|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
33-432 |
0e+00 |
|
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: 734.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 33 SICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVIIVTHAYGNRKGIRYLANGLKVYYLPLKVMYNQSTATTLFHSLPLL 112
Cdd:cd03796 1 RICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVITHAYGNRVGVRYLTNGLKVYYLPFKVFYNQSTLPTLFSTFPLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 113 RYIFVRERVTIVHSHSSFSSMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNHIICVSYTSKENTV 192
Cdd:cd03796 81 RNILIRERIQIVHGHQAFSSLAHEALFHARTLGLKTVFTDHSLFGFADASSILTNKLLRFSLADIDHVICVSHTSKENTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 193 LRAALNPEIVSVIPNAVDPTDFTPDPSRRDDSMITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGEGPKRIVLE 272
Cdd:cd03796 161 LRASLDPRIVSVIPNAVDSSDFTPDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 273 EVRERYQLHDRVRLLGALEHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSV 352
Cdd:cd03796 241 EMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 353 KSLCDGLEKAVAQIRSGTlPTPETIHNKVKTFYTWRNVAERTEKVYDRVADEVVLPMDKRLdRLISHCGSVTGCIFALFA 432
Cdd:cd03796 321 EDIVRKLEEAISILRTGK-HDPWSFHNRVKKMYSWEDVARRTEKVYDRILSTPNRPFLERL-KRYYNCGPIAGKIFCLLA 398
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
34-398 |
2.54e-59 |
|
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: 199.30 E-value: 2.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 34 ICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVIIVTHAYGNRKGIRYLANGLKVYYLPLKVMYnqstatTLFHSLPLLR 113
Cdd:cd03801 2 ILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALL------RARRLLRELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 114 YIFVRERVTIVHSHSSFSsmAHDALFHAKTMGLQTVFTDHSLFGF------ADVSSVLTNKLLTVSLCDtnHIICVSYTS 187
Cdd:cd03801 76 PLLRLRKFDVVHAHGLLA--ALLAALLALLLGAPLVVTLHGAEPGrlllllAAERRLLARAEALLRRAD--AVIAVSEAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 188 KENTVLRAALNPEIVSVIPNAVDPTDFTPDPSRRDDSM---ITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHF-LVGG 263
Cdd:cd03801 152 RDELRALGGIPPEKIVVIPNGVDLERFSPPLRRKLGIPpdrPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLvIVGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 264 EGPKRIVLEEvrERYQLHDRVRLLGALEHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLP-- 341
Cdd:cd03801 232 DGPLRAELEE--LELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEdg 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985329438 342 ENLIILCEPSVKSLCDGLEKAVAQirsgtlptPETI-------HNKVKTFYTWRNVAERTEKVY 398
Cdd:cd03801 310 EGGLVVPPDDVEALADALLRLLAD--------PELRarlgraaRERVAERFSWERVAERLLDLY 365
|
|
| PIGA |
pfam08288 |
PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol ... |
71-160 |
2.34e-51 |
|
PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol n-acetylglucosaminyltransferase proteins. These proteins are involved in GPI anchor biosynthesis and are associated with disease the paroxysmal nocturnal haemoglobinuria.
Pssm-ID: 400541 Cd Length: 90 Bit Score: 168.97 E-value: 2.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 71 HAYGNRKGIRYLANGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRERVTIVHSHSSFSSMAHDALFHAKTMGLQTVF 150
Cdd:pfam08288 1 HAYGDRTGVRYLTNGLKVYYVPFLVIYRQSTFPTVFGTFPLFRNILLRERIDIVHGHGSFSTLAHEAILHARTMGLKTVF 80
|
90
....*....|
gi 1985329438 151 TDHSLFGFAD 160
Cdd:pfam08288 81 TDHSLFGFAD 90
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
34-350 |
1.31e-41 |
|
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: 151.74 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 34 ICMVSDFFYpnMGGVESHIYQLSQCLIERGHKVIIVTHayGNRKGIRYLANGLKVyylplkvMYNQSTATTLFHSLPLLR 113
Cdd:cd03819 1 ILMLTPALE--IGGAETYILDLARALAERGHRVLVVTA--GGPLLPRLRQIGIGL-------PGLKVPLLRALLGNVRLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 114 YIFVRERVTIVHSHSSFSSMAhdALFHAKTMGLQTVFTDHSLfgfaDVSSVLTNKLLTVSLCDTNHIICVSYTSKENTVL 193
Cdd:cd03819 70 RLIRRERIDLIHAHSRAPAWL--GWLASRLTGVPLVTTVHGS----YLATYHPKDFALAVRARGDRVIAVSELVRDHLIE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 194 RAALNPEIVSVIPNAVDPTDFTPDPSRR-------DDSMITVVVVSRLVYRKGIDLLSGIIPELcQKYPDLHFLVGGEGP 266
Cdd:cd03819 144 ALGVDPERIRVIPNGVDTDRFPPEAEAEeraqlglPEGKPVVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAGDGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 267 KRIVLEEVRERYQLHDRVRLLGALEhqDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLII 346
Cdd:cd03819 223 ERDEIRRLVERLGLRDRVTFTGFRE--DVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTG 300
|
....
gi 1985329438 347 LCEP 350
Cdd:cd03819 301 LLVP 304
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
44-364 |
9.70e-38 |
|
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: 141.69 E-value: 9.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 44 NMGGVESHIYQL--SQCLIERGHKVIIVTH--AYGNRkgirYLANGLKVYYLPLKVMYnqstattLFHSLPLLRYIFVRE 119
Cdd:cd03807 10 NVGGAETMLLRLleHMDKSRFEHVVISLTGdgVLGEE----LLAAGVPVVCLGLSSGK-------DPGVLLRLAKLIRKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 120 RVTIVHSHssfssMAHDALFHAKTMGLQ----TVFTDHSLFGFADVSSVL--TNKLLTVSLCDTnhiICVSYTSKEnTVL 193
Cdd:cd03807 79 NPDVVHTW-----MYHADLIGGLAAKLAggvkVIWSVRSSNIPQRLTRLVrkLCLLLSKFSPAT---VANSSAVAE-FHQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 194 RAALNPEIVSVIPNAVDPTDFTPDPSRR---------DDSMITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGE 264
Cdd:cd03807 150 EQGYAKNKIVVIYNGIDLFKLSPDDASRararrrlglAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 265 GPKRIVLEEVRERYQLHDRVRLLGalEHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENL 344
Cdd:cd03807 230 GPERPNLERLLLELGLEDRVHLLG--ERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDGT 307
|
330 340
....*....|....*....|.
