|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
3-358 |
1.05e-111 |
|
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: 330.09 E-value: 1.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 3 IGIDGNEANvEKKVGVSNYTYHMLLYFNEvasEKKQFVVFLRDDPRNDLPKENR------YFKYKVIKAKFLWRDVFLPL 76
Cdd:cd03809 2 ILIDGRSLA-QRLTGIGRYTRELLKALAK---NDPDESVLAVPPLPGELLRLLReypelsLGVIKIKLWRELALLRWLQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 77 SLYRKKHIDLFFSPAHYTP-RFCPVPIVVTIHDVSYIHFPDEFLEKDLYKLTHWTAHAVTQARKIIAVSESTKKDIIAHY 155
Cdd:cd03809 78 LLPKKDKPDLLHSPHNTAPlLLKGCPQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPISLRRADAIITVSEATRDDIIKFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 156 HISKNNINVIYNGYEKY--TPSIKKDSSLYSLPQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGKKGWLYG 233
Cdd:cd03809 158 GVPPEKIVVIPLGVDPSffPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 234 DIFDKALELGLEDSVIFSGYVSNEQLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPEVGGKACLYFNP 313
Cdd:cd03809 238 ELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDAALYFDP 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1084038999 314 YDEEELEKAMIKVATNEKLHKELVEKGKQRVKEFSWEKCAKETLA 358
Cdd:cd03809 318 LDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
17-361 |
1.66e-66 |
|
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: 214.32 E-value: 1.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 17 GVSNYTYHMLLYFnevASEKKQFVVFLRDDPrnDLPKENRYFKYKVIKAKFLWRDVFLPLSLYRKK-------------H 83
Cdd:cd03801 15 GAERHVRELARAL---AARGHDVTVLTPADP--GEPPEELEDGVIVPLLPSLAALLRARRLLRELRpllrlrkfdvvhaH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 84 IDLFFSPAHYTPRFCPVPIVVTIHDvSYIHFPDEFLEKDLYKLTHWTAhAVTQARKIIAVSESTKKDIIAHYHISKNNIN 163
Cdd:cd03801 90 GLLAALLAALLALLLGAPLVVTLHG-AEPGRLLLLLAAERRLLARAEA-LLRRADAVIAVSEALRDELRALGGIPPEKIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 164 VIYNGYEKYTPSIKKDSSLYSLPQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGKKGWLYGDIfdKALELG 243
Cdd:cd03801 168 VIPNGVDLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLRAEL--EELELG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 244 LEDSVIFSGYVSNEQLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPEV--GGKACLYFNPYDEEELEK 321
Cdd:cd03801 246 LGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVveDGEGGLVVPPDDVEALAD 325
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1084038999 322 AMIKVATNEKLHKELVEKGKQRVKE-FSWEKCAKETLAVLE 361
Cdd:cd03801 326 ALLRLLADPELRARLGRAARERVAErFSWERVAERLLDLYR 366
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
25-347 |
1.61e-43 |
|
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: 154.05 E-value: 1.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 25 MLLYFNEVASEKKQFVVFLRDDPRNDLPKENRYFKYKVIKAKFLW-RDVFLPLSLYRKKH------IDLFFSPAHYTPRF 97
Cdd:cd03811 18 LLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKlIKLGLLKAILKLKRilkrakPDVVISFLGFATYI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 98 ------CPVPIVVTIH-DVSYIHFPDEFLEKDLYKLThwtahavtQARKIIAVSESTKKDIIAHYHISKNNINVIYNGYE 170
Cdd:cd03811 98 vaklaaARSKVIAWIHsSLSKLYYLKKKLLLKLKLYK--------KADKIVCVSKGIKEDLIRLGPSPPEKIEVIYNPID 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 171 kyTPSIKKDS---SLYSLPQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGkKGWLYGDIFDKALELGLEDS 247
Cdd:cd03811 170 --IDRIRALAkepILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILG-DGPLREELEKLAKELGLAER 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 248 VIFSGYVSNeqLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPEV--GGKACLYFNPYDEEELEKAMIK 325
Cdd:cd03811 247 VIFLGFQSN--PYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREIldDGENGLLVPDGDAAALAGILAA 324
|
330 340
....*....|....*....|..
gi 1084038999 326 VATNEKLHKELVEKGKQRVKEF 347
Cdd:cd03811 325 LLQKKLDAALRERLAKAQEAVF 346
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
189-343 |
1.60e-42 |
|
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: 145.49 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 189 PYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGKKGWLYGdIFDKALELGLEDSVIFSGYVSNEQLSRLYKNALC 268
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKR-LKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084038999 269 CVVPSLYEGFGLPVLESMGQNCPVIASNISSIPEV--GGKACLYFNPYDEEELEKAMIKVATNEKLHKELVEKGKQR 343
Cdd:pfam00534 82 FVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVvkDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
59-351 |
2.31e-38 |
|
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: 140.07 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 59 KYKVIKAKFLWRDVFLPLSLYRKK-HIDLFFSPAHYTPRFC-----PVPIVVTIHdVSYIHFPDEFLEKDLYKLthwtah 132
Cdd:cd03820 62 KYSHFKLLLKYFKKVRRLRKYLKNnKPDVVISFRTSLLTFLaliglKSKLIVWEH-NNYEAYNKGLRRLLLRRL------ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 133 AVTQARKIIAVsesTKKDIIAHYHISKNNINVIYNgyekytPSIKKDSSLYSLPQGPYFLYVGTIQPRKNIKRLIEAFGK 212
Cdd:cd03820 135 LYKRADKIVVL---TEADKLKKYKQPNSNVVVIPN------PLSFPSEEPSTNLKSKRILAVGRLTYQKGFDLLIEAWAL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 213 LLKKHPNYKLVIVGKkGWLYGDIFDKALELGLEDSVIFSGYVSNeqLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPV 292
Cdd:cd03820 206 IAKKHPDWKLRIYGD-GPEREELEKLIDKLGLEDRVKLLGPTKN--IAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPI 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084038999 293 IASNISSIPE---VGGKACLYFNPYDEEELEKAMIKVATNEKLHKELVEKGKQRVKEFSWEK 351
Cdd:cd03820 283 ISFDCPTGPSeiiEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAERFSIEK 344
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
80-363 |
1.19e-35 |
|
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: 133.66 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 80 RKKHIDLFFspAHY-TP---------RFCPVPIVVTIHDvSYIH-FPDEFLEKDLYKlthwtaHAVTQARKIIAVSESTK 148
Cdd:cd03798 92 RRGPPDLIH--AHFaYPagfaaallaRLYGVPYVVTEHG-SDINvFPPRSLLRKLLR------WALRRAARVIAVSKALA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 149 kDIIAHYHISKNNINVIYNGY--EKYTPSikkDSSLYSLPQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVG 226
Cdd:cd03798 163 -EELVALGVPRDRVDVIPNGVdpARFQPE---DRGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 227 kkgwlyGDIFDKALE-----LGLEDSVIFSGYVSNEQLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIP 301
Cdd:cd03798 239 ------DGPLREALRalaedLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIP 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084038999 302 EV--GGKACLYFNPYDEEELEKAMIKVAtNEKLHKELVEKGKQRV-KEFSWEKCAKETLAVLESA 363
Cdd:cd03798 313 EVvgDPETGLLVPPGDADALAAALRRAL-AEPYLRELGEAARARVaERFSWVKAADRIAAAYRDV 376
