|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
4-358 |
1.08e-54 |
|
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: 183.89 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 4 ILFTESSSDIGGQELQALAQMTALQKQGHSVLLACREKSKIAPEARKRGHDVTFIP--FRNSLHLPSILRLRRIIGEFKP 81
Cdd:cd03801 4 LLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPslAALLRARRLLRELRPLLRLRKF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 82 DLVICHSGHDSNIAGLSRLIC-------CHRFSIVRQKTYITRKTR----TFSLNYLCDFIVVPSSAMMAHLMAEGV--R 148
Cdd:cd03801 84 DVVHAHGLLAALLAALLALLLgaplvvtLHGAEPGRLLLLLAAERRllarAEALLRRADAVIAVSEALRDELRALGGipP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 149 TPVTVIPPGFDWPALHNEAMRPLPLHihawaasaDNVPLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWLVVGAGREe 228
Cdd:cd03801 164 EKIVVIPNGVDLERFSPPLRRKLGIP--------PDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGP- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 229 YEARLRQQTEHLGmsGDVLMAGALFPA--LPVYRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTG 306
Cdd:cd03801 235 LRAELEELELGLG--DRVRFLGFVPDEelPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGG 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446898486 307 TLLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIECRFDINRTAQIIVSL 358
Cdd:cd03801 313 LVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDL 364
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
3-349 |
1.65e-51 |
|
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: 174.85 E-value: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 3 KILFTESSSDIGGQELQALAQMTALQKQGHSVLLACREKSKIAPEARKRGHDVTFIPFRNSLH-----LPSILRLRRIIG 77
Cdd:cd03811 1 KILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLiklglLKAILKLKRILK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 78 EFKPDLVICHSGHDSNIAGL-----SRLICCHRFSIVRQKTYITRKTRTFSLNYLCDFIVVPSSAMMAHLMAEGVRTP-- 150
Cdd:cd03811 81 RAKPDVVISFLGFATYIVAKlaaarSKVIAWIHSSLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSPPek 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 151 VTVIPPGFDWPalhneamRPLPLHIHAWAASADNVPLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWLVVGAGreEYE 230
Cdd:cd03811 161 IEVIYNPIDID-------RIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDG--PLR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 231 ARLRQQTEHLGMSGDVLMAGALFPALPVYRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLP 310
Cdd:cd03811 232 EELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVP 311
|
330 340 350
....*....|....*....|....*....|....*....
gi 446898486 311 VGDVSAWTGALRDFLSRPERFRMMAASAREDIECRFDIN 349
Cdd:cd03811 312 DGDAAALAGILAALLQKKLDAALRERLAKAQEAVFREYT 350
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
4-346 |
8.94e-39 |
|
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: 141.34 E-value: 8.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 4 ILFTESSSDIGGQELQALAQMTALQKQGHSVLLACREKSKiAPEARKRGHDVTFIPFRNSLHLPSILRLRRIIGEFKPDL 83
Cdd:cd03819 1 ILMLTPALEIGGAETYILDLARALAERGHRVLVVTAGGPL-LPRLRQIGIGLPGLKVPLLRALLGNVRLARLIRRERIDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 84 VICHSGhdsnIAGLSRLICCHRFSI--------VRQKTYITRKTRTFSLNYLCDFIVVpsSAMMAHLMAEGVRTP---VT 152
Cdd:cd03819 80 IHAHSR----APAWLGWLASRLTGVplvttvhgSYLATYHPKDFALAVRARGDRVIAV--SELVRDHLIEALGVDperIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 153 VIPPGFDWPALHNEAMRPLPlhihAWAASADNVPLIVQVGMLRPEKGHEFMLRVLYQLKmEGKSFRWLVVGAGREEyeAR 232
Cdd:cd03819 154 VIPNGVDTDRFPPEAEAEER----AQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELK-DEPDFRLLVAGDGPER--DE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 233 LRQQTEHLGMSGDVLMAGALFPALPVYRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLPVG 312
Cdd:cd03819 227 IRRLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPG 306
|
330 340 350
....*....|....*....|....*....|....*
gi 446898486 313 DVSAWTGALRDFLSRPE-RFRMMAASAREDIECRF 346
Cdd:cd03819 307 DAEALADAIRAAKLLPEaREKLQAAAALTEAVREL 341