gi 1985329438 345 IILCEP-SVKSLCDGLEKAVA 364
Cdd:cd03807 308 GFLVPAgDPQALADAIRALLE 328
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
40-401 |
6.63e-36 |
|
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: 136.74 E-value: 6.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 40 FFYPN--MGGVESHIYQLSQCLIERGHKVIIVTHAYGNRKGIRYLANGLKVYYLPLKVMYNQSTATTLFHSLPL------ 111
Cdd:cd03798 6 NIYPNanSPGRGIFVRRQVRALSRRGVDVEVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLrapsla 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 112 -LRYIFVRERVTIVHSHSSFSSMAHDALFHAKTmGLQTVFTDHS--LFGFADVSSVLTNKLLTVSLCDtnhiiCVSYTSK 188
Cdd:cd03798 86 kLLKRRRRGPPDLIHAHFAYPAGFAAALLARLY-GVPYVVTEHGsdINVFPPRSLLRKLLRWALRRAA-----RVIAVSK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 189 E--NTVLRAALNPEIVSVIPNAVDPTDFTPDPSRRD--DSMITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGE 264
Cdd:cd03798 160 AlaEELVALGVPRDRVDVIPNGVDPARFQPEDRGLGlpLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 265 GPKRIVLEEVRERYQLHDRVRLLGALEHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVL-PEN 343
Cdd:cd03798 240 GPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVgDPE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1985329438 344 LIILCEP-SVKSLCDGLEKAVAQIRSGTLptPETIHNKVKTFYTWRNVAERTEKVYDRV 401
Cdd:cd03798 320 TGLLVPPgDADALAAALRRALAEPYLREL--GEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
34-401 |
3.75e-35 |
|
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: 134.71 E-value: 3.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 34 ICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVIIVT----HAYGNRKGIRYLANGLkvyylPLKVMYNQSTATTLFHSL 109
Cdd:cd03817 2 IAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITpsdpGAEDEEEVVRYRSFSI-----PIRKYHRQHIPFPFKKAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 110 PLlryIFVRERVTIVHSHSSFSSMAHdALFHAKTMGLQTVFTDHSL---------FGFADVSSVLtnKLLTVSLCD-TNH 179
Cdd:cd03817 77 ID---RIKELGPDIIHTHTPFSLGKL-GLRIARKLKIPIVHTYHTMyedylhyipKGKLLVKAVV--RKLVRRFYNhTDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 180 IICVSYTSKEntVLRAALNPEIVSVIPNAVDPTDFTPDPSR--------RDDSMItVVVVSRLVYRKGIDLLSGIIPELC 251
Cdd:cd03817 151 VIAPSEKIKD--TLREYGVKGPIEVIPNGIDLDKFEKPLNTeerrklglPPDEPI-LLYVGRLAKEKNIDFLLRAFAELK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 252 QKyPDLHFLVGGEGPKRIVLEEVRERYQLHDRVRLLGALEHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVST 331
Cdd:cd03817 228 KE-PNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAA 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985329438 332 RVGGIPEVLpENLI--ILCEPSVkslcDGLEKAVAQIRSGTLPTPETIHNKVKTFYTWRnVAERTEKVYDRV 401
Cdd:cd03817 307 KDPAASELV-EDGEngFLFEPND----ETLAEKLLHLRENLELLRKLSKNAEISAREFA-FAKSVEKLYEEV 372
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
40-366 |
4.58e-35 |
|
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.
Pssm-ID: 340839 [Multi-domain] Cd Length: 351 Bit Score: 134.02 E-value: 4.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 40 FFYPNM--GGVESHIYQLSQCLIERGHKVIIVTHAYGNRKGIrYLANGLKVYYLPLKVMYNQSTAttLFHSLPLLRYIFV 117
Cdd:cd03811 4 FVIPSLsgGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDK-QLNGDVKLIRLLIRVLKLIKLG--LLKAILKLKRILK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 118 RERVTIVHSHSSFSSmahDALFHAKTMGLQTVFTDHSlfgFADVSSVLTNKLLTVSLC--DTNHIICVSYTSKENTVLRA 195
Cdd:cd03811 81 RAKPDVVISFLGFAT---YIVAKLAAARSKVIAWIHS---SLSKLYYLKKKLLLKLKLykKADKIVCVSKGIKEDLIRLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 196 ALNPEIVSVIPNAVDPTDFTPDPSRRDDSM----ITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGEGPKRIVL 271
Cdd:cd03811 155 PSPPEKIEVIYNPIDIDRIRALAKEPILNEpedgPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 272 EEVRERYQLHDRVRLLGalEHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENL-IILCEP 350
Cdd:cd03811 235 EKLAKELGLAERVIFLG--FQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGEnGLLVPD 312
|
330
....*....|....*.
gi 1985329438 351 SVKSLCDGLEKAVAQI 366
Cdd:cd03811 313 GDAAALAGILAALLQK 328
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
44-361 |
3.08e-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: 126.17 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 44 NMGGVESHIYQLSQCLIERGHKVIIVTHayGNRKGIRYL-ANGLKVYYLPLKV-----MYNqstattlFHSLPLLRYIFV 117
Cdd:cd03808 8 VDGGFQSFRLPLIKALVKKGYEVHVIAP--DGDKLSDELkELGVKVIDIPILRrginpLKD-------LKALFKLYKLLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 118 RERVTIVHSHSSFSSM-AHDALFHAKTMglQTVFTDHSLfGFADVSSVLTNKLLTV----SLCDTNHIICVSYTSKENTV 192
Cdd:cd03808 79 KEKPDIVHCHTPKPGIlGRLAARLAGVP--KVIYTVHGL-GFVFTEGKLLRLLYLLleklALLFTDKVIFVNEDDRDLAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 193 -LRAALNPEIVSVIPNAVDPTDFTPDPSRRDDSMITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGEGPKRIVL 271
Cdd:cd03808 156 kKGIIKKKKTVLIPGSGVDLDRFQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 272 EEVRERYQLHDRVRLLGalEHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPE-VLPENLIILCEP 350
Cdd:cd03808 236 EILIEKLGLEGRIEFLG--FRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRElVIDGVNGFLVPP 313
|
330
....*....|..
gi 1985329438 351 -SVKSLCDGLEK 361
Cdd:cd03808 314 gDVEALADAIEK 325
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
44-330 |
1.68e-28 |
|
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: 115.80 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 44 NMGGVESHIYQLSQCLIERGHKVIIVTHAYGNRKGIRYLANGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRER--V 121
Cdd:cd03820 11 NAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYELDDNIKIKNLGDRKYSHFKLLLKYFKKVRRLRKYLKNNKpdV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 122 TIVHSHSSFSSMAhdalfhAKTMGLQTVFTDHSLFGFA-DVSSVLTNKLLTVSLCDTnhIICVSYTSKENTvlRAALNPE 200
Cdd:cd03820 91 VISFRTSLLTFLA------LIGLKSKLIVWEHNNYEAYnKGLRRLLLRRLLYKRADK--IVVLTEADKLKK--YKQPNSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 201 IVsVIPNAVDPTDFTP--DPSRRddsmiTVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGEGPKRIVLEEVRERY 278
Cdd:cd03820 161 VV-VIPNPLSFPSEEPstNLKSK-----RILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1985329438 279 QLHDRVRLLGALehQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVS 330
Cdd:cd03820 235 GLEDRVKLLGPT--KNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIIS 284
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
37-398 |
4.16e-27 |
|
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: 111.65 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 37 VSDFFYPN-MGGVESHIYQLSQCLIERGHKVIIVT--------HAYGNRKGIRYLANGLKVYYLPLKVMYNQSTaTTLFH 107
Cdd:cd03823 5 VNSLYPPQrVGGAEISVHDLAEALVAEGHEVAVLTagvgppgqATVARSVVRYRRAPDETLPLALKRRGYELFE-TYNPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 108 SLPLLRYIFVRERVTIVHSHSsFSSMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVslcdtnhiICVS-YT 186
Cdd:cd03823 84 LRRLLARLLEDFRPDVVHTHN-LSGLGASLLDAARDLGIPVVHTLHDYWLLCPRQFLFKKGGDAV--------LAPSrFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 187 skENTVLRAALNPEIVSVIPNAVDPTDFTPDPSRRDDSMITVVVVSRLVYRKGIDLLSGIIPELcqKYPDLHFLVGGEGP 266
Cdd:cd03823 155 --ANLHEANGLFSARISVIPNAVEPDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRL--PREDIELVIAGHGP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 267 krivlEEVRERYQLHDRVRLLGALEHQDVRNVLVQGHIFLNTSL-TEAFCMAIVEAASCGLQVVSTRVGGIPE-VLPENL 344
Cdd:cd03823 231 -----LSDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAElIQPGVN 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1985329438 345 IILCEPSVKslcDGLEKAVAQ-IRSGTLPTPETIHNKVKTFYTWRnvAERTEKVY 398
Cdd:cd03823 306 GLLFAPGDA---EDLAAAMRRlLTDPALLERLRAGAEPPRSTESQ--AEEYLKLY 355
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
46-395 |
4.84e-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: 109.64 E-value: 4.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 46 GGVESHIYQLSQCLIERGHKVIIVTHAYGNRKG-IRYLANGLKVYYLPL----KVMYNQstattLFHSLP-----LLRYI 115
Cdd:cd03800 21 GGQNVYVLELARALAELGYQVDIFTRRISPADPeVVEIAPGARVIRVPAgppeYLPKEE-----LWPYLEefadgLLRFI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 116 FVRE-RVTIVHSHSSFSSMAhdALFHAKTMGLQTVFTDHSL-------FGFADVSSV---LTNKLLTVSLCDTnhIICVS 184
Cdd:cd03800 96 AREGgRYDLIHSHYWDSGLV--GALLARRLGVPLVHTFHSLgrvkyrhLGAQDTYHPslrITAEEQILEAADR--VIAST 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 185 YTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPSRRDDSMI--------TVVVVSRLVYRKGIDLL---SGIIPELCQK 253
Cdd:cd03800 172 PQEADELISLYGADPSRINVVPPGVDLERFFPVDRAEARRARlllppdkpVVLALGRLDPRKGIDTLvraFAQLPELREL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 254 yPDLHFLVGGEGPK----RIVLEEVRERYQLHDRVRLLGALEHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVV 329
Cdd:cd03800 252 -ANLVLVGGPSDDPlsmdREELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVV 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985329438 330 STRVGGIPE-VLPENLIILCEP-SVKSLCDGLEKAVAQ-IRSGTLptPETIHNKVKTFYTWRNVAERTE 395
Cdd:cd03800 331 ATAVGGLQDiVRDGRTGLLVDPhDPEALAAALRRLLDDpALWQRL--SRAGLERARAHYTWESVADQLL 397
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
227-361 |