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
188-329 |
1.58e-33 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 121.08 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 188 GPYFLYVGTIQPR-KNIKRLIEAFGKLLKKHPNYKLVIVGKkgwlyGDIFD-KALELGLEDSVIFSGYVsnEQLSRLYKN 265
Cdd:pfam13692 1 RPVILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVGD-----GPEEElEELAAGLEDRVIFTGFV--EDLAELLAA 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084038999 266 ALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPE-VGGKACLYFNPYDEEELEKAMIKVATN 329
Cdd:pfam13692 74 ADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPElVDGENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
133-358 |
1.58e-32 |
|
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: 125.43 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 133 AVTQARKIIAVSESTKKDIIAHYHISKNNINVIYNGY--EKYTPSIKKDSSLYSL---PQGPYFLYVGTIQPRKNIKRLI 207
Cdd:cd03800 160 ILEAADRVIASTPQEADELISLYGADPSRINVVPPGVdlERFFPVDRAEARRARLllpPDKPVVLALGRLDPRKGIDTLV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 208 EAFGKLLKKHPNYKLVIVGkkgwlyGDIFDK-----------ALELGLEDSVIFSGYVSNEQLSRLYKNALCCVVPSLYE 276
Cdd:cd03800 240 RAFAQLPELRELANLVLVG------GPSDDPlsmdreelaelAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 277 GFGLPVLESMGQNCPVIASNISSIPE--VGGKACLYFNPYDEEELEKAMIKVATNEKLHKELVEKGKQRVKE-FSWEKCA 353
Cdd:cd03800 314 PFGLTAIEAMACGTPVVATAVGGLQDivRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAhYTWESVA 393
|
....*
gi 1084038999 354 KETLA 358
Cdd:cd03800 394 DQLLT 398
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
138-355 |
1.78e-32 |
|
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: 124.74 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 138 RKIIAVSESTKKDIIAhYHISKNNINVIYNGYE--KYTPSIKKDSSLYS---LPQGPYFL-YVGTIQPRKNIKRLIEAFG 211
Cdd:cd03807 135 PATVANSSAVAEFHQE-QGYAKNKIVVIYNGIDlfKLSPDDASRARARRrlgLAEDRRVIgIVGRLHPVKDHSDLLRAAA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 212 KLLKKHPNYKLVIVGkKGWLYGDIFDKALELGLEDSVIFSGYVSNeqLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCP 291
Cdd:cd03807 214 LLVETHPDLRLLLVG-RGPERPNLERLLLELGLEDRVHLLGERSD--VPALLPAMDIFVLSSRTEGFPNALLEAMACGLP 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084038999 292 VIASNISSIPE-VGGKACLYFNPYDEEELEKAMIKVATNEKLHKELVEKGKQRV-KEFSWEKCAKE 355
Cdd:cd03807 291 VVATDVGGAAElVDDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIaNEFSIDAMVRR 356
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
101-357 |
2.61e-32 |
|
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: 124.24 E-value: 2.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 101 PIVVTIHDVSYiHFPDEFLEKDLYKLTHWTAHAVTQarKIIAVSESTKKDIIAHYHISKNNINVIY---NGYEKYTPSik 177
Cdd:cd03808 107 KVIYTVHGLGF-VFTEGKLLRLLYLLLEKLALLFTD--KVIFVNEDDRDLAIKKGIIKKKKTVLIPgsgVDLDRFQYS-- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 178 kdssLYSLPQGPY-FLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGKkGWLYGDIFDKALELGLEDSVIFSGYVSN 256
Cdd:cd03808 182 ----PESLPSEKVvFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGD-GELENPSEILIEKLGLEGRIEFLGFRSD 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 257 eqLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPEV--GGKACLYFNPYDEEELEKAMIKVATNEKLHK 334
Cdd:cd03808 257 --VPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELviDGVNGFLVPPGDVEALADAIEKLIEDPELRK 334
|
250 260
....*....|....*....|....
gi 1084038999 335 ELVEKGKQRV-KEFSWEKCAKETL 357
Cdd:cd03808 335 EMGEAARKRVeEKFDEEKVVNKLL 358
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
56-351 |
7.09e-30 |
|
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: 117.77 E-value: 7.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 56 RYFKYKVIKAKFLWR-DV---FLPLSLY-------RKKHIdlffspahytprfcpvPIVVTIH-----DVSYIHFPDEFL 119
Cdd:cd03817 70 FPFKKAVIDRIKELGpDIihtHTPFSLGklglriaRKLKI----------------PIVHTYHtmyedYLHYIPKGKLLV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 120 EKDLYKLTHWTAHavtQARKIIAVSESTKkDIIAHYHISKNnINVIYNG-----YEKYtPSIKKDSSLYSLPQGPYFLYV 194
Cdd:cd03817 134 KAVVRKLVRRFYN---HTDAVIAPSEKIK-DTLREYGVKGP-IEVIPNGidldkFEKP-LNTEERRKLGLPPDEPILLYV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 195 GTIQPRKNIKRLIEAFgKLLKKHPNYKLVIVGKkGWLYGDIFDKALELGLEDSVIFSGYVSNEQLSRLYKNALCCVVPSL 274
Cdd:cd03817 208 GRLAKEKNIDFLLRAF-AELKKEPNIKLVIVGD-GPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFAST 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084038999 275 YEGFGLPVLESMGQNCPVIASNISSIPEV--GGKACLYFNPyDEEELEKAMIKVATNEKLHKELVEKGKQRVKEFSWEK 351
Cdd:cd03817 286 TETQGLVYLEAMAAGLPVVAAKDPAASELveDGENGFLFEP-NDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAK 363
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
96-347 |
8.64e-30 |
|
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: 117.07 E-value: 8.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 96 RFCPVPIVVTIHDVSYIHFpdefLEKDLYKLTHwtahavTQARKIIAVSESTKKDIIAHYHISKNNINVIYNG--YEKYT 173
Cdd:cd03819 96 RLTGVPLVTTVHGSYLATY----HPKDFALAVR------ARGDRVIAVSELVRDHLIEALGVDPERIRVIPNGvdTDRFP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 174 PSIKKDSSLYSLPQG--PYFLYVGTIQPRKNIKRLIEAFGKLlKKHPNYKLVIVGKkGWLYGDIFDKALELGLEDSVIFS 251
Cdd:cd03819 166 PEAEAEERAQLGLPEgkPVVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAGD-GPERDEIRRLVERLGLRDRVTFT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 252 GYvsNEQLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPE--VGGKACLYFNPYDEEELEKAMIKVATN 329
Cdd:cd03819 244 GF--REDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREivVHGRTGLLVPPGDAEALADAIRAAKLL 321
|
250 260
....*....|....*....|
gi 1084038999 330 EKLHKELVEKGKQ--RVKEF 347
Cdd:cd03819 322 PEAREKLQAAAALteAVREL 341
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
107-359 |
8.94e-29 |
|
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: 114.80 E-value: 8.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 107 HDVSYIHFPDEFleKDLYkLTHWTAHAVTQARKIIAVSESTKKDIIAHYHISKNninVIYNGY--EKYTP-SIKKDSSL- 182
Cdd:TIGR04047 112 GFVRTVHHLDDF--DDPR-LAACQERAIVEADAVLCVSAAWAAELRAEWGIDAT---VVPNGVdaARFSPaADAADAALr 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 183 --YSLPQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGKKGWL----YGDIFDKAL-ELGLE-DSVIFSGYV 254
Cdd:TIGR04047 186 rrLGLRGGPYVLAVGGIEPRKNTIDLLEAFALLRARRPQAQLVIAGGATLFdydaYRREFRARAaELGVDpGPVVITGPV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 255 SNEQLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPE-VGGKACLYFNPYDEEELEKAMIKvATNEKLH 333
Cdd:TIGR04047 266 PDADLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEyLGRFDAAWADPSDPDSIADALAL-ALDPARR 344
|
250 260
....*....|....*....|....*.
