|
Name |
Accession |
Description |
Interval |
E-value |
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
51-409 |
1.60e-111 |
|
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: 332.34 E-value: 1.60e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 51 KIAIVTETWPPEINGVALSLLQLCQGLQKQGHKILLVRPEQKAKcHDFLPEQECLVMSQAIPKYPTLQFGWPQYLKVSKA 130
Cdd:cd03814 1 RIALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVAPGPFDE-AESAEGRVVSVPSFPLPFYPEYRLALPLPRRVRRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 131 FEKFVPDVVHIVTEGPLGLTAMQAAKAKDIPVSSGFHSPFQDFSRFFDLAFLVKPIQKYLCWFHNNTQVTCVPSRDTEEA 210
Cdd:cd03814 80 IKEFQPDIIHIATPGPLGLAALRAARRLGLPVVTSYHTDFPEYLSYYTLGPLSWLAWAYLRWFHNPFDTTLVPSPSIARE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 211 LRGFGITcPLVVVGRGVDTTRFSPKHRSESLRQQWGVDsDTRVMLYVGRLSPEKEVQLIVESYAAMQniQQQKTKLVVVG 290
Cdd:cd03814 160 LEGHGFE-RVRLWPRGVDTELFHPSRRDAALRRRLGPP-GRPLLLYVGRLAPEKNLEALLDADLPLA--ASPPVRLVVVG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 291 DGPDLARLKA-LPeakNVIFTGSLRGHDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLIHGVNG 369
Cdd:cd03814 236 DGPARAELEArGP---DVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTG 312
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1344404431 370 WLSPLGHKNHFIQQIYQL---PsiQQLREMGIQACHKVQQSGW 409
Cdd:cd03814 313 ALVEPGDAAAFAAALRALledP--ELRRRMAARARAEAERYSW 353
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
51-376 |
5.02e-78 |
|
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: 246.42 E-value: 5.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 51 KIAIVTETWPPEINGVALSLLQLCQGLQKQGHKILLVRPeqKAKCHDFlPEQECLVMSQAIPKYPTLQFGWPQYLK--VS 128
Cdd:cd03817 1 KIAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITP--SDPGAED-EEEVVRYRSFSIPIRKYHRQHIPFPFKkaVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 129 KAFEKFVPDVVHIVTEGPLGLTAMQAAKAKDIPVSSGFHSPFQDFSRFFDLAFLVKP--IQKYLCWFHNNTQVTCVPSRD 206
Cdd:cd03817 78 DRIKELGPDIIHTHTPFSLGKLGLRIARKLKIPIVHTYHTMYEDYLHYIPKGKLLVKavVRKLVRRFYNHTDAVIAPSEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 207 TEEALRGFGITCPLVVVGRGVDTTRFsPKHRSESLRQQWGVDSDTRVMLYVGRLSPEKEVQLIVESYAamQNIQQQKTKL 286
Cdd:cd03817 158 IKDTLREYGVKGPIEVIPNGIDLDKF-EKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFA--ELKKEPNIKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 287 VVVGDGPDLARLKALPE----AKNVIFTGSLRGHDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQY 362
Cdd:cd03817 235 VIVGDGPEREELKELARelglADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASEL 314
|
330
....*....|....
gi 1344404431 363 LIHGVNGWLSPLGH 376
Cdd:cd03817 315 VEDGENGFLFEPND 328
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
47-421 |
1.24e-56 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 193.39 E-value: 1.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 47 RPRlKIAIVTETWP-PEINGVALSLLQLCQGLQKQGHKILLVRPEQKakchdflPEQEC----LVMSQ--AIPKYPTLQF 119
Cdd:PLN02871 57 RPR-RIALFVEPSPfSYVSGYKNRFQNFIRYLREMGDEVLVVTTDEG-------VPQEFhgakVIGSWsfPCPFYQKVPL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 120 GWPQYLKVSKAFEKFVPDVVHIVTEGPLGLTAMQAAKAKDIPVSSGFHSPFQDFSRFFDLAFLVKPIQKYLCWFHNNTQV 199
Cdd:PLN02871 129 SLALSPRIISEVARFKPDLIHASSPGIMVFGALFYAKLLCVPLVMSYHTHVPVYIPRYTFSWLVKPMWDIIRFLHRAADL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 200 TCVPSRDTEEALRGFGIT-CPLVVV-GRGVDTTRFSPKHRSESLRQQW-GVDSDTRVMLYVGRLSPEKEVQLIVESYAAM 276
Cdd:PLN02871 209 TLVTSPALGKELEAAGVTaANRIRVwNKGVDSESFHPRFRSEEMRARLsGGEPEKPLIVYVGRLGAEKNLDFLKRVMERL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 277 QNiqqqkTKLVVVGDGPDLARLKALPEAKNVIFTGSLRGHDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAY-- 354
Cdd:PLN02871 289 PG-----ARLAFVGDGPYREELEKMFAGTPTVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAAra 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1344404431 355 ----DYACAHQyliHGVNGWLSPLGHKNHFIQQIYQLPSIQQLRE-MGIQACHKVQQSGWQLPVQQLEQAFY 421
Cdd:PLN02871 364 ggipDIIPPDQ---EGKTGFLYTPGDVDDCVEKLETLLADPELRErMGAAAREEVEKWDWRAATRKLRNEQY 432
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
51-406 |
1.46e-53 |
|
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: 182.74 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 51 KIAIVTETWPPEINGVALSLLQLCQGLQKQGHKILLVRPEQKakcHDFLPEQECLVMSQAIPKYPTLQFGWPQYLKVSKA 130
Cdd:cd03801 1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADP---GEPPEELEDGVIVPLLPSLAALLRARRLLRELRPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 131 FEKFVPDVVHIVTEGPLGLTAMqAAKAKDIPVSSGFHSPFQDFSRFFdLAFLVKPIQKYLCWFHNNTQVTCVpSRDTEEA 210
Cdd:cd03801 78 LRLRKFDVVHAHGLLAALLAAL-LALLLGAPLVVTLHGAEPGRLLLL-LAAERRLLARAEALLRRADAVIAV-SEALRDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 211 LRGFGIT--CPLVVVGRGVDTTRFSPKHRSESlrqqwGVDSDTRVMLYVGRLSPEKEVQLIVESYAAMQNiQQQKTKLVV 288
Cdd:cd03801 155 LRALGGIppEKIVVIPNGVDLERFSPPLRRKL-----GIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLR-RGPDVRLVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 289 VG-DGPDLARLKA--LPEAKNVIFTGSLRGHDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLIH 365
Cdd:cd03801 229 VGgDGPLRAELEEleLGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVED 308
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1344404431 366 GVNGWLSPLGHKNHFIQQI-YQLPSIQQLREMGIQACHKVQQ 406
Cdd:cd03801 309 GEGGLVVPPDDVEALADALlRLLADPELRARLGRAARERVAE 350
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
51-418 |
4.94e-40 |
|
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: 147.13 E-value: 4.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 51 KIAIVTETWPPEINGVALSLLQLCQGLQKQGHKILLVrpeqkaKCHDFLPEQECLVMSQAIPkyPTLQFGWPQYLKVSK- 129
Cdd:cd03821 1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIV------STGDGYESLVVEENGRYIP--PQDGFASIPLLRQGAg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 130 --AFEKFVP----------DVVHIV-TEGPLGLTAMQAAKAKDIPVssgFHSPFQDFSRF-FDLAFLVKPIQKYLCWFHN 195
