|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
17-423 |
5.39e-136 |
|
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: 397.00 E-value: 5.39e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 17 RVAIFTDHADPLAPIGAGYMGGENVYVLELTRALSRLGWHTDVYTRASSLKTTHIAKVSQDARVIRLKAGPVSFVPRDKL 96
Cdd:cd03800 1 RIALISVHGSPLAQPGGADTGGQNVYVLELARALAELGYQVDIFTRRISPADPEVVEIAPGARVIRVPAGPPEYLPKEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 97 FTYMPEYVESFLKFQKENKLEYLLIHGNYYFSGWAALQSAKVLGIPFVNTFHTLGIVRHNFLKDTD-PSPHERIAIEKEI 175
Cdd:cd03800 81 WPYLEEFADGLLRFIAREGGRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHSLGRVKYRHLGAQDtYHPSLRITAEEQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 176 MTADNRIIATSPQMRDEMIRLYGTNPKKITVIPGGVNLNRFQPTPQLLARR-VLHFSINRLIALYVGRIERRKGIDTLLE 254
Cdd:cd03800 161 LEAADRVIASTPQEADELISLYGADPSRINVVPPGVDLERFFPVDRAEARRaRLLLPPDKPVVLALGRLDPRKGIDTLVR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 255 AVAElarlMPDKRPIMRCYIAGGNPkghkskvmEPSELKEWERLQGIVDKLGIKDIVRFLGGINRELLTFYYAAADVTVV 334
Cdd:cd03800 241 AFAQ----LPELRELANLVLVGGPS--------DDPLSMDREELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 335 PSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERVK-LFS 413
Cdd:cd03800 309 PSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARaHYT 388
|
410
....*....|
gi 1083501128 414 WDNIADQMSD 423
Cdd:cd03800 389 WESVADQLLT 398
|
|
| mycothiol_MshA |
TIGR03449 |
D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively ... |
18-427 |
8.31e-97 |
|
D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively in the Actinobacteria, are MshA, the glycosyltransferase of mycothiol biosynthesis. Mycothiol replaces glutathione in these species.
Pssm-ID: 132490 [Multi-domain] Cd Length: 405 Bit Score: 297.42 E-value: 8.31e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 18 VAIFTDHADPLAPIGAGYMGGENVYVLELTRALSRLGWHTDVYTRASSLKTTHIAKVSQDARVIRLKAGPVSFVPRDKLF 97
Cdd:TIGR03449 1 VAMISMHTSPLQQPGTGDAGGMNVYILETATELARRGIEVDIFTRATRPSQPPVVEVAPGVRVRNVVAGPYEGLDKEDLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 98 TYMPEYVESFLK-FQKENKLEYLLIHGNYYFSGWAALQSAKVLGIPFVNTFHTLGIVRHNFLKDTD-PSPHERIAIEKEI 175
Cdd:TIGR03449 81 TQLCAFTGGVLRaEARHEPGYYDLIHSHYWLSGQVGWLLRDRWGVPLVHTAHTLAAVKNAALADGDtPEPEARRIGEQQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 176 MTADNRIIATSPQMRDEMIRLYGTNPKKITVIPGGVNLNRFQPTPQLLARRVLHFSINRLIALYVGRIERRKGIDTLLEA 255
Cdd:TIGR03449 161 VDNADRLIANTDEEARDLVRHYDADPDRIDVVAPGADLERFRPGDRATERARLGLPLDTKVVAFVGRIQPLKAPDVLLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 256 VAELARLMPDKRpiMRCYIAGGnPKGhkskvmepSELKEWERLQGIVDKLGIKDIVRFLGGINRELLTFYYAAADVTVVP 335
Cdd:TIGR03449 241 VAELLDRDPDRN--LRVIVVGG-PSG--------SGLATPDALIELAAELGIADRVRFLPPRPPEELVHVYRAADVVAVP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 336 SYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERVKLFSWD 415
Cdd:TIGR03449 310 SYNESFGLVAMEAQACGTPVVAARVGGLPVAVADGETGLLVDGHDPADWADALARLLDDPRTRIRMGAAAVEHAAGFSWA 389
|
410
....*....|..
gi 1083501128 416 NIADQMSDLYQD 427
Cdd:TIGR03449 390 ATADGLLSSYRD 401
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
17-426 |
2.54e-73 |
|
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: 235.51 E-value: 2.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 17 RVAIFTDHADPlapigagYMGGENVYVLELTRALSRLGWHTDVYTRASslkTTHIAKVSQDARVIRLKAGPVSFVPRDKL 96
Cdd:cd03801 1 KILLLSPELPP-------PVGGAERHVRELARALAARGHDVTVLTPAD---PGEPPEELEDGVIVPLLPSLAALLRARRL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 97 FTYMpEYVESFLKFQkenkleylLIHGNYYFSGWAALQSAKVLGIPFVNTFHTLGIVRHNFLKDTDPSpheRIAIEKEIM 176
Cdd:cd03801 71 LREL-RPLLRLRKFD--------VVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERR---LLARAEALL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 177 TADNRIIATSPQMRDEMIRLYGTNPKKITVIPGGVNLNRFQPTpqllARRVLHFSINRLIALYVGRIERRKGIDTLLEAV 256
Cdd:cd03801 139 RRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSPP----LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEAL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 257 AELARLMPDkrpiMRCYIAGGnpkghkskvmEPSELKEWERLqgivdKLGIKDIVRFLGGINRELLTFYYAAADVTVVPS 336
Cdd:cd03801 215 AKLLRRGPD----VRLVIVGG----------DGPLRAELEEL-----ELGLGDRVRFLGFVPDEELPALYAAADVFVLPS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 337 YYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERV-KLFSWD 415
Cdd:cd03801 276 RYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVaERFSWE 355
|
410
....*....|.
gi 1083501128 416 NIADQMSDLYQ 426
Cdd:cd03801 356 RVAERLLDLYR 366
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
37-428 |
3.22e-60 |
|
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: 201.45 E-value: 3.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 37 GGENVYVLELTRALSRLGW--HTDVYTRASSLKTTHIAKVSQDARVIRLKAGPVSFVPRdkLFTYMPEYVESFLKFQKE- 113
Cdd:cd03798 14 PGRGIFVRRQVRALSRRGVdvEVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPR--LRLLAPLRAPSLAKLLKRr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 114 NKLEYLLIHGNY-YFSGWAALQSAKVLGIPFVNTFHTLGIVRHnflkdtDPSPHERiAIEKEIMTADNRIIATSPQMRDE 192
Cdd:cd03798 92 RRGPPDLIHAHFaYPAGFAAALLARLYGVPYVVTEHGSDINVF------PPRSLLR-KLLRWALRRAARVIAVSKALAEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 193 MIRLyGTNPKKITVIPGGVNLNRFQPTPqllarRVLHFSINRLIALYVGRIERRKGIDTLLEAVAELARLMPDkrpiMRC 272
Cdd:cd03798 165 LVAL-GVPRDRVDVIPNGVDPARFQPED-----RGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPD----VVL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 273 YIAGGNPkghkskvmepselkEWERLQGIVDKLGIKDIVRFLGGINRELLTFYYAAADVTVVPSYYEPFGLVPLESMASG 352
Cdd:cd03798 235 LIVGDGP--------------LREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACG 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083501128 353 TPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERVKLFSWDNIADQMSDLYQDV 428
Cdd:cd03798 301 LPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALAEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
17-425 |
8.94e-49 |
|
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: 170.94 E-value: 8.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 17 RVAIFTDhadPLAPIGagymGGENVYVLELTRALSRLGWHTDVYTrasslKTTHIAKVSQDARVIRLKAGPvsfvprdkL 96
Cdd:cd03814 1 RIALVTD---TYHPQV----NGVVRTLERLVDHLRRRGHEVRVVA-----PGPFDEAESAEGRVVSVPSFP--------L 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 97 FTYmPEYVESFLKFQKENKLEYL----LIH-GNYYFSGWAALQSAKVLGIPFVNTFHTL--GIVRHNFLkdtDPSPHERI 169
Cdd:cd03814 61 PFY-PEYRLALPLPRRVRRLIKEfqpdIIHiATPGPLGLAALRAARRLGLPVVTSYHTDfpEYLSYYTL---GPLSWLAW 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 170 AIEKEIMTADNRIIATSPQMRDEmirLYGTNPKKITVIPGGVNLNRFQPTPQLLARRVLHFSINRLIALYVGRIERRKGI 249
Cdd:cd03814 137 AYLRWFHNPFDTTLVPSPSIARE---LEGHGFERVRLWPRGVDTELFHPSRRDAALRRRLGPPGRPLLLYVGRLAPEKNL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 250 DTLLEAVAELARLMPdkrpiMRCYIAGGNPkghkskvmEPSELKEwERLQgivdklgikdiVRFLGGINRELLTFYYAAA 329
Cdd:cd03814 214 EALLDADLPLAASPP-----VRLVVVGDGP--------ARAELEA-RGPD-----------VIFTGFLTGEELARAYASA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 330 DVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERV 409
Cdd:cd03814 269 DVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEA 348
|
410
....*....|....*.