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
5-345 |
1.14e-38 |
|
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: 141.66 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 5 LFTESSSDIGGQELQALAQMTA-LQKQGHSVLLacrekskIAPEARKR----GHDVTF-----IPFRNS--LHLPSILRL 72
Cdd:cd03814 4 LVTDTYHPQVNGVVRTLERLVDhLRRRGHEVRV-------VAPGPFDEaesaEGRVVSvpsfpLPFYPEyrLALPLPRRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 73 RRIIGEFKPDLVichsgHDSN--IAGLSRLICCHRFSIVRQKTYITR-----KTRTFSL------NYL------CDFIVV 133
Cdd:cd03814 77 RRLIKEFQPDII-----HIATpgPLGLAALRAARRLGLPVVTSYHTDfpeylSYYTLGPlswlawAYLrwfhnpFDTTLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 134 PSSAMMAHLMAEGVRtPVTVIPPGFDW----PALHNEAMRPlplhihAWAASADnvPLIVQVGMLRPEKGHEFMLRVLYQ 209
Cdd:cd03814 152 PSPSIARELEGHGFE-RVRLWPRGVDTelfhPSRRDAALRR------RLGPPGR--PLLLYVGRLAPEKNLEALLDADLP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 210 LKmEGKSFRWLVVGAGREEYEARLRQQTEH-LGMSGDVLMAGALfpalpvyriAS--VVVMPSENEAFGMVLAEASVSGV 286
Cdd:cd03814 223 LA-ASPPVRLVVVGDGPARAELEARGPDVIfTGFLTGEELARAY---------ASadVFVFPSRTETFGLVVLEAMASGL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446898486 287 PVIASETGGIPDVIQKNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIECR 345
Cdd:cd03814 293 PVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERY 351
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
3-358 |
5.50e-36 |
|
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: 134.37 E-value: 5.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 3 KILFTESSSDIGGQELQALAQM-TALQKQGHSVLLACREKSKIAPEARKRGHDVTFIPFRNSLHLPSILRLRRIIGEFKP 81
Cdd:cd03807 1 KVAHVITGLNVGGAETMLLRLLeHMDKSRFEHVVISLTGDGVLGEELLAAGVPVVCLGLSSGKDPGVLLRLAKLIRKRNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 82 DLVICHSGHDSNIAGLSRL--------ICCHRFSIVRQKTYITRKTRTFSLNYLCDFIVVpSSAMMAHLMAEGVR-TPVT 152
Cdd:cd03807 81 DVVHTWMYHADLIGGLAAKlaggvkviWSVRSSNIPQRLTRLVRKLCLLLSKFSPATVAN-SSAVAEFHQEQGYAkNKIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 153 VIPPGFDWPALHNEAMRPLPlhIHAWAASADNVPLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWLVVGagREEYEAR 232
Cdd:cd03807 160 VIYNGIDLFKLSPDDASRAR--ARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVG--RGPERPN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 233 LRQQTEHLGMSGDVLMAG------ALFPALPVYriasvvVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNvTG 306
Cdd:cd03807 236 LERLLLELGLEDRVHLLGersdvpALLPAMDIF------VLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TG 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446898486 307 TLLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIECRFDINRTAQIIVSL 358
Cdd:cd03807 309 FLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETL 360
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
50-350 |
1.02e-33 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340859 [Multi-domain] Cd Length: 370 Bit Score: 128.24 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 50 KRGHDVTFI----PFRNSLHLPSIL-----------------------RLRRIIGEFKPDLVICHSGHDSNIAG-LSRLI 101
Cdd:cd04962 27 ERGHEVHFIssaiPFRLNLYSGNIFfhevevpnyplfeyppytlalasKIVEVAKEHKLDVLHAHYAIPHASCAyLAREI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 102 CCHRFSIVR--QKTYITRKTRTFSLNYLCDFIVVPS---SAMMAHLMAE-----GVRTPVTVIPPGFD---WPALHNEam 168
Cdd:cd04962 107 LGEKIPIVTtlHGTDITLVGYDPSLQPAVRFSINKSdrvTAVSSSLRQEtyelfDVDKDIEVIHNFIDedvFKRKPAG-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 169 rplplHIHAWAASADNVPLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSfRWLVVGAGREEyeARLRQQTEHLGMSGDVLM 248
Cdd:cd04962 185 -----ALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIPA-KLLLVGDGPER--VPAEELARELGVEDRVLF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 249 AGALFPALPVYRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLPVGDVSAWTGALRDFLSRP 328
Cdd:cd04962 257 LGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDD 336
|
330 340
....*....|....*....|..
