|
Name |
Accession |
Description |
Interval |
E-value |
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
7-375 |
1.62e-145 |
|
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: 417.85 E-value: 1.62e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 7 IALISETYPPEVNGVANTLGRLHAGLQQLGHRVQVVRPRQPgDDGRRSDAELVLTRGWPLPGYPGLQWGMSSLHKLLRCW 86
Cdd:cd03814 2 IALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVAPGPF-DEAESAEGRVVSVPSFPLPFYPEYRLALPLPRRVRRLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 87 KRQRPDVLYIATEGPLGFSALRAARRLGIPAVSGFHTNFQQYSEHYGFGPLTRLVTGYLRWFHNRTQMTLVPSGSQRMEL 166
Cdd:cd03814 81 KEFQPDIIHIATPGPLGLAALRAARRLGLPVVTSYHTDFPEYLSYYTLGPLSWLAWAYLRWFHNPFDTTLVPSPSIAREL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 167 QRRGFERLNLLSRGVDSQLFHPSRRDPELRRRWGLGEqDIAVLHVGRLAAEKNLGLLGGTFRALCAAHPqlkLRLVLVGD 246
Cdd:cd03814 161 EGHGFERVRLWPRGVDTELFHPSRRDAALRRRLGPPG-RPLLLYVGRLAPEKNLEALLDADLPLAASPP---VRLVVVGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 247 GPERKHLERDLPEALFCGVQRGETLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNGVLAA 326
Cdd:cd03814 237 GPARAELEARGPDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVE 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15596039 327 PGDKSGFVEVASWLLDDQERLRRVRLNARQHASRQGWDSIVEHFQNYLE 375
Cdd:cd03814 317 PGDAAAFAAALRALLEDPELRRRMAARARAEAERYSWEAFLDNLLDYYA 365
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
7-360 |
4.04e-69 |
|
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: 222.54 E-value: 4.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 7 IALISETYPPEVNGVANTLGRLHAGLQQLGHRVQVVRPRQPGDDGRRSDaELVLTRGWPLPGYPGLQWGMSSLHKLLRCW 86
Cdd:cd03817 2 IAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEEV-VRYRSFSIPIRKYHRQHIPFPFKKAVIDRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 87 KRQRPDVLYIATEGPLGFSALRAARRLGIPAVSGFHTNFQQYSeHY---GFGPLTRLVTGYLRWFHNRTQMTLVPSGSQR 163
Cdd:cd03817 81 KELGPDIIHTHTPFSLGKLGLRIARKLKIPIVHTYHTMYEDYL-HYipkGKLLVKAVVRKLVRRFYNHTDAVIAPSEKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 164 MELQRRGFER-LNLLSRGVDSQLFHPSRrDPELRRRWGLGEQDIAVLHVGRLAAEKNLGLLggtFRALCAAHPQLKLRLV 242
Cdd:cd03817 160 DTLREYGVKGpIEVIPNGIDLDKFEKPL-NTEERRKLGLPPDEPILLYVGRLAKEKNIDFL---LRAFAELKKEPNIKLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 243 LVGDGPERKHLER-----DLPE-ALFCGVQRGETLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHI 316
Cdd:cd03817 236 IVGDGPEREELKElarelGLADkVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELV 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15596039 317 RHGHNGVLAAPGDksgfVEVASWL---LDDQERLRRVRLNARQHASR 360
Cdd:cd03817 316 EDGENGFLFEPND----ETLAEKLlhlRENLELLRKLSKNAEISARE 358
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
2-363 |
9.51e-66 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 216.50 E-value: 9.51e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 2 SRPLSIALISETYP-PEVNGVANTLGRLHAGLQQLGHRVQVVRPrQPGDDGRRSDAELVLTRGWPLPGYPGLQWGMSSLH 80
Cdd:PLN02871 56 SRPRRIALFVEPSPfSYVSGYKNRFQNFIRYLREMGDEVLVVTT-DEGVPQEFHGAKVIGSWSFPCPFYQKVPLSLALSP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 81 KLLRCWKRQRPDVLYIATEGPLGFSALRAARRLGIPAVSGFHTNFQQYSEHYGFGPLTRLVTGYLRWFHNRTQMTLVPSG 160
Cdd:PLN02871 135 RIISEVARFKPDLIHASSPGIMVFGALFYAKLLCVPLVMSYHTHVPVYIPRYTFSWLVKPMWDIIRFLHRAADLTLVTSP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 161 SQRMELQRRGF---ERLNLLSRGVDSQLFHPSRRDPELRRRWGLGEQD-IAVLHVGRLAAEKNLGLLggtfRALCAAHPQ 236
Cdd:PLN02871 215 ALGKELEAAGVtaaNRIRVWNKGVDSESFHPRFRSEEMRARLSGGEPEkPLIVYVGRLGAEKNLDFL----KRVMERLPG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 237 LklRLVLVGDGPERKHLER---DLPeALFCGVQRGETLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAfdqAAAG 313
Cdd:PLN02871 291 A--RLAFVGDGPYREELEKmfaGTP-TVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVA---ARAG 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596039 314 --QHI----RHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHASRQGW 363
Cdd:PLN02871 365 giPDIippdQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEKWDW 420
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
7-375 |
1.64e-52 |
|
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: 179.27 E-value: 1.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 7 IALISETYPPEVNGVANTLGRLHAGLQQLGHRVQVVRPRQPGDDGRRSDAELVLTRGWPLPGYPGLQwgmSSLHKLLRCW 86
Cdd:cd03801 2 ILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRAR---RLLRELRPLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 87 KRQRPDVLyIATEGPLGFSALRAARRLGIPAVSGFHtNFQQYSEHYGFGPLTRLVTGYLRWFHNRTQMtLVPSGSQRMEL 166
Cdd:cd03801 79 RLRKFDVV-HAHGLLAALLAALLALLLGAPLVVTLH-GAEPGRLLLLLAAERRLLARAEALLRRADAV-IAVSEALRDEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 167 QRRGFERLNLLSR---GVDSQLFHPsrrdpELRRRWGLGEQDIAVLHVGRLAAEKNLGLLGGTFRALCAAHPQLklRLVL 243
Cdd:cd03801 156 RALGGIPPEKIVVipnGVDLERFSP-----PLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDV--RLVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 244 VG-DGPERKHLERDLPEAL----FCGVQRGETLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRH 318
Cdd:cd03801 229 VGgDGPLRAELEELELGLGdrvrFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVED 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596039 319 GHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHASRQ-GWDSIVEHFQNYLE 375
Cdd:cd03801 309 GEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERfSWERVAERLLDLYR 366
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
7-369 |
6.24e-30 |
|
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.