gi 1083501128 410 KLFSWDNIADQMSDLY 425
Cdd:cd03814 349 ERYSWEAFLDNLLDYY 364
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
33-421 |
8.98e-48 |
|
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: 168.31 E-value: 8.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 33 AGYMGGENVYVLELTRALSRLGWHTDVYTRASSLKTTHIAKVSQDARVIrlkaGPVSFVPRDKLFTYmpeyveSFLKFQK 112
Cdd:cd03809 10 AQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSL----GVIKIKLWRELALL------RWLQILL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 113 ENKLEYLLIHGNYYFSGWaalqsaKVLGIPFVNTFHTLGIVRHnflkdtdpsPHERIAIEKEIM---------TADnRII 183
Cdd:cd03809 80 PKKDKPDLLHSPHNTAPL------LLKGCPQVVTIHDLIPLRY---------PEFFPKRFRLYYrlllpislrRAD-AII 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 184 ATSPQMRDEMIRLYGTNPKKITVIPGGVNLNRFqPTPQLLARRVLHFSINRLIaLYVGRIERRKGIDTLLEAVAELARLM 263
Cdd:cd03809 144 TVSEATRDDIIKFYGVPPEKIVVIPLGVDPSFF-PPESAAVLIAKYLLPEPYF-LYVGTLEPRKNHERLLKAFALLKKQG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 264 PDKRPImrcyIAGGnpKGHKSkvmepselkewERLQGIVDKLGIKDIVRFLGGINRELLTFYYAAADVTVVPSYYEPFGL 343
Cdd:cd03809 222 GDLKLV----IVGG--KGWED-----------EELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGL 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083501128 344 VPLESMASGTPVVASRVGGIQwTIrDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERVKLFSWDNIADQM 421
Cdd:cd03809 285 PVLEAMACGTPVIASNISVLP-EV-AGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKT 360
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
35-408 |
1.75e-47 |
|
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: 167.15 E-value: 1.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 35 YMGGENVYVLELTRALSRLGWHTDVYTRASSLktTHIAKVSQDARVIRLKAGPVSFVPRDKLFTYMpeyvesflkfqKEN 114
Cdd:cd03819 9 EIGGAETYILDLARALAERGHRVLVVTAGGPL--LPRLRQIGIGLPGLKVPLLRALLGNVRLARLI-----------RRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 115 KLEylLIHGNYYFSGWAALQSAKVLGIPFVNTFHTLGIVRHNFLkdtdpspheriAIEKEIMTADNRIIATSPQMRDEMI 194
Cdd:cd03819 76 RID--LIHAHSRAPAWLGWLASRLTGVPLVTTVHGSYLATYHPK-----------DFALAVRARGDRVIAVSELVRDHLI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 195 RLYGTNPKKITVIPGGVNLNRFQPTPQLLARRVLHFSINRLIALYVGRIERRKGIDTLLEAVAELarlmpDKRPIMRCYI 274
Cdd:cd03819 143 EALGVDPERIRVIPNGVDTDRFPPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAEL-----KDEPDFRLLV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 275 AGGNPkghkskvmepselkEWERLQGIVDKLGIKDIVRFLGgiNRELLTFYYAAADVTVVPSYYEPFGLVPLESMASGTP 354
Cdd:cd03819 218 AGDGP--------------ERDEIRRLVERLGLRDRVTFTG--FREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTP 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1083501128 355 VVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIER 408
Cdd:cd03819 282 VVATDVGGAREIVVHGRTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAALT 335
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
17-428 |
2.23e-44 |
|
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: 159.37 E-value: 2.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 17 RVAIFTDHADPlapigagYMGGENVYVLELTRALSRLGwHtDVYtrassLKTTHIAKVSQDA--RVIRLKAGPVSFVPRD 94
Cdd:cd03817 1 KIAIFTDTYLP-------QVNGVATSVRNLARALEKRG-H-EVY-----VITPSDPGAEDEEevVRYRSFSIPIRKYHRQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 95 KLFTYMPEYVESFLKFQKENkleylLIHGNYYFS-GWAALQSAKVLGIPFVNTFHTLGIV-RHNFLKdtdPSPHERIAIE 172
Cdd:cd03817 67 HIPFPFKKAVIDRIKELGPD-----IIHTHTPFSlGKLGLRIARKLKIPIVHTYHTMYEDyLHYIPK---GKLLVKAVVR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 173 KEIMTADNR---IIATSPQMRDEMIRlYGtNPKKITVIPGGVNLNRFQPTPQLLARRVLHFSINRLIALYVGRIERRKGI 249
Cdd:cd03817 139 KLVRRFYNHtdaVIAPSEKIKDTLRE-YG-VKGPIEVIPNGIDLDKFEKPLNTEERRKLGLPPDEPILLYVGRLAKEKNI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 250 DTLLEAVAELarlmpDKRPIMRCYIAGGNPkghkskvmepsELKEWERLqgiVDKLGIKDIVRFLGGINRELLTFYYAAA 329
Cdd:cd03817 217 DFLLRAFAEL-----KKEPNIKLVIVGDGP-----------EREELKEL---ARELGLADKVIFTGFVPREELPEYYKAA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 330 DVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKaFAERIRYLMTHATAHKLLRENGIERV 409
Cdd:cd03817 278 DLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDET-LAEKLLHLRENLELLRKLSKNAEISA 356
|
410
....*....|....*....
gi 1083501128 410 KLFSwdnIADQMSDLYQDV 428
Cdd:cd03817 357 REFA---FAKSVEKLYEEV 372
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
233-408 |
3.72e-43 |
|
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: 149.35 E-value: 3.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 233 NRLIALYVGRIERRKGIDTLLEAVAELarlmPDKRPIMRCYIAGGNPkghkskvmepselkEWERLQGIVDKLGIKDIVR 312
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALL----KEKNPNLKLVIAGDGE--------------EEKRLKKLAEKLGLGDNVI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 313 FLGGINRELLTFYYAAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLM 392
Cdd:pfam00534 63 FLGFVSDEDLPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLL 142
|
170
....*....|....*.
gi 1083501128 393 THATAHKLLRENGIER 408
Cdd:pfam00534 143 EDEELRERLGENARKR 158
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
37-412 |
8.75e-41 |
|
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: 149.05 E-value: 8.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 37 GGENVyVLELTRALSRLGWHTDVYTRASSlktthIAKVSQDARVIRLKAGPVSFVPRDKLFtyMPEYVESFLKFQKENKL 116
Cdd:cd03811 13 GAERV-LLNLANALDKRGYDVTLVLLRDE-----GDLDKQLNGDVKLIRLLIRVLKLIKLG--LLKAILKLKRILKRAKP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 117 EYLLIHGNYYFSGWAALQSAKvlgIPFVntfhtlgIVRHNFLKDTDPSPHERIAIEKEIMTADnRIIATSPQMRDEMIRL 196
Cdd:cd03811 85 DVVISFLGFATYIVAKLAAAR---SKVI-------AWIHSSLSKLYYLKKKLLLKLKLYKKAD-KIVCVSKGIKEDLIRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 197 YGTNPKKITVIPGGVNLNRFQPTPQLlarRVLHFSINRLIALYVGRIERRKGIDTLLEAVAELARLMPDkrpiMRCYIAG 276
Cdd:cd03811 154 GPSPPEKIEVIYNPIDIDRIRALAKE---PILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPD----VKLVILG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 277 GNPkghkskvmepseLKEweRLQGIVDKLGIKDIVRFLGginrelltF------YYAAADVTVVPSYYEPFGLVPLESMA 350
Cdd:cd03811 227 DGP------------LRE--ELEKLAKELGLAERVIFLG--------FqsnpypYLKKADLFVLSSRYEGFPNVLLEAMA 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083501128 351 SGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERVKLF 412
Cdd:cd03811 285 LGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEAVF 346
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
136-422 |
9.31e-41 |
|
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: 149.28 E-value: 9.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 136 AKVLGIP-FVNTFHTLGIVrhnflkDTDPSPHERIA--IEKEIMTADNRIIATSPQMRDEMIRLYGTNPKKITVIPG-GV 211
Cdd:cd03808 100 ARLAGVPkVIYTVHGLGFV------FTEGKLLRLLYllLEKLALLFTDKVIFVNEDDRDLAIKKGIIKKKKTVLIPGsGV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 212 NLNRFQPTPQLLARRVLHFsinrliaLYVGRIERRKGIDTLLEAvaelARLMPDKRPIMRCYIAGGNPKGHKSKVmepse 291
Cdd:cd03808 174 DLDRFQYSPESLPSEKVVF-------LFVARLLKDKGIDELIEA----AKILKKKGPNVRFLLVGDGELENPSEI----- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 292 lkewerlqgIVDKLGIKDIVRFLGGIN--RElltfYYAAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRD 369
Cdd:cd03808 238 ---------LIEKLGLEGRIEFLGFRSdvPE----LLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVID 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1083501128 370 GKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERV-KLFSWDNIADQMS 422
Cdd:cd03808 305 GVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVeEKFDEEKVVNKLL 358
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
17-427 |
2.96e-39 |
|
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: 145.16 E-value: 2.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 17 RVAIFTDHADPLApigagyMGGENVYVLELTRALSRLGWHTDVYT--RASSLKTTHIAKVsqdarVIRLKAGPVSFVPRD 94
Cdd:cd03823 1 KILLVNSLYPPQR------VGGAEISVHDLAEALVAEGHEVAVLTagVGPPGQATVARSV-----VRYRRAPDETLPLAL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 95 KLFTYMPEYVESF-LKFQKENKLEYL---LIHGNYyFSGW--AALQSAKVLGIPFVNTFHTLGIVRHN---FLKDTDpsp 165
Cdd:cd03823 70 KRRGYELFETYNPgLRRLLARLLEDFrpdVVHTHN-LSGLgaSLLDAARDLGIPVVHTLHDYWLLCPRqflFKKGGD--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 166 heriaiekeimtadnRIIATSpqmRDeMIRLYGTN---PKKITVIPggvnlNRFQPTPQLLARRVlhFSINRLIALYVGR 242
Cdd:cd03823 146 ---------------AVLAPS---RF-TANLHEANglfSARISVIP-----NAVEPDLAPPPRRR--PGTERLRFGYIGR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 243 IERRKGIDTLLEAVAELARLMPdkrpimRCYIAGGNPKghkskvmepSELKEWErlqgivdklgIKDIVRFLGGINRELL 322
Cdd:cd03823 200 LTEEKGIDLLVEAFKRLPREDI------ELVIAGHGPL---------SDERQIE----------GGRRIAFLGRVPTDDI 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 323 TFYYAAADVTVVPS-YYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLL 401
Cdd:cd03823 255 KDFYEKIDVLVVPSiWPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERL 334
|
410 420
....*....|....*....|....*.