gi 1084038999 334 KELVEKGKQRVKEFSWEKCAKETLAV 359
Cdd:TIGR04047 345 PALRAAGPELAARYTWDASARAHLEF 370
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
262-364 |
9.27e-28 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 105.46 E-value: 9.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 262 LYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPEV--GGKACLYFNPYDEEELEKAMIKVATNEKLHKELVEK 339
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVieDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96
|
90 100
....*....|....*....|....*.
gi 1084038999 340 GKQRVKE-FSWEKCAKETLAVLESAI 364
Cdd:COG0438 97 ARERAEErFSWEAIAERLLALYEELL 122
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
100-357 |
1.63e-26 |
|
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: 108.61 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 100 VPIVVTIH-DVSYIHFPDEFLEKDLYKltHW-TAHAVTQARKIIAVSESTKKDIiaHYHISKNNINVIYNGY--EKYTPS 175
Cdd:cd03821 116 IPYVVSPHgMLDPWALQQKHWKKRIAL--HLiERRNLNNAALVHFTSEQEADEL--RRFGLEPPIAVIPNGVdiPEFDPG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 176 IKKDSSLYSLPQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGKKGWLYGDIFDKALELGLEDSVIFSGYVS 255
Cdd:cd03821 192 LRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDGAYPAFLQLQSSLGLGDRVTFTGPLY 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 256 NEQLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPEVGGKACLYFNPYDEEELEKA---MIKVATNEKL 332
Cdd:cd03821 272 GEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAGCGVVVDPNVSSLAEAlaeALRDPADRKR 351
|
250 260
....*....|....*....|....*
gi 1084038999 333 HKELVEKGKQRVKEFSWEKCAKETL 357
Cdd:cd03821 352 LGEMARRARQVEENFSWEAVAGQLG 376
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
108-311 |
1.41e-23 |
|
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: 97.47 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 108 DVSYIHFPDeflekdlyklTHWTAHAVTQARKIIAvsestkkdIIAHYHISknnINVIYNGYEKYTPSIKKDSSLYSlpq 187
Cdd:cd01635 56 DVVHAHSPH----------AAALAALLAARLLGIP--------IVVTVHGP---DSLESTRSELLALARLLVSLPLA--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 188 gpYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGKKGWLYGDIFDKALELGLEDSVIFSGYVSNEQLSRLYKNAL 267
Cdd:cd01635 112 --DKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAAD 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1084038999 268 CCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPE--VGGKACLYF 311
Cdd:cd01635 190 VFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEfvVDGENGLLV 235
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
100-336 |
3.08e-23 |
|
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: 98.94 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 100 VPIVVTIHDVsyihfpdeflekdlykltHWTAHAVTQARK----IIAVSESTKKDIIAHYHISKNnINVIYNGYEkytPS 175
Cdd:cd03823 121 IPVVHTLHDY------------------WLLCPRQFLFKKggdaVLAPSRFTANLHEANGLFSAR-ISVIPNAVE---PD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 176 IKKDSSLYSLPQGPYFLYVGTIQPRKNIKRLIEAFGKLlkKHPNYKLVIVGKkGWLygdifDKALELGLEDSVIFSGYVS 255
Cdd:cd03823 179 LAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRL--PREDIELVIAGH-GPL-----SDERQIEGGRRIAFLGRVP 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 256 NEQLSRLYKNALCCVVPSL-YEGFGLPVLESMGQNCPVIASNISSIPE--VGGKACLYFNPYDEEELEKAMIKVATNEKL 332
Cdd:cd03823 251 TDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAEliQPGVNGLLFAPGDAEDLAAAMRRLLTDPAL 330
|
....
gi 1084038999 333 HKEL 336
Cdd:cd03823 331 LERL 334
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
123-348 |
6.11e-23 |
|
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: 98.29 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 123 LYKLTHWTAHAVTQarkiiaVSESTKKDIIAHYHISKNNINVIYNG-----YEKYTPSIKKDSSLYSLPQGPY-FLYVGT 196
Cdd:cd04951 123 IYRLTDFLCDITTN------VSREALDEFIAKKAFSKNKSVPVYNGidlnkFKKDINVRLKIRNKLNLKNDEFvILNVGR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 197 IQPRKNIKRLIEAFGKLLKKHPNYKLVIVGKkGWLYGDIFDKALELGLEDSVIFSGYVSNeqLSRLYKNALCCVVPSLYE 276
Cdd:cd04951 197 LTEAKDYPNLLLAISELILSKNDFKLLIAGD-GPLRNELERLICNLNLVDRVILLGQISN--ISEYYNAADLFVLSSEWE 273
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084038999 277 GFGLPVLESMGQNCPVIASNISSIPEVGGKACLYFNPYDEEELEKAMIKVATNE-KLHKELVEKGKQRVKEFS 348
Cdd:cd04951 274 GFGLVVAEAMACERPVVATDAGGVAEVVGDHNYVVPVSDPQLLAEKIKEIFDMSdEERDILGNKNEYIAKNFS 346
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
96-354 |
2.25e-22 |
|
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: 97.03 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 96 RFCPVPIVVTIHDVsyihFPDEFLE------KDLYKLTHWTAHAVTQ-ARKIIAVSESTKKDIIAHYhISKNNINVIYNG 168
Cdd:cd03794 120 KLRGAPFILDVRDL----WPESLIAlgvlkkGSLLKLLKKLERKLYRlADAIIVLSPGLKEYLLRKG-VPKEKIIVIPNW 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 169 Y--EKYTPSIKKDSSLYSLPQGPY-FLYVGTIQPRKNIKRLIEAFgKLLKKHPNYKLVIVGKkGWLYGDIFDKALELGLE 245
Cdd:cd03794 195 AdlEEFKPPPKDELRKKLGLDDKFvVVYAGNIGKAQGLETLLEAA-ERLKRRPDIRFLFVGD-GDEKERLKELAKARGLD 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 246 DsVIFSGYVSNEQLSRLYKNALCCVVP---SLYEGFGLP--VLESMGQNCPVIASN--ISSIPEVGGKACLYFNPYDEEE 318
Cdd:cd03794 273 N-VTFLGRVPKEEVPELLSAADVGLVPlkdNPANRGSSPskLFEYMAAGKPILASDdgGSDLAVEINGCGLVVEPGDPEA 351
|
250 260 270
....*....|....*....|....*....|....*..
