|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
1-380 |
0e+00 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 757.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 1 MIKKIIFTVTPIFSIPPRGAAAVETWIYQVAKRLSIPNAIACIKNAGYPEYNKINDNCDIHYIGFSKVYKRLFQKWTRLD 80
Cdd:PRK15484 1 MIDKIIFTVTPIFSIPPRGAAAVETWIYQVAKRTSIPNRIACIKNPGYPEYTKVNDNCDIHYIGFSRIYKRLFQKWTRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 81 PLPYSQRILNIRDKVTTQEDSVIVIHNSMKLYRQIRERNPNAKLVMHMHNAFEPELPDNDAKIIVPSQFLKAFYEERLPA 160
Cdd:PRK15484 81 PLPYSQRILNIAHKFTITKDSVIVIHNSMKLYRQIRERAPQAKLVMHMHNAFEPELLDKNAKIIVPSQFLKKFYEERLPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 161 AAVSIVPNGFCAETYKRNPQDNLRQQLNIAEDATVLLYAGRISPDKGILLLLQAFKQLRTLRSNIKLVVVGDPYASRKGE 240
Cdd:PRK15484 161 ADISIVPNGFCLETYQSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGDPTASSKGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 241 KAEYQKKVLDAAKEIGTDCIMAGGQSPDQMHNFYHIADLVIVPSQVEEAFCMVAVEAMAAGKAVLASKKGGISEFVLDGI 320
Cdd:PRK15484 241 KAAYQKKVLEAAKRIGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGI 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 321 TGYHLAEPMSSDSIINDINRALADKERHQIAEKAKSLVFSKYSWENVAQRFEEQMKNWFD 380
Cdd:PRK15484 321 TGYHLAEPMTSDSIISDINRTLADPELTQIAEQAKDFVFSKYSWEGVTQRFEEQIHNWFD 380
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
4-373 |
1.74e-51 |
|
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: 175.80 E-value: 1.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 4 KIIFtVTPIFSIPPRGaaaVETWIYQVAKRLsipnaiaciKNAGYpeynkindncDIHYIGFS---------KVYKRLFQ 74
Cdd:cd03801 1 KILL-LSPELPPPVGG---AERHVRELARAL---------AARGH----------DVTVLTPAdpgeppeelEDGVIVPL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 75 KWTRLDPLPYSQRILNIRDKVTTQEDSVIVIHNSM-KLYRQIRERNPNAKLVMHMHNAFEPELPDNDA------------ 141
Cdd:cd03801 58 LPSLAALLRARRLLRELRPLLRLRKFDVVHAHGLLaALLAALLALLLGAPLVVTLHGAEPGRLLLLLAaerrllaraeal 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 142 -----KIIVPSQFLKAFYEERLPAAA--VSIVPNGFcaetYKRNPQDNLRQQLNIAEDATVLLYAGRISPDKGILLLLQA 214
Cdd:cd03801 138 lrradAVIAVSEALRDELRALGGIPPekIVVIPNGV----DLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 215 FKQLRTLRSNIKLVVVGDpyasrkgeKAEYQKKVLDAAKEIGTDCIMAGGQSPDQMHNFYHIADLVIVPSqVEEAFCMVA 294
Cdd:cd03801 214 LAKLLRRGPDVRLVIVGG--------DGPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPS-RYEGFGLVV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 295 VEAMAAGKAVLASKKGGISEFVLDGITGYhLAEPMSSDSIINDINRALADKE-RHQIAEKAKSLVFSKYSWENVAQRFEE 373
Cdd:cd03801 285 LEAMAAGLPVVATDVGGLPEVVEDGEGGL-VVPPDDVEALADALLRLLADPElRARLGRAARERVAERFSWERVAERLLD 363
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
195-355 |
1.53e-40 |
|
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: 140.49 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 195 VLLYAGRISPDKGILLLLQAFKQLRTLRSNIKLVVVGDpyasrkgEKAEYQKKVLDAAKEIGTDCIMAGGQSPDQMHNFY 274
Cdd:pfam00534 4 IILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGD-------GEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 275 HIADLVIVPSQVEeAFCMVAVEAMAAGKAVLASKKGGISEFVLDGITGYhLAEPMSSDSIINDINRALADKE-RHQIAEK 353
Cdd:pfam00534 77 KIADVFVLPSRYE-GFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGF-LVKPNNAEALAEAIDKLLEDEElRERLGEN 154
|
..
gi 132488 354 AK 355
Cdd:pfam00534 155 AR 156
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
163-370 |
1.66e-35 |
|
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: 133.90 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 163 VSIVPNGFCAETYkrNPQD---NLRQQLNIAEDATVLLYAGRISPDKGILLLLQAFKQLRTLRSNIKLVVVGDPYASRKg 239
Cdd:cd03800 189 INVVPPGVDLERF--FPVDraeARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGGPSDDPL- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 240 EKAEYQKKVLDAAKEIGTDCIMAGGQSPDQMHNFYHIADLVIVPSQVEeAFCMVAVEAMAAGKAVLASKKGGISEFVLDG 319
Cdd:cd03800 266 SMDREELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYE-PFGLTAIEAMACGTPVVATAVGGLQDIVRDG 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 132488 320 ITGYhLAEPMSSDSIINDINRALADKE-RHQIAEKAKSLVFSKYSWENVAQR 370
Cdd:cd03800 345 RTGL-LVDPHDPEALAAALRRLLDDPAlWQRLSRAGLERARAHYTWESVADQ 395
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
141-374 |
1.22e-31 |
|
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: 122.87 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 141 AKIIVPSQFLKA-FYEERLPAAAVSIVPNGFCAETYKrnPQDnlrQQLNIAEDATVLLYAGRISPDKGILLLLQAFKQLR 219
Cdd:cd03798 152 ARVIAVSKALAEeLVALGVPRDRVDVIPNGVDPARFQ--PED---RGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 220 TLRSNIKLVVVGDpyasrkGEKAEYQKKVLDAAKeIGTDCIMAGGQSPDQMHNFYHIADLVIVPSqVEEAFCMVAVEAMA 299
Cdd:cd03798 227 KARPDVVLLIVGD------GPLREALRALAEDLG-LGDRVTFTGRLPHEQVPAYYRACDVFVLPS-RHEGFGLVLLEAMA 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 132488 300 AGKAVLASKKGGISEFVLDGITGYhLAEPMSSDSIINDINRALADKERHQIAEKAKSLVFSKYSWENVAQRFEEQ 374
Cdd:cd03798 299 CGLPVVATDVGGIPEVVGDPETGL-LVPPGDADALAAALRRALAEPYLRELGEAARARVAERFSWVKAADRIAAA 372
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
102-372 |
7.80e-30 |
|
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: 117.82 E-value: 7.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 102 VIVIHN----SMKLYRQIRERNpnAKLVMHMHNAF------EPELPDNDAkIIVPSQFLKAFYEERLPAAA-VSIVPNGF 170
Cdd:cd03823 99 VVHTHNlsglGASLLDAARDLG--IPVVHTLHDYWllcprqFLFKKGGDA-VLAPSRFTANLHEANGLFSArISVIPNAV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 171 CAETYKRNPQDNLRQQLNIAedatvllYAGRISPDKGILLLLQAFKQLRtlRSNIKLVVVGDPYASRkgekaEYQKKVLD 250
Cdd:cd03823 176 EPDLAPPPRRRPGTERLRFG-------YIGRLTEEKGIDLLVEAFKRLP--REDIELVIAGHGPLSD-----ERQIEGGR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 251 AAKEIGTdcimaggQSPDQMHNFYHIADLVIVPSQVEEAFCMVAVEAMAAGKAVLASKKGGISEFVLDGITGYHLAePMS 330