Cdd:cd03821 73 rtDFSPGLPnwlrrnlreyDVVHIHgVWTYTSLAACKLARRRGIPY---VVSPHGMLDPWaLQQKHWKKRIALHLIERRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 196 NTQVTCV--PSRDTEEALRGFGITCPLVVVGRGVDTTRFSPKHRsesLRQQWGVDSDTRVMLYVGRLSPEKEVQLIVESY 273
Cdd:cd03821 150 LNNAALVhfTSEQEADELRRFGLEPPIAVIPNGVDIPEFDPGLR---DRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 274 AAMQNiQQQKTKLVVVGDGPD--LARLKALPEAKN---VIFTGSLRGHDLAVAYASADVFVFASQVETFGNVVLEAMASG 348
Cdd:cd03821 227 RKLAE-QGRDWHLVIAGPDDGayPAFLQLQSSLGLgdrVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACG 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1344404431 349 LPVIAYDYACAHQYLIHGVNGWLSPLGHK-NHFIQQIYQLPSIQQ-LREMGIQACHKVQQSGWQLPVQQLEQ 418
Cdd:cd03821 306 LPVVITDKCGLSELVEAGCGVVVDPNVSSlAEALAEALRDPADRKrLGEMARRARQVEENFSWEAVAGQLGE 377
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
52-423 |
1.67e-39 |
|
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: 145.60 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 52 IAIVTETWPPEIN-GVALSLLQLCQGLQKQGHKILLVRPEQ-------KAKCHDFLPEQECLVMSQAIPKYPTLQFGW-- 121
Cdd:cd03798 1 VLILTNIYPNANSpGRGIFVRRQVRALSRRGVDVEVLAPAPwgpaaarLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPlr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 122 -PQYLKVSKAFEKFVPDVVHIVTEGPLGLTAMQAAKAKDIPVSSGFHSpfqdfSRFFDLAF--LVKPIQKYLcWFHNnTQ 198
Cdd:cd03798 81 aPSLAKLLKRRRRGPPDLIHAHFAYPAGFAAALLARLYGVPYVVTEHG-----SDINVFPPrsLLRKLLRWA-LRRA-AR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 199 VTCVPSRDTEEALRGFGITCPLVVVGRGVDTTRFSPkhrsesLRQQWGVDSDTRVMLYVGRLSPEKEVQLIVESYA---- 274
Cdd:cd03798 154 VIAVSKALAEELVALGVPRDRVDVIPNGVDPARFQP------EDRGLGLPLDAFVILFVGRLIPRKGIDLLLEAFArlak 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 275 AMQNIqqqktKLVVVGDGPDLARLKALPEA----KNVIFTGSLRGHDLAVAYASADVFVFASQVETFGNVVLEAMASGLP 350
Cdd:cd03798 228 ARPDV-----VLLIVGDGPLREALRALAEDlglgDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLP 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1344404431 351 VIAYDYACAHQYLIHGVNGWLSPLGHKNHFIQQIYQLPSIQQLREMGIQACHKVQQ-SGWQLPVQQLEQAFYQV 423
Cdd:cd03798 303 VVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALAEPYLRELGEAARARVAErFSWVKAADRIAAAYRDV 376
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
51-395 |
2.39e-36 |
|
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.
Pssm-ID: 340839 [Multi-domain] Cd Length: 351 Bit Score: 136.33 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 51 KIAIVTETWPpeINGVALSLLQLCQGLQKQGHKI-LLVRPEQKAKCHdFLPEQECLVMSQAIPKYPTLQFGWPQYLKVSK 129
Cdd:cd03811 1 KILFVIPSLS--GGGAERVLLNLANALDKRGYDVtLVLLRDEGDLDK-QLNGDVKLIRLLIRVLKLIKLGLLKAILKLKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 130 AFEKFVPDVVHIVTEGPLGLTAmqAAKAKDIPVSSGFHSPF--QDFSRFFDLAFLVKpiqkylcwFHNNTQVTCVpSRDT 207
Cdd:cd03811 78 ILKRAKPDVVISFLGFATYIVA--KLAAARSKVIAWIHSSLskLYYLKKKLLLKLKL--------YKKADKIVCV-SKGI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 208 EEALRGFGITCP--LVVVGRGVDTTRFspkhRSESLRQQWGVDSDTRVMLYVGRLSPEKEVQLIVESYAAMqNIQQQKTK 285
Cdd:cd03811 147 KEDLIRLGPSPPekIEVIYNPIDIDRI----RALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKL-RKKYPDVK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 286 LVVVGDGPDLARLKALPE----AKNVIFTGSLrgHDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQ 361
Cdd:cd03811 222 LVILGDGPLREELEKLAKelglAERVIFLGFQ--SNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPRE 299
|
330 340 350
....*....|....*....|....*....|....*..
gi 1344404431 362 YLIHGVNGWLSPLGHKNHFIQQ---IYQLPSIQQLRE 395
Cdd:cd03811 300 ILDDGENGLLVPDGDAAALAGIlaaLLQKKLDAALRE 336
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
252-387 |
7.83e-33 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 120.69 E-value: 7.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 252 RVMLYVGRLSPE-KEVQLIVEsyaAMQNIQQQK--TKLVVVGDGPDLA-RLKALPEAKNVIFTGSLRghDLAVAYASADV 327
Cdd:pfam13692 2 PVILFVGRLHPNvKGVDYLLE---AVPLLRKRDndVRLVIVGDGPEEElEELAAGLEDRVIFTGFVE--DLAELLAAADV 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 328 FVFASQVETFGNVVLEAMASGLPVIAYDyACAHQYLIHGVNGWLSPLGHKNHFIQQIYQL 387
Cdd:pfam13692 77 FVLPSLYEGFGLKLLEAMAAGLPVVATD-VGGIPELVDGENGLLVPPGDPEALAEAILRL 135
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
250-400 |
2.08e-32 |
|
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: 120.07 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 250 DTRVMLYVGRLSPEKEVQLIVESYAAMQnIQQQKTKLVVVGDGPDLARLKALPEA----KNVIFTGSLRGHDLAVAYASA 325
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLK-EKNPNLKLVIAGDGEEEKRLKKLAEKlglgDNVIFLGFVSDEDLPELLKIA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1344404431 326 DVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLIHGVNGWLSPLGHKNHFIQQIYQLPSIQQLREMGIQA 400
Cdd:pfam00534 80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGEN 154
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
136-373 |
4.81e-32 |
|
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: 124.39 E-value: 4.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 136 PDVVHIVTEGPlGLTAMQAAKAKDIPVSSGFHSpfqdfSRFfdLAFLVKPIQKYLCWFHNNTQVTCVPSRDTEEALRGFG 215
Cdd:cd03819 77 IDLIHAHSRAP-AWLGWLASRLTGVPLVTTVHG-----SYL--ATYHPKDFALAVRARGDRVIAVSELVRDHLIEALGVD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 216 ITcPLVVVGRGVDTTRFSPKHRSESLRQqWGVDSDTRVMLYVGRLSPEKEVQLIVEsyaAMQNIQQQKTK-LVVVGDGPD 294
Cdd:cd03819 149 PE-RIRVIPNGVDTDRFPPEAEAEERAQ-LGLPEGKPVVGYVGRLSPEKGWLLLVD---AAAELKDEPDFrLLVAGDGPE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 295 LARLKALPE----AKNVIFTGSLrgHDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLIHGVNGW 370
Cdd:cd03819 224 RDEIRRLVErlglRDRVTFTGFR--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGL 301
|
...
