|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
1-430 |
0e+00 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 822.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 1 MTIAEVRPEDGEDDSPPLLDPEINSIPRRIALFIEPSPFAYVSGYKNRFQNFIRYLREMGDEVMVVTTHEGVPEEFYGAK 80
Cdd:PLN02871 32 AVLVSVRRVASSEAPPPLLDTDSRSRPRRIALFVEPSPFSYVSGYKNRFQNFIRYLREMGDEVLVVTTDEGVPQEFHGAK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 81 LIGSRSFPCPLYHKVPLSLALSPRIISEVVRFKPDIIHASSPGIMVFGALIIAKLSSVPLVLSYHTHVPVYIPRYTFSWL 160
Cdd:PLN02871 112 VIGSWSFPCPFYQKVPLSLALSPRIISEVARFKPDLIHASSPGIMVFGALFYAKLLCVPLVMSYHTHVPVYIPRYTFSWL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 161 VKPMWLVIKFLHRAADLTLVPSAAIGMDLEAERVTAANKIRLWNKGVDSASFHPRFRSQEMRLRLSGDEPDKPLIIHVGR 240
Cdd:PLN02871 192 VKPMWDIIRFLHRAADLTLVTSPALGKELEAAGVTAANRIRVWNKGVDSESFHPRFRSEEMRARLSGGEPEKPLIVYVGR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 241 LGVEKSLDFLKRIMDRLPEARIAIVGDGPYREELEKMFTGMPAVFTGMLSGEELSQAYASSDIFVMPSESETLGLVVLEA 320
Cdd:PLN02871 272 LGAEKNLDFLKRVMERLPGARLAFVGDGPYREELEKMFAGTPTVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 321 MSSGIPVIGARAGGVPDIIPPEQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARKEMEKYDWKAATRIIRNEH 400
Cdd:PLN02871 352 MASGVPVVAARAGGIPDIIPPDQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEKWDWRAATRKLRNEQ 431
|
410 420 430
....*....|....*....|....*....|
gi 1279756475 401 YNLAIWFWRKKRVEFLRPFQWLFNRIFPSP 430
Cdd:PLN02871 432 YSAAIWFWRKKRAQLLGPVQWLPAQLFPAP 461
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
29-401 |
5.49e-140 |
|
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: 404.75 E-value: 5.49e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 29 RIALFIEPSPFAyVSGYKNRFQNFIRYLREMGDEVMVVTTHEGVPEEFYGAKLIGSRSFPCPLYHKVPLSLALSPRIISE 108
Cdd:cd03814 1 RIALVTDTYHPQ-VNGVVRTLERLVDHLRRRGHEVRVVAPGPFDEAESAEGRVVSVPSFPLPFYPEYRLALPLPRRVRRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 109 VVRFKPDIIHASSPGIMVFGALIIAKLSSVPLVLSYHTHVPVYIPRYTFSWLVKPMWLVIKFLHRAADLTLVPSAAIGMD 188
Cdd:cd03814 80 IKEFQPDIIHIATPGPLGLAALRAARRLGLPVVTSYHTDFPEYLSYYTLGPLSWLAWAYLRWFHNPFDTTLVPSPSIARE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 189 LEAervTAANKIRLWNKGVDSASFHPRFRSQEMRLRLSgdEPDKPLIIHVGRLGVEKSLDFLKRIMDRLPE---ARIAIV 265
Cdd:cd03814 160 LEG---HGFERVRLWPRGVDTELFHPSRRDAALRRRLG--PPGRPLLLYVGRLAPEKNLEALLDADLPLAAsppVRLVVV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 266 GDGPYREELEkmFTGMPAVFTGMLSGEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIppeQDG 345
Cdd:cd03814 235 GDGPARAELE--ARGPDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIV---RPG 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1279756475 346 KIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARKEMEKYDWKAATRIIRNEHY 401
Cdd:cd03814 310 GTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERYSWEAFLDNLLDYYA 365
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
29-388 |
3.57e-66 |
|
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: 215.61 E-value: 3.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 29 RIALFIEpSPFAYVSGYKNRFQNFIRYLREMGDEVMVVTT---HEGVPEEFYGaklIGSRSFPCPLYHKVPLSLALSPRI 105
Cdd:cd03817 1 KIAIFTD-TYLPQVNGVATSVRNLARALEKRGHEVYVITPsdpGAEDEEEVVR---YRSFSIPIRKYHRQHIPFPFKKAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 106 ISEVVRFKPDIIHASSPGIMVFGALIIAKLSSVPLVLSYHTHVPVYIPRYTFSWLVKP---MWLVIKFLHRAaDLTLVPS 182
Cdd:cd03817 77 IDRIKELGPDIIHTHTPFSLGKLGLRIARKLKIPIVHTYHTMYEDYLHYIPKGKLLVKavvRKLVRRFYNHT-DAVIAPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 183 AAIGMDLEAERVTaaNKIRLWNKGVDSASFhpRFRSQEMRLRLSGDEPDKPLIIHVGRLGVEKSLDFLKRIMDRL---PE 259
Cdd:cd03817 156 EKIKDTLREYGVK--GPIEVIPNGIDLDKF--EKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELkkePN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 260 ARIAIVGDGPYREELEKMFTGMPA----VFTGMLSGEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGV 335
Cdd:cd03817 232 IKLVIVGDGPEREELKELARELGLadkvIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAA 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1279756475 336 PDIIppeQDGKIGHLYTPGDIdDCLNKLKPLLDNRELRETMGKAARKEMEKYD 388
Cdd:cd03817 312 SELV---EDGENGFLFEPNDE-TLAEKLLHLRENLELLRKLSKNAEISAREFA 360
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
29-398 |
1.25e-57 |
|
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: 193.52 E-value: 1.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 29 RIALFIePSPFAYVSGYKNRFQNFIRYLREMGDEVMVVTT-HEGVPEEFYGAKLIGSRSFPCPLYHKVPLSLAlspRIIS 107
Cdd:cd03801 1 KILLLS-PELPPPVGGAERHVRELARALAARGHDVTVLTPaDPGEPPEELEDGVIVPLLPSLAALLRARRLLR---ELRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 108 EVVRFKPDIIHASSPGIMVFGALIiAKLSSVPLVLSYHTHVPVYIPRYTF---SWLVKpmwlvIKFLHRAADLTLVPSAA 184
Cdd:cd03801 77 LLRLRKFDVVHAHGLLAALLAALL-ALLLGAPLVVTLHGAEPGRLLLLLAaerRLLAR-----AEALLRRADAVIAVSEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 185 IGMDLEAERVTAANKIRLWNKGVDSASFHPRFRsqemrlRLSGDEPDKPLIIHVGRL----GVEKSLDFLKRIMDRLPEA 260
Cdd:cd03801 151 LRDELRALGGIPPEKIVVIPNGVDLERFSPPLR------RKLGIPPDRPVLLFVGRLsprkGVDLLLEALAKLLRRGPDV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 261 RIAIVG-DGPYREELEKMFTGMPA--VFTGMLSGEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPD 337
Cdd:cd03801 225 RLVIVGgDGPLRAELEELELGLGDrvRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPE 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279756475 338 IIppeQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARKE-MEKYDWKAATRIIRN 398
Cdd:cd03801 305 VV---EDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERvAERFSWERVAERLLD 363
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
51-402 |
6.14e-41 |
|
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: 149.45 E-value: 6.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 51 NFIRYLREMGDEVMVVTT-HEGVPEEFYGAKLIGSRSFPCPLYHKVPLSLALSPRI----------ISEVVRFKPDIIHA 119
Cdd:cd03798 22 RQVRALSRRGVDVEVLAPaPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAplrapslaklLKRRRRGPPDLIHA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 120 SSPGIMVFGALIIAKLSSVPLVLSYHTHvpvyiPRYTFSW--LVKPMwlvIKFLHRAADLTLVPSAAIGMDLEAERVTAA 197
Cdd:cd03798 102 HFAYPAGFAAALLARLYGVPYVVTEHGS-----DINVFPPrsLLRKL---LRWALRRAARVIAVSKALAEELVALGVPRD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 198 NKIRLWNkGVDSASFHPRfrsqemrLRLSGDEPDKPLIIHVGRL----GVEKSLDFLKRIMDRLPEARIAIVGDGPYREE 273
Cdd:cd03798 174 RVDVIPN-GVDPARFQPE-------DRGLGLPLDAFVILFVGRLiprkGIDLLLEAFARLAKARPDVVLLIVGDGPLREA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 274 LEKM--FTGMPA--VFTGMLSGEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIPpeqDGKIGH 349
Cdd:cd03798 246 LRALaeDLGLGDrvTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVG---DPETGL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1279756475 350 LYTPGDIDDCLNKLKPLLDNRELRETMGKAARKEMEKYDWKAATRIIRnEHYN 402
Cdd:cd03798 323 LVPPGDADALAAALRRALAEPYLRELGEAARARVAERFSWVKAADRIA-AAYR 374
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
38-381 |
1.32e-36 |
|
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.