Cdd:cd03823 242 RIAFLGR-------VPTDDIKDFYEKIDVLVVPSIWPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFA-PGD 313
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 132488 331 SDSIINDINRALADKERHQ-IAEKAKSLVFSKYSWENVAQRFE 372
Cdd:cd03823 314 AEDLAAAMRRLLTDPALLErLRAGAEPPRSTESQAEEYLKLYR 356
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
143-375 |
2.08e-29 |
|
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: 116.99 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 143 IIVPSQFLKAFYEERLPAAAVSIVPNGFCAETYKRNPQDNLRQQLNIAEDATVLLYAGRISPDKGILLLLQAFKQLRTlR 222
Cdd:cd03817 151 VIAPSEKIKDTLREYGVKGPIEVIPNGIDLDKFEKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKK-E 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 223 SNIKLVVVGDPYASRKGEKAEYQKKVLDAAKEIGTdcimaggQSPDQMHNFYHIADLVIVPSQVeEAFCMVAVEAMAAGK 302
Cdd:cd03817 230 PNIKLVIVGDGPEREELKELARELGLADKVIFTGF-------VPREELPEYYKAADLFVFASTT-ETQGLVYLEAMAAGL 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 132488 303 AVLASKKGGISEFVLDGITGYHLAEpmSSDSIINDINRALADKERHQIAEKAKSLVFSKYSWENVAQRFEEQM 375
Cdd:cd03817 302 PVVAAKDPAASELVEDGENGFLFEP--NDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAKSVEKLYEEV 372
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
127-325 |
2.18e-27 |
|
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: 108.26 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 127 HMHNAFEPELPDNDAKIIV----PSQFLKAFYEERLPAAAVSIVPNGFCAETYKRNPQDNLRQQLNIAEDATVLlYAGRI 202
Cdd:cd01635 41 LALRRILKKLLELKPDVVHahspHAAALAALLAARLLGIPIVVTVHGPDSLESTRSELLALARLLVSLPLADKV-SVGRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 203 SPDKGILLLLQAFKQLRTLRSNIKLVVVGDpyasrkGEKAEYQKKVLDAAKEIGTDCIMAGGQSPDQMHNFYHIADLVIV 282
Cdd:cd01635 120 VPEKGIDLLLEALALLKARLPDLVLVLVGG------GGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 132488 283 PSQVEeAFCMVAVEAMAAGKAVLASKKGGISEFVLDGITGYHL 325
Cdd:cd01635 194 PSRSE-GFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
195-344 |
6.69e-27 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 103.75 E-value: 6.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 195 VLLYAGRISPD-KGILLLLQAFKQLRTLRSNIKLVVVGDpyasrkGEKAEYQKKvldaAKEIGTDCIMAGGQspDQMHNF 273
Cdd:pfam13692 3 VILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVGD------GPEEELEEL----AAGLEDRVIFTGFV--EDLAEL 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 132488 274 YHIADLVIVPSqVEEAFCMVAVEAMAAGKAVLASKKGGISEfVLDGITGYhLAEPMSSDSIINDINRALAD 344
Cdd:pfam13692 71 LAAADVFVLPS-LYEGFGLKLLEAMAAGLPVVATDVGGIPE-LVDGENGL-LVPPGDPEALAEAILRLLED 138
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
142-370 |
8.53e-26 |
|
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: 106.68 E-value: 8.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 142 KIIVPSQF----LKAFYeeRLPAAAVSIVPNGfcAETYKRNPQDNLRQQLNIAEDATVLLYAGRISPDKGILLLLQAFKQ 217
Cdd:cd03809 141 AIITVSEAtrddIIKFY--GVPPEKIVVIPLG--VDPSFFPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFAL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 218 LRTLRSNIKLVVVGdpyasRKGEKAEYQKKVLDAAkEIGTDCIMAGGQSPDQMHNFYHIADLVIVPSQVeEAFCMVAVEA 297
Cdd:cd03809 217 LKKQGGDLKLVIVG-----GKGWEDEELLDLVKKL-GLGGRVRFLGYVSDEDLPALYRGARAFVFPSLY-EGFGLPVLEA 289
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 132488 298 MAAGKAVLASKkggISefVLDGITGYH--LAEPMSSDSIINDINRAL-ADKERHQIAEKAKSLVfSKYSWENVAQR 370
Cdd:cd03809 290 MACGTPVIASN---IS--VLPEVAGDAalYFDPLDPESIADAILRLLeDPSLREELIRKGLERA-KKFSWEKTAEK 359
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
109-373 |
1.69e-25 |
|
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: 105.86 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 109 MKLYRQIRERNP----------------------NAKLVMHMHNAFEPE------------LPDNDAKIIVPSQFLKAFY 154
Cdd:cd03807 69 LRLAKLIRKRNPdvvhtwmyhadligglaaklagGVKVIWSVRSSNIPQrltrlvrklcllLSKFSPATVANSSAVAEFH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 155 EER-LPAAAVSIVPNGFcaETYKRNPQDN----LRQQLNIAEDATVLLYAGRISPDKGILLLLQAFKQLRTLRSNIKLVV 229
Cdd:cd03807 149 QEQgYAKNKIVVIYNGI--DLFKLSPDDAsrarARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 230 VGDpyASRKGEKAEYQKKVLDAAKEIGTdcimagGQSPDqMHNFYHIADLVIVPSqVEEAFCMVAVEAMAAGKAVLASKK 309
Cdd:cd03807 227 VGR--GPERPNLERLLLELGLEDRVHLL------GERSD-VPALLPAMDIFVLSS-RTEGFPNALLEAMACGLPVVATDV 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 132488 310 GGISEFVLDGiTGYhLAEPMSSDSIINDINRALADKE-RHQIAEKAKSLVFSKYSWENVAQRFEE 373
Cdd:cd03807 297 GGAAELVDDG-TGF-LVPAGDPQALADAIRALLEDPEkRARLGRAARERIANEFSIDAMVRRYET 359
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
23-357 |
3.66e-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: 104.74 E-value: 3.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 23 VETWIYQVAKRLSIPNA---IACIKNAGYPEYNKINDncdihyigfskVYKRLFQKWTRlDPLPysqrILNIRDKVTTQE 99
Cdd:cd03819 13 AETYILDLARALAERGHrvlVVTAGGPLLPRLRQIGI-----------GLPGLKVPLLR-ALLG----NVRLARLIRRER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 100 DSVIVIHNS-MKLYRQIRERNPNAKLVMHMHN--AFEPELPD-------NDAKIIVPSQFLKAFYEERLPAAA--VSIVP 167
Cdd:cd03819 77 IDLIHAHSRaPAWLGWLASRLTGVPLVTTVHGsyLATYHPKDfalavraRGDRVIAVSELVRDHLIEALGVDPerIRVIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 168 NGFCAETYKRNPQDNLRQQLNIAEDATVLLYAGRISPDKGILLLLQAFKQLRTLRsNIKLVVVGD----PYASRKGEKAE 243
Cdd:cd03819 157 NGVDTDRFPPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEP-DFRLLVAGDgperDEIRRLVERLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 244 YQKKVldaakeigtdcIMAGGqsPDQMHNFYHIADLVIVPSqVEEAFCMVAVEAMAAGKAVLASKKGGISEFVLDGITGY 323
Cdd:cd03819 236 LRDRV-----------TFTGF--REDVPAALAASDVVVLPS-LHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGL 301
|
330 340 350
....*....|....*....|....*....|....