gi 1083501128 402 RENGIERVklfSWDNIADQMSDLYQD 427
Cdd:cd03823 335 RAGAEPPR---STESQAEEYLKLYRD 357
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
37-421 |
1.09e-35 |
|
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: 135.96 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 37 GGENVYVLELTRALSRLGWHTDVYTRASSLKTthiAKVSQDARVI--RLKAGPVSFVPRDKLFTYMPEYVESFLKfqkEN 114
Cdd:cd03821 14 GGPVKVVLRLAAALAALGHEVTIVSTGDGYES---LVVEENGRYIppQDGFASIPLLRQGAGRTDFSPGLPNWLR---RN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 115 KLEY--LLIHGNYYFSGWAALQSAKVLGIPFVNTFHTlgivrhnflkDTDP------SPHERIA---IEKEIMTADNRII 183
Cdd:cd03821 88 LREYdvVHIHGVWTYTSLAACKLARRRGIPYVVSPHG----------MLDPwalqqkHWKKRIAlhlIERRNLNNAALVH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 184 ATSPQMRDEMIRLYGTNPkkITVIPGGVNLNRFQPtpQLLARRVLHFSINRLIALYVGRIERRKGIDTLLEAVAELArlm 263
Cdd:cd03821 158 FTSEQEADELRRFGLEPP--IAVIPNGVDIPEFDP--GLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLA--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 264 pDKRPIMRCYIAGGNPKGHkskvmepselkewERLQGIVDKLGIKDIVRFLGGINRELLTFYYAAADVTVVPSYYEPFGL 343
Cdd:cd03821 231 -EQGRDWHLVIAGPDDGAY-------------PAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 344 VPLESMASGTPVVASRVGGIqWTIRDGKSGYLVEPgNAKAFAERIRYLMTHATAHKLLRENG---IERVKLFSWDNIADQ 420
Cdd:cd03821 297 VVAEALACGLPVVITDKCGL-SELVEAGCGVVVDP-NVSSLAEALAEALRDPADRKRLGEMArraRQVEENFSWEAVAGQ 374
|
.
gi 1083501128 421 M 421
Cdd:cd03821 375 L 375
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
234-394 |
1.15e-35 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 128.78 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 234 RLIALYVGRI-ERRKGIDTLLEAVAELARlmpdKRPIMRCYIAGGNPkghkskvmePSELKEWERlqgivdklGIKDIVR 312
Cdd:pfam13692 1 RPVILFVGRLhPNVKGVDYLLEAVPLLRK----RDNDVRLVIVGDGP---------EEELEELAA--------GLEDRVI 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 313 FLGGINrELLTfYYAAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIrDGKSGYLVEPGNAKAFAERIRYLM 392
Cdd:pfam13692 60 FTGFVE-DLAE-LLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLL 136
|
..
gi 1083501128 393 TH 394
Cdd:pfam13692 137 ED 138
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
325-429 |
3.96e-35 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 127.03 E-value: 3.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 325 YYAAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLREN 404
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96
|
90 100
....*....|....*....|....*.
gi 1083501128 405 GIERV-KLFSWDNIADQMSDLYQDVV 429
Cdd:COG0438 97 ARERAeERFSWEAIAERLLALYEELL 122
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
112-428 |
2.43e-33 |
|
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: 129.39 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 112 KENKLEylLIHGNYYFS-GWAALQSAKVLG--IPFVNTFHTLGIVrhnfLKDTDPS--PHERIAIEKEimtadNRIIATS 186
Cdd:cd04962 81 KEHKLD--VLHAHYAIPhASCAYLAREILGekIPIVTTLHGTDIT----LVGYDPSlqPAVRFSINKS-----DRVTAVS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 187 PQMRDEMIRLYGTNpKKITVIPGGVNLNRF--QPTPQLLARRVLHFSINRLIalYVGRIERRKGIDTLLEAVAELARLMP 264
Cdd:cd04962 150 SSLRQETYELFDVD-KDIEVIHNFIDEDVFkrKPAGALKRRLLAPPDEKVVI--HVSNFRPVKRIDDVVRVFARVRRKIP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 265 dkrpiMRCYIAGGNPkghkskvmEPSELKEWERlqgivdKLGIKDIVRFLGgiNRELLTFYYAAADVTVVPSYYEPFGLV 344
Cdd:cd04962 227 -----AKLLLVGDGP--------ERVPAEELAR------ELGVEDRVLFLG--KQDDVEELLSIADLFLLPSEKESFGLA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 345 PLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIER-VKLFSWDNIADQMSD 423
Cdd:cd04962 286 ALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRaAERFDPERIVPQYEA 365
|
....*
gi 1083501128 424 LYQDV 428
Cdd:cd04962 366 YYRRL 370
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
197-420 |
1.03e-32 |
|
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: 126.97 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 197 YGTNPKKITVIPGGVNLNRFQPTPQLLARRVLhfsinrlialYVGRIERRKGIDTLLEAVAELARLMPDkrpiMRCYIAG 276
Cdd:cd03820 154 YKQPNSNVVVIPNPLSFPSEEPSTNLKSKRIL----------AVGRLTYQKGFDLLIEAWALIAKKHPD----WKLRIYG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 277 -GNPKghkskvmepselkewERLQGIVDKLGIKDIVRFLGGINRelLTFYYAAADVTVVPSYYEPFGLVPLESMASGTPV 355
Cdd:cd03820 220 dGPER---------------EELEKLIDKLGLEDRVKLLGPTKN--IAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPI 282
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083501128 356 VA----SRVGGIqwtIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERVKLFSWDNIADQ 420
Cdd:cd03820 283 ISfdcpTGPSEI---IEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAERFSIEKIIKQ 348
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
17-420 |
4.10e-32 |
|
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: 126.30 E-value: 4.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 17 RVAIFTDHAdPLAPIGAGYMggenvyVLELTRALSRLGWHTDVYT----RASSLKTTHIAKVSQDARVIRLKAGPVSFVP 92
Cdd:cd03794 1 KILLISQYY-PPPKGAAAAR------VYELAKELVRRGHEVTVLTpspnYPLGRIFAGATETKDGIRVIRVKLGPIKKNG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 93 RDKLFTYMPEYVESFLKFQKENKLEYLLIH--GNYYFSGWAALQSAKVLGIPFVNTFH---------TLGIVRHNFLKDT 161
Cdd:cd03794 74 LIRRLLNYLSFALAALLKLLVREERPDVIIaySPPITLGLAALLLKKLRGAPFILDVRdlwpesliaLGVLKKGSLLKLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 162 DPspheriaIEKEIMTADNRIIATSPQMRDEMIRLyGTNPKKITVIPGGVNLNRFQPTPQLLARRVLHFSiNRLIALYVG 241
Cdd:cd03794 154 KK-------LERKLYRLADAIIVLSPGLKEYLLRK-GVPKEKIIVIPNWADLEEFKPPPKDELRKKLGLD-DKFVVVYAG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 242 RIERRKGIDTLLEAVAELARlmpdkRPIMRCYIAGGnpkghkskVMEPSELKEWERLQGIvdklgikDIVRFLGGINREL 321
Cdd:cd03794 225 NIGKAQGLETLLEAAERLKR-----RPDIRFLFVGD--------GDEKERLKELAKARGL-------DNVTFLGRVPKEE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 322 LTFYYAAADVTVVPsyYEP----FGLVP---LESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTH 394
Cdd:cd03794 285 VPELLSAADVGLVP--LKDnpanRGSSPsklFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDD 362
|
410 420
....*....|....*....|....*..