gi 1084038999 319 LEKAMIKVATNEKLHKELVEKGKQRVKE-FSWEKCAK 354
Cdd:cd03794 352 LADAILELLDDPELRRAMGENGRELAEEkFSREKLAD 388
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
101-359 |
6.53e-22 |
|
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: 95.50 E-value: 6.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 101 PIVVTIH--DVSYIHFpDEFLekdlyklTHWTAHAVTQARKIIAVSESTKKDIIAHYHISKNnINVIYNGYE------KY 172
Cdd:cd04962 112 PIVTTLHgtDITLVGY-DPSL-------QPAVRFSINKSDRVTAVSSSLRQETYELFDVDKD-IEVIHNFIDedvfkrKP 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 173 TPSIKKDssLYSLPQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNyKLVIVGKkGWLYGDIFDKALELGLEDSVIFSG 252
Cdd:cd04962 183 AGALKRR--LLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIPA-KLLLVGD-GPERVPAEELARELGVEDRVLFLG 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 253 yvSNEQLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPEV--GGKACLYFNPYDEEELEKAMIKVATNE 330
Cdd:cd04962 259 --KQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVvkHGETGFLSDVGDVDAMAKSALSILEDD 336
|
250 260 270
....*....|....*....|....*....|
gi 1084038999 331 KLHKELVEKG-KQRVKEFSWEKCAKETLAV 359
Cdd:cd04962 337 ELYNRMGRAArKRAAERFDPERIVPQYEAY 366
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
99-352 |
8.60e-19 |
|
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: 85.82 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 99 PVPIVVTIHD--VSYIHFPDEFLEKDLYKlthwtaHAVTQARKIIAVSEST---KKDIIAHYHISKNnINVIYNGYekyt 173
Cdd:cd04949 77 PAKKGAVLHNehVKNNDDPEHSLIKNFYK------YVFENLNKYDAIIVSTeqqKQDLSERFNKYPP-IFTIPVGY---- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 174 pSIKKDSSLYSLPQGPY-FLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGkkgwlYGDIFDKAL----ELGLEDSV 248
Cdd:cd04949 146 -VDQLDTAESNHERKSNkIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYG-----YGEEREKLKklieELHLEDNV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 249 IFSGYVSNeqLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPE---VGGKACLYFNPYDEEELEKAMIK 325
Cdd:cd04949 220 FLKGYHSN--LDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKYGPSeliEDGENGYLIEKNNIDALADKIIE 297
|
250 260
....*....|....*....|....*..
gi 1084038999 326 VATNEKLHKELVEKGKQRVKEFSWEKC 352
Cdd:cd04949 298 LLNDPEKLQQFSEESYKIAEKYSTENV 324
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
186-351 |
3.84e-18 |
|
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: 84.65 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 186 PQGPYFLYVGTIQPRKNIKRLIEAFGKLlKKHPNYKLVIVGkkgwlyGDIFDKALELGLEDsVIFSGYVSNEQLSRLYKN 265
Cdd:cd03814 196 PGRPLLLYVGRLAPEKNLEALLDADLPL-AASPPVRLVVVG------DGPARAELEARGPD-VIFTGFLTGEELARAYAS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 266 ALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPEV---GGKACLYfNPYDEEELEKAMIKVATNEKLHKELVEKGKQ 342
Cdd:cd03814 268 ADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIvrpGGTGALV-EPGDAAAFAAALRALLEDPELRRRMAARARA 346
|
....*....
gi 1084038999 343 RVKEFSWEK 351
Cdd:cd03814 347 EAERYSWEA 355
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
123-347 |
1.79e-16 |
|
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: 79.63 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 123 LYK-LTHWTAHAVTQarkIIAVS-----------ESTKKDIIAHYHISKNNINVIYNGYEKYTPSIKKdsslyslpqGPY 190
Cdd:cd03795 126 LYKpLMTRFLRRADR---IIATSpnyvetsptlrEFKNKVRVIPLGIDKNVYNIPRVDFENIKREKKG---------KKI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 191 FLYVGTIQPRKNIKRLIEAFGKLlkkhpNYKLVIVGKkGWLYGDIFDKAlELGLEDSVIFSGYVSNEQLSRLYKNALCCV 270
Cdd:cd03795 194 FLFIGRLVYYKGLDYLIEAAQYL-----NYPIVIGGE-GPLKPDLEAQI-ELNLLDNVKFLGRVDDEEKVIYLHLCDVFV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 271 VPSLY--EGFGLPVLESMGQNCPVIASNI-SSIPEVG--GKACLYFNPYDEEELEKAMIKVATNEKLHKELVEKGKQRVK 345
Cdd:cd03795 267 FPSVLrsEAFGIVLLEAMMCGKPVISTNIgTGVPYVNnnGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFE 346
|
..
gi 1084038999 346 EF 347
Cdd:cd03795 347 EL 348
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
96-347 |
7.40e-16 |
|
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: 78.53 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 96 RFCPVPIVVTIHDV----SYIHFPDEFLEKDLYKlTHWTAH-------AVTQARKIIAVSESTKKDIIaHYHISKNNINV 164
Cdd:cd03813 194 HRRGIPFLLTEHGIytreRKIEILQSTWIMGYIK-KLWIRFferlgklAYQQADKIISLYEGNRRRQI-RLGADPDKTRV 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 165 IYNGYE--KYTPSIKKDSSlyslPQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKlvivgkkGWLYGDIFDK---- 238
Cdd:cd03813 272 IPNGIDiqRFAPAREERPE----KEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAE-------GWLIGPEDEDpeya 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 239 ------ALELGLEDSVIFSGYVsneQLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPEV-------GG 305
Cdd:cd03813 341 qeckrlVASLGLENKVKFLGFQ---NIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELiygaddaLG 417
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1084038999 306 KACLYFNPYDEEELEKAMIKVATNEKLHKELVEKGKQRVKEF 347
Cdd:cd03813 418 QAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKY 459
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
100-354 |
1.20e-15 |
|
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: 77.11 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 100 VPIVVTIH--DVS-----YIHFPDEFLekdlYKLTHWTAhAVTQARKIIAVSESTKKDIIAHyHISKNNINVIYNGYE-- 170
Cdd:cd05844 105 VPLVVTFHgfDITtsrawLAASPGWPS----QFQRHRRA-LQRPAALFVAVSGFIRDRLLAR-GLPAERIHVHYIGIDpa 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 171 KYTPSIKKdsslyslPQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGkKGWLYGDIFDKALELGledSVIF 250
Cdd:cd05844 179 KFAPRDPA-------ERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAG-DGPLRPALQALAAALG---RVRF 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 251 SGYVSNEQLSRLYKNALCCVVPSLY------EGFGLPVLESMGQNCPVIASNISSIPE-VG-GKACLYFNPYDEEELEKA 322
Cdd:cd05844 248 LGALPHAEVQDWMRRAEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEaILdGETGFLVPEGDVDALADA 327
|
250 260 270
....*....|....*....|....*....|...