Pssm-ID: 340828 [Multi-domain] Cd Length: 376 Bit Score: 119.02 E-value: 6.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 7 IALISETYPPEVNGVAN--TLGRLHAgLQQLGHRVQVVRPRQPG----DDGRRSDAELVLTRG--WPLPGYPGL---QWG 75
Cdd:cd03798 1 VLILTNIYPNANSPGRGifVRRQVRA-LSRRGVDVEVLAPAPWGpaaaRLLRKLLGEAVPPRDgrRLLPLKPRLrllAPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 76 M-SSLHKLLRCWKRQRPDVLYIATEGPLGFSALRAARRLGIPAVSGFHTNfqqyseHYGFGPLTRLVTGYLRWFHNRTQM 154
Cdd:cd03798 80 RaPSLAKLLKRRRRGPPDLIHAHFAYPAGFAAALLARLYGVPYVVTEHGS------DINVFPPRSLLRKLLRWALRRAAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 155 TLVPSGSQRMELQRRGFERLN--LLSRGVDSQLFHPSRRDPelrrrwGLGEQDIAVLHVGRLAAEKNLGLLGGTFRALCA 232
Cdd:cd03798 154 VIAVSKALAEELVALGVPRDRvdVIPNGVDPARFQPEDRGL------GLPLDAFVILFVGRLIPRKGIDLLLEAFARLAK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 233 AHPQLKLrlVLVGDGPERKHLERdLPEAL-------FCGVQRGETLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVV 305
Cdd:cd03798 228 ARPDVVL--LIVGDGPLREALRA-LAEDLglgdrvtFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVV 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596039 306 AFDQAAAGQHIRHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHASRQGWDSIVEH 369
Cdd:cd03798 305 ATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALAEPYLRELGEAARARVAERFSWVKAADR 368
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
208-343 |
7.07e-28 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 106.83 E-value: 7.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 208 VLHVGRLAAE-KNLGLLGGTFRALCAAhpQLKLRLVLVGDGPER--KHLERDLPEA-LFCGVQrgETLAAHYASGDLFLF 283
Cdd:pfam13692 4 ILFVGRLHPNvKGVDYLLEAVPLLRKR--DNDVRLVIVGDGPEEelEELAAGLEDRvIFTGFV--EDLAELLAAADVFVL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 284 PSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIrHGHNGVLAAPGDKSGFVEVASWLLDD 343
Cdd:pfam13692 80 PSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
7-360 |
7.11e-28 |
|
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: 112.81 E-value: 7.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 7 IALISETYPP-EVNGVANTLGRLHAGLQQLGHRVQVVRPRqPGDDGRRSDAELVLTRGWPLPG--YPGLQWGMSSL---- 79
Cdd:cd03823 2 ILLVNSLYPPqRVGGAEISVHDLAEALVAEGHEVAVLTAG-VGPPGQATVARSVVRYRRAPDEtlPLALKRRGYELfety 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 80 -----HKLLRCWKRQRPDVLYIATEGPLGFSALRAARRLGIPAVSGFHTNFQQYSEHYGFGPLTRLVTGYLRWFHNRtqm 154
Cdd:cd03823 81 npglrRLLARLLEDFRPDVVHTHNLSGLGASLLDAARDLGIPVVHTLHDYWLLCPRQFLFKKGGDAVLAPSRFTANL--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 155 tlvpsgsqrmeLQRRGFE--RLNLLSRGVDSQLFHPSRRDPELRRrwglgeqdIAVLHVGRLAAEKNLGLLGGTFRALca 232
Cdd:cd03823 158 -----------HEANGLFsaRISVIPNAVEPDLAPPPRRRPGTER--------LRFGYIGRLTEEKGIDLLVEAFKRL-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 233 ahPQLKLRLVLVGDGPERKHLERDLPEAL-FCGVQRGETLAAHYASGDLFLFPSL-SETFGNVVLEAQAAGLAVVAFDQA 310
Cdd:cd03823 217 --PREDIELVIAGHGPLSDERQIEGGRRIaFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLG 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15596039 311 AAGQHIRHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHASR 360
Cdd:cd03823 295 GIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRST 344
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
208-357 |
1.01e-27 |
|
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 107.36 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 208 VLHVGRLAAEKNLGLLGGTFRALCAAHPQLKLrlVLVGDGPERKHLERdlpEALFCGVQRG---------ETLAAHYASG 278
Cdd:pfam00534 5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNLKL--VIAGDGEEEKRLKK---LAEKLGLGDNviflgfvsdEDLPELLKIA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596039 279 DLFLFPSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQH 357
Cdd:pfam00534 80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
59-368 |
4.92e-27 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 110.48 E-value: 4.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 59 VLTRGWPLPGYPGLQWGMSSLH------KLLRCWKRQRPDVLYIATEGPLGFSALrAARRLGIPAV--SGFHTNFQQYSe 130
Cdd:cd03807 42 VLGEELLAAGVPVVCLGLSSGKdpgvllRLAKLIRKRNPDVVHTWMYHADLIGGL-AAKLAGGVKViwSVRSSNIPQRL- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 131 hygfgplTRLVTGYLRWFHNRTQMTLVPSGSQRMELQRRGF--ERLNLLSRGVDSQLFHPS-RRDPELRRRWGLGEQDIA 207
Cdd:cd03807 120 -------TRLVRKLCLLLSKFSPATVANSSAVAEFHQEQGYakNKIVVIYNGIDLFKLSPDdASRARARRRLGLAEDRRV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 208 VLHVGRLAAEKNLGLLGGTFRALCAAHPQLklRLVLVGDGPERKHLERDLPE------ALFCGvQRGETlAAHYASGDLF 281
Cdd:cd03807 193 IGIVGRLHPVKDHSDLLRAAALLVETHPDL--RLLLVGRGPERPNLERLLLElgledrVHLLG-ERSDV-PALLPAMDIF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 282 LFPSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGhNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQH-ASR 360
Cdd:cd03807 269 VLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERiANE 347
|
....*...
