|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
2-356 |
0e+00 |
|
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: 575.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 2 RVLHFYKTYLSEtVGGIEQVIFQLCESSGSWGIDNHVLTLSSDPHPPVVPFGGHVVHRARLDLQLASTGFSLSVFKQFRE 81
Cdd:cd03795 1 KVLHVFKFYYPD-IGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIRIHRVKSFLNVASTPFSPSYIKRFKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 82 LAAEADVVNYHFPWPFMDLVHFLTGMNKPSVVTYHSDIIRQRVLLKLYRPLMSRFLHSVDRIVAASPNYFSTSDVLRQYR 161
Cdd:cd03795 80 LAKEYDIIHYHFPNPLADLLLFFSGAKKPVVVHWHSDIVKQKKLLKLYKPLMTRFLRRADRIIATSPNYVETSPTLREFK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 162 EKTRVITYGLDKDGYPKPATQRLEHWREKLGPRFFLFVGVMRYYKGLHILLDALQGTDYPVVIVGAGPLQAELYAQAAAL 241
Cdd:cd03795 160 NKVRVIPLGIDKNVYNIPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLIEAAQYLNYPIVIGGEGPLKPDLEAQIELN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 242 GLRNVHFLGRVDDEDKVALLQLSYAMVFPSHLRSEAFGISLLEGAMYGKPMISSEIGTGTSYINIHGETGLVVPPSQPAA 321
Cdd:cd03795 240 LLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNNGETGLVVPPKDPDA 319
|
330 340 350
....*....|....*....|....*....|....*
gi 15600640 322 FRQAMRWLWEHPQQAEEMGRNAEARYRQLFTAEEM 356
Cdd:cd03795 320 LAEAIDKLLSDEELRESYGENAKKRFEELFTAEKM 354
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-365 |
1.47e-57 |
|
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: 191.60 E-value: 1.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 2 RVLHFyKTYLSETVGGIEQVIFQLCESSGSWGIDNHVLTLSSDPHPPVvPFGGHVVHRARLDLQLASTGFSLSVFKQFRE 81
Cdd:cd03801 1 KILLL-SPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPE-ELEDGVIVPLLPSLAALLRARRLLRELRPLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 82 LAAEADVVNYHFPWPFMDLVHFLTGMNKPSVVTYHS-DIIRQRVLLKLYRPLMSR---FLHSVDRIVAASPnyfSTSDVL 157
Cdd:cd03801 79 RLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGaEPGRLLLLLAAERRLLARaeaLLRRADAVIAVSE---ALRDEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 158 RQY----REKTRVITYGLDKDGYPKPATQRLEHwreKLGPRFFLFVGVMRYYKGLHILLDAL-----QGTDYPVVIVGA- 227
Cdd:cd03801 156 RALggipPEKIVVIPNGVDLERFSPPLRRKLGI---PPDRPVLLFVGRLSPRKGVDLLLEALakllrRGPDVRLVIVGGd 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 228 GPLQAELYAQAAALGlRNVHFLGRVDDEDKVALLQLSYAMVFPShlRSEAFGISLLEGAMYGKPMISSEIGTGTSYInIH 307
Cdd:cd03801 233 GPLRAELEELELGLG-DRVRFLGFVPDEELPALYAAADVFVLPS--RYEGFGLVVLEAMAAGLPVVATDVGGLPEVV-ED 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600640 308 GETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQLFTAEEMGRRWSELYR 365
Cdd:cd03801 309 GEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
192-346 |
9.24e-39 |
|
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: 135.86 E-value: 9.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 192 GPRFFLFVGVMRYYKGLHILLDAL-----QGTDYPVVIVGAGPLQAELYAQAAALGLR-NVHFLGRVDDEDKVALLQLSY 265
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFallkeKNPNLKLVIAGDGEEEKRLKKLAEKLGLGdNVIFLGFVSDEDLPELLKIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 266 AMVFPSHlrSEAFGISLLEGAMYGKPMISSEIGtGTSYINIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEA 345
Cdd:pfam00534 81 VFVLPSR--YEGFGIVLLEAMACGLPVIASDVG-GPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157
|
.
gi 15600640 346 R 346
Cdd:pfam00534 158 R 158
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
2-355 |
1.01e-35 |
|
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: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 2 RVLHFYKTYlseTVGGIEQVIFQLCESSGSWGIDNHVLTLSSDPHPPVVPFGGHVVHRARLDLQLASTGFSLSVFKQFRE 81
Cdd:cd03811 1 KILFVIPSL---SGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 82 LAAEA--DVV-NYHFPWPFMdlVHFLTGMNKPSVVTYHSDIIRQRvLLKLYRPLMSRFLHSVDRIVAASP---NYFStsD 155
Cdd:cd03811 78 ILKRAkpDVViSFLGFATYI--VAKLAAARSKVIAWIHSSLSKLY-YLKKKLLLKLKLYKKADKIVCVSKgikEDLI--R 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 156 VLRQYREKTRVITYGLDKDGYPKPAtqRLEHWREKLGPRFFLFVGVMRYYKGLHILLDALQ-----GTDYPVVIVGAGPL 230
Cdd:cd03811 153 LGPSPPEKIEVIYNPIDIDRIRALA--KEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAklrkkYPDVKLVILGDGPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 231 QAELYAQAAALGLRN-VHFLGRVDdeDKVALLQLSYAMVFPShlRSEAFGISLLEGAMYGKPMISSEIGtGTSYINIHGE 309
Cdd:cd03811 231 REELEKLAKELGLAErVIFLGFQS--NPYPYLKKADLFVLSS--RYEGFPNVLLEAMALGTPVVSTDCP-GPREILDDGE 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15600640 310 TGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQLFTAEE 355
Cdd:cd03811 306 NGLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEAVFREYTI 351
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
15-362 |
4.18e-33 |
|
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: 126.58 E-value: 4.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 15 VGGIEQVIFQLCESSGSWGIDNHVLTLSSDPHPPVVPFGGHVVHRARLDLQLASTGFSLSVFKQFREL-----AAEADVV 89
Cdd:cd03820 12 AGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYELDDNIKIKNLGDRKYSHFKLLLKYFKKVRRLrkylkNNKPDVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 90 -NYHFPwpFMDLVHFLtGMNKPSVVTYHSDIIRQRvllKLYRPLMSRFLH--SVDRIVAaspnyFSTSDVLRQY---REK 163
Cdd:cd03820 92 iSFRTS--LLTFLALI-GLKSKLIVWEHNNYEAYN---KGLRRLLLRRLLykRADKIVV-----LTEADKLKKYkqpNSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 164 TRVItygldkdgyPKPATqrlEHWREKLGPR---FFLFVGVMRYYKGLHILLDA-----LQGTDYPVVIVGAGPLQAELY 235