gi 1083501128 395 ATAHKLLRENGIERVKL-FSWDNIADQ 420
Cdd:cd03794 363 PELRRAMGENGRELAEEkFSREKLADR 389
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
120-392 |
3.99e-31 |
|
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: 122.95 E-value: 3.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 120 LIHGNYYFSGWAALQSAKVLGIPFVNTFHTLGIV--RHNFL----KDTDPSPHERIAIEKEIMtadnrIIATSPQMRDEM 193
Cdd:cd05844 84 LVHAHFGRDGVYALPLARALGVPLVVTFHGFDITtsRAWLAaspgWPSQFQRHRRALQRPAAL-----FVAVSGFIRDRL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 194 IRLyGTNPKKITVIPGGVNLNRFQP-TPQLLARRVLHfsinrlialyVGRIERRKGIDTLLEAVAELARLMPDKRPImrc 272
Cdd:cd05844 159 LAR-GLPAERIHVHYIGIDPAKFAPrDPAERAPTILF----------VGRLVEKKGCDVLIEAFRRLAARHPTARLV--- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 273 yIAGGNPkghkskvmepselkEWERLQGIVDKLGIkdiVRFLGGINRELLTFYYAAADVTVVPSYY------EPFGLVPL 346
Cdd:cd05844 225 -IAGDGP--------------LRPALQALAAALGR---VRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdsEGLGIVLL 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1083501128 347 ESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLM 392
Cdd:cd05844 287 EAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALL 332
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
182-425 |
3.92e-30 |
|
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: 120.11 E-value: 3.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 182 IIATSPQMRdEMIRLYGTNPKKITVIPGGVNLNRFQPTP--QLLARRVLHFSINRLIALYVGRIERRKGIDTLLEAvael 259
Cdd:cd03807 137 TVANSSAVA-EFHQEQGYAKNKIVVIYNGIDLFKLSPDDasRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRA---- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 260 ARLMPDKRPIMRCYIAGGNPkghkskvmepselkEWERLQGIVDKLGIKDIVRFLGgiNRELLTFYYAAADVTVVPSYYE 339
Cdd:cd03807 212 AALLVETHPDLRLLLVGRGP--------------ERPNLERLLLELGLEDRVHLLG--ERSDVPALLPAMDIFVLSSRTE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 340 PFGLVPLESMASGTPVVASRVGGIQWTIRDGkSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERV-KLFSWDNIA 418
Cdd:cd03807 276 GFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIaNEFSIDAMV 354
|
....*..
gi 1083501128 419 DQMSDLY 425
Cdd:cd03807 355 RRYETLY 361
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
182-428 |
1.24e-29 |
|
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: 118.97 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 182 IIATSPQMRDEMIRLYGTNPKKITVIPGGVNLNRFQPTPQLLARRVLHFSINRLIALYVGR--IERRKGIDTLLEAVAEL 259
Cdd:cd03825 141 IVAPSRWLADMVRRSPLLKGLPVVVIPNGIDTEIFAPVDKAKARKRLGIPQDKKVILFGAEsvTKPRKGFDELIEALKLL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 260 ARLmpdkrPIMRCYIAGGNPKghkskvmepselkewerlqgivDKLGIKDIVRFLGGI-NRELLTFYYAAADVTVVPSYY 338
Cdd:cd03825 221 ATK-----DDLLLVVFGKNDP----------------------QIVILPFDIISLGYIdDDEQLVDIYSAADLFVHPSLA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 339 EPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERVKL-FSWDNI 417
Cdd:cd03825 274 DNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENhFDQRVQ 353
|
250
....*....|.
gi 1083501128 418 ADQMSDLYQDV 428
Cdd:cd03825 354 AQRYLELYKDL 364
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
37-413 |
3.60e-28 |
|
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: 114.68 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 37 GGENVYVLELTRALSRLGWHTDVYTrasslktthiakVSQDA--RVIRLKAGPVSFVPRDKLFTYMPEYVESFLKFQKEN 114
Cdd:cd03795 14 GGIEQVIYDLAEGLKKKGIEVDVLC------------FSKEKetPEKEENGIRIHRVKSFLNVASTPFSPSYIKRFKKLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 115 KlEYLLIHgnyYFSGWAALQSAKVLGI---PFVNTFHtLGIVRHNFLKDTdPSPHERIAIEKEimtadNRIIATSPQMRD 191
Cdd:cd03795 82 K-EYDIIH---YHFPNPLADLLLFFSGakkPVVVHWH-SDIVKQKKLLKL-YKPLMTRFLRRA-----DRIIATSPNYVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 192 --EMIRLYgtnPKKITVIPGGVNLNRFqPTPQLLARRVLHFSINRLIALYVGRIERRKGIDTLLEAVAELarlmpdKRPI 269
Cdd:cd03795 151 tsPTLREF---KNKVRVIPLGIDKNVY-NIPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLIEAAQYL------NYPI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 270 mrcYIAGGNPkghkskvmepselkEWERLQGIVDKLGIKDiVRFLGGINRELLTFYYAAADVTVVPSYY--EPFGLVPLE 347
Cdd:cd03795 221 ---VIGGEGP--------------LKPDLEAQIELNLLDN-VKFLGRVDDEEKVIYLHLCDVFVFPSVLrsEAFGIVLLE 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083501128 348 SMASGTPVVASRVG-GIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERVK-LFS 413
Cdd:cd03795 283 AMMCGKPVISTNIGtGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEeLFT 350
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
16-442 |
5.50e-26 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 110.19 E-value: 5.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 16 KRVAIFTDHAdPLAPIgAGYmggENVYvLELTRALSRLGWHTDVYTrasslktTHiAKVSQD---ARVIRLKAGPVSFVP 92
Cdd:PLN02871 59 RRIALFVEPS-PFSYV-SGY---KNRF-QNFIRYLREMGDEVLVVT-------TD-EGVPQEfhgAKVIGSWSFPCPFYQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 93 RDKLFTYMPEYVES-FLKFQKEnkleylLIH----GnyyFSGWAALQSAKVLGIPFVNTFHT---LGIVRHNFLKDTDPS 164
Cdd:PLN02871 125 KVPLSLALSPRIISeVARFKPD------LIHasspG---IMVFGALFYAKLLCVPLVMSYHThvpVYIPRYTFSWLVKPM 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 165 pherIAIEKEIMTADNRIIATSPQMRDEMIRLYGTNPKKITVIPGGVNLNRFQPTPQLLARRVlhfsinRL--------I 236
Cdd:PLN02871 196 ----WDIIRFLHRAADLTLVTSPALGKELEAAGVTAANRIRVWNKGVDSESFHPRFRSEEMRA------RLsggepekpL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 237 ALYVGRIERRKGIDtlleavaELARLMpDKRPIMRCYIAGGNPkghkskvmEPSELKEWerLQGIVdklgikdiVRFLGG 316
Cdd:PLN02871 266 IVYVGRLGAEKNLD-------FLKRVM-ERLPGARLAFVGDGP--------YREELEKM--FAGTP--------TVFTGM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 317 INRELLTFYYAAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRD---GKSGYLVEPGNAKAFAERIRYLMT 393
Cdd:PLN02871 320 LQGDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGDVDDCVEKLETLLA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1083501128 394 HATAHKLLRENGIERVKLFSWDNIADQMSDLYQDVVIDYFYRKAFHLAN 442
Cdd:PLN02871 400 DPELRERMGAAAREEVEKWDWRAATRKLRNEQYSAAIWFWRKKRAQLLG 448
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
37-214 |
6.57e-26 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 103.38 E-value: 6.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 37 GGENVYVLELTRALSRLGWHTDVYTRASSLKTthiakvsqDARVIRLKAGPVSFVPRDKLFTYMPEYVESFLKFQKENKL 116
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPL--------AEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 117 EylLIHGNYYFS-GWAALQSAKVLGIPFVNTFHTLGIVRHNFLKDTDPSPHERIAIEKEIMTADNRIIATSPQMRDEMIR 195
Cdd:pfam13439 73 D--VVHAHSPFPlGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRR 150
|
170
....*....|....*....