gi 15596039 361 QGWDSIVE 368
Cdd:cd03807 348 FSIDAMVR 355
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
271-379 |
1.11e-26 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 103.15 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 271 LAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRV 350
Cdd:COG0438 14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRL 93
|
90 100 110
....*....|....*....|....*....|
gi 15596039 351 RLNARQHASRQ-GWDSIVEHFQNYLEDACA 379
Cdd:COG0438 94 GEAARERAEERfSWEAIAERLLALYEELLA 123
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
7-368 |
7.74e-26 |
|
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: 107.71 E-value: 7.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 7 IALISE-TYPPEVNGVANTLG------RLHAGLQQLGHRVQVV----RPRQPGDDGRRSDAELVLTRGWPLPGYP-GLQW 74
Cdd:cd03800 2 IALISVhGSPLAQPGGADTGGqnvyvlELARALAELGYQVDIFtrriSPADPEVVEIAPGARVIRVPAGPPEYLPkEELW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 75 G--MSSLHKLLRCWKRQ--RPDVLyIATEGPLGFSALRAARRLGIPAVSGFHT----NFQQYSEHYGFGPLTRLvTGYLR 146
Cdd:cd03800 82 PylEEFADGLLRFIAREggRYDLI-HSHYWDSGLVGALLARRLGVPLVHTFHSlgrvKYRHLGAQDTYHPSLRI-TAEEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 147 WFHNRTQmtLVPSGSQRMELQRRGFE----RLNLLSRGVDSQLFHPSRRDPELRRRWGLGEQDIAVLHVGRLAAEKNLGL 222
Cdd:cd03800 160 ILEAADR--VIASTPQEADELISLYGadpsRINVVPPGVDLERFFPVDRAEARRARLLLPPDKPVVLALGRLDPRKGIDT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 223 LggtFRALCA-AHPQLKLRLVLVGdGPERKHLERDLPEAL-------------FCGVQRGETLAAHYASGDLFLFPSLSE 288
Cdd:cd03800 238 L---VRAFAQlPELRELANLVLVG-GPSDDPLSMDREELAelaeelglidrvrFPGRVSRDDLPELYRAADVFVVPSLYE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 289 TFGNVVLEAQAAGLAVVAfdqAAAGQH---IRHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHASRQ-GWD 364
Cdd:cd03800 314 PFGLTAIEAMACGTPVVA---TAVGGLqdiVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHyTWE 390
|
....
gi 15596039 365 SIVE 368
Cdd:cd03800 391 SVAD 394
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
7-372 |
1.00e-25 |
|
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: 107.07 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 7 IALISETYPPEVNGVANTLGRLHAGLQQLGHRVQVV---RPRQPGDDGR--RSDAELVLTRGWPLPGyPGLQWGMSSLHK 81
Cdd:cd03821 2 ILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVstgDGYESLVVEEngRYIPPQDGFASIPLLR-QGAGRTDFSPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 82 LLRCWKRQR-PDVLYI-ATEGPLGFSALRAARRLGIPAVSGFHTNFqqysEHYGFGPLTRLVTGYLRWF--HNRTQMTLV 157
Cdd:cd03821 81 PNWLRRNLReYDVVHIhGVWTYTSLAACKLARRRGIPYVVSPHGML----DPWALQQKHWKKRIALHLIerRNLNNAALV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 158 -PSGSQRMELQRRGF--ERLNLLSRGVDSQLFHPSRRDPelRRRWGLGEQDIaVLHVGRLAAEKNLGLLGGTFRALCAAH 234
Cdd:cd03821 157 hFTSEQEADELRRFGlePPIAVIPNGVDIPEFDPGLRDR--RKHNGLEDRRI-ILFLGRIHPKKGLDLLIRAARKLAEQG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 235 PqlKLRLVLVG-DGPERKHLERDLPEA------LFCGVQRGETLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAF 307
Cdd:cd03821 234 R--DWHLVIAGpDDGAYPAFLQLQSSLglgdrvTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVIT 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596039 308 DQAAAGQHIRHGhNGVLAAPGDkSGFVEVASWLLDD---QERLRRVRLNARQHASRQGWDSIVEHFQN 372
Cdd:cd03821 312 DKCGLSELVEAG-CGVVVDPNV-SSLAEALAEALRDpadRKRLGEMARRARQVEENFSWEAVAGQLGE 377
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
32-359 |
2.20e-25 |
|
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: 105.51 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 32 LQQLGHRVQVVRPRQPGDDGRRSDAELVLTRGWPLPGYPglqWGMSSLHKLLRcwkRQRPDVLYIATEGPlGFSALRAAR 111
Cdd:cd03819 24 LAERGHRVLVVTAGGPLLPRLRQIGIGLPGLKVPLLRAL---LGNVRLARLIR---RERIDLIHAHSRAP-AWLGWLASR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 112 RLGIPAVSGFHtnfQQYSEHYGFGPLTRLVtgylRWFHNRTQMTLVPSGSQRMELQRRGFERLNLLSRGVDSQLFHPsRR 191
Cdd:cd03819 97 LTGVPLVTTVH---GSYLATYHPKDFALAV----RARGDRVIAVSELVRDHLIEALGVDPERIRVIPNGVDTDRFPP-EA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 192 DPELRRRWGLGEQDIAVLHVGRLAAEKNLGLLggtFRALCAAHPQLKLRLVLVGDGPERKHLERDLPEAL------FCGV 265
Cdd:cd03819 169 EAEERAQLGLPEGKPVVGYVGRLSPEKGWLLL---VDAAAELKDEPDFRLLVAGDGPERDEIRRLVERLGlrdrvtFTGF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 266 QrgETLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNGVLAAPGDKSGFVEVASWLLDDQE 345
Cdd:cd03819 246 R--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALADAIRAAKLLPE 323
|
330
....*....|....