gi 132488 324 hLAEPMSSDSIINDINRALADKERHQIAEKAKSL 357
Cdd:cd03819 302 -LVPPGDAEALADAIRAAKLLPEAREKLQAAAAL 334
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
142-372 |
3.91e-24 |
|
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: 101.90 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 142 KIIVPSQFLKAFYEERLPAAAVS---IVPNGFCAETYKRNPqdnlrqqLNIAEDATVLLYAGRISPDKGILLLLQAFKQL 218
Cdd:cd03808 142 KVIFVNEDDRDLAIKKGIIKKKKtvlIPGSGVDLDRFQYSP-------ESLPSEKVVFLFVARLLKDKGIDELIEAAKIL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 219 RTLRSNIKLVVVGDPYasrkgEKAEYQKKVLDAAKEigtDCIMAGGQSPDqMHNFYHIADLVIVPSqVEEAFCMVAVEAM 298
Cdd:cd03808 215 KKKGPNVRFLLVGDGE-----LENPSEILIEKLGLE---GRIEFLGFRSD-VPELLAESDVFVLPS-YREGLPRSLLEAM 284
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 132488 299 AAGKAVLASKKGGISEFVLDGITGYhLAEPMSSDSIINDINRALADKE-RHQIAEKAKSLVFSKYSWENVAQRFE 372
Cdd:cd03808 285 AAGRPVITTDVPGCRELVIDGVNGF-LVPPGDVEALADAIEKLIEDPElRKEMGEAARKRVEEKFDEEKVVNKLL 358
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
127-375 |
1.07e-23 |
|
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: 100.83 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 127 HMHNAFEpelpdndaKIIVPSQFLKAFYEERlPAAAVSIVPNGFCAETYK-RNPQDNLRQQLNiAEDATVLLYAGRISPD 205
Cdd:cd03814 141 WFHNPFD--------TTLVPSPSIARELEGH-GFERVRLWPRGVDTELFHpSRRDAALRRRLG-PPGRPLLLYVGRLAPE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 206 KGILLLLQAFKQLrTLRSNIKLVVVGDpyasrkGEkaeyQKKVLDAAkeiGTDCIMAGGQSPDQMHNFYHIADLVIVPSq 285
Cdd:cd03814 211 KNLEALLDADLPL-AASPPVRLVVVGD------GP----ARAELEAR---GPDVIFTGFLTGEELARAYASADVFVFPS- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 286 VEEAFCMVAVEAMAAGKAVLASKKGGISEFVLDGITGYhLAEPMSSDSIINDINRALADKERHQIAEKAKSLVFSKYSWE 365
Cdd:cd03814 276 RTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGA-LVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERYSWE 354
|
250
....*....|
gi 132488 366 NVAQRFEEQM 375
Cdd:cd03814 355 AFLDNLLDYY 364
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
273-373 |
6.54e-23 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 92.75 E-value: 6.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 273 FYHIADLVIVPSqVEEAFCMVAVEAMAAGKAVLASKKGGISEFVLDGITGYhLAEPMSSDSIINDINRALADKE-RHQIA 351
Cdd:COG0438 17 LLAAADVFVLPS-RSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGL-LVPPGDPEALAEAILRLLEDPElRRRLG 94
|
90 100
....*....|....*....|..
gi 132488 352 EKAKSLVFSKYSWENVAQRFEE 373
Cdd:COG0438 95 EAARERAEERFSWEAIAERLLA 116
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
104-372 |
9.38e-23 |
|
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: 98.57 E-value: 9.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 104 VIHNSMKLYRQIRERNP--NAKLVMHMHNAFEPELPDNDAKIIVPSQFLKAFYEER-LPAAAVSIVPNGFCAETYKRNPQ 180
Cdd:cd03794 126 FILDVRDLWPESLIALGvlKKGSLLKLLKKLERKLYRLADAIIVLSPGLKEYLLRKgVPKEKIIVIPNWADLEEFKPPPK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 181 DNLRQqLNIAEDATVLLYAGRISPDKGILLLLQAFKQLRTlRSNIKLVVVGDpyasrkGEKAEYQKKVLDAAKEigTDCI 260
Cdd:cd03794 206 DELRK-KLGLDDKFVVVYAGNIGKAQGLETLLEAAERLKR-RPDIRFLFVGD------GDEKERLKELAKARGL--DNVT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 261 MAGGQSPDQMHNFYHIADLVIVPsQVEEAFCMVAV-----EAMAAGKAVLASKKGGISEFVLDGITGYhLAEPMSSDSII 335
Cdd:cd03794 276 FLGRVPKEEVPELLSAADVGLVP-LKDNPANRGSSpsklfEYMAAGKPILASDDGGSDLAVEINGCGL-VVEPGDPEALA 353
|
250 260 270
....*....|....*....|....*....|....*...
gi 132488 336 NDINRALADKE-RHQIAEKAKSLVFSKYSWENVAQRFE 372
Cdd:cd03794 354 DAILELLDDPElRRAMGENGRELAEEKFSREKLADRLL 391
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
138-373 |
1.45e-21 |
|
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.
Pssm-ID: 340848 [Multi-domain] Cd Length: 377 Bit Score: 94.74 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 138 DNDAKIIVPSQFLKAFYEERLPAAAVSIVPNGFCAETYKrnPQDNLRQQLNIAEDATVLLYAGRISPDKGILLLLQAFKQ 217
Cdd:cd03821 151 NNAALVHFTSEQEADELRRFGLEPPIAVIPNGVDIPEFD--PGLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 218 LRTLRSNIKLVVVGdpyasrKGEKAeYQKKVLDAAKEIGTDCI-MAGGQSPDQMHNFYHIADLVIVPSqVEEAFCMVAVE 296
Cdd:cd03821 229 LAEQGRDWHLVIAG------PDDGA-YPAFLQLQSSLGLGDRVtFTGPLYGEAKWALYASADLFVLPS-YSENFGNVVAE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 297 AMAAGKAVLASKKGGISEFVLDGItGYhLAEPmSSDSIINDINRALADKERHQI----AEKAKSLVfSKYSWENVAQRFE 372
Cdd:cd03821 301 ALACGLPVVITDKCGLSELVEAGC-GV-VVDP-NVSSLAEALAEALRDPADRKRlgemARRARQVE-ENFSWEAVAGQLG 376
|
.