gi 1083501128 196 LYGTNPKKITVIPGGVNLN 214
Cdd:pfam13439 151 LYGVPPEKIRVIPNGVDLE 169
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
127-425 |
8.12e-26 |
|
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: 109.73 E-value: 8.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 127 FSGWAALQSAKVLGIPFVNTFHtlGIV----RHNFLKDTDPSP---------HERIAieKEIMTADNRIIATSPQMRDEM 193
Cdd:cd03813 184 YAGLLGALARHRRGIPFLLTEH--GIYtrerKIEILQSTWIMGyikklwirfFERLG--KLAYQQADKIISLYEGNRRRQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 194 IRLyGTNPKKITVIPGGVNLNRFQPtpqllARRVLHFSINRLIALyVGRIERRKGIDTLLEAVAELARLMPDkrpiMRCY 273
Cdd:cd03813 260 IRL-GADPDKTRVIPNGIDIQRFAP-----AREERPEKEPPVVGL-VGRVVPIKDVKTFIRAFKLVRRAMPD----AEGW 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 274 IAGGNPKghkskvmEPSELKEWERLqgiVDKLGIKDIVRFLGGINRellTFYYAAADVTVVPSYYEPFGLVPLESMASGT 353
Cdd:cd03813 329 LIGPEDE-------DPEYAQECKRL---VASLGLENKVKFLGFQNI---KEYYPKLGLLVLTSISEGQPLVILEAMASGV 395
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083501128 354 PVVASRVGGIQWTIRD-----GKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERV-KLFSWDNIADQMSDLY 425
Cdd:cd03813 396 PVVATDVGSCRELIYGaddalGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVeKYYTLEGMIDSYRKLY 473
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
41-427 |
1.15e-24 |
|
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274943 [Multi-domain] Cd Length: 373 Bit Score: 104.79 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 41 VYVLELTRALSRLGWHTDVYTRASSLKTthiakVSQDARViRLKAGPVSFVPRDKLFTYMPEYVESFLKFQKENKLEYLL 120
Cdd:TIGR04047 16 VHTLELAEALTALGHDVTVWALAADGFG-----FFRDPPC-AVRLVPVAPAPGDTDAMVEQRIARSIDHLRAHFARGFDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 121 IHGNYYFSGWAALQSAKVLGIP-FVNTFHTLgivrhnflkDTDPSPHERIAIEKEIMTADNRIiATSPQMRDEMIRLYGT 199
Cdd:TIGR04047 90 VHAQDCISGNALATLRAEGLIPgFVRTVHHL---------DDFDDPRLAACQERAIVEADAVL-CVSAAWAAELRAEWGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 200 NPkkiTVIPGGVNLNRFQPTP-----QLLARRVLHFSinrLIALYVGRIERRKGIDTLLEAVAELARLMPDKRPImrcyI 274
Cdd:TIGR04047 160 DA---TVVPNGVDAARFSPAAdaadaALRRRLGLRGG---PYVLAVGGIEPRKNTIDLLEAFALLRARRPQAQLV----I 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 275 AGGnpkghkskvmepSELKEW----ERLQGIVDKLGIK-DIVRFLGGINRELLTFYYAAADVTVVPSYYEPFGLVPLESM 349
Cdd:TIGR04047 230 AGG------------ATLFDYdayrREFRARAAELGVDpGPVVITGPVPDADLPALYRCADAFAFPSLKEGFGLVVLEAL 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083501128 350 ASGTPVVASRVGGIQWTIRDGkSGYLVEPGNAKAFAERIRyLMTHATAHKLLRENGIERVKLFSWDNIADQMSDLYQD 427
Cdd:TIGR04047 298 ASGIPVVASDIAPFTEYLGRF-DAAWADPSDPDSIADALA-LALDPARRPALRAAGPELAARYTWDASARAHLEFYRR 373
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
27-428 |
3.31e-24 |
|
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: 102.75 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 27 PLAPIGAGYMGGENVYVLELTRALSRLGWHTDVYTRASSLKTTHIAKVSQDARvirlkaGPVSFVPRDKLFtympEYVES 106
Cdd:cd03802 8 PRGPVPPGKYGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSAPLVAVIPRAL------RLDPIPQESKLA----ELLEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 107 FLKFQKENklEYLLIHGNYYfsgWAALQSAKVLGIPFVNTFHTLGIVRHNFLKDTDPSPHeriaiekeimtadnrIIATS 186
Cdd:cd03802 78 LEVQLRAS--DFDVIHNHSY---DWLPPFAPLIGTPFVTTLHGPSIPPSLAIYAAEPPVN---------------YVSIS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 187 PQMRDEMIRLygtnpKKITVIPGGVNLNRFQPTPQllARRVLHFsinrlialyVGRIERRKGIDTLLEAVAELarlmpdK 266
Cdd:cd03802 138 DAQRAATPPI-----DYLTVVHNGLDPADYRFQPD--PEDYLAF---------LGRIAPEKGLEDAIRVARRA------G 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 267 RPImrcYIAGGNPKGHKSKvmepselKEWERLQGivdklgikDIVRFLGGIN----RELLtfyyAAADVTVVPS-YYEPF 341
Cdd:cd03802 196 LPL---KIAGKVRDEDYFY-------YLQEPLPG--------PRIEFIGEVGhdekQELL----GGARALLFPInWDEPF 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 342 GLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGnaKAFAERIRYLMTHATAHklLRENGIERvklFSWDNIADQM 421
Cdd:cd03802 254 GLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDSV--EEMAEAIANIDRIDRAA--CRRYAEDR---FSAARMADRY 326
|
....*..
gi 1083501128 422 SDLYQDV 428
Cdd:cd03802 327 EALYRKV 333
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
220-376 |
1.89e-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: 98.63 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 220 PQLLARRVLHFSINRLIALYVGRIERRKGIDTLLEAVAELARLMPDkrpiMRCYIAGGNPKghkskvmepselkEWERLQ 299
Cdd:cd01635 96 SELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALLKARLPD----LVLVLVGGGGE-------------REEEEA 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083501128 300 GIVDKLGIKDIVRFLGGINRELLTFYYAAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLV 376
Cdd:cd01635 159 LAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
211-420 |
2.99e-21 |
|
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: 95.35 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 211 VNLNRFQPTPQLLARRVLHFSINRLIALYVGRIERRKGIDTLLEAVAEL-ARLMPDKRPimRCYIAGGnpkgHKSKVMEP 289
Cdd:cd03805 188 VDTDSFDSTSEDPDPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLkQKLPEFENV--RLVIAGG----YDPRVAEN 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 290 SE-LKEwerLQGIVDKL-GIKDIVRFLGGINRELLTFYYAAAD-VTVVPSYyEPFGLVPLESMASGTPVVASRVGGIQWT 366
Cdd:cd03805 262 VEyLEE---LQRLAEELlNVEDQVLFLRSISDSQKEQLLSSALaLLYTPSN-EHFGIVPLEAMYAGKPVIACNSGGPLET 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1083501128 367 IRDGKSGYLVEPgNAKAFAERIRYLMTHATAHKLLRENGIERV-KLFSWDNIADQ 420
Cdd:cd03805 338 VVEGVTGFLCEP-TPEAFAEAMLKLANDPDLADRMGAAGRKRVkEKFSREAFAER 391
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
120-427 |
8.15e-21 |
|
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: 94.55 E-value: 8.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 120 LIHGNYYFSG------WAALQSAKVLGIPFVNTFHTL---GIVRHNFLKDTDPSPHERIAIEKE-----------IMTAD 179
Cdd:cd03791 131 IIHANDWHTAlvpaylKTRYRGPGFKKIKTVFTIHNLayqGLFPLDTLAELGLPPELFHIDGLEfygqinflkagIVYAD 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 180 nRIIATSPQMRDEMI------RLYG---TNPKKITVIPGGVNLNRFQP-TPQLLARrvlHFSINRL-------IAL---- 238
Cdd:cd03791 211 -RVTTVSPTYAKEILtpeygeGLDGvlrARAGKLSGILNGIDYDEWNPaTDKLIPA---NYSANDLegkaenkAALqkel 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 239 ------------YVGRIERRKGIDTLLEAVAELARLmpdkrpIMRCYIAGGNPKGHKSkvmepsELKEWERLQgivdklg 306
Cdd:cd03791 287 glpvdpdaplfgFVGRLTEQKGVDLILDALPELLEE------GGQLVVLGSGDPEYEQ------AFRELAERY------- 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 307 iKDIVRFLGGINRELLTFYYAAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDG------KSGYLVEPGN 380
Cdd:cd03791 348 -PGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYdpetgeGTGFVFEDYD 426
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1083501128 381 AKAFAERIRYLMTHATAHKL---LRENGIERVklFSWDNIADQMSDLYQD 427
Cdd:cd03791 427 AEALLAALRRALALYRNPELwrkLQKNAMKQD--FSWDKSAKEYLELYRS 474
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
71-426 |
1.73e-19 |
|
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: 89.75 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 71 IAKVSQDARVIRLKAGPVSFVP---RDKLFTYMP-----------EYVESFLKFQKENKLEYLLIHGNYYFS------GW 130
Cdd:cd03822 15 IATYTDDLVEGLRKGGPVVIVVivsPQDEILKDDdfevpneikswNSNEYFRLLDHLNFKKPDVVHIQHEFGifggkyGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 131 AALQSAKVLGIPFVNTFHTLgivrhnflKDTDPSPHERIAIEKEIMTADNRIIATSPQMRDEMIRLYGTNPKKITVIPGG 210
Cdd:cd03822 95 YALGLLLHLRIPVITTLHTV--------LDLSDPGKQALKVLFRIATLSERVVVMAPISRFLLVRIKLIPAVNIEVIPHG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 211 VNLNRFQPTPqllARRVLHFSINRLIALYVGRIERRKGIDTLLEAVAELarlmPDKRPIMRCYIAGGNpkgHKSKVMEPS 290
Cdd:cd03822 167 VPEVPQDPTT---ALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPEL----KAEFPDVRLVIAGEL---HPSLARYEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 291 ELKEWERlqgiVDKLGIKDIVRF-LGGINRELLTFYYAAADVTVVPsYYEpfglvpLESMASGT---------PVVASRV 360
Cdd:cd03822 237 ERYRKAA----IEELGLQDHVDFhNNFLPEEEVPRYISAADVVVLP-YLN------TEQSSSGTlsyaiacgkPVISTPL 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083501128 361 GGIQWTIRDGkSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERVKLFSWDNIADQMSDLYQ 426
Cdd:cd03822 306 RHAEELLADG-RGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADRYLRLFN 370
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
127-433 |
1.90e-19 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 89.85 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 127 FSGWAALQ----SAKVLGI-PFVNTFHTLGIVRHNFLK----DTDPSPHERI------AIEKEIMTADNRIIATSPQMRD 191
Cdd:PRK15484 73 FQKWTRLDplpySQRILNIaHKFTITKDSVIVIHNSMKlyrqIRERAPQAKLvmhmhnAFEPELLDKNAKIIVPSQFLKK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 192 emirLYGTN--PKKITVIPGGVNLNRFQPTPQLLARRVLHFSINRLIALYVGRIERRKGIDTLLEAVAELARLMPDKRPI 269
Cdd:PRK15484 153 ----FYEERlpNADISIVPNGFCLETYQSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 270 MRcyiagGNPKGhKSKvmepSELKEWER-LQGIVDKLGIKDIVrfLGGINRELLTFYYAAADVTVVPSYY-EPFGLVPLE 347
Cdd:PRK15484 229 VV-----GDPTA-SSK----GEKAAYQKkVLEAAKRIGDRCIM--LGGQPPEKMHNYYPLADLVVVPSQVeEAFCMVAVE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 348 SMASGTPVVASRVGGIQWTIRDGKSGY-LVEPGNAKAFAERIRYLMTHATAHKlLRENGIERV-KLFSWDNIADQmsdlY 425
Cdd:PRK15484 297 AMAAGKPVLASTKGGITEFVLEGITGYhLAEPMTSDSIISDINRTLADPELTQ-IAEQAKDFVfSKYSWEGVTQR----F 371
|
....*...