gi 1084038999 323 MIKVATNEKLHKELVEKGKQRVKE-FSWEKCAK 354
Cdd:cd05844 328 LQALLADRALADRMGGAARAFVCEqFDIRVQTA 360
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
164-297 |
1.92e-15 |
|
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: 76.56 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 164 VIYNGYE----KYTPSIKKDSSLYSLPQGPYFL-YVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGKkGWLYGDIFDK 238
Cdd:cd03812 162 VIPNGIDiekyKFNKEKRRKRRKLLILEDKLVLgHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGE-GELKEKIKEK 240
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1084038999 239 ALELGLEDSVIFSGYVSNeqLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNI 297
Cdd:cd03812 241 VKELGLEDKVIFLGFRND--VSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDT 297
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
90-303 |
2.38e-15 |
|
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: 76.17 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 90 PAHYTPRFCPVPIVVTIHDVSyihFPDEFLEKDLYKLTHWtahavtqarkiIAVSESTkkdiiAHYHISKNNINVIYNGY 169
Cdd:cd03802 97 WLPPFAPLIGTPFVTTLHGPS---IPPSLAIYAAEPPVNY-----------VSISDAQ-----RAATPPIDYLTVVHNGL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 170 ekytpsikkDSSLY--SLPQGPYFLYVGTIQPRKNIKRLIEAFGKLlkkhpNYKLVIVGKKGWLygDIFDKALELGLEDS 247
Cdd:cd03802 158 ---------DPADYrfQPDPEDYLAFLGRIAPEKGLEDAIRVARRA-----GLPLKIAGKVRDE--DYFYYLQEPLPGPR 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084038999 248 VIFSGYVSNEQLSRLYKNALCCVVPSLY-EGFGLPVLESMGQNCPVIASNISSIPEV 303
Cdd:cd03802 222 IEFIGEVGHDEKQELLGGARALLFPINWdEPFGLVMIEAMACGTPVIAYRRGGLPEV 278
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
111-348 |
5.34e-15 |
|
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.
Pssm-ID: 340834 [Multi-domain] Cd Length: 392 Bit Score: 75.32 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 111 YIHFPD------EFLEKDLYK--LTHWTAHAVTQARKIIAVSESTKKDIIAHY-HISKNNINVIY-----NGYEKyTPSI 176
Cdd:cd03805 121 YCHFPDqllaqrKSLLKRLYRkpFDWLEEFTTGMADQIVVNSNFTAGVFKKTFpSLAKNPPEVLYpcvdtDSFDS-TSED 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 177 KKDSSLYSLPQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHP---NYKLVIVGkkGwlygdiFDKALE------------ 241
Cdd:cd03805 200 PDPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQKLPefeNVRLVIAG--G------YDPRVAenveyleelqrl 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 242 ----LGLEDSVIFSGYVSNEQLSRLYKNALCCV-VPSlYEGFGLPVLESMGQNCPVIASNI-----SSIPEVGGKAClyf 311
Cdd:cd03805 272 aeelLNVEDQVLFLRSISDSQKEQLLSSALALLyTPS-NEHFGIVPLEAMYAGKPVIACNSggpleTVVEGVTGFLC--- 347
|
250 260 270
....*....|....*....|....*....|....*...
gi 1084038999 312 nPYDEEELEKAMIKVATNEKLHKELVEKGKQRVKE-FS 348
Cdd:cd03805 348 -EPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEkFS 384
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
95-362 |
6.31e-14 |
|
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: 71.98 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 95 PRFCP-VPIVVTIHD----VSYIHFPDEF------------------LEKDL------YKLTHWTAHAVTqarkIIAVSE 145
Cdd:cd03825 71 FKLLRrKPVVWTLHDmwpfTGGCHYPMECegwktgcgncpnlnsyppAKKDLsrqlfrRKREALAKKRLT----IVAPSR 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 146 STKKDIIAHYHISKNNINVIYNGY--EKYTPSIKKDS-SLYSLPQGPY---FLYVGTIQPRKNIKRLIEAFgKLLKKHPN 219
Cdd:cd03825 147 WLADMVRRSPLLKGLPVVVIPNGIdtEIFAPVDKAKArKRLGIPQDKKvilFGAESVTKPRKGFDELIEAL-KLLATKDD 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 220 YKLVIVGK----KGWLYGDIfdkaLELGLEDSVifsgyvsnEQLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIAS 295
Cdd:cd03825 226 LLLVVFGKndpqIVILPFDI----ISLGYIDDD--------EQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAF 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084038999 296 NISSIPEV-----GGKAClyfNPYDEEELEKAMIKVATNEKLHKELVEKGKQRV-KEFSWEKCAKETLAVLES 362
Cdd:cd03825 294 DTGGSPEIvqhgvTGYLV---PPGDVQALAEAIEWLLANPKERESLGERARALAeNHFDQRVQAQRYLELYKD 363
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
139-362 |
3.42e-13 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 69.82 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 139 KIIAVSESTKKdiiaHY--HISKNNINVIYNGYEKYT----PSIKKDSSLYSLPQGPYFLYVGTIQPRKNIKRLIEAFGK 212
Cdd:PRK15484 142 KIIVPSQFLKK----FYeeRLPNADISIVPNGFCLETyqsnPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 213 LLKKHPNYKLVIVG--------KKGWLYGDIFDKALELGleDSVIFSGYVSNEQLSRLYKNALCCVVPSLY-EGFGLPVL 283
Cdd:PRK15484 218 LATAHSNLKLVVVGdptasskgEKAAYQKKVLEAAKRIG--DRCIMLGGQPPEKMHNYYPLADLVVVPSQVeEAFCMVAV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 284 ESMGQNCPVIASNISSIPE-VGGKACLYF--NPYDEEELEKAMIKVATNEKLHkELVEKGKQRVKE-FSWEKCAKETLAV 359
Cdd:PRK15484 296 EAMAAGKPVLASTKGGITEfVLEGITGYHlaEPMTSDSIISDINRTLADPELT-QIAEQAKDFVFSkYSWEGVTQRFEEQ 374
|
...