gi 1344404431 371 LSP 373
Cdd:cd03819 302 LVP 304
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
51-400 |
9.27e-30 |
|
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: 118.47 E-value: 9.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 51 KIAIVTETWPpeinGVALSLLQLCQGLQKQGHKILLVRPEQKAKchdflpEQECLVMSQAIPKYPTLQFG------WPQY 124
Cdd:cd03808 1 KILFIVNVDG----GFQSFRLPLIKALVKKGYEVHVIAPDGDKL------SDELKELGVKVIDIPILRRGinplkdLKAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 125 LKVSKAFEKFVPDVVHIVTEGPlGLTAMQAAK-AKDIPV---SSGFHSPFQDFSRffdLAFLVKPIQKYLcwFHNNTQVT 200
Cdd:cd03808 71 FKLYKLLKKEKPDIVHCHTPKP-GILGRLAARlAGVPKViytVHGLGFVFTEGKL---LRLLYLLLEKLA--LLFTDKVI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 201 CVPSRDTEEALRGFGITCPLVVVGRG--VDTTRFSPKhrSESLRqqwgvdSDTRVMLYVGRLSPEKEVQLIVEsyaAMQN 278
Cdd:cd03808 145 FVNEDDRDLAIKKGIIKKKKTVLIPGsgVDLDRFQYS--PESLP------SEKVVFLFVARLLKDKGIDELIE---AAKI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 279 IQQQ--KTKLVVVGDGPDL----ARLKALPEAKNVIFTGSLRghDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVI 352
Cdd:cd03808 214 LKKKgpNVRFLLVGDGELEnpseILIEKLGLEGRIEFLGFRS--DVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVI 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1344404431 353 AYDyACAHQYLI-HGVNGWLSPLGHKNHFIQQIYQLPSIQQLR-EMGIQA 400
Cdd:cd03808 292 TTD-VPGCRELViDGVNGFLVPPGDVEALADAIEKLIEDPELRkEMGEAA 340
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
50-375 |
8.18e-28 |
|
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: 113.22 E-value: 8.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 50 LKIAIVTEtwpPEINGVALSLLQLCQGLQKQGHKILLV---RPEQKAKCHDFLPEQECLVMSQAIPKYPTLQFGWPQylK 126
Cdd:cd04962 1 MKIGIVCY---PSYGGSGVVATELGLELAERGHEVHFIssaIPFRLNLYSGNIFFHEVEVPNYPLFEYPPYTLALAS--K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 127 VSKAFEKFVPDVVHIVTEGPLGLTAMQAAK--AKDIPVSS----------GFHSPFQDFSRFfdlaflvkPIQKylcwfh 194
Cdd:cd04962 76 IVEVAKEHKLDVLHAHYAIPHASCAYLAREilGEKIPIVTtlhgtditlvGYDPSLQPAVRF--------SINK------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 195 nNTQVTCVPSRDTEEALRGFGITCPLVVVGRGVDTTRFSPKHRSESLRQQWGVDsDTRVMLYVGRLSPEKEVQLIVESYA 274
Cdd:cd04962 142 -SDRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKPAGALKRRLLAPP-DEKVVIHVSNFRPVKRIDDVVRVFA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 275 AMQNiqQQKTKLVVVGDGPDLARLKALPEA----KNVIFTGSLrgHDLAVAYASADVFVFASQVETFGNVVLEAMASGLP 350
Cdd:cd04962 220 RVRR--KIPAKLLLVGDGPERVPAEELARElgveDRVLFLGKQ--DDVEELLSIADLFLLPSEKESFGLAALEAMACGVP 295
|
330 340
....*....|....*....|....*
gi 1344404431 351 VIAYDYACAHQYLIHGVNGWLSPLG 375
Cdd:cd04962 296 VVSSNAGGIPEVVKHGETGFLSDVG 320
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
72-415 |
3.50e-27 |
|
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: 111.18 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 72 QLCQGLQKQGHKILLVRPEQKAKCHDF-LPEQ-ECLVMsqAIPKYPTLQFGWpQYLKVSKAFEKFV----PDVVhiVTEG 145
Cdd:cd03820 21 NLANHLAKKGYDVTIISLDSAEKPPFYeLDDNiKIKNL--GDRKYSHFKLLL-KYFKKVRRLRKYLknnkPDVV--ISFR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 146 PLGLTAMQAAKAKDIPVSSgFHspfqdFSRFFDLAFLVKPIQKYLCWFHNNTqVTCVPSRDTEEALRGFGItcPLVVVGR 225
Cdd:cd03820 96 TSLLTFLALIGLKSKLIVW-EH-----NNYEAYNKGLRRLLLRRLLYKRADK-IVVLTEADKLKKYKQPNS--NVVVIPN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 226 GVDttrFSPKHRSESLRQqwgvdsdtRVMLYVGRLSPEKEVQLIVESYAamqNIQQQKT--KLVVVGDGPDLARLKALPE 303
Cdd:cd03820 167 PLS---FPSEEPSTNLKS--------KRILAVGRLTYQKGFDLLIEAWA---LIAKKHPdwKLRIYGDGPEREELEKLID 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 304 AKN----VIFTGSLRghDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLI-HGVNGWLSPLGHKN 378
Cdd:cd03820 233 KLGledrVKLLGPTK--NIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCPTGPSEIIeDGENGLLVPNGDVD 310
|
330 340 350
....*....|....*....|....*....|....*...
