALAFYHLATVAALPSRM-EGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGL-LVRPLDPAAWAEALERLLG 322
Cdd:PRK15484 265 QP-PEKMHNYYPLADLVVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYhLAEPMTSDSIISDINRTLA 343
|
250 260 270
....*....|....*....|....*....|..
gi 1125431435 323 DGALArRLAHAGRALVRREFTLERTAERTEAV 354
Cdd:PRK15484 344 DPELT-QIAEQAKDFVFSKYSWEGVTQRFEEQ 374
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
190-358 |
6.52e-10 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 60.49 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 190 RPVVAMVSRLKDQ---HVVLQALP-LIQRGVVVACVGT-EPD--GRLGALAQALPDRHRVVF---VPLSERALAfyhlat 259
Cdd:COG0297 295 APLIGMVSRLTEQkglDLLLEALDeLLEEDVQLVVLGSgDPEyeEAFRELAARYPGRVAVYIgydEALAHRIYA------ 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 260 vAA----LPSRME--GLSQalLEAMALG-LPVVaSDAGG--------NPEMvrSGETGLLVRPLDPAAWAEALERllgdg 324
Cdd:COG0297 369 -GAdfflMPSRFEpcGLNQ--MYALRYGtVPIV-RRTGGladtvidyNEAT--GEGTGFVFDEYTAEALLAAIRR----- 437
|
170 180 190
....*....|....*....|....*....|....*....
gi 1125431435 325 ALA-RRLAHAGRALVRR----EFTLERTAERTEAVYREA 358
Cdd:COG0297 438 ALAlYRDPEAWRKLQRNamkqDFSWEKSAKEYLELYREL 476
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
131-356 |
1.20e-08 |
|
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.
Pssm-ID: 340849 [Multi-domain] Cd Length: 370 Bit Score: 56.24 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 131 TADRTIAVSEAVARALRR-RLHPGARLRVVPNGIalervdaPPPPADLAAARAALGDPGGRPVVAM---VSRLKDQHVVL 206
Cdd:cd03822 134 LSERVVVMAPISRFLLVRiKLIPAVNIEVIPHGV-------PEVPQDPTTALKRLLLPEGKKVILTfgfIGPGKGLEILL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 207 QALPLI----QRGVVVACVGTEPD---GRLGALAQALPDRHRVV--------FVPLSErALAFYHLATVAALP--SRMEG 269
Cdd:cd03822 207 EALPELkaefPDVRLVIAGELHPSlarYEGERYRKAAIEELGLQdhvdfhnnFLPEEE-VPRYISAADVVVLPylNTEQS 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 270 LSQALLEAMALGLPVVASDAGGNPEMVRSGEtGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRALvRREFTLERTAE 349
Cdd:cd03822 286 SSGTLSYAIACGKPVISTPLRHAEELLADGR-GVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAY-ARAMTWESIAD 363
|
....*..
gi 1125431435 350 RTEAVYR 356
Cdd:cd03822 364 RYLRLFN 370
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
226-337 |
2.57e-08 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 55.81 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 226 DGRL----GALAQALPDRHRVVFVPLSERALAFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGET 301
Cdd:PRK15179 556 GGPLlesvREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVT 635
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1125431435 302 GLLVRPLDPAA--WAEALERLL----GDGALARRLAHAGRAL 337
Cdd:PRK15179 636 GLTLPADTVTApdVAEALARIHdmcaADPGIARKAADWASAR 677
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
132-355 |
6.75e-08 |
|
GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.
Pssm-ID: 411604 [Multi-domain] Cd Length: 489 Bit Score: 54.17 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 132 ADRTIAVSEAvarALRRRLHPGA---RLRVVPNGIALERVDAPPPPAdlaaaraalgDPGGRPVVAMVSR---LKDQHVV 205
Cdd:NF038011 258 ADPIVALYEG---NRLRQIADGAppeRTRVIPNGIDLPRLAPLRAQR----------PAGIPPVVGLIGRvvpIKDIKTF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 206 LQALpliqRGVVVA-------CVGTEPDGRLGA-----LAQALPDRHRVVFvplseraLAFYHLAT------VAALPSRM 267
Cdd:NF038011 325 IRAM----RTVVRAmpeaegwIVGPEEEDPAYAaecrsLVASLGLQDKVKF-------LGFQKIDDllpqvgLMVLSSIS 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 268 EGLSQALLEAMALGLPVVASDAGGNPEMVRS--------GETGLLVRPLDPAAWAEALERLLGDGALARRLAHAGRALVR 339
Cdd:NF038011 394 EALPLVVLEAFAAGVPVVTTDVGSCRQLIEGldeedralGAAGEVVAIADPQALARAALDLLRDPQRWQAAQAAGLARVE 473
|
250
....*....|....*.
gi 1125431435 340 REFTLERTAERTEAVY 355
Cdd:NF038011 474 RYYTEELMFDRYRELY 489
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
19-162 |
1.50e-07 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 50.48 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 19 GSTQSIFDLGQHLARRGHRVLVGCRADVLLARLARDAGLPVVPLSFLPRGVL------ARALEDLLARERVDVVNSHATL 92
Cdd:pfam13579 2 GIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPVPPRPSPladlaaLRRLRRLLRAERPDVVHAHSPT 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125431435 93 DRRALTWMRWRGRLPqaFVVTRRTMPRTSPVELLP---------VGLTADRTIAVSEAVARALRRRLHPGARLRVVPNG 162
Cdd:pfam13579 82 AGLAARLARRRRGVP--LVVTVHGLALDYGSGWKRrlaralerrLLRRADAVVVVSEAEAELLRALGVPAARVVVVPNG 158
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
255-340 |
1.55e-07 |
|
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.
Pssm-ID: 340855 [Multi-domain] Cd Length: 328 Bit Score: 52.69 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 255 YHLATVAALPSRMEGLSQALLEAMALGLPVVASDAG-GNPEMVRSGETGLLVRPLDPAAWAEALERLLGDGALARRLAHA 333
Cdd:cd04949 232 YQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEE 311
|
....*..
gi 1125431435 334 GRALVRR 340
Cdd:cd04949 312 SYKIAEK 318
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
239-355 |
2.85e-07 |
|
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.
Pssm-ID: 340857 [Multi-domain] Cd Length: 360 Bit Score: 51.68 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 239 RHRVVFVPLSERALAFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVrsGETGLLVRPLDPAAWAEALE 318
Cdd:cd04951 244 VDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVV--GDHNYVVPVSDPQLLAEKIK 321
|
90 100 110
....*....|....*....|....*....|....*..
gi 1125431435 319 RLLGDGALARRLAHAGRALVRREFTLERTAERTEAVY 355
Cdd:cd04951 322 EIFDMSDEERDILGNKNEYIAKNFSINTIVNEWERLY 358
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
228-304 |
2.01e-06 |
|
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.
Pssm-ID: 340854 [Multi-domain] Cd Length: 401 Bit Score: 49.38 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 228 RLGALAQALPDRHRVVF---VPLSErALAFY--HLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETG 302
Cdd:cd04946 271 RLEKLAENKLENVKVNFtgeVSNKE-VKQLYkeNDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNG 349
|
..
gi 1125431435 303 LL 304
Cdd:cd04946 350 LL 351
|
|
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
235-326 |
5.40e-06 |
|
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.
Pssm-ID: 274147 [Multi-domain] Cd Length: 1050 Bit Score: 48.62 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 235 ALPDRHRVVFVPlseralAFYHLAT----VAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPLDP 310
Cdd:TIGR02468 551 AYPKHHKQSDVP------DIYRLAAktkgVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQ 624
|
90
....*....|....*.
gi 1125431435 311 AAWAEALERLLGDGAL 326
Cdd:TIGR02468 625 QAIADALLKLVADKQL 640
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
132-324 |
1.24e-05 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).
Pssm-ID: 340840 [Multi-domain] Cd Length: 357 Bit Score: 46.90 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 132 ADRTIAVSEAVARALRRRLHPGaRLRVVPNGIALERVDAPPPPADLAAARAALGDpggRPVVAMVSRLKDQ--HV----V 205
Cdd:cd03812 137 STKYLACSEDAGEWLFGEVENG-KFKVIPNGIDIEKYKFNKEKRRKRRKLLILED---KLVLGHVGRFNEQknHSflidI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 206 LQALPLIQRGVVVACVGT-EPDGRLGALAQALPDRHRVVFVPLSERALAFYHLATVAALPSRMEGLSQALLEAMALGLPV 284
Cdd:cd03812 213 FEELKKKNPNVKLVLVGEgELKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPC 292
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1125431435 285 VASDAGGNPEMVRSGETGLlvrPLD--PAAWAEALERLLGDG 324
Cdd:cd03812 293 LLSDTITKECDITNNVEFL---PLNetPSTWAEKILKLIKRK 331
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
226-305 |
5.88e-05 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 45.08 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 226 DGRLGALAQALPDR----HRVVFVPLSERALAFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGET 301
Cdd:PRK15490 437 DGDLRAEAQKRAEQlgilERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGSAECFIEGVS 516
|
....