Pssm-ID: 340846 [Multi-domain] Cd Length: 345 Bit Score: 137.10 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 38 PFAYVSGYKNRFQNFIRYLREMGDEVMVVTTheGVPE-EFYGAKLIGSRSFPCPLYHkVPLSLALSPRIISevvRFKPDI 116
Cdd:cd03819 6 PALEIGGAETYILDLARALAERGHRVLVVTA--GGPLlPRLRQIGIGLPGLKVPLLR-ALLGNVRLARLIR---RERIDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 117 IHASSPGIMVFGALIiAKLSSVPLVLSYHTHVPVYIPRYTFSWLVKPMWL----VIKFLHRAADltlvpsAAIGMDleae 192
Cdd:cd03819 80 IHAHSRAPAWLGWLA-SRLTGVPLVTTVHGSYLATYHPKDFALAVRARGDrviaVSELVRDHLI------EALGVD---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 193 rvtaANKIRLWNKGVDSASFHPRfrSQEMRLRLSGDEPDKPLIIHVGRLGVEKSLDFLKRIMDRLPEA---RIAIVGDGP 269
Cdd:cd03819 149 ----PERIRVIPNGVDTDRFPPE--AEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEpdfRLLVAGDGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 270 YREELEKMFTGM---PAV-FTGMLsgEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIPPeqdG 345
Cdd:cd03819 223 ERDEIRRLVERLglrDRVtFTGFR--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVH---G 297
|
330 340 350
....*....|....*....|....*....|....*.
gi 1279756475 346 KIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAAR 381
Cdd:cd03819 298 RTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAA 333
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
231-382 |
1.23e-35 |
|
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: 128.93 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 231 DKPLIIHVGRLGVEKSLDFL----KRIMDRLPEARIAIVGDGPYREELEKM--FTGMPA--VFTGMLSGEELSQAYASSD 302
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLikafALLKEKNPNLKLVIAGDGEEEKRLKKLaeKLGLGDnvIFLGFVSDEDLPELLKIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 303 IFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIppeQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARK 382
Cdd:pfam00534 81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV---KDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
102-381 |
2.34e-34 |
|
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340860 [Multi-domain] Cd Length: 365 Bit Score: 131.42 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 102 SPRIISEVVRFKPDIIHASspgimvFG-----ALIIAKLSSVPLVLSYH-THVPVYIPRYTFS--WLVKPMwLVIKFLHR 173
Cdd:cd05844 70 SAPRLGGAAGLAPALVHAH------FGrdgvyALPLARALGVPLVVTFHgFDITTSRAWLAASpgWPSQFQ-RHRRALQR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 174 AADLTLVPSAAIgMDLEAERVTAANKIRLWNKGVDSASFHPRFRSqemrlrlsgdePDKPLIIHVGRLGVEKSLDFL--- 250
Cdd:cd05844 143 PAALFVAVSGFI-RDRLLARGLPAERIHVHYIGIDPAKFAPRDPA-----------ERAPTILFVGRLVEKKGCDVLiea 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 251 -KRIMDRLPEARIAIVGDGPYREELEKMFTGMPAV-FTGMLSGEELSQAYASSDIFVMPS------ESETLGLVVLEAMS 322
Cdd:cd05844 211 fRRLAARHPTARLVIAGDGPLRPALQALAAALGRVrFLGALPHAEVQDWMRRAEIFCLPSvtaasgDSEGLGIVLLEAAA 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1279756475 323 SGIPVIGARAGGVPDIIppeQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAAR 381
Cdd:cd05844 291 CGVPVVSSRHGGIPEAI---LDGETGFLVPEGDVDALADALQALLADRALADRMGGAAR 346
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
50-387 |
7.26e-33 |
|
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: 127.05 E-value: 7.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 50 QNFIRYLREMGDEVMVVT-THEGVpeefYGAKLigsRSFPCPLYH---KVPLSLALSPRIISEVVRFKPDIIHASSPGIM 125
Cdd:cd03807 19 LRLLEHMDKSRFEHVVISlTGDGV----LGEEL---LAAGVPVVClglSSGKDPGVLLRLAKLIRKRNPDVVHTWMYHAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 126 VFGAlIIAKLSS-VPLVLSYHThvpvyipRYTFSWLVKPMWLVIKFLHRAADLTLVPSAAIGMDLEAERVtAANKIRLWN 204
Cdd:cd03807 92 LIGG-LAAKLAGgVKVIWSVRS-------SNIPQRLTRLVRKLCLLLSKFSPATVANSSAVAEFHQEQGY-AKNKIVVIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 205 KGVDSASFHPRFRSQEMRLRLSGDEPDKPLIIHVGRLGVEKS-LDFLK---RIMDRLPEARIAIVGDGPYREELEKMF-- 278
Cdd:cd03807 163 NGIDLFKLSPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDhSDLLRaaaLLVETHPDLRLLLVGRGPERPNLERLLle 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 279 TGMPA--VFTGmlSGEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIPPeqdgKIGHLYTPGDI 356
Cdd:cd03807 243 LGLEDrvHLLG--ERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDD----GTGFLVPAGDP 316
|
330 340 350
....*....|....*....|....*....|.
gi 1279756475 357 DDCLNKLKPLLDNRELRETMGKAARKEMEKY 387
Cdd:cd03807 317 QALADAIRALLEDPEKRARLGRAARERIANE 347
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
113-394 |
4.50e-31 |
|
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: 122.73 E-value: 4.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 113 KPDIIHAS-SPGIMVfgALIIAKLSSVPLVLSYHTHVPVYIPRYTFSWLVKPMWLVI--KFLHRAADLTLVPSAAIGMDL 189
Cdd:cd03800 101 RYDLIHSHyWDSGLV--GALLARRLGVPLVHTFHSLGRVKYRHLGAQDTYHPSLRITaeEQILEAADRVIASTPQEADEL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 190 EAERVTAANKIRLWNKGVDSASFHPRFRSQEMRLRLsGDEPDKPLIIHVGRLGVEKSLDFLKRIMDRLPE----ARIAIV 265
Cdd:cd03800 179 ISLYGADPSRINVVPPGVDLERFFPVDRAEARRARL-LLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPElrelANLVLV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 266 G---------DGPYREELEKMFTGMPAV-FTGMLSGEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGV 335
Cdd:cd03800 258 GgpsddplsmDREELAELAEELGLIDRVrFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGL 337
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 336 PDIIppeQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARKE-MEKYDWKAATR 394
Cdd:cd03800 338 QDIV---RDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERaRAHYTWESVAD 394
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
232-369 |
4.63e-30 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 113.38 E-value: 4.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 232 KPLIIHVGRLGVE-KSLDFL----KRIMDRLPEARIAIVGDGPyREELEKMFTGMPA--VFTGMLsgEELSQAYASSDIF 304
Cdd:pfam13692 1 RPVILFVGRLHPNvKGVDYLleavPLLRKRDNDVRLVIVGDGP-EEELEELAAGLEDrvIFTGFV--EDLAELLAAADVF 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279756475 305 VMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIppeqDGKIGHLYTPGDIDDCLNKLKPLLDN 369
Cdd:pfam13692 78 VLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV----DGENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
51-387 |
8.81e-29 |
|
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: 115.53 E-value: 8.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 51 NFIRYLREMGDEVMVVTTHEGVPEEFYGAKLIGSRSFPCP-LYHKVPLSLALSPRIISEVVRFKPDIIHAsspgIMVFGA 129
Cdd:cd03811 20 NLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRvLKLIKLGLLKAILKLKRILKRAKPDVVIS----FLGFAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 130 LIIAKLSSVPLVLSYHTHVPvYIPRYTFSWLVKPMWLVIKFlhraADLTLVPSAAIGMDLEAERVTAANKIRLWNKGVDS 209
Cdd:cd03811 96 YIVAKLAAARSKVIAWIHSS-LSKLYYLKKKLLLKLKLYKK----ADKIVCVSKGIKEDLIRLGPSPPEKIEVIYNPIDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 210 ASFhpRFRSQEMRLRlsgDEPDKPLIIHVGRLGVEKSLDFL----KRIMDRLPEARIAIVGDGPYREELEKM-------- 277
Cdd:cd03811 171 DRI--RALAKEPILN---EPEDGPVILAVGRLDPQKGHDLLieafAKLRKKYPDVKLVILGDGPLREELEKLakelglae 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 278 ---FTGM---PAVFtgmlsgeelsqaYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIppeQDGKIGHLY 351
Cdd:cd03811 246 rviFLGFqsnPYPY------------LKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREIL---DDGENGLLV 310
|
330 340 350
....*....|....*....|....*....|....*....