gi 132488 373 E 373
Cdd:cd03821 377 E 377
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
79-364 |
1.89e-21 |
|
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: 94.35 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 79 LDPLPYSQRILNIRDKVTtqedsVIVIHNSMKLYRQIRERNPNAKLVMHMHNafepelpdndaKIIVPSQFLKAFYEERL 158
Cdd:cd03811 91 LGFATYIVAKLAAARSKV-----IAWIHSSLSKLYYLKKKLLLKLKLYKKAD-----------KIVCVSKGIKEDLIRLG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 159 PAAA--VSIVPNGFCAETYKRNPQDNLrqqLNIAEDATVLLYAGRISPDKGILLLLQAFKQLRTLRSNIKLVVVGDpyAS 236
Cdd:cd03811 155 PSPPekIEVIYNPIDIDRIRALAKEPI---LNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGD--GP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 237 RKGEKAEYQKKvLDAAKEIgtdcIMAGGQSpdqmhN-FYHI--ADLVIVPSqVEEAFCMVAVEAMAAGKAVLASKKGGIS 313
Cdd:cd03811 230 LREELEKLAKE-LGLAERV----IFLGFQS-----NpYPYLkkADLFVLSS-RYEGFPNVLLEAMALGTPVVSTDCPGPR 298
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 132488 314 EFVLDGITGYhLAEPMSSD---SIINDINRALADKERHQIAEKAKSLVFSKYSW 364
Cdd:cd03811 299 EILDDGENGL-LVPDGDAAalaGILAALLQKKLDAALRERLAKAQEAVFREYTI 351
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
121-373 |
2.60e-21 |
|
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: 93.84 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 121 NAKLVMHMHNAFEPELPDNDA------------KIIVPSQFLKaFYEERLPAAAVSIVPNgFCAETyKRNPQDNLRQqln 188
Cdd:cd03820 108 KSKLIVWEHNNYEAYNKGLRRlllrrllykradKIVVLTEADK-LKKYKQPNSNVVVIPN-PLSFP-SEEPSTNLKS--- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 189 iaedaTVLLYAGRISPDKGILLLLQAFKQLRTLRSNIKLVVVGDpyasrkGEKAEYQKKVLDAAKeIGTDCIMAGGQSpd 268
Cdd:cd03820 182 -----KRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGD------GPEREELEKLIDKLG-LEDRVKLLGPTK-- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 269 QMHNFYHIADLVIVPSQVeEAFCMVAVEAMAAGKAVLASK-KGGISEFVLDGITGYhLAEPMSSDSIINDINRALADKE- 346
Cdd:cd03820 248 NIAEEYANSSIFVLSSRY-EGFPMVLLEAMAYGLPIISFDcPTGPSEIIEDGENGL-LVPNGDVDALAEALLRLMEDEEl 325
|
250 260
....*....|....*....|....*..
gi 132488 347 RHQIAEKAKSLVfSKYSWENVAQRFEE 373
Cdd:cd03820 326 RKKMGKNARKNA-ERFSIEKIIKQWEE 351
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
143-371 |
5.62e-19 |
|
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.
Pssm-ID: 340851 [Multi-domain] Cd Length: 364 Bit Score: 87.39 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 143 IIVPSQFLKAFYEE--RLPAAAVSIVPNGFCAETYKRNPQDNLRQQLNIAEDATVLLYAGR--ISPDKGILLLLQAFKQL 218
Cdd:cd03825 141 IVAPSRWLADMVRRspLLKGLPVVVIPNGIDTEIFAPVDKAKARKRLGIPQDKKVILFGAEsvTKPRKGFDELIEALKLL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 219 RTLRsNIKLVVVGdpyasrkgekaeyqkkVLDAAKEIGTDCIMAGGQSPD--QMHNFYHIADLVIVPSqVEEAFCMVAVE 296
Cdd:cd03825 221 ATKD-DLLLVVFG----------------KNDPQIVILPFDIISLGYIDDdeQLVDIYSAADLFVHPS-LADNLPNTLLE 282
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 132488 297 AMAAGKAVLASKKGGISEFVLDGITGYhLAEPMSSDSIINDINRALAD-KERHQIAEKAKSLVFSKYSWENVAQRF 371
Cdd:cd03825 283 AMACGTPVVAFDTGGSPEIVQHGVTGY-LVPPGDVQALAEAIEWLLANpKERESLGERARALAENHFDQRVQAQRY 357
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
163-371 |
1.40e-16 |
|
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: 80.09 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 163 VSIVPNGFCAETYKRNPQDNLRQQLNIAEDATVLLYAGRISPDKGILLLLQAFKQLRTlRSNIKLVVVGD-PyasrkgEK 241
Cdd:cd04962 166 IEVIHNFIDEDVFKRKPAGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRR-KIPAKLLLVGDgP------ER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 242 AEYQKKvldaAKEIGT--DCIMAGGQspDQMHNFYHIADLVIVPSQVEeAFCMVAVEAMAAGKAVLASKKGGISEFVLDG 319
Cdd:cd04962 239 VPAEEL----ARELGVedRVLFLGKQ--DDVEELLSIADLFLLPSEKE-SFGLAALEAMACGVPVVSSNAGGIPEVVKHG 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 132488 320 ITGYhLAEPMSSDSIINDINRALADKERHQiaekakslVFSKYSWENVAQRF 371
Cdd:cd04962 312 ETGF-LSDVGDVDAMAKSALSILEDDELYN--------RMGRAARKRAAERF 354
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
4-318 |
9.55e-15 |
|
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: 74.79 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 4 KIIFTVTPIfsipprGAAAVETWIYQVAKRLSIPN---AIACIknAGYPEYNKINDNCDIHYIGFSKVYKRLFQKWTRLD 80
Cdd:cd04951 1 KILYVITGL------GLGGAEKQTVLLADQMFIRGhdvNIVYL--TGEVEVKPLNNNIIIYNLGMDKNPRSLLKALLKLK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 81 plpysqrilNIRDKVTTQedsviVIHNSMK----LYRQIRERNPNAKLVMHMHNAFEP--------ELPD--NDAKIIVP 146
Cdd:cd04951 73 ---------KIISAFKPD-----VVHSHMFhaniFARFLRMLYPIPLLICTAHNKNEGgrirmfiyRLTDflCDITTNVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 147 SQFLKAFYEER-LPAAAVSIVPNGFCAETYKRNP--QDNLRQQLNIAEDATVLLYAGRISPDKGILLLLQAFKQLRTLRS 223
Cdd:cd04951 139 REALDEFIAKKaFSKNKSVPVYNGIDLNKFKKDInvRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 224 NIKLVVVGDpyasrkgekAEYQKKVLDAAKEIG--TDCIMAGgqSPDQMHNFYHIADLVIVPSQvEEAFCMVAVEAMAAG 301
Cdd:cd04951 219 DFKLLIAGD---------GPLRNELERLICNLNlvDRVILLG--QISNISEYYNAADLFVLSSE-WEGFGLVVAEAMACE 286
|
330
....*....|....*..