gi 1344404431 379 HFIQQIYQLPSIQQLRE-MGIQACHKVQQSGWQLPVQQ 415
Cdd:cd03820 311 ALAEALLRLMEDEELRKkMGKNARKNAERFSIEKIIKQ 348
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
222-418 |
1.23e-26 |
|
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: 110.41 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 222 VVGRGVDTTRFSPKHRSESLRQQWGVDSDTRVMLYVGRLSPEKEVQLIVESYAAMQNIQQQKTKLVVVGDGPDLA----- 296
Cdd:cd03800 191 VVPPGVDLERFFPVDRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGGPSDDPLsmdre 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 297 RLKALPE----AKNVIFTGSLRGHDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLIHGVNGWLS 372
Cdd:cd03800 271 ELAELAEelglIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLV 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1344404431 373 PLGHKNHF---IQQIYQLPSI-QQLREMGIQacHKVQQSGWQLPVQQLEQ 418
Cdd:cd03800 351 DPHDPEALaaaLRRLLDDPALwQRLSRAGLE--RARAHYTWESVADQLLT 398
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
52-371 |
7.57e-26 |
|
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: 104.79 E-value: 7.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 52 IAIVTETWPPEINGVALSLLQLCQGLQKQGHKILLVrpeqkAKCHDFLPEQECLVMSQaipkyptlqfgwpqylkvskaf 131
Cdd:cd01635 1 ILLVTGEYPPLRGGLELHVRALARALAALGHEVTVL-----ALLLLALRRILKKLLEL---------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 132 ekfVPDVVHIVTEGPLGLTAMQAAKAKDIPVSSGFHSPFQDFSRFfdlaflvkpiqkylcwfhnntqvtcvpsrdtEEAL 211
Cdd:cd01635 54 ---KPDVVHAHSPHAAALAALLAARLLGIPIVVTVHGPDSLESTR-------------------------------SELL 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 212 RGFGITCPLVVVGRgvdttrfspkhrseslrqqwgvdsdtrvmLYVGRLSPEKEVQLIVESYAAMQNiQQQKTKLVVVGD 291
Cdd:cd01635 100 ALARLLVSLPLADK-----------------------------VSVGRLVPEKGIDLLLEALALLKA-RLPDLVLVLVGG 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 292 GPDLARLKALPEAK-----NVIFTGSLRGHDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLIHG 366
Cdd:cd01635 150 GGEREEEEALAAALgllerVVIIGGLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDG 229
|
....*
gi 1344404431 367 VNGWL 371
Cdd:cd01635 230 ENGLL 234
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
219-384 |
4.97e-24 |
|
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: 102.41 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 219 PLVVVGRGVDTTRFSPKHRsESLRQQWGVDSDTRVMLYVGR--LSPEKEVQLIVESYAAMQniQQQKTKLVVVG-DGPDL 295
Cdd:cd03825 162 PVVVIPNGIDTEIFAPVDK-AKARKRLGIPQDKKVILFGAEsvTKPRKGFDELIEALKLLA--TKDDLLLVVFGkNDPQI 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 296 ARLKAlpeakNVIFTGSLR-GHDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLIHGVNGWLSPL 374
Cdd:cd03825 239 VILPF-----DIISLGYIDdDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPP 313
|
170
....*....|
gi 1344404431 375 GHKNHFIQQI 384
Cdd:cd03825 314 GDVQALAEAI 323
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
227-371 |
1.00e-23 |
|
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: 101.59 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 227 VDTTRFSPKHRSESLrqqwgvdsdtrvMLYVGRLSPEKEVQLIVESYAAMQNiqqqktKLVVVGDGPDLARLKALpEAKN 306
Cdd:cd03804 187 VDTDAFAPAADKEDY------------YLTASRLVPYKRIDLAVEAFNELPK------RLVVIGDGPDLDRLRAM-ASPN 247
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1344404431 307 VIFTGSLRGHDLAVAYASADVFVFASQvETFGNVVLEAMASGLPVIAYDYACAHQYLIHGVNGWL 371
Cdd:cd03804 248 VEFLGYQPDEVLKELLSKARAFVFAAE-EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGIL 311
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
125-355 |
2.28e-23 |
|
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: 100.47 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 125 LKVSKAFEKFVPDVVHIVTEGPLGLTAMQAAKAKDIPVSSGFHSP--FQDFSRFfdLAFLVKPIQKYLCwfhnntQVTCV 202
Cdd:cd03807 69 LRLAKLIRKRNPDVVHTWMYHADLIGGLAAKLAGGVKVIWSVRSSniPQRLTRL--VRKLCLLLSKFSP------ATVAN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 203 PSRDTEEALRGFGITCPLVVVGRGVDTTRFSP-KHRSESLRQQWGVDSDTRVMLYVGRLSPEKEVQLIVESyAAMQNIQQ 281
Cdd:cd03807 141 SSAVAEFHQEQGYAKNKIVVIYNGIDLFKLSPdDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRA-AALLVETH 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1344404431 282 QKTKLVVVGDGP---DLARL-KALPEAKNVIFTGSlrGHDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAYD 355
Cdd:cd03807 220 PDLRLLLVGRGPerpNLERLlLELGLEDRVHLLGE--RSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATD 295
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
51-375 |
7.42e-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: 7.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 51 KIAIVTETWPPEINGVAL-SLLQLCQGLQKQGHKILLV-----RPEQKAKCHDF----LPEQECLVMSQAIPKYPTLQFG 120
Cdd:cd03823 1 KILLVNSLYPPQRVGGAEiSVHDLAEALVAEGHEVAVLtagvgPPGQATVARSVvryrRAPDETLPLALKRRGYELFETY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 121 WPQ-YLKVSKAFEKFVPDVVHIVTEGPLGLTAMQAAKAKDIPVSSGFHspfqDFSRFFDLAFLvkpiqkylcwFHNNTQV 199
Cdd:cd03823 81 NPGlRRLLARLLEDFRPDVVHTHNLSGLGASLLDAARDLGIPVVHTLH----DYWLLCPRQFL----------FKKGGDA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 200 TCVPSRDTEEALRGFGITCPLVVVGR-GVdttrfspkhRSESLRQQWGVDSDTR-VMLYVGRLSPEKEVQLIVEsyaAMQ 277
Cdd:cd03823 147 VLAPSRFTANLHEANGLFSARISVIPnAV---------EPDLAPPPRRRPGTERlRFGYIGRLTEEKGIDLLVE---AFK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 278 NIQQQKTKLVVVGDGPDLaRLKALPEAKNVIFTGSLRGHDLAVAYASADVFVFASQ-VETFGNVVLEAMASGLPVIAYDY 356
Cdd:cd03823 215 RLPREDIELVIAGHGPLS-DERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDL 293
|
330
....*....|....*....
gi 1344404431 357 ACAHQYLIHGVNGWLSPLG 375
Cdd:cd03823 294 GGIAELIQPGVNGLLFAPG 312
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
64-229 |
2.64e-22 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 92.98 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 64 NGVALSLLQLCQGLQKQGHKILLVRPEQKAKcHDFLPEQECLVMSQAIPKYPTLQFGWPQYLKVSKAFEKFVPDVVHIVT 143
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGP-LAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 144 EGPLGLTAMQAAKAKDIPVSSGFHSPFQDFSRF-FDLAFLVKPIQKYLCWFHNNTQVTCVPSRDTEEALR-GFGIT-CPL 220
Cdd:pfam13439 80 PFPLGLAALAARLRLGIPLVVTYHGLFPDYKRLgARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRrLYGVPpEKI 159
|
....*....
gi 1344404431 221 VVVGRGVDT 229
Cdd:pfam13439 160 RVIPNGVDL 168
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
51-400 |
5.54e-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: 5.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 51 KIAIVTETWPPEINGVALSLLQLCQGLQKQGHKILLVRPEqkakCHDFLPEQECLVMSQ----AIPKYPTLQFGWPQ--- 123
Cdd:cd03794 1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPS----PNYPLGRIFAGATETkdgiRVIRVKLGPIKKNGlir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 124 ------------YLKVSKAFEKfvPDVVHiVTEGP--LGLTAMQAAKAKDIPVssGFHspFQDFsrFFDLA--------- 180
Cdd:cd03794 77 rllnylsfalaaLLKLLVREER--PDVII-AYSPPitLGLAALLLKKLRGAPF--ILD--VRDL--WPESLialgvlkkg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 181 ---FLVKPIQKYLCwfhNNTQVTCVPSRDTEEALRGFGI-TCPLVVVGRGVDTTRFSPKHRSEslRQQWGVDSDTRVMLY 256
Cdd:cd03794 148 sllKLLKKLERKLY---RLADAIIVLSPGLKEYLLRKGVpKEKIIVIPNWADLEEFKPPPKDE--LRKKLGLDDKFVVVY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 257 VGRLSPEKEVQLIVEsyaAMQNIQQQKT-KLVVVGDGPDLARLKALPEAK---NVIFTGSLRGHDLAVAYASADV-FVFA 331
Cdd:cd03794 223 AGNIGKAQGLETLLE---AAERLKRRPDiRFLFVGDGDEKERLKELAKARgldNVTFLGRVPKEEVPELLSAADVgLVPL 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1344404431 332 SQVETFGNVV----LEAMASGLPVIAYDYACAHQYLIHGVNGWLSPLGHKNHFIQQIYQL-PSIQQLREMGIQA 400
Cdd:cd03794 300 KDNPANRGSSpsklFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELlDDPELRRAMGENG 373
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
314-425 |
9.62e-22 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 90.05 E-value: 9.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 314 RGHD--LAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLIHGVNGWLSPLGHKNHFIQQIYQLPSIQ 391
Cdd:COG0438 8 KGLDllLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDP 87
|
90 100 110
....*....|....*....|....*....|....*.
gi 1344404431 392 QLRE-MGIQACHKVQQS-GWQLPVQQLEQAFYQVVK 425
Cdd:COG0438 88 ELRRrLGEAARERAEERfSWEAIAERLLALYEELLA 123
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
51-400 |
2.70e-21 |
|
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: 94.65 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 51 KIAIVTETWPPEINGVALSLLQLCQGLQKQGH--KILLVRPEQKAKCHDFLPEQECLVMSQAIPKYPTLQFG-WPQYLKV 127
Cdd:cd03795 1 KVLHVFKFYYPDIGGIEQVIYDLAEGLKKKGIevDVLCFSKEKETPEKEENGIRIHRVKSFLNVASTPFSPSyIKRFKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 128 SKAfekfvPDVVHIVTEGPLG--LTAMQAAKAKDIpVSsgFHSpfqDFSRFFDLAFLVKPIQKylcWFHNNTQVTCVPS- 204
Cdd:cd03795 81 AKE-----YDIIHYHFPNPLAdlLLFFSGAKKPVV-VH--WHS---DIVKQKKLLKLYKPLMT---RFLRRADRIIATSp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 205 --RDTEEALRGFgiTCPLVVVGRGVDTTrfSPKHRSESLRQQWGVDSDTRVMLYVGRLSPEKEVQLIVEsyaAMQNIqqq 282
Cdd:cd03795 147 nyVETSPTLREF--KNKVRVIPLGIDKN--VYNIPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLIE---AAQYL--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 283 KTKLVVVGDGPDLARLKALPEA---KNVIFTGSLRGHDLAVAYASADVFVFAS--QVETFGNVVLEAMASGLPVIAYDYA 357
Cdd:cd03795 217 NYPIVIGGEGPLKPDLEAQIELnllDNVKFLGRVDDEEKVIYLHLCDVFVFPSvlRSEAFGIVLLEAMMCGKPVISTNIG 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1344404431 358 CAHQYL-IHGVNGWLSPLGHKNHFIQQIYQLPSIQQLRE-MGIQA 400
Cdd:cd03795 297 TGVPYVnNNGETGLVVPPKDPDALAEAIDKLLSDEELREsYGENA 341
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
65-353 |
3.57e-21 |
|
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: 94.35 E-value: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 65 GVALSLLQLCQGLQKQGHKILLVRPEQKAKCHDFLPEQECLVMSQAIPKYPTLQFGWPQYLKVSKAFeKFVPDVVHIVT- 143
Cdd:cd03809 15 GIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPK-KDKPDLLHSPHn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 144 EGPLGLtamqaakaKDIPVSSGFH--SPFqDFSRFFDLAFLVKPIQKYLCWFHNNTQVTCVpSRDT-EEALRGFGITCPL 220
Cdd:cd03809 94 TAPLLL--------KGCPQVVTIHdlIPL-RYPEFFPKRFRLYYRLLLPISLRRADAIITV-SEATrDDIIKFYGVPPEK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 221 VVVGRGVDTTRFSPKHRSESLRQQWGVDSDTrvMLYVGRLSPEKEVQLIVEsyaAMQNIQQQKT--KLVVVGDGPD---- 294
Cdd:cd03809 164 IVVIPLGVDPSFFPPESAAVLIAKYLLPEPY--FLYVGTLEPRKNHERLLK---AFALLKKQGGdlKLVIVGGKGWedee 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 295 -LARLKALPEAKNVIFTGSLRGHDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIA 353
Cdd:cd03809 239 lLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIA 298
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
204-375 |
2.71e-20 |
|
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.
Pssm-ID: 132132 [Multi-domain] Cd Length: 374 Bit Score: 91.71 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 204 SRDTEEALRGfGITCP---LVVVGRGVDTTRFSPKH--RSESLRQQWGVDsDTRVMLYVGRLSPEKEVQLIVESYAAMQN 278
Cdd:TIGR03088 144 SRDLEDWLRG-PVKVPpakIHQIYNGVDTERFHPSRgdRSPILPPDFFAD-ESVVVGTVGRLQAVKDQPTLVRAFALLVR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 279 IQ---QQKTKLVVVGDGPDLARLKALPEAKNVIFTGSLRGH--DLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIA 353
Cdd:TIGR03088 222 QLpegAERLRLVIVGDGPARGACEQMVRAAGLAHLVWLPGErdDVPALMQALDLFVLPSLAEGISNTILEAMASGLPVIA 301
|
170 180
....*....|....*....|..