gi 1084038999 360 LES 362
Cdd:PRK15484 375 IHN 377
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
100-350 |
6.44e-13 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 69.35 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 100 VPIVVTIHdvsyIHFPD-------EFLEK---DLYKLTHWTAHaVTqarkiIAVSESTKKDIIAHYHISKNNINVIYNGY 169
Cdd:PLN02871 169 VPLVMSYH----THVPVyiprytfSWLVKpmwDIIRFLHRAAD-LT-----LVTSPALGKELEAAGVTAANRIRVWNKGV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 170 --EKYTPSIKKDSSLYSL----PQGPYFLYVGTIQPRKNIKRLIEafgkLLKKHPNYKLVIVGKKGwlygdiFDKALELG 243
Cdd:PLN02871 239 dsESFHPRFRSEEMRARLsggePEKPLIVYVGRLGAEKNLDFLKR----VMERLPGARLAFVGDGP------YREELEKM 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 244 LEDS-VIFSGYVSNEQLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPEV-----GGKACLYFNPYDEE 317
Cdd:PLN02871 309 FAGTpTVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIippdqEGKTGFLYTPGDVD 388
|
250 260 270
....*....|....*....|....*....|...
gi 1084038999 318 ELEKAMIKVATNEKLHKELVEKGKQRVKEFSWE 350
Cdd:PLN02871 389 DCVEKLETLLADPELRERMGAAAREEVEKWDWR 421
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
17-168 |
1.59e-12 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 64.86 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 17 GVSNYTYHMLLYFnevASEKKQFVVFLRDDPRNDLPKENRYFKYKVI---KAKFLWRDVFLPLSLYR---KKHIDL---- 86
Cdd:pfam13439 2 GVERYVLELARAL---ARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVplpLPPRLLRSLAFLRRLRRllrRERPDVvhah 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 87 ----FFSPAHYTPRFCPVPIVVTIHDVSYIHFPDEFLEKDLYKLTH-WTAHAVTQARKIIAVSESTKKDIIAHYHISKNN 161
Cdd:pfam13439 79 spfpLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRrLERRLLRRADRVIAVSEAVADELRRLYGVPPEK 158
|
....*..
gi 1084038999 162 INVIYNG 168
Cdd:pfam13439 159 IRVIPNG 165
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
14-361 |
3.50e-12 |
|
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: 67.02 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 14 KKVGVSNYTYHMLLYFNEvASEKKQFVVFLRDDPRNDLPKENRYFKYKVIKAKFLWRdvfLPLSLYRKK----HIDL--- 86
Cdd:cd03822 11 RKCGIATYTDDLVEGLRK-GGPVVIVVIVSPQDEILKDDDFEVPNEIKSWNSNEYFR---LLDHLNFKKpdvvHIQHefg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 87 FFSPAHYTP-----RFCPVPIVVTIHDVSYihfPDEFLEKDLYKLthwtAHAVTQARKIIAVSESTKKDIIAHYHISKNN 161
Cdd:cd03822 87 IFGGKYGLYalgllLHLRIPVITTLHTVLD---LSDPGKQALKVL----FRIATLSERVVVMAPISRFLLVRIKLIPAVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 162 INVIYNG-YEKYTPSIKKDSSLYsLPQGPY-FLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGK--KGWLYGDIFD 237
Cdd:cd03822 160 IEVIPHGvPEVPQDPTTALKRLL-LPEGKKvILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGElhPSLARYEGER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 238 K----ALELGLEDSVIF-SGYVSNEQLSRLYKNALCCVVPSLYEGFGLP--VLESMGQNCPVIASNISSIPE-VGGKACL 309
Cdd:cd03822 239 YrkaaIEELGLQDHVDFhNNFLPEEEVPRYISAADVVVLPYLNTEQSSSgtLSYAIACGKPVISTPLRHAEElLADGRGV 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1084038999 310 YFNPYDEEELEKAMIKVATNEKLHKELVEKGKQRVKEFSWEKCAKETLAVLE 361
Cdd:cd03822 319 LVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADRYLRLFN 370
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
109-302 |
4.78e-12 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 66.27 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 109 VSYIHFpdeflekDLYKLTHWTAHAVTQARKIIAVSESTKKDIIAhYHISKNNINVIYNGYEKYT---PSIKKDSSLYsl 185
Cdd:PRK09922 113 FSWPHF-------SLDHKKHAECKKITCADYHLAISSGIKEQMMA-RGISAQRISVIYNPVEIKTiiiPPPERDKPAV-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 186 pqgpyFLYVGTIQ--PRKNIKRLIEAFGKLlkkHPNYKLVIVGKkgwlyGDIFDK----ALELGLEDSVIFSGYVSN--E 257
Cdd:PRK09922 183 -----FLYVGRLKfeGQKNVKELFDGLSQT---TGEWQLHIIGD-----GSDFEKckaySRELGIEQRIIWHGWQSQpwE 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1084038999 258 QLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPE 302
Cdd:PRK09922 250 VVQQKIKNVSALLLTSKFEGFPMTLLEAMSYGIPCISSDCMSGPR 294
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
180-348 |
3.47e-10 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 61.29 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 180 SSLYSLP-----QGPYFLYVGTIQPRKNIKRLIEAFGKLLKK----HPNYKLVIVG---KKGWL--YGDIFDKALELGLE 245
Cdd:PLN02949 255 SGLQALPlerseDPPYIISVAQFRPEKAHALQLEAFALALEKldadVPRPKLQFVGscrNKEDEerLQKLKDRAKELGLD 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 246 DSVIFSGYVSNEQLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISS------IPEVGGKAClyFNPYDEEEL 319
Cdd:PLN02949 335 GDVEFHKNVSYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGpkmdivLDEDGQQTG--FLATTVEEY 412
|
170 180 190
....*....|....*....|....*....|..
gi 1084038999 320 EKAMIKVAT---NEKLhkELVEKGKQRVKEFS 348
Cdd:PLN02949 413 ADAILEVLRmreTERL--EIAAAARKRANRFS 442
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
186-358 |
1.15e-09 |
|
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: 59.30 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 186 PQGPYFLYVG-TIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGKKGWLYG-------DIFDKAL-ELGLEDS-VIFSGYVS 255
Cdd:cd03818 211 AGDPVITYVArNLEPYRGFHVFMRALPRIQARRPDARVVVVGGDGVSYGspppdggSWKQKMLaELGVDLErVHFVGKVP 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 256 NEQLSRLYKNALCCVVPsLYEgFGLP--VLESMGQNCPVIASNISSIPEV--GGKACLYFNPYDEEELEKAMIKVATNEK 331
Cdd:cd03818 291 YDQYVRLLQLSDAHVYL-TYP-FVLSwsLLEAMACGCPVIGSDTAPVREVirDGRNGLLVDFFDPDALAAAVLELLEDPD 368
|
170 180
....*....|....*....|....*...