8.15e-25 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 99.51 E-value: 8.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 227 TVVVVSRLV-YRKGIDLLSGIIPELCQKYPDLHFLVGGEGPKRIVLEEVREryqLHDRVRLLGALEhqDVRNVLVQGHIF 305
Cdd:pfam13692 3 VILFVGRLHpNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEELAAG---LEDRVIFTGFVE--DLAELLAAADVF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1985329438 306 LNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEP-SVKSLCDGLEK 361
Cdd:pfam13692 78 VLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENGLLVPPgDPEALAEAILR 134
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
226-362 |
2.60e-24 |
|
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: 98.89 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 226 ITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGEGPKRIVLEEVRERYQLHDRVRLLGALEHQDVRNVLVQGHIF 305
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVF 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1985329438 306 LNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLI-ILCEP-SVKSLCDGLEKA 362
Cdd:pfam00534 83 VLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETgFLVKPnNAEALAEAIDKL 141
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
34-343 |
8.27e-24 |
|
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: 99.79 E-value: 8.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 34 ICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVIIVThaygnRKGIRYLAnglkvyylplkvmynqstattlfhslplLR 113
Cdd:cd01635 1 ILLVTGEYPPLRGGLELHVRALARALAALGHEVTVLA-----LLLLALRR----------------------------IL 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 114 YIFVRERVTIVHSHSSFSSMAHdALFHAKTMGLQTVFTDHSLFGFAdvssvltnklltvslcdtnhiicvsytskentvl 193
Cdd:cd01635 48 KKLLELKPDVVHAHSPHAAALA-ALLAARLLGIPIVVTVHGPDSLE---------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 194 raalnpeivsvipnAVDPTDFTPDPSRRDDSMITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGEGPKRIVLEE 273
Cdd:cd01635 93 --------------STRSELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEA 158
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985329438 274 VRERYQLHDRVRLLGALEHQDVRNVLVQG-HIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPEN 343
Cdd:cd01635 159 LAAALGLLERVVIIGGLVDDEVLELLLAAaDVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDG 229
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
33-395 |
4.82e-23 |
|
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: 100.49 E-value: 4.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 33 SICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVIIVTHAYGNRKGIRYLA-----NGLKVYYLPLKVMYNQSTATTLFH 107
Cdd:cd03794 1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGatetkDGIRVIRVKLGPIKKNGLIRRLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 108 ----SLPLLRYIFVRER---VTIVHSHSSFSSMAhdALFHAKTMGLQTVFTDHSLFGFADVS-SVLTNKLL--------- 170
Cdd:cd03794 81 ylsfALAALLKLLVREErpdVIIAYSPPITLGLA--ALLLKKLRGAPFILDVRDLWPESLIAlGVLKKGSLlkllkkler 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 171 -TVSLCDtnHIICVSYTSKENtVLRAALNPEIVSVIPNAVDPTDFTPDPSRRDDSMITVVVVSRLVY------RKGIDLL 243
Cdd:cd03794 159 kLYRLAD--AIIVLSPGLKEY-LLRKGVPKEKIIVIPNWADLEEFKPPPKDELRKKLGLDDKFVVVYagnigkAQGLETL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 244 SGIIPELcQKYPDLHFLVGGEGPKRIVLEEVRERYQLhDRVRLLGALEHQDVRNVLVQGHIFLNTSLTEAFCMAIV---- 319
Cdd:cd03794 236 LEAAERL-KRRPDIRFLFVGDGDEKERLKELAKARGL-DNVTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGSSpskl 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 320 -EAASCGLQVVSTRVGGIPE-VLPENLIILCEP-SVKSLCDGLEKAVAQirsgtlptPETIHNK-------VKTFYTWRN 389
Cdd:cd03794 314 fEYMAAGKPILASDDGGSDLaVEINGCGLVVEPgDPEALADAILELLDD--------PELRRAMgengrelAEEKFSREK 385
|
....*.
gi 1985329438 390 VAERTE 395
Cdd:cd03794 386 LADRLL 391
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
34-396 |
2.21e-22 |
|
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: 98.20 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 34 ICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVIIVTHAYGNRKGIRYLANGLKVYYLPLKVMYNQSTATTLFhslpLLR 113
Cdd:cd03809 2 ILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRW----LQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 114 YIFVRERVTIVHSHSSFSSMahdalfhaKTMGLQTVFTDHSLF------GFADVSSVLTNKLLTVSLCDTNHIICVSYTS 187
Cdd:cd03809 78 LLPKKDKPDLLHSPHNTAPL--------LLKGCPQVVTIHDLIplrypeFFPKRFRLYYRLLLPISLRRADAIITVSEAT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 188 KENTVLRAALNPEIVSVIPNAVDPTDFTPDPSRRDDSMI-----TVVVVSRLVYRKGIDLLSGIIPELCQKYPDLH-FLV 261
Cdd:cd03809 150 RDDIIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYllpepYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKlVIV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 262 GGEGPKRIVLEEVRERYQLHDRVRLLGALEHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLP 341
Cdd:cd03809 230 GGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAG 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1985329438 342 ENlIILCEP-SVKSLCDGLEKAV--AQIRSGtlpTPETIHNKVKTFyTWRNVAERTEK 396
Cdd:cd03809 310 DA-ALYFDPlDPESIADAILRLLedPSLREE---LIRKGLERAKKF-SWEKTAEKTLE 362
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
34-395 |
7.05e-22 |
|
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: 97.05 E-value: 7.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 34 ICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVIIVTHA--YGNRKGIRYLANGLKVYYLPLKVMYNQS---TATTLFHS 108
Cdd:cd03821 2 ILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGdgYESLVVEENGRYIPPQDGFASIPLLRQGagrTDFSPGLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 109 LPLLRYIfvrERVTIVHSHSSFSSMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNHI---ICVSY 185
Cdd:cd03821 82 NWLRRNL---REYDVVHIHGVWTYTSLAACKLARRRGIPYVVSPHGMLDPWALQQKHWKKRIALHLIERRNLnnaALVHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 186 TS-KENTVLRAALNPEIVSVIPNAVDPTDFTPDPSRRDDSMIT-----VVVVSRLVYRKGIDLLSGIIPELCQKYPDLHF 259
Cdd:cd03821 159 TSeQEADELRRFGLEPPIAVIPNGVDIPEFDPGLRDRRKHNGLedrriILFLGRIHPKKGLDLLIRAARKLAEQGRDWHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 260 LVGGEGPKrivLEEVRERYQ----LHDRVRLLGALEHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGG 335
Cdd:cd03821 239 VIAGPDDG---AYPAFLQLQsslgLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985329438 336 IPEVLPENLIILCEPSVKSLCDGL---------EKAVAQIRSGTLPTPETihnkvktfYTWRNVAERTE 395
Cdd:cd03821 316 LSELVEAGCGVVVDPNVSSLAEALaealrdpadRKRLGEMARRARQVEEN--------FSWEAVAGQLG 376
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
180-338 |
7.44e-21 |
|
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: 93.67 E-value: 7.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 180 IICVSYTSKENtVLRAALNPEIVSVIPNAVDPTDFTPDPSRRDDSmiTVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHF 259
Cdd:cd05844 147 FVAVSGFIRDR-LLARGLPAERIHVHYIGIDPAKFAPRDPAERAP--TILFVGRLVEKKGCDVLIEAFRRLAARHPTARL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 260 LVGGEGPKRIVLEEVRERYqlhDRVRLLGALEHQDVRNVLVQGHIFLNTSLT------EAFCMAIVEAASCGLQVVSTRV 333
Cdd:cd05844 224 VIAGDGPLRPALQALAAAL---GRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRH 300
|
....*
gi 1985329438 334 GGIPE 338
Cdd:cd05844 301 GGIPE 305
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
34-342 |
5.78e-20 |
|
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: 91.20 E-value: 5.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 34 ICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVIIVT----HAYGNRKGIRYLANGLKV-----YYLPLKVMynqstatt 104
Cdd:cd03814 2 IALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVApgpfDEAESAEGRVVSVPSFPLpfypeYRLALPLP-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 105 lfhslPLLRYIFVRERVTIVHSHSSFSsMAHDALFHAKTMGLQTVFTDHSLF-------GFADVSSVLTNKLLTVS-LCD 176
Cdd:cd03814 74 -----RRVRRLIKEFQPDIIHIATPGP-LGLAALRAARRLGLPVVTSYHTDFpeylsyyTLGPLSWLAWAYLRWFHnPFD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 177 TnhIICVSYTSKEntvLRAALNPEIVSVIPNAVDPTDFtpDPSRRDDSM---------ITVVVVSRLVYRKGIDLLSGII 247
Cdd:cd03814 148 T--TLVPSPSIAR---ELEGHGFERVRLWPRGVDTELF--HPSRRDAALrrrlgppgrPLLLYVGRLAPEKNLEALLDAD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 248 PELCQKYPdLHFLVGGEGPKRivlEEVRERYqlhDRVRLLGALEHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQ 327
Cdd:cd03814 221 LPLAASPP-VRLVVVGDGPAR---AELEARG---PDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLP 293
|
330
....*....|....*
gi 1985329438 328 VVSTRVGGIPEVLPE 342
Cdd:cd03814 294 VVAADAGGPRDIVRP 308
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
46-211 |
1.17e-19 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 86.05 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 46 GGVESHIYQLSQCLIERGHKVIIVTHAYGNRKGIRYLAnglkVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRERVTIVH 125
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVR----VVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 126 SHSSFSSMAhDALFHAKTMGLQTVFTDHSLF-------GFADVSSVLTNKLLTVSLCDTNHIICVSYTSKENTVLRAALN 198
Cdd:pfam13439 77 AHSPFPLGL-AALAARLRLGIPLVVTYHGLFpdykrlgARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVP 155
|
170
....*....|...
gi 1985329438 199 PEIVSVIPNAVDP 211
Cdd:pfam13439 156 PEKIRVIPNGVDL 168
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
33-335 |
1.60e-18 |
|
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: 86.94 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 33 SICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVIIVThaYGNRKGIR-YLANGLKVYYLPLKVMYNqstATTLFHSLPl 111
Cdd:cd03795 1 KVLHVFKFYYPDIGGIEQVIYDLAEGLKKKGIEVDVLC--FSKEKETPeKEENGIRIHRVKSFLNVA---STPFSPSYI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 112 LRYIFVRERVTIVHSHSSFSSMahDALFHAKTMGLQTVFTDHslfgfadvSSVLTNK--------LLTVSLCDTNHIICV 183
Cdd:cd03795 75 KRFKKLAKEYDIIHYHFPNPLA--DLLLFFSGAKKPVVVHWH--------SDIVKQKkllklykpLMTRFLRRADRIIAT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 184 SYTSKENT-VLRAALNPeiVSVIPNAVDPTDFTPD------PSRRDDSMITVVVVSRLVYRKGIDLLsgIIPELCQKYPd 256
Cdd:cd03795 145 SPNYVETSpTLREFKNK--VRVIPLGIDKNVYNIPrvdfenIKREKKGKKIFLFIGRLVYYKGLDYL--IEAAQYLNYP- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 257 lhFLVGGEGPKRIVLEEVRErYQLHDRVRLLGALEHQDVRNVLVQGHIFLNTSL--TEAFCMAIVEAASCGLQVVSTRVG 334
Cdd:cd03795 220 --IVIGGEGPLKPDLEAQIE-LNLLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVISTNIG 296
|
.
gi 1985329438 335 G 335
Cdd:cd03795 297 T 297
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
48-344 |
3.98e-18 |
|
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: 85.58 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 48 VESHIYQLSQC--LIERGHKVIIVThaygnrkgiryLANGLKVYYLPLKVMYNQSTATTLFHSLPLLRyifvRERVTIVH 125
Cdd:cd03799 11 VLSETFILNQItgLIDRGHEVDIYA-----------VNPGDLVKRHPDVEKYNVPSLNLLYAIVGLNK----KGAYDIIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 126 SHSSFSSMAHDALFHAKTMGLQTVFTDHSlfgfADVSSVLTNKLLTV--SLCDTNHI---ICVSYTSKentVLRAALNPE 200
Cdd:cd03799 76 CQFGPLGALGALLRRLKVLKGKLVTSFRG----YDISMYVILEGNKVypQLFAQGDLflpNCELFKHR---LIALGCDEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 201 IVSVIPNAVDPTDFTPDPsRRD--DSMITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGEGPKRIVLEEVRERY 278
Cdd:cd03799 149 KIIVHRSGIDCNKFRFKP-RYLplDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQEL 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985329438 279 QLHDRVRLLGALEHQDVRNVLVQGHIFLNTSLT------EAFCMAIVEAASCGLQVVSTRVGGIPEVLPENL 344
Cdd:cd03799 228 NIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTaadgdqDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGV 299
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
45-346 |
4.23e-18 |
|
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: 85.57 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 45 MGGVESHIYQLSQCLIERGHKVIIVtHAYGNRKgIRYLANGLKVYYLPLKvmynqSTATTLFHSLPLLRYIFVRERVTIV 124
Cdd:cd04951 11 LGGAEKQTVLLADQMFIRGHDVNIV-YLTGEVE-VKPLNNNIIIYNLGMD-----KNPRSLLKALLKLKKIISAFKPDVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 125 HSHssfssMAHDALF------HAKTMGLqtVFTDHSlfgfADVSSVLTNKL--LTVSLCD--TNhiicVSYTSKENTVLR 194
Cdd:cd04951 84 HSH-----MFHANIFarflrmLYPIPLL--ICTAHN----KNEGGRIRMFIyrLTDFLCDitTN----VSREALDEFIAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 195 AALNPEIVSVIPNAVDPTDFTPDPSRRD---------DSMITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGEG 265
Cdd:cd04951 149 KAFSKNKSVPVYNGIDLNKFKKDINVRLkirnklnlkNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 266 PKRIVLEEVRERYQLHDRVRLLGAleHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVL-PENL 344
Cdd:cd04951 229 PLRNELERLICNLNLVDRVILLGQ--ISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVgDHNY 306
|
..
gi 1985329438 345 II 346
Cdd:cd04951 307 VV 308
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
46-401 |
1.28e-17 |
|
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.
Pssm-ID: 340832 [Multi-domain] Cd Length: 333 Bit Score: 83.88 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 46 GGVESHIYQLSQCLIERGHKVIIVthAYGNRKGiryLANGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIfVRERVTIVH 125
Cdd:cd03802 18 GGTELVVSALTEGLVRRGHEVTLF--APGDSHT---SAPLVAVIPRALRLDPIPQESKLAELLEALEVQL-RASDFDVIH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 126 SHSSFSsmahdALFHAKTMGLQTVFTDHslfGFADVSSvltnkLLTVSLCDTNHIICVSYTSkentvlRAALNP-EIVSV 204
Cdd:cd03802 92 NHSYDW-----LPPFAPLIGTPFVTTLH---GPSIPPS-----LAIYAAEPPVNYVSISDAQ------RAATPPiDYLTV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 205 IPNAVDPTDFTPDPSRRDDsmitVVVVSRLVYRKGIDLlsGIipELCQKyPDLHFLVGGEGPKRIVLEEVRERYqLHDRV 284
Cdd:cd03802 153 VHNGLDPADYRFQPDPEDY----LAFLGRIAPEKGLED--AI--RVARR-AGLPLKIAGKVRDEDYFYYLQEPL-PGPRI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 285 RLLGALEHQDVRNVLVQGHIFLNTSL-TEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENliilcepSVKSLCDGLEKAV 363
Cdd:cd03802 223 EFIGEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHG-------ETGFLVDSVEEMA 295
|
330 340 350
....*....|....*....|....*....|....*....
gi 1985329438 364 AQIRS-GTLPtPETIHNKVKTFYTWRNVAERTEKVYDRV 401
Cdd:cd03802 296 EAIANiDRID-RAACRRYAEDRFSAARMADRYEALYRKV 333
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
42-343 |
2.42e-17 |
|
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: 83.56 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 42 YPNMGGVESHIYQLSQCLIERGHKVIIVTHAYGNRKgIRYLANglkVYYLPLKVMyNQSTATTLFHSLPL---LRYIFVR 118
Cdd:cd04962 8 YPSYGGSGVVATELGLELAERGHEVHFISSAIPFRL-NLYSGN---IFFHEVEVP-NYPLFEYPPYTLALaskIVEVAKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 119 ERVTIVHSHSSfssMAHD-ALFHAKTM---GLQTVFTDHSlfgfADVSSVLTNK----LLTVSLCDTNHIICVSYTSKEN 190
Cdd:cd04962 83 HKLDVLHAHYA---IPHAsCAYLAREIlgeKIPIVTTLHG----TDITLVGYDPslqpAVRFSINKSDRVTAVSSSLRQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 191 TVLRAALNPEIvSVIPNAVDPTDFTPDPSRRDDS--MIT-----VVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGg 263
Cdd:cd04962 156 TYELFDVDKDI-EVIHNFIDEDVFKRKPAGALKRrlLAPpdekvVIHVSNFRPVKRIDDVVRVFARVRRKIPAKLLLVG- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 264 EGPKRIVLEEVRERYQLHDRVRLLGALEHqdVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPEN 343
Cdd:cd04962 234 DGPERVPAEELARELGVEDRVLFLGKQDD--VEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHG 311
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
44-329 |
1.58e-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: 74.63 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 44 NMGGVESHIYQLSQCLIERGHKVIIVthAYGNRKGIRY---LANGLKVYYLPLKVMYNqstattLFHSLPLLRYIFVrER 120
Cdd:cd03812 10 NVGGIETFLMNLYRKLDKSKIEFDFL--ATSDDKGEYDeelEELGGKIFYIPPKKKNI------IKYFIKLLKLIKK-EK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 121 VTIVHSHSSFSSMAhdALFHAKTMGLQT-VFTDH-----SLFGFADVSSVLTNKLLTVSlcdTNHIICvsyTSKENTVLR 194
Cdd:cd03812 81 YDIVHVHGSSSNGI--ILLLAAKAGVPVrIAHSHntkdsSIKLRKIRKNVLKKLIERLS---TKYLAC---SEDAGEWLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 195 AALNPEIVSVIPNAVDPTDFTPDPSRRD--------DSMITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGEGP 266
Cdd:cd03812 153 GEVENGKFKVIPNGIDIEKYKFNKEKRRkrrkllilEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985329438 267 KRIVLEE-VRERyQLHDRVRLLGALEhqDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVV 329
Cdd:cd03812 233 LKEKIKEkVKEL-GLEDKVIFLGFRN--DVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCL 293
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
303-401 |
5.82e-14 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 68.48 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 303 HIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLI-ILCEP-SVKSLCDGLEKAVAQiRSGTLPTPETIHNK 380
Cdd:COG0438 22 DVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETgLLVPPgDPEALAEAILRLLED-PELRRRLGEAARER 100
|
90 100
....*....|....*....|.