gi 1279756475 352 TPGDIDDCLNKLKPLLDN---RELRETMGKAARKEMEKY 387
Cdd:cd03811 311 PDGDAAALAGILAALLQKkldAALRERLAKAQEAVFREY 349
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
51-400 |
1.38e-28 |
|
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: 115.39 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 51 NFIRYLREMGDEVMVVT-THEGVPEEFygaKLIGSRSFPCPLYHKVP------LSLALSPRIISEVvrfKPDIIHASS-- 121
Cdd:cd03808 18 PLIKALVKKGYEVHVIApDGDKLSDEL---KELGVKVIDIPILRRGInplkdlKALFKLYKLLKKE---KPDIVHCHTpk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 122 PGIMvfgALIIAKLSSVPLVLsYHTHVPvyipRYTFS------WLVKPMWlviKFLHRAADLTLVPSAAigmdlEAERVT 195
Cdd:cd03808 92 PGIL---GRLAARLAGVPKVI-YTVHGL----GFVFTegkllrLLYLLLE---KLALLFTDKVIFVNED-----DRDLAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 196 AANKIRLWNK------GVDSASFHPRfrsqemrlrLSGDEPDKPLIIHVGRLGVEKSLDFL----KRIMDRLPEARIAIV 265
Cdd:cd03808 156 KKGIIKKKKTvlipgsGVDLDRFQYS---------PESLPSEKVVFLFVARLLKDKGIDELieaaKILKKKGPNVRFLLV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 266 GDGPYREELEKMFTGMPA----VFTGMLSgeELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIpp 341
Cdd:cd03808 227 GDGELENPSEILIEKLGLegriEFLGFRS--DVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELV-- 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 342 eQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARKEME-KYDwkaaTRIIRNEH 400
Cdd:cd03808 303 -IDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEeKFD----EEKVVNKL 357
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
49-398 |
4.09e-28 |
|
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: 114.00 E-value: 4.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 49 FQNFIRYLREMGDEVMVVTTHEGVPEEFYGAKLIGSRSFPCPLYHKVPLSLALSPRIISEVVRFKPDIIHASSPgimvfg 128
Cdd:cd03809 20 TRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKPDLLHSPHN------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 129 aLIIAKLSSVPLVLSYHTHVPVYIPRYtFSWL-VKPMWLVIKFLHRAADLTLVPSAAIGMDLEAERVTAANKIRLWNKGV 207
Cdd:cd03809 94 -TAPLLLKGCPQVVTIHDLIPLRYPEF-FPKRfRLYYRLLLPISLRRADAIITVSEATRDDIIKFYGVPPEKIVVIPLGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 208 DSASFHPRfrsQEMRLRLSGDEPDkPLIIHVGRLGVEKSLDFLKRIMDRLPEA----RIAIVG-DGPYREELEKMFTGMP 282
Cdd:cd03809 172 DPSFFPPE---SAAVLIAKYLLPE-PYFLYVGTLEPRKNHERLLKAFALLKKQggdlKLVIVGgKGWEDEELLDLVKKLG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 283 A----VFTGMLSGEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARaggvpdiIP--PEQDGKIGHLYTPGDI 356
Cdd:cd03809 248 LggrvRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASN-------ISvlPEVAGDAALYFDPLDP 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1279756475 357 DDCLNKLKPLLDNRELRETMGKAARKEMEKYDWKAATRIIRN 398
Cdd:cd03809 321 ESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
52-396 |
6.21e-28 |
|
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: 113.98 E-value: 6.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 52 FIRYLREMGDEVMVVTTHEGVPEEFYGAKLIGSRS------FPCPLYHKVP--------LSLALSPRIISEVVRFKPDII 117
Cdd:cd03794 23 LAKELVRRGHEVTVLTPSPNYPLGRIFAGATETKDgirvirVKLGPIKKNGlirrllnyLSFALAALLKLLVREERPDVI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 118 HASSPGIM-VFGALIIAKLSSVPLVLSYHTHVP---VYIPRYTFSWLVKPMWLVIKFLHRAADLTLVPSAAIgMDLEAER 193
Cdd:cd03794 103 IAYSPPITlGLAALLLKKLRGAPFILDVRDLWPeslIALGVLKKGSLLKLLKKLERKLYRLADAIIVLSPGL-KEYLLRK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 194 VTAANKIRLWNKGVDsasfHPRFRSQ-EMRLRLSGDEPDKPLIIHVGRLGVEKSLDFLKRIMDRL---PEARIAIVGDGP 269
Cdd:cd03794 182 GVPKEKIIVIPNWAD----LEEFKPPpKDELRKKLGLDDKFVVVYAGNIGKAQGLETLLEAAERLkrrPDIRFLFVGDGD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 270 YREELEKMFT--GMPAV-FTGMLSGEELSQAYASSDIFVMP-SESETLGLVV----LEAMSSGIPVIGARAGGVPDIIpp 341
Cdd:cd03794 258 EKERLKELAKarGLDNVtFLGRVPKEEVPELLSAADVGLVPlKDNPANRGSSpsklFEYMAAGKPILASDDGGSDLAV-- 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1279756475 342 eQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARKE-MEKYDWKAATRII 396
Cdd:cd03794 336 -EINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELaEEKFSREKLADRL 390
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
70-386 |
6.78e-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: 113.14 E-value: 6.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 70 EGVPEEFYGAKLIGSRSFpcplyhKVPLSLALSPRIISEVVRF--KPDIIHASSPGIMVFGALIIAKLSSvPLVLSYHTH 147
Cdd:cd03795 44 ETPEKEENGIRIHRVKSF------LNVASTPFSPSYIKRFKKLakEYDIIHYHFPNPLADLLLFFSGAKK-PVVVHWHSD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 148 VpvyIPRYTFSWLVKPmwLVIKFLHRAaDLTLVPS---AAIGMDLEAERvtaaNKIRLWNKGVDSASF-HPRFRSQEMRL 223
Cdd:cd03795 117 I---VKQKKLLKLYKP--LMTRFLRRA-DRIIATSpnyVETSPTLREFK----NKVRVIPLGIDKNVYnIPRVDFENIKR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 224 RLSGdepdKPLIIHVGRLGVEKSLDFLKRIMDRLpEARIAIVGDGPYREELEKMFT--GMPAV-FTGMLSGEELSQAYAS 300
Cdd:cd03795 187 EKKG----KKIFLFIGRLVYYKGLDYLIEAAQYL-NYPIVIGGEGPLKPDLEAQIElnLLDNVkFLGRVDDEEKVIYLHL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 301 SDIFVMPS--ESETLGLVVLEAMSSGIPVIGAR-AGGVPDIIppeQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMG 377
Cdd:cd03795 262 CDVFVFPSvlRSEAFGIVLLEAMMCGKPVISTNiGTGVPYVN---NNGETGLVVPPKDPDALAEAIDKLLSDEELRESYG 338
|
....*....
gi 1279756475 378 KAARKEMEK 386
Cdd:cd03795 339 ENAKKRFEE 347
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
51-391 |
1.22e-27 |
|
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: 112.33 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 51 NFIRYLREMGDEVMVVTTHEGVPEEFY----GAKLIgsrSFPCPLYHKVPLSLA---LSPRIISEVVRFKPDIIHASSPG 123
Cdd:cd03820 21 NLANHLAKKGYDVTIISLDSAEKPPFYelddNIKIK---NLGDRKYSHFKLLLKyfkKVRRLRKYLKNNKPDVVISFRTS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 124 IMVFGALIIAKlssVPLVLSYHTHVPVYIPRYTFSWLvkpmwlvIKFLHRAADLTLVPSAAigmDLEAERVTAANKIRLW 203
Cdd:cd03820 98 LLTFLALIGLK---SKLIVWEHNNYEAYNKGLRRLLL-------RRLLYKRADKIVVLTEA---DKLKKYKQPNSNVVVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 204 NKGVDSASFHPrfrsqemrlrlSGDEPDKpLIIHVGRLGVEKSLDFL----KRIMDRLPEARIAIVGDGPYREELEKMFT 279
Cdd:cd03820 165 PNPLSFPSEEP-----------STNLKSK-RILAVGRLTYQKGFDLLieawALIAKKHPDWKLRIYGDGPEREELEKLID 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 280 G---------MPAVftgmlsgEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIG-ARAGGVPDIIppeQDGKIGH 349
Cdd:cd03820 233 KlgledrvklLGPT-------KNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISfDCPTGPSEII---EDGENGL 302
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1279756475 350 LYTPGDIDDCLNKLKPLLDNRELRETMGKAARKEMEKYDWKA 391
Cdd:cd03820 303 LVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAERFSIEK 344
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
99-394 |
2.02e-27 |
|
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.
Pssm-ID: 132132 [Multi-domain] Cd Length: 374 Bit Score: 112.12 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 99 LALSPRIISEVVRFKPDIIHasSPGIMVFGALIIAKLSSVPLVLSYHTHVPVYIP---RYTFSWL---VKPmwLVIKFLH 172
Cdd:TIGR03088 67 VAVYPQLYRLLRQLRPDIVH--TRNLAALEAQLPAALAGVPARIHGEHGRDVFDLdgsNWKYRWLrrlYRP--LIHHYVA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 173 RAADLTLVPSAAIGmdleaerVTAANKIRLWNkGVDSASFHPRFRSQEMRLRLSGDEPDKPLIIHVGRLGVEKSLDFLKR 252
Cdd:TIGR03088 143 VSRDLEDWLRGPVK-------VPPAKIHQIYN-GVDTERFHPSRGDRSPILPPDFFADESVVVGTVGRLQAVKDQPTLVR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 253 ----IMDRLPE----ARIAIVGDGPYREELEKMFTGMPAVFTGMLSGE--ELSQAYASSDIFVMPSESETLGLVVLEAMS 322
Cdd:TIGR03088 215 afalLVRQLPEgaerLRLVIVGDGPARGACEQMVRAAGLAHLVWLPGErdDVPALMQALDLFVLPSLAEGISNTILEAMA 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279756475 323 SGIPVIGARAGGVPDIIppeQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARKEME-KYDWKAATR 394
Cdd:TIGR03088 295 SGLPVIATAVGGNPELV---QHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEqQFSINAMVA 364
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
56-391 |
4.47e-27 |
|
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: 111.31 E-value: 4.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 56 LREMGDEVMVVTT---HEGVPEEFYGAKLIGSRSFP-CPLYHKVPLSLALSPRIISEVVRF--KPDIIHasSPGI---MV 126
Cdd:cd03821 27 LAALGHEVTIVSTgdgYESLVVEENGRYIPPQDGFAsIPLLRQGAGRTDFSPGLPNWLRRNlrEYDVVH--IHGVwtyTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 127 FGALIIAKLSSVPLVLSYHTHVPvyipryTFSW---LVKPMWLVIKFLHRAADLTLVPSAAIGMDLEA-ERVTAANKIRL 202
Cdd:cd03821 105 LAACKLARRRGIPYVVSPHGMLD------PWALqqkHWKKRIALHLIERRNLNNAALVHFTSEQEADElRRFGLEPPIAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 203 WNKGVDSasfhPRFRSQEMRLRLSGDEPDKPLIIHVGRLGVEKSLDFL----KRIMDRLPEARIAIVG--DGPYREELEK 276
Cdd:cd03821 179 IPNGVDI----PEFDPGLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLiraaRKLAEQGRDWHLVIAGpdDGAYPAFLQL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 277 M--FTGMPAV-FTGMLSGEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIPPEqDGKIGHLytp 353
Cdd:cd03821 255 QssLGLGDRVtFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG-CGVVVDP--- 330
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1279756475 354 gDIDDCLNKLKPLLDNRELRET---MGKAARKEMEKYDWKA 391
Cdd:cd03821 331 -NVSSLAEALAEALRDPADRKRlgeMARRARQVEENFSWEA 370
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
297-394 |
2.27e-26 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 102.76 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 297 AYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIppeQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETM 376
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVI---EDGETGLLVPPGDPEALAEAILRLLEDPELRRRL 93
|
90
....*....|....*....
gi 1279756475 377 GKAARKEME-KYDWKAATR 394
Cdd:COG0438 94 GEAARERAEeRFSWEAIAE 112
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
51-208 |
6.74e-26 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 103.00 E-value: 6.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 51 NFIRYLREMGDEVMVVTTHEGVPEEFYGAKLIGSRSFPCPLYHKVPLSLALSPRIISEVVRFKPDIIHASSPGIMVFGAL 130
Cdd:pfam13439 9 ELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSPFPLGLAAL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279756475 131 IIAKLSSVPLVLSYHTHVPVYIPRYTFSWLVKPM-WLVIKFLHRAADLTLVPSAAIGMDLEAERVTAANKIRLWNKGVD 208
Cdd:pfam13439 89 AARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLlRRLERRLLRRADRVIAVSEAVADELRRLYGVPPEKIRVIPNGVD 167
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
90-386 |
1.21e-24 |
|
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: 104.36 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 90 PLYHKVPLSLALSPRIISEVVRFKPDIIHA------SSPGIMVfGALIIAKLssvPLVLSYH-THVpvyipryTFSWLVK 162
Cdd:cd04962 61 PLFEYPPYTLALASKIVEVAKEHKLDVLHAhyaiphASCAYLA-REILGEKI---PIVTTLHgTDI-------TLVGYDP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 163 PMWLVIKF-LHRAADLTLVPSAaigmdLEAERVT---AANKIRLWNKGVDSAsfhpRFRSQEMR--LRLSGDEPDKPLII 236
Cdd:cd04962 130 SLQPAVRFsINKSDRVTAVSSS-----LRQETYElfdVDKDIEVIHNFIDED----VFKRKPAGalKRRLLAPPDEKVVI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 237 HVGRLGVEKSLDFLKRIMDRLPE---ARIAIVGDGPYREELE----KMFTGMPAVFTGmlSGEELSQAYASSDIFVMPSE 309
Cdd:cd04962 201 HVSNFRPVKRIDDVVRVFARVRRkipAKLLLVGDGPERVPAEelarELGVEDRVLFLG--KQDDVEELLSIADLFLLPSE 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279756475 310 SETLGLVVLEAMSSGIPVIGARAGGVPDIIppeQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARKEMEK 386
Cdd:cd04962 279 KESFGLAALEAMACGVPVVSSNAGGIPEVV---KHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAE 352
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
56-392 |
6.73e-23 |
|
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: 98.94 E-value: 6.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 56 LREMGDEVMVVTTHEGVPEEFYGAKLIGSRSFPCPLYHKVPLSLALS-------PRIISEVVR----FKPDIIHASSpgI 124
Cdd:cd03823 28 LVAEGHEVAVLTAGVGPPGQATVARSVVRYRRAPDETLPLALKRRGYelfetynPGLRRLLARlledFRPDVVHTHN--L 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 125 MVFGALII--AKLSSVPLVLSYHTHvpvyiprytfsWLVKPmwlVIKFLHRAADLTLVPSAAIGMDLEAERVTAANKIRL 202
Cdd:cd03823 106 SGLGASLLdaARDLGIPVVHTLHDY-----------WLLCP---RQFLFKKGGDAVLAPSRFTANLHEANGLFSARISVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 203 WNkGVDSasfhprfrsqEMRLRLSGDEPDKPL-IIHVGRLGVEKSLDFLKRIMDRLP--EARIAIVGDGPyrEELEKMFT 279
Cdd:cd03823 172 PN-AVEP----------DLAPPPRRRPGTERLrFGYIGRLTEEKGIDLLVEAFKRLPreDIELVIAGHGP--LSDERQIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 280 GMPAV-FTGMLSGEELSQAYASSDIFVMPSE-SETLGLVVLEAMSSGIPVIGARAGGVPDIIppeQDGKIGHLYTPGDID 357
Cdd:cd03823 239 GGRRIaFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAELI---QPGVNGLLFAPGDAE 315
|
330 340 350
....*....|....*....|....*....|....*
gi 1279756475 358 DCLNKLKPLLDNRELRETMGKAARkEMEKYDWKAA 392
Cdd:cd03823 316 DLAAAMRRLLTDPALLERLRAGAE-PPRSTESQAE 349
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
198-387 |
4.10e-22 |
|
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: 97.02 E-value: 4.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 198 NKIRLWNKGVDSASFHPRFRsQEMRLRLsGDEPDKPLIIhVGRLGVE---KSLDFLKRIMDRLP-EARIAIVGDGPYREE 273
Cdd:cd03825 161 LPVVVIPNGIDTEIFAPVDK-AKARKRL-GIPQDKKVIL-FGAESVTkprKGFDELIEALKLLAtKDDLLLVVFGKNDPQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 274 LEKMftGMPAVFTGMLS-GEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIppeQDGKIGHLYT 352
Cdd:cd03825 238 IVIL--PFDIISLGYIDdDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIV---QHGVTGYLVP 312
|
170 180 190
....*....|....*....|....*....|....*
gi 1279756475 353 PGDIDDCLNKLKPLLDNRELRETMGKAARKEMEKY 387
Cdd:cd03825 313 PGDVQALAEAIEWLLANPKERESLGERARALAENH 347
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
113-387 |
1.39e-20 |
|
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: 93.55 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 113 KPDIIHASSPGIMVFGALIIAKLSSVPLVLSYH--------------THVPVYIprytfswlvKPMWlvIKFLHRAADLT 178
Cdd:cd03813 173 EADLYHSVSTGYAGLLGALARHRRGIPFLLTEHgiytrerkieilqsTWIMGYI---------KKLW--IRFFERLGKLA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 179 LVPSAAI-----GMDLEAERVTA-ANKIRLWNKGVDSASFHPrfrsqemrLRLSGDEPDKPLIIHVGRLGVEKSLDFLKR 252
Cdd:cd03813 242 YQQADKIislyeGNRRRQIRLGAdPDKTRVIPNGIDIQRFAP--------AREERPEKEPPVVGLVGRVVPIKDVKTFIR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 253 IMD----RLPEARIAIVG----DGPYREELEKMFTGM----PAVFTGMLSGEElsqAYASSDIFVMPSESETLGLVVLEA 320
Cdd:cd03813 314 AFKlvrrAMPDAEGWLIGpedeDPEYAQECKRLVASLglenKVKFLGFQNIKE---YYPKLGLLVLTSISEGQPLVILEA 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279756475 321 MSSGIPVIGARAGGVPDII--PPEQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARKEMEKY 387
Cdd:cd03813 391 MASGVPVVATDVGSCRELIygADDALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKY 459
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
30-345 |
1.33e-19 |
|
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: 87.46 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 30 IALFIEPSPFAYvSGYKNRFQNFIRYLREMGDEVMVVTthegvpeefygakligsrsfpcplyhkvpLSLALSPRIISEV 109
Cdd:cd01635 1 ILLVTGEYPPLR-GGLELHVRALARALAALGHEVTVLA-----------------------------LLLLALRRILKKL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 110 VRFKPDIIHASSPGIMVFGALIIAKLSSVPLVLSYHTHVPVYIPRYTFSWLVKPMWLVIKFLHraadltlvpsaaigmdl 189
Cdd:cd01635 51 LELKPDVVHAHSPHAAALAALLAARLLGIPIVVTVHGPDSLESTRSELLALARLLVSLPLADK----------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 190 eaervtaankirlwnkgvdsasfhprfrsqemrlrlsgdepdkpliIHVGRLGVEKSLDFLKRIMDRLPEARIA----IV 265
Cdd:cd01635 114 ----------------------------------------------VSVGRLVPEKGIDLLLEALALLKARLPDlvlvLV 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 266 GDGPYREELEKMFT----GMPAVFTGMLSGEELSQAY-ASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIP 340
Cdd:cd01635 148 GGGGEREEEEALAAalglLERVVIIGGLVDDEVLELLlAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVV 227
|
....*
gi 1279756475 341 PEQDG 345
Cdd:cd01635 228 DGENG 232
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
94-344 |
1.05e-18 |
|
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.
Pssm-ID: 340857 [Multi-domain] Cd Length: 360 Bit Score: 87.12 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 94 KVPLSLALSP-RIISEVVRFKPDIIHASspgimVFGALIIAKLS-----SVPLVLSYHT-----HVPVYIPRYTfswlvk 162
Cdd:cd04951 59 KNPRSLLKALlKLKKIISAFKPDVVHSH-----MFHANIFARFLrmlypIPLLICTAHNkneggRIRMFIYRLT------ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 163 pmwlviKFLhraADLTLVPSAAIGMDLEAERVTAANKIRLWNKGVDSASFHprfRSQEMRLRLS---GDEPDKPLIIHVG 239
Cdd:cd04951 128 ------DFL---CDITTNVSREALDEFIAKKAFSKNKSVPVYNGIDLNKFK---KDINVRLKIRnklNLKNDEFVILNVG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 240 RLGVEKS----LDFLKRIMDRLPEARIAIVGDGPYREELEKMFTGMPAVFTGMLSG--EELSQAYASSDIFVMPSESETL 313
Cdd:cd04951 196 RLTEAKDypnlLLAISELILSKNDFKLLIAGDGPLRNELERLICNLNLVDRVILLGqiSNISEYYNAADLFVLSSEWEGF 275
|
250 260 270
....*....|....*....|....*....|.
gi 1279756475 314 GLVVLEAMSSGIPVIGARAGGVPDIIPPEQD 344
Cdd:cd04951 276 GLVVAEAMACERPVVATDAGGVAEVVGDHNY 306
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
197-388 |
8.86e-18 |
|
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.
Pssm-ID: 340829 [Multi-domain] Cd Length: 350 Bit Score: 84.04 E-value: 8.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 197 ANKIRLWNKGVDSASFhprfrsqemRLRLSGDEPDKPL-IIHVGRL----GVEKSLDFLKRIMDRLPEARIAIVGDGPYR 271
Cdd:cd03799 147 EKKIIVHRSGIDCNKF---------RFKPRYLPLDGKIrILTVGRLtekkGLEYAIEAVAKLAQKYPNIEYQIIGDGDLK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 272 EELEKMFTGMPAVFTGMLSG----EELSQAYASSDIFVMPS------ESETLGLVVLEAMSSGIPVIGARAGGVPDIIpp 341
Cdd:cd03799 218 EQLQQLIQELNIGDCVKLLGwkpqEEIIEILDEADIFIAPSvtaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELV-- 295
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1279756475 342 eQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARKEME-KYD 388
Cdd:cd03799 296 -EDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEeEYD 342
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
173-395 |
2.38e-17 |
|
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: 83.21 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 173 RAADLTLVPSAAIGMDLEAERVTAANKIrlwNKGVDSASFHPRFRSQEMRLRLSGDEPDKPLIIHVGrlGVEK---SLDF 249
Cdd:TIGR04047 137 VEADAVLCVSAAWAAELRAEWGIDATVV---PNGVDAARFSPAADAADAALRRRLGLRGGPYVLAVG--GIEPrknTIDL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 250 LK---RIMDRLPEARIAIVGD------GPYREELEKMFTGM-----PAVFTGMLSGEELSQAYASSDIFVMPSESETLGL 315
Cdd:TIGR04047 212 LEafaLLRARRPQAQLVIAGGatlfdyDAYRREFRARAAELgvdpgPVVITGPVPDADLPALYRCADAFAFPSLKEGFGL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 316 VVLEAMSSGIPVIgaraggVPDIIP--PEQDGKIGHLYTPGDIDDCLNKLKPLLDnRELRETMGKAARKEMEKYDWKAAT 393
Cdd:TIGR04047 292 VVLEALASGIPVV------ASDIAPftEYLGRFDAAWADPSDPDSIADALALALD-PARRPALRAAGPELAARYTWDASA 364
|
..
gi 1279756475 394 RI 395
Cdd:TIGR04047 365 RA 366
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
229-387 |
2.55e-17 |
|
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: 82.35 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 229 EPDKPLIIHVGRLGVEKSLDFLKRIM----DRLPEARIAIVGDGPYREELEKMFTGMPA----VFTGMLSGeeLSQAYAS 300
Cdd:cd04949 157 ERKSNKIITISRLAPEKQLDHLIEAVakavKKVPEITLDIYGYGEEREKLKKLIEELHLednvFLKGYHSN--LDQEYQD 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 301 SDIFVMPSESETLGLVVLEAMSSGIPVIGARAG-GVPDIIppeQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKA 379
Cdd:cd04949 235 AYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELI---EDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEE 311
|
....*...
gi 1279756475 380 ARKEMEKY 387
Cdd:cd04949 312 SYKIAEKY 319
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
219-394 |
2.83e-17 |
|
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: 83.77 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 219 QEmRLRLSGDePDKPLIIHVGRLGVEKSLDFLKRIMDRLPE--ARIAIVGDGPYREE-----LEKMFTGMPAVFTGMLsg 291
Cdd:cd03791 283 QK-ELGLPVD-PDAPLFGFVGRLTEQKGVDLILDALPELLEegGQLVVLGSGDPEYEqafreLAERYPGKVAVVIGFD-- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 292 EELSQ-AYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGG----VPDIIPPEQDG---KIGHlYTPGDIDDCLNKL 363
Cdd:cd03791 359 EALAHrIYAGADFFLMPSRFEPCGLVQMYAMRYGTLPIVRRTGGladtVFDYDPETGEGtgfVFED-YDAEALLAALRRA 437
|
170 180 190
....*....|....*....|....*....|..
gi 1279756475 364 KPLLDNRELRETMGKAArkeMEK-YDWKAATR 394
Cdd:cd03791 438 LALYRNPELWRKLQKNA---MKQdFSWDKSAK 466
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
113-344 |
9.12e-17 |
|
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: 81.18 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 113 KPDIIHA---SSPGIMvfgaLIIAKLSSVPlVLSYHTHvpvyIPRYTFSWLVKPMWLVIKFL-HRAADLTLVPSAAIGMD 188
Cdd:cd03812 80 KYDIVHVhgsSSNGII----LLLAAKAGVP-VRIAHSH----NTKDSSIKLRKIRKNVLKKLiERLSTKYLACSEDAGEW 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 189 L--EAERvtaaNKIRLWNKGVDSASFHPrfrSQEMR--LRLSGDEPDKPLIIHVGRLGVEKSLDFLKRIMDRLPE----A 260
Cdd:cd03812 151 LfgEVEN----GKFKVIPNGIDIEKYKF---NKEKRrkRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKknpnV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 261 RIAIVGDGPYREELEKMFTGMP----AVFTGMLSgeELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIgaraggVP 336
Cdd:cd03812 224 KLVLVGEGELKEKIKEKVKELGledkVIFLGFRN--DVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCL------LS 295
|
....*...
gi 1279756475 337 DIIPPEQD 344
Cdd:cd03812 296 DTITKECD 303
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
43-198 |
2.76e-14 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 70.12 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 43 SGYKNRFQNFIRYLREMGDEVMVVTTHEGVPEEFYGAKLIGSRSFPCPLYHKVPLSLALSPRIISEVVRFKPDIIHASSP 122
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPVPPRPSPLADLAALRRLRRLLRAERPDVVHAHSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279756475 123 GIMvFGALIIAKLSSVPLVLSYHTHVpvyiPRYTFSWLVKPMWLVIKFLHRAADLTLVPSAAIGMDLEAERVTAAN 198
Cdd:pfam13579 81 TAG-LAARLARRRRGVPLVVTVHGLA----LDYGSGWKRRLARALERRLLRRADAVVVVSEAEAELLRALGVPAAR 151
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
219-394 |
1.08e-13 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 72.43 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 219 QEMRLRLsgdEPDKPLIIHVGRLGVEKSLDFLKRIMDRLPE--ARIAIVGDGPyrEELEKMFTGMPAVFTGMLS---G-- 291
Cdd:COG0297 285 EELGLPV---DPDAPLIGMVSRLTEQKGLDLLLEALDELLEedVQLVVLGSGD--PEYEEAFRELAARYPGRVAvyiGyd 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 292 EELS-QAYASSDIFVMPSESETLGLVVLEAMSSG-IPVigARA-GG----VPDIIPPEQDGkIGHLYTPGDIDDCLNKLK 364
Cdd:COG0297 360 EALAhRIYAGADFFLMPSRFEPCGLNQMYALRYGtVPI--VRRtGGladtVIDYNEATGEG-TGFVFDEYTAEALLAAIR 436
|
170 180 190
....*....|....*....|....*....|....
gi 1279756475 365 PLLD---NRELRETMGKAArkeMEK-YDWKAATR 394
Cdd:COG0297 437 RALAlyrDPEAWRKLQRNA---MKQdFSWEKSAK 467
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
235-386 |
2.68e-13 |
|
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: 70.95 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 235 IIHVGRlgVEKSLDFLKRIMDRLPEARIAI--VGDGPYREELEKMFTGMP----AVFTGMLSGEELSQAYA--SSDIFVM 306
Cdd:cd04946 233 IVPVKR--IDLIIETLNSLCVAHPSICISWthIGGGPLKERLEKLAENKLenvkVNFTGEVSNKEVKQLYKenDVDVFVN 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 307 PSESETLGLVVLEAMSSGIPVIGARAGGVPDIIppeQDGKIGHL----YTPGDIDDCLNKlkpLLDNRELRETMGKAARK 382
Cdd:cd04946 311 VSESEGIPVSIMEAISFGIPVIATNVGGTREIV---ENETNGLLldkdPTPNEIVSSIMK---FYLDGGDYKTMKISARE 384
|
....
gi 1279756475 383 EMEK 386
Cdd:cd04946 385 CWEE 388
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
56-350 |
1.06e-12 |
|
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: 68.85 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 56 LREMGDEVMVVTTHEGVP----EEFYGAKLI-GSRSFPCPLYHKVPLSLALSPRiisevvrFKPDIIHASSPgimvFGAL 130
Cdd:cd03802 31 LVRRGHEVTLFAPGDSHTsaplVAVIPRALRlDPIPQESKLAELLEALEVQLRA-------SDFDVIHNHSY----DWLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 131 IIAKLSSVPLVLSYHTHVPVYIPRYtFSWLVKPMWLVIKFLHRAADLTLVPSAAIGmdleaervtaankirlwnKGVDSA 210
Cdd:cd03802 100 PFAPLIGTPFVTTLHGPSIPPSLAI-YAAEPPVNYVSISDAQRAATPPIDYLTVVH------------------NGLDPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 211 SFHPRFRsqemrlrlsgdepDKPLIIHVGRL----GVEKSLDFLKRImdRLPEARIAIVGDGPYREELEKMFTGMPAVFT 286
Cdd:cd03802 161 DYRFQPD-------------PEDYLAFLGRIapekGLEDAIRVARRA--GLPLKIAGKVRDEDYFYYLQEPLPGPRIEFI 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279756475 287 GMLSGEE----LSQAYAssdIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIppeQDGKIGHL 350
Cdd:cd03802 226 GEVGHDEkqelLGGARA---LLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVI---QHGETGFL 287
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
198-388 |
9.32e-12 |
|
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).