gi 132488 302 KAVLASKKGGISEFVLD 318
Cdd:cd04951 287 RPVVATDAGGVAEVVGD 303
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
59-358 |
1.98e-14 |
|
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: 73.89 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 59 DIHYIGFSkvYKRLFQKWT-----RLDPLPYSQRILNIRDkvtTQEDSVIVI--HNSMK-LYR-QIRERNPNAKLVMHMH 129
Cdd:cd03792 58 DKPELSEE--DKEIYLEWIeenasRYPLLDGDADVVVIHD---PQPALLPKIkkKRDRKwIWRcHIDISTPLTEPQPRVW 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 130 NAFEPELPDNDAKIIVPSQFLKAFYEERLPAAAVSIVP-NGFCAETYKRNPQDNLRQQLNIAEDATVLLYAGRISPDKGI 208
Cdd:cd03792 133 DFLWNYIEGYDLFVFHPPEFVPPQVPPPKFYIPPSIDPlSGKNKDLSPADIRYYLEKPFVIDPERPYILQVARFDPSKDP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 209 LLLLQAFKQLRTLRSNIKLVVVGDPyASRKGEKAEYQKKVLDAAKEIGTDCIMAGGqSPDQMHNFYHIADLVIVPSQVEE 288
Cdd:cd03792 213 LGVIDAYKLFKRRAEEPQLVICGHG-AVDDPEGSVVYEEVMEYAGDDHDIHVLRLP-PSDQEINALQRAATVVLQLSTRE 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 132488 289 AFCMVAVEAMAAGKAVLASKKGGISEFVLDGITGYhLAEPMSSDSIinDINRALADKE-RHQIAEKAKSLV 358
Cdd:cd03792 291 GFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGF-LVNSVEGAAV--RILRLLTDPElRRKMGLAAREHV 358
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
142-371 |
2.73e-14 |
|
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: 73.39 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 142 KIIVPSQFLKAFYEE---RLPAAAVSIV-PngfCAET--YKRNPQDNLRQQLNIAEDATVLLYAGRISPDKGILLLLQAF 215
Cdd:cd03805 157 QIVVNSNFTAGVFKKtfpSLAKNPPEVLyP---CVDTdsFDSTSEDPDPGDLIAKSNKKFFLSINRFERKKNIALAIEAF 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 216 KQLR---TLRSNIKLVVVGDpYASRKGEKAEYQKKVLDAAKEIGTDCIMAGGQ---SPDQMHNFYHIADLVI-VPSqvEE 288
Cdd:cd03805 234 AKLKqklPEFENVRLVIAGG-YDPRVAENVEYLEELQRLAEELLNVEDQVLFLrsiSDSQKEQLLSSALALLyTPS--NE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 289 AFCMVAVEAMAAGKAVLASKKGGISEFVLDGITGYhLAEPMSSdsiindinrALADKERHQIAEKAKSLVFSKYSWENVA 368
Cdd:cd03805 311 HFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGF-LCEPTPE---------AFAEAMLKLANDPDLADRMGAAGRKRVK 380
|
...
gi 132488 369 QRF 371
Cdd:cd03805 381 EKF 383
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
158-330 |
2.87e-14 |
|
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: 73.09 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 158 LPAAAVSIVPNGFCAETYKRNPQDnlrqqlniaEDatVLLYAGRISPDKGILLLLQAFKqlrtlRSNIKLVVVGdpyasR 237
Cdd:cd03802 145 PPIDYLTVVHNGLDPADYRFQPDP---------ED--YLAFLGRIAPEKGLEDAIRVAR-----RAGLPLKIAG-----K 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 238 KGEKAEYQKKVldaAKEIGTDCIMAGGQSPDQMHNFYHIADLVIVPSQVEEAFCMVAVEAMAAGKAVLASKKGGISEFVL 317
Cdd:cd03802 204 VRDEDYFYYLQ---EPLPGPRIEFIGEVGHDEKQELLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQ 280
|
170
....*....|...
gi 132488 318 DGITGYhLAEPMS 330
Cdd:cd03802 281 HGETGF-LVDSVE 292
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
92-371 |
6.00e-14 |
|
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: 72.42 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 92 RDKVTTQEDSVIVIHNSM-KLYRQIRErnPNAKLVMHMHNAF-EPELPDNDAKIIV------PSQFLKAFYEERL----- 158
Cdd:cd03822 76 PDVVHIQHEFGIFGGKYGlYALGLLLH--LRIPVITTLHTVLdLSDPGKQALKVLFriatlsERVVVMAPISRFLlvrik 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 159 --PAAAVSIVPNGfcAETYKRNPQDNLRQQLNIaEDATVLLYAGRISPDKGILLLLQAFKQLRTLRSNIKLVVVGDPYAS 236
Cdd:cd03822 154 liPAVNIEVIPHG--VPEVPQDPTTALKRLLLP-EGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGELHPS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 237 RKGEKAEYQKKVldAAKEIGTDCIMA---GGQSPDQMHNFYHIADLVIVPSQ-VEEAFCMVAVEAMAAGKAVLASKKGGI 312
Cdd:cd03822 231 LARYEGERYRKA--AIEELGLQDHVDfhnNFLPEEEVPRYISAADVVVLPYLnTEQSSSGTLSYAIACGKPVISTPLRHA 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 132488 313 SEFVLDGitGYHLAEPMSSDSIINDINRAL-ADKERHQIAEKAKSLvfSKY-SWENVAQRF 371
Cdd:cd03822 309 EELLADG--RGVLVPFDDPSAIAEAILRLLeDDERRQAIAERAYAY--ARAmTWESIADRY 365
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
141-345 |
7.40e-14 |
|
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: 72.10 E-value: 7.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 141 AKIIVPSQFLKAFYEER-LPAAAVSIVPNGfcAETYKRNPQDnlrqqlnIAEDATVLLYAGRISPDKGILLLLQAFKQLR 219
Cdd:cd05844 145 ALFVAVSGFIRDRLLARgLPAERIHVHYIG--IDPAKFAPRD-------PAERAPTILFVGRLVEKKGCDVLIEAFRRLA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 220 TLRSNIKLVVVGDpyasrKGEKAEYQkkvlDAAKEIGTdCIMAGGQSPDQMHNFYHIADLVIVPSQV-----EEAFCMVA 294
Cdd:cd05844 216 ARHPTARLVIAGD-----GPLRPALQ----ALAAALGR-VRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdSEGLGIVL 285
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 132488 295 VEAMAAGKAVLASKKGGISEFVLDGITGYhLAEPMSSDSIINDINRALADK 345
Cdd:cd05844 286 LEAAACGVPVVSSRHGGIPEAILDGETGF-LVPEGDVDALADALQALLADR 335
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
197-371 |
9.91e-14 |
|
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: 71.55 E-value: 9.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 197 LYAGRISPDKGILLLLQAFKQLrtlrsNIKLVVVGDpyasrkGEKAEYQKKVLDAAKEIgtdcimAGGQSPDQMHNFYHI 276
Cdd:cd03804 203 LTASRLVPYKRIDLAVEAFNEL-----PKRLVVIGD------GPDLDRLRAMASPNVEF------LGYQPDEVLKELLSK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 277 ADLVIVPSqvEEAFCMVAVEAMAAGKAVLASKKGGISEFVLDGITGYHLAEPmSSDSI---INDINRALADKERHQIAEK 353
Cdd:cd03804 266 ARAFVFAA--EEDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQ-TVESLkaaVEEFEQNFDRFKPQAIRAN 342
|
170
....*....|....*...