Cdd:cd03820 161 VVVI---------PNPLS---FPSEEPSTNLkskRILAVGRLTYQKGFDLLIEAwaliaKKHPDWKLRIYGDGPEREELE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 236 AQAAALGLRN-VHFLGRVDDEDkvALLQLSYAMVFPShlRSEAFGISLLEgAM-YGKPMISSEIGTGTSYINIHGETGLV 313
Cdd:cd03820 229 KLIDKLGLEDrVKLLGPTKNIA--EEYANSSIFVLSS--RYEGFPMVLLE-AMaYGLPIISFDCPTGPSEIIEDGENGLL 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15600640 314 VPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQlFTAEEMGRRWSE 362
Cdd:cd03820 304 VPNGDVDALAEALLRLMEDEELRKKMGKNARKNAER-FSIEKIIKQWEE 351
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
9-360 |
7.63e-30 |
|
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: 117.85 E-value: 7.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 9 TYLSETVGGIEQVIFQLCESSGSWGIDNHVLTLSSDPHPPVVPFGGHVVHRARLDLQLASTGFSLSVFKQFRELAAEADV 88
Cdd:cd03809 7 RSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKPD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 89 VnYHFPWPFMDLVHFltgmNKPSVVTYHsDII-------RQRVLLKLYRPLMSRFLHSVDRIVAASpnYFSTSDVLRQY- 160
Cdd:cd03809 87 L-LHSPHNTAPLLLK----GCPQVVTIH-DLIplrypefFPKRFRLYYRLLLPISLRRADAIITVS--EATRDDIIKFYg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 161 --REKTRVITYGLDKDGYPKPATQRLEHwREKLGPRFFLFVGVMRYYKGLHILLDAL-----QGTDYPVVIVGA-GPLQA 232
Cdd:cd03809 159 vpPEKIVVIPLGVDPSFFPPESAAVLIA-KYLLPEPYFLYVGTLEPRKNHERLLKAFallkkQGGDLKLVIVGGkGWEDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 233 ELYAQAAALGLR-NVHFLGRVDDEDKVALLQLSYAMVFPSHlrSEAFGISLLEGAMYGKPMISSEIgtgTSYINIHGETG 311
Cdd:cd03809 238 ELLDLVKKLGLGgRVRFLGYVSDEDLPALYRGARAFVFPSL--YEGFGLPVLEAMACGTPVIASNI---SVLPEVAGDAA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15600640 312 LVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARyRQLFTAEEMGRRW 360
Cdd:cd03809 313 LYFDPLDPESIADAILRLLEDPSLREELIRKGLER-AKKFSWEKTAEKT 360
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-360 |
8.38e-29 |
|
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: 115.52 E-value: 8.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 2 RVLHFYKTYLSETvGGIEQVIFQLCESSGSWGIDNHVLTlsSDPHPPVVPFGGHV--------VHRARL---------DL 64
Cdd:cd03794 1 KILLISQYYPPPK-GAAAARVYELAKELVRRGHEVTVLT--PSPNYPLGRIFAGAtetkdgirVIRVKLgpikkngliRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 65 QLASTGFSLSVFKQFRELAAEADVVNYHFPWPFMDLVHFLTG--MNKPSVVTYHS---------DIIRQRVLLKLYRPLM 133
Cdd:cd03794 78 LLNYLSFALAALLKLLVREERPDVIIAYSPPITLGLAALLLKklRGAPFILDVRDlwpeslialGVLKKGSLLKLLKKLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 134 SRFLHSVDRIVAASPnyfSTSDVLRQ---YREKTRVITYGLDKDGYPKPATQRLEHWREKLGPRFFLFVGVMRYYKGLHI 210
Cdd:cd03794 158 RKLYRLADAIIVLSP---GLKEYLLRkgvPKEKIIVIPNWADLEEFKPPPKDELRKKLGLDDKFVVVYAGNIGKAQGLET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 211 LLDALQGT----DYPVVIVGAGPLQAELYAQAAALGLRNVHFLGRVDDEDKVALLQLSYAMVFP---SHLRSEAFGISLL 283
Cdd:cd03794 235 LLEAAERLkrrpDIRFLFVGDGDEKERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLVPlkdNPANRGSSPSKLF 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600640 284 EGAMYGKPMISSEIGTGTSYINIHGeTGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQLFTAEEMGRRW 360
Cdd:cd03794 315 EYMAAGKPILASDDGGSDLAVEING-CGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRL 390
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
20-367 |
2.05e-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: 114.01 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 20 QVIFQLCESSGSWGIDNHVLTLSSDPHPPVVPFGGHVVHRARLDLQLASTGFSLSVFKQFRelaaeADVVNYHFPWPFMD 99
Cdd:cd03798 35 EVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAPSLAKLLKRRRRGP-----PDLIHAHFAYPAGF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 100 LVHFLTGM-NKPSVVTYH-SDIIRQRVLlKLYRPLMSRFLHSVDRIVAASPnyFSTSDVLRQ--YREKTRVITYGLDKDg 175
Cdd:cd03798 110 AAALLARLyGVPYVVTEHgSDINVFPPR-SLLRKLLRWALRRAARVIAVSK--ALAEELVALgvPRDRVDVIPNGVDPA- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 176 YPKPATQRLEHwreKLGPRFFLFVGVMRYYKGLHILLDALQ--GTDYPVV---IVGAGPLQAELYAQAAALGLRN-VHFL 249
Cdd:cd03798 186 RFQPEDRGLGL---PLDAFVILFVGRLIPRKGIDLLLEAFArlAKARPDVvllIVGDGPLREALRALAEDLGLGDrVTFT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 250 GRVDDEDKVALLQLSYAMVFPShlRSEAFGISLLEGAMYGKPMISSEIGtGTSYINIHGETGLVVPP-SQPAAFRQAMRW 328
Cdd:cd03798 263 GRLPHEQVPAYYRACDVFVLPS--RHEGFGLVLLEAMACGLPVVATDVG-GIPEVVGDPETGLLVPPgDADALAAALRRA 339
|
330 340 350
....*....|....*....|....*....|....*....
gi 15600640 329 LWEHPqqAEEMGRNAEARYRQLFTAEEMGRRWSELYREL 367
Cdd:cd03798 340 LAEPY--LRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
110-343 |
4.31e-28 |
|
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: 112.83 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 110 PSVVTYHSDIIRQrvllKLYRPLMSRFLHSVDRIVAASPNyfsTSDVLRQY----REKTRVITYGLDKDGY-PKPATQRL 184
Cdd:cd03819 101 PLVTTVHGSYLAT----YHPKDFALAVRARGDRVIAVSEL---VRDHLIEAlgvdPERIRVIPNGVDTDRFpPEAEAEER 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 185 EHWREKLGPRFFLFVGVMRYYKGLHILLDALQ----GTDYPVVIVGAGPLQAELYAQAAALGLRN-VHFLGRVDDEDkvA 259
Cdd:cd03819 174 AQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAelkdEPDFRLLVAGDGPERDEIRRLVERLGLRDrVTFTGFREDVP--A 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 260 LLQLSYAMVFPShlRSEAFGISLLEGAMYGKPMISSEIGtGTSYINIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEM 339
Cdd:cd03819 252 ALAASDVVVLPS--LHEEFGRVALEAMACGTPVVATDVG-GAREIVVHGRTGLLVPPGDAEALADAIRAAKLLPEAREKL 328
|
....