gi 446898486 329 ERFRMMAASAREDIECRFDINR 350
Cdd:cd04962 337 ELYNRMGRAARKRAAERFDPER 358
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
186-341 |
4.12e-33 |
|
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: 120.84 E-value: 4.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 186 PLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRwLVVgAGREEYEARLRQQTEHLGMSGDVLMAGAL-FPALP-VYRIAS 263
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLK-LVI-AGDGEEEKRLKKLAEKLGLGDNVIFLGFVsDEDLPeLLKIAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446898486 264 VVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAASARED 341
Cdd:pfam00534 81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
3-357 |
4.48e-32 |
|
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: 123.47 E-value: 4.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 3 KILFTeSSSDIGGQELQaLAQMTALQKQGHSVLLACREKSKIapEARKRGHDVTFIPFR------NSLH-LPSILRLRRI 75
Cdd:cd03808 1 KILFI-VNVDGGFQSFR-LPLIKALVKKGYEVHVIAPDGDKL--SDELKELGVKVIDIPilrrgiNPLKdLKALFKLYKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 76 IGEFKPDLVICHS-------GHDSNIAGLSRLIC-CHRFSIVRQKTYITRKTRT----FSLNYLCDFIVVpsSAMMAHLM 143
Cdd:cd03808 77 LKKEKPDIVHCHTpkpgilgRLAARLAGVPKVIYtVHGLGFVFTEGKLLRLLYLllekLALLFTDKVIFV--NEDDRDLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 144 AE--GVRTPVTVIPPGFDWPALHNEAMRPlplhihawaASADNVPLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWLV 221
Cdd:cd03808 155 IKkgIIKKKKTVLIPGSGVDLDRFQYSPE---------SLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 222 VGAGREEYEARlrQQTEHLGMSGDVLMAGALFPALPVYRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQ 301
Cdd:cd03808 226 VGDGELENPSE--ILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVI 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446898486 302 KNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIECRFDInrtaQIIVS 357
Cdd:cd03808 304 DGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDE----EKVVN 355
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
13-355 |
2.90e-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: 121.72 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 13 IGGQELQALAQMTALQKQGHSVLLACREKSKIAPEARKRGHDVTFIPFRN---------------SLHLPSILRLRRIIG 77
Cdd:cd03798 13 SPGRGIFVRRQVRALSRRGVDVEVLAPAPWGPAAARLLRKLLGEAVPPRDgrrllplkprlrllaPLRAPSLAKLLKRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 78 EFKPDLVICHSGHDSNIAGlsrlICCHRFSIVR-------------QKTYITRKTRTFSLNyLCDFIVVPSSAMMAHLMA 144
Cdd:cd03798 93 RGPPDLIHAHFAYPAGFAA----ALLARLYGVPyvvtehgsdinvfPPRSLLRKLLRWALR-RAARVIAVSKALAEELVA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 145 EGV-RTPVTVIPPGFDwPALHNEAMRPLPLhihawaasADNVPLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWLVVG 223
Cdd:cd03798 168 LGVpRDRVDVIPNGVD-PARFQPEDRGLGL--------PLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 224 AGREEyeARLRQQTEHLGMSGDVLMAGAL-FPALP-VYRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQ 301
Cdd:cd03798 239 DGPLR--EALRALAEDLGLGDRVTFTGRLpHEQVPaYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVG 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446898486 302 KNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAAsAREDIECRFDINRTAQII 355
Cdd:cd03798 317 DPETGLLVPPGDADALAAALRRALAEPYLRELGEA-ARARVAERFSWVKAADRI 369
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
3-350 |
3.12e-30 |
|
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: 118.49 E-value: 3.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 3 KILF-TESSSDIGGQELQALAQMTALQKQGHSVLLACREKSKIAP--------EARKRGHDVTFIPFRNSLHLPSILRLR 73
Cdd:cd03820 1 KIAIvIPSISNAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPfyelddniKIKNLGDRKYSHFKLLLKYFKKVRRLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 74 RIIGEFKPDLVICHSGHD-SNIAGL---SRLICCHRFSIVRQKtYITRKTRTFSLNY-LCDFIVVPSSAMMAHLMAEGvR 148
Cdd:cd03820 81 KYLKNNKPDVVISFRTSLlTFLALIglkSKLIVWEHNNYEAYN-KGLRRLLLRRLLYkRADKIVVLTEADKLKKYKQP-N 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 149 TPVTVIPPGFDWPALHNEAmrPLPLHIhawaasadnvplIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWLVVGAGREE 228
Cdd:cd03820 159 SNVVVIPNPLSFPSEEPST--NLKSKR------------ILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 229 yeARLRQQTEHLGMSGDVLMAGALFPALPVYRIASVVVMPSENEAFGMVLAEASVSGVPVIASE-TGGIPDVIQKNVTGT 307