gi 1985329438 381 VKTFYTWRNVAERTEKVYDRV 401
Cdd:COG0438 101 AEERFSWEAIAERLLALYEEL 121
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
199-340 |
2.27e-12 |
|
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: 68.90 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 199 PEIVSVIPNAVDPTDFTPDPSRRDDSM-ITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHF-LVGGEGPKRIVLEEVRE 276
Cdd:cd03813 266 PDKTRVIPNGIDIQRFAPAREERPEKEpPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGwLIGPEDEDPEYAQECKR 345
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985329438 277 RYQ---LHDRVRLLGaleHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVL 340
Cdd:cd03813 346 LVAslgLENKVKFLG---FQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELI 409
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
186-333 |
1.41e-10 |
|
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: 62.32 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 186 TSKENTVLRAALNPEI-VSVIPNAVDPTDFTP--DPSRRDDSMITVvvvSRLVYRKGIDLLSGIIPELCQKYPDLHFLVG 262
Cdd:cd04949 121 TEQQKQDLSERFNKYPpIFTIPVGYVDQLDTAesNHERKSNKIITI---SRLAPEKQLDHLIEAVAKAVKKVPEITLDIY 197
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985329438 263 GEGPKRIVLEEVRERYQLHDRVRLLGAleHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRV 333
Cdd:cd04949 198 GYGEEREKLKKLIEELHLEDNVFLKGY--HSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDV 266
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
223-361 |
2.00e-09 |
|
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: 59.40 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 223 DSMITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFL---VGGeGPKRIVLEEVRERYQLHDRVRLLGALEHQDVRNVL 299
Cdd:cd04946 222 EGDLRLVSCSSIVPVKRIDLIIETLNSLCVAHPSICISwthIGG-GPLKERLEKLAENKLENVKVNFTGEVSNKEVKQLY 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985329438 300 VQG--HIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLpEN----LIILCEPSVKSLCDGLEK 361
Cdd:cd04946 301 KENdvDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIV-ENetngLLLDKDPTPNEIVSSIMK 367
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
202-365 |
3.98e-09 |
|
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: 58.11 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 202 VSVIPNAVDPTDFTPDPSR---------RDDSMITVVVVSRLVYRKGIDLLsgiIPELCQ--KYPDLHFLVGGEGPKRIV 270
Cdd:cd03825 163 VVVIPNGIDTEIFAPVDKAkarkrlgipQDKKVILFGAESVTKPRKGFDEL---IEALKLlaTKDDLLLVVFGKNDPQIV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 271 LEEVRERY--QLHDRVRLlgalehqdvRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVL--PENLII 346
Cdd:cd03825 240 ILPFDIISlgYIDDDEQL---------VDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVqhGVTGYL 310
|
170
....*....|....*....
gi 1985329438 347 LCEPSVKSLCDGLEKAVAQ 365
Cdd:cd03825 311 VPPGDVQALAEAIEWLLAN 329
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
202-397 |
1.07e-07 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 54.03 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 202 VSVIPNAVDPTDFTPDPS---RRD---DSMITVVVVS-RLVYRKGIDLLSGIIPELCQKYPDLHFLVGGE------GPKR 268
Cdd:PRK15484 163 ISIVPNGFCLETYQSNPQpnlRQQlniSPDETVLLYAgRISPDKGILLLMQAFEKLATAHSNLKLVVVGDptasskGEKA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 269 IVLEEVRE-RYQLHDRVRLLGALEHQDVRNVL-VQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLI- 345
Cdd:PRK15484 243 AYQKKVLEaAKRIGDRCIMLGGQPPEKMHNYYpLADLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITg 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1985329438 346 -ILCEP-SVKSLCDGLEKAVAQirsgtlPTPETIHNKVKTF----YTWRNVAERTEKV 397
Cdd:PRK15484 323 yHLAEPmTSDSIISDINRTLAD------PELTQIAEQAKDFvfskYSWEGVTQRFEEQ 374
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
46-155 |
2.00e-06 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 47.78 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 46 GGVESHIYQLSQCLIERGHKVIIVTHAYGNRkGIRYLANGLKVYYLPLkvmYNQSTATTLFHSLPLLRYIFVRERVTIVH 125
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPG-RPELVGDGVRVHRLPV---PPRPSPLADLAALRRLRRLLRAERPDVVH 76
|
90 100 110
....*....|....*....|....*....|
gi 1985329438 126 SHSSFSSMAhdALFHAKTMGLQTVFTDHSL 155
Cdd:pfam13579 77 AHSPTAGLA--ARLARRRRGVPLVVTVHGL 104
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
202-340 |
1.36e-05 |
|
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: 47.36 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 202 VSVIPNAVDPTDFTPDPSRR-----------DDSMITVVVVSRLVYRkGIDLLSGIIPELCQKYPDLHFL-VGGEG---- 265
Cdd:cd03818 181 ISVIHDGVDTDRLAPDPAARlrllngtelkaGDPVITYVARNLEPYR-GFHVFMRALPRIQARRPDARVVvVGGDGvsyg 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 266 --PKRivLEEVRERY--QL---HDRVRLLGALEHQDVRNVL--VQGHIFLntslTEAFCM--AIVEAASCGLQVVSTRVG 334
Cdd:cd03818 260 spPPD--GGSWKQKMlaELgvdLERVHFVGKVPYDQYVRLLqlSDAHVYL----TYPFVLswSLLEAMACGCPVIGSDTA 333
|
....*.