gi 132488 354 AKslvfsKYSWENVAQRF 371
Cdd:cd03804 343 AE-----RFSRARFRQEI 355
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
157-373 |
6.38e-13 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 69.57 E-value: 6.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 157 RLPAAAVSIVPNGFCAETYKRNPQDNLRQQLNIaedatvlLYAGRISPDKGILLLLQAFKQLRTLRSNIKLVVVGD-Pya 235
Cdd:cd03796 164 SLDPRIVSVIPNAVDSSDFTPDPSKPDPNKITI-------VVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDgP-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 236 SRKG-----EKAEYQKKVldaakeigtdcIMAGGQSPDQMHNFYHIADLVIVPSQVEeAFCMVAVEAMAAGKAVLASKKG 310
Cdd:cd03796 235 KRIEleemrEKYQLQDRV-----------ELLGAVPHEEVRDVLVQGHIFLNTSLTE-AFCIAIVEAASCGLLVVSTRVG 302
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 311 GISEfVL--DGITgyhLAEPmSSDSIINDINRALADKER-----HQIAEKAKSLvfskYSWENVAQRFEE 373
Cdd:cd03796 303 GIPE-VLppDMIL---LAEP-DPEDIVRKLEEAISILRTgkhdpWSFHNRVKKM----YSWEDVARRTEK 363
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
54-340 |
8.07e-13 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).
Pssm-ID: 340840 [Multi-domain] Cd Length: 357 Bit Score: 68.86 E-value: 8.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 54 INDNCDIHYIGFSKVYkrlfqkwtrldPLPYSQRILNIRDKVTTQEDSVIVIHNSMKLYRQIRERNpNAKLVMHMHN--- 130
Cdd:cd03812 49 EELGGKIFYIPPKKKN-----------IIKYFIKLLKLIKKEKYDIVHVHGSSSNGIILLLAAKAG-VPVRIAHSHNtkd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 131 -----------AFEPELPDNDAKIIVPSQ------FLKAFYEErlpaaaVSIVPNGFCAETYKRNPQ-DNLRQQLNIAED 192
Cdd:cd03812 117 ssiklrkirknVLKKLIERLSTKYLACSEdagewlFGEVENGK------FKVIPNGIDIEKYKFNKEkRRKRRKLLILED 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 193 ATVLLYAGRISPDKGILLLLQAFKQLRTLRSNIKLVVVGDpyasrkGEKaEYQKKVLDAAKEIGTDCIMAGGQSPdqMHN 272
Cdd:cd03812 191 KLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGE------GEL-KEKIKEKVKELGLEDKVIFLGFRND--VSE 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 273 FYHIADLVIVPSQVeEAFCMVAVEAMAAGKAVLASKKGGISEFVLDGITGYHLAEPMS--SDSIINDINR 340
Cdd:cd03812 262 ILSAMDVFLFPSLY-EGLPLVAVEAQASGLPCLLSDTITKECDITNNVEFLPLNETPStwAEKILKLIKR 330
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
183-373 |
9.68e-13 |
|
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: 69.13 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 183 LRQQLNIAEDATVLLYA--GRISPDKGILLLLQAFKQLrtLRSNIKLVVVG--DPY----ASRKGEKAEYQKKVLdaake 254
Cdd:cd03791 282 LQKELGLPVDPDAPLFGfvGRLTEQKGVDLILDALPEL--LEEGGQLVVLGsgDPEyeqaFRELAERYPGKVAVV----- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 255 IGTD-----CIMAGgqspdqmhnfyhiADLVIVPSqveeAF--C-MVAVEAMAAGKAVLASKKGGISEFVLDGI------ 320
Cdd:cd03791 355 IGFDealahRIYAG-------------ADFFLMPS----RFepCgLVQMYAMRYGTLPIVRRTGGLADTVFDYDpetgeg 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 132488 321 TGYHLaEPMSSDSIINDINRALA---DKE-RHQIAEKAKSLVFskySWENVAQRFEE 373
Cdd:cd03791 418 TGFVF-EDYDAEALLAALRRALAlyrNPElWRKLQKNAMKQDF---SWDKSAKEYLE 470
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
23-355 |
1.64e-11 |
|
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: 64.99 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 23 VETWIYQVAKRLS---IPNAIACI-KNAGYPEYNKIND-------NCDIHYIGFS-KVYKRLFQKWTRLD------PLPY 84
Cdd:cd03795 16 IEQVIYDLAEGLKkkgIEVDVLCFsKEKETPEKEENGIrihrvksFLNVASTPFSpSYIKRFKKLAKEYDiihyhfPNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 85 ---SQRILNIRDKVTTQEDSVIVIHNS-MKLYRqirernPnakLVMHMHNafepelpdnDAKIIVP--------SQFLKA 152
Cdd:cd03795 96 adlLLFFSGAKKPVVVHWHSDIVKQKKlLKLYK------P---LMTRFLR---------RADRIIAtspnyvetSPTLRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 153 FYEErlpaaaVSIVPNGFCAETYKRNPQDNLRQQLNIAEDATVLlYAGRISPDKGILLLLQAFKQLrtlrsNIKLVVVGD 232
Cdd:cd03795 158 FKNK------VRVIPLGIDKNVYNIPRVDFENIKREKKGKKIFL-FIGRLVYYKGLDYLIEAAQYL-----NYPIVIGGE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 233 -PyasrkgEKAEYQKKvldaAKEIGTDCI-MAGGQSPDQMHNFYHIADLVIVPSQVE-EAFCMVAVEAMAAGKAVLASKK 309
Cdd:cd03795 226 gP------LKPDLEAQ----IELNLLDNVkFLGRVDDEEKVIYLHLCDVFVFPSVLRsEAFGIVLLEAMMCGKPVISTNI 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 132488 310 GGISEFV-LDGITGYhLAEPMSSDSIINDINRALAD-KERHQIAEKAK 355
Cdd:cd03795 296 GTGVPYVnNNGETGL-VVPPKDPDALAEAIDKLLSDeELRESYGENAK 342
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
154-362 |
9.14e-11 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340841 [Multi-domain] Cd Length: 474 Bit Score: 63.12 E-value: 9.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 154 YEERL--PAAAVSIVPNGFCAETYK--RNPQDNlrqqlniaEDATVLLYAGRISPDKGILLLLQAFKQLRTLRSNIKLVV 229
Cdd:cd03813 258 RQIRLgaDPDKTRVIPNGIDIQRFApaREERPE--------KEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 230 VGDPYasrkgEKAEYQKKVLDAAKEIGTD--CIMAGgqsPDQMHNFYHIADLVIVPSqVEEAFCMVAVEAMAAGKAVLAS 307
Cdd:cd03813 330 IGPED-----EDPEYAQECKRLVASLGLEnkVKFLG---FQNIKEYYPKLGLLVLTS-ISEGQPLVILEAMASGVPVVAT 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 132488 308 KKGGISEFVLDGITGYHLA----EPMSSDSIINDINRALADKERHQIAEKAKSLVFSKY 362
Cdd:cd03813 401 DVGSCRELIYGADDALGQAglvvPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKY 459
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
196-378 |
1.23e-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: 61.93 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 196 LLYAGRISPDKGILLLLQAFKQLRTLRSNIKLvvvgDPYasrkGEKAEYQK-KVLDAAKEIGTDCIMAGGQS-PDQMhnf 273
Cdd:cd04949 163 IITISRLAPEKQLDHLIEAVAKAVKKVPEITL----DIY----GYGEEREKlKKLIEELHLEDNVFLKGYHSnLDQE--- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 274 YHIADLVIVPSQVeEAFCMVAVEAMAAGKAVLASK-KGGISEFVLDGITGYhLAEpmssdsiINDINrALADKERHQIAE 352
Cdd:cd04949 232 YQDAYLSLLTSQM-EGFGLTLMEAIGHGLPVVSYDvKYGPSELIEDGENGY-LIE-------KNNID-ALADKIIELLND 301
|
170 180
....*....|....*....|....*...