Pssm-ID: 340845 [Multi-domain] Cd Length: 396 Bit Score: 66.23 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 198 NKIRLWNKGVDSASFHPRFRSQEMRLRLSGDEPDKPLIIHVGRlGVEKSLDF------LKRIMDRLPEARIAIVGD---- 267
Cdd:cd03818 179 DRISVIHDGVDTDRLAPDPAARLRLLNGTELKAGDPVITYVAR-NLEPYRGFhvfmraLPRIQARRPDARVVVVGGdgvs 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 268 --------GPYREELEKMFTGMPA--VFTGMLSGEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPD 337
Cdd:cd03818 258 ygspppdgGSWKQKMLAELGVDLErvHFVGKVPYDQYVRLLQLSDAHVYLTYPFVLSWSLLEAMACGCPVIGSDTAPVRE 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1279756475 338 IIppeQDGKIGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARKEMEKYD 388
Cdd:cd03818 338 VI---RDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSD 385
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
224-408 |
4.21e-11 |
|
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: 64.26 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 224 RLSGDEPDKPLIIHVGRL----GVEKSLDFLKRIMDRLPEARIAIVG----DGP-----YREELEkMFTGMPAVFTGMLS 290
Cdd:cd03792 189 KPFVIDPERPYILQVARFdpskDPLGVIDAYKLFKRRAEEPQLVICGhgavDDPegsvvYEEVME-YAGDDHDIHVLRLP 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 291 G--EELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIppeQDGKIGHLYTPGDIDDClnKLKPLLD 368
Cdd:cd03792 268 PsdQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQV---IDGETGFLVNSVEGAAV--RILRLLT 342
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1279756475 369 NRELRETMGKAARKEM-EKYDwkaATRIIRNehYNLAIWFW 408
Cdd:cd03792 343 DPELRRKMGLAAREHVrDNFL---ITGNLRA--WLYLIAKL 378
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
179-393 |
1.03e-10 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 62.89 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 179 LVPSAAIgMDLEAERVTAANkIRLWNKGVDSASFHPRFrSQEMRLRLSGDePDKPLIIHVGRLGVEKSLDFLKRIMDRLP 258
Cdd:PRK15484 144 IVPSQFL-KKFYEERLPNAD-ISIVPNGFCLETYQSNP-QPNLRQQLNIS-PDETVLLYAGRISPDKGILLLMQAFEKLA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 259 EAR----IAIVGD---------GPYREELEKMFT--GMPAVFTGMLSGEELSQAYASSDIFVMPSE-SETLGLVVLEAMS 322
Cdd:PRK15484 220 TAHsnlkLVVVGDptasskgekAAYQKKVLEAAKriGDRCIMLGGQPPEKMHNYYPLADLVVVPSQvEEAFCMVAVEAMA 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279756475 323 SGIPVIGARAGGVPDIIppeQDGKIG-HLYTPGDIDDCLNKLKPLLDNRELRETMGKAARKEMEKYDWKAAT 393
Cdd:PRK15484 300 AGKPVLASTKGGITEFV---LEGITGyHLAEPMTSDSIISDINRTLADPELTQIAEQAKDFVFSKYSWEGVT 368
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
207-342 |
2.71e-10 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 61.87 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 207 VDSASFHPRFRSQEmrlrlsgdePDKPLIIHVGRLGVEKSLDFLKRIMDRL----PEARIAIVGDGPYREELEKM---FT 279
Cdd:cd03796 177 VDSSDFTPDPSKPD---------PNKITIVVISRLVYRKGIDLLVGIIPRIckkhPNVRFIIGGDGPKRIELEEMrekYQ 247
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279756475 280 GMPAV-FTGMLSGEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIPPE 342
Cdd:cd03796 248 LQDRVeLLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPD 311
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
292-363 |
7.04e-10 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 60.11 E-value: 7.04e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279756475 292 EELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARA-GGVPDIIppeQDGKIGHLYTPGDIDDCLNKL 363
Cdd:PRK09922 249 EVVQQKIKNVSALLLTSKFEGFPMTLLEAMSYGIPCISSDCmSGPRDII---KPGLNGELYTPGNIDEFVGKL 318
|
|
| COG4641 |
COG4641 |
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]; |
44-382 |
2.43e-09 |
|
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443679 [Multi-domain] Cd Length: 303 Bit Score: 58.02 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 44 GYKNRFQNFIRYLREMGDEVMVVTTHEGVPEEFYGAKLIgsrsfpcplyhkvplslalspriisevVRFKPDIIHASSPG 123
Cdd:COG4641 7 GHATYYRGLLRALAALGHEVTFLEPDDPWHDPLYAAELL---------------------------DAFRPDLVLVISGV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 124 imvfGALIIAKLSSVPLVlSYHTHVPVYIPRYtfswlvkpmwlviKFLHRAADLTLVPSAAIGMDLEAErvtAANKIRLW 203
Cdd:COG4641 60 ----ELVAALRARGIPTV-FWDTDDPVTLDRF-------------RELLPLYDLVFTFDGDCVEEYRAL---GARRVFYL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 204 NKGVDSASFHPRFRsqemRLRLSGDepdkplIIHVGRLGVEKSlDFLKRIMDRLPEARIAIVGDGpYREELekmftgMPA 283
Cdd:COG4641 119 PFAADPELHRPVPP----EARFRYD------VAFVGNYYPDRR-ARLEELLLAPAGLRLKIYGPG-WPKLA------LPA 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 284 VFT--GMLSGEELSQAYASSDIFV----MPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIPPEQDgkighLYTPGDID 357
Cdd:COG4641 181 NVRrgGHLPGEEHPAAYASSKITLnvnrMAASPDSPTRRTFEAAACGAFLLSDPWEGLEELFEPGEE-----VLVFRDGE 255
|
330 340
....*....|....*....|....*
gi 1279756475 358 DCLNKLKPLLDNRELRETMGKAARK 382
Cdd:COG4641 256 ELAEKLRYLLADPEERRAIAEAGRR 280
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
238-351 |
3.20e-09 |
|
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: 58.07 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 238 VGRLGVEKSLDFLKRIMDRLPEaRIAIVGDGPYREELEKMfTGMPAVFTGMLSGEELSQAYASSDIFVMPSEsETLGLVV 317
Cdd:cd03804 205 ASRLVPYKRIDLAVEAFNELPK-RLVVIGDGPDLDRLRAM-ASPNVEFLGYQPDEVLKELLSKARAFVFAAE-EDFGIVP 281
|
90 100 110
....*....|....*....|....*....|....
gi 1279756475 318 LEAMSSGIPVIGARAGGVPDIIppeQDGKIGHLY 351
Cdd:cd03804 282 VEAQACGTPVIAFGKGGALETV---RPGPTGILF 312
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
219-360 |
4.46e-08 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 55.12 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 219 QEMRLrlsgDEPDKPLIIHVGRLGVEKSLDFLKRIMDRLPE--ARIAIVGDGPYreELEKMFTGMPAVFTGMLS---G-- 291
Cdd:PRK00654 273 ERFGL----PDDDAPLFAMVSRLTEQKGLDLVLEALPELLEqgGQLVLLGTGDP--ELEEAFRALAARYPGKVGvqiGyd 346
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279756475 292 EELS-QAYASSDIFVMPSESETLGLVVLEAMSSG-IPvIGARAGGVPD-IIPPEQDGKIG-----HLYTPGDIDDCL 360
Cdd:PRK00654 347 EALAhRIYAGADMFLMPSRFEPCGLTQLYALRYGtLP-IVRRTGGLADtVIDYNPEDGEAtgfvfDDFNAEDLLRAL 422
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
101-357 |
1.95e-07 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 53.50 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 101 LSPRIISEVVRFKP-------DIIHASSPGIMVFGALIiAKLSSVP-LVLSYHTHVPVYIP-RY------TFSWL--VKP 163
Cdd:PRK15179 381 LPKQIIEGTTKLTDvmrssvpSVVHIWQDGSIFACALA-ALLAGVPrIVLSVRTMPPVDRPdRYrveydiIYSELlkMRG 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 164 MWLV---IKFLHRAADLTLVPSAAIGM------DLEAERVTAANKIRLwnkGVDSASFHPRFR-SQEMRLrlsgdEPDK- 232
Cdd:PRK15179 460 VALSsnsQFAAHRYADWLGVDERRIPVvynglaPLKSVQDDACTAMMA---QFDARTSDARFTvGTVMRV-----DDNKr 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 233 PliihvgRLGVEKSLDFLKRimdrLPEARIAIVGDGPYREEL----EKMFTGMPAVFTGMlsGEELSQAYASSDIFVMPS 308
Cdd:PRK15179 532 P------FLWVEAAQRFAAS----HPKVRFIMVGGGPLLESVrefaQRLGMGERILFTGL--SRRVGYWLTQFNAFLLLS 599
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1279756475 309 ESETLGLVVLEAMSSGIPVIGARAGGVPDIIppeQDGKIGHLYTPGDID 357
Cdd:PRK15179 600 RFEGLPNVLIEAQFSGVPVVTTLAGGAGEAV---QEGVTGLTLPADTVT 645
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
310-382 |
3.35e-07 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 47.98 E-value: 3.35e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279756475 310 SETLGLVVLEAMSSGIPVIGARAGGVPDIIPPEQdgkigHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARK 382
Cdd:pfam13524 9 PDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGE-----EILLYRDPEELAEKIRYLLEHPEERRAIAAAGRE 76
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
89-382 |
3.46e-07 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 51.90 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 89 CPLYhkVP------------LSLALSPR-IISEVVRFKPDIIHASSPGIMVF-GALIIAKLSSVPLVLsyhtHVPVYIPR 154
Cdd:PRK10307 71 CPLY--VPkqpsglkrllhlGSFALSSFfPLLAQRRWRPDRVIGVVPTLFCApGARLLARLSGARTWL----HIQDYEVD 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 155 YTFSW-LVKPMWL------VIKFLHRAADLTLVPSAAIGMDLEAERVTAANKIRLWNkGVDSASFHPRFRSQEMRLRLS- 226
Cdd:PRK10307 145 AAFGLgLLKGGKVarlataFERSLLRRFDNVSTISRSMMNKAREKGVAAEKVIFFPN-WSEVARFQPVADADVDALRAQl 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 227 GDEPDKPLIIHVGRL----GVEKSLDFLKRIMDRlPEARIAIVGDGPYREELEKM--FTGMPAV-FTGMLSGEELSQAYA 299
Cdd:PRK10307 224 GLPDGKKIVLYSGNIgekqGLELVIDAARRLRDR-PDLIFVICGQGGGKARLEKMaqCRGLPNVhFLPLQPYDRLPALLK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 300 SSDIFVMPSESETLGLVV---LEAM-SSGIPVIG-ARAG-GVPDIIPPeqdgkIGHLYTPGDIDDCLNKLKPLLDNRELR 373
Cdd:PRK10307 303 MADCHLLPQKAGAADLVLpskLTNMlASGRNVVAtAEPGtELGQLVEG-----IGVCVEPESVEALVAAIAALARQALLR 377
|
....*....