gi 15596039 346 RLRRVRLNARQHAS 359
Cdd:cd03819 324 AREKLQAAAALTEA 337
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
77-372 |
2.46e-25 |
|
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: 105.40 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 77 SSLHKLLRCWKRQRPDVLYiaTEGPLGFSALrAARRLGIPAVSGFHTNFQQYSEHYGFGPLTRLvtgYLRWFHNRTqmtl 156
Cdd:cd03820 74 KKVRRLRKYLKNNKPDVVI--SFRTSLLTFL-ALIGLKSKLIVWEHNNYEAYNKGLRRLLLRRL---LYKRADKIV---- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 157 VPSGSQRMELQRRGFERL----NLLSRGVDSQLFHPSRRdpelrrrwglgeqdiAVLHVGRLAAEKNLGLLGGTFRALCA 232
Cdd:cd03820 144 VLTEADKLKKYKQPNSNVvvipNPLSFPSEEPSTNLKSK---------------RILAVGRLTYQKGFDLLIEAWALIAK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 233 AHPQLKLRLVlvGDGPERKHLER-----DLPE-ALFCGVQRGetLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVA 306
Cdd:cd03820 209 KHPDWKLRIY--GDGPEREELEKlidklGLEDrVKLLGPTKN--IAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIIS 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596039 307 FD-QAAAGQHIRHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHASRQGWDSIVEHFQN 372
Cdd:cd03820 285 FDcPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAERFSIEKIIKQWEE 351
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
19-361 |
4.93e-25 |
|
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: 104.75 E-value: 4.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 19 NGVANTLGRLHAGLQQLGHRVQVVRPRQPGDDGRRSDAELVLTRGWPLPGYpglqwgMSSLHKLLRCW------KRQRPD 92
Cdd:cd03811 12 GGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLK------LIKLGLLKAILklkrilKRAKPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 93 VLyIATEGPLGFsALRAARRLGIPAVSGFHTNFQqyseHYGFGPLTRLVTGYLRWFHNRTqmtLVPSGSQRMELQRRGFE 172
Cdd:cd03811 86 VV-ISFLGFATY-IVAKLAAARSKVIAWIHSSLS----KLYYLKKKLLLKLKLYKKADKI---VCVSKGIKEDLIRLGPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 173 RLNLLS---RGVDSQLFHPSRRDPELRRrwglGEQDIAVLHVGRLAAEKNLGLLGGTFRALCAAHPqlKLRLVLVGDGPE 249
Cdd:cd03811 157 PPEKIEviyNPIDIDRIRALAKEPILNE----PEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYP--DVKLVILGDGPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 250 RKHLE---RDL---PEALFCGVQrgETLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNGV 323
Cdd:cd03811 231 REELEklaKELglaERVIFLGFQ--SNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15596039 324 LAAPGDKSGFVEVASWLLDDQER--LRRVRLNARQHASRQ 361
Cdd:cd03811 309 LVPDGDAAALAGILAALLQKKLDaaLRERLAKAQEAVFRE 348
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
19-182 |
7.34e-25 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 99.91 E-value: 7.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 19 NGVANTLGRLHAGLQQLGHRVQVVRPRQPGDDGRRsDAELVLTRGWPLPGYPGLQWGMSSLHKLLRCWKRQRPDVLYIAT 98
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEE-VVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 99 EGPLGFSALRAARRLGIPAVSGFHTNFQQYSEHYGF-GPLTRLVTGYLRWFHNRTQMTLVPSGSQRMELQRR-GF--ERL 174
Cdd:pfam13439 80 PFPLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARlSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLyGVppEKI 159
|
....*...
gi 15596039 175 NLLSRGVD 182
Cdd:pfam13439 160 RVIPNGVD 167
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
180-375 |
2.31e-24 |
|
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.
Pssm-ID: 340851 [Multi-domain] Cd Length: 364 Bit Score: 103.18 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 180 GVDSQLFHPSRRdPELRRRWGLGEQDIAVLhVGRLAAEKNLGLLGGTFRALCAAHPQLKLRLVLVGDGPER----KHLER 255
Cdd:cd03825 169 GIDTEIFAPVDK-AKARKRLGIPQDKKVIL-FGAESVTKPRKGFDELIEALKLLATKDDLLLVVFGKNDPQivilPFDII 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 256 DLPEalfcgVQRGETLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNGVLAAPGDKSGFVE 335
Cdd:cd03825 247 SLGY-----IDDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAE 321
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15596039 336 VASWLLDDQERLRRVRLNARQHASRQgWDSIVEhFQNYLE 375
Cdd:cd03825 322 AIEWLLANPKERESLGERARALAENH-FDQRVQ-AQRYLE 359
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
51-361 |
4.93e-22 |
|
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: 96.37 E-value: 4.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 51 GRRSDAEL------VLTRGWPLPGYPGLQWGMSSLH---KLLRCWKRQRPDVLYiATEGPLGFSALRAARRLGIPAVSGF 121
Cdd:cd05844 33 GCRRLAPApfdgvaLRALGGSGPLRWLRQMAQRLLGwsaPRLGGAAGLAPALVH-AHFGRDGVYALPLARALGVPLVVTF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 122 H-TNFQQYSEHYGFGPLTRLVTGYLRWFHNRTQMTLVP-SGSQRMELQRRGF--ERLNLLSRGVDSQLFHPSRRDPELRR 197
Cdd:cd05844 112 HgFDITTSRAWLAASPGWPSQFQRHRRALQRPAALFVAvSGFIRDRLLARGLpaERIHVHYIGIDPAKFAPRDPAERAPT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 198 rwglgeqdiaVLHVGRLAAEKNLGLLGGTFRALCAAHPQLklRLVLVGDGPERKHLE---RDLPEALFCGVQRGETLAAH 274
Cdd:cd05844 192 ----------ILFVGRLVEKKGCDVLIEAFRRLAARHPTA--RLVIAGDGPLRPALQalaAALGRVRFLGALPHAEVQDW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 275 YASGDLFLFPSL------SETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNGVLAAPGDKSGFVEVASWLLDDQERLR 348
Cdd:cd05844 260 MRRAEIFCLPSVtaasgdSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALAD 339
|
330
....*....|...