gi 15600640 340 GRNA 343
Cdd:cd03819 329 QAAA 332
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
10-359 |
1.88e-27 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
Pssm-ID: 340837 [Multi-domain] Cd Length: 358 Bit Score: 111.15 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 10 YLSETVGGIEQVIFQLCESSGSWGIDNHVltlssdphppVVPFGGHVVHRARL------DLQLASTGFS-----LSVFKQ 78
Cdd:cd03808 4 FIVNVDGGFQSFRLPLIKALVKKGYEVHV----------IAPDGDKLSDELKElgvkviDIPILRRGINplkdlKALFKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 79 FRELAAEA-DVVNYHFPWPFM--DLVHFLTGmNKPSVVTYH-------SDIIRQRVLLKLYRpLMSRFLHSV------DR 142
Cdd:cd03808 74 YKLLKKEKpDIVHCHTPKPGIlgRLAARLAG-VPKVIYTVHglgfvftEGKLLRLLYLLLEK-LALLFTDKVifvnedDR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 143 IVAASPNyfstsdvLRQYREKTRVITYGLDKDGY-PKPATQRLEHWReklgprfFLFVGVMRYYKGLHILLDAL-----Q 216
Cdd:cd03808 152 DLAIKKG-------IIKKKKTVLIPGSGVDLDRFqYSPESLPSEKVV-------FLFVARLLKDKGIDELIEAAkilkkK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 217 GTDYPVVIVGAGPLQAELYAQAAALGLR-NVHFLGRVDDedKVALLQLSYAMVFPSHlrSEAFGISLLEGAMYGKPMISS 295
Cdd:cd03808 218 GPNVRFLLVGDGELENPSEILIEKLGLEgRIEFLGFRSD--VPELLAESDVFVLPSY--REGLPRSLLEAMAAGRPVITT 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600640 296 EIGtGTSYINIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQLFTAEEMGRR 359
Cdd:cd03808 294 DVP-GCRELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNK 356
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
196-332 |
4.66e-27 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 104.52 E-value: 4.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 196 FLFVGVM-RYYKGLHILLDAL-----QGTDYPVVIVGAGPlQAELYAQAAALGlRNVHFLGRVDDedKVALLQLSYAMVF 269
Cdd:pfam13692 4 ILFVGRLhPNVKGVDYLLEAVpllrkRDNDVRLVIVGDGP-EEELEELAAGLE-DRVIFTGFVED--LAELLAAADVFVL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600640 270 PShlRSEAFGISLLEGAMYGKPMISSEIGtGTSYInIHGETGLVVPPSQPAAFRQAMRWLWEH 332
Cdd:pfam13692 80 PS--LYEGFGLKLLEAMAAGLPVVATDVG-GIPEL-VDGENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
14-365 |
1.61e-26 |
|
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: 108.56 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 14 TVGGIEQVIFQLCESSGSWGIDNHVLTLSSD---------PHPPVVPFGGHVVHRARLDLQLAstgfslsvfKQFRELAA 84
Cdd:cd03807 10 NVGGAETMLLRLLEHMDKSRFEHVVISLTGDgvlgeellaAGVPVVCLGLSSGKDPGVLLRLA---------KLIRKRNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 85 eaDVVNYHFPWP--FMDLVHFLTGmNKPSVVTYHSDIIRQRVLLKLYRplMSRFLHSVDR-IVAASPnyfstsDVLRQYR 161
Cdd:cd03807 81 --DVVHTWMYHAdlIGGLAAKLAG-GVKVIWSVRSSNIPQRLTRLVRK--LCLLLSKFSPaTVANSS------AVAEFHQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 162 E------KTRVITYGLDKDGYPKPATQRLEHWRE-KLGPRFFLFVGVMRYY--KGLHILLDAL-----QGTDYPVVIVGA 227
Cdd:cd03807 150 EqgyaknKIVVIYNGIDLFKLSPDDASRARARRRlGLAEDRRVIGIVGRLHpvKDHSDLLRAAallveTHPDLRLLLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 228 GPLQAELYAQAAALGLRN-VHFLGRVDDEDkvALLQLSYAMVFPShlRSEAFGISLLEGAMYGKPMISSEIGtGTSYInI 306
Cdd:cd03807 230 GPERPNLERLLLELGLEDrVHLLGERSDVP--ALLPAMDIFVLSS--RTEGFPNALLEAMACGLPVVATDVG-GAAEL-V 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600640 307 HGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQLFTAEEMGRRWSELYR 365
Cdd:cd03807 304 DDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
259-369 |
2.16e-26 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 101.99 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 259 ALLQLSYAMVFPShlRSEAFGISLLEGAMYGKPMISSEIGtGTSYINIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEE 338
Cdd:COG0438 16 ALLAAADVFVLPS--RSEGFGLVLLEAMAAGLPVIATDVG-GLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRR 92
|
90 100 110
....*....|....*....|....*....|.
gi 15600640 339 MGRNAEARYRQLFTAEEMGRRWSELYRELLE 369
Cdd:COG0438 93 LGEAARERAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
110-362 |
3.35e-24 |
|
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: 102.15 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 110 PSVVTYH-SDIIRQRVLLKLYRPLMSRF-LHsvdRIVAASP--NYFSTSDVLRQY-------REKTRVITYGLDkdgyPK 178
Cdd:cd05844 106 PLVVTFHgFDITTSRAWLAASPGWPSQFqRH---RRALQRPaaLFVAVSGFIRDRllarglpAERIHVHYIGID----PA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 179 PATQRLEHWREklgpRFFLFVGVMRYYKGLHILLDAL-----QGTDYPVVIVGAGPLQAELYAQAAALGlrNVHFLGRVD 253
Cdd:cd05844 179 KFAPRDPAERA----PTILFVGRLVEKKGCDVLIEAFrrlaaRHPTARLVIAGDGPLRPALQALAAALG--RVRFLGALP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 254 DEDKVALLQLSYAMVFPSHL----RSEAFGISLLEGAMYGKPMISSEIGTGTSYInIHGETGLVVPPSQPAAFRQAMRWL 329
Cdd:cd05844 253 HAEVQDWMRRAEIFCLPSVTaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEAI-LDGETGFLVPEGDVDALADALQAL 331
|
250 260 270
....*....|....*....|....*....|...