gi 1083501128 426 QDVVIDYF 433
Cdd:PRK15484 372 EEQIHNWF 379
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
115-394 |
5.29e-19 |
|
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: 87.89 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 115 KLEYLLIHGNYYFSGW--AALQSAKVLGIPFVNTFHTLGIVRhnFLKDTDPSPHERIAIEKEIMtadnriIATSPQMRDE 192
Cdd:cd03799 68 KGAYDIIHCQFGPLGAlgALLRRLKVLKGKLVTSFRGYDISM--YVILEGNKVYPQLFAQGDLF------LPNCELFKHR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 193 MIRLyGTNPKKITVIPGGVNLNRFQPTPQLLArrvlhfSINRLIALYVGRIERRKGIDTLLEAVAELARLMPDkrpiMRC 272
Cdd:cd03799 140 LIAL-GCDEKKIIVHRSGIDCNKFRFKPRYLP------LDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPN----IEY 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 273 YIAGGNPkghkskvmepseLKEweRLQGIVDKLGIKDIVRFLGGINRELLTFYYAAADVTVVPSYYEPFG------LVPL 346
Cdd:cd03799 209 QIIGDGD------------LKE--QLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTAADGdqdgppNTLK 274
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1083501128 347 ESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTH 394
Cdd:cd03799 275 EAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEH 322
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
37-210 |
5.67e-19 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 83.60 E-value: 5.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 37 GGENVYVLELTRALSRLGWHTDVYTRASSLKTTHIakVSQDARVIRLKagpvsfVPRDKLFTYMPEYVESFLKFQKENKl 116
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPEL--VGDGVRVHRLP------VPPRPSPLADLAALRRLRRLLRAER- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 117 eYLLIHGNYYFSGWAALQSAKVLGIPFVNTFHTLGIVRHNFLKdtdpsPHERIAIEKEIMTADNRIIATSPQMRDEMIRl 196
Cdd:pfam13579 72 -PDVVHAHSPTAGLAARLARRRRGVPLVVTVHGLALDYGSGWK-----RRLARALERRLLRRADAVVVVSEAEAELLRA- 144
|
170
....*....|....
gi 1083501128 197 YGTNPKKITVIPGG 210
Cdd:pfam13579 145 LGVPAARVVVVPNG 158
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
191-425 |
8.90e-19 |
|
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: 87.50 E-value: 8.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 191 DEMIRLYGTNPKKITVIPGGVNLNRFQ--PTPQLLARRVLHFSINRLIALYVGRIERRKGIDTLLEAVAELARLMPDKRP 268
Cdd:cd04951 143 DEFIAKKAFSKNKSVPVYNGIDLNKFKkdINVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 269 ImrcyIAGGNPKGhkskvmepselKEWERLqgiVDKLGIKDIVRFLGGINRelLTFYYAAADVTVVPSYYEPFGLVPLES 348
Cdd:cd04951 223 L----IAGDGPLR-----------NELERL---ICNLNLVDRVILLGQISN--ISEYYNAADLFVLSSEWEGFGLVVAEA 282
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083501128 349 MASGTPVVASRVGGIQWTIRDgkSGYLVEPGNAKAFAERIRYLMTHAT-AHKLLRENGIERVKLFSWDNIADQMSDLY 425
Cdd:cd04951 283 MACERPVVATDAGGVAEVVGD--HNYVVPVSDPQLLAEKIKEIFDMSDeERDILGNKNEYIAKNFSINTIVNEWERLY 358
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
37-358 |
7.81e-18 |
|
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: 84.65 E-value: 7.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 37 GGENVYVLELTRALSRLGWHTDVYTrasslktTHIAKVSQDARVIRLKAGPVSFVPRDKlftYMPEYVESFLKFQKENKl 116
Cdd:cd03812 12 GGIETFLMNLYRKLDKSKIEFDFLA-------TSDDKGEYDEELEELGGKIFYIPPKKK---NIIKYFIKLLKLIKKEK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 117 eYLLIHGNYYFSGWAALQSAKVLGIPfVNTFHTlgivrHNflkdTDPSPHERIAI-----EKEIMTADNRIIATSpqmrD 191
Cdd:cd03812 81 -YDIVHVHGSSSNGIILLLAAKAGVP-VRIAHS-----HN----TKDSSIKLRKIrknvlKKLIERLSTKYLACS----E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 192 EMIR-LYGTN-PKKITVIPGGVNLNRFQPTPQL-LARRVLHFSINRLIALYVGRIERRKGIDTLLEAVAELarlmPDKRP 268
Cdd:cd03812 146 DAGEwLFGEVeNGKFKVIPNGIDIEKYKFNKEKrRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEEL----KKKNP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 269 IMRCYIAGgnpkghkskvmEPSELKEWERLqgiVDKLGIKDIVRFLGgiNRELLTFYYAAADVTVVPSYYEPFGLVPLES 348
Cdd:cd03812 222 NVKLVLVG-----------EGELKEKIKEK---VKELGLEDKVIFLG--FRNDVSEILSAMDVFLFPSLYEGLPLVAVEA 285
|
330
....*....|
gi 1083501128 349 MASGTPVVAS 358
Cdd:cd03812 286 QASGLPCLLS 295
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
182-420 |
3.00e-15 |
|
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: 76.57 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 182 IIATSPQMRDEMIRLYGTnpKKITVIPGGVnlnrfqpTPQLLARRVLHFSiNRLIALYVGRIERRKGIDTLLEAVAELAR 261
Cdd:cd04949 118 IVSTEQQKQDLSERFNKY--PPIFTIPVGY-------VDQLDTAESNHER-KSNKIITISRLAPEKQLDHLIEAVAKAVK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 262 lmpdKRPIMRCYIAGgnpkghkskvmepsELKEWERLQGIVDKLGIKDIVRFLGGINRelLTFYYAAADVTVVPSYYEPF 341
Cdd:cd04949 188 ----KVPEITLDIYG--------------YGEEREKLKKLIEELHLEDNVFLKGYHSN--LDQEYQDAYLSLLTSQMEGF 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 342 GLVPLESMASGTPVVASRVG-GIQWTIRDGKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERVKLFSWDNIADQ 420
Cdd:cd04949 248 GLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAEKYSTENVMEK 327
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
203-388 |
6.36e-15 |
|
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: 76.25 E-value: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 203 KITVIPGGVNLNRFQPTPQllARRVL----HFSINRLIALYVGR-IERRKGIDTLLEAVAELARLMPDKRPImrcyIAGG 277
Cdd:cd03818 180 RISVIHDGVDTDRLAPDPA--ARLRLlngtELKAGDPVITYVARnLEPYRGFHVFMRALPRIQARRPDARVV----VVGG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 278 NPKGHKSkvmEPSELKEWeRLQGIVDKLGIKDIVRFLGGINRELLTFYYAAADVTVVPSYyePF----GLvpLESMASGT 353
Cdd:cd03818 254 DGVSYGS---PPPDGGSW-KQKMLAELGVDLERVHFVGKVPYDQYVRLLQLSDAHVYLTY--PFvlswSL--LEAMACGC 325
|
170 180 190
....*....|....*....|....*....|....*
gi 1083501128 354 PVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERI 388
Cdd:cd03818 326 PVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAV 360
|
|
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
37-414 |
2.31e-14 |
|
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: 75.59 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 37 GGENVYVLELTRALSRLG--WHTDVYTRASS--------------LKTTHIAKVSQD------ARVIRLKAGPVS-FVPR 93
Cdd:TIGR02468 195 GGQVKYVVELARALGSMPgvYRVDLLTRQVSspdvdwsygeptemLTPRSSENDGDEmgessgAYIIRIPFGPRDkYIPK 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 94 DKLFTYMPEYVESFLK--FQKENKL-EYL---------LIHGNYYFSGWAALQSAKVLGIPFVNTFHTLGIVR-HNFLKD 160
Cdd:TIGR02468 275 EELWPYIPEFVDGALShiVNMSKVLgEQIgsghpvwpyVIHGHYADAGDSAALLSGALNVPMVLTGHSLGRDKlEQLLKQ 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 161 TDPSPHE---------RIAIEKEIMTADNRIIATSPQMRDEMIRLY-GTNPK---------------------KITVIPG 209
Cdd:TIGR02468 355 GRMSKEEinstykimrRIEAEELSLDASEIVITSTRQEIEEQWGLYdGFDVIlerklrararrgvscygrfmpRMAVIPP 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 210 GVNLNRF-------------------QPTPQLLARrVLHFSIN--RLIALYVGRIERRKGIDTLLEAVAE------LARL 262
Cdd:TIGR02468 435 GMEFSHIvphdgdmdgetegneehpaKPDPPIWSE-IMRFFTNprKPMILALARPDPKKNITTLVKAFGEcrplreLANL 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 263 ---MPDKRPIMRcyIAGGNpkghkSKVMEpSELKewerlqgIVDKLGIKDIVRFLGGINR-ELLTFYYAAAD---VTVVP 335
Cdd:TIGR02468 514 tliMGNRDDIDE--MSSGS-----SSVLT-SVLK-------LIDKYDLYGQVAYPKHHKQsDVPDIYRLAAKtkgVFINP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 336 SYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERIRYLMthatAHKLL----RENGIERVKL 411
Cdd:TIGR02468 579 AFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKLV----ADKQLwaecRQNGLKNIHL 654
|
...
gi 1083501128 412 FSW 414
Cdd:TIGR02468 655 FSW 657
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
191-428 |
1.15e-13 |
|
GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.
Pssm-ID: 411604 [Multi-domain] Cd Length: 489 Bit Score: 72.66 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 191 DEMIRLYGTN----------PKKITVIPGGVNLNRFQPtpqLLARRVLHfsINRLIALyVGRIERRKGIDTLLEAVAELA 260
Cdd:NF038011 259 DPIVALYEGNrlrqiadgapPERTRVIPNGIDLPRLAP---LRAQRPAG--IPPVVGL-IGRVVPIKDIKTFIRAMRTVV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 261 RLMPDkrpiMRCYIAGgnPKGHkskvmEPSELKEwerLQGIVDKLGIKDIVRFLGGIN-RELLtfyyAAADVTVVPSYYE 339
Cdd:NF038011 333 RAMPE----AEGWIVG--PEEE-----DPAYAAE---CRSLVASLGLQDKVKFLGFQKiDDLL----PQVGLMVLSSISE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 340 PFGLVPLESMASGTPVVASRVGGIQWTI-------RD-GKSGYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIERVKL 411
Cdd:NF038011 395 ALPLVVLEAFAAGVPVVTTDVGSCRQLIegldeedRAlGAAGEVVAIADPQALARAALDLLRDPQRWQAAQAAGLARVER 474
|
250
....*....|....*..
gi 1083501128 412 FSWDniaDQMSDLYQDV 428
Cdd:NF038011 475 YYTE---ELMFDRYREL 488
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
228-410 |
1.54e-13 |
|
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: 71.97 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 228 LHFSIN--RLIALYVGRIERRKGIDTLLEAVAELARLMPDKRPImrcYIAGGNPKGHKSKVMepseLKEWERLQGIvdkl 305
Cdd:cd03792 189 KPFVIDpeRPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLV---ICGHGAVDDPEGSVV----YEEVMEYAGD---- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 306 gIKDI-VRFLGGINRELLTFYyAAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAF 384
Cdd:cd03792 258 -DHDIhVLRLPPSDQEINALQ-RAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAV 335
|
170 180
....*....|....*....|....*.
gi 1083501128 385 aeRIRYLMTHATAHKLLRENGIERVK 410
Cdd:cd03792 336 --RILRLLTDPELRRKMGLAAREHVR 359
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
120-363 |
2.79e-13 |
|
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: 71.12 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 120 LIHGNYYFSGWA--ALQSAKVLGIPFVNTFHTL-------GIVRHNFLKDTdpspheriaiekeiMTADNRIIATSPQMR 190
Cdd:cd03796 91 IVHGHQAFSSLAheALFHARTLGLKTVFTDHSLfgfadasSILTNKLLRFS--------------LADIDHVICVSHTSK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 191 DEMIRLYGTNPKKITVIPGGVNLNRFQPTPQllarrvlHFSINRLIALYVGRIERRKGIDTLLEAVAELARLMPDKRPIm 270
Cdd:cd03796 157 ENTVLRASLDPRIVSVIPNAVDSSDFTPDPS-------KPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFI- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 271 rcyIAGGNPKGHkskvmepselkeweRLQGIVDKLGIKDIVRFLGGIN----RELLTfyyaAADVTVVPSYYEPFGLVPL 346
Cdd:cd03796 229 ---IGGDGPKRI--------------ELEEMREKYQLQDRVELLGAVPheevRDVLV----QGHIFLNTSLTEAFCIAIV 287
|
250
....*....|....*..
gi 1083501128 347 ESMASGTPVVASRVGGI 363
Cdd:cd03796 288 EAASCGLLVVSTRVGGI 304
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
326-428 |
5.03e-13 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 70.89 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 326 YAAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRD------GKSGYLVEPGNAKAFAERIRY---LMTHAT 396
Cdd:COG0297 367 YAGADFFLMPSRFEPCGLNQMYALRYGTVPIVRRTGGLADTVIDyneatgEGTGFVFDEYTAEALLAAIRRalaLYRDPE 446
|
90 100 110
....*....|....*....|....*....|..
gi 1083501128 397 AHKLLRENGIERvkLFSWDNIADQMSDLYQDV 428
Cdd:COG0297 447 AWRKLQRNAMKQ--DFSWEKSAKEYLELYREL 476
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
326-429 |
4.77e-10 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 61.29 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 326 YAAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDG------KSGYLVEPGNAKAFAERIRYLMTHATAHK 399
Cdd:PRK00654 354 YAGADMFLMPSRFEPCGLTQLYALRYGTLPIVRRTGGLADTVIDYnpedgeATGFVFDDFNAEDLLRALRRALELYRQPP 433
|
90 100 110
....*....|....*....|....*....|...
gi 1083501128 400 L---LRENGIERVklFSWDNIADQMSDLYQDVV 429
Cdd:PRK00654 434 LwraLQRQAMAQD--FSWDKSAEEYLELYRRLL 464
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
183-375 |
6.42e-10 |
|
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: 60.38 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 183 IATSPQMRDEMIRLYGtnpKKITVIPGGVNLNRFQPtpqlLARRVLHFsinrliaLYVGRIERRKGIDTLLEAVAELARl 262
Cdd:cd03804 162 IANSQFVARRIKKFYG---RESTVIYPPVDTDAFAP----AADKEDYY-------LTASRLVPYKRIDLAVEAFNELPK- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 263 mpdkrpimRCYIAGGNPkghkskvmepselkEWERLQGIVdklgiKDIVRFLGGINRELLTFYYAAADVTVVPSYyEPFG 342
Cdd:cd03804 227 --------RLVVIGDGP--------------DLDRLRAMA-----SPNVEFLGYQPDEVLKELLSKARAFVFAAE-EDFG 278
|
170 180 190
....*....|....*....|....*....|...
gi 1083501128 343 LVPLESMASGTPVVASRVGGIQWTIRDGKSGYL 375
Cdd:cd03804 279 IVPVEAQACGTPVIAFGKGGALETVRPGPTGIL 311
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
150-408 |
2.85e-09 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 58.83 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 150 LGIVRHNFLKdtdpspheRIA--IEKEIMTADNRIIATSPQMRDEMIRlYGTNPKKITVIPGGVNLNRFQPTPQ---LLA 224
Cdd:PRK10307 149 LGLLKGGKVA--------RLAtaFERSLLRRFDNVSTISRSMMNKARE-KGVAAEKVIFFPNWSEVARFQPVADadvDAL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 225 RRVLHFSINRLIALYVGRIERRKGIDTLLEAvaelARLMPDKRPIMRCYIAGGNPKGhkskvmepsELKEWERLQGIvdk 304
Cdd:PRK10307 220 RAQLGLPDGKKIVLYSGNIGEKQGLELVIDA----ARRLRDRPDLIFVICGQGGGKA---------RLEKMAQCRGL--- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 305 lgikDIVRFLGGINRELLTFYYAAADVTVVPSYYEPFGLV-P--LESM-ASGTPVVAsrvggiqwTIRDGKS-------- 372
Cdd:PRK10307 284 ----PNVHFLPLQPYDRLPALLKMADCHLLPQKAGAADLVlPskLTNMlASGRNVVA--------TAEPGTElgqlvegi 351
|
250 260 270
....*....|....*....|....*....|....*.