Cdd:cd03820 225 --EELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDcPTGPSEIIEDGENGL 302
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446898486 308 LLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIEcRFDINR 350
Cdd:cd03820 303 LVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAE-RFSIEK 344
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
26-340 |
4.13e-30 |
|
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: 118.54 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 26 ALQKQGHSVLLACreksKIAPEARKRGHDVTFIPFRNSLH--------LPSILRLRRIIGEFKPDLVICHSGHDSNIAGL 97
Cdd:cd03817 26 ALEKRGHEVYVIT----PSDPGAEDEEEVVRYRSFSIPIRkyhrqhipFPFKKAVIDRIKELGPDIIHTHTPFSLGKLGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 98 -----SRLICCH-------------RFSIVRQKTYITRKTRTFsLNYlCDFIVVPSSAMMAHLMAEGVRTPVTVIPPGFD 159
Cdd:cd03817 102 riarkLKIPIVHtyhtmyedylhyiPKGKLLVKAVVRKLVRRF-YNH-TDAVIAPSEKIKDTLREYGVKGPIEVIPNGID 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 160 ---WPALHNEAMR-PLPLhihawaasADNVPLIVQVGMLRPEKGHEFMLRVLYQLKMEgKSFRWLVVGAGreEYEARLRQ 235
Cdd:cd03817 180 ldkFEKPLNTEERrKLGL--------PPDEPILLYVGRLAKEKNIDFLLRAFAELKKE-PNIKLVIVGDG--PEREELKE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 236 QTEHLGMSGDVLMAGALFPA-LP-VYRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLPVGD 313
Cdd:cd03817 249 LARELGLADKVIFTGFVPREeLPeYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPND 328
|
330 340
....*....|....*....|....*..
gi 446898486 314 VsAWTGALRDFLSRPERFRMMAASARE 340
Cdd:cd03817 329 E-TLAEKLLHLRENLELLRKLSKNAEI 354
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
128-353 |
5.72e-28 |
|
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: 113.10 E-value: 5.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 128 CDFIVVPSSAMMAHLMA--EGVRTPVTVIPPGFDW-----PALHNEAMRPLPLHIHAwaasadnvPLIVQVGMLRPEKGH 200
Cdd:cd03800 164 ADRVIASTPQEADELISlyGADPSRINVVPPGVDLerffpVDRAEARRARLLLPPDK--------PVVLALGRLDPRKGI 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 201 EFMLRVLYQLKMEGKSFRWLVVGAGREEYEAR----LRQQTEHLGMSGDVLMAGALFPA--LPVYRIASVVVMPSENEAF 274
Cdd:cd03800 236 DTLVRAFAQLPELRELANLVLVGGPSDDPLSMdreeLAELAEELGLIDRVRFPGRVSRDdlPELYRAADVFVVPSLYEPF 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446898486 275 GMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIECRFDINRTAQ 353
Cdd:cd03800 316 GLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVAD 394
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
186-326 |
3.79e-27 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 104.52 E-value: 3.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 186 PLIVQVG-MLRPEKGHEFMLRVLYQLKMEGKSFRWLVVGAG-REEYEARLRqqtehlGMSGDVLMAGALFPALPVYRIAS 263
Cdd:pfam13692 2 PVILFVGrLHPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGpEEELEELAA------GLEDRVIFTGFVEDLAELLAAAD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446898486 264 VVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQkNVTGTLLPVGDVSAWTGALRDFLS 326
Cdd:pfam13692 76 VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVD-GENGLLVPPGDPEALAEAILRLLE 137
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
259-358 |
3.90e-25 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 98.52 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 259 YRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAASA 338
Cdd:COG0438 18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEAA 97
|
90 100
....*....|....*....|
gi 446898486 339 REDIECRFDINRTAQIIVSL 358
Cdd:COG0438 98 RERAEERFSWEAIAERLLAL 117
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
44-309 |
7.00e-25 |
|
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: 101.33 E-value: 7.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 44 IAPEARKRGHDVTFIpfrnSLHLPSILRLRRIIGEFKPDLVICHSGHDSNIAGLSRLIcchrfsivrqktyitrktrtfs 123
Cdd:cd01635 22 LARALAALGHEVTVL----ALLLLALRRILKKLLELKPDVVHAHSPHAAALAALLAAR---------------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 124 lnylcdfivvpssammahlmAEGVRTPVTVIPPGFDWPALHNEAMRPLPLHIHAWAAsadnvplIVQVGMLRPEKGHEFM 203
Cdd:cd01635 76 --------------------LLGIPIVVTVHGPDSLESTRSELLALARLLVSLPLAD-------KVSVGRLVPEKGIDLL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 204 LRVLYQLKMEGKSFRWLVVGAGREEYEