|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-387 |
7.32e-65 |
|
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: 210.86 E-value: 7.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 2 KILLIT-DYATPTGGAEILTIALRDGLRSRGHDARLFASSARPMNAESQADYRCFGTTSSFRTLLQTANFWAfgKLRQVL 80
Cdd:cd03801 1 KILLLSpELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLR--ELRPLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 81 AEFQPDVVHVTIFLTQLSPLILPLLKNVPSLYYAvwyrsicptgtkilpngtacqvkmgmpcyqnHCLPLWDWLPLMIQM 160
Cdd:cd03801 79 RLRKFDVVHAHGLLAALLAALLALLLGAPLVVTL-------------------------------HGAEPGRLLLLLAAE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 161 KLW----QRWSNAFNLFVAPSQAVKQHLMGAGINS---VEIVWHGTPIQPQRPPLTL-------PPTVAFAGRLVKEKGA 226
Cdd:cd03801 128 RRLlaraEALLRRADAVIAVSEALRDELRALGGIPpekIVVIPNGVDLERFSPPLRRklgippdRPVLLFVGRLSPRKGV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 227 EVLLKAIALVVNQIPEARLLLVG-DGAEKEVLKQQiiDLNITANVFMPGLMSRLEIEKLFSTAWVQVVPSIWpEPFGTVV 305
Cdd:cd03801 208 DLLLEALAKLLRRGPDVRLVIVGgDGPLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRY-EGFGLVV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 306 IEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKTHYSQDIYVDKFLEL 385
Cdd:cd03801 285 LEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDL 364
|
..
gi 505028579 386 YQ 387
Cdd:cd03801 365 YR 366
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
211-368 |
2.71e-51 |
|
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: 168.99 E-value: 2.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 211 PPTVAFAGRLVKEKGAEVLLKAIALVVNQIPEARLLLVGDGAEKEVLKQQIIDLNITANVFMPGLMSRLEIEKLFSTAWV 290
Cdd:pfam00534 2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505028579 291 QVVPSIWpEPFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREV 368
Cdd:pfam00534 82 FVLPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
2-386 |
6.25e-45 |
|
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: 158.65 E-value: 6.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 2 KILLITDYATP--TGGAEILTIALRDGLRSRGHDARLFASSARP---MNAESQADYRCFGTTSS--------FRTLLQTA 68
Cdd:cd03823 1 KILLVNSLYPPqrVGGAEISVHDLAEALVAEGHEVAVLTAGVGPpgqATVARSVVRYRRAPDETlplalkrrGYELFETY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 69 NFWAFGKLRQVLAEFQPDVVHVTiFLTQLSPLILPLLK--NVPSLYYAVWYRSICPTGTKILPNGtacqvkmgmpcyqnh 146
Cdd:cd03823 81 NPGLRRLLARLLEDFRPDVVHTH-NLSGLGASLLDAARdlGIPVVHTLHDYWLLCPRQFLFKKGG--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 147 clplwdwlplmiqmklwqrwsnafNLFVAPSQAVKQHLMGAGINSVEI--VWHGTPIQPQRPPLTLPPT----VAFAGRL 220
Cdd:cd03823 145 ------------------------DAVLAPSRFTANLHEANGLFSARIsvIPNAVEPDLAPPPRRRPGTerlrFGYIGRL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 221 VKEKGAEVLLKAIALVvnQIPEARLLLVGDGAEKEvLKQQIIDLNITANvfmpGLMSRLEIEKLFSTAWVQVVPSIWPEP 300
Cdd:cd03823 201 TEEKGIDLLVEAFKRL--PREDIELVIAGHGPLSD-ERQIEGGRRIAFL----GRVPTDDIKDFYEKIDVLVVPSIWPEP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 301 FGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKTHYSqdiyVD 380
Cdd:cd03823 274 FGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQ----AE 349
|
....*.
gi 505028579 381 KFLELY 386
Cdd:cd03823 350 EYLKLY 355
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
2-383 |
1.89e-43 |
|
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: 154.68 E-value: 1.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 2 KILLItdyATPTGGAEILTIALRDGLRSRGHDARLFASSARPMNAESQAD-YRCFGTTSSFRTLLQTANFWAFGKLRQVL 80
Cdd:cd03808 1 KILFI---VNVDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKELgVKVIDIPILRRGINPLKDLKALFKLYKLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 81 AEFQPDVVH-VTI----------FLTQLSPLI-----LPLLKNVPS----LYYAVwYRSICPTGTKILpngtacqvkmgm 140
Cdd:cd03808 78 KKEKPDIVHcHTPkpgilgrlaaRLAGVPKVIytvhgLGFVFTEGKllrlLYLLL-EKLALLFTDKVI------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 141 pcYQNHclplwDWLPLMIQMKlwqrwsnafnlFVAPSQAVKqhLMGAGINSveivwhgTPIQPQRPPL-TLPPTVAFAGR 219
Cdd:cd03808 145 --FVNE-----DDRDLAIKKG-----------IIKKKKTVL--IPGSGVDL-------DRFQYSPESLpSEKVVFLFVAR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 220 LVKEKGAEVLLKAIALVVNQIPEARLLLVGDGAEKEVLKQQIIDLNITANVFMPGLMSrlEIEKLFSTAWVQVVPSIWpE 299
Cdd:cd03808 198 LLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRS--DVPELLAESDVFVLPSYR-E 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 300 PFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKTHYSQDIYV 379
Cdd:cd03808 275 GLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVV 354
|
....
gi 505028579 380 DKFL 383
Cdd:cd03808 355 NKLL 358
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
2-386 |
1.92e-42 |
|
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: 152.06 E-value: 1.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 2 KILLITDYATPTGGAEILTIA-LRDGLRSRGHDARLFASSARPMNAESQAD------YRCFgTTSSFRTLLQtanfwAFG 74
Cdd:cd03814 1 RIALVTDTYHPQVNGVVRTLErLVDHLRRRGHEVRVVAPGPFDEAESAEGRvvsvpsFPLP-FYPEYRLALP-----LPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 75 KLRQVLAEFQPDVVHVTifltqlSPLILPLlknvpslyYAVWYRSIcptgtKILPNGTACQVKMgmPCYqnhcLPLWDWL 154
Cdd:cd03814 75 RVRRLIKEFQPDIIHIA------TPGPLGL--------AALRAARR-----LGLPVVTSYHTDF--PEY----LSYYTLG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 155 PLMIQMKLWQRW-SNAFNLFVAPSQAVKQHLMGAGINSVEIVWHGTPIQ---PQRPPLTLP--------PTVAFAGRLVK 222
Cdd:cd03814 130 PLSWLAWAYLRWfHNPFDTTLVPSPSIARELEGHGFERVRLWPRGVDTElfhPSRRDAALRrrlgppgrPLLLYVGRLAP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 223 EKGAEVLLKAIALVVNQIPeARLLLVGDGAEKEVLKQQiiDLNITanvFMpGLMSRLEIEKLFSTAWVQVVPSIwPEPFG 302
Cdd:cd03814 210 EKNLEALLDADLPLAASPP-VRLVVVGDGPARAELEAR--GPDVI---FT-GFLTGEELARAYASADVFVFPSR-TETFG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 303 TVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKThYSQDIYVDKF 382
Cdd:cd03814 282 LVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAER-YSWEAFLDNL 360
|
....
gi 505028579 383 LELY 386
Cdd:cd03814 361 LDYY 364
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
2-368 |
1.33e-40 |
|
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: 147.12 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 2 KILLITDyATPTGGAEILTIALRDGLRSRGHDARLFASSA-RPMNAESQADYRCFGTTSSFRTLLQTANFWAFGKLRQVL 80
Cdd:cd03811 1 KILFVIP-SLSGGGAERVLLNLANALDKRGYDVTLVLLRDeGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 81 AEFQPDVVHVTIFLtqlsplilpllknvpslyYAVWYRSICPTGTKILpngtacqvkmgmpcYQNHCLPLWDWLPLMIQM 160
Cdd:cd03811 80 KRAKPDVVISFLGF------------------ATYIVAKLAAARSKVI--------------AWIHSSLSKLYYLKKKLL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 161 KLWQRWSNAfNLFVAPSQAVKQHLMGAGINSVE--------IVWHGTPIQPQRPPLTLP---PTVAFAGRLVKEKGAEVL 229
Cdd:cd03811 128 LKLKLYKKA-DKIVCVSKGIKEDLIRLGPSPPEkieviynpIDIDRIRALAKEPILNEPedgPVILAVGRLDPQKGHDLL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 230 LKAIALVVNQIPEARLLLVGDGAEKEVLKQQIIDLNITANVFMPGLMSrlEIEKLFSTAWVQVVPSIWpEPFGTVVIEAM 309
Cdd:cd03811 207 IEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGLAERVIFLGFQS--NPYPYLKKADLFVLSSRY-EGFPNVLLEAM 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505028579 310 IRGTAVIVSASGGLPEIVQNNETGLIVPPGN---YQVLAAALLRILQNRELAEQMGKKAREV 368
Cdd:cd03811 284 ALGTPVVSTDCPGPREILDDGENGLLVPDGDaaaLAGILAALLQKKLDAALRERLAKAQEAV 345
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
2-384 |
4.13e-40 |
|
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: 145.46 E-value: 4.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 2 KILLITDYATPTGGAEILTIALRDGLRSRGHDARLFASSARPMNA----ESQADYRCFGTTSSFRTLLQTANFWAFGKLR 77
Cdd:cd03820 1 KIAIVIPSISNAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPfyelDDNIKIKNLGDRKYSHFKLLLKYFKKVRRLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 78 QVLAEFQPDVVhVTIFLTQLSplILPLLKNvPSLYYaVWYRsicptgtkilpngtacqvkmgMPCYQNHCLPLWDWLplm 157
Cdd:cd03820 81 KYLKNNKPDVV-ISFRTSLLT--FLALIGL-KSKLI-VWEH---------------------NNYEAYNKGLRRLLL--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 158 iQMKLWQRwsnaFNLFVAPSQAVKQHLMGAGINSVEIVWHgtpiqpqrpPLTLPPT----------VAFAGRLVKEKGAE 227
Cdd:cd03820 132 -RRLLYKR----ADKIVVLTEADKLKKYKQPNSNVVVIPN---------PLSFPSEepstnlkskrILAVGRLTYQKGFD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 228 VLLKAIALVVNQIPEARLLLVGDGAEKEVLKQQIIDLNITANVFMPGlmSRLEIEKLFSTAWVQVVPSIWpEPFGTVVIE 307
Cdd:cd03820 198 LLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLG--PTKNIAEEYANSSIFVLSSRY-EGFPMVLLE 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505028579 308 AMIRGTAVIVSAS-GGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKtHYSQDIYVDKFLE 384
Cdd:cd03820 275 AMAYGLPIISFDCpTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAE-RFSIEKIIKQWEE 351
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
2-389 |
7.53e-40 |
|
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: 145.50 E-value: 7.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 2 KILLITD-YATPTGGAEILTIALRDGLRSRGHDARLFASSarPMNAESQADYRcfgTTSSFRTLLQTAN--FWAFGKLRQ 78
Cdd:cd03817 1 KIAIFTDtYLPQVNGVATSVRNLARALEKRGHEVYVITPS--DPGAEDEEEVV---RYRSFSIPIRKYHrqHIPFPFKKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 79 V---LAEFQPDVVHvtiflTQlSPLILPLLknvpslyyavwyrsicptGTKIlpngtacQVKMGMPC-YQNHcLPLWDWL 154
Cdd:cd03817 76 VidrIKELGPDIIH-----TH-TPFSLGKL------------------GLRI-------ARKLKIPIvHTYH-TMYEDYL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 155 PLMIQMKLWQRW---------SNAFNLFVAPSQAVKQHLMGAGINS-VEIVWHGTPIQP--------QRPPLTLPPT--- 213
Cdd:cd03817 124 HYIPKGKLLVKAvvrklvrrfYNHTDAVIAPSEKIKDTLREYGVKGpIEVIPNGIDLDKfekplnteERRKLGLPPDepi 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 214 VAFAGRLVKEKGAEVLLKAIALVVNQiPEARLLLVGDGAEKEVLKQQIIDLNITANVFMPGLMSRLEIEKLFSTAWVQVV 293
Cdd:cd03817 204 LLYVGRLAKEKNIDFLLRAFAELKKE-PNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 294 PSIwPEPFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNyQVLAAALLRILQNRELAEQMGKKAREVAKTHY 373
Cdd:cd03817 283 AST-TETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPND-ETLAEKLLHLRENLELLRKLSKNAEISAREFA 360
|
410
....*....|....*.
gi 505028579 374 sqdiYVDKFLELYQNL 389
Cdd:cd03817 361 ----FAKSVEKLYEEV 372
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
12-389 |
1.24e-39 |
|
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.