gi 1344404431 354 YDYACAHQYLIHGVNGWLSPLG 375
Cdd:TIGR03088 302 TAVGGNPELVQHGVTGALVPPG 323
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
118-375 |
5.76e-17 |
|
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340860 [Multi-domain] Cd Length: 365 Bit Score: 81.73 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 118 QFGWPQYLKVSKAFekFVPDVVHiVTEGPLGLTAMQAAKAKDIPVSSGFHSPFQDFSRFFDLAFLVKPIQKYLCWFHNNT 197
Cdd:cd05844 66 LLGWSAPRLGGAAG--LAPALVH-AHFGRDGVYALPLARALGVPLVVTFHGFDITTSRAWLAASPGWPSQFQRHRRALQR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 198 Q---VTCVpSRDTEEALRGFGITCPLVVVGR-GVDTTRFSPKHRSEslrqqwgvdsDTRVMLYVGRLSPEKEVQLIVESY 273
Cdd:cd05844 143 PaalFVAV-SGFIRDRLLARGLPAERIHVHYiGIDPAKFAPRDPAE----------RAPTILFVGRLVEKKGCDVLIEAF 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 274 AAMQNiQQQKTKLVVVGDGPDLARLKALP-EAKNVIFTGSLRGHDLAVAYASADVFVFASQV------ETFGNVVLEAMA 346
Cdd:cd05844 212 RRLAA-RHPTARLVIAGDGPLRPALQALAaALGRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdsEGLGIVLLEAAA 290
|
250 260
....*....|....*....|....*....
gi 1344404431 347 SGLPVIAYDYACAHQYLIHGVNGWLSPLG 375
Cdd:cd05844 291 CGVPVVSSRHGGIPEAILDGETGFLVPEG 319
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
254-387 |
1.56e-16 |
|
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: 80.04 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 254 MLYVGRLSPEKEVQLIVESYA-AMQNIQQqkTKLVVVGDGPDLARLKALPE----AKNVIFTGSLRghDLAVAYASADVF 328
Cdd:cd04949 163 IITISRLAPEKQLDHLIEAVAkAVKKVPE--ITLDIYGYGEEREKLKKLIEelhlEDNVFLKGYHS--NLDQEYQDAYLS 238
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 329 VFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLI-HGVNGWLSPLGHKNHFIQQIYQL 387
Cdd:cd04949 239 LLTSQMEGFGLTLMEAIGHGLPVVSYDVKYGPSELIeDGENGYLIEKNNIDALADKIIEL 298
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
125-355 |
1.74e-16 |
|
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: 80.57 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 125 LKVSKAFEKFVPDVVHivtegplgltamqaakakdipvSSGFHSP-FQDFSRFFdlaflvKPIQKYLCWFHN-----NTQ 198
Cdd:cd04951 69 LKLKKIISAFKPDVVH----------------------SHMFHANiFARFLRML------YPIPLLICTAHNkneggRIR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 199 VTCVPSRD---------TEEALRGFgIT------CPLVVVGRGVDTTRFSPKHRS-ESLRQQWGVDSDTRVMLYVGRLSP 262
Cdd:cd04951 121 MFIYRLTDflcdittnvSREALDEF-IAkkafskNKSVPVYNGIDLNKFKKDINVrLKIRNKLNLKNDEFVILNVGRLTE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 263 EKEVQLIVESYAAMQNIQQqKTKLVVVGDGP---DLARL-KALPEAKNVIFTGSLRghDLAVAYASADVFVFASQVETFG 338
Cdd:cd04951 200 AKDYPNLLLAISELILSKN-DFKLLIAGDGPlrnELERLiCNLNLVDRVILLGQIS--NISEYYNAADLFVLSSEWEGFG 276
|
250
....*....|....*..
gi 1344404431 339 NVVLEAMASGLPVIAYD 355
Cdd:cd04951 277 LVVAEAMACERPVVATD 293
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
51-402 |
3.08e-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: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 51 KIAIVTETW----PPEINGVALSLLQLCQGLQKQGHKILLVRPE-QKAKCHDFLPEQECLVMSQAIPKYPTLQFgwpqyl 125
Cdd:cd03802 1 RIAQVSPPRgpvpPGKYGGTELVVSALTEGLVRRGHEVTLFAPGdSHTSAPLVAVIPRALRLDPIPQESKLAEL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 126 kvSKAFEKFVP----DVVHIVTEGPLGltamqaakakdiPVSSGFHSPFQDFSRFFDLAflvkPIQKYlCWFHNNTQVTC 201
Cdd:cd03802 75 --LEALEVQLRasdfDVIHNHSYDWLP------------PFAPLIGTPFVTTLHGPSIP----PSLAI-YAAEPPVNYVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 202 VPSRDTEEALRGFGITcplvVVGRGVDTTRFSPkhrseslrqqwgVDSDTRVMLYVGRLSPEKEVQLIVEsyAAmqniQQ 281
Cdd:cd03802 136 ISDAQRAATPPIDYLT----VVHNGLDPADYRF------------QPDPEDYLAFLGRIAPEKGLEDAIR--VA----RR 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 282 QKTKLVVVG--DGPDLARLKALPE-AKNVIFTGSLRGHDLAVAYASADVFVFASQV-ETFGNVVLEAMASGLPVIAYDYA 357
Cdd:cd03802 194 AGLPLKIAGkvRDEDYFYYLQEPLpGPRIEFIGEVGHDEKQELLGGARALLFPINWdEPFGLVMIEAMACGTPVIAYRRG 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1344404431 358 CAHQYLIHGVNGWLSPlgHKNHFIQQIYQLPSIQQlremgiQACH 402
Cdd:cd03802 274 GLPEVIQHGETGFLVD--SVEEMAEAIANIDRIDR------AACR 310
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
108-355 |
2.61e-14 |
|
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: 73.86 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 108 SQAIPKYptlqfgwpqYLKVSKAFEKFVPDVVHIVTEGPLGLTAMQAAKAKdIPVS-SGFH-SPFQDFSRFFDLAFLVKP 185
Cdd:cd03812 62 KKNIIKY---------FIKLLKLIKKEKYDIVHVHGSSSNGIILLLAAKAG-VPVRiAHSHnTKDSSIKLRKIRKNVLKK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 186 IQKYlcwfhNNTQVTCVpSRDTEEALRGFGITCPLVVVGRGVDTTRFSPKHRSESLRQQWGVDSDTRVMLYVGRLSPEKE 265
Cdd:cd03812 132 LIER-----LSTKYLAC-SEDAGEWLFGEVENGKFKVIPNGIDIEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 266 VQLIVESYAAMQNIQQqKTKLVVVGDGPDLARLKALPE----AKNVIFTGSLRghDLAVAYASADVFVFASQVETFGNVV 341
Cdd:cd03812 206 HSFLIDIFEELKKKNP-NVKLVLVGEGELKEKIKEKVKelglEDKVIFLGFRN--DVSEILSAMDVFLFPSLYEGLPLVA 282
|
250
....*....|....