gi 15596039 349 RVRLNARQHASRQ 361
Cdd:cd05844 340 RMGGAARAFVCEQ 352
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
6-368 |
8.39e-21 |
|
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: 93.18 E-value: 8.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 6 SIALISETYPPEVNGVANTLGRLHAGLQQLGHRVQVVRPRQPGDDGRRSDAELVLTRGWPL----------PGYPGLQWG 75
Cdd:cd03794 1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGATETKDGIRVirvklgpikkNGLIRRLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 76 MSSL---HKLLRCWKRQRPDVLyIATEGP--LGFSALRAARRLGIPAVSGFHTNFQQYSEHYGF---GPLTRLVTGYLRW 147
Cdd:cd03794 81 YLSFalaALLKLLVREERPDVI-IAYSPPitLGLAALLLKKLRGAPFILDVRDLWPESLIALGVlkkGSLLKLLKKLERK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 148 FHNRTQMTLVPSGSQRMELQRRGF--ERLNLLSRGVDSQLFHPSRRDpELRRRWGLgEQDIAVLHVGrlaaekNLGL--- 222
Cdd:cd03794 160 LYRLADAIIVLSPGLKEYLLRKGVpkEKIIVIPNWADLEEFKPPPKD-ELRKKLGL-DDKFVVVYAG------NIGKaqg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 223 LGGTFRALCAAHPQLKLRLVLVGDGPERKHL-----ERDLPEALFCGVQRGETLAAHYASGDLFLFPsLSETFGNV---- 293
Cdd:cd03794 232 LETLLEAAERLKRRPDIRFLFVGDGDEKERLkelakARGLDNVTFLGRVPKEEVPELLSAADVGLVP-LKDNPANRgssp 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596039 294 --VLEAQAAGLAVVAFDQAAAGQHIRHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHASRQG-WDSIVE 368
Cdd:cd03794 311 skLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFsREKLAD 388
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
173-371 |
2.10e-20 |
|
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: 91.71 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 173 RLNLLSRGVDSQLFHPSRRD-PELRRRWGLGEQDIAVLHVGRLAAEKNLGLLGGTFRALCAAHPQL--KLRLVLVGDGPE 249
Cdd:TIGR03088 161 KIHQIYNGVDTERFHPSRGDrSPILPPDFFADESVVVGTVGRLQAVKDQPTLVRAFALLVRQLPEGaeRLRLVIVGDGPA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 250 RKHLERDLPEAlfcGVQR-----GET--LAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNG 322
Cdd:TIGR03088 241 RGACEQMVRAA---GLAHlvwlpGERddVPALMQALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTG 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15596039 323 VLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHASRQ-GWDSIVEHFQ 371
Cdd:TIGR03088 318 ALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQfSINAMVAAYA 367
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
21-377 |
1.37e-19 |
|
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: 89.33 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 21 VANTLGrlhAGLQQLGHRVQVVRPRQP----GDDGRRSDAElVLTRGWPLPGYPGLQWGMSSlhKLLRCWKRQRPDVLYI 96
Cdd:cd04962 17 VATELG---LELAERGHEVHFISSAIPfrlnLYSGNIFFHE-VEVPNYPLFEYPPYTLALAS--KIVEVAKEHKLDVLHA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 97 ATEGPLGFSALRAARRLG--IPAVSGFH-TNFQQYSEHYGFGPLTRLVtgylrwFHNRTQMTLVpSGSQRMELqRRGFE- 172
Cdd:cd04962 91 HYAIPHASCAYLAREILGekIPIVTTLHgTDITLVGYDPSLQPAVRFS------INKSDRVTAV-SSSLRQET-YELFDv 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 173 --RLNLLSRGVDSQLFHPSRRDPELRRRWGLGEQDIaVLHVGRLAAEKNLGLLGGTFRALcaaHPQLKLRLVLVGDGPER 250
Cdd:cd04962 163 dkDIEVIHNFIDEDVFKRKPAGALKRRLLAPPDEKV-VIHVSNFRPVKRIDDVVRVFARV---RRKIPAKLLLVGDGPER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 251 ---KHLERDL---PEALFCGVQrgETLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNGVL 324
Cdd:cd04962 239 vpaEELARELgveDRVLFLGKQ--DDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFL 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15596039 325 AAPGDKSGFVEVASWLLDDQERLRRVRLNAR-QHASRQGWDSIVEHFQNYLEDA 377
Cdd:cd04962 317 SDVGDVDAMAKSALSILEDDELYNRMGRAARkRAAERFDPERIVPQYEAYYRRL 370
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
78-360 |
6.13e-19 |
|
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: 87.27 E-value: 6.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 78 SLHKLLrcwKRQRPDVLYIATEGPlGFSALRAARRLGIP----AVSGFHTNFqqysehyGFGPLTRLVTGYL-RWFHNRT 152
Cdd:cd03808 72 KLYKLL---KKEKPDIVHCHTPKP-GILGRLAARLAGVPkviyTVHGLGFVF-------TEGKLLRLLYLLLeKLALLFT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 153 QMTLVPSGSQRMELQRRGFERLN----LLSRGVDSQLFHPSRRDPElrrrwglgEQDIAVLHVGRLAAEKNLGLLGGTFR 228
Cdd:cd03808 141 DKVIFVNEDDRDLAIKKGIIKKKktvlIPGSGVDLDRFQYSPESLP--------SEKVVFLFVARLLKDKGIDELIEAAK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 229 ALCAAHPqlKLRLVLVGDGPERKHLERDLPEALFCGVQR--GET--LAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAV 304
Cdd:cd03808 213 ILKKKGP--NVRFLLVGDGELENPSEILIEKLGLEGRIEflGFRsdVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPV 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596039 305 VAFDQAAAGQHIRHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHASR 360
Cdd:cd03808 291 ITTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEE 346
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
208-359 |
2.00e-15 |
|
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: 76.93 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 208 VLHVGRLAAEKNlgllggtFRALCAAHPQLKLRLVLVGDGPERKHLERDLPEAL-----FCGVQRGETLAAHYASGDLFL 282
Cdd:cd03795 194 FLFIGRLVYYKG-------LDYLIEAAQYLNYPIVIGGEGPLKPDLEAQIELNLldnvkFLGRVDDEEKVIYLHLCDVFV 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 283 FPSL--SETFGNVVLEAQAAGLAVVAFDQAAAGQHI-RHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHAS 359
Cdd:cd03795 267 FPSVlrSEAFGIVLLEAMMCGKPVISTNIGTGVPYVnNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFE 346
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
7-324 |
3.27e-15 |
|
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: 74.75 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 7 IALISETYPPEVNGVANTLGRLHAGLQQLGHRVQVVrprqpgddGRRSDAelvltrgwplpgypglqwgmssLHKLLRCW 86
Cdd:cd01635 1 ILLVTGEYPPLRGGLELHVRALARALAALGHEVTVL--------ALLLLA----------------------LRRILKKL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 87 KRQRPDVLYIATEGPLGFSALRAARRLGIPAVSGFHTNFQQYSEHYGFGPLTRlVTGYLRWFHnrtqmtlvpsgsqrmel 166
Cdd:cd01635 51 LELKPDVVHAHSPHAAALAALLAARLLGIPIVVTVHGPDSLESTRSELLALAR-LLVSLPLAD----------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 167 qrrgferlnllsrgvdsqlfhpsrrdpelrrrwglgeqdiaVLHVGRLAAEKNLGLLGGTFRALCAAHPqlKLRLVLVGD 246
Cdd:cd01635 113 -----------------------------------------KVSVGRLVPEKGIDLLLEALALLKARLP--DLVLVLVGG 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 247 GPERKHLE------RDLPEALFCG-VQRGETLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHG 319
Cdd:cd01635 150 GGEREEEEalaaalGLLERVVIIGgLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDG 229
|
....*
gi 15596039 320 HNGVL 324
Cdd:cd01635 230 ENGLL 234
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
209-324 |
1.06e-13 |
|
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: 71.93 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 209 LHVGRLAAEKNLGLLGGTFRalcaahpQLKLRLVLVGDGPERKHLE-RDLPEALFCGVQRGETLAAHYASGDLFLFPSlS 287
Cdd:cd03804 203 LTASRLVPYKRIDLAVEAFN-------ELPKRLVVIGDGPDLDRLRaMASPNVEFLGYQPDEVLKELLSKARAFVFAA-E 274
|
90 100 110
....*....|....*....|....*....|....*..
