|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
82-391 |
1.46e-58 |
|
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: 194.89 E-value: 1.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 82 RLIRRLGLKRLGQNLDIRLDGLGIdiaFFNARSATPIRLSRHSYMFTVWDLCHRDHPEFpevFANREFERREQILKAVLP 161
Cdd:cd03809 64 KLWRELALLRWLQILLPKKDKPDL---LHSPHNTAPLLLKGCPQVVTIHDLIPLRYPEF---FPKRFRLYYRLLLPISLR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 162 KAVAVIADSEIGADKIASWYAVDRARVHVIPFLPSASVRTYARgestssPQAVREKYGLPNDYIFYPAQMWAHKNHVYLL 241
Cdd:cd03809 138 RADAIITVSEATRDDIIKFYGVPPEKIVVIPLGVDPSFFPPES------AAVLIAKYLLPEPYFLYVGTLEPRKNHERLL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 242 EGIAELKSRYGLtIGAALSGGDKGNKDYLRACAQKLGIADQVFFLGFVDDDEIPALYDGAKALVMPSYFGPTNLPPVEAA 321
Cdd:cd03809 212 KAFALLKKQGGD-LKLVIVGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAM 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 322 LLGCPVIYADQPAFRAQMGDAALYCDLTAPPSLAEHLRTVIEDASKVRRLKAAGHTLAETLRDDTTPQKL 391
Cdd:cd03809 291 ACGTPVIASNISVLPEVAGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKT 360
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-382 |
7.95e-34 |
|
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: 129.58 E-value: 7.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 2 RIAVFVENALH-SGGAFQQTLSMVQTLQSLpGHDVVVLTPIAENIDHLRERKIEAHLYADGAWTRFcdtigglmprseRV 80
Cdd:cd03801 1 KILLLSPELPPpVGGAERHVRELARALAAR-GHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALL------------RA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 81 LRLIRRLGLKRLGQNLDI---RLDGLGIDIAFFNARSATPIRLSRHSYMFTVWDLCHRDHPEFpevfanreFERREQILK 157
Cdd:cd03801 68 RRLLRELRPLLRLRKFDVvhaHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRL--------LARAEALLR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 158 avlpKAVAVIADSEIGADKIASWYAVDRARVHVIPflPSASVRTYARgestsspqAVREKYGLPND--YIFYPAQMWAHK 235
Cdd:cd03801 140 ----RADAVIAVSEALRDELRALGGIPPEKIVVIP--NGVDLERFSP--------PLRRKLGIPPDrpVLLFVGRLSPRK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 236 NHVYLLEGIAELKSRYG---LTIGaalsGGDKGNKDYLRAcaQKLGIADQVFFLGFVDDDEIPALYDGAKALVMPSYFGP 312
Cdd:cd03801 206 GVDLLLEALAKLLRRGPdvrLVIV----GGDGPLRAELEE--LELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEG 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822200741 313 TNLPPVEAALLGCPVIYADQPAFR--AQMGDAALYCDLTAPPSLAEHLRTVIEDASKVRRLKAAGHTLAETL 382
Cdd:cd03801 280 FGLVVLEAMAAGLPVVATDVGGLPevVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAER 351
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
224-375 |
2.85e-22 |
|
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: 92.34 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 224 YIFYPAQMWAHKNHVYLLEGIAELKSRYG---LTIGaalsgGDKGNKDYLRACAQKLGIADQVFFLGFVDDDEIPALYDG 300
Cdd:pfam00534 4 IILFVGRLEPEKGLDLLIKAFALLKEKNPnlkLVIA-----GDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822200741 301 AKALVMPSYFGPTNLPPVEAALLGCPVIYADQPAFR--AQMGDAALYCDLTAPPSLAEHLRTVIEDASKVRRLKAAG 375