gi 1083501128 373 GYLVEPGNAKAFAERIRYLMTHATAHKLLRENGIER 408
Cdd:PRK10307 352 GVCVEPESVEALVAAIAALARQALLRPKLGTVAREY 387
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
242-388 |
4.03e-09 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 58.84 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 242 RIERRKGIDTLLEAVAELARLmpdkRPIMRCYIAGGNPKGHKSKVMEpsELKEWERLQGIVDKLGIKDIVRFLGG-INR- 319
Cdd:PLN00142 581 RLDRVKNLTGLVEWYGKNKRL----RELVNLVVVGGFIDPSKSKDRE--EIAEIKKMHSLIEKYNLKGQFRWIAAqTNRv 654
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083501128 320 ---ELltfYYAAAD---VTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKAFAERI 388
Cdd:PLN00142 655 rngEL---YRYIADtkgAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDEAANKI 726
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
334-421 |
4.12e-07 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 47.98 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 334 VPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEpgNAKAFAERIRYLMTHATAHKLLRENGIERVKL-F 412
Cdd:pfam13524 5 PSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERVLAeH 82
|
....*....
gi 1083501128 413 SWDNIADQM 421
Cdd:pfam13524 83 TYAHRAEQL 91
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
254-426 |
1.32e-06 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 50.80 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 254 EAVAELARLMPDKRPIMRCYIAGGNPKGH-KSKVMEPSELKEWERLQGIVDKLGIKDIVRFLGGINRelLTFYYAAADVT 332
Cdd:PRK15179 518 FTVGTVMRVDDNKRPFLWVEAAQRFAASHpKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRR--VGYWLTQFNAF 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 333 VVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYLVEPGNAKA--FAERIRYLMTHATAHKLLRENGIERV- 409
Cdd:PRK15179 596 LLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTApdVAEALARIHDMCAADPGIARKAADWAs 675
|
170
....*....|....*..
gi 1083501128 410 KLFSWDNIADQMSDLYQ 426
Cdd:PRK15179 676 ARFSLNQMIASTVRCYQ 692
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
166-388 |
3.01e-06 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 49.32 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 166 HERIAIEKEIMTADNRIIATSPqMRDEMIRLyGTNPKKITVIPGGVNLNRfQPTPQLLARRVLHFsinrliaLYVGRI-- 243
Cdd:PRK09922 122 HKKHAECKKITCADYHLAISSG-IKEQMMAR-GISAQRISVIYNPVEIKT-IIIPPPERDKPAVF-------LYVGRLkf 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 244 ERRKGIDTLLEAVAELarlmpdKRPIMRCYIAGGNpkghkskvmEPSELKEWERlqgivdKLGIKDIVRFLGGINR--EL 321
Cdd:PRK09922 192 EGQKNVKELFDGLSQT------TGEWQLHIIGDGS---------DFEKCKAYSR------ELGIEQRIIWHGWQSQpwEV 250
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083501128 322 LTFYYAAADVTVVPSYYEPFGLVPLESMASGTPVVASR-VGGIQWTIRDGKSGYLVEPGNAKAFAERI 388
Cdd:PRK09922 251 VQQKIKNVSALLLTSKFEGFPMTLLEAMSYGIPCISSDcMSGPRDIIKPGLNGELYTPGNIDEFVGKL 318
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
327-429 |
6.56e-06 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 48.56 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 327 AAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGK---------SGYLVEPGNAKAFA---ERIRYLMTH 394
Cdd:PRK14099 368 AGADALLVPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVDANemaiatgvaTGVQFSPVTADALAaalRKTAALFAD 447
|
90 100 110
....*....|....*....|....*....|....*
gi 1083501128 395 ATAHKLLRENGIerVKLFSWDNIADQMSDLYQDVV 429
Cdd:PRK14099 448 PVAWRRLQRNGM--TTDVSWRNPAQHYAALYRSLV 480
|
|
| PHA01633 |
PHA01633 |
putative glycosyl transferase group 1 |
240-356 |
1.83e-05 |
|
putative glycosyl transferase group 1
Pssm-ID: 107050 [Multi-domain] Cd Length: 335 Bit Score: 46.51 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 240 VGRIERRKGIDTLLEAVAELARLMPDKRPIMRCYIAGgnpkgHKskvmepsELKEWERLQGIvdklgikDIVRFLGGINR 319
Cdd:PHA01633 154 VSGLTKRKNMDLMLQVFNELNTKYPDIAKKIHFFVIS-----HK-------QFTQLEVPANV-------HFVAEFGHNSR 214
|
90 100 110
....*....|....*....|....*....|....*..
gi 1083501128 320 ELLTFYYAAADVTVVPSYYEPFGLVPLESMASGTPVV 356
Cdd:PHA01633 215 EYIFAFYGAMDFTIVPSGTEGFGMPVLESMAMGTPVI 251
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
166-429 |
2.03e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 166 HERIAIEKEIMTADNRIIATSP----QMRDEMIR-LYGT---NPKKITVIPGGVNLNRFQP-TPQLLArrvLHFSINRLI 236
Cdd:PLN02939 681 HGRINVVKGAIVYSNIVTTVSPtyaqEVRSEGGRgLQDTlkfHSKKFVGILNGIDTDTWNPsTDRFLK---VQYNANDLQ 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 237 ALYVGRIERRKGI-----DTLLEAVAELARLMPDKR-PIMRCYIAGGNPKGHKSKVMEPSELKEWER-LQGIVDKLGIKD 309
Cdd:PLN02939 758 GKAANKAALRKQLglssaDASQPLVGCITRLVPQKGvHLIRHAIYKTAELGGQFVLLGSSPVPHIQReFEGIADQFQSNN 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 310 IVRFLGGINRELLTFYYAAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDG---------KSGYLVEPGN 380
Cdd:PLN02939 838 NIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSVFDFddetipvelRNGFTFLTPD 917
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1083501128 381 AKAFAERIRYLMTHATAHKLLRENGIERVKL--FSWDNIADQMSDLYQDVV 429
Cdd:PLN02939 918 EQGLNSALERAFNYYKRKPEVWKQLVQKDMNidFSWDSSASQYEELYQRAV 968
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
247-375 |
1.83e-04 |
|
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.
Pssm-ID: 340854 [Multi-domain] Cd Length: 401 Bit Score: 43.60 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 247 KGIDTLLEAVAELARLMPDKRpIMRCYIAGGnpkghkskvmepselKEWERLQGIVDKLGIKDIVRFLGGI-NRELLTFY 325
Cdd:cd04946 237 KRIDLIIETLNSLCVAHPSIC-ISWTHIGGG---------------PLKERLEKLAENKLENVKVNFTGEVsNKEVKQLY 300
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1083501128 326 YA-AADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRDGKSGYL 375
Cdd:cd04946 301 KEnDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLL 351
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
326-369 |
2.10e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 40.62 E-value: 2.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1083501128 326 YAAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIRD 369
Cdd:PLN02316 917 YAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTVFD 960
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
327-428 |
4.86e-03 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 39.33 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 327 AAADVTVVPSYYEPFGLVPLESMASGTPVVASRVGGIQWTIR----DGKSGYLVEPGNAKAFAERIRYLMthATAH---- 398
Cdd:PRK14098 380 AGLDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETIEevseDKGSGFIFHDYTPEALVAKLGEAL--ALYHdeer 457
|
90 100 110
....*....|....*....|....*....|..
gi 1083501128 399 --KLLRENgieRVKLFSWDNIADQMSDLYQDV 428
Cdd:PRK14098 458 weELVLEA---MERDFSWKNSAEEYAQLYREL 486
|
|
| GT3_GSY2-like |
cd03793 |
glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related ... |
333-441 |
6.41e-03 |
|
glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related to the GT3 family of glycosyltransferases, catalyzes the transfer of a glucose molecule from UDP-glucose to a terminal branch of a glycogen molecule, a rate-limit step of glycogen biosynthesis. GSY2, the member of this family in S. cerevisiae, has been shown to possess glycogen synthase activity.
Pssm-ID: 340824 [Multi-domain] Cd Length: 590 Bit Score: 38.89 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083501128 333 VVPSYYEPFGLVPLESMASGTPVVASRVGG----IQWTIRDGKS-GYLVEPGNAKAFAERI----RYLMTHATAHKllRE 403
Cdd:cd03793 479 VFPSYYEPWGYTPAECTVMGIPSITTNLSGfgcfMEEHIEDPKSyGIYIVDRRFKSPDESVqqltQYMYEFCQQSR--RQ 556
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90 100 110
....*....|....*....|....*....|....*...
gi 1083501128 404 NGIERvklfswdNIADQMSDLYQDVVIDYFYRKAFHLA 441
Cdd:cd03793 557 RIIQR-------NRTERLSDLLDWRYLGRFYRKARQLA 587
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