gi 15596039 288 ETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNGVL 324
Cdd:cd03804 275 EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGIL 311
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
19-173 |
1.24e-13 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 68.20 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 19 NGVANTLGRLHAGLQQLGHRVQVVRPRQPGDDGRRSDAELVLTRgWPLPGYPGLQWGMSSLHKLLRCWKRQRPDVLYIAT 98
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHR-LPVPPRPSPLADLAALRRLRRLLRAERPDVVHAHS 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596039 99 eGPLGFSALRAARRLGIPAVSGFHTNfqqySEHYGFGPLTRLVTGYLRWFHNRTQMTLVPSGSQRMELQRRGFER 173
Cdd:pfam13579 80 -PTAGLAARLARRRRGVPLVVTVHGL----ALDYGSGWKRRLARALERRLLRRADAVVVVSEAEAELLRALGVPA 149
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
30-368 |
1.64e-12 |
|
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: 68.16 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 30 AGLQQL-GHRVQVVRPRQPGDDGRRSDAELVLTRGWplpgYPGLQWGMSSLHKLL--RCWKRQRPDVLYIAT-EGPLgfs 105
Cdd:cd03809 25 KALAKNdPDESVLAVPPLPGELLRLLREYPELSLGV----IKIKLWRELALLRWLqiLLPKKDKPDLLHSPHnTAPL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 106 alraaRRLGIPAVSGFHT-NFQQYSEHYGFGPLTRLVTGYLRWFHNRTQMtLVPSGSQRMELQRRGFERLNLLS--RGVD 182
Cdd:cd03809 98 -----LLKGCPQVVTIHDlIPLRYPEFFPKRFRLYYRLLLPISLRRADAI-ITVSEATRDDIIKFYGVPPEKIVviPLGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 183 SQLFHPSRRDPELRRRWGLGEQDIavLHVGRLAAEKNLGLLGGTFRALCAAHPqlKLRLVLVGDGPERKhleRDLPEALF 262
Cdd:cd03809 172 DPSFFPPESAAVLIAKYLLPEPYF--LYVGTLEPRKNHERLLKAFALLKKQGG--DLKLVIVGGKGWED---EELLDLVK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 263 CGVQRG----------ETLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFDQAA----AGQHirhghnGVLAAPG 328
Cdd:cd03809 245 KLGLGGrvrflgyvsdEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVlpevAGDA------ALYFDPL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15596039 329 DKSGFVEVASWLLDDQERLRRVRLNARQHASRQGWDSIVE 368
Cdd:cd03809 319 DPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAE 358
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
180-308 |
1.62e-11 |
|
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: 65.00 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 180 GVDSQLFHPSRRDPELRRRWGLGEQDIAVLHVGRLAAEKNLGLLGGTFRALCAAHPqlKLRLVLVGDGPERKHL-----E 254
Cdd:cd03812 166 GIDIEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNP--NVKLVLVGEGELKEKIkekvkE 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15596039 255 RDLPE-ALFCGVQrgETLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFD 308
Cdd:cd03812 244 LGLEDkVIFLGFR--NDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSD 296
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
166-308 |
3.48e-11 |
|
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: 64.00 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 166 LQRRGFERLN--LLSRGVDSQLFhpsRRDPE----LRRRWGLGEQDIAVLHVGRLAAEKNLGLLGGTFRALCAAHPQLKL 239
Cdd:cd04951 146 IAKKAFSKNKsvPVYNGIDLNKF---KKDINvrlkIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKL 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596039 240 rlVLVGDGPERKHLER-----DLPEALFCGVQRGEtLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFD 308
Cdd:cd04951 223 --LIAGDGPLRNELERlicnlNLVDRVILLGQISN-ISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATD 293
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
6-306 |
9.03e-11 |
|
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: 63.03 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 6 SIALISETYPPEVNGVANTLGRLHAGLQQLGHRVQVVRPRQPGDDGRRsdaelVLTRG------WPLPGYPGLQWG-MSS 78
Cdd:cd03796 1 RICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVITHAYGNRVGVR-----YLTNGlkvyylPFKVFYNQSTLPtLFS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 79 LHKLLR-CWKRQRPDVLYI-ATEGPLGFSALRAARRLGIPAVsgfhtnfqqYSEH--YGFGPLTRLVTG-YLRWF-HNRT 152
Cdd:cd03796 76 TFPLLRnILIRERIQIVHGhQAFSSLAHEALFHARTLGLKTV---------FTDHslFGFADASSILTNkLLRFSlADID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 153 QMTLVPSGSQRMELQRRGF--ERLNLLSRGVDSQLFHP--SRRDPElrrrwglgeqDIAVLHVGRLAAEKNLGLLGGTFR 228
Cdd:cd03796 147 HVICVSHTSKENTVLRASLdpRIVSVIPNAVDSSDFTPdpSKPDPN----------KITIVVISRLVYRKGIDLLVGIIP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 229 ALCAAHPqlKLRLVLVGDGPERKHLE--------RDLPEALfcGVQRGETLAAHYASGDLFLFPSLSETFGNVVLEAQAA 300
Cdd:cd03796 217 RICKKHP--NVRFIIGGDGPKRIELEemrekyqlQDRVELL--GAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASC 292
|
....*.