gi 132488 353 KAKSLVFSKYSWENvAQRF--EEQMKNW 378
Cdd:cd04949 302 PEKLQQFSEESYKI-AEKYstENVMEKW 328
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
183-373 |
4.30e-08 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 54.71 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 183 LRQQLNIAEDATVLLYA--GRISPDKGILLLLQAFKQLrtLRSNIKLVVVGDpyasrkGEKaEYQKKVLDAAKE------ 254
Cdd:COG0297 283 LQEELGLPVDPDAPLIGmvSRLTEQKGLDLLLEALDEL--LEEDVQLVVLGS------GDP-EYEEAFRELAARypgrva 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 255 --IGTD-----CIMAGgqspdqmhnfyhiADLVIVPSQVEEafC----MVaveAMAAGkAV-LASKKGGISEFVLD---- 318
Cdd:COG0297 354 vyIGYDealahRIYAG-------------ADFFLMPSRFEP--CglnqMY---ALRYG-TVpIVRRTGGLADTVIDynea 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 132488 319 --GITGYHLAEPmSSDSIINDINRALA---DKER-HQIAEKAKSlvfSKYSWENVAQRFEE 373
Cdd:COG0297 415 tgEGTGFVFDEY-TAEALLAAIRRALAlyrDPEAwRKLQRNAMK---QDFSWEKSAKEYLE 471
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
144-365 |
2.35e-07 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 52.41 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 144 IVPSQFLKafyeERLPAAAVSIVPN------GFCAETYkrNPQ---DNLRQQLNIAE-DATVLLYAGRISPDKGILLLLQ 213
Cdd:PLN02871 210 LVTSPALG----KELEAAGVTAANRirvwnkGVDSESF--HPRfrsEEMRARLSGGEpEKPLIVYVGRLGAEKNLDFLKR 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 214 AFKQLrtlrSNIKLVVVGD-PYasrkgeKAEYQKKVLdaakeiGTDCIMAGGQSPDQMHNFYHIADLVIVPSQvEEAFCM 292
Cdd:PLN02871 284 VMERL----PGARLAFVGDgPY------REELEKMFA------GTPTVFTGMLQGDELSQAYASGDVFVMPSE-SETLGF 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 132488 293 VAVEAMAAGKAVLASKKGGISEFV---LDGITGYhLAEPMSSDSIINDINRALADKE-RHQIAEKAKSLVfSKYSWE 365
Cdd:PLN02871 347 VVLEAMASGVPVVAARAGGIPDIIppdQEGKTGF-LYTPGDVDDCVEKLETLLADPElRERMGAAAREEV-EKWDWR 421
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
155-232 |
1.87e-06 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 49.59 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 155 EERLPAAAVSIVPNGFCAETYKRNPQDN---LRQQLNIAEDATVLLYAGRISPDKGILLLLQAFKQLRTlRSNIKLVVVG 231
Cdd:PRK10307 188 EKGVAAEKVIFFPNWSEVARFQPVADADvdaLRAQLGLPDGKKIVLYSGNIGEKQGLELVIDAARRLRD-RPDLIFVICG 266
|
.
gi 132488 232 D 232
Cdd:PRK10307 267 Q 267
|
|
| COG4641 |
COG4641 |
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]; |
62-377 |
2.07e-06 |
|
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443679 [Multi-domain] Cd Length: 303 Bit Score: 48.77 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 62 YIGFSKVYKRLFQKWTRLDPLPYSQRILNIRDKVTTQEDSVIVIHNSMKLYRQIRERNpnAKLVMH------MHNAFEPE 135
Cdd:COG4641 12 YRGLLRALAALGHEVTFLEPDDPWHDPLYAAELLDAFRPDLVLVISGVELVAALRARG--IPTVFWdtddpvTLDRFREL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 136 LPDNDAkIIVPSQFLKAFYEeRLPAAAVSIVPNGFCAETYKRNPQDnlrqqlniAEDATVLLYAGRISPDKGILL--LLQ 213
Cdd:COG4641 90 LPLYDL-VFTFDGDCVEEYR-ALGARRVFYLPFAADPELHRPVPPE--------ARFRYDVAFVGNYYPDRRARLeeLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 214 AFKQLRtlrsniklVVVGDPYasrkgekaeYQKKVLDAAKEIGtdcimaGGQSPDQMHNFYHIADLVI-VPSQVEEAFcM 292
Cdd:COG4641 160 APAGLR--------LKIYGPG---------WPKLALPANVRRG------GHLPGEEHPAAYASSKITLnVNRMAASPD-S 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 293 VAV---EAMAAGKAVLASKKGGISEFVLDGiTGYHLAEpmSSDSIINDINRALADK-ERHQIAEKAKSLVFSKYSWENVA 368
Cdd:COG4641 216 PTRrtfEAAACGAFLLSDPWEGLEELFEPG-EEVLVFR--DGEELAEKLRYLLADPeERRAIAEAGRRRVLAEHTYAHRA 292
|
....*....
gi 132488 369 QRFEEQMKN 377
Cdd:COG4641 293 RELLAILEE 301
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
196-327 |
1.33e-05 |
|
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: 46.67 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 196 LLYAGRISPDKGILLLLQAFKQLRTLRSNIKLVVVGDpyasrkGEKAEyQKKVLDAAKEIGTDCIMAGGQSPDQMHNFYH 275
Cdd:cd03799 177 ILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGD------GDLKE-QLQQLIQELNIGDCVKLLGWKPQEEIIEILD 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 132488 276 IADLVIVPSQV-----EEAFCMVAVEAMAAGKAVLASKKGGISEFVLDGITGYHLAE 327
Cdd:cd03799 250 EADIFIAPSVTaadgdQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPE 306
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
195-363 |
2.75e-05 |
|
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: 45.68 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 195 VLLYAGRISPDKGILLLLQAFKQLRT-----LRSNIKLVVVG-----DPYASRKGEKAEYQKKVLDAAKEIGTDCimagg 264
Cdd:cd03806 239 QILSIAQFRPEKNHPLQLRAFAELLKrlpesIRSNPKLVLIGscrneEDKERVEALKLLAKELILEDSVEFVVDA----- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 265 qSPDQMHNFYHIAdLVIVPSQVEEAFCMVAVEAMAAGKAVLASKKGG----ISEFVLDGITGYHLAEPmssDSIINDINR 340
Cdd:cd03806 314 -PYEELKELLSTA-SIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGplldIVVPWDGGPTGFLASTP---EEYAEAIEK 388
|
170 180
....*....|....*....|....*
gi 132488 341 ALA--DKERHQIAEKAKSlVFSKYS 363
Cdd:cd03806 389 ILTlsEEERLQRREAARS-SAERFS 412
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
206-370 |
3.00e-05 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 46.13 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 206 KGILLLLQAFKQLRTLRSNIKLVVVG---DPYASRKGEKAEYQKKVLDAAKEIGTDcimagGQ------SPDQMHN---F 273
Cdd:PLN00142 586 KNLTGLVEWYGKNKRLRELVNLVVVGgfiDPSKSKDREEIAEIKKMHSLIEKYNLK-----GQfrwiaaQTNRVRNgelY 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 274 YHIADL--VIVPSQVEEAFCMVAVEAMAAGKAVLASKKGGISEFVLDGITGYHLaEPM----SSDSIINDINRALADKER 347
Cdd:PLN00142 661 RYIADTkgAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHI-DPYhgdeAANKIADFFEKCKEDPSY 739
|
170 180
....*....|....*....|....