Cdd:pfam00534 79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPevVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENA 155
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
10-380 |
3.51e-18 |
|
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: 85.10 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 10 ALHSGGAFQQTLSMVQTLqSLPGHDVVVLTPiaenidhlrerkieahlyADGAWTRFCDTIGGLMPRSERVLRliRRLGL 89
Cdd:cd03819 7 ALEIGGAETYILDLARAL-AERGHRVLVVTA------------------GGPLLPRLRQIGIGLPGLKVPLLR--ALLGN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 90 KRLgqnldIRLdGLGIDIAFFNARSATPIRLSrhsymftvWDLCHRDHPEFPEVFANREFERREQILKAVLPKAVA--VI 167
Cdd:cd03819 66 VRL-----ARL-IRRERIDLIHAHSRAPAWLG--------WLASRLTGVPLVTTVHGSYLATYHPKDFALAVRARGdrVI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 168 ADSEIGADKIASWYAVDRARVHVIP-------FLPSASVRTYARgestsspqavrekYGLPNDY--IFYPAQMWAHKNHV 238
Cdd:cd03819 132 AVSELVRDHLIEALGVDPERIRVIPngvdtdrFPPEAEAEERAQ-------------LGLPEGKpvVGYVGRLSPEKGWL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 239 YLLEGIAELKSRYGLTigaALSGGDKGNKDYLRACAQKLGIADQVFFLGFVDDdeIPALYDGAKALVMPSYFGPTNLPPV 318
Cdd:cd03819 199 LLVDAAAELKDEPDFR---LLVAGDGPERDEIRRLVERLGLRDRVTFTGFRED--VPAALAASDVVVLPSLHEEFGRVAL 273
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822200741 319 EAALLGCPVIYADQPAFRA--QMGDAALYCDLTAPPSLAEHLRTVIEDASKVRRLKAAGHTLAE 380
Cdd:cd03819 274 EAMACGTPVVATDVGGAREivVHGRTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAALTEA 337
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
147-376 |
1.02e-17 |
|
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: 84.21 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 147 REFERREQILKAVLPKAVAVIADSEIGADKIASWYAVDRARVHVIPflPSASVRTYargESTSSPQAVREKYGLPND--Y 224
Cdd:cd03800 148 YHPSLRITAEEQILEAADRVIASTPQEADELISLYGADPSRINVVP--PGVDLERF---FPVDRAEARRARLLLPPDkpV 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 225 IFYPAQMWAHKNHVYLLEGIAELKSRYGLT----IGAALSGGDKGNKDYLRACAQKLGIADQVFFLGFVDDDEIPALYDG 300
Cdd:cd03800 223 VLALGRLDPRKGIDTLVRAFAQLPELRELAnlvlVGGPSDDPLSMDREELAELAEELGLIDRVRFPGRVSRDDLPELYRA 302
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822200741 301 AKALVMPSYFGPTNLPPVEAALLGCPVIYADQ--PAFRAQMGDAALYCDLTAPPSLAEHLRTVIEDASKVRRLKAAGH 376
Cdd:cd03800 303 ADVFVVPSLYEPFGLTAIEAMACGTPVVATAVggLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGL 380
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
2-383 |
1.29e-15 |
|
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: 77.40 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 2 RIAvFVENALHSGGAFQQTLSMVQTLQSLpGHDVVVLTpIAENIDHLRERKIEAHLYadGAWTRFCDTIGGLMPRSERVL 81
Cdd:cd03811 1 KIL-FVIPSLSGGGAERVLLNLANALDKR-GYDVTLVL-LRDEGDLDKQLNGDVKLI--RLLIRVLKLIKLGLLKAILKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 82 RLIrrlgLKRLgqNLDIRLDGLGIDIAFFNARSATPIRL--SRHSYMFTVWDLchrdhpefpevfanrefERREQILKAV 159
Cdd:cd03811 76 KRI----LKRA--KPDVVISFLGFATYIVAKLAAARSKViaWIHSSLSKLYYL-----------------KKKLLLKLKL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 160 LPKAVAVIADSEIGADKIASWYAVDRARVHVI--PFLPsasvrTYARGESTSSPQAVREKYglpnDYIFYPAQMWAHKNH 237
Cdd:cd03811 133 YKKADKIVCVSKGIKEDLIRLGPSPPEKIEVIynPIDI-----DRIRALAKEPILNEPEDG----PVILAVGRLDPQKGH 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 238 VYLLEGIAELKSRYG---LTIgaaLsgGDKGNKDYLRACAQKLGIADQVFFLGFVDDdeIPALYDGAKALVMPSYF--GP 312
Cdd:cd03811 204 DLLIEAFAKLRKKYPdvkLVI---L--GDGPLREELEKLAKELGLAERVIFLGFQSN--PYPYLKKADLFVLSSRYegFP 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822200741 313 TNLppVEAALLGCPVIYADQPAFRAQM--GDAALYCDLTAPPSLAEHLRTVIEDASKVRRLKAAGHTLAETLR 383
Cdd:cd03811 277 NVL--LEAMALGTPVVSTDCPGPREILddGENGLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEAVFR 347
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
224-364 |
4.26e-14 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 68.69 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 224 YIFYPAQMWA-HKNHVYLLEGIAELKSRYG---LTIGaalsgGDkGNKDYLRACAQklGIADQVFFLGFVDDdeIPALYD 299
Cdd:pfam13692 3 VILFVGRLHPnVKGVDYLLEAVPLLRKRDNdvrLVIV-----GD-GPEEELEELAA--GLEDRVIFTGFVED--LAELLA 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822200741 300 GAKALVMPSYFGPTNLPPVEAALLGCPVIYADQPAFRAQM-GDAALYCDLTAPPSLAEHLRTVIED 364
Cdd:pfam13692 73 AADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVdGENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
185-382 |
9.06e-14 |
|
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: 71.92 E-value: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 185 RARVHVIPFLPSASVRTYARGestsSPQAVREKYGLPNDYIFYPAqMWAHKNHVYLLEGIAELKsrYGLTIGaalsgGDK 264
Cdd:cd03795 159 KNKVRVIPLGIDKNVYNIPRV----DFENIKREKKGKKIFLFIGR-LVYYKGLDYLIEAAQYLN--YPIVIG-----GEG 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 265 GNKDYLRACAQKLGIaDQVFFLGFVDDDEIPALYDGAKALVMPSY-----FGPTNLppvEAALLGCPVIYADQPA---FR 336
Cdd:cd03795 227 PLKPDLEAQIELNLL-DNVKFLGRVDDEEKVIYLHLCDVFVFPSVlrseaFGIVLL---EAMMCGKPVISTNIGTgvpYV 302
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1822200741 337 AQMGDAAlycdLTAPP----SLAEHLRTVIEDASKVRRLKAAGHTLAETL 382
Cdd:cd03795 303 NNNGETG----LVVPPkdpdALAEAIDKLLSDEELRESYGENAKKRFEEL 348
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
9-328 |
1.33e-13 |
|
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: 71.64 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 9 NALHSGGAFQqTLSMVQTLQSLpGHDVVVLTPIAEnidHLRERKIEAHLYADGAWTRFCDTIGGLMPRSERVLRLIRRLG 88
Cdd:cd03798 10 NANSPGRGIF-VRRQVRALSRR-GVDVEVLAPAPW---GPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAPSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 89 LKRLGQNLDIRLDGlgidIAFFNARSATPI-----RLSRHSYMFTVWDlchRDHPEFPEVFANREFERReqilkaVLPKA 163
Cdd:cd03798 85 AKLLKRRRRGPPDL----IHAHFAYPAGFAaallaRLYGVPYVVTEHG---SDINVFPPRSLLRKLLRW------ALRRA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 164 VAVIADSEIGADKIASwYAVDRARVHVIPFlpsaSVrtyarGESTSSPQAVREKYGLPNDYIFYPAQMWAHKNHVYLLEG 243
Cdd:cd03798 152 ARVIAVSKALAEELVA-LGVPRDRVDVIPN----GV-----DPARFQPEDRGLGLPLDAFVILFVGRLIPRKGIDLLLEA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 244 IAELKSRYgLTIGAALSGGDKgNKDYLRACAQKLGIADQVFFLGFVDDDEIPALYDGAKALVMPSYFGPTNLPPVEAALL 323
Cdd:cd03798 222 FARLAKAR-PDVVLLIVGDGP-LREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMAC 299
|
....*
gi 1822200741 324 GCPVI 328
Cdd:cd03798 300 GLPVV 304
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
155-376 |
6.97e-12 |
|
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: 66.24 E-value: 6.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 155 ILKAVLPKAVAVIADSEIGADKIASwyAVDRARVHVIP---FLPsasvrtyaRGESTSSPQavREKYGLPND-YIFYPAQ 230
Cdd:cd03821 145 IERRNLNNAALVHFTSEQEADELRR--FGLEPPIAVIPngvDIP--------EFDPGLRDR--RKHNGLEDRrIILFLGR 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 231 MWAHKNHVYLLEGIAELKS---RYGLTIgaalSGGDKGNKDYLRACAQKLGIADQVFFLGFVDDDEIPALYDGAKALVMP 307
Cdd:cd03821 213 IHPKKGLDLLIRAARKLAEqgrDWHLVI----AGPDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLP 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 308 SYFGPTNLPPVEAALLGCPVIYADQPAFRAQM-GDAALYCDLTApPSLAEHLRTVIEDASKVRRLKAAGH 376
Cdd:cd03821 289 SYSENFGNVVAEALACGLPVVITDKCGLSELVeAGCGVVVDPNV-SSLAEALAEALRDPADRKRLGEMAR 357
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
142-328 |
9.58e-12 |
|
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: 64.35 E-value: 9.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 142 EVFANREFERREQILKAVLPKAVAVIADSEIgadkIASWYAVDRARVHVIPFLPSASVRTYARGESTSSPQAVREKYGLP 221
Cdd:cd01635 34 TVLALLLLALRRILKKLLELKPDVVHAHSPH----AAALAALLAARLLGIPIVVTVHGPDSLESTRSELLALARLLVSLP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 222 NDYIFYPAQMWAHKNHVYLLEGIAELKSRYG---LTIGaalsgGDKGNKDYLRACAQKLGIADQVFFLGFVDDDE-IPAL 297
Cdd:cd01635 110 LADKVSVGRLVPEKGIDLLLEALALLKARLPdlvLVLV-----GGGGEREEEEALAAALGLLERVVIIGGLVDDEvLELL 184
|
170 180 190
....*....|....*....|....*....|.
gi 1822200741 298 YDGAKALVMPSYFGPTNLPPVEAALLGCPVI 328
Cdd:cd01635 185 LAAADVFVLPSRSEGFGLVLLEAMAAGKPVI 215
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
165-342 |
1.44e-11 |
|
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: 65.38 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 165 AVIADSEIGADKIASwYAVDRaRVHVIP-------FLPSASVrtyargestsspqAVREKYGLPND--YIFYPAQMWAHK 235
Cdd:cd03817 150 AVIAPSEKIKDTLRE-YGVKG-PIEVIPngidldkFEKPLNT-------------EERRKLGLPPDepILLYVGRLAKEK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 236 NHVYLLEGIAELKSRYG--LTIGaalsgGDKGNKDYLRACAQKLGIADQVFFLGFVDDDEIPALYDGAKALVMPSY---F 310
Cdd:cd03817 215 NIDFLLRAFAELKKEPNikLVIV-----GDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTtetQ 289
|
170 180 190
....*....|....*....|....*....|..
gi 1822200741 311 GPTNLppvEAALLGCPVIYADQPAFRAQMGDA 342
Cdd:cd03817 290 GLVYL---EAMAAGLPVVAAKDPAASELVEDG 318
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
294-381 |
6.27e-11 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 59.62 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 294 IPALYDGAKALVMPSYFGPTNLPPVEAALLGCPVIYADQPAFRAQM--GDAALYCDLTAPPSLAEHLRTVIEDASKVRRL 371
Cdd:COG0438 14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIedGETGLLVPPGDPEALAEAILRLLEDPELRRRL 93
|
90
....*....|
gi 1822200741 372 KAAGHTLAET 381
Cdd:COG0438 94 GEAARERAEE 103
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
2-380 |
6.42e-11 |
|
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: 63.41 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 2 RIAVFVENALHSGGAFQQTLSMVQTLqSLPGHDVVVLT----------PIAENIdHLRERKIEAHLYADGAWTRFcdtig 71
Cdd:cd03820 1 KIAIVIPSISNAGGAERVAINLANHL-AKKGYDVTIISldsaekppfyELDDNI-KIKNLGDRKYSHFKLLLKYF----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 72 glmprsERVLRLIRRLglKRlgQNLDIRLDGLGIDIAFFNARSATPIRLsrhsymftVWDlcHRDHpefpevFANREFER 151
Cdd:cd03820 74 ------KKVRRLRKYL--KN--NKPDVVISFRTSLLTFLALIGLKSKLI--------VWE--HNNY------EAYNKGLR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 152 REQILKAVLPKAVAVIADSEigADKIASwYAVDRARVHVIP-FLPSASVRTYARGESTsspqavrekyglpndYIFYPAQ 230
Cdd:cd03820 128 RLLLRRLLYKRADKIVVLTE--ADKLKK-YKQPNSNVVVIPnPLSFPSEEPSTNLKSK---------------RILAVGR 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 231 MWAHKNHVYLLEGIAELKSRYG---LTIGaalsgGDKGNKDYLRACAQKLGIADQVFFLGFVDDdeIPALYDGAKALVMP 307
Cdd:cd03820 190 LTYQKGFDLLIEAWALIAKKHPdwkLRIY-----GDGPEREELEKLIDKLGLEDRVKLLGPTKN--IAEEYANSSIFVLS 262
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822200741 308 SYF-GptnLPPV--EAALLGCPVIYADQPAFRAQM---GDAALYCDLTAPPSLAEHLRTVIEDASKVRRLKAAGHTLAE 380
Cdd:cd03820 263 SRYeG---FPMVllEAMAYGLPIISFDCPTGPSEIiedGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAE 338
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-381 |
6.31e-10 |
|
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: 60.43 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 2 RIAVFVENALHSGGAFQQTLS-MVQTLQSLpGHDVVVLTPIaENIDHLRERKIEAHLYaDGAWTRFCDTI----GGLMPR 76
Cdd:cd03794 1 KILLISQYYPPPKGAAAARVYeLAKELVRR-GHEVTVLTPS-PNYPLGRIFAGATETK-DGIRVIRVKLGpikkNGLIRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 77 SERVLRLIRRLGLKRLGQNLDIrldglgiDIAFFNARSATPI-------RLSRHSYMFTVWDLchrdhpeFPEVFANREF 149
Cdd:cd03794 78 LLNYLSFALAALLKLLVREERP-------DVIIAYSPPITLGlaalllkKLRGAPFILDVRDL-------WPESLIALGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 150 ERREQILKA-------VLPKAVAVIADSEIGADKIASWYaVDRARVHVIPFlpSASVRTYARGESTSSpqavREKYGLPN 222
Cdd:cd03794 144 LKKGSLLKLlkklerkLYRLADAIIVLSPGLKEYLLRKG-VPKEKIIVIPN--WADLEEFKPPPKDEL----RKKLGLDD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 223 DYIFYPAQMWAHKNHV-YLLEGIAELKSRYGLTIgaaLSGGDKGNKDYLRACAQKLGIADqVFFLGFVDDDEIPALYDGA 301
Cdd:cd03794 217 KFVVVYAGNIGKAQGLeTLLEAAERLKRRPDIRF---LFVGDGDEKERLKELAKARGLDN-VTFLGRVPKEEVPELLSAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 302 KALVMPSYFGPTNLP-----PVEAALLGCPVIYADQPAFRA--QMGDAALYCDLTAPPSLAEHLRTVIEDASKVRRLKAA 374
Cdd:cd03794 293 DVGLVPLKDNPANRGsspskLFEYMAAGKPILASDDGGSDLavEINGCGLVVEPGDPEALADAILELLDDPELRRAMGEN 372
|
....*..
gi 1822200741 375 GHTLAET 381
Cdd:cd03794 373 GRELAEE 379
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
225-380 |
5.53e-09 |
|
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: 57.22 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 225 IFYPAQMWAHKNHVYLLEGIAELKSRYG----LTIGaalsGGDKGNKDYLRAcaQKLGIADQVFFLGFVDDdeIPALYDG 300
Cdd:cd03808 192 FLFVARLLKDKGIDELIEAAKILKKKGPnvrfLLVG----DGELENPSEILI--EKLGLEGRIEFLGFRSD--VPELLAE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 301 AKALVMPSYF-G-PTNLppVEAALLGCPVIYADQPA-----------FRAQMGDAAlycdltappSLAEHLRTVIEDASK 367
Cdd:cd03808 264 SDVFVLPSYReGlPRSL--LEAMAAGRPVITTDVPGcrelvidgvngFLVPPGDVE---------ALADAIEKLIEDPEL 332
|
170
....*....|...
gi 1822200741 368 VRRLKAAGHTLAE 380
Cdd:cd03808 333 RKEMGEAARKRVE 345
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
152-372 |
3.58e-08 |
|
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: 54.99 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 152 REQILKAVLPK-AVAVIADSEIGADKIASWyaVDRARVHVIP-------FLPSASVRtyargestsspQAVREKYGLPND 223
Cdd:cd03812 125 RKNVLKKLIERlSTKYLACSEDAGEWLFGE--VENGKFKVIPngidiekYKFNKEKR-----------RKRRKLLILEDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 224 YIFYpaqmwaH-------KNHVYLLEGIAELKSRYG----LTIGAalsgGDKGNKdyLRACAQKLGIADQVFFLGFVDDd 292
Cdd:cd03812 192 LVLG------HvgrfneqKNHSFLIDIFEELKKKNPnvklVLVGE----GELKEK--IKEKVKELGLEDKVIFLGFRND- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 293 eIPALYDGAKALVMPSYF-GptnLP--PVEAALLGCPVIYADQPAFRAQMGDAALYCDLTAPPSLAEhlRTVIEDASKVR 369
Cdd:cd03812 259 -VSEILSAMDVFLFPSLYeG---LPlvAVEAQASGLPCLLSDTITKECDITNNVEFLPLNETPSTWA--EKILKLIKRKR 332
|
...
gi 1822200741 370 RLK 372
Cdd:cd03812 333 RIN 335
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
2-374 |
4.39e-07 |
|
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: 51.56 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 2 RIAVFVE--NALHSGGAFQQTLSMVQTLQSLpGHDVVVLTPIAEN--IDHLRERKIeaHLYADGAWTRFCDTIGGLMPRS 77
Cdd:cd03823 1 KILLVNSlyPPQRVGGAEISVHDLAEALVAE-GHEVAVLTAGVGPpgQATVARSVV--RYRRAPDETLPLALKRRGYELF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 78 E----RVLRLIRRLgLKRLgqNLDI----RLDGLGIDIAFFNARSATPIRLSRHSYmftvWDLCHRDHPEFPevfanref 149
Cdd:cd03823 78 EtynpGLRRLLARL-LEDF--RPDVvhthNLSGLGASLLDAARDLGIPVVHTLHDY----WLLCPRQFLFKK-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 150 erreqilkavlpKAVAVIADSEIGADKIASWyAVDRARVHVIPFLPSASVRtyARGESTSSPQAVRekyglpndyIFYPA 229
Cdd:cd03823 143 ------------GGDAVLAPSRFTANLHEAN-GLFSARISVIPNAVEPDLA--PPPRRRPGTERLR---------FGYIG 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 230 QMWAHKNhVYLLEGIAELKSRYGLTIGAAlsgGDKGNKDYLRACAQklgiaDQVFFLGFVDDDEIPALYDGAKALVMPSY 309
Cdd:cd03823 199 RLTEEKG-IDLLVEAFKRLPREDIELVIA---GHGPLSDERQIEGG-----RRIAFLGRVPTDDIKDFYEKIDVLVVPSI 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822200741 310 FgPTNLPPV--EAALLGCPVIYADQ--PAFRAQMGDAALYCDLTAPPSLAEHLRTVIEDASKVRRLKAA 374
Cdd:cd03823 270 W-PEPFGLVvrEAIAAGLPVIASDLggIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAG 337
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
212-373 |
4.76e-07 |
|
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.
Pssm-ID: 340857 [Multi-domain] Cd Length: 360 Bit Score: 51.29 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 212 QAVREKYGLPND--YIFYPAQMWAHKNHVYLLEGIAEL---KSRYGLTIGaalsgGDKGNKDYLRACAQKLGIADQVFFL 286
Cdd:cd04951 176 LKIRNKLNLKNDefVILNVGRLTEAKDYPNLLLAISELilsKNDFKLLIA-----GDGPLRNELERLICNLNLVDRVILL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 287 GFVDDdeIPALYDGAKALVMPSYFGPTNLPPVEAALLGCPVIYADQPAFRAQMGDAALYCDLTAPPSLAEHLRTVIEDAS 366
Cdd:cd04951 251 GQISN--ISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHNYVVPVSDPQLLAEKIKEIFDMSD 328
|
....*..
gi 1822200741 367 KVRRLKA 373
Cdd:cd04951 329 EERDILG 335
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
2-381 |
4.85e-06 |
|
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: 48.06 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 2 RIAVFVENALHSGGAFQQTL-SMVQTLQSLpGHDVVVLTPiaenidHLRERKIEAHLYADGAWTRFCDTIGGL---MPRS 77
Cdd:cd03814 1 RIALVTDTYHPQVNGVVRTLeRLVDHLRRR-GHEVRVVAP------GPFDEAESAEGRVVSVPSFPLPFYPEYrlaLPLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 78 ERVLRLIRRLglkrlgqNLDIrldglgIDIA--FFNARSATPIRLSRHSYMFTVwdlCHRDHPEFPEVFANREFERR-EQ 154
Cdd:cd03814 74 RRVRRLIKEF-------QPDI------IHIAtpGPLGLAALRAARRLGLPVVTS---YHTDFPEYLSYYTLGPLSWLaWA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 155 ILKAVLPKAVAVIADSEIGADKIASWyavDRARVHVIP-------FLPSAsvRTyargestsspQAVREKYGLPNDYIF- 226
Cdd:cd03814 138 YLRWFHNPFDTTLVPSPSIARELEGH---GFERVRLWPrgvdtelFHPSR--RD----------AALRRRLGPPGRPLLl 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 227 YPAQMWAHKNHVYLLEGIAELKSRYGLTIgaaLSGGDKGNKDYLRACAqklgiaDQVFFLGFVDDDEIPALYDGAKALVM 306
Cdd:cd03814 203 YVGRLAPEKNLEALLDADLPLAASPPVRL---VVVGDGPARAELEARG------PDVIFTGFLTGEELARAYASADVFVF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 307 PS---YFGPTNLppvEAALLGCPVIYADQPAFR--AQMGDAALYCDLTAPPSLAEHLRTVIEDASKVRRLKAAGHTLAET 381
Cdd:cd03814 274 PSrteTFGLVVL---EAMASGLPVVAADAGGPRdiVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAER 350
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
262-375 |
3.58e-05 |
|
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: 45.42 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 262 GDKGNKDYLRACAQKLGIADQVFFLGfvDDDEIPALYDGAKALVMPSY---FGptnLPPVEAALLGCPVIYADQ---PAF 335
Cdd:cd04962 233 GDGPERVPAEELARELGVEDRVLFLG--KQDDVEELLSIADLFLLPSEkesFG---LAALEAMACGVPVVSSNAggiPEV 307
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1822200741 336 RAQmGDAALYCDLTAPPSLAEHLRTVIEDASKVRRLKAAG 375
Cdd:cd04962 308 VKH-GETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAA 346
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
14-192 |
2.71e-04 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 41.23 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 14 GGAFQQTLSMVQTLQSLpGHDVVVLTPiaenidhlRERKIEAHLYADGAWTRFCDtiggLMPRSERVLRLIRRLGLKRLg 93
Cdd:pfam13579 1 GGIGVYVLELARALAAL-GHEVRVVTP--------GGPPGRPELVGDGVRVHRLP----VPPRPSPLADLAALRRLRRL- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 94 qnldirLDGLGIDIAF-FNARSATPIRL----SRHSYMFTVWDLCHRDHPEFPEVFAnREFERReqilkaVLPKAVAVIA 168
Cdd:pfam13579 67 ------LRAERPDVVHaHSPTAGLAARLarrrRGVPLVVTVHGLALDYGSGWKRRLA-RALERR------LLRRADAVVV 133
|
170 180
....*....|....*....|....
gi 1822200741 169 DSEIGADKIASWYaVDRARVHVIP 192
Cdd:pfam13579 134 VSEAEAELLRALG-VPAARVVVVP 156
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
14-192 |
5.53e-04 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 40.59 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 14 GGAFQQTLSMVQTLQSLpGHDVVVLTPiaenidhlreRKIEAHLYADGAWTRFCDTIGGLMPRSERVLRLIRRLglKRLg 93
Cdd:pfam13439 1 GGVERYVLELARALARR-GHEVTVVTP----------GGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRL--RRL- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 94 qnldirLDGLGIDI-----------AFFNARSATPIRL--SRHSymfTVWDLCHRDHPEFPEVFANREFERReqilkaVL 160
Cdd:pfam13439 67 ------LRRERPDVvhahspfplglAALAARLRLGIPLvvTYHG---LFPDYKRLGARLSPLRRLLRRLERR------LL 131
|
170 180 190
....*....|....*....|....*....|..
gi 1822200741 161 PKAVAVIADSEIGADKIASWYAVDRARVHVIP 192
Cdd:pfam13439 132 RRADRVIAVSEAVADELRRLYGVPPEKIRVIP 163
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
145-375 |
6.20e-04 |
|
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: 41.67 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 145 ANREFERREQILKAvlpKAVAVIADSEIGADK-IASWYAVDRARVHVIPFLPsASVRTYARGEstsspqavrekyglPND 223
Cdd:cd05844 129 WPSQFQRHRRALQR---PAALFVAVSGFIRDRlLARGLPAERIHVHYIGIDP-AKFAPRDPAE--------------RAP 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 224 YIFYPAQMWAHKNHVYLLEGIAELKSRYGLTigAALSGGDKGNKDYLRACAQKLGiadQVFFLGFVDDDEIPALYDGAKA 303
Cdd:cd05844 191 TILFVGRLVEKKGCDVLIEAFRRLAARHPTA--RLVIAGDGPLRPALQALAAALG---RVRFLGALPHAEVQDWMRRAEI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 304 LVMPSYFGPTN----LPPV--EAALLGCPVIYADQPAFRAQMGDAAlyCDLTAPP----SLAEHLRTVIEDASKVRRLKA 373
Cdd:cd05844 266 FCLPSVTAASGdsegLGIVllEAAACGVPVVSSRHGGIPEAILDGE--TGFLVPEgdvdALADALQALLADRALADRMGG 343
|
..
gi 1822200741 374 AG 375
Cdd:cd05844 344 AA 345
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
263-328 |
1.74e-03 |
|
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: 39.96 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 263 DKGNKDYLRACAQ---KLGIA------------------DQVFFLGFVDDDEIPALYDGAKALVMPSY----FGptnLPP 317
Cdd:cd03802 181 EKGLEDAIRVARRaglPLKIAgkvrdedyfyylqeplpgPRIEFIGEVGHDEKQELLGGARALLFPINwdepFG---LVM 257
|
90
....*....|.
gi 1822200741 318 VEAALLGCPVI 328
Cdd:cd03802 258 IEAMACGTPVI 268
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
232-328 |
3.28e-03 |
|
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: 39.49 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822200741 232 WAHKNHVYLLEGIAELKSRYGLTIGAAL--SGG-DKG---NKDYL----RACAQKLGIADQVFFLGFVDDDEIPALYDGA 301
Cdd:cd03805 221 ERKKNIALAIEAFAKLKQKLPEFENVRLviAGGyDPRvaeNVEYLeelqRLAEELLNVEDQVLFLRSISDSQKEQLLSSA 300
|
90 100 110
....*....|....*....|....*....|
gi 1822200741 302 KALV-MPSY--FGPTnlpPVEAALLGCPVI 328
Cdd:cd03805 301 LALLyTPSNehFGIV---PLEAMYAGKPVI 327
|
|
| |