gi 1344404431 342 LEAMASGLPVIAYD 355
Cdd:cd03812 283 VEAQASGLPCLLSD 296
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
202-353 |
1.10e-13 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 72.13 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 202 VPSRDTEEALRGFGITCPLVVVGRGVDTTRFSpKHRSESLRQQWGVDSDTRVMLYVGRLSPEKEVQLIVESYAAMQNIQQ 281
Cdd:PRK15484 145 VPSQFLKKFYEERLPNADISIVPNGFCLETYQ-SNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 282 QkTKLVVVGD------GPDLA-RLKALPEAKNV----IFTGSLRGHDLAVAYASADVFVFASQV-ETFGNVVLEAMASGL 349
Cdd:PRK15484 224 N-LKLVVVGDptasskGEKAAyQKKVLEAAKRIgdrcIMLGGQPPEKMHNYYPLADLVVVPSQVeEAFCMVAVEAMAAGK 302
|
....
gi 1344404431 350 PVIA 353
Cdd:PRK15484 303 PVLA 306
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
51-373 |
1.47e-10 |
|
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: 62.47 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 51 KIAIVTETWPpeINGVALSLLQLCqGLQKQGHK--ILLVRPEQKAKCHdflpeqeclvmsQAIPKY--PTLQFgwpqYLK 126
Cdd:cd03799 1 KIAFIVDEFP--VLSETFILNQIT-GLIDRGHEvdIYAVNPGDLVKRH------------PDVEKYnvPSLNL----LYA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 127 VSKAFEKFVPDVVHiVTEGPLGLTAmqaAKAKDIPVSSG-----FH----SPF------QDFSRFFDLAFLVKPIQKylC 191
Cdd:cd03799 62 IVGLNKKGAYDIIH-CQFGPLGALG---ALLRRLKVLKGklvtsFRgydiSMYvilegnKVYPQLFAQGDLFLPNCE--L 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 192 WFHNNTQVTCVPSRdteealrgfgitcpLVVVGRGVDTTRFSPKHRSESLRQQWGVdsdtrvmLYVGRLSPEKEVQLIVE 271
Cdd:cd03799 136 FKHRLIALGCDEKK--------------IIVHRSGIDCNKFRFKPRYLPLDGKIRI-------LTVGRLTEKKGLEYAIE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 272 SYAAMQ----NIQQQktklvVVGDGPDLARLKALPE----AKNVIFTGSLRGHDLAVAYASADVFVFASQVETFG----- 338
Cdd:cd03799 195 AVAKLAqkypNIEYQ-----IIGDGDLKEQLQQLIQelniGDCVKLLGWKPQEEIIEILDEADIFIAPSVTAADGdqdgp 269
|
330 340 350
....*....|....*....|....*....|....*.
gi 1344404431 339 -NVVLEAMASGLPVIAYDYACAHQYLIHGVNGWLSP 373
Cdd:cd03799 270 pNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVP 305
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
64-226 |
2.38e-08 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 53.17 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 64 NGVALSLLQLCQGLQKQGHKILLVRPEQKAKCHdflPEQECLVMSQAIPKYPTLQ-FGWPQYL-KVSKAFEKFVPDVVHI 141
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRP---ELVGDGVRVHRLPVPPRPSpLADLAALrRLRRLLRAERPDVVHA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 142 VTeGPLGLTAMQAAKAKDIPVSSGFHS-PFQDFSRFfdLAFLVKPIQKylcWFHNNTQVTCVPSRDTEEALRGFGITC-P 219
Cdd:pfam13579 78 HS-PTAGLAARLARRRRGVPLVVTVHGlALDYGSGW--KRRLARALER---RLLRRADAVVVVSEAEAELLRALGVPAaR 151
|
....*..
gi 1344404431 220 LVVVGRG 226
Cdd:pfam13579 152 VVVVPNG 158
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
222-355 |
2.48e-08 |
|
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: 55.80 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 222 VVGRGVDTTRFSP--KHRSESlrqqwgvdsDTRVMLYVGRLSPEKEVQLIVESYAAMQNiQQQKTKLVVVG---DGPDLA 296
Cdd:cd03813 271 VIPNGIDIQRFAParEERPEK---------EPPVVGLVGRVVPIKDVKTFIRAFKLVRR-AMPDAEGWLIGpedEDPEYA 340
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1344404431 297 ----RL-KALPEAKNVIFTGSLRGHDlavAYASADVFVFASQVETFGNVVLEAMASGLPVIAYD 355
Cdd:cd03813 341 qeckRLvASLGLENKVKFLGFQNIKE---YYPKLGLLVLTSISEGQPLVILEAMASGVPVVATD 401
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
241-407 |
5.22e-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: 54.63 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 241 LRQQWGVDSDTRVMLYVGRLSPEKEVQLIVESYAAMQNiQQQKTKLVVVG----DGPDLARL----KALPEAKNVIFTGS 312
Cdd:cd03792 187 LEKPFVIDPERPYILQVARFDPSKDPLGVIDAYKLFKR-RAEEPQLVICGhgavDDPEGSVVyeevMEYAGDDHDIHVLR 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 313 LRGHD--LAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLIHGVNGWLSPLGHKNHFiqQIYQLPSI 390
Cdd:cd03792 266 LPPSDqeINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAV--RILRLLTD 343
|
170
....*....|....*...
gi 1344404431 391 QQLRE-MGIQACHKVQQS 407
Cdd:cd03792 344 PELRRkMGLAAREHVRDN 361
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
260-371 |
1.01e-07 |
|
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: 53.62 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 260 LSPEKEVQLIVESYAAMQNIQQQ-KTKLVVVGDGPDLARLKAL----PEAKNVIFTGSLRGHDLAVAYA--SADVFVFAS 332
Cdd:cd04946 233 IVPVKRIDLIIETLNSLCVAHPSiCISWTHIGGGPLKERLEKLaenkLENVKVNFTGEVSNKEVKQLYKenDVDVFVNVS 312
|
90 100 110
....*....|....*....|....*....|....*....
gi 1344404431 333 QVETFGNVVLEAMASGLPVIAYDYACAHQYLIHGVNGWL 371
Cdd:cd04946 313 ESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLL 351
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
257-379 |
3.21e-07 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 52.73 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 257 VGRLSPEKEVQLIVESyAAMQNIQQQKTKLVVVGDGPDLARLKALPE----AKNVIFTGsLRGHdLAVAYASADVFVFAS 332
Cdd:PRK15179 523 VMRVDDNKRPFLWVEA-AQRFAASHPKVRFIMVGGGPLLESVREFAQrlgmGERILFTG-LSRR-VGYWLTQFNAFLLLS 599
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1344404431 333 QVETFGNVVLEAMASGLPVIAYDYACAHQYLIHGVNGWLSPLGHKNH 379
Cdd:PRK15179 600 RFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTA 646
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
222-384 |
4.51e-07 |
|
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: 51.59 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 222 VVGRGVDTTRFSPKHRSEsLRQQWG--VDSDTRVMLYVGR-LSPEKEVQLIVESYAAMQNIQQQKTKLVVVGDG------ 292
Cdd:cd03818 183 VIHDGVDTDRLAPDPAAR-LRLLNGteLKAGDPVITYVARnLEPYRGFHVFMRALPRIQARRPDARVVVVGGDGvsygsp 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 293 -PDLA--RLKALPEA----KNVIFTGsLRGHDLAVAYASA-DVFVFAsqveTFGNV----VLEAMASGLPVIAYDYACAH 360
Cdd:cd03818 262 pPDGGswKQKMLAELgvdlERVHFVG-KVPYDQYVRLLQLsDAHVYL----TYPFVlswsLLEAMACGCPVIGSDTAPVR 336
|
170 180
....*....|....*....|....