gi 15596039 301 GLAVVA 306
Cdd:cd03796 293 GLLVVS 298
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
7-359 |
1.75e-10 |
|
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: 61.92 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 7 IALISETY----PPEVNGVANTLGRLHAGLQQLGHRVQVVRPrqPGDDGRRSDAELV--LTRGWPLPGYPGLQWGMSSLH 80
Cdd:cd03802 2 IAQVSPPRgpvpPGKYGGTELVVSALTEGLVRRGHEVTLFAP--GDSHTSAPLVAVIprALRLDPIPQESKLAELLEALE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 81 KLLRCWKRqrpDVLYIATEGPLgfsaLRAARRLGIPAVSGFHtnfqqysehygFGPLTRLVTGYLRwfHNRTQMTLVPSg 160
Cdd:cd03802 80 VQLRASDF---DVIHNHSYDWL----PPFAPLIGTPFVTTLH-----------GPSIPPSLAIYAA--EPPVNYVSISD- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 161 sqrmeLQRRGFERLNLLSR---GVDSQLFHPSRRDPELrrrwglgeqdiaVLHVGRLAAEKNLGLlggtfrALCAAHpQL 237
Cdd:cd03802 139 -----AQRAATPPIDYLTVvhnGLDPADYRFQPDPEDY------------LAFLGRIAPEKGLED------AIRVAR-RA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 238 KLRLVLVG-----DGPERKHLERDLPEALFCGVQRGETLAAHYASGDLFLFPSL-SETFGNVVLEAQAAGLAVVAFDQAA 311
Cdd:cd03802 195 GLPLKIAGkvrdeDYFYYLQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGG 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15596039 312 AGQHIRHGHNGVLAAPgdksgfVEVASWLLDDQERLRR--VRLNARQHAS 359
Cdd:cd03802 275 LPEVIQHGETGFLVDS------VEEMAEAIANIDRIDRaaCRRYAEDRFS 318
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
172-360 |
3.37e-10 |
|
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: 61.58 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 172 ERLNLLSRGVDSQLFHPSRRDPElrrrwglgEQDIAVLH-VGRLAAEKNLGLLGGTFRALCAAHPQLKLRLVlvgdGPER 250
Cdd:cd03813 267 DKTRVIPNGIDIQRFAPAREERP--------EKEPPVVGlVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLI----GPED 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 251 KHLE-----RDLPEAL-------FCGVQRgetLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVVAFD-----QAAAG 313
Cdd:cd03813 335 EDPEyaqecKRLVASLglenkvkFLGFQN---IKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDvgscrELIYG 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15596039 314 QHIRHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHASR 360
Cdd:cd03813 412 ADDALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEK 458
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
208-360 |
6.41e-10 |
|
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: 60.01 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 208 VLHVGRLAAEKNLGLLggtFRALCAAHPQL-KLRLVLVGDGPERKHL-----ERDLPEALFcgvQRGET--LAAHYASGD 279
Cdd:cd04949 163 IITISRLAPEKQLDHL---IEAVAKAVKKVpEITLDIYGYGEEREKLkklieELHLEDNVF---LKGYHsnLDQEYQDAY 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 280 LFLFPSLSETFGNVVLEAQAAGLAVVAFD-QAAAGQHIRHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHA 358
Cdd:cd04949 237 LSLLTSQMEGFGLTLMEAIGHGLPVVSYDvKYGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIA 316
|
..
gi 15596039 359 SR 360
Cdd:cd04949 317 EK 318
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
193-376 |
1.07e-09 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 59.80 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 193 PELRRRWGLGEQDIAVLHVGRLAAEKNLGLLGGTFRALCAAHPQLKlrLVLVGDGPERKHLE--------RDLPEAL--- 261
Cdd:PRK15484 181 PNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLK--LVVVGDPTASSKGEkaayqkkvLEAAKRIgdr 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 262 --FCGVQRGETLAAHYASGDLFLFPS-LSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNGV-LAAPGDKSGFVEVA 337
Cdd:PRK15484 259 ciMLGGQPPEKMHNYYPLADLVVVPSqVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYhLAEPMTSDSIISDI 338
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15596039 338 SWLLDDQERLrRVRLNARQHA-SRQGWDSIVEHFQNYLED 376
Cdd:PRK15484 339 NRTLADPELT-QIAEQAKDFVfSKYSWEGVTQRFEEQIHN 377
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
180-360 |
1.12e-08 |
|
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: 56.60 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 180 GVDSQLFHPsrrDPELRRRwglgEQDIAVLHVGRLA---AEKNLGLLGG--TF-RALC---AAHPQLklRLVLVGD---- 246
Cdd:cd03818 187 GVDTDRLAP---DPAARLR----LLNGTELKAGDPVityVARNLEPYRGfhVFmRALPriqARRPDA--RVVVVGGdgvs 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 247 --------GPERKHLERDLP----EALFCG-VQRGETLAAHYASgDLFLFPslseTFGNV----VLEAQAAGLAVVAFDQ 309
Cdd:cd03818 258 ygspppdgGSWKQKMLAELGvdleRVHFVGkVPYDQYVRLLQLS-DAHVYL----TYPFVlswsLLEAMACGCPVIGSDT 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15596039 310 AAAGQHIRHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHASR 360
Cdd:cd03818 333 APVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVER 383
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
7-360 |
1.08e-07 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 53.44 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 7 IALISETYPPEVNGVANTLGRLHAGLQQLGHRVQVVR--PRQP------GDDGRRSDAELVL-TRGW--PL--PGYPG-- 71
Cdd:PRK10307 3 ILVYGINYAPELTGIGKYTGEMAEWLAARGHEVRVITapPYYPqwrvgeGYSAWRYRRESEGgVTVWrcPLyvPKQPSgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 72 ------LQWGMSSLHKLLRcWKRQRPDVLyIATEGPLgFS---ALRAARRLGipAVSGFHtnFQQYSEHYGF-------G 135
Cdd:PRK10307 83 krllhlGSFALSSFFPLLA-QRRWRPDRV-IGVVPTL-FCapgARLLARLSG--ARTWLH--IQDYEVDAAFglgllkgG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 136 PLTRLVTGYLRW----FHNrtqmtlVPSGSQRM--ELQRRGF--ERLNLLSRGVDSQLFHP--SRRDPELRRRWGLGEQD 205
Cdd:PRK10307 156 KVARLATAFERSllrrFDN------VSTISRSMmnKAREKGVaaEKVIFFPNWSEVARFQPvaDADVDALRAQLGLPDGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 206 IAVLHVGRLAAEKNLGLLGGTFRALcAAHPQLKLrlVLVGDGPERKHLE-----RDLPEALFCGVQRGETLAAHYASGDL 280
Cdd:PRK10307 230 KIVLYSGNIGEKQGLELVIDAARRL-RDRPDLIF--VICGQGGGKARLEkmaqcRGLPNVHFLPLQPYDRLPALLKMADC 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 281 FLFPSLSETfGNVVLEAQ-----AAGLAVVAFDQAAAGQHIRHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNAR 355
Cdd:PRK10307 307 HLLPQKAGA-ADLVLPSKltnmlASGRNVVATAEPGTELGQLVEGIGVCVEPESVEALVAAIAALARQALLRPKLGTVAR 385
|
....*
gi 15596039 356 QHASR 360
Cdd:PRK10307 386 EYAER 390
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
172-345 |
3.60e-07 |
|
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: 51.68 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 172 ERLNLLSRGVDSQLFHPS-RRDPElrrrwglgEQDIAVLHVGRLAAEKNLGLLGGTFRALCAAHPQLKLRLVlvGDGPER 250
Cdd:cd03799 148 KKIIVHRSGIDCNKFRFKpRYLPL--------DGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQII--GDGDLK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 251 KHLERDLPE------ALFCGVQRGETLAAHYASGDLFLFPSLSETFG------NVVLEAQAAGLAVVAFDQAAAGQHIRH 318
Cdd:cd03799 218 EQLQQLIQElnigdcVKLLGWKPQEEIIEILDEADIFIAPSVTAADGdqdgppNTLKEAMAMGLPVISTEHGGIPELVED 297
|
170 180
....*....|....*....|....*..
gi 15596039 319 GHNGVLAAPGDKSGFVEVASWLLDDQE 345
Cdd:cd03799 298 GVSGFLVPERDAEAIAEKLTYLIEHPA 324
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
285-374 |
1.76e-05 |
|
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.