gi 15600640 330 WEHPQQAEEMGRNAEARYRQLFTAeemgRRWSE 362
Cdd:cd05844 332 LADRALADRMGGAARAFVCEQFDI----RVQTA 360
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
2-370 |
6.60e-24 |
|
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: 101.22 E-value: 6.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 2 RVLHFYKTYLSeTVGGIEQVIFQLCESSGSWGIDNHVLTlsSDPHPPVVPFGGHVVH--------RARLDLQLASTGFSL 73
Cdd:cd03814 1 RIALVTDTYHP-QVNGVVRTLERLVDHLRRRGHEVRVVA--PGPFDEAESAEGRVVSvpsfplpfYPEYRLALPLPRRVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 74 SVFKQFR----ELAAEadvvnyhFPWPFMDLvHFLTGMNKPSVVTYHSDI---IRQRVLLKLYRPL---MSRFLHSVDRI 143
Cdd:cd03814 78 RLIKEFQpdiiHIATP-------GPLGLAAL-RAARRLGLPVVTSYHTDFpeyLSYYTLGPLSWLAwayLRWFHNPFDTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 144 VAASPnyfSTSDVLRQY-REKTRVITYGLDKDGYpKPAtQRLEHWREKLGP---RFFLFVGVMRYYKGLHILLDA----L 215
Cdd:cd03814 150 LVPSP---SIARELEGHgFERVRLWPRGVDTELF-HPS-RRDAALRRRLGPpgrPLLLYVGRLAPEKNLEALLDAdlplA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 216 QGTDYPVVIVGAGPLQAELyaqaaALGLRNVHFLGRVDDEDKVALLQLSYAMVFPShlRSEAFGISLLEgAM-YGKPMIS 294
Cdd:cd03814 225 ASPPVRLVVVGDGPARAEL-----EARGPDVIFTGFLTGEELARAYASADVFVFPS--RTETFGLVVLE-AMaSGLPVVA 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600640 295 SEIGtGTSYINIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARyrqlftAEEMGrrWSELYRELLEE 370
Cdd:cd03814 297 ADAG-GPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAE------AERYS--WEAFLDNLLDY 363
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
33-365 |
3.57e-22 |
|
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: 96.24 E-value: 3.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 33 GIDNHVLTLSSDPHPP--------VVPFGGHVV----HRARLDLQLASTGFSLSVFKQFRELAAEA--DVVNYHFPWPF- 97
Cdd:cd03823 30 AEGHEVAVLTAGVGPPgqatvarsVVRYRRAPDetlpLALKRRGYELFETYNPGLRRLLARLLEDFrpDVVHTHNLSGLg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 98 MDLVHFLTGMNKPSVVTYHSdiirqrVLLKLYRPLMsrFLHSVDRIVAASpNYFstsdvLRQYRE------KTRVITYGL 171
Cdd:cd03823 110 ASLLDAARDLGIPVVHTLHD------YWLLCPRQFL--FKKGGDAVLAPS-RFT-----ANLHEAnglfsaRISVIPNAV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 172 DKDGYPKPATQRLehwREKLGprfFLFVGVMRYYKGLHILLDALQG---TDYPVVIVGAGPLQAElyaqAAALGLRNVHF 248
Cdd:cd03823 176 EPDLAPPPRRRPG---TERLR---FGYIGRLTEEKGIDLLVEAFKRlprEDIELVIAGHGPLSDE----RQIEGGRRIAF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 249 LGRVDDEDKVALLQLSYAMVFPShLRSEAFGISLLEGAMYGKPMISSEIGtGTSYINIHGETGLVVPPSQPAAFRQAMRW 328
Cdd:cd03823 246 LGRVPTDDIKDFYEKIDVLVVPS-IWPEPFGLVVREAIAAGLPVIASDLG-GIAELIQPGVNGLLFAPGDAEDLAAAMRR 323
|
330 340 350
....*....|....*....|....*....|....*..
gi 15600640 329 LWEHPQQAEEMGRNAEARYRQLFTAEEMgrrwSELYR 365
Cdd:cd03823 324 LLTDPALLERLRAGAEPPRSTESQAEEY----LKLYR 356
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
99-352 |
2.46e-21 |
|
sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
Pssm-ID: 340830 [Multi-domain] Cd Length: 398 Bit Score: 94.61 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 99 DLVH---FLTGM---------NKPSVVTYHS-DIIRQRVLLKLYRP-LMSRF------LHSVDRIVAASPN--YFSTSDV 156
Cdd:cd03800 103 DLIHshyWDSGLvgallarrlGVPLVHTFHSlGRVKYRHLGAQDTYhPSLRItaeeqiLEAADRVIASTPQeaDELISLY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 157 lRQYREKTRVITYGLDKDGYPKPATQRLEHWREKLGP--RFFLFVGVMRYYKGLHILLDAL-----QGTDYPVVIVGAG- 228
Cdd:cd03800 183 -GADPSRINVVPPGVDLERFFPVDRAEARRARLLLPPdkPVVLALGRLDPRKGIDTLVRAFaqlpeLRELANLVLVGGPs 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 229 --------PLQAELyaqAAALGLRN-VHFLGRVDDEDKVALLQLSYAMVFPSHlrSEAFGISLLEGAMYGKPMISSEIGt 299
Cdd:cd03800 262 ddplsmdrEELAEL---AEELGLIDrVRFPGRVSRDDLPELYRAADVFVVPSL--YEPFGLTAIEAMACGTPVVATAVG- 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15600640 300 GTSYINIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQLFT 352
Cdd:cd03800 336 GLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYT 388
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
2-354 |
5.10e-21 |
|
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: 93.20 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 2 RVLHfYKTYLSETVGGIEQVIFQLCESSGSWGIDNHVLTLS----SDPHPPVVPFGGHVVHRARLDLQLASTG---FSLS 74
Cdd:cd03821 1 KILH-VTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGdgyeSLVVEENGRYIPPQDGFASIPLLRQGAGrtdFSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 75 VFKQFRELAAEADVVNYHFPWPFMDL----VHFLTGMnkPSVVTYHSDI-----IRQRVLLKLYRPLmsrFLHSVDRIVA 145
Cdd:cd03821 80 LPNWLRRNLREYDVVHIHGVWTYTSLaackLARRRGI--PYVVSPHGMLdpwalQQKHWKKRIALHL---IERRNLNNAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 146 ASpnYFSTSDVLR-----QYREKTRVITYGLDKDGYPKPATQRLEHWREKlGPRFFLFVGVMRYYKGLHILLDAL----- 215
Cdd:cd03821 155 LV--HFTSEQEADelrrfGLEPPIAVIPNGVDIPEFDPGLRDRRKHNGLE-DRRIILFLGRIHPKKGLDLLIRAArklae 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 216 QGTDYPVVIVGAGPlQAELY--AQAAALGLRN-VHFLGRVDDEDKVALLQLSYAMVFPSHlrSEAFGISLLEGAMYGKPM 292
Cdd:cd03821 232 QGRDWHLVIAGPDD-GAYPAflQLQSSLGLGDrVTFTGPLYGEAKWALYASADLFVLPSY--SENFGNVVAEALACGLPV 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600640 293 ISseigtgTSYINIHGET----GLVVPPSQP---AAFRQAMRwLWEHPQQAEEMGRNAeARYRQLFTAE 354
Cdd:cd03821 309 VI------TDKCGLSELVeagcGVVVDPNVSslaEALAEALR-DPADRKRLGEMARRA-RQVEENFSWE 369
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
99-367 |
9.52e-20 |
|
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.
Pssm-ID: 340844 [Multi-domain] Cd Length: 372 Bit Score: 89.65 E-value: 9.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 99 DLVH----FLTG---------MNKPSVVTYH---SDIIRQRVLLKLY-----RPLMSRFLHSVDRIVAASPnyfSTSDVL 157
Cdd:cd03817 86 DIIHthtpFSLGklglriarkLKIPIVHTYHtmyEDYLHYIPKGKLLvkavvRKLVRRFYNHTDAVIAPSE---KIKDTL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 158 RQYREKT--RVITYGLDKDGYPKPAT--QRLEHWREKLGPRFfLFVGVMRYYKGLHILLDALQGTDYPV----VIVGAGP 229
Cdd:cd03817 163 REYGVKGpiEVIPNGIDLDKFEKPLNteERRKLGLPPDEPIL-LYVGRLAKEKNIDFLLRAFAELKKEPniklVIVGDGP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 230 LQAELYAQAAALGL-RNVHFLGRVDDEDKVALLQLSYAMVFPSHlrSEAFGISLLEGAMYGKPMISSEIGTGTSYINiHG 308
Cdd:cd03817 242 EREELKELARELGLaDKVIFTGFVPREELPEYYKAADLFVFAST--TETQGLVYLEAMAAGLPVVAAKDPAASELVE-DG 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600640 309 ETGLVVPPSQPAAFRQAMRWLwEHPQQAEEMGRNAEARYRQLftaeEMGRRWSELYREL 367
Cdd:cd03817 319 ENGFLFEPNDETLAEKLLHLR-ENLELLRKLSKNAEISAREF----AFAKSVEKLYEEV 372
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
116-314 |
4.71e-18 |
|
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: 82.45 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 116 HSDIIRQRVLLKLYRPLMSRFLHSVDRIVAASPNYFSTSDVLRQYREKTRVITYGLDKDGYPKPATQRLEHWREKLGPRF 195
Cdd:cd01635 31 HEVTVLALLLLALRRILKKLLELKPDVVHAHSPHAAALAALLAARLLGIPIVVTVHGPDSLESTRSELLALARLLVSLPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 196 F--LFVGVMRYYKGLHILLDAL-----QGTDYPVVIVGAGPLQAELYAQAAALGL--RNVHFLGRVDDEDKVALLQLSYA 266
Cdd:cd01635 111 AdkVSVGRLVPEKGIDLLLEALallkaRLPDLVLVLVGGGGEREEEEALAAALGLleRVVIIGGLVDDEVLELLLAAADV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600640 267 MVFPShlRSEAFGISLLEGAMYGKPMISSEIGtGTSYINIHGETGLVV 314
Cdd:cd01635 191 FVLPS--RSEGFGLVLLEAMAAGKPVIATDVG-GIPEFVVDGENGLLV 235
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
107-365 |
5.09e-18 |
|
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: 85.08 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 107 MNKPSVVTYHS--------DIIRQRVLLKLYRPLMSRFLHSVDRIV--AASPNYfSTSDVLRQY-------REKTRVITY 169
Cdd:cd03813 196 RGIPFLLTEHGiytrerkiEILQSTWIMGYIKKLWIRFFERLGKLAyqQADKII-SLYEGNRRRqirlgadPDKTRVIPN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 170 GLDKDGYPKPATQRlehwREKLGPRFFLfVGVMRYYKGLHILLDAL-----QGTDYPVVIVGAgPLQAELYAQ-----AA 239
Cdd:cd03813 275 GIDIQRFAPAREER----PEKEPPVVGL-VGRVVPIKDVKTFIRAFklvrrAMPDAEGWLIGP-EDEDPEYAQeckrlVA 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 240 ALGLRN-VHFLGRVDDEDKVALLQLsyaMVFPShlRSEAFGISLLEGAMYGKPMISSEIGTGTSYI----NIHGETGLVV 314
Cdd:cd03813 349 SLGLENkVKFLGFQNIKEYYPKLGL---LVLTS--ISEGQPLVILEAMASGVPVVATDVGSCRELIygadDALGQAGLVV 423
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15600640 315 PPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQLFTAEEMGRRWSELYR 365
Cdd:cd03813 424 PPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
16-367 |
2.68e-17 |
|
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: 81.95 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 16 GGIEQVIFQLCESSGSWGIDNHVL-TLSSDPHPPVVPFGGHVVHRARLDLQLASTGFSLSVFKQFRelAAEADVVNYHFP 94
Cdd:cd03802 18 GGTELVVSALTEGLVRRGHEVTLFaPGDSHTSAPLVAVIPRALRLDPIPQESKLAELLEALEVQLR--ASDFDVIHNHSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 95 WPFMDLVHFLTgmnKPSVVTYHSDIIRQRVLLKLYRPlmsrflhsvdrivaaSPNYFSTSDVLRQYREKTRVITY---GL 171
Cdd:cd03802 96 DWLPPFAPLIG---TPFVTTLHGPSIPPSLAIYAAEP---------------PVNYVSISDAQRAATPPIDYLTVvhnGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 172 DKDGYPkPATQrlehwreklGPRFFLFVGvmRYY--KGLHILLDALQGTDYPVVIVGAGPLQAELYAQAAALGLRNVHFL 249
Cdd:cd03802 158 DPADYR-FQPD---------PEDYLAFLG--RIApeKGLEDAIRVARRAGLPLKIAGKVRDEDYFYYLQEPLPGPRIEFI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 250 GRVDDEDKVALLQLSYAMVFPShLRSEAFGISLLEGAMYGKPMISSEIGtGTSYINIHGETGLVVPPsqPAAFRQAMRwl 329
Cdd:cd03802 226 GEVGHDEKQELLGGARALLFPI-NWDEPFGLVMIEAMACGTPVIAYRRG-GLPEVIQHGETGFLVDS--VEEMAEAIA-- 299
|
330 340 350
....*....|....*....|....*....|....*....