gi 1279756475 374 ETMGKAARK 382
Cdd:PRK10307 378 PKLGTVARE 386
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
215-388 |
1.07e-06 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 50.89 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 215 RFRSQEMRLRLSGDEPDKPLIIHVGRLgveKSLDFLKRIMDRLPEARIAIVGDGPYREELEKMFTGMPAVFTGMLSGEE- 293
Cdd:PRK14098 293 KALLEEVGLPFDEETPLVGVIINFDDF---QGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTe 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 294 -----LSQAYASSDIFVMPSESETLGLVVLEAMSSG-IPVIGArAGGVPDIIpPEQDGKIG-----HLYTPGDIDDCLNK 362
Cdd:PRK14098 370 ftdafFHLAIAGLDMLLMPGKIESCGMLQMFAMSYGtIPVAYA-GGGIVETI-EEVSEDKGsgfifHDYTPEALVAKLGE 447
|
170 180 190
....*....|....*....|....*....|...
gi 1279756475 363 LKPLLDNRE-----LRETMGK--AARKEMEKYD 388
Cdd:PRK14098 448 ALALYHDEErweelVLEAMERdfSWKNSAEEYA 480
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
247-334 |
8.42e-05 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 44.69 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 247 LDFLKRIMDRLPEARIAIVGDGPYREELEKMFTGMPAVFTGMLSGEELSQAY--ASSDIFVMPSESETLGLVVLEAMSSG 324
Cdd:PRK15490 417 IDFAARYLQHHPATRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYwlQKMNVFILFSRYEGLPNVLIEAQMVG 496
|
90
....*....|
gi 1279756475 325 IPVIGARAGG 334
Cdd:PRK15490 497 VPVISTPAGG 506
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
229-339 |
2.77e-04 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 43.17 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 229 EPDKPLIIHVGRLGVEKSLDFLkriMDRLPE-----ARIAIVGDGpyREELEKMFTGMPAVFTGMLSG-----EELS-QA 297
Cdd:PRK14099 292 DPDALLLGVISRLSWQKGLDLL---LEALPTllgegAQLALLGSG--DAELEARFRAAAQAYPGQIGVvigydEALAhLI 366
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1279756475 298 YASSDIFVMPSESETLGLVVLEAMSSG-IPVIgARAGGVPDII 339
Cdd:PRK14099 367 QAGADALLVPSRFEPCGLTQLCALRYGaVPVV-ARVGGLADTV 408
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
114-394 |
1.23e-03 |
|
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.
Pssm-ID: 340849 [Multi-domain] Cd Length: 370 Bit Score: 40.83 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 114 PDIIHASSPGIMVF---GALIIAKLSSVPLVLSYHTHVPVYIPRYTFSWLVKPMWL---VIKFLHRAADLTLVPSAAIGM 187
Cdd:cd03822 68 LDHLNFKKPDVVHIqheFGIFGGKYGLYALGLLLHLRIPVITTLHTVLDLSDPGKQalkVLFRIATLSERVVVMAPISRF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 188 DLEAERVTAANKIRLWNKGVdsasFHPRFRSQEMRLRLSGDEpDKPLIIHVGRL----GVEKSLDFLKRIMDRLPEARIA 263
Cdd:cd03822 148 LLVRIKLIPAVNIEVIPHGV----PEVPQDPTTALKRLLLPE-GKKVILTFGFIgpgkGLEILLEALPELKAEFPDVRLV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 264 IVG---DGPYREELEKMFTGMPA---------VFTGMLSGEELSQAYASSDIFVMP--SESETLGLVVLEAMSSGIPVIG 329
Cdd:cd03822 223 IAGelhPSLARYEGERYRKAAIEelglqdhvdFHNNFLPEEEVPRYISAADVVVLPylNTEQSSSGTLSYAIACGKPVIS 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279756475 330 ARAGGVPDIIPPEQdgkiGHLYTPGDIDDCLNKLKPLLDNRELRETMGKAARKEMEKYDWKAATR 394
Cdd:cd03822 303 TPLRHAEELLADGR----GVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIAD 363
|
|
| PHA01630 |
PHA01630 |
putative group 1 glycosyl transferase |
289-369 |
1.36e-03 |
|
putative group 1 glycosyl transferase
Pssm-ID: 164861 Cd Length: 331 Bit Score: 40.54 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 289 LSGEELSQAYASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPDIIPPEQDG-----------------KIGHLY 351
Cdd:PHA01630 198 LPDDDIYSLFAGCDILFYPVRGGAFEIPVIEALALGLDVVVTEKGAWSEWVLSNLDVywiksgrkpklwytnpiHVGYFL 277
|
90
....*....|....*...
gi 1279756475 352 TPgDIDDCLNKLKPLLDN 369
Cdd:PHA01630 278 DP-DIEDAYQKLLEALAN 294
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
223-342 |
1.53e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.04 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 223 LRLSGDEPDKPLIIHVGRLGVEKSLDFLKRIMDRLPE--ARIAIVGDGPYrEELEKMFTGMPAVFTG-------MLSGEE 293
Cdd:PLN02939 770 LGLSSADASQPLVGCITRLVPQKGVHLIRHAIYKTAElgGQFVLLGSSPV-PHIQREFEGIADQFQSnnnirliLKYDEA 848
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279756475 294 LSQA-YASSDIFVMPSESETLGLVVLEAMSSGIPVIGARAGGVPD--------IIPPE 342
Cdd:PLN02939 849 LSHSiYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDsvfdfddeTIPVE 906
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
244-387 |
2.23e-03 |
|
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.
Pssm-ID: 340835 [Multi-domain] Cd Length: 419 Bit Score: 39.90 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 244 EKSLDFLKRIMDRL-PEARIAIVGDGPYREELEKMFTgmpavftgmlsgeelsqayASSDIFVMpsESETLGLVVLEAMS 322
Cdd:cd03806 288 KERVEALKLLAKELiLEDSVEFVVDAPYEELKELLST-------------------ASIGLHTM--WNEHFGIGVVEYMA 346
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279756475 323 SG-IPVIGARAGGVPDIIPPEQDGKIGHLY-TPGDIDDCLNKLkpLLDNRELRETMGKAARKEMEKY 387
Cdd:cd03806 347 AGlIPLAHASAGPLLDIVVPWDGGPTGFLAsTPEEYAEAIEKI--LTLSEEERLQRREAARSSAERF 411
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
50-145 |
2.79e-03 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 38.07 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 50 QNFIRYLREMGDEVMVVTTHEGVPEEFYGAkliGSRSFPCPLYHKVPLSLALSPRIISEVVRFKPDIIH---ASSPGImv 126
Cdd:pfam13477 14 LRWADALADRGYDVHVISSKGPAKDELIAE---GIHVHRLKVPRKGPLGYLKAFRLKKLIKKIKPDVVHvhyAKPYGL-- 88
|
90
....*....|....*....
gi 1279756475 127 FGALIIAKLSSVPLVLSYH 145
Cdd:pfam13477 89 LAGLAARLSGFPPVVLSAW 107
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
309-387 |
3.72e-03 |
|
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.
Pssm-ID: 340834 [Multi-domain] Cd Length: 392 Bit Score: 39.49 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279756475 309 ESETLGLVVLEAMSSGIPVIGARAGGvpdiiPPE--QDGKIGHLYTPgDIDDCLNKLKPLLDNRELRETMGKAARKEMEK 386
Cdd:cd03805 308 SNEHFGIVPLEAMYAGKPVIACNSGG-----PLEtvVEGVTGFLCEP-TPEAFAEAMLKLANDPDLADRMGAAGRKRVKE 381
|
.
gi 1279756475 387 Y 387
Cdd:cd03805 382 K 382
|
|
| |