Pssm-ID: 340823 [Multi-domain] Cd Length: 378 Bit Score: 46.55 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 285 SLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNGVLAAPGDKSGfVEVASwLLDDQERLRRVRLNARQHASRQGwd 364
Cdd:cd03792 287 STREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAA-VRILR-LLTDPELRRKMGLAAREHVRDNF-- 362
|
90
....*....|
gi 15596039 365 SIVEHFQNYL 374
Cdd:cd03792 363 LITGNLRAWL 372
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
194-291 |
5.11e-05 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 45.08 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 194 ELRRRWGLGEQD----IAVlhVGRLAAEKNLGLLGGTFRALCaahpQLKLRLVLVGDGPER-----KHLERDLPEAlfCG 264
Cdd:COG0297 282 ALQEELGLPVDPdaplIGM--VSRLTEQKGLDLLLEALDELL----EEDVQLVVLGSGDPEyeeafRELAARYPGR--VA 353
|
90 100 110
....*....|....*....|....*....|.
gi 15596039 265 VQRG--ETLAaH--YASGDLFLFPSLSETFG 291
Cdd:COG0297 354 VYIGydEALA-HriYAGADFFLMPSRFEPCG 383
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
218-324 |
1.97e-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: 43.22 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 218 KNLGLLGGTFRALCAAHPQLKLRLVLVGDGPERKHLERD---LPEAL---FCGVQRGETLAAHYA--SGDLFLFPSLSET 289
Cdd:cd04946 237 KRIDLIIETLNSLCVAHPSICISWTHIGGGPLKERLEKLaenKLENVkvnFTGEVSNKEVKQLYKenDVDVFVNVSESEG 316
|
90 100 110
....*....|....*....|....*....|....*
gi 15596039 290 FGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNGVL 324
Cdd:cd04946 317 IPVSIMEAISFGIPVIATNVGGTREIVENETNGLL 351
|
|
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
281-397 |
4.81e-04 |
|
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.
Pssm-ID: 274147 [Multi-domain] Cd Length: 1050 Bit Score: 42.46 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 281 FLFPSLSETFGNVVLEAQAAGLAVVAFDQAAAGQHIRHGHNGVLAAPGDKSGFVEVASWLLDDQERLRRVRLNARQHASR 360
Cdd:TIGR02468 575 FINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKLVADKQLWAECRQNGLKNIHL 654
|
90 100 110
....*....|....*....|....*....|....*....
gi 15596039 361 QGWDsivEHFQNYLEDACASPLVQP--ARSKPERPPAED 397
Cdd:TIGR02468 655 FSWP---EHCKTYLSRIASCRPRHPqwQRDTDDGEEASE 690
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
194-301 |
1.05e-03 |
|
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: 41.01 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 194 ELRRRWGLGEQDIAVL--HVGRLAAEKNLGLLGGTFRALCaahpQLKLRLVLVGDGPER-----KHLERDLPEAlfCGVQ 266
Cdd:cd03791 281 ALQKELGLPVDPDAPLfgFVGRLTEQKGVDLILDALPELL----EEGGQLVVLGSGDPEyeqafRELAERYPGK--VAVV 354
|
90 100 110
....*....|....*....|....*....|....*....
gi 15596039 267 RG--ETLAaH--YASGDLFLFPSLSETFGNVVLEAQAAG 301
Cdd:cd03791 355 IGfdEALA-HriYAGADFFLMPSRFEPCGLVQMYAMRYG 392
|
|
| GT33_ALG1-like |
cd03816 |
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ... |
300-383 |
2.55e-03 |
|
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.
Pssm-ID: 340843 [Multi-domain] Cd Length: 411 Bit Score: 39.95 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 300 AGLAVVAFDQAAAGQHIRHGHNGVLAAPGDksgfvEVA----SWLLDD-QERLRRVRLNARQhASRQGWDsivehfQNYl 374
Cdd:cd03816 337 CGLPVCAMDFKCIGELVKHGVNGLVFGDSE-----ELAeqliDLLSDFdRGKLNVLKKGAQE-ESENRWD------ENW- 403
|
....*....
gi 15596039 375 eDACASPLV 383
Cdd:cd03816 404 -DRVAGPLF 411
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
194-291 |
3.52e-03 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 39.33 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 194 ELRRRWGLGEQDIAVL-HVGRLAAEKNLGLLGGTFRALCAAHPQLklrlVLVGDGpER------KHLERDLPEAlfCGVQ 266
Cdd:PRK00654 270 ALQERFGLPDDDAPLFaMVSRLTEQKGLDLVLEALPELLEQGGQL----VLLGTG-DPeleeafRALAARYPGK--VGVQ 342
|
90 100
....*....|....*....|....*....
gi 15596039 267 RG--ETLAaH--YASGDLFLFPSLSETFG 291
Cdd:PRK00654 343 IGydEALA-HriYAGADMFLMPSRFEPCG 370
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
232-329 |
5.33e-03 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 38.86 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 232 AAHPqlKLRLVLVGDGP---ERKHLERDL---PEALFCGVQRgeTLAAHYASGDLFLFPSLSETFGNVVLEAQAAGLAVV 305
Cdd:PRK15179 544 ASHP--KVRFIMVGGGPlleSVREFAQRLgmgERILFTGLSR--RVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVV 619
|
90 100
....*....|....*....|....
gi 15596039 306 AFDQAAAGQHIRHGHNGVLAAPGD 329
Cdd:PRK15179 620 TTLAGGAGEAVQEGVTGLTLPADT 643
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
27-118 |
7.86e-03 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 36.53 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596039 27 RLHAGLQQLGHRVQVVRPRQPGDDGRRSDAELVLTrgWPLPG-YPGLQWGMSSLHKLlrcWKRQRPDVLYIATEGPLGFS 105
Cdd:pfam13477 15 RWADALADRGYDVHVISSKGPAKDELIAEGIHVHR--LKVPRkGPLGYLKAFRLKKL---IKKIKPDVVHVHYAKPYGLL 89
|
90
....*....|...
gi 15596039 106 ALRAARRLGIPAV 118
Cdd:pfam13477 90 AGLAARLSGFPPV 102
|
|
| |