gi 1344404431 361 QYLIHGVNGWLSPLGHKNHFIQQI 384
Cdd:cd03818 337 EVIRDGRNGLLVDFFDPDALAAAV 360
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
70-191 |
1.31e-06 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 47.70 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 70 LLQLCQGLQKQGHKILLVRPEQKAKchDFLPEQECLVMSQAIP-KYPtlqFGWPQYLKVSKAFEKFVPDVVHIVTEGPLG 148
Cdd:pfam13477 13 TLRWADALADRGYDVHVISSKGPAK--DELIAEGIHVHRLKVPrKGP---LGYLKAFRLKKLIKKIKPDVVHVHYAKPYG 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1344404431 149 LTAMQAAK-AKDIPVSSGFHSpfQDFSRFFDLAFLVKPIQKYLC 191
Cdd:pfam13477 88 LLAGLAARlSGFPPVVLSAWG--LDVYKFPNKSRLKKLLLKLNL 129
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
52-353 |
3.21e-06 |
|
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: 49.16 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 52 IAIVTETWPPEINGVALSLLQLCQGLQKQGHKILL----------VR---PEQKAKCHDFLPeqeclVMSQAIpkYPTLQ 118
Cdd:cd03796 2 ICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVithaygnrvgVRyltNGLKVYYLPFKV-----FYNQST--LPTLF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 119 FGWPQYLKVskafekFVPDVVHIV----TEGPLGLTAMQAAKakdipvSSGFHSPFQDFSRF-F-DLAFLVkpIQKYLCW 192
Cdd:cd03796 75 STFPLLRNI------LIRERIQIVhghqAFSSLAHEALFHAR------TLGLKTVFTDHSLFgFaDASSIL--TNKLLRF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 193 F-HNNTQVTCVpSRDTEE--ALRGfGITCPLV-VVGRGVDTTRFSPkhrSESLRqqwgvDSDTRVMLYVGRLSPEKEVQL 268
Cdd:cd03796 141 SlADIDHVICV-SHTSKEntVLRA-SLDPRIVsVIPNAVDSSDFTP---DPSKP-----DPNKITIVVISRLVYRKGIDL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 269 IVEsyaAMQNIQQQ--KTKLVVVGDGPDLARLKALPEAKN----VIFTGSLRGHDLAVAYASADVFVFASQVETFGNVVL 342
Cdd:cd03796 211 LVG---IIPRICKKhpNVRFIIGGDGPKRIELEEMREKYQlqdrVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIV 287
|
330
....*....|.
gi 1344404431 343 EAMASGLPVIA 353
Cdd:cd03796 288 EAASCGLLVVS 298
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
239-353 |
9.00e-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: 47.94 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 239 ESLRQQWG--VDSDTRVMLYVGRLSPEKEVQLIVEsyaAMQNIQQQKTKLVVVGDGPDL--ARLKAL----PEAKNVIFt 310
Cdd:cd03791 280 AALQKELGlpVDPDAPLFGFVGRLTEQKGVDLILD---ALPELLEEGGQLVVLGSGDPEyeQAFRELaeryPGKVAVVI- 355
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1344404431 311 gslrGHDLAVA---YASADVFVFASQVETFGNVVLEAMASGLPVIA 353
Cdd:cd03791 356 ----GFDEALAhriYAGADFFLMPSRFEPCGLVQMYAMRYGTLPIV 397
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
249-373 |
2.10e-05 |
|
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: 46.43 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 249 SDTRVMLYVGRLSPEKEVQLIVESYAAM--QNIQQQKTKLVVVGdGPD------------LARL--KALPEAKNVIFTGS 312
Cdd:cd03805 209 SNKKFFLSINRFERKKNIALAIEAFAKLkqKLPEFENVRLVIAG-GYDprvaenveyleeLQRLaeELLNVEDQVLFLRS 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1344404431 313 LRGHDLAVAYASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLIHGVNGWLSP 373
Cdd:cd03805 288 ISDSQKEQLLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCE 348
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
249-371 |
2.34e-05 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 46.24 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 249 SDTRVMLYVGRLSPEKEVQLiVESYAAMQNIQQQkTKLVVVGDGPDLARLKALPE----AKNVIFTG--SLRGHDLAVAY 322
Cdd:PRK09922 178 DKPAVFLYVGRLKFEGQKNV-KELFDGLSQTTGE-WQLHIIGDGSDFEKCKAYSRelgiEQRIIWHGwqSQPWEVVQQKI 255
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1344404431 323 ASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLIH-GVNGWL 371
Cdd:PRK09922 256 KNVSALLLTSKFEGFPMTLLEAMSYGIPCISSDCMSGPRDIIKpGLNGEL 305
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
227-309 |
1.42e-04 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 43.81 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 227 VDTTRFSP--KHRSESLRQQWGVDSDTRVMLYVGRLSPEKEVQLIVESYAAMQNiqqqKTKL--VVVGDGPDLARLKALP 302
Cdd:PRK10307 203 SEVARFQPvaDADVDALRAQLGLPDGKKIVLYSGNIGEKQGLELVIDAARRLRD----RPDLifVICGQGGGKARLEKMA 278
|
90
....*....|
gi 1344404431 303 EAK---NVIF 309
Cdd:PRK10307 279 QCRglpNVHF 288
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
231-351 |
1.47e-04 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 43.93 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 231 RFSPKHRS------ESLRQQWGVDSDTRVML--YVGRLSPEKEVQLIVEsyaAMQNIQQQKTKLVVVGDG-PDL-ARLKA 300
Cdd:COG0297 267 NYSADDLEgkaankAALQEELGLPVDPDAPLigMVSRLTEQKGLDLLLE---ALDELLEEDVQLVVLGSGdPEYeEAFRE 343
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1344404431 301 LPEA--KNVIFTgslRGHDLAVA---YASADVFVFASQVETFGNVVLEAMASG-LPV 351
Cdd:COG0297 344 LAARypGRVAVY---IGYDEALAhriYAGADFFLMPSRFEPCGLNQMYALRYGtVPI 397
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
248-371 |
3.41e-04 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 42.76 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344404431 248 DSDTR---VMLYVGRLSPEKEVqliveSYAAMQNIQQQKTKLVVVGDGPDLA----RLKALPEAKNVIFTGSLRghDLAV 320
Cdd:PRK15490 396 DADTTiggVFRFVGDKNPFAWI-----DFAARYLQHHPATRFVLVGDGDLRAeaqkRAEQLGILERILFVGASR--DVGY 468
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1344404431 321 AYASADVFVFASQVETFGNVVLEAMASGLPVIAYDYACAHQYLIHGVNGWL 371
Cdd:PRK15490 469 WLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGSAECFIEGVSGFI 519
|
|
| |
