|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-366 |
1.62e-68 |
|
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: 220.10 E-value: 1.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 2 RIGMVCPYSFDVPGGVQAHAIDLCEEFIRRGHEVSLIGPAsvqaDVPDFVVRGGAAIPIPYNGSVARLSFGPRTSRRVRT 81
Cdd:cd03801 1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPA----DPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 82 WIEEGSFDILHIHEPNSPSFSMLSLVNSVGPIVATYHSAATDSLALKLAT--PFLRKYLERIRGG---IAVSEVARRWQV 156
Cdd:cd03801 77 LLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAerRLLARAEALLRRAdavIAVSEALRDELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 157 EQLGGDP---VLIPNGVRVGDFEscPAASSLPEIPPRRegfYRLVFLGRFDEsRKGFDVLLDALPAIRAEIPQLEVCVVG 233
Cdd:cd03801 157 ALGGIPPekiVVIPNGVDLERFS--PPLRRKLGIPPDR---PVLLFVGRLSP-RKGVDLLLEALAKLLRRGPDVRLVIVG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 234 DGD--VAAARRKAGRNADVLHFVGRLSEDAKASILADADAYIAPQRGgESFGIVLVEAMAAGAPVISSDIDAFKLVLDDG 311
Cdd:cd03801 231 GDGplRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRY-EGFGLVVLEAMAAGLPVVATDVGGLPEVVEDG 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 740843613 312 HYGLHFENGNSVDLADAVVRLLTQPKLGEELRALGHKR-AWEYDWSQVADGVLRVY 366
Cdd:cd03801 310 EGGLVVPPDDVEALADALLRLLADPELRARLGRAARERvAERFSWERVAERLLDLY 365
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
15-344 |
3.41e-38 |
|
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: 140.19 E-value: 3.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 15 GGVQAHAIDLCEEFIRRGHEVSLIgpaSVQADVPDFVVRGGAAIPIPYNGSVARLSFG--PRTSRRVRTWIEEGSFDILH 92
Cdd:cd03811 12 GGAERVLLNLANALDKRGYDVTLV---LLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLglLKAILKLKRILKRAKPDVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 93 IHEPNSPSFSMlSLVNSVGPIVATYHSAATDSLALKLATPFLRKYLERIRGGIAVSEVARRWqVEQLGGDP----VLIPN 168
Cdd:cd03811 89 SFLGFATYIVA-KLAAARSKVIAWIHSSLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKED-LIRLGPSPpekiEVIYN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 169 GVrvgDFESCPAASSLPEIPPRREGFYrLVFLGRFDEsRKGFDVLLDALPAIRAEIPQLEVCVVGDGDVAAARRKAGRNA 248
Cdd:cd03811 167 PI---DIDRIRALAKEPILNEPEDGPV-ILAVGRLDP-QKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 249 DV---LHFVGRLSeDAkASILADADAYIAPQRGgESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHYGLhFENGNSVDL 325
Cdd:cd03811 242 GLaerVIFLGFQS-NP-YPYLKKADLFVLSSRY-EGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGL-LVPDGDAAA 317
|
330
....*....|....*....
gi 740843613 326 ADAVVRLLTQPKLGEELRA 344
Cdd:cd03811 318 LAGILAALLQKKLDAALRE 336
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
2-369 |
4.38e-37 |
|
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: 137.80 E-value: 4.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 2 RIGMVCPYSFDVPGGVQAHAIDLCEEFIRRGHEVSLIGPASVQADVPDFVVR---GGAAIPIPYNGSVARLsFGPRTSRR 78
Cdd:cd03817 1 KIAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEEVVRyrsFSIPIRKYHRQHIPFP-FKKAVIDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 79 VRTWieegSFDILHIHEPnspsFSMLSLVNSVG-----PIVATYHSAATD---------SLALKLATPFLRKYLERIRGG 144
Cdd:cd03817 80 IKEL----GPDIIHTHTP----FSLGKLGLRIArklkiPIVHTYHTMYEDylhyipkgkLLVKAVVRKLVRRFYNHTDAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 145 IAVSE-VARRWQVEQLGGDPVLIPNGVRVGDFESCPAASSLPEIPPRREGFyRLVFLGRFDEsRKGFDVLLDALPAIRAE 223
Cdd:cd03817 152 IAPSEkIKDTLREYGVKGPIEVIPNGIDLDKFEKPLNTEERRKLGLPPDEP-ILLYVGRLAK-EKNIDFLLRAFAELKKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 224 iPQLEVCVVGDG-DVAAARRKAGRN--ADVLHFVGRLSEDAKASILADADAYIAPQRGgESFGIVLVEAMAAGAPVISSD 300
Cdd:cd03817 230 -PNIKLVIVGDGpEREELKELARELglADKVIFTGFVPREELPEYYKAADLFVFASTT-ETQGLVYLEAMAAGLPVVAAK 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740843613 301 IDAFKLVLDDGHYGLHFENGNsVDLADAVVRLLTQPKLGEELRALGHKRAWEYDwsqVADGVLRVYDTV 369
Cdd:cd03817 308 DPAASELVEDGENGFLFEPND-ETLAEKLLHLRENLELLRKLSKNAEISAREFA---FAKSVEKLYEEV 372
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
196-334 |
2.88e-33 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 120.69 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 196 RLVFLGRFDESRKGFDVLLDALPAIRAEIPQLEVCVVGDGDVAAARRKAGRNADVLHFVGRLSEdaKASILADADAYIAP 275
Cdd:pfam13692 3 VILFVGRLHPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEELAAGLEDRVIFTGFVED--LAELLAAADVFVLP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 740843613 276 QRgGESFGIVLVEAMAAGAPVISSDIDAFKLVLdDGHYGLHFENGNSVDLADAVVRLLT 334
Cdd:pfam13692 81 SL-YEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLE 137
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
15-352 |
8.97e-33 |
|
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: 125.85 E-value: 8.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 15 GGVQAHAIDLCEEFIRRGHEVSLIGpASVQADVPDFVVRGGAAIPIPYNGSVARLSFGPRTSRRVRTWIEEgsFDILHIH 94
Cdd:cd03795 14 GGIEQVIYDLAEGLKKKGIEVDVLC-FSKEKETPEKEENGIRIHRVKSFLNVASTPFSPSYIKRFKKLAKE--YDIIHYH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 95 EPNsPSFSMLSL-VNSVGPIVATYHSaatDSL----ALKLATPFLRKYLERIRGGIAVSEVARRwQVEQLGG--DPV-LI 166
Cdd:cd03795 91 FPN-PLADLLLFfSGAKKPVVVHWHS---DIVkqkkLLKLYKPLMTRFLRRADRIIATSPNYVE-TSPTLREfkNKVrVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 167 PNGVrvgDFESCPAASSLPEIPPRREGFYRLV-FLGRFDEsRKGFDVLLDALPAIRAEIpqlevCVVGDGDVAA---ARR 242
Cdd:cd03795 166 PLGI---DKNVYNIPRVDFENIKREKKGKKIFlFIGRLVY-YKGLDYLIEAAQYLNYPI-----VIGGEGPLKPdleAQI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 243 KAGrNADVLHFVGRLSEDAKASILADADAYIAPQ--RGgESFGIVLVEAMAAGAPVISSDID-AFKLVLDDGHYGLHFEN 319
Cdd:cd03795 237 ELN-LLDNVKFLGRVDDEEKVIYLHLCDVFVFPSvlRS-EAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVPP 314
|
330 340 350
....*....|....*....|....*....|...
gi 740843613 320 GNSVDLADAVVRLLTQPKLGEELRALGHKRAWE 352
Cdd:cd03795 315 KDPDALAEAIDKLLSDEELRESYGENAKKRFEE 347
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
2-363 |
3.12e-32 |
|
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: 124.40 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 2 RIGMVCPYSFDVPGGVQAHAIDLCEEFIRRGHEVSLIGPASVQADVPDFVVRGGAAIPIPYNGSVARLSFGPRTSRRVRt 81
Cdd:cd03809 1 KILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 82 wIEEGSFDILHIHEPNSPsfsmlsLVNSVGPIVATYHsaatDSLALKLA---TPFLRKYLERI--------RGGIAVSEV 150
Cdd:cd03809 80 -PKKDKPDLLHSPHNTAP------LLLKGCPQVVTIH----DLIPLRYPeffPKRFRLYYRLLlpislrraDAIITVSEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 151 ARRwQVEQLGGDP----VLIPNGVRVGDF--ESCPAASSLPEIPPRregfYrLVFLGRFDEsRKGFDVLLDALPAIRAEI 224
Cdd:cd03809 149 TRD-DIIKFYGVPpekiVVIPLGVDPSFFppESAAVLIAKYLLPEP----Y-FLYVGTLEP-RKNHERLLKAFALLKKQG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 225 PQLEVCVVGDGD-----VAAARRKAGRNADVlHFVGRLSEDAKASILADADAYIAPQRGgESFGIVLVEAMAAGAPVISS 299
Cdd:cd03809 222 GDLKLVIVGGKGwedeeLLDLVKKLGLGGRV-RFLGYVSDEDLPALYRGARAFVFPSLY-EGFGLPVLEAMACGTPVIAS 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740843613 300 DIDAFKLVLDDGhyGLHFENGNSVDLADAVVRLLTQPKLGEELRALGHKRAWEYDWSQVADGVL 363
Cdd:cd03809 300 NISVLPEVAGDA--ALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTL 361
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
24-367 |
1.16e-31 |
|
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: 122.79 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 24 LCEEFIRRGHEVSLIGP-ASVQADVPDFVVRGGAAIPIPYNGSVaRLSFGPRTSRRVRtwIEEGSFDILHIHEPNSPSFS 102
Cdd:cd03814 23 LVDHLRRRGHEVRVVAPgPFDEAESAEGRVVSVPSFPLPFYPEY-RLALPLPRRVRRL--IKEFQPDIIHIATPGPLGLA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 103 MLSLVNSVG-PIVATYH-------SAATDSLALKLATPFLRKYLERIRG----GIAVSEVARRWQVEQLggdpVLIPNGV 170
Cdd:cd03814 100 ALRAARRLGlPVVTSYHtdfpeylSYYTLGPLSWLAWAYLRWFHNPFDTtlvpSPSIARELEGHGFERV----RLWPRGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 171 RVGDFEscPAASSlPEIPPRR--EGFYRLVFLGRFdESRKGFDVLLDALPAIRAEIPqLEVCVVGDGDVAAARRKAGRNA 248
Cdd:cd03814 176 DTELFH--PSRRD-AALRRRLgpPGRPLLLYVGRL-APEKNLEALLDADLPLAASPP-VRLVVVGDGPARAELEARGPDV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 249 dvlHFVGRLSEDAKASILADADAYIAPQRGgESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHYGLHFENGNSVDLADA 328
Cdd:cd03814 251 ---IFTGFLTGEELARAYASADVFVFPSRT-ETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAA 326
|
330 340 350
....*....|....*....|....*....|....*....
gi 740843613 329 VVRLLTQPKLGEELRALGHKRAWEYDWSQVADGVLRVYD 367
Cdd:cd03814 327 LRALLEDPELRRRMAARARAEAERYSWEAFLDNLLDYYA 365
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
12-369 |
1.33e-30 |
|
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: 120.18 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 12 DVPGGVQAHAIDLCEEFIRRGHEVSLIGPA---------SVQADVPDFVVRGGAAIPIPYNGSVARLSFGPRTSRRVRTW 82
Cdd:cd03798 11 ANSPGRGIFVRRQVRALSRRGVDVEVLAPApwgpaaarlLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAPSLAKLLKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 83 IEEGSFDILHIH--EPNSPSFSMLSLVNSVgPIVATYHSAATDSLALK-LATPFLRKYLERIRGGIAVS-EVARRWQVEQ 158
Cdd:cd03798 91 RRRGPPDLIHAHfaYPAGFAAALLARLYGV-PYVVTEHGSDINVFPPRsLLRKLLRWALRRAARVIAVSkALAEELVALG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 159 LGGDPV-LIPNGVRVGDFESCPAASSLPEIPPRregfyrLVFLGRFdESRKGFDVLLDALPAIRAEIPQLEVCVVGDG-- 235
Cdd:cd03798 170 VPRDRVdVIPNGVDPARFQPEDRGLGLPLDAFV------ILFVGRL-IPRKGIDLLLEAFARLAKARPDVVLLIVGDGpl 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 236 -DVAAARRKAGRNADVLHFVGRLSEDAKASILADADAYIAPQRGgESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHYG 314
Cdd:cd03798 243 rEALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRH-EGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETG 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 740843613 315 LHFENGNSVDLADAVVRLLTQPKLGEELRALGHKRAWEYDWSQVADGVLRVYDTV 369
Cdd:cd03798 322 LLVPPGDADALAAALRRALAEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
2-361 |
2.90e-30 |
|
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: 119.40 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 2 RIGMVCPYSFDVPGGVQAHAIDLCEEFIRRGHEVSLIGPA-------SVQADVPDFVVRGGAAIPIPYNGSVaRLSFGPR 74
Cdd:cd03821 1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGdgyeslvVEENGRYIPPQDGFASIPLLRQGAG-RTDFSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 75 TSRRVRTWIEEgsFDILHIH---EPNSPSFSMLSLVNSVgPIVATYHsAATDSLALKLATPFLRKYLERI--------RG 143
Cdd:cd03821 80 LPNWLRRNLRE--YDVVHIHgvwTYTSLAACKLARRRGI-PYVVSPH-GMLDPWALQQKHWKKRIALHLIerrnlnnaAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 144 GIAVSEVARRWQVE-QLGGDPVLIPNGVRVGDFESCPAASSLPEIPPRREgfyRLVFLGRFDEsRKGFDVLLDALPAIRA 222
Cdd:cd03821 156 VHFTSEQEADELRRfGLEPPIAVIPNGVDIPEFDPGLRDRRKHNGLEDRR---IILFLGRIHP-KKGLDLLIRAARKLAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 223 EIPQLEVCVVG--DGDVAAARRKAGR--NADVLHFVGRLSEDAKASILADADAYIAPQRGgESFGIVLVEAMAAGAPVIS 298
Cdd:cd03821 232 QGRDWHLVIAGpdDGAYPAFLQLQSSlgLGDRVTFTGPLYGEAKWALYASADLFVLPSYS-ENFGNVVAEALACGLPVVI 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740843613 299 SDIDAFKLVLDDGhyglhfeNGNSVD-----LADAVVRLLTQPKLGEELRALGHK-RAWE--YDWSQVADG 361
Cdd:cd03821 311 TDKCGLSELVEAG-------CGVVVDpnvssLAEALAEALRDPADRKRLGEMARRaRQVEenFSWEAVAGQ 374
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
197-349 |
5.40e-28 |
|
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: 107.36 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 197 LVFLGRFdESRKGFDVLLDALPAIRAEIPQLEVCVVGDGDVAA---ARRKAGRNADVLHFVGRLSEDAKASILADADAYI 273
Cdd:pfam00534 5 ILFVGRL-EPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKrlkKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFV 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740843613 274 APQRGgESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHYGLHFENGNSVDLADAVVRLLTQPKLGEELRALGHKR 349
Cdd:pfam00534 84 LPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
13-350 |
4.50e-27 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
Pssm-ID: 340837 [Multi-domain] Cd Length: 358 Bit Score: 109.99 E-value: 4.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 13 VPGGVQAHAIDLCEEFIRRGHEVSLIgpASVQADVPDFVVRGGA-AIPIPYNgsvaRLSFGP----RTSRRVRTWIEEGS 87
Cdd:cd03808 8 VDGGFQSFRLPLIKALVKKGYEVHVI--APDGDKLSDELKELGVkVIDIPIL----RRGINPlkdlKALFKLYKLLKKEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 88 FDILHIHEPNSPSFSML-SLVNSVGPIVAT---YHSAATDSLALKlatpFLRKYLERIRGG-----IAVSE----VARRW 154
Cdd:cd03808 82 PDIVHCHTPKPGILGRLaARLAGVPKVIYTvhgLGFVFTEGKLLR----LLYLLLEKLALLftdkvIFVNEddrdLAIKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 155 QVEQLGGDPVLIPNGVRVGDFEscpaasslPEIPPRREGFYRLVFLGRFDEsRKGFDVLLDALPAIRAEIPQLEVCVVGD 234
Cdd:cd03808 158 GIIKKKKTVLIPGSGVDLDRFQ--------YSPESLPSEKVVFLFVARLLK-DKGIDELIEAAKILKKKGPNVRFLLVGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 235 GDV---AAARRKAGRNADVLHFVGRLSEdaKASILADADAYIAPQRGgESFGIVLVEAMAAGAPVISSDIDAFKLVLDDG 311
Cdd:cd03808 229 GELenpSEILIEKLGLEGRIEFLGFRSD--VPELLAESDVFVLPSYR-EGLPRSLLEAMAAGRPVITTDVPGCRELVIDG 305
|
330 340 350
....*....|....*....|....*....|....*....
gi 740843613 312 HYGLHFENGNSVDLADAVVRLLTQPKLGEELRALGHKRA 350
Cdd:cd03808 306 VNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRV 344
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
2-352 |
2.44e-26 |
|
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: 108.09 E-value: 2.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 2 RIGMVCPySFDVPGGVQAHAIDLCEEFIRRGHEVSLIGPASVQA----DVPDFVVRggAAIPIPYNGSVARLSFGPRTSR 77
Cdd:cd03820 1 KIAIVIP-SISNAGGAERVAINLANHLAKKGYDVTIISLDSAEKppfyELDDNIKI--KNLGDRKYSHFKLLLKYFKKVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 78 RVRTWIEEGSFDILHIHEPNSPSFsmLSLVNSVGPIVATYHSAatdslaLKLATPFLRKYLERIRGG------IAVSEVA 151
Cdd:cd03820 78 RLRKYLKNNKPDVVISFRTSLLTF--LALIGLKSKLIVWEHNN------YEAYNKGLRRLLLRRLLYkradkiVVLTEAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 152 RRWQVEQLGGDPVLIPNgvrvgdfescPAASSLPEIPPRREGFyRLVFLGRFdESRKGFDVLLDALPAIRAEIPQLEVCV 231
Cdd:cd03820 150 KLKKYKQPNSNVVVIPN----------PLSFPSEEPSTNLKSK-RILAVGRL-TYQKGFDLLIEAWALIAKKHPDWKLRI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 232 VGDGDVAAA-RRKAGRN--ADVLHFVGRLSEdaKASILADADAYIAPQRGgESFGIVLVEAMAAGAPVISSDID-AFKLV 307
Cdd:cd03820 218 YGDGPEREElEKLIDKLglEDRVKLLGPTKN--IAEEYANSSIFVLSSRY-EGFPMVLLEAMAYGLPIISFDCPtGPSEI 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 740843613 308 LDDGHYGLHFENGNSVDLADAVVRLLTQpklgEELRALGHKRAWE 352
Cdd:cd03820 295 IEDGENGLLVPNGDVDALAEALLRLMED----EELRKKMGKNARK 335
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-360 |
2.96e-24 |
|
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: 102.81 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 2 RIGMVCPYSFDVPGGVQAHAIDLCEEFIRRGHEVSLIGPASVQADVPDFV----VRGGAAI---PIPY---NGSVARLSF 71
Cdd:cd03794 1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAgateTKDGIRVirvKLGPikkNGLIRRLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 72 GPRTSRRVRTWI--EEGSFDILHIHEPnSPSFSMLSLV---NSVGPIVATYH----------SAATDSLALKLATPFLRK 136
Cdd:cd03794 81 YLSFALAALLKLlvREERPDVIIAYSP-PITLGLAALLlkkLRGAPFILDVRdlwpeslialGVLKKGSLLKLLKKLERK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 137 YLERIRGGIAVSEVARRwQVEQLGGDP---VLIPNGVRVGDFESCPAASSLPEIPPRREgfYRLVFLGRFDESRkGFDVL 213
Cdd:cd03794 160 LYRLADAIIVLSPGLKE-YLLRKGVPKekiIVIPNWADLEEFKPPPKDELRKKLGLDDK--FVVVYAGNIGKAQ-GLETL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 214 LDALPAIRaEIPQLEVCVVGDGDvAAARRKAGRNADVL---HFVGRLSEDAKASILADADAYIAPQRGGESFGIV----L 286
Cdd:cd03794 236 LEAAERLK-RRPDIRFLFVGDGD-EKERLKELAKARGLdnvTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGSspskL 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740843613 287 VEAMAAGAPVISSDIDAFKLVLDDGHYGLHFENGNSVDLADAVVRLLTQPKLGEELRALGHKRAWE-YDWSQVAD 360
Cdd:cd03794 314 FEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEkFSREKLAD 388
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
15-344 |
3.05e-24 |
|
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: 102.02 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 15 GGVQAHAIDLCEEFIRRGHEVSLIGPA---SVQADVPDFVVRGGAAI------PIPYNGSVARLSFGPRTSRRVRTWIEE 85
Cdd:cd03823 15 GGAEISVHDLAEALVAEGHEVAVLTAGvgpPGQATVARSVVRYRRAPdetlplALKRRGYELFETYNPGLRRLLARLLED 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 86 GSFDILHIHEPNSPSFSMLSLVNSVG-PIVATYHSAatdslalklatpflrkYLERIRGG---------IAVSE-VARRW 154
Cdd:cd03823 95 FRPDVVHTHNLSGLGASLLDAARDLGiPVVHTLHDY----------------WLLCPRQFlfkkggdavLAPSRfTANLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 155 QVEQLGGDPV-LIPNGVrvgdfescPAASSLPEIPPRREGFYRLVFLGRfDESRKGFDVLLDALPAIRAeiPQLEVCVVG 233
Cdd:cd03823 159 EANGLFSARIsVIPNAV--------EPDLAPPPRRRPGTERLRFGYIGR-LTEEKGIDLLVEAFKRLPR--EDIELVIAG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 234 DGDVAAARRKAGrnADVLHFVGRLSEDAKASILADADAYIAPQRGGESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHY 313
Cdd:cd03823 228 HGPLSDERQIEG--GRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVN 305
|
330 340 350
....*....|....*....|....*....|.
gi 740843613 314 GLHFENGNSVDLADAVVRLLTQPKLGEELRA 344
Cdd:cd03823 306 GLLFAPGDAEDLAAAMRRLLTDPALLERLRA 336
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
15-364 |
2.16e-23 |
|
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: 100.39 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 15 GGVQAHAIDLCEEFIRRGHEVSLIGPASVQADVPdfvvrggaAIPIPYNGSVARLSFGPRT--------------SRRVR 80
Cdd:cd03800 21 GGQNVYVLELARALAELGYQVDIFTRRISPADPE--------VVEIAPGARVIRVPAGPPEylpkeelwpyleefADGLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 81 TWI--EEGSFDILHIHepnspsFSMLSLVNSVG------PIVATYHSAATDSLALKLATPfLRKYLERIRGGIAVSEVAR 152
Cdd:cd03800 93 RFIarEGGRYDLIHSH------YWDSGLVGALLarrlgvPLVHTFHSLGRVKYRHLGAQD-TYHPSLRITAEEQILEAAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 153 R----------WQVEQLGGDPV---LIPNGVRVGDFescpaaSSLPEIPPRREGF------YRLVFLGRFDEsRKGFDVL 213
Cdd:cd03800 166 RviastpqeadELISLYGADPSrinVVPPGVDLERF------FPVDRAEARRARLllppdkPVVLALGRLDP-RKGIDTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 214 LDALPAIRAEIPQLEVCVVG----DGDVAAARRKAG-----RNADVLHFVGRLSEDAKASILADADAYIAPQRGgESFGI 284
Cdd:cd03800 239 VRAFAQLPELRELANLVLVGgpsdDPLSMDREELAElaeelGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLY-EPFGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 285 VLVEAMAAGAPVISSDIDAFKLVLDDGHYGLHFENGNSVDLADAVVRLLTQPKLGEELRALGHKRAWE-YDWSQVADGVL 363
Cdd:cd03800 318 TAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAhYTWESVADQLL 397
|
.
gi 740843613 364 R 364
Cdd:cd03800 398 T 398
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
13-350 |
6.60e-23 |
|
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: 98.20 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 13 VPGGVQAHAIDLCEEFIRRGHEVSLIGpasvqADVPDFVVRGGAAIPIPYNGSVARLSFGPRTSRRVRTWIEEgsFDILH 92
Cdd:cd03819 9 EIGGAETYILDLARALAERGHRVLVVT-----AGGPLLPRLRQIGIGLPGLKVPLLRALLGNVRLARLIRRER--IDLIH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 93 IHEPNSPSFSMLSLVNSVGPIVATYHSAATDSLALKLATPFLRKYLERIrggIAVSEVARRWQVEQLGGDPV---LIPNG 169
Cdd:cd03819 82 AHSRAPAWLGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVRARGDRV---IAVSELVRDHLIEALGVDPErirVIPNG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 170 VRVGDFESCPAASSLPEIPPRrEGFYRLVFLGRFDESrKGFDVLLDALPAIRAEIPQLEVcVVGDG----DVAAARRKAG 245
Cdd:cd03819 159 VDTDRFPPEAEAEERAQLGLP-EGKPVVGYVGRLSPE-KGWLLLVDAAAELKDEPDFRLL-VAGDGperdEIRRLVERLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 246 RnADVLHFVGRLseDAKASILADADAYIAPQRGgESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHYGLHFENGNSVDL 325
Cdd:cd03819 236 L-RDRVTFTGFR--EDVPAALAASDVVVLPSLH-EEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEAL 311
|
330 340
....*....|....*....|....*
gi 740843613 326 ADAVVRLLTQPKLGEELRALGHKRA 350
Cdd:cd03819 312 ADAIRAAKLLPEAREKLQAAAALTE 336
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
14-346 |
8.67e-23 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 98.16 E-value: 8.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 14 PGGVQAHAIDLCEEFIRRGHE---VSLIGPASVQADVPDFvvrggaaiPIPYNGSVARLSFGPRTSRRVRTWIEEGSFDI 90
Cdd:cd03807 11 VGGAETMLLRLLEHMDKSRFEhvvISLTGDGVLGEELLAA--------GVPVVCLGLSSGKDPGVLLRLAKLIRKRNPDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 91 LHIHEPNSPSFSMLS-LVNSVGPIVATYHSAaTDSLALKLATPFLRKYLER-IRGGIAVSEVARRwQVEQLGGDP---VL 165
Cdd:cd03807 83 VHTWMYHADLIGGLAaKLAGGVKVIWSVRSS-NIPQRLTRLVRKLCLLLSKfSPATVANSSAVAE-FHQEQGYAKnkiVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 166 IPNGVRVGDF--ESCPAASSLPEIPPRREGfYRLVFLGRFDEsRKGFDVLLDALPAIRAEIPQLEVCVVGDGDV---AAA 240
Cdd:cd03807 161 IYNGIDLFKLspDDASRARARRRLGLAEDR-RVIGIVGRLHP-VKDHSDLLRAAALLVETHPDLRLLLVGRGPErpnLER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 241 RRKAGRNADVLHFVGRLSEdaKASILADADAYIAPQRGgESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHYGLhFENG 320
Cdd:cd03807 239 LLLELGLEDRVHLLGERSD--VPALLPAMDIFVLSSRT-EGFPNALLEAMACGLPVVATDVGGAAELVDDGTGFL-VPAG 314
|
330 340
....*....|....*....|....*.
gi 740843613 321 NSVDLADAVVRLLtqpKLGEELRALG 346
Cdd:cd03807 315 DPQALADAIRALL---EDPEKRARLG 337
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
255-370 |
8.77e-23 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 92.36 E-value: 8.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 255 GRLS-----EDAKASILADADAYIAPQRGgESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHYGLHFENGNSVDLADAV 329
Cdd:COG0438 2 GRLVprkglDLLLEALLAAADVFVLPSRS-EGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAI 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 740843613 330 VRLLTQPKLGEELRALGHKRA-WEYDWSQVADGVLRVYDTVR 370
Cdd:COG0438 81 LRLLEDPELRRRLGEAARERAeERFSWEAIAERLLALYEELL 122
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
15-170 |
1.10e-21 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 90.67 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 15 GGVQAHAIDLCEEFIRRGHEVSLIGPASvqADVPDFVVRGGAAIPIPYNGSVARLSFGPRTSRRVRTWIEEGSFDILHIH 94
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGG--PGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 95 EPNSPSFSMLSLVNSVG-PIVATYHSAATD--------SLALKLATPFLRKYLERIRGGIAVSEVARRWQVEQLGGDP-- 163
Cdd:pfam13439 79 SPFPLGLAALAARLRLGiPLVVTYHGLFPDykrlgarlSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVPPek 158
|
....*...
gi 740843613 164 -VLIPNGV 170
Cdd:pfam13439 159 iRVIPNGV 166
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
2-369 |
6.00e-21 |
|
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: 92.35 E-value: 6.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 2 RIGMVCPYSFDVP----GGVQAHAIDLCEEFIRRGHEVSLIGPASVQADVPDFVV--RGGAAIPIPYNGSVARLSFgprt 75
Cdd:cd03802 1 RIAQVSPPRGPVPpgkyGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSAPLVAVipRALRLDPIPQESKLAELLE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 76 srRVRTWIEEGSFDILHIHEPNsPSFSMLSLVNSvgPIVATYHSAAT-DSLALKLATPFlrkyleriRGGIAVSEVARRw 154
Cdd:cd03802 77 --ALEVQLRASDFDVIHNHSYD-WLPPFAPLIGT--PFVTTLHGPSIpPSLAIYAAEPP--------VNYVSISDAQRA- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 155 qvEQLGGDPVL-IPNGVRVGDFESCPaasslpeippRREGFyrLVFLGRFDESrKGFDVLLDAlpAIRAEIPqLEVcVVG 233
Cdd:cd03802 143 --ATPPIDYLTvVHNGLDPADYRFQP----------DPEDY--LAFLGRIAPE-KGLEDAIRV--ARRAGLP-LKI-AGK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 234 DGDVAAARRK-AGRNADVLHFVGRLSEDAKASILADADAYIAPQRGGESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGH 312
Cdd:cd03802 204 VRDEDYFYYLqEPLPGPRIEFIGEVGHDEKQELLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGE 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 740843613 313 YGlhFENGNSVDLADAVVRLLTQPklgeelRALGHKRAWE-YDWSQVADGVLRVYDTV 369
Cdd:cd03802 284 TG--FLVDSVEEMAEAIANIDRID------RAACRRYAEDrFSAARMADRYEALYRKV 333
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
89-369 |
3.62e-19 |
|
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: 87.77 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 89 DILHIHEPNSPSFSMLSLVNSVG--PIVATYH-------------------------------SAATDSLALKLatpFLR 135
Cdd:cd03825 53 DIIHLHWIHGGYLSLKALFKLLRrkPVVWTLHdmwpftggchypmecegwktgcgncpnlnsyPPAKKDLSRQL---FRR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 136 K-YLERIRGGIAVSevARRWQVEQLGGDPVL-------IPNGVRVGDFESCPAASSLP--EIPPRRegfyRLVFLG--RF 203
Cdd:cd03825 130 KrEALAKKRLTIVA--PSRWLADMVRRSPLLkglpvvvIPNGIDTEIFAPVDKAKARKrlGIPQDK----KVILFGaeSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 204 DESRKGFDVLLDALPAIrAEIPQLEVCVVGDGDVaaarRKAGRNADVLHFvGRLSEDAK-ASILADADAYIAPQRGgESF 282
Cdd:cd03825 204 TKPRKGFDELIEALKLL-ATKDDLLLVVFGKNDP----QIVILPFDIISL-GYIDDDEQlVDIYSAADLFVHPSLA-DNL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 283 GIVLVEAMAAGAPVISSDIDAFKLVLDDGHYGLHFENGNSVDLADAVVRLLTQPKLGEELRALGHKRA-WEYDWSQVADG 361
Cdd:cd03825 277 PNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAeNHFDQRVQAQR 356
|
....*...
gi 740843613 362 VLRVYDTV 369
Cdd:cd03825 357 YLELYKDL 364
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
112-346 |
4.79e-19 |
|
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: 87.51 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 112 PIVATYH-SAATDSLALKLATPFLRKYLERIR--------GGIAVSEVARRwqveqlggdpVLIPNGVRVGDFESCPAAS 182
Cdd:cd05844 106 PLVVTFHgFDITTSRAWLAASPGWPSQFQRHRralqrpaaLFVAVSGFIRD----------RLLARGLPAERIHVHYIGI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 183 SLPEIPPRREG--FYRLVFLGRFDEsRKGFDVLLDALPAIRAEIPQLEVCVVGDGDVAAARRKAGRNADVLHFVGRLSED 260
Cdd:cd05844 176 DPAKFAPRDPAerAPTILFVGRLVE-KKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAALGRVRFLGALPHA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 261 AKASILADADAYIAPQ---RGG--ESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHYGLHFENGNSVDLADAVVRLLTQ 335
Cdd:cd05844 255 EVQDWMRRAEIFCLPSvtaASGdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLAD 334
|
250
....*....|.
gi 740843613 336 PKLGEELRALG 346
Cdd:cd05844 335 RALADRMGGAA 345
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
194-317 |
1.91e-18 |
|
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 83.61 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 194 FYRLVFLGRFDEsRKGFDVLLDALPAIRAEIPQLEVCVVGDGD----VAAARRKAGRNADVLHFVGRLSEDAKASILADA 269
Cdd:cd01635 110 LADKVSVGRLVP-EKGIDLLLEALALLKARLPDLVLVLVGGGGereeEEALAAALGLLERVVIIGGLVDDEVLELLLAAA 188
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 740843613 270 DAYIAPqRGGESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHYGLHF 317
Cdd:cd01635 189 DVFVLP-SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
1-352 |
4.10e-14 |
|
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: 72.77 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 1 MRIGMVCPYSFdvpGGVQAHAIDLCEEFIRRGHEVSLIGpasvqADVPdFVVRGGAAIPIPYNGSV---ARLSFGPRT-- 75
Cdd:cd04962 1 MKIGIVCYPSY---GGSGVVATELGLELAERGHEVHFIS-----SAIP-FRLNLYSGNIFFHEVEVpnyPLFEYPPYTla 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 76 -SRRVRTWIEEGSFDILHIHE--PNSPSFSML-SLVNSVGPIVATYHsaATDSLAL---KLATPFLRKYLERIRGGIAVS 148
Cdd:cd04962 72 lASKIVEVAKEHKLDVLHAHYaiPHASCAYLArEILGEKIPIVTTLH--GTDITLVgydPSLQPAVRFSINKSDRVTAVS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 149 EVARRWQVEQLGGD-PV-LIPNGVRVGDFESCPAasslPEIPPRR---EGFYRLVFLGRFDESRKGFDVLlDALPAIRAE 223
Cdd:cd04962 150 SSLRQETYELFDVDkDIeVIHNFIDEDVFKRKPA----GALKRRLlapPDEKVVIHVSNFRPVKRIDDVV-RVFARVRRK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 224 IPQlEVCVVGDG-DVAAARRKA---GRNADVLhFVGRLSEDAKasILADADAYIAPQrGGESFGIVLVEAMAAGAPVISS 299
Cdd:cd04962 225 IPA-KLLLVGDGpERVPAEELArelGVEDRVL-FLGKQDDVEE--LLSIADLFLLPS-EKESFGLAALEAMACGVPVVSS 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 740843613 300 DIDAFKLVLDDGHYGLHFENGNSVDLADAVVRLLTQPKLGEELRALGHKRAWE 352
Cdd:cd04962 300 NAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAE 352
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
15-169 |
2.29e-12 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 64.34 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 15 GGVQAHAIDLCEEFIRRGHEVSLIGPASvQADVPDFVVRGGAAIPIPYnGSVARLSFGPRTSRRVRTWIEEGSFDILHIH 94
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGG-PPGRPELVGDGVRVHRLPV-PPRPSPLADLAALRRLRRLLRAERPDVVHAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 95 EPNSPSFSMLSLVNSVGPIVATYHSAATD---SLALKLATPFLRKYLERIRGGIAVSEVARRwQVEQLGGDP---VLIPN 168
Cdd:pfam13579 79 SPTAGLAARLARRRRGVPLVVTVHGLALDygsGWKRRLARALERRLLRRADAVVVVSEAEAE-LLRALGVPAarvVVVPN 157
|
.
gi 740843613 169 G 169
Cdd:pfam13579 158 G 158
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
208-366 |
2.86e-12 |
|
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.
Pssm-ID: 340849 [Multi-domain] Cd Length: 370 Bit Score: 67.41 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 208 KGFDVLLDALPAIRAEIPQLEVCVVGdGDVAAARRKAGRNA-----------DVLHFVGR-LSEDAKASILADADAYIAP 275
Cdd:cd03822 200 KGLEILLEALPELKAEFPDVRLVIAG-ELHPSLARYEGERYrkaaieelglqDHVDFHNNfLPEEEVPRYISAADVVVLP 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 276 -QRGGESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHyGLHFENGNSVDLADAVVRLLTQPKLGEELRALGHKRAWEYD 354
Cdd:cd03822 279 yLNTEQSSSGTLSYAIACGKPVISTPLRHAEELLADGR-GVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMT 357
|
170
....*....|..
gi 740843613 355 WSQVADGVLRVY 366
Cdd:cd03822 358 WESIADRYLRLF 369
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
166-360 |
3.32e-12 |
|
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: 67.39 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 166 IPNGVRVGDFESCPAAS-SLPEIPPRREGFYRLVFLGRFDESRKGFDVLLDALPAIRAEIPQLEVCVVGDGDV------- 237
Cdd:cd03818 184 IHDGVDTDRLAPDPAARlRLLNGTELKAGDPVITYVARNLEPYRGFHVFMRALPRIQARRPDARVVVVGGDGVsygsppp 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 238 --AAARRKAGRNADV----LHFVGRLSEDAKASILADADAYIAPQRGG-ESFGivLVEAMAAGAPVISSDIDAFKLVLDD 310
Cdd:cd03818 264 dgGSWKQKMLAELGVdlerVHFVGKVPYDQYVRLLQLSDAHVYLTYPFvLSWS--LLEAMACGCPVIGSDTAPVREVIRD 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740843613 311 GHYGLHFENGNSVDLADAVVRLLTQPKLGEELRALGHKRAWEYDWSQVAD 360
Cdd:cd03818 342 GRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCL 391
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
179-297 |
8.93e-12 |
|
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: 65.77 E-value: 8.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 179 PAASSLPEIPPRREGFYrlVFLGRFdESRKGFDVLLDALpairAEIPqLEVCVVGDG-DVAAARRKAGRNadvLHFVGRL 257
Cdd:cd03804 186 PVDTDAFAPAADKEDYY--LTASRL-VPYKRIDLAVEAF----NELP-KRLVVIGDGpDLDRLRAMASPN---VEFLGYQ 254
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 740843613 258 SEDAKASILADADAYIAPqrGGESFGIVLVEAMAAGAPVI 297
Cdd:cd03804 255 PDEVLKELLSKARAFVFA--AEEDFGIVPVEAQACGTPVI 292
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
145-353 |
1.40e-11 |
|
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: 65.43 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 145 IAVSEVARRWQVEqLGGDP---VLIPNGVRVGDFescpaaSSLPEIPPRREGFyRLVFLGRFDESrKGFDVLLDALPAIR 221
Cdd:cd03813 249 ISLYEGNRRRQIR-LGADPdktRVIPNGIDIQRF------APAREERPEKEPP-VVGLVGRVVPI-KDVKTFIRAFKLVR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 222 AEIPQLEVCVVG--DGDVAAArrkagrnADVLHFVGRLSEDAKASILAD---ADAYiaPQRG-------GESFGIVLVEA 289
Cdd:cd03813 320 RAMPDAEGWLIGpeDEDPEYA-------QECKRLVASLGLENKVKFLGFqniKEYY--PKLGllvltsiSEGQPLVILEA 390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740843613 290 MAAGAPVISSDIDAFKLVLDD-----GHYGLHFENGNSVDLADAVVRLLTQPKLGEELRALGHKRAWEY 353
Cdd:cd03813 391 MASGVPVVATDVGSCRELIYGaddalGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKY 459
|
|
| thiol_BshA |
TIGR03999 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, ... |
1-369 |
1.20e-10 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, a glycosyltransferase required for bacillithiol biosynthesis. This enzyme combines UDP-GlcNAc and L-malate to form N-acetyl-alpha-D-glucosaminyl L-malate synthase. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
Pssm-ID: 274914 [Multi-domain] Cd Length: 374 Bit Score: 62.24 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 1 MRIGMVCPYSFdvpGGVQAHAIDLCEEFIRRGHEVSLIGpasvqADVPdfvVRGGAAIPIPYNGSV-----ARLSFGPRT 75
Cdd:TIGR03999 1 MKIGITCYPTY---GGSGVVATELGKALAERGHEVHFIT-----SSQP---FRLEKFHPNIFFHEVevnqyPLFQYPPYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 76 ---SRRVRTWIEEGSFDILHIHE--PNSPSF----SMLSLVNSVGPIVATYHsaATDsLALKLATPFlrkYLERIRGGI- 145
Cdd:TIGR03999 70 lalASKIAEVAKEEKLDLLHVHYaiPHAIAAylarQMLGKEGIDIPIVTTLH--GTD-ITLVGADPS---FKPAVRFSIe 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 146 ------AVSEVARR--WQVEQLGGDPVLIPNGVRVGDF-----ESCPAASSLPEipprreGFYRLVFLGRFDESRKGFDV 212
Cdd:TIGR03999 144 ksdgvtAVSESLKEetYELFDIDKPIEVIPNFVDTDRYrrkndPALKRKLGAPE------DEKVLIHISNFRPVKRVEDV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 213 LlDALPAIRAEIPQlEVCVVGDG-DVAAARRKA---GRNADVLhFVGRLseDAKASILADADAYIAPQrGGESFGIVLVE 288
Cdd:TIGR03999 218 I-EVFARVQQEVPA-KLLLVGDGpERSPAEQLVrelGLTDRVL-FLGKQ--DDVAELLSISDLFLLPS-EKESFGLAALE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 289 AMAAGAPVISSDIDAFKLVLDDGHYGLHFENGNSVDLADAVVRLLTQPKLGEELRALGHKRAWE-YDWSQVADGVLRVYD 367
Cdd:TIGR03999 292 AMACGVPVIASNAGGIPEVVEHGVTGFLCDVGDVETMAEYAISLLEDEELLQRFSAAARERAKErFDSEKIVPQYEALYR 371
|
..
gi 740843613 368 TV 369
Cdd:TIGR03999 372 RL 373
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
197-355 |
2.65e-10 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 61.65 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 197 LVFLGRFdesrkGFDVLLDALPAIRAEIPQLEVCVVGDGDVAAARRK--AGRNAdvlHFVGRLSEDAKASILADADAYIA 274
Cdd:PLN02871 266 IVYVGRL-----GAEKNLDFLKRVMERLPGARLAFVGDGPYREELEKmfAGTPT---VFTGMLQGDELSQAYASGDVFVM 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 275 PQRGgESFGIVLVEAMAAGAPVISSDIDAFKLVLDD---GHYGLHFENGnsvDLADAVVR---LLTQPKLGEELRALGHK 348
Cdd:PLN02871 338 PSES-ETLGFVVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPG---DVDDCVEKletLLADPELRERMGAAARE 413
|
....*..
gi 740843613 349 RAWEYDW 355
Cdd:PLN02871 414 EVEKWDW 420
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
2-369 |
3.26e-10 |
|
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: 61.10 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 2 RIGMVCPYSFDVPGGVQAHAIDLCEEFIRRGHEVSLIgpasVQADVPDFVVR---GGAA---IPIP--YNGSVARLSFGp 73
Cdd:cd03796 1 RICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVI----THAYGNRVGVRyltNGLKvyyLPFKvfYNQSTLPTLFS- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 74 rTSRRVRTWIEEGSFDILHIHEpnspSFSMLSL-----VNSVG-PIVATYHS----AATDSLalkLATPFLRKYLERIRG 143
Cdd:cd03796 76 -TFPLLRNILIRERIQIVHGHQ----AFSSLAHealfhARTLGlKTVFTDHSlfgfADASSI---LTNKLLRFSLADIDH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 144 GIAVSEVARRWQVEQLGGDP---VLIPNGVRVGDFESCPAASSLPEIpprregfyRLVFLGRFDEsRKGFDVLLDALPAI 220
Cdd:cd03796 148 VICVSHTSKENTVLRASLDPrivSVIPNAVDSSDFTPDPSKPDPNKI--------TIVVISRLVY-RKGIDLLVGIIPRI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 221 RAEIPQLEVCVVGDG---DVAAARRKAGRNADVLHFVGRLSEDAKASILADADAYIAPQRgGESFGIVLVEAMAAGAPVI 297
Cdd:cd03796 219 CKKHPNVRFIIGGDGpkrIELEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSL-TEAFCIAIVEAASCGLLVV 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740843613 298 SSDIDAFKLVLDDGHygLHFENGNSVDLAD----AVVRLLTQPKLGEELralgHKRAWE-YDWSQVADGVLRVYDTV 369
Cdd:cd03796 298 STRVGGIPEVLPPDM--ILLAEPDPEDIVRkleeAISILRTGKHDPWSF----HNRVKKmYSWEDVARRTEKVYDRI 368
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
273-360 |
4.47e-09 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 52.99 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 273 IAPQRGGESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHYGLHFENGNsvDLADAVVRLLTQPKLGEELRALGHKRAW- 351
Cdd:pfam13524 3 LNPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYRDPE--ELAEKIRYLLEHPEERRAIAAAGRERVLa 80
|
....*....
gi 740843613 352 EYDWSQVAD 360
Cdd:pfam13524 81 EHTYAHRAE 89
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
28-354 |
7.69e-09 |
|
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: 56.69 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 28 FIRRGHEVSLIGPASVQADV--PDFvvrggaaipIPYNGSVARLSFgprtsrRVRTWIEEGSFDILHIH--EPNSPSFSM 103
Cdd:cd03799 24 LIDRGHEVDIYAVNPGDLVKrhPDV---------EKYNVPSLNLLY------AIVGLNKKGAYDIIHCQfgPLGALGALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 104 LSLVNSVGPIVATYHSAATdslalklaTPFLRKYlerirgGIAVSE-----------VARRWQVE--QLGGDPVLIpNGV 170
Cdd:cd03799 89 RRLKVLKGKLVTSFRGYDI--------SMYVILE------GNKVYPqlfaqgdlflpNCELFKHRliALGCDEKKI-IVH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 171 RVG-DFESCPAAsslpeipPRR---EGFYRLVFLGRFDEsRKGFDVLLDALPAIRAEIPQLEVCVVGDGDVAAARRKAGR 246
Cdd:cd03799 154 RSGiDCNKFRFK-------PRYlplDGKIRILTVGRLTE-KKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 247 NADVLHFVGRLSEDAKASI---LADADAYIAPQ---RGGESFGIV--LVEAMAAGAPVISSDIDAFKLVLDDGHYGLHFE 318
Cdd:cd03799 226 ELNIGDCVKLLGWKPQEEIieiLDEADIFIAPSvtaADGDQDGPPntLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVP 305
|
330 340 350
....*....|....*....|....*....|....*..
gi 740843613 319 NGNSVDLADAVVRLLTQPKLGEELRALGHKR-AWEYD 354
Cdd:cd03799 306 ERDAEAIAEKLTYLIEHPAIWPEMGKAGRARvEEEYD 342
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
197-366 |
1.73e-08 |
|
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: 56.03 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 197 LVFLGRFDEsRKGFDVLLDALPAIRAEIPQLeVcVVGDGDVA---AARRKAGRNADVLHFVGRLSEDAKASILADADAYI 273
Cdd:cd03791 297 FGFVGRLTE-QKGVDLILDALPELLEEGGQL-V-VLGSGDPEyeqAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 274 APQRgGESFGIVLVEAMAAGAPVISS----------DIDAFKLVLDdghyGLHFENGNSVDLADAVVRLLT---QPKLGE 340
Cdd:cd03791 374 MPSR-FEPCGLVQMYAMRYGTLPIVRrtggladtvfDYDPETGEGT----GFVFEDYDAEALLAALRRALAlyrNPELWR 448
|
170 180
....*....|....*....|....*.
gi 740843613 341 ELRALGHKRAWeyDWSQVADGVLRVY 366
Cdd:cd03791 449 KLQKNAMKQDF--SWDKSAKEYLELY 472
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
197-359 |
1.83e-08 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 55.57 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 197 LVFLGRFDESrKGFDVLLDALPAIRAEIPQLEVCVVGD------GDVAAARRK----AGRNADVLHFVGRLSEDAKASIL 266
Cdd:PRK15484 196 LLYAGRISPD-KGILLLMQAFEKLATAHSNLKLVVVGDptasskGEKAAYQKKvleaAKRIGDRCIMLGGQPPEKMHNYY 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 267 ADADAYIAPQRGGESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHYGLHFENGNSVD-LADAVVRLLTQPKLgEELRAL 345
Cdd:PRK15484 275 PLADLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLAEPMTSDsIISDINRTLADPEL-TQIAEQ 353
|
170
....*....|....*
gi 740843613 346 GHKRAWE-YDWSQVA 359
Cdd:PRK15484 354 AKDFVFSkYSWEGVT 368
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
128-369 |
2.00e-08 |
|
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.
Pssm-ID: 132132 [Multi-domain] Cd Length: 374 Bit Score: 55.50 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 128 KLATPFLRKYlerirggIAVSEVARRWQVEQLGGDP---VLIPNGVRVGDFEscPAASSLPEI-PPRREGFYRLVFL--G 201
Cdd:TIGR03088 131 RLYRPLIHHY-------VAVSRDLEDWLRGPVKVPPakiHQIYNGVDTERFH--PSRGDRSPIlPPDFFADESVVVGtvG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 202 RFdESRKGFDVLLDALPAIRAEIPQ----LEVCVVGDGDVAAARRKAGRNADVLHFVGRLSE-DAKASILADADAYIAPQ 276
Cdd:TIGR03088 202 RL-QAVKDQPTLVRAFALLVRQLPEgaerLRLVIVGDGPARGACEQMVRAAGLAHLVWLPGErDDVPALMQALDLFVLPS 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 277 RGgESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHYGLHFENGNSVDLADAVVRLLTQPKLGEELRALGHKRA-WEYDW 355
Cdd:TIGR03088 281 LA-EGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAeQQFSI 359
|
250
....*....|....
gi 740843613 356 SQVADGVLRVYDTV 369
Cdd:TIGR03088 360 NAMVAAYAGLYDQL 373
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
179-358 |
4.33e-07 |
|
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: 51.15 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 179 PAASSLPEIPPRREGF---YRLVFLGRFdESRKGFDVLLDALPAIRAEIPQLEVCVVGDGD---VAAARRKAGRNADVLH 252
Cdd:cd04949 142 PVGYVDQLDTAESNHErksNKIITISRL-APEKQLDHLIEAVAKAVKKVPEITLDIYGYGEereKLKKLIEELHLEDNVF 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 253 FVGRLSEDAKasILADADAYIAPQRGgESFGIVLVEAMAAGAPVISSDID----AFklvLDDGHYGLHFENGNSVDLADA 328
Cdd:cd04949 221 LKGYHSNLDQ--EYQDAYLSLLTSQM-EGFGLTLMEAIGHGLPVVSYDVKygpsEL---IEDGENGYLIEKNNIDALADK 294
|
170 180 190
....*....|....*....|....*....|
gi 740843613 329 VVRLLTQPKLGEELRALGHKRAWEYDWSQV 358
Cdd:cd04949 295 IIELLNDPEKLQQFSEESYKIAEKYSTENV 324
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
198-313 |
8.44e-06 |
|
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: 47.44 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 198 VFL--GRFDESrKGFDVLLDALPAIRAEIPQLEVCVVGDGdvaAARRKAGRNADVLHFVGRL----SEDAKASILADADA 271
Cdd:cd04951 190 VILnvGRLTEA-KDYPNLLLAISELILSKNDFKLLIAGDG---PLRNELERLICNLNLVDRVillgQISNISEYYNAADL 265
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 740843613 272 YIAPQRGgESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHY 313
Cdd:cd04951 266 FVLSSEW-EGFGLVVAEAMACERPVVATDAGGVAEVVGDHNY 306
|
|
| COG4641 |
COG4641 |
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]; |
187-353 |
1.02e-05 |
|
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443679 [Multi-domain] Cd Length: 303 Bit Score: 46.85 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 187 IPPRREGFYRLVFLG-RFDESRKGFDVLLDALPAIRaeipqleVCVVGDG-DVAAARRKAgrnadvlHFVGRLSEDAKAS 264
Cdd:COG4641 130 VPPEARFRYDVAFVGnYYPDRRARLEELLLAPAGLR-------LKIYGPGwPKLALPANV-------RRGGHLPGEEHPA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 265 ILADADAYIAPQRGGESFGIV---LVEAMAAGAPVISSDIDAFKLVLDDGHYGLHFENGNsvDLADAVVRLLTQPKLGEE 341
Cdd:COG4641 196 AYASSKITLNVNRMAASPDSPtrrTFEAAACGAFLLSDPWEGLEELFEPGEEVLVFRDGE--ELAEKLRYLLADPEERRA 273
|
170
....*....|..
gi 740843613 342 LRALGHKRAWEY 353
Cdd:COG4641 274 IAEAGRRRVLAE 285
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
202-349 |
4.89e-05 |
|
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: 45.00 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 202 RFDESrKGFDVLLDALPAIR--AEIPQLEVC---VVGDGDVAAARRKAGRNADvlhfvgrLSEDAKASILADADAYI-AP 275
Cdd:cd03792 205 RFDPS-KDPLGVIDAYKLFKrrAEEPQLVICghgAVDDPEGSVVYEEVMEYAG-------DDHDIHVLRLPPSDQEInAL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 276 QRGG---------ESFGIVLVEAMAAGAPVISSDIDAFKLVLDDGHYGLHFengNSVD-LADAVVRLLTQPKLGEELRAL 345
Cdd:cd03792 277 QRAAtvvlqlstrEGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLV---NSVEgAAVRILRLLTDPELRRKMGLA 353
|
....
gi 740843613 346 GHKR 349
Cdd:cd03792 354 AREH 357
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
20-140 |
1.12e-04 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 41.92 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 20 HAIDLCEEFIRRGHEVSLIGPASVQADVPdfVVRGGAAIPIPYNGSVARLSFgprTSRRVRTWIEEGSFDILHIHEPNSP 99
Cdd:pfam13477 12 HTLRWADALADRGYDVHVISSKGPAKDEL--IAEGIHVHRLKVPRKGPLGYL---KAFRLKKLIKKIKPDVVHVHYAKPY 86
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 740843613 100 SF--SMLSLVNSVGPIVATYHsaATDSLALKLATPFLRKYLER 140
Cdd:pfam13477 87 GLlaGLAARLSGFPPVVLSAW--GLDVYKFPNKSRLKKLLLKL 127
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
206-298 |
2.72e-04 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 42.78 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 206 SRKGFDVLLDALPAIRAEIPQLEVCVVGDGDV-----AAARRKAGRNADVLHFvgrlSEDAKASILADADAYIAPQRgGE 280
Cdd:PRK14099 306 WQKGLDLLLEALPTLLGEGAQLALLGSGDAELearfrAAAQAYPGQIGVVIGY----DEALAHLIQAGADALLVPSR-FE 380
|
90
....*....|....*....
gi 740843613 281 SFGIVLVEAMAAGA-PVIS 298
Cdd:PRK14099 381 PCGLTQLCALRYGAvPVVA 399
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
258-349 |
7.22e-04 |
|
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: 41.42 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 258 SEDAKASILADADAYI-APQRggESFGIVLVEAMAAGAPVIssdidafklVLDDGhyG-----LHFENG-----NSVDLA 326
Cdd:cd03805 289 SDSQKEQLLSSALALLyTPSN--EHFGIVPLEAMYAGKPVI---------ACNSG--GpletvVEGVTGflcepTPEAFA 355
|
90 100
....*....|....*....|...
gi 740843613 327 DAVVRLLTQPKLGEELRALGHKR 349
Cdd:cd03805 356 EAMLKLANDPDLADRMGAAGRKR 378
|
|
| HEM4 |
pfam02602 |
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD ... |
157-296 |
2.41e-03 |
|
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD EC:4.2.1.75 also known as Hydroxymethylbilane hydrolyase (cyclizing) from eukaryotes, bacteria and archaea. This enzyme catalyzes the reaction: Hydroxymethylbilane <=> uroporphyrinogen-III + H(2)O. Some members of this family are multi-functional proteins possessing other enzyme activities related to porphyrin biosynthesis, such as Swiss:Q59294 with pfam00590, however the aligned region corresponds with the uroporphyrinogen-III synthase EC:4.2.1.75 activity only. Uroporphyrinogen-III synthase is the fourth enzyme in the heme pathway. Mutant forms of the Uroporphyrinogen-III synthase gene cause congenital erythropoietic porphyria in humans a recessive inborn error of metabolism also known as Gunther disease.
Pssm-ID: 426866 [Multi-domain] Cd Length: 230 Bit Score: 39.23 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 157 EQLGGDPVLIPngvrVGDFESCPAASSLPEIPPRREGFYRLVFLgrfdeSRKGFDVLLDAL---PAIRAEIPQLEVCVVG 233
Cdd:pfam02602 7 EALGAEPLELP----LIEIVPPEDRAELDEALKDLGEYDWLIFT-----SANAVRAFFEALkleGEDLRALANIKIAAVG 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740843613 234 DGDVAAARRkAGRNADvlhFVGRLSEDAKAsiLADA-DAYIAPQ-----RGGESFGIVLVEAMAAGAPV 296
Cdd:pfam02602 78 PKTARALRE-AGLTPD---FVPSEEGTAEG--LAEElAELLAGKrvlllRGNIGRDDLAEALRERGAEV 140
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
197-356 |
2.44e-03 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 39.69 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 197 LVFLGRFDEsRKGFDVLLDALPAIRAEipQLEVCVVGDGD---VAAARRKAGRNADVLHFVGRLSEdAKA-SILADADAY 272
Cdd:COG0297 298 IGMVSRLTE-QKGLDLLLEALDELLEE--DVQLVVLGSGDpeyEEAFRELAARYPGRVAVYIGYDE-ALAhRIYAGADFF 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 273 IAPQRgGESFGIVLVEAMAAGA-PVISS---------DIDAFklvlDDGHYGLHFENGNSVDLADAVVRLLT---QPKLG 339
Cdd:COG0297 374 LMPSR-FEPCGLNQMYALRYGTvPIVRRtggladtviDYNEA----TGEGTGFVFDEYTAEALLAAIRRALAlyrDPEAW 448
|
170
....*....|....*..
gi 740843613 340 EELRalghKRAWEYDWS 356
Cdd:COG0297 449 RKLQ----RNAMKQDFS 461
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
280-350 |
3.91e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 38.95 E-value: 3.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740843613 280 ESFGIVLVEAMAAGAPVISSDIDAFKL--VLDDGHYGLHFENGNSVDLADAVVRLLTQPKLG-EELRALGHKRA 350
Cdd:PLN02949 365 EHFGISVVEYMAAGAVPIAHNSAGPKMdiVLDEDGQQTGFLATTVEEYADAILEVLRMRETErLEIAAAARKRA 438
|
|
| GATase1_FGAR_AT |
cd01740 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
233-308 |
7.18e-03 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site
Pssm-ID: 153211 [Multi-domain] Cd Length: 238 Bit Score: 37.59 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843613 233 GDGDVAAARRKAGRNADVLHFVGRLSEDAKasiLADADAYIAPqrGGESFGIVL-VEAMAAGAPVISSDIDAF----KLV 307
Cdd:cd01740 11 CDRDMAYAFELAGFEAEDVWHNDLLAGRKD---LDDYDGVVLP--GGFSYGDYLrAGAIAAASPLLMEEVKEFaergGLV 85
|
.
gi 740843613 308 L 308
Cdd:cd01740 86 L 86
|
|
| |