gi 1084038999 332 LHKELVEKGKQRV-KEFSWEKCAKETLA 358
Cdd:cd03818 369 RAAALRRAARRTVeRSDSLDVCLARYLA 396
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
108-364 |
4.16e-09 |
|
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: 57.63 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 108 DVSYIHfpdeflekdLYKLTHWTAHAVTQArkiIAVSESTKKDIIAHYHISKNNINVIYNGYE--KYTPSIKKDSslysl 185
Cdd:cd03796 128 DASSIL---------TNKLLRFSLADIDHV---ICVSHTSKENTVLRASLDPRIVSVIPNAVDssDFTPDPSKPD----- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 186 PQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVG---KKgwlygDIFDKALE-LGLEDSVIFSGYVSNEQLSR 261
Cdd:cd03796 191 PNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGdgpKR-----IELEEMREkYQLQDRVELLGAVPHEEVRD 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 262 L------YKNalccvvPSLYEGFGLPVLESMGQNCPVIASNISSIPEVGGKACLYFNPYDEEELEKAMIKVATNEKLHKE 335
Cdd:cd03796 266 VlvqghiFLN------TSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPDPEDIVRKLEEAISILRTGKH 339
|
250 260 270
....*....|....*....|....*....|
gi 1084038999 336 LVEKGKQRVKEF-SWEKCAKETLAVLESAI 364
Cdd:cd03796 340 DPWSFHNRVKKMySWEDVARRTEKVYDRIL 369
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
85-323 |
1.06e-08 |
|
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.
Pssm-ID: 340833 [Multi-domain] Cd Length: 356 Bit Score: 56.14 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 85 DLFFSPAHytprfCPVPIVVT----IHdVSYIHFP-------------DEFLEKD---------LYKLTHWTAHAVTQAR 138
Cdd:cd03804 86 DLVISSSH-----AVAKGVLTrpdqLH-VCYVHSPiryawdlyhqylaESGLGKGiksllaslfLHYLRLWDVRTAQRVD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 139 KIIAVSESTKKDIIAHYHISKNninVIYngyekytPSIKKDSSLYSLPQGPYFLYVGTIQPRKNIKRLIEAFGKLlkkhp 218
Cdd:cd03804 160 LFIANSQFVARRIKKFYGREST---VIY-------PPVDTDAFAPAADKEDYYLTASRLVPYKRIDLAVEAFNEL----- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 219 NYKLVIVGkKGWLYGDIFDKAlelglEDSVIFSGYVSNEQLSRLYKNALCCVVPSlYEGFGLPVLESMGQNCPVIASNIS 298
Cdd:cd03804 225 PKRLVVIG-DGPDLDRLRAMA-----SPNVEFLGYQPDEVLKELLSKARAFVFAA-EEDFGIVPVEAQACGTPVIAFGKG 297
|
250 260
....*....|....*....|....*..
gi 1084038999 299 SIPEV--GGKACLYFNPYDEEELEKAM 323
Cdd:cd03804 298 GALETvrPGPTGILFGEQTVESLKAAV 324
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
186-346 |
1.31e-08 |
|
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: 55.79 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 186 PQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGK------KGWLygdIFDKALELGLEDSVIfsgYV----- 254
Cdd:cd03792 195 PERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHgavddpEGSV---VYEEVMEYAGDDHDI---HVlrlpp 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 255 SNEQLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPE--VGGKACLYFNPydEEELEKAMIKVATNEKL 332
Cdd:cd03792 269 SDQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLqvIDGETGFLVNS--VEGAAVRILRLLTDPEL 346
|
170
....*....|....
gi 1084038999 333 HKELVEKGKQRVKE 346
Cdd:cd03792 347 RRKMGLAAREHVRD 360
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
192-346 |
1.84e-08 |
|
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: 55.53 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 192 LYVGTIQPRKNIKRLIEAFGKLLKKHPNYKLVIVGkKGWLYGDIFDKALELGLEDSVIFSGYVSNEQLSRLYKNALCCVV 271
Cdd:cd03799 178 LTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIG-DGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 272 PSL------YEGFGLPVLESMGQNCPVIASNISSIPEV--GGKACLYFNPYDEEELEKAMIKVATNEKLHKELVEKGKQR 343
Cdd:cd03799 257 PSVtaadgdQDGPPNTLKEAMAMGLPVISTEHGGIPELveDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRAR 336
|
...
gi 1084038999 344 VKE 346
Cdd:cd03799 337 VEE 339
|
|
| COG4641 |
COG4641 |
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]; |
66-364 |
1.45e-07 |
|
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443679 [Multi-domain] Cd Length: 303 Bit Score: 52.24 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 66 KFLWRDVFLPLSLYRKKHIDLFfSPAhytprfcpvpIVVTIHDVSYIhfpdEFLEKDLYKLTHWTAHA-VTQARKIIAVS 144
Cdd:COG4641 27 TFLEPDDPWHDPLYAAELLDAF-RPD----------LVLVISGVELV----AALRARGIPTVFWDTDDpVTLDRFRELLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 145 E-----STKKDIIAHYH-ISKNNINVIYNGY--EKYTPSIKKDSSLYSLpqgpyfLYVGTIQPrkniKRlIEAFGKLLKK 216
Cdd:COG4641 92 LydlvfTFDGDCVEEYRaLGARRVFYLPFAAdpELHRPVPPEARFRYDV------AFVGNYYP----DR-RARLEELLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 217 HPNYKLVIVGKkGWLygdifdkalELGLEDSVIFSGYVSNEQLSRLYKNALCCV-VPSLYEGFGLP---VLESMGQNCPV 292
Cdd:COG4641 161 PAGLRLKIYGP-GWP---------KLALPANVRRGGHLPGEEHPAAYASSKITLnVNRMAASPDSPtrrTFEAAACGAFL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084038999 293 IASNISSIPE--VGGKACLYFNpyDEEELEKAMIKVATNEKLHKELVEKGKQRV-KEFSWEKCAKETLAVLESAI 364
Cdd:COG4641 231 LSDPWEGLEElfEPGEEVLVFR--DGEELAEKLRYLLADPEERRAIAEAGRRRVlAEHTYAHRARELLAILEELG 303
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
86-362 |
1.45e-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: 49.87 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 86 LFFSPAHYTPRFCPVPIVVTIHDVSYI-HFPDEFLEKDLYKLTHWTAHAVTQ-------------ARKIIAVSESTKKDI 151
Cdd:cd03791 144 AYLKTRYRGPGFKKIKTVFTIHNLAYQgLFPLDTLAELGLPPELFHIDGLEFygqinflkagivyADRVTTVSPTYAKEI 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 152 IA------HYHISKNNINVIY---NG--YEKYTPSIKKDS-SLYS-------------------LPQ---GPYFLYVGTI 197
Cdd:cd03791 224 LTpeygegLDGVLRARAGKLSgilNGidYDEWNPATDKLIpANYSandlegkaenkaalqkelgLPVdpdAPLFGFVGRL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 198 QPRKNIKRLIEAFGKLLKKhpNYKLVIVGKKGWLYGDIFDKALELGLEDSVIFSGYvsNEQLS-RLYKNALCCVVPSLYE 276
Cdd:cd03791 304 TEQKGVDLILDALPELLEE--GGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGF--DEALAhRIYAGADFFLMPSRFE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 277 GFGLPVLESMGQNCPVIASN-------ISSIPEVGGKACLY-FNPYDEEELEKAM---IKVATNEKLHKELVEKGKQRvk 345
Cdd:cd03791 380 PCGLVQMYAMRYGTLPIVRRtggladtVFDYDPETGEGTGFvFEDYDAEALLAALrraLALYRNPELWRKLQKNAMKQ-- 457
|
330
....*....|....*..