gi 15600640 330 wehpqQAEEMGRNAEARY-RQLFTAEEMGRRWSELYREL 367
Cdd:cd03802 300 -----NIDRIDRAACRRYaEDRFSAARMADRYEALYRKV 333
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
114-351 |
3.40e-17 |
|
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: 81.95 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 114 TYHSDIIRQRVLLKLYRPLMSRFLH-----------SVDRIVAASPnyFSTSDVLRQYREKTRVItygldkdgYPKPATQ 182
Cdd:cd03804 121 LYHQYLAESGLGKGIKSLLASLFLHylrlwdvrtaqRVDLFIANSQ--FVARRIKKFYGRESTVI--------YPPVDTD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 183 RLEHWREKLGprFFLFVGVMRYYKGLHILLDALQGTDYPVVIVGAGPLQAELYAQAAalglRNVHFLGRVDDEDKVALLQ 262
Cdd:cd03804 191 AFAPAADKED--YYLTASRLVPYKRIDLAVEAFNELPKRLVVIGDGPDLDRLRAMAS----PNVEFLGYQPDEVLKELLS 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 263 LSYAMVFPShlrSEAFGISLLEGAMYGKPMISSEIGtGTSYINIHGETGLVVPPSQPAAFRQAM------RWLWEHPQQA 336
Cdd:cd03804 265 KARAFVFAA---EEDFGIVPVEAQACGTPVIAFGKG-GALETVRPGPTGILFGEQTVESLKAAVeefeqnFDRFKPQAIR 340
|
250
....*....|....*
gi 15600640 337 EEMGRNAEARYRQLF 351
Cdd:cd03804 341 ANAERFSRARFRQEI 355
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
1-367 |
3.98e-16 |
|
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: 78.91 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 1 MRVLHFyKTYLSEtvGGIEQVIFQLCESSGSWGIDNHVL-----TLSSDP---HPPVVPFggHVVHrarldlqlaSTGFS 72
Cdd:cd03825 1 MKVLHI-NTVDLS--GGAARAAYRLHQALLAYGIDSTMLvgrkkNLISKPefiEADIIHL--HWIH---------GGYLS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 73 LSVFkqFRELAAEADVVNYHFPWPFMDLVHFLTGMNK--------PSVVTY---HSDIIRQRVLLKLYRPLMSRFLhsvd 141
Cdd:cd03825 67 LKAL--FKLLRRKPVVWTLHDMWPFTGGCHYPMECEGwktgcgncPNLNSYppaKKDLSRQLFRRKREALAKKRLT---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 142 rIVAASP---NYFSTSDVLRQYreKTRVITYGLDKDgYPKPATQRLEhwREKLG---PRFFLFVGVMRY---YKGLHILL 212
Cdd:cd03825 141 -IVAPSRwlaDMVRRSPLLKGL--PVVVIPNGIDTE-IFAPVDKAKA--RKRLGipqDKKVILFGAESVtkpRKGFDELI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 213 DALQGTDYP----VVIVGAGPlqaelyAQAAALGLrNVHFLGRVDDEDKVALLqLSYA--MVFPShlRSEAFGISLLEGA 286
Cdd:cd03825 215 EALKLLATKddllLVVFGKND------PQIVILPF-DIISLGYIDDDEQLVDI-YSAAdlFVHPS--LADNLPNTLLEAM 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 287 MYGKPMISSEIGtGTSYINIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQLFTAEEMGRRWSELYRE 366
Cdd:cd03825 285 ACGTPVVAFDTG-GSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYKD 363
|
.
gi 15600640 367 L 367
Cdd:cd03825 364 L 364
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
223-367 |
1.98e-15 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340859 [Multi-domain] Cd Length: 370 Bit Score: 77.01 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 223 VIVGAGPLQAELYAQAAALGLRN-VHFLGRVDDEDKvaLLQLSYAMVFPSHlrSEAFGISLLEGAMYGKPMISSEIGtGT 301
Cdd:cd04962 230 LLVGDGPERVPAEELARELGVEDrVLFLGKQDDVEE--LLSIADLFLLPSE--KESFGLAALEAMACGVPVVSSNAG-GI 304
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600640 302 SYINIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQLFTAEEMGRRWSELYREL 367
Cdd:cd04962 305 PEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
16-172 |
1.06e-12 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 65.63 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 16 GGIEQVIFQLCESSGSWGIDNHVLTLSSDPHPPVVPFGGHVVHRARLDLqLASTGFSLSVFKQFRELAAE--ADVVNYHF 93
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPL-PPRLLRSLAFLRRLRRLLRRerPDVVHAHS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 94 PWPFM-DLVHFLTGMNKPSVVTYHSDII-------RQRVLLKLYRPLMSRFLHSVDRIVAASPnyfSTSDVLRQY----R 161
Cdd:pfam13439 80 PFPLGlAALAARLRLGIPLVVTYHGLFPdykrlgaRLSPLRRLLRRLERRLLRRADRVIAVSE---AVADELRRLygvpP 156
|
170
....*....|.
gi 15600640 162 EKTRVITYGLD 172
Cdd:pfam13439 157 EKIRVIPNGVD 167
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
160-355 |
1.55e-10 |
|
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: 62.00 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 160 YREKTRVITYGLDKDGY-PKPATQRLEHW--REKLGPRFFLFVG-VMRYYKGLHILLDAL-----QGTDYPVVIVG---- 226
Cdd:cd03818 177 YRDRISVIHDGVDTDRLaPDPAARLRLLNgtELKAGDPVITYVArNLEPYRGFHVFMRALpriqaRRPDARVVVVGgdgv 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 227 --------AGPLQAELYAQAAaLGLRNVHFLGRVDDEDKVALLQLSYAMVFPshLRSEAFGISLLEGAMYGKPMISSEIG 298
Cdd:cd03818 257 sygspppdGGSWKQKMLAELG-VDLERVHFVGKVPYDQYVRLLQLSDAHVYL--TYPFVLSWSLLEAMACGCPVIGSDTA 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600640 299 TGTSYINiHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQLFTAEE 355
Cdd:cd03818 334 PVREVIR-DGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDV 389
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
246-359 |
2.41e-10 |
|
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: 61.45 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 246 VHFLGRVDDEDKVALLQLSYAMVF-PSHlrsEAFGISLLEGAMYGKPMISSEIGTGTSYInIHGETGLVVPPSqPAAFRQ 324
Cdd:cd03805 282 VLFLRSISDSQKEQLLSSALALLYtPSN---EHFGIVPLEAMYAGKPVIACNSGGPLETV-VEGVTGFLCEPT-PEAFAE 356
|
90 100 110
....*....|....*....|....*....|....*
gi 15600640 325 AMRWLWEHPQQAEEMGRNAEARYRQLFTAEEMGRR 359
Cdd:cd03805 357 AMLKLANDPDLADRMGAAGRKRVKEKFSREAFAER 391
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
197-365 |
2.92e-10 |
|
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: 61.25 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 197 LFVGVMRYYKGLHILLDALQ-----GTDYPVVIVGA-GP----LQAELY--AQAAALGLRNVHFLGR--VDDEDKVALLQ 262
Cdd:cd03822 191 LTFGFIGPGKGLEILLEALPelkaeFPDVRLVIAGElHPslarYEGERYrkAAIEELGLQDHVDFHNnfLPEEEVPRYIS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 263 LSYAMVFPSHLRSEAFGISLLEGAMYGKPMISSEigTGTSYINIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRN 342
Cdd:cd03822 271 AADVVVLPYLNTEQSSSGTLSYAIACGKPVISTP--LRHAEELLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAER 348
|
170 180
....*....|....*....|...
gi 15600640 343 AEARYRQLfTAEEMGRRWSELYR 365
Cdd:cd03822 349 AYAYARAM-TWESIADRYLRLFN 370
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
110-364 |
2.66e-08 |
|
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: 55.14 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 110 PSVVTYHSDIIRQRVLLKLYRplMSRFLHSVDRIVA-ASPNYFSTSDVLRqyREKTRVITYGLDKDGYPKPATQRLEhWR 188
Cdd:cd04951 105 LLICTAHNKNEGGRIRMFIYR--LTDFLCDITTNVSrEALDEFIAKKAFS--KNKSVPVYNGIDLNKFKKDINVRLK-IR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 189 EKLGPRF----FLFVGVMRYYKGLHILLDALQGT-----DYPVVIVGAGPLQAELYAQAAALGLR-NVHFLGRVDD-EDk 257
Cdd:cd04951 180 NKLNLKNdefvILNVGRLTEAKDYPNLLLAISELilsknDFKLLIAGDGPLRNELERLICNLNLVdRVILLGQISNiSE- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 258 vaLLQLSYAMVFPShlRSEAFGISLLEGAMYGKPMISSEIGtGTSyiNIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAE 337
Cdd:cd04951 259 --YYNAADLFVLSS--EWEGFGLVVAEAMACERPVVATDAG-GVA--EVVGDHNYVVPVSDPQLLAEKIKEIFDMSDEER 331
|
250 260
....*....|....*....|....*..
gi 15600640 338 EMGRNAEARYRQLFTAEEMGRRWSELY 364
Cdd:cd04951 332 DILGNKNEYIAKNFSINTIVNEWERLY 358
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
216-306 |
1.25e-07 |
|
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: 53.06 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 216 QGTDYPVVIVGAGPLQAELYAQAAALGL-RNVHFLGRVddEDKVALLQLSYAMVFPSHLrsEAFGISLLEGAMYGKPMIS 294
Cdd:cd03812 219 KNPNVKLVLVGEGELKEKIKEKVKELGLeDKVIFLGFR--NDVSEILSAMDVFLFPSLY--EGLPLVAVEAQASGLPCLL 294
|
90
....*....|....*....
gi 15600640 295 SE-------IGTGTSYINI 306
Cdd:cd03812 295 SDtitkecdITNNVEFLPL 313
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
199-360 |
7.79e-07 |
|
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: 50.40 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 199 VGVMRYYKGLHILLDALQgtdypVVIVGAG----PLQAELYAQ--AAALGLRNVHFLgRVDDEDKV--ALLQLSYAMVFP 270
Cdd:cd03792 213 LGVIDAYKLFKRRAEEPQ-----LVICGHGavddPEGSVVYEEvmEYAGDDHDIHVL-RLPPSDQEinALQRAATVVLQL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 271 ShlRSEAFGISLLEGAMYGKPMISSEIGtGTSYINIHGETGLVVPPSQPAAFRqaMRWLWEHPQQAEEMGRNAEARYRQL 350
Cdd:cd03792 287 S--TREGFGLTVSEALWKGKPVIATPAG-GIPLQVIDGETGFLVNSVEGAAVR--ILRLLTDPELRRKMGLAAREHVRDN 361
|
170
....*....|
gi 15600640 351 FTAEEMGRRW 360
Cdd:cd03792 362 FLITGNLRAW 371
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
137-366 |
1.14e-06 |
|
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: 50.25 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 137 LHSVDRIVAASPNY----------FSTSDVLRQYREKTRVITYGLDKDGYpKPATQRL-----------EHW------RE 189
Cdd:cd03791 206 IVYADRVTTVSPTYakeiltpeygEGLDGVLRARAGKLSGILNGIDYDEW-NPATDKLipanysandleGKAenkaalQK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 190 KLG----PRFFL--FVGVMRYYKGLHILLDALQ---GTDYPVVIVGAG-PLQAELYAQAAALGLRNVHFLGRVDdedkVA 259
Cdd:cd03791 285 ELGlpvdPDAPLfgFVGRLTEQKGVDLILDALPellEEGGQLVVLGSGdPEYEQAFRELAERYPGKVAVVIGFD----EA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 260 LLQLSYA----MVFPShlRSEAFGISLLEgAM-YGKPMISSEIG----TGTSYINIHGE-TGLVVPPSQPAAFRQAMR-- 327
Cdd:cd03791 361 LAHRIYAgadfFLMPS--RFEPCGLVQMY-AMrYGTLPIVRRTGgladTVFDYDPETGEgTGFVFEDYDAEALLAALRra 437
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15600640 328 -WLWEHPQQAEEMGRNAearYRQLFTAEEMGRRWSELYRE 366
Cdd:cd03791 438 lALYRNPELWRKLQKNA---MKQDFSWDKSAKEYLELYRS 474
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
244-360 |
2.33e-06 |
|
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: 48.84 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 244 RNVHFLGRVDDEDKValLQLSYAMVFPSHlrSEAFGISLLEGAMYGKPMISSEIGTGTSYINIHGETGLVVPPSQPAAFR 323
Cdd:cd04949 217 DNVFLKGYHSNLDQE--YQDAYLSLLTSQ--MEGFGLTLMEAIGHGLPVVSYDVKYGPSELIEDGENGYLIEKNNIDALA 292
|
90 100 110
....*....|....*....|....*....|....*..
gi 15600640 324 QAMRWLWEHPQQAEEMGRNAEARYRQlFTAEEMGRRW 360
Cdd:cd04949 293 DKIIELLNDPEKLQQFSEESYKIAEK-YSTENVMEKW 328
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
232-364 |
7.41e-06 |
|
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: 47.62 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 232 AELYAQAAALGL-RNVHFLG--RVDD-EDKVALLQLSYAmvfpshlrSEAFGISLLEGAMYGKPMISSEIGTGTSYIN-- 305
Cdd:NF038011 354 AECRSLVASLGLqDKVKFLGfqKIDDlLPQVGLMVLSSI--------SEALPLVVLEAFAAGVPVVTTDVGSCRQLIEgl 425
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600640 306 -----IHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQLFTAEEMGRRWSELY 364
Cdd:NF038011 426 deedrALGAAGEVVAIADPQALARAALDLLRDPQRWQAAQAAGLARVERYYTEELMFDRYRELY 489
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
197-346 |
1.34e-05 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 46.89 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 197 LFVGVMRYYKGLHILLDALQG----TDYPVVIVGAGPLQAELYAQAAALGLRNVHFLGRVDDEDKVALLQLSYAMVFPSh 272
Cdd:PRK10307 233 LYSGNIGEKQGLELVIDAARRlrdrPDLIFVICGQGGGKARLEKMAQCRGLPNVHFLPLQPYDRLPALLKMADCHLLPQ- 311
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600640 273 lRSEAFGI---SLLEG--AMYGKPMISSEIGTGTSyiNIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEAR 346
Cdd:PRK10307 312 -KAGAADLvlpSKLTNmlASGRNVVATAEPGTELG--QLVEGIGVCVEPESVEALVAAIAALARQALLRPKLGTVAREY 387
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
206-346 |
2.84e-05 |
|
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: 45.52 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 206 KGLHILLDAL-----QGTDYPVVIVGAGPLQAELYAQAAALGLRN-VHFLGRVDDEDKVALLQLSYAMVFPSHLRS---- 275
Cdd:cd03799 187 KGLEYAIEAVaklaqKYPNIEYQIIGDGDLKEQLQQLIQELNIGDcVKLLGWKPQEEIIEILDEADIFIAPSVTAAdgdq 266
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600640 276 EAFGISLLEGAMYGKPMISSEIGtGTSYINIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEAR 346
Cdd:cd03799 267 DGPPNTLKEAMAMGLPVISTEHG-GIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRAR 336
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
107-345 |
4.34e-05 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 45.47 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 107 MNKPSVVTYHSDI---IRQRVLLKLYRPLMS--RFLHS-VDRIVAASPnyfSTSDVLRQYR----EKTRVITYGLDKDGY 176
Cdd:PLN02871 167 LCVPLVMSYHTHVpvyIPRYTFSWLVKPMWDiiRFLHRaADLTLVTSP---ALGKELEAAGvtaaNRIRVWNKGVDSESF 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 177 -PKpatQRLEHWREKLG---PRFFLFVGVMRY--YKGLHIL---LDALQGTDypVVIVGAGPLQAELYAQAAALglrNVH 247
Cdd:PLN02871 244 hPR---FRSEEMRARLSggePEKPLIVYVGRLgaEKNLDFLkrvMERLPGAR--LAFVGDGPYREELEKMFAGT---PTV 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 248 FLGRVDDEDkvalLQLSYA----MVFPSHlrSEAFGISLLEGAMYGKPMISSEIGTGTSYIN--IHGETGLVVPPSQPAA 321
Cdd:PLN02871 316 FTGMLQGDE----LSQAYAsgdvFVMPSE--SETLGFVVLEAMASGVPVVAARAGGIPDIIPpdQEGKTGFLYTPGDVDD 389
|
250 260
....*....|....*....|....