Pssm-ID: 340828 [Multi-domain] Cd Length: 376 Bit Score: 144.83 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 12 PTGGAEILTIALrdGLRSRGHDARLFASSARPMNAESQADYRCFGTTSSFRTLLQTANFW-----------AFGKLRQVL 80
Cdd:cd03798 14 PGRGIFVRRQVR--ALSRRGVDVEVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPrlrllaplrapSLAKLLKRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 81 AEFQPDVVHVtIFLTqlsplilpllknvPSLYYAVWYR--SICPTGTKILpnGTACQVKMGMPcyqnhclplwdwLPLMI 158
Cdd:cd03798 92 RRGPPDLIHA-HFAY-------------PAGFAAALLArlYGVPYVVTEH--GSDINVFPPRS------------LLRKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 159 QMKLWQRWSNAFnlFVAPSQAVKQHLMGAGINSVEIVWHGTPI---QPQRPPLTLP---PTVAFAGRLVKEKGAEVLLKA 232
Cdd:cd03798 144 LRWALRRAARVI--AVSKALAEELVALGVPRDRVDVIPNGVDParfQPEDRGLGLPldaFVILFVGRLIPRKGIDLLLEA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 233 IALVVNQIPEARLLLVGDGAEKEVLKQQIIDLNITANVFMPGLMSRLEIEKLFSTAWVQVVPSiWPEPFGTVVIEAMIRG 312
Cdd:cd03798 222 FARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPS-RHEGFGLVLLEAMACG 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505028579 313 TAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILqNRELAEQMGKKAREVAKTHYSQDIYVDKFLELYQNL 389
Cdd:cd03798 301 LPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRAL-AEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
198-383 |
3.03e-37 |
|
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: 138.91 E-value: 3.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 198 GTPIQPQRPPLTLP---PTVAFAGRLVKEKGAEVLLKAIALVVNQIPEARLLLVG----DGAEKEVLKQQII--DLNITA 268
Cdd:cd03800 204 VDRAEARRARLLLPpdkPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGgpsdDPLSMDREELAELaeELGLID 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 269 NVFMPGLMSRLEIEKLFSTAWVQVVPSiWPEPFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAAL 348
Cdd:cd03800 284 RVRFPGRVSRDDLPELYRAADVFVVPS-LYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAAL 362
|
170 180 190
....*....|....*....|....*....|....*
gi 505028579 349 LRILQNRELAEQMGKKAREVAKTHYSQDIYVDKFL 383
Cdd:cd03800 363 RRLLDDPALWQRLSRAGLERARAHYTWESVADQLL 397
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
3-367 |
1.64e-36 |
|
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: 135.95 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 3 ILLITDYAtPTGGAEILTIALRDGLRSRGHDArLFASSARPMNAESQADyrcfGTTSSFRTLLQTANFWAFGKLRQVLAE 82
Cdd:cd03819 1 ILMLTPAL-EIGGAETYILDLARALAERGHRV-LVVTAGGPLLPRLRQI----GIGLPGLKVPLLRALLGNVRLARLIRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 83 FQPDVVHVTifltqlsplilpllKNVPSLYYAVWYRSicpTGTKIlpngtacqvkmgmpCYQNHCLPlwdwlPLMIQMKL 162
Cdd:cd03819 75 ERIDLIHAH--------------SRAPAWLGWLASRL---TGVPL--------------VTTVHGSY-----LATYHPKD 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 163 WQRWSNAFNLFV-APSQAVKQHL---MGAGINSVEIVWHGTPIQPQRPPLTLP-----------PTVAFAGRLVKEKGAE 227
Cdd:cd03819 119 FALAVRARGDRViAVSELVRDHLieaLGVDPERIRVIPNGVDTDRFPPEAEAEeraqlglpegkPVVGYVGRLSPEKGWL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 228 VLLKAIALVVNQiPEARLLLVGDGAEKEVLKQQIIDLNITANVFMPGLmsRLEIEKLFSTAWVQVVPSIWpEPFGTVVIE 307
Cdd:cd03819 199 LLVDAAAELKDE-PDFRLLVAGDGPERDEIRRLVERLGLRDRVTFTGF--REDVPAALAASDVVVLPSLH-EEFGRVALE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 308 AMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKARE 367
Cdd:cd03819 275 AMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAAL 334
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
160-373 |
1.27e-34 |
|
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: 131.04 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 160 MKLWQRWSNAFNLFVAPSQAVKQHLMGAGINSVEIVWHGTPIQP----QRPPLTLPPTVAFAGRLVKEKGAEVLLKAIAL 235
Cdd:cd05844 134 QRHRRALQRPAALFVAVSGFIRDRLLARGLPAERIHVHYIGIDPakfaPRDPAERAPTILFVGRLVEKKGCDVLIEAFRR 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 236 VVNQIPEARLLLVGDGAEKEVLKQQIIDLnitANVFMPGLMSRLEIEKLFSTAWVQVVPSIWP-----EPFGTVVIEAMI 310
Cdd:cd05844 214 LAARHPTARLVIAGDGPLRPALQALAAAL---GRVRFLGALPHAEVQDWMRRAEIFCLPSVTAasgdsEGLGIVLLEAAA 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505028579 311 RGTAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKTHY 373
Cdd:cd05844 291 CGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQF 353
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
211-354 |
3.42e-34 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 123.39 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 211 PPTVAFAGRLVKE-KGAEVLLKAIALVVNQIPEARLLLVGDGAEKEvLKQQIidLNITANVFMPGlmSRLEIEKLFSTAW 289
Cdd:pfam13692 1 RPVILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEE-LEELA--AGLEDRVIFTG--FVEDLAELLAAAD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505028579 290 VQVVPSIWpEPFGTVVIEAMIRGTAVIVSASGGLPEIVQnNETGLIVPPGNYQVLAAALLRILQN 354
Cdd:pfam13692 76 VFVLPSLY-EGFGLKLLEAMAAGLPVVATDVGGIPELVD-GENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-383 |
9.21e-33 |
|
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: 126.69 E-value: 9.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 2 KILLITDYATPTGGAE---ILTIALRdgLRSRGHDARLFASSARPMNAESQADY--------------RCFGTTSSFRTL 64
Cdd:cd03794 1 KILLISQYYPPPKGAAaarVYELAKE--LVRRGHEVTVLTPSPNYPLGRIFAGAtetkdgirvirvklGPIKKNGLIRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 65 LQTANFWAFGKLRQVLAEFQPDVVHVT--IFLTQLSPLILPLLKNVPSLY--YAVWYRSIcptgtkilpngtacqVKMGM 140
Cdd:cd03794 79 LNYLSFALAALLKLLVREERPDVIIAYspPITLGLAALLLKKLRGAPFILdvRDLWPESL---------------IALGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 141 pcyqnhcLPLWDWLPLmiqMKLWQRWS-NAFNLFVAPSQAVKQHLMGAGINS--VEIVWHG--------TPIQPQRPPLT 209
Cdd:cd03794 144 -------LKKGSLLKL---LKKLERKLyRLADAIIVLSPGLKEYLLRKGVPKekIIVIPNWadleefkpPPKDELRKKLG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 210 LPP--TVAFAGRLVKEKGAEVLLKAIALvVNQIPEARLLLVGDGAEKEVLKQQIIDLNITaNVFMPGLMSRLEIEKLFST 287
Cdd:cd03794 214 LDDkfVVVYAGNIGKAQGLETLLEAAER-LKRRPDIRFLFVGDGDEKERLKELAKARGLD-NVTFLGRVPKEEVPELLSA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 288 AWVQVVP-SIWPEPFGTV---VIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGK 363