gi 1125431435 302 GLLV 305
Cdd:PRK15490 517 GFIL 520
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
273-319 |
2.02e-04 |
|
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: 43.04 E-value: 2.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1125431435 273 ALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPLDPAAWAEALER 319
Cdd:cd03804 280 VPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEE 326
|
|
| COG4641 |
COG4641 |
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]; |
208-359 |
3.78e-04 |
|
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443679 [Multi-domain] Cd Length: 303 Bit Score: 41.84 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 208 ALPLIQRGVVVACVGTEPDGRLGALAQA---LPDRHRVVFVplseRALAFYHLATVAALPSrmeGLSQALLEAMALGLPV 284
Cdd:COG4641 158 LLAPAGLRLKIYGPGWPKLALPANVRRGghlPGEEHPAAYA----SSKITLNVNRMAASPD---SPTRRTFEAAACGAFL 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125431435 285 VASDAGGNPEMVRSGETGLLVRplDPAAWAEALERLLGDGALARRLAHAGRALVRREFTLERTAERTEAVYREAL 359
Cdd:COG4641 231 LSDPWEGLEELFEPGEEVLVFR--DGEELAEKLRYLLADPEERRAIAEAGRRRVLAEHTYAHRARELLAILEELG 303
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
224-361 |
1.01e-03 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 40.87 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 224 EPDGRLGALAQALPDRHRVVFvplsERALAFYHLAtVAAL-----PSRMEGLSQALLEAMALGLPVVASDAGGNPEMV-- 296
Cdd:PRK14098 348 EYEKRFQDFAEEHPEQVSVQT----EFTDAFFHLA-IAGLdmllmPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETIee 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125431435 297 ---RSGeTGLLVRPLDPAAWAEALE---RLLGDGALARRLAHagRALVRReFTLERTAERTEAVYREALAR 361
Cdd:PRK14098 423 vseDKG-SGFIFHDYTPEALVAKLGealALYHDEERWEELVL--EAMERD-FSWKNSAEEYAQLYRELLGP 489
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
189-364 |
1.32e-03 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 40.47 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 189 GRPVVAMVSRLKDQH---VVLQALPLIQR-GVVVACVG---TEPDGRLGALAQALPDRHRVVFVplSERALAFYHLATVA 261
Cdd:PRK14099 294 DALLLGVISRLSWQKgldLLLEALPTLLGeGAQLALLGsgdAELEARFRAAAQAYPGQIGVVIG--YDEALAHLIQAGAD 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 262 AL--PSRME--GLSQalLEAMALG-LPVVASDAGGNPEMVRSGE--------TGLLVRPLDPAAWAEALER---LLGDGA 325
Cdd:PRK14099 372 ALlvPSRFEpcGLTQ--LCALRYGaVPVVARVGGLADTVVDANEmaiatgvaTGVQFSPVTADALAAALRKtaaLFADPV 449
|
170 180 190
....*....|....*....|....*....|....*....
gi 1125431435 326 LARRLAHAGRALvrrEFTLERTAERTEAVYREALARRAP 364
Cdd:PRK14099 450 AWRRLQRNGMTT---DVSWRNPAQHYAALYRSLVAERRP 485
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
29-374 |
1.48e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 40.63 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 29 QHLARRGHRVLVGCRADVLLARLARD---AGLPVVPLSFLPRGV-----LARALEDLLA---------------RERVD- 84
Cdd:COG3321 784 EALLADGVRVFLEVGPGPVLTGLVRQclaAAGDAVVLPSLRRGEdelaqLLTALAQLWVagvpvdwsalypgrgRRRVPl 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 85 --------------VVNSHATLDRRALTWMRWRGRLPQAFVVTRRTMPRTSPVELLPVGLTADRTIAVSEAVARALRRRL 150
Cdd:COG3321 864 ptypfqredaaaalLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALL 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 151 HPGARLRVVPNGIALERVDAPPPPADLAAARAALGDPGGRPVVAMVSRLKDQHVVLQALPLIQRGVVVACVGTEPDGRLG 230
Cdd:COG3321 944 ALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLA 1023
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 231 ALAQALPDRHRVVFVPLSERALAFYHLATVAALPSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETGLLVRPLDP 310
Cdd:COG3321 1024 LAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALA 1103
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125431435 311 AAWAEALERLLGDGALARRLAHAGRALVRREFTLERTAERTEAVYREALARRAPGRLLAAAAPR 374
Cdd:COG3321 1104 AALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAAL 1167
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
264-361 |
2.32e-03 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 39.53 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431435 264 PSRMEGLSQALLEAMALGLPVVASDAGGNPEMVRSGETgLLVRPlDPAAWAEALERLLGDGALARRLAHAGRALVRREFT 343
Cdd:cd03796 276 TSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMI-LLAEP-DPEDIVRKLEEAISILRTGKHDPWSFHNRVKKMYS 353
|
90
....*....|....*...
gi 1125431435 344 LERTAERTEAVYREALAR 361
Cdd:cd03796 354 WEDVARRTEKVYDRILST 371
|
|
| |