gi 1084038999 346 EFSWEKCAKETLAVLES 362
Cdd:cd03791 458 DFSWDKSAKEYLELYRS 474
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
276-358 |
4.76e-06 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 44.52 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 276 EGFGLPVLESMGQNCPVIASNISSIPE--VGGKACLYFNpyDEEELEKAMIKVATNEKLHKELVEKGKQRV-KEFSWEKC 352
Cdd:pfam13524 10 DSPNMRVFEAAACGAPLLTDRTPGLEElfEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERVlAEHTYAHR 87
|
....*.
gi 1084038999 353 AKETLA 358
Cdd:pfam13524 88 AEQLLD 93
|
|
| PHA01633 |
PHA01633 |
putative glycosyl transferase group 1 |
161-302 |
2.86e-05 |
|
putative glycosyl transferase group 1
Pssm-ID: 107050 [Multi-domain] Cd Length: 335 Bit Score: 45.36 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 161 NINVIYNGyEKYTPSIKKDSSlYSLPQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHPNyklviVGKKGWLYGDIFDKAL 240
Cdd:PHA01633 123 NFKIVENA-EKLVPQLKQKLD-KDFPDTIKFGIVSGLTKRKNMDLMLQVFNELNTKYPD-----IAKKIHFFVISHKQFT 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084038999 241 ELGLEDSVIFS---GYVSNEQLSRLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASNISSIPE 302
Cdd:PHA01633 196 QLEVPANVHFVaefGHNSREYIFAFYGAMDFTIVPSGTEGFGMPVLESMAMGTPVIHQLMPPLDE 260
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
192-296 |
3.84e-05 |
|
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.
Pssm-ID: 340835 [Multi-domain] Cd Length: 419 Bit Score: 45.29 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 192 LYVGTIQPRKNIKRLIEAFGKLLKKHP-----NYKLVIVGK------KGWLYgDIFDKALELGLEDSVIFSGYVSNEQLS 260
Cdd:cd03806 241 LSIAQFRPEKNHPLQLRAFAELLKRLPesirsNPKLVLIGScrneedKERVE-ALKLLAKELILEDSVEFVVDAPYEELK 319
|
90 100 110
....*....|....*....|....*....|....*.
gi 1084038999 261 RLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIASN 296
Cdd:cd03806 320 ELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHA 355
|
|
| GT4-like |
cd04955 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
182-355 |
1.04e-04 |
|
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 in certain bacteria and Archaea.
Pssm-ID: 340858 [Multi-domain] Cd Length: 379 Bit Score: 44.03 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 182 LYSLPQGPYFLYVGTIQPRKNIKRLIEAFgklLKKHPNYKLVIVGK-KGWLYGDIFDKALELGLEDSVIFSGYVSNEQLS 260
Cdd:cd04955 202 EKGVKPGKYYLIVGRFVPENNYETMIREF---MKSSTKRDLVIITNvEGNAYYELLLKKTAFDHDERIKFVGTVYDQELL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 261 R---------LYKNALCCVVPSLyegfglpvLESMGQNCPVIASNISSIPEVGGKACLYFNpydEEELEKAMIKV-ATNE 330
Cdd:cd04955 279 KyirenafayLHGHEVGGTNPSL--------LEALGSTDLNLLLDVGFNREVAEDAALYWK---KEPLASLIDEVdNLNP 347
|
170 180
....*....|....*....|....*.
gi 1084038999 331 KLHKELVEKGKQRVKE-FSWEKCAKE 355
Cdd:cd04955 348 DEISDLGKKAKQRIEEaYTWEKIVDE 373
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
115-295 |
8.01e-04 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 41.56 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 115 PDEFLEK--DLYKlthwtahAVTQARKIIAVSESTKKdiiAHYH-----ISKNNINVIYNGYEKY----TPSIKKDSSLY 183
Cdd:PRK15179 440 PDRYRVEydIIYS-------ELLKMRGVALSSNSQFA---AHRYadwlgVDERRIPVVYNGLAPLksvqDDACTAMMAQF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 184 SLPQGPYFLYVGTI---QPRKNIKRLIEAFGKLLKKHPNYKLVIVGkKGWLYGDIFDKALELGLEDSVIFSGyVSNeQLS 260
Cdd:PRK15179 510 DARTSDARFTVGTVmrvDDNKRPFLWVEAAQRFAASHPKVRFIMVG-GGPLLESVREFAQRLGMGERILFTG-LSR-RVG 586
|
170 180 190
....*....|....*....|....*....|....*
gi 1084038999 261 RLYKNALCCVVPSLYEGFGLPVLESMGQNCPVIAS 295
Cdd:PRK15179 587 YWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTT 621
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
139-303 |
1.76e-03 |
|
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: 40.14 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 139 KIIAVSESTKKDIIAHYHISKNNINVIYNGYekytpSIKKDSSLYSLPQGPYFLYVGTIQPRKNIKRLIEAFGKLLKKHP 218
Cdd:cd04946 180 AVFLISKEGKDYLQKCYPAYKEKIFVSRLGV-----SDKEQYSKVKKEGDLRLVSCSSIVPVKRIDLIIETLNSLCVAHP 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 219 --NYKLVIVGKkGWLYGDIFDKALELGLEDSVIFSGYVSNEQLSRLYKNALCCVVPSLYEGFGLPV--LESMGQNCPVIA 294
Cdd:cd04946 255 siCISWTHIGG-GPLKERLEKLAENKLENVKVNFTGEVSNKEVKQLYKENDVDVFVNVSESEGIPVsiMEAISFGIPVIA 333
|
....*....
gi 1084038999 295 SNISSIPEV 303
Cdd:cd04946 334 TNVGGTREI 342
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
270-357 |
2.99e-03 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 39.58 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038999 270 VVPSLYEGFGLPVLESMgqNC--PVIASNISSIPE--VGGKACLYFNPYDEEELEKAMI----KVATNEKLHKELVEKGK 341
Cdd:PLN00142 671 VQPALYEAFGLTVVEAM--TCglPTFATCQGGPAEiiVDGVSGFHIDPYHGDEAANKIAdffeKCKEDPSYWNKISDAGL 748
|
90
....*....|....*..
gi 1084038999 342 QRVKE-FSWEKCAKETL 357
Cdd:PLN00142 749 QRIYEcYTWKIYAERLL 765
|
|
| |