Cdd:cd03794 292 ADVGLVPlKDNPANRGSSpskLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGE 371
|
410 420
....*....|....*....|
gi 505028579 364 KAREVAKTHYSQDIYVDKFL 383
Cdd:cd03794 372 NGRELAEEKFSREKLADRLL 391
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
276-390 |
2.48e-32 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 118.17 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 276 MSRLEIEK--------LFSTAWVQVVPSIWpEPFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAA 347
Cdd:COG0438 1 MGRLVPRKgldllleaLLAAADVFVLPSRS-EGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 505028579 348 LLRILQNRELAEQMGKKAREVAKTHYSQDIYVDKFLELYQNLC 390
Cdd:COG0438 80 ILRLLEDPELRRRLGEAARERAEERFSWEAIAERLLALYEELL 122
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
172-381 |
2.58e-31 |
|
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: 121.79 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 172 LFVAPSQAVKQHLMGAGINSVEIVWHGTPIQPQR---PPLTLPPT----VAFAGRLVKEKGAEVLLKAIALVVNQIPEAR 244
Cdd:cd03799 128 LFLPNCELFKHRLIALGCDEKKIIVHRSGIDCNKfrfKPRYLPLDgkirILTVGRLTEKKGLEYAIEAVAKLAQKYPNIE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 245 LLLVGDGAEKEVLKQQIIDLNITANVFMPGLMSRLEIEKLFSTAWVQVVPSIWP-----EPFGTVVIEAMIRGTAVIVSA 319
Cdd:cd03799 208 YQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTAadgdqDGPPNTLKEAMAMGLPVISTE 287
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505028579 320 SGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKTHYSQDIYVDK 381
Cdd:cd03799 288 HGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDINKLNDE 349
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
2-379 |
9.99e-31 |
|
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: 120.46 E-value: 9.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 2 KILLITDYATPT-GGAEILTIALRDGLRSRGHDARLFAssarpMNAESQADYRCFGTTSSFRT------LLQTANFWAFG 74
Cdd:cd03795 1 KVLHVFKFYYPDiGGIEQVIYDLAEGLKKKGIEVDVLC-----FSKEKETPEKEENGIRIHRVksflnvASTPFSPSYIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 75 KLRQVLAEfqPDVVHVTifltqlSPL----ILPLLKNVPSLYYAVWYRSIcptgtkilpngtacqVKmgmpcyQNHCLPL 150
Cdd:cd03795 76 RFKKLAKE--YDIIHYH------FPNpladLLLFFSGAKKPVVVHWHSDI---------------VK------QKKLLKL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 151 WDwlPLMIqmklwqRWSNAFNLFVAPSQ------------AVKQHLMGAGINSVEIVWHGTPIQPQRPPLTLPPTVAFAG 218
Cdd:cd03795 127 YK--PLMT------RFLRRADRIIATSPnyvetsptlrefKNKVRVIPLGIDKNVYNIPRVDFENIKREKKGKKIFLFIG 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 219 RLVKEKGAEVLLKAIalvvnQIPEARLLLVGDGAEKEVLKQQIiDLNITANVFMPGLMSRLEIEKLFSTAWVQVVPSIW- 297
Cdd:cd03795 199 RLVYYKGLDYLIEAA-----QYLNYPIVIGGEGPLKPDLEAQI-ELNLLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVLr 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 298 PEPFGTVVIEAMIRGTAVIVSA-SGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKTHYSQD 376
Cdd:cd03795 273 SEAFGIVLLEAMMCGKPVISTNiGTGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAE 352
|
...
gi 505028579 377 IYV 379
Cdd:cd03795 353 KMK 355
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
234-389 |
9.75e-28 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340859 [Multi-domain] Cd Length: 370 Bit Score: 112.45 E-value: 9.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 234 ALVVNQIPeARLLLVGDGAEKEVLKQQIIDLNITANVFMPGlmSRLEIEKLFSTAWVQVVPSiWPEPFGTVVIEAMIRGT 313
Cdd:cd04962 219 ARVRRKIP-AKLLLVGDGPERVPAEELARELGVEDRVLFLG--KQDDVEELLSIADLFLLPS-EKESFGLAALEAMACGV 294
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505028579 314 AVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKTHYSQDIYVDKFLELYQNL 389
Cdd:cd04962 295 PVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
182-386 |
1.91e-27 |
|
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: 113.20 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 182 QHLMGAGINSVEIVWHGTPIQPQRPPLTL-----PPTVAFAGRLVKEKGAEVLLKAIALVVNQIPEARLLLVGDGAEKEV 256
Cdd:cd03813 259 QIRLGADPDKTRVIPNGIDIQRFAPAREErpekePPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIGPEDEDPE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 257 L----KQQIIDLNITANVFMPGLMSRLEIeklFSTAWVQVVPSIwPEPFGTVVIEAMIRGTAVIVSASGGLPEIV----- 327
Cdd:cd03813 339 YaqecKRLVASLGLENKVKFLGFQNIKEY---YPKLGLLVLTSI-SEGQPLVILEAMASGVPVVATDVGSCRELIygadd 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505028579 328 QNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKTHYSQDIYVDKFLELY 386
Cdd:cd03813 415 ALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLY 473
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
2-386 |
5.01e-27 |
|
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: 110.10 E-value: 5.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 2 KILLITDYATPtGGAEILTIALRDGLRSRGHDARLFASSAR-PMNAE---SQADYRCFGTTS--SFRTLLqtanfwafgK 75
Cdd:cd03807 1 KVAHVITGLNV-GGAETMLLRLLEHMDKSRFEHVVISLTGDgVLGEEllaAGVPVVCLGLSSgkDPGVLL---------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 76 LRQVLAEFQPDVVHVTIFLTQLSPLILPLLKNVPSLYYAVwyrsicptgtkilpngtacqvkmgmpcyqnHCLPLWDWLP 155
Cdd:cd03807 71 LAKLIRKRNPDVVHTWMYHADLIGGLAAKLAGGVKVIWSV------------------------------RSSNIPQRLT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 156 LMIqMKLWQRWSNAFNLFVAPSQAVKQHLMGAGINSVEIV----------WHGTPIQPQRPPLTLP-----PTVAFAGRL 220
Cdd:cd03807 121 RLV-RKLCLLLSKFSPATVANSSAVAEFHQEQGYAKNKIVviyngidlfkLSPDDASRARARRRLGlaedrRVIGIVGRL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 221 VKEKGAEVLLKAIALVVNQIPEARLLLVGDGAEKEVLKQQIIDLNITANVF-------MPGLMSRLEIeklFstawvqVV 293
Cdd:cd03807 200 HPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERLLLELGLEDRVHllgersdVPALLPAMDI---F------VL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 294 PSIWpEPFGTVVIEAMIRGTAVIVSASGGLPEIVqNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKTHY 373
Cdd:cd03807 271 SSRT-EGFPNALLEAMACGLPVVATDVGGAAELV-DDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEF 348
|
410
....*....|...