gi 1985329438 335 GIPEVL 340
Cdd:cd03818 334 PVREVI 339
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
203-356 |
2.18e-05 |
|
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: 46.51 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 203 SVIPNAVDPTDFTPDPSRRDDsmitVVVVSRLVYRKGIDLlsgiIPELCQKYPdLHFLVGGEGPKrivLEEVRERYQlhD 282
Cdd:cd03804 181 TVIYPPVDTDAFAPAADKEDY----YLTASRLVPYKRIDL----AVEAFNELP-KRLVVIGDGPD---LDRLRAMAS--P 246
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985329438 283 RVRLLGALEHQDVRNVLVQGHIFLNTSlTEAFCMAIVEAASCGLQVVSTRVGGIPEVLP--ENLIILCEPSVKSLC 356
Cdd:cd03804 247 NVEFLGYQPDEVLKELLSKARAFVFAA-EEDFGIVPVEAQACGTPVIAFGKGGALETVRpgPTGILFGEQTVESLK 321
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
228-293 |
3.08e-05 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 46.24 E-value: 3.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985329438 228 VVVVSRLVYRKGIDLLSGIIPELCQKypDLHFLVGGEGPKRIV--LEEVRERYqlHDRVRL-LG---ALEHQ 293
Cdd:COG0297 298 IGMVSRLTEQKGLDLLLEALDELLEE--DVQLVVLGSGDPEYEeaFRELAARY--PGRVAVyIGydeALAHR 365
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
228-286 |
4.06e-05 |
|
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: 46.02 E-value: 4.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985329438 228 VVVVSRLVYRKGIDLLSGIIPELCQKypDLHFLVGGEGPKRI--VLEEVRERYqlHDRVRL 286
Cdd:cd03791 297 FGFVGRLTEQKGVDLILDALPELLEE--GGQLVVLGSGDPEYeqAFRELAERY--PGKVAV 353
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
204-366 |
7.69e-05 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 45.41 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 204 VIPNAVDPTDFTPDP----------SRRDDSMITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGEGPkriVLEE 273
Cdd:PRK15179 486 VVYNGLAPLKSVQDDactammaqfdARTSDARFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGP---LLES 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 274 VRE---RYQLHDRVRLLGALEHqdVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEP 350
Cdd:PRK15179 563 VREfaqRLGMGERILFTGLSRR--VGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLP 640
|
170
....*....|....*.
gi 1985329438 351 SVKSLCDGLEKAVAQI 366
Cdd:PRK15179 641 ADTVTAPDVAEALARI 656
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
228-337 |
3.54e-04 |
|
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: 42.69 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 228 VVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGEGPKR-----IVLEEVRERYQLHDRVRLLGALEHQDVRNVLVQG 302
Cdd:cd03792 200 ILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDdpegsVVYEEVMEYAGDDHDIHVLRLPPSDQEINALQRA 279
|
90 100 110
....*....|....*....|....*....|....*.
gi 1985329438 303 -HIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIP 337
Cdd:cd03792 280 aTVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIP 315
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
238-398 |
1.31e-03 |
|
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: 40.83 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 238 KGIDLLSGIIPELCQKYPDLHFLVGGE---GPKRIVLEEVRERYQ----LHDRVRL-LGALEHQDV------RNVLVQGH 303
Cdd:cd03822 200 KGLEILLEALPELKAEFPDVRLVIAGElhpSLARYEGERYRKAAIeelgLQDHVDFhNNFLPEEEVpryisaADVVVLPY 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 304 IFLNTSLTEAFCMAIveaaSCGLQVVSTRVGGIPEVLPE-NLIILCEPSVKSLCDGLekavaqIRSGTLPTP----ETIH 378
Cdd:cd03822 280 LNTEQSSSGTLSYAI----ACGKPVISTPLRHAEELLADgRGVLVPFDDPSAIAEAI------LRLLEDDERrqaiAERA 349
|
170 180
....*....|....*....|
gi 1985329438 379 NKVKTFYTWRNVAERTEKVY 398
Cdd:cd03822 350 YAYARAMTWESIADRYLRLF 369
|
|
| PHA01633 |
PHA01633 |
putative glycosyl transferase group 1 |
230-329 |
2.19e-03 |
|
putative glycosyl transferase group 1
Pssm-ID: 107050 [Multi-domain] Cd Length: 335 Bit Score: 40.35 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 230 VVSRLVYRKGIDLLSGIIPELCQKYPD----LHFLVggegpkriVLEEVRERYQLHDRVRLLGALEHQDVRNVL----VQ 301
Cdd:PHA01633 153 IVSGLTKRKNMDLMLQVFNELNTKYPDiakkIHFFV--------ISHKQFTQLEVPANVHFVAEFGHNSREYIFafygAM 224
|
90 100
....*....|....*....|....*...
gi 1985329438 302 GHIFLNTSlTEAFCMAIVEAASCGLQVV 329
Cdd:PHA01633 225 DFTIVPSG-TEGFGMPVLESMAMGTPVI 251
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
204-370 |
3.42e-03 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 40.07 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 204 VIPNAVDPTDFTPDP------SRRDDSMITVVVVSRLVYRKGIDLLSGIIPELCQKYPDLHFLVGGEGPKRIVLEEVRER 277
Cdd:PRK15490 371 VLPPSTEPSSEVPHKiwqqftQKTQDADTTIGGVFRFVGDKNPFAWIDFAARYLQHHPATRFVLVGDGDLRAEAQKRAEQ 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985329438 278 YQLHDRVRLLGAleHQDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENL--IILCEPSVKSL 355
Cdd:PRK15490 451 LGILERILFVGA--SRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGSAECFIEGVsgFILDDAQTVNL 528
|
170
....*....|....*...
gi 1985329438 356 ---CDGLEKAVAQIRSGT 370
Cdd:PRK15490 529 dqaCRYAEKLVNLWRSRT 546
|
|
| |