gi 15600640 322 FRQAMRWLWEHPQQAEEMGRNAEA 345
Cdd:PLN02871 390 CVEKLETLLADPELRERMGAAARE 413
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
16-170 |
1.71e-04 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 41.62 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 16 GGIEQVIFQLCESSGSWGIDNHVLTLSSDPHPPVVPFGGHVVHRARLDLQLASTGFSLSVFKQFRELAAE-ADVVnyHFP 94
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPVPPRPSPLADLAALRRLRRLLRAErPDVV--HAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 95 WPFMDLVHFLTGMNK--PSVVTYHSDIIRQ--RVLLKLYRPLMSRFLHSVDRIVAASPnyfSTSDVLRQY---REKTRVI 167
Cdd:pfam13579 79 SPTAGLAARLARRRRgvPLVVTVHGLALDYgsGWKRRLARALERRLLRRADAVVVVSE---AEAELLRALgvpAARVVVV 155
|
...
gi 15600640 168 TYG 170
Cdd:pfam13579 156 PNG 158
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
141-367 |
2.51e-04 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 42.77 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 141 DRIVAASPNY----------FSTSDVLRQYREKTRVITYGLDKDGYpKPATQRL-----------------EHWREKLG- 192
Cdd:COG0297 211 DRVTTVSPTYareiqtpefgEGLDGLLRARSGKLSGILNGIDYDVW-NPATDPYlpanysaddlegkaankAALQEELGl 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 193 ---PRFFLFVGVMR--YYKGLHILLDALQG---TDYPVVIVGAGP--LQAELYAQAAALGlRNVHFLGRVDDedkvALLQ 262
Cdd:COG0297 290 pvdPDAPLIGMVSRltEQKGLDLLLEALDElleEDVQLVVLGSGDpeYEEAFRELAARYP-GRVAVYIGYDE----ALAH 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 263 LSYA---MVF-PShlRSEAFGISLLEGAMYGKPMISSEIG----TGTSYINIHGE-TGLVVPPSQPAAFRQAMRW---LW 330
Cdd:COG0297 365 RIYAgadFFLmPS--RFEPCGLNQMYALRYGTVPIVRRTGgladTVIDYNEATGEgTGFVFDEYTAEALLAAIRRalaLY 442
|
250 260 270
....*....|....*....|....*....|....*..
gi 15600640 331 EHPQQAEEMGRNAearYRQLFTAEEMGRRWSELYREL 367
Cdd:COG0297 443 RDPEAWRKLQRNA---MKQDFSWEKSAKEYLELYREL 476
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
141-368 |
2.53e-04 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 42.80 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 141 DRIVAASPNY----------FSTSDVLRQYREKTRVITYGLDKDGYpKPATQRL-------EHW----------REKLG- 192
Cdd:PRK00654 199 DRVTTVSPTYareittpefgYGLEGLLRARSGKLSGILNGIDYDIW-NPETDPLlaanysaDDLegkaenkralQERFGl 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 193 --PRFFLFVGVMR--YYKGLHILLDALQGT---DYPVVIVGAG--PLQAELyAQAAAlglrnvHFLGRV------DDedk 257
Cdd:PRK00654 278 pdDDAPLFAMVSRltEQKGLDLVLEALPELleqGGQLVLLGTGdpELEEAF-RALAA------RYPGKVgvqigyDE--- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 258 vALLQLSYA----MVFPShlRSEAFGISLLEGAMYGKPMISSEIG----TGTSYINIHGE-TGLVVPPSQPAAFRQAMR- 327
Cdd:PRK00654 348 -ALAHRIYAgadmFLMPS--RFEPCGLTQLYALRYGTLPIVRRTGgladTVIDYNPEDGEaTGFVFDDFNAEDLLRALRr 424
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15600640 328 --WLWEHPQQAEEMGRNAearYRQLFTAEEMGRRWSELYRELL 368
Cdd:PRK00654 425 alELYRQPPLWRALQRQA---MAQDFSWDKSAEEYLELYRRLL 464
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
225-354 |
4.81e-04 |
|
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: 42.06 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 225 VGAGPLQAELYAQAAALgLRN--VHFLGRVDDEDKVALLQLSYAMVFPSHLRSEAFGISLLEGAMYGKPMISSEIGtGTS 302
Cdd:cd04946 263 IGGGPLKERLEKLAENK-LENvkVNFTGEVSNKEVKQLYKENDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVG-GTR 340
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15600640 303 YINIHGETGLVvpPSQPAAFRQ---AMRWLWEHPQQAEEMGRNAEARYRQLFTAE 354
Cdd:cd04946 341 EIVENETNGLL--LDKDPTPNEivsSIMKFYLDGGDYKTMKISARECWEERFNAE 393
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
223-356 |
9.02e-04 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 41.22 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 223 VIVGAGPLQAELYAQAAALG-LRNVHFLGrVDDEDKVALLQLSYAMVFPshlRSEAFGISLLEGAMYGKPMISSEIGtGT 301
Cdd:PRK15490 433 VLVGDGDLRAEAQKRAEQLGiLERILFVG-ASRDVGYWLQKMNVFILFS---RYEGLPNVLIEAQMVGVPVISTPAG-GS 507
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600640 302 SYINIHGETGLVVPPSQPAAFRQAMRW------LWehpQQAEEMGRNAEARYRQLFTAEEM 356
Cdd:PRK15490 508 AECFIEGVSGFILDDAQTVNLDQACRYaeklvnLW---RSRTGICQQTQSFLQERFTVEHM 565
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
189-310 |
4.84e-03 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 38.54 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600640 189 EKLGPRFFLFVGVMRYY--KGLHILLDALQGT--DYPVVIVGAGPLQAELYAQAAALGLR-NVHFLG--------RVDDE 255
Cdd:PRK09922 176 ERDKPAVFLYVGRLKFEgqKNVKELFDGLSQTtgEWQLHIIGDGSDFEKCKAYSRELGIEqRIIWHGwqsqpwevVQQKI 255
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600640 256 DKVALLQLSyamvfpSHLrsEAFGISLLEGAMYGKPMISSEIGTGTSYI---NIHGET 310
Cdd:PRK09922 256 KNVSALLLT------SKF--EGFPMTLLEAMSYGIPCISSDCMSGPRDIikpGLNGEL 305
|
|
| |