gi 505028579 374 SQDIYVDKFLELY 386
Cdd:cd03807 349 SIDAMVRRYETLY 361
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
173-389 |
5.19e-27 |
|
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: 110.58 E-value: 5.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 173 FVAPSQAVKQHLMGA-GI--NSVEIVWHG------TPIQPQRPPLTLPP-------TVAFAGRLVKEKGAEVLLKAIALV 236
Cdd:TIGR03088 140 YVAVSRDLEDWLRGPvKVppAKIHQIYNGvdterfHPSRGDRSPILPPDffadesvVVGTVGRLQAVKDQPTLVRAFALL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 237 VNQIPE----ARLLLVGDGAEKEVLKQQIIDLNITANVFMPGlmSRLEIEKLFSTAWVQVVPSIwPEPFGTVVIEAMIRG 312
Cdd:TIGR03088 220 VRQLPEgaerLRLVIVGDGPARGACEQMVRAAGLAHLVWLPG--ERDDVPALMQALDLFVLPSL-AEGISNTILEAMASG 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505028579 313 TAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKTHYSQDIYVDKFLELYQNL 389
Cdd:TIGR03088 297 LPVIATAVGGNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSINAMVAAYAGLYDQL 373
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
14-389 |
8.25e-27 |
|
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: 109.30 E-value: 8.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 14 GGAEILTIALRDGLRSRGHDARLFASsarpmnAESQADYRCFGTTSSFRTLLQTANFWAFGKLRQVLAEFQP----DVVH 89
Cdd:cd03802 18 GGTELVVSALTEGLVRRGHEVTLFAP------GDSHTSAPLVAVIPRALRLDPIPQESKLAELLEALEVQLRasdfDVIH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 90 VTIFLTQLSPLILPLLKNVPSLyyavwyrsicpTGTKILPNGTACQvkmgmpcyqnhclplwdwlplmiqmklwqrwSNA 169
Cdd:cd03802 92 NHSYDWLPPFAPLIGTPFVTTL-----------HGPSIPPSLAIYA-------------------------------AEP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 170 FNLFVAPSQAVKQHLMGagINSVEIVWHGTPIQPQRPPLTLPPTVAFAGRLVKEKGAEVllkAIALVVnqipEARLLLVG 249
Cdd:cd03802 130 PVNYVSISDAQRAATPP--IDYLTVVHNGLDPADYRFQPDPEDYLAFLGRIAPEKGLED---AIRVAR----RAGLPLKI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 250 DG-AEKEVLKQQIIDLNITANVFMPGLMSRLEIEKLFSTAWVQVVPSIWPEPFGTVVIEAMIRGTAVIVSASGGLPEIVQ 328
Cdd:cd03802 201 AGkVRDEDYFYYLQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQ 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505028579 329 NNETGLIVPPgnYQVLAAALLRILQ-NRelaeqmgKKAREVAKTHYSQDIYVDKFLELYQNL 389
Cdd:cd03802 281 HGETGFLVDS--VEEMAEAIANIDRiDR-------AACRRYAEDRFSAARMADRYEALYRKV 333
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
80-370 |
1.53e-25 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 107.49 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 80 LAEFQPDVVHVTifltqlSPLILpllknvpsLYYAVWYRSicptgtkilpngtacqvKMGMP---CYQNHC---LPLWDW 153
Cdd:PLN02871 140 VARFKPDLIHAS------SPGIM--------VFGALFYAK-----------------LLCVPlvmSYHTHVpvyIPRYTF 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 154 LPLMIQMKLWQR-WSNAFNLFVAPSQAVKQHLMGAGINSVE--IVWHG--------------------TPIQPQRPpltl 210
Cdd:PLN02871 189 SWLVKPMWDIIRfLHRAADLTLVTSPALGKELEAAGVTAANriRVWNKgvdsesfhprfrseemrarlSGGEPEKP---- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 211 ppTVAFAGRLvkekGAEVLLKAIALVVNQIPEARLLLVGDGAEKEVLKQQIIDLNItanVFMpGLMSRLEIEKLFSTAWV 290
Cdd:PLN02871 265 --LIVYVGRL----GAEKNLDFLKRVMERLPGARLAFVGDGPYREELEKMFAGTPT---VFT-GMLQGDELSQAYASGDV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 291 QVVPSiWPEPFGTVVIEAMIRGTAVIVSASGGLPEIV---QNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAR- 366
Cdd:PLN02871 335 FVMPS-ESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAARe 413
|
....
gi 505028579 367 EVAK 370
Cdd:PLN02871 414 EVEK 417
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
214-381 |
7.31e-24 |
|
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: 100.84 E-value: 7.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 214 VAFAGRLVKEKGAEVLLKAIALVVNQIPEARLLLVGDGAEKEVLKQQIIDLNITANVFMPGLMSRLEIEklFSTAWVQVV 293
Cdd:cd04949 163 IITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQE--YQDAYLSLL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 294 PSIWpEPFGTVVIEAMIRGTAVI-VSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKTh 372
Cdd:cd04949 241 TSQM-EGFGLTLMEAIGHGLPVVsYDVKYGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAEK- 318
|
....*....
gi 505028579 373 YSQDIYVDK 381
Cdd:cd04949 319 YSTENVMEK 327
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
1-389 |
7.69e-24 |
|
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.
Pssm-ID: 340851 [Multi-domain] Cd Length: 364 Bit Score: 101.25 E-value: 7.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 1 MKILLITDYATpTGGAEILTIALRDGLRSRGHDARLFASSARPmnaesqadyrcfgttssfrtLLQTANFwafgklrqvl 80
Cdd:cd03825 1 MKVLHINTVDL-SGGAARAAYRLHQALLAYGIDSTMLVGRKKN--------------------LISKPEF---------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 81 aeFQPDVVHVTIFLTQ-LSPLILP-LLKNVPslyyAVWYRSIC-P-TGtkilpngtACQVKMGMPCYQNHCLP---LWDW 153
Cdd:cd03825 50 --IEADIIHLHWIHGGyLSLKALFkLLRRKP----VVWTLHDMwPfTG--------GCHYPMECEGWKTGCGNcpnLNSY 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 154 LPLMI--QMKLWQRWSNAFN----LFVAPSQAVKQHLMGAGI---NSVEIVWHGTPIQ----------------PQRPPL 208
Cdd:cd03825 116 PPAKKdlSRQLFRRKREALAkkrlTIVAPSRWLADMVRRSPLlkgLPVVVIPNGIDTEifapvdkakarkrlgiPQDKKV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 209 TLPPTVAFAGRlvkEKGAEVLLKAIALVVnQIPEARLLLVG-DGAEKEVLKQQIIDLNITANVfmpglmSRLEIekLFST 287
Cdd:cd03825 196 ILFGAESVTKP---RKGFDELIEALKLLA-TKDDLLLVVFGkNDPQIVILPFDIISLGYIDDD------EQLVD--IYSA 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 288 AWVQVVPSIwPEPFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQMGKKARE 367
Cdd:cd03825 264 ADLFVHPSL-ADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARA 342
|
410 420
....*....|....*....|..
gi 505028579 368 VAKTHYSQDIYVDKFLELYQNL 389
Cdd:cd03825 343 LAENHFDQRVQAQRYLELYKDL 364
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
216-336 |
2.30e-23 |
|
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 97.47 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 216 FAGRLVKEKGAEVLLKAIALVVNQIPEARLLLVGDGAEKEVLKQQIIDLNITANVFMPGLMSRLEIEKLFS-TAWVQVVP 294
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLaAADVFVLP 194
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 505028579 295 SIWpEPFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIV 336
Cdd:cd01635 195 SRS-EGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
14-386 |
1.14e-22 |
|
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: 97.90 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 14 GGAEILTIALRDGLRSRGHDARLFA----SSARPMNAESQADYrcFGTTSSFRTLLQtanfwAFGKLRQVLAEFQPDVVH 89
Cdd:cd04951 12 GGAEKQTVLLADQMFIRGHDVNIVYltgeVEVKPLNNNIIIYN--LGMDKNPRSLLK-----ALLKLKKIISAFKPDVVH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 90 VTIFLTQLSPLILPLLKNVPSLyyavwyrsICPTGTKILPNgtacqvKMGMPCYQnhclpLWDWLPlMIQMKLWQRWSNA 169
Cdd:cd04951 85 SHMFHANIFARFLRMLYPIPLL--------ICTAHNKNEGG------RIRMFIYR-----LTDFLC-DITTNVSREALDE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 170 FNLFVAPSQAvKQHLMGAGINSVEIVWHGTPIQPQRPPLTLPPTVAF---AGRLVKEKGAEVLLKAIALVVNQIPEARLL 246
Cdd:cd04951 145 FIAKKAFSKN-KSVPVYNGIDLNKFKKDINVRLKIRNKLNLKNDEFVilnVGRLTEAKDYPNLLLAISELILSKNDFKLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 247 LVGDGAEKEVLKQQIIDLNITANVFMPGlmSRLEIEKLFSTAWVQVVPSIWpEPFGTVVIEAMIRGTAVIVSASGGLPEI 326
Cdd:cd04951 224 IAGDGPLRNELERLICNLNLVDRVILLG--QISNISEYYNAADLFVLSSEW-EGFGLVVAEAMACERPVVATDAGGVAEV 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 327 VQNNEtgLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKTHYSQDIYVDKFLELY 386
Cdd:cd04951 301 VGDHN--YVVPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFSINTIVNEWERLY 358
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
2-384 |
1.55e-21 |
|
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: 95.13 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 2 KILLITDYATPTGGAEILTIA-LRDGLRSRGHDARLFASSARPMNAESQADYRCFGTTSSFRTL--LQTANFWAF--GKL 76
Cdd:cd03821 1 KILHVTPSISPKAGGPVKVVLrLAAALAALGHEVTIVSTGDGYESLVVEENGRYIPPQDGFASIplLRQGAGRTDfsPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 77 RQVLAEF--QPDVVHVTIFLTQlsplilpllknvPSLYYAVWYRS------ICPTGTkilpngtacqvkmgmpcyqnhcL 148
Cdd:cd03821 81 PNWLRRNlrEYDVVHIHGVWTY------------TSLAACKLARRrgipyvVSPHGM----------------------L 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 149 PLWDW--------LPLMIQMKlwqRWSNAFNLFVAPSQAVKQHLMGAGINS-VEIVWHGTPIqPQRPPLTLP-------- 211
Cdd:cd03821 127 DPWALqqkhwkkrIALHLIER---RNLNNAALVHFTSEQEADELRRFGLEPpIAVIPNGVDI-PEFDPGLRDrrkhngle 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 212 --PTVAFAGRLVKEKGAEVLLKAIALVVNQIPEARLLLVG-DGAEKEVLKQQIIDLNITANVFMPGLMSRLEIEKLFSTA 288
Cdd:cd03821 203 drRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGpDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 289 WVQVVPSiWPEPFGTVVIEAMIRGTAVIVSASGGLPEIVQnNETGLIVPPgNYQVLAAALLRILQNRELAEQMGKKAREV 368
Cdd:cd03821 283 DLFVLPS-YSENFGNVVAEALACGLPVVITDKCGLSELVE-AGCGVVVDP-NVSSLAEALAEALRDPADRKRLGEMARRA 359
|
410
....*....|....*...
gi 505028579 369 AKT--HYSQDIYVDKFLE 384
Cdd:cd03821 360 RQVeeNFSWEAVAGQLGE 377
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
158-370 |
3.47e-20 |
|
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: 90.89 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 158 IQMKLWQRWS--NAfNLFVAPSQAVKQ---HLMGAGINSVEIVWHGT----PIQPQRPPLTL-----PPTVAFAGRLVKE 223
Cdd:cd03809 126 LYYRLLLPISlrRA-DAIITVSEATRDdiiKFYGVPPEKIVVIPLGVdpsfFPPESAAVLIAkyllpEPYFLYVGTLEPR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 224 KGAEVLLKAIALVVNQIPEARLLLVG-DGAEKEVLKQQIIDLNITANVFMPGLMSRLEIEKLFSTAWVQVVPSIWpEPFG 302
Cdd:cd03809 205 KNHERLLKAFALLKKQGGDLKLVIVGgKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLY-EGFG 283
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505028579 303 TVVIEAMIRGTAVIVSASGGLPEIVQNNetGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAK 370
Cdd:cd03809 284 LPVLEAMACGTPVIASNISVLPEVAGDA--ALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAK 349
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
174-388 |
2.82e-18 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 85.61 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 174 VAPSQAVK----QHLMGAGInsvEIVWHGT--------PIQPQRPPLTLPP---TVAFAGRLVKEKGAEVLLKAIALVVN 238
Cdd:PRK15484 144 IVPSQFLKkfyeERLPNADI---SIVPNGFcletyqsnPQPNLRQQLNISPdetVLLYAGRISPDKGILLLMQAFEKLAT 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 239 QIPEARLLLVGD-----GAEKEVLKQQIIDL--NITANVFMPGLMSRLEIEKLFSTAWVQVVPSIWPEPFGTVVIEAMIR 311
Cdd:PRK15484 221 AHSNLKLVVVGDptassKGEKAAYQKKVLEAakRIGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVEEAFCMVAVEAMAA 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505028579 312 GTAVIVSASGGLPEIVQNNETGL-IVPPGNYQVLAAALLRILQNRELAeQMGKKAREVAKTHYSQDIYVDKFLELYQN 388
Cdd:PRK15484 301 GKPVLASTKGGITEFVLEGITGYhLAEPMTSDSIISDINRTLADPELT-QIAEQAKDFVFSKYSWEGVTQRFEEQIHN 377
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
224-373 |
4.20e-18 |
|
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: 85.07 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 224 KGAEVLLKAIALVVNQIPEARLLLVGDGAE---------KEVLKQQIIDLNITanvFMPGLMSRLEIEKLFSTAWVQVVP 294
Cdd:cd03792 210 KDPLGVIDAYKLFKRRAEEPQLVICGHGAVddpegsvvyEEVMEYAGDDHDIH---VLRLPPSDQEINALQRAATVVLQL 286
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505028579 295 SIwPEPFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGnyQVLAAALLRILQNRELAEQMGKKAREVAKTHY 373
Cdd:cd03792 287 ST-REGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSV--EGAAVRILRLLTDPELRRKMGLAAREHVRDNF 362
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
218-334 |
4.37e-13 |
|
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: 69.63 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 218 GRLVKEKGAEVLLKAIALVVNQIPEARLLLVGDGAEKEVLKQQIIDLNITANVFMPGlmSRLEIEKLFSTAWVQVVPSIW 297
Cdd:cd03812 198 GRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLEDKVIFLG--FRNDVSEILSAMDVFLFPSLY 275
|
90 100 110
....*....|....*....|....*....|....*..
gi 505028579 298 pEPFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGL 334
Cdd:cd03812 276 -EGLPLVAVEAQASGLPCLLSDTITKECDITNNVEFL 311
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
203-384 |
2.63e-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: 67.77 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 203 PQRPPLTLP--------PTVAFAGR-LVKEKGAEVLLKAIALVVNQIPEARLLLVGD-----GAE--------KEVLKQQ 260
Cdd:cd03818 197 PAARLRLLNgtelkagdPVITYVARnLEPYRGFHVFMRALPRIQARRPDARVVVVGGdgvsyGSPppdggswkQKMLAEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 261 IIDLNitaNVFMPGLMSRLEIEKLFSTAWVQVVPSiwpEPFGTV--VIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPP 338
Cdd:cd03818 277 GVDLE---RVHFVGKVPYDQYVRLLQLSDAHVYLT---YPFVLSwsLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDF 350
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505028579 339 GNYQVLAAALLRILQNRELAEQMGKKAREVAKTHYSQDIYVDKFLE 384
Cdd:cd03818 351 FDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCLARYLA 396
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
299-382 |
4.33e-11 |
|
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: 63.76 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 299 EPFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPgNYQVLAAALLRILQNRELAEQMGKKAREVAKTHYSQDIY 378
Cdd:cd03805 310 EHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAF 388
|
....
gi 505028579 379 VDKF 382
Cdd:cd03805 389 AERL 392
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
14-197 |
5.74e-11 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 60.62 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 14 GGAEILTIALRDGLRSRGHDARLFASSARPMNAESQADYRCFGTTSSFRTLLQTANFWAFGKLRQVLAEFQPDVVHV-TI 92
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAhSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 93 FLTQLSPLILPLLKNVPSLYYavwyrsicptgtkilPNGTAcqvkmgmpcYQNHCLPLWDWLPLMIQMKLWQRWSNAFNL 172
Cdd:pfam13439 81 FPLGLAALAARLRLGIPLVVT---------------YHGLF---------PDYKRLGARLSPLRRLLRRLERRLLRRADR 136
|
170 180
....*....|....*....|....*..
gi 505028579 173 FVAPSQAVKQHLMGA-GINSVEI-VWH 197
Cdd:pfam13439 137 VIAVSEAVADELRRLyGVPPEKIrVIP 163
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
179-387 |
2.13e-10 |
|
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: 61.63 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 179 AVKQHLMGAgiNSVEIVWHGTPIQPQRP--------PLTLPPTVAFAGRLVKEKGAEVLLKAIALVVNQIPEARLLLVG- 249
Cdd:cd03822 149 LVRIKLIPA--VNIEVIPHGVPEVPQDPttalkrllLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGe 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 250 --DGAEKEV----LKQQIIDLNITANVFMP-GLMSRLEIEKLFSTAWVQVVPsiWPEPFGT---VVIEAMIRGTAVIVSA 319
Cdd:cd03822 227 lhPSLARYEgeryRKAAIEELGLQDHVDFHnNFLPEEEVPRYISAADVVVLP--YLNTEQSssgTLSYAIACGKPVISTP 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505028579 320 SGGLPEIVQNNEtGLIVPPGNYQVLAAALLRILQNRELAEQMGKKAREVAKTHYSQDIyVDKFLELYQ 387
Cdd:cd03822 305 LRHAEELLADGR-GVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESI-ADRYLRLFN 370
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
213-387 |
2.90e-10 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 61.97 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 213 TVAFAGRLVKEKGAEVLLKAIALVVNQIPEARLLLVGDGAEKEVLKQQIIDLNITANVFMPGLMSRleIEKLFSTAWVQV 292
Cdd:PRK15179 519 TVGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRR--VGYWLTQFNAFL 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 293 VPSIWpEPFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNYQV--LAAALLRILQNRELAEQMGKKAREVAK 370
Cdd:PRK15179 597 LLSRF-EGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTApdVAEALARIHDMCAADPGIARKAADWAS 675
|
170
....*....|....*..
gi 505028579 371 THYSQDIYVDKFLELYQ 387
Cdd:PRK15179 676 ARFSLNQMIASTVRCYQ 692
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
223-370 |
3.69e-09 |
|
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.
Pssm-ID: 340835 [Multi-domain] Cd Length: 419 Bit Score: 58.00 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 223 EKGAEVLLKAIALVVNQIPE-----ARLLLVG------DGAEKEVLKQQIIDLNITANV-FMPGLMSRlEIEKLFSTAWV 290
Cdd:cd03806 249 EKNHPLQLRAFAELLKRLPEsirsnPKLVLIGscrneeDKERVEALKLLAKELILEDSVeFVVDAPYE-ELKELLSTASI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 291 QVvPSIWPEPFGTVVIEAMIRGTAVIVSASGG-LPEIV---QNNETG-LIVPPGNYqvlAAALLRILQ-NRELAEQMGKK 364
Cdd:cd03806 328 GL-HTMWNEHFGIGVVEYMAAGLIPLAHASAGpLLDIVvpwDGGPTGfLASTPEEY---AEAIEKILTlSEEERLQRREA 403
|
....*.
gi 505028579 365 AREVAK 370
Cdd:cd03806 404 ARSSAE 409
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
151-382 |
4.32e-08 |
|
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.
Pssm-ID: 340833 [Multi-domain] Cd Length: 356 Bit Score: 54.60 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 151 WDWLPLMIQMKL-------W-QRWSNAFNLFVAPSQAVKQHLMGA-GINSVEIVwhgTPIQPQRPPLTLPPTVAF--AGR 219
Cdd:cd03804 131 LGKGIKSLLASLflhylrlWdVRTAQRVDLFIANSQFVARRIKKFyGRESTVIY---PPVDTDAFAPAADKEDYYltASR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 220 LVKEKGAEVLLKAIalvvNQIPEaRLLLVGDGAEKEVLKQQIidlniTANVFMPGLMSRLEIEKLFSTAWVQVVPSiwPE 299
Cdd:cd03804 208 LVPYKRIDLAVEAF----NELPK-RLVVIGDGPDLDRLRAMA-----SPNVEFLGYQPDEVLKELLSKARAFVFAA--EE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 300 PFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNRELAEQmgKKAREVAkTHYSQDIYV 379
Cdd:cd03804 276 DFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEFEQNFDRFKP--QAIRANA-ERFSRARFR 352
|
...
gi 505028579 380 DKF 382
Cdd:cd03804 353 QEI 355
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
212-365 |
2.42e-07 |
|
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: 52.57 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 212 PTVAFAGRLVKEKGAEVLLKAIALVVNQipEARLLLVGDG------AEKEVLKQQI--IDLNITANVFMPGLMsrleiek 283
Cdd:cd03791 295 PLFGFVGRLTEQKGVDLILDALPELLEE--GGQLVVLGSGdpeyeqAFRELAERYPgkVAVVIGFDEALAHRI------- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 284 lFSTAWVQVVPSIWpEPFGTVVIEAMIRGTAVIVSASGGLPEIVQN-NE-----TGLIVPPGNYQVLAAALLRIL---QN 354
Cdd:cd03791 366 -YAGADFFLMPSRF-EPCGLVQMYAMRYGTLPIVRRTGGLADTVFDyDPetgegTGFVFEDYDAEALLAALRRALalyRN 443
|
170
....*....|.
gi 505028579 355 RELAEQMGKKA 365
Cdd:cd03791 444 PELWRKLQKNA 454
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
1-389 |
2.21e-06 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 49.32 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 1 MKILLITDYATPTGGAEILTIALRDGLRSRGH--DARLFaSSARPMNAE--SQADYRCFGTTSSFRTLLQTANFWAFGKl 76
Cdd:PRK09922 1 MKIAFIGEAVSGFGGMETVISNVINTFEESKIncEMFFF-CRNDKMDKAwlKEIKYAQSFSNIKLSFLRRAKHVYNFSK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 77 rqVLAEFQPDVVhvtifltqlsplilpllknvpslyyavwyrsICPTGTKILPNGTACQvKMGMPCyqnhclPLWDWLPL 156
Cdd:PRK09922 79 --WLKETQPDIV-------------------------------ICIDVISCLYANKARK-KSGKQF------KIFSWPHF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 157 MIQMKLWQRWSNAFNL--FVAPSQAVKQHLMGAGINSVEIVWHGTPIQPQ-----RPPLTLPPTVAFAGRLV--KEKGAE 227
Cdd:PRK09922 119 SLDHKKHAECKKITCAdyHLAISSGIKEQMMARGISAQRISVIYNPVEIKtiiipPPERDKPAVFLYVGRLKfeGQKNVK 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 228 VLLKAIALVVNQIpeaRLLLVGDGAEKEVLKQQIIDLNITANVFMPGLMSRLeieklfstaWVQVVPSIWP--------- 298
Cdd:PRK09922 199 ELFDGLSQTTGEW---QLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQP---------WEVVQQKIKNvsallltsk 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 299 -EPFGTVVIEAMIRGTAVIVSASGGLPE-IVQNNETGLIVPPGNYQVLAAALLRILQnrelaeqmgkkarevAKTHYSQD 376
Cdd:PRK09922 267 fEGFPMTLLEAMSYGIPCISSDCMSGPRdIIKPGLNGELYTPGNIDEFVGKLNKVIS---------------GEVKYQHD 331
|
410
....*....|...
gi 505028579 377 IYVDKFLELYQNL 389
Cdd:PRK09922 332 AIPNSIERFYEVL 344
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
199-338 |
5.27e-05 |
|
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: 44.92 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 199 TPIQPQRPPLTLppTVAFAGRLVKEKGAEVLLKAIALVVNQIPEARLLLVGDGAeKEVLKQQIIDLNitanvfmpGLMSR 278
Cdd:cd03796 183 TPDPSKPDPNKI--TIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGP-KRIELEEMREKY--------QLQDR 251
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505028579 279 LEIEKLFSTAWVQVV---------PSIwPEPFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPP 338
Cdd:cd03796 252 VELLGAVPHEEVRDVlvqghiflnTSL-TEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPD 319
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
14-109 |
1.07e-04 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 42.39 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 14 GGAEILTIALRDGLRSRGHDARLFASSARPMNAESQAD----YRC-FGTTSSFRTLLQTAnfWAfgkLRQVLAEFQPDVV 88
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDgvrvHRLpVPPRPSPLADLAAL--RR---LRRLLRAERPDVV 75
|
90 100
....*....|....*....|.
gi 505028579 89 HVTIFLTQLSPLILPLLKNVP 109
Cdd:pfam13579 76 HAHSPTAGLAARLARRRRGVP 96
|
|
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
299-357 |
1.15e-04 |
|
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.
Pssm-ID: 274147 [Multi-domain] Cd Length: 1050 Bit Score: 44.39 E-value: 1.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 505028579 299 EPFGTVVIEAMIRGTAVIVSASGGLPEIVQNNETGLIVPPGNYQVLAAALLRILQNREL 357
Cdd:TIGR02468 582 EPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKLVADKQL 640
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
205-376 |
2.21e-04 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 43.04 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 205 RPPLTLPPT---VAFAGRLVKEKGAEVLLKAIALVVNQiPEARLLLVGDGAEKEVLKQQIIDLNITANVFMPgLMSRLEI 281
Cdd:PRK10307 220 RAQLGLPDGkkiVLYSGNIGEKQGLELVIDAARRLRDR-PDLIFVICGQGGGKARLEKMAQCRGLPNVHFLP-LQPYDRL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 282 EKLFSTAWVQVVPSIwpepfgtvvieamiRGTA--VIVS------ASGG-----------LPEIVQNNetGLIVPPGNYQ 342
Cdd:PRK10307 298 PALLKMADCHLLPQK--------------AGAAdlVLPSkltnmlASGRnvvataepgteLGQLVEGI--GVCVEPESVE 361
|
170 180 190
....*....|....*....|....*....|....
gi 505028579 343 VLAAALLRILQNRELAEQMGKKAREVAKTHYSQD 376
Cdd:PRK10307 362 ALVAAIAALARQALLRPKLGTVAREYAERTLDKE 395
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
211-366 |
1.29e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 40.88 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 211 PPTVAFAGRLVKEKGAEVLLKAIALVVNQ----IPEARLLLVG----DGAEKEV--LKQQIIDLNITANV-FMPGLMSRl 279
Cdd:PLN02949 268 PPYIISVAQFRPEKAHALQLEAFALALEKldadVPRPKLQFVGscrnKEDEERLqkLKDRAKELGLDGDVeFHKNVSYR- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 280 EIEKLFSTAwVQVVPSIWPEPFGTVVIEAMIRGTAVIVSASGGlP--EIVQNN---ETGLIVppGNYQVLAAALLRILQN 354
Cdd:PLN02949 347 DLVRLLGGA-VAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAG-PkmDIVLDEdgqQTGFLA--TTVEEYADAILEVLRM 422
|
170
....*....|...
gi 505028579 355 RELA-EQMGKKAR 366
Cdd:PLN02949 423 RETErLEIAAAAR 435
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
2-116 |
1.80e-03 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 38.46 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028579 2 KILLITDyatptgGAEILTIALRDGLRSRGHDARLFASSARPMNAESQADYR--CFGTTSSFRTLLQTANfwafgKLRQV 79
Cdd:pfam13477 1 KILLLAN------ADSIHTLRWADALADRGYDVHVISSKGPAKDELIAEGIHvhRLKVPRKGPLGYLKAF-----RLKKL 69
|
90 100 110
....*....|....*....|....*....|....*...
gi 505028579 80 LAEFQPDVVHV-TIFLTQLSPLILPLLKNVPSLYYAVW 116
Cdd:pfam13477 70 IKKIKPDVVHVhYAKPYGLLAGLAARLSGFPPVVLSAW 107
|
|
| |