gi 132488 348 -HQIAEKAKSLVFSKYSWENVAQR 370
Cdd:PLN00142 740 wNKISDAGLQRIYECYTWKIYAER 763
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
296-373 |
4.46e-05 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 41.82 E-value: 4.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 132488 296 EAMAAGKAVLASKKGGISEFVLDGITGYhLAEpmSSDSIINDINRALAD-KERHQIAEKAKSLVFSKYSWENVAQRFEE 373
Cdd:pfam13524 18 EAAACGAPLLTDRTPGLEELFEPGEEIL-LYR--DPEELAEKIRYLLEHpEERRAIAAAGRERVLAEHTYAHRAEQLLD 93
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
102-371 |
1.13e-04 |
|
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: 43.89 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 102 VIVIHNSMKLYRQIRERNPNAKLV------MHMHNA---FEPELP---DNDAKI-----------------IVPSQFLKa 152
Cdd:cd03818 92 VVVGHPGWGEALFVKDVFPDVPLIgyceyyYRAEGAdvgFDPEFPldlMIRCRLrnrnialllsleqadlgVTPTRWQR- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 153 fyeERLPAAA---VSIVPNGFCAETYKRNPQDNLRQqLNIAE---DATVLLYAGR-ISPDKGILLLLQAFKQLRTLRSNI 225
Cdd:cd03818 171 ---SLFPAAYrdrISVIHDGVDTDRLAPDPAARLRL-LNGTElkaGDPVITYVARnLEPYRGFHVFMRALPRIQARRPDA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 226 KLVVVGD---PYASRKGEKAEYQKKVLDaakEIGTD---CIMAGGQSPDQMHNFYHIADLVIVPSqveeaFCMVA----V 295
Cdd:cd03818 247 RVVVVGGdgvSYGSPPPDGGSWKQKMLA---ELGVDlerVHFVGKVPYDQYVRLLQLSDAHVYLT-----YPFVLswslL 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 132488 296 EAMAAGKAVLASKKGGISEFVLDGITGYhLAEPMSSDSIINDINRALAD-KERHQIAEKAKSLVFSKYSWENVAQRF 371
Cdd:cd03818 319 EAMACGCPVIGSDTAPVREVIRDGRNGL-LVDFFDPDALAAAVLELLEDpDRAAALRRAARRTVERSDSLDVCLARY 394
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
161-373 |
3.40e-04 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 42.40 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 161 AAVSIVPNGFCAETYKRNPQDN--LRQQLNIAEDATVLLYA--GRISPDKGILLLLQAFKQLrtLRSNIKLVVVGDpyas 236
Cdd:PRK14099 259 ATDELIAATYDVETLAARAANKaaLQARFGLDPDPDALLLGviSRLSWQKGLDLLLEALPTL--LGEGAQLALLGS---- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 237 rkGEkAEYQKKVLDAAK--------EIGTDCIMAggqspdqmHNFYHIADLVIVPSQVEEafC-MVAVEAMAAGKAVLAS 307
Cdd:PRK14099 333 --GD-AELEARFRAAAQaypgqigvVIGYDEALA--------HLIQAGADALLVPSRFEP--CgLTQLCALRYGAVPVVA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 308 KKGGISEFVLD--------GI-TGYHLAePMSSDSIINDINRA---LADKE---RHQIAEKAkslvfSKYSWENVAQRFE 372
Cdd:PRK14099 400 RVGGLADTVVDanemaiatGVaTGVQFS-PVTADALAAALRKTaalFADPVawrRLQRNGMT-----TDVSWRNPAQHYA 473
|
.
gi 132488 373 E 373
Cdd:PRK14099 474 A 474
|
|
| GT20_TPS |
cd03788 |
trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a ... |
181-350 |
1.95e-03 |
|
trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a glycosyltransferase that catalyses the synthesis of alpha,alpha-1,1-trehalose-6-phosphate from glucose-6-phosphate using a UDP-glucose donor. It is a key enzyme in the trehalose synthesis pathway. Trehalose is a nonreducing disaccharide present in a wide variety of organisms and may serve as a source of energy and carbon. It is characterized most notably in insect, plant, and microbial cells. Its production is often associated with a variety of stress conditions, including desiccation, dehydration, heat, cold, and oxidation. This family represents the catalytic domain of the TPS. Some members of this domain family coexist with a C-terminal trehalose phosphatase domain.
Pssm-ID: 340820 [Multi-domain] Cd Length: 463 Bit Score: 40.26 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 181 DNLRQQLNiaeDATVLLYAGRISPDKGILLLLQAFKQL----RTLRSNIKLVVVGDPYASRKGEKAEYQKKVLDAAKEI- 255
Cdd:cd03788 258 RELRERYK---GKKLIVGVDRLDYTKGIPEKLLAFERFleryPEWRGKVVLVQVAVPSRTDVEEYQELRREVEELVGRIn 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 256 ---GTD-----CIMAGGQSPDQMHNFYHIADLVIVPSqVEEAFCMVAVEAMAA---GKAVLAskkggISEFvldgiTGyh 324
Cdd:cd03788 335 grfGTLdwtpvVYLHQSLDREELLALYRAADVALVTS-LRDGMNLVAKEYVACqrdNPGVLI-----LSEF-----AG-- 401
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 132488 325 lAEPMSSDSII---ND-------INRALAD-----KERHQI 350
Cdd:cd03788 402 -AASELDGAILvnpWDieevaeaINRALTMspeerKERHQK 441
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
201-343 |
2.29e-03 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 40.02 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132488 201 RISPDKGILLLLQAFKQLRTLRSNIKLVVVGDpyasrkgekAEYQKKVLDAAKEIG-TDCIMAGGQSpDQMHNFYHIADL 279
Cdd:PRK15179 525 RVDDNKRPFLWVEAAQRFAASHPKVRFIMVGG---------GPLLESVREFAQRLGmGERILFTGLS-RRVGYWLTQFNA 594
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 132488 280 VIVPSQVEeAFCMVAVEAMAAGKAVLASKKGGISEFVLDGITGYHLAepmSSDSIINDINRALA 343
Cdd:PRK15179 595 FLLLSRFE-GLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLP---ADTVTAPDVAEALA 654
|
|
| |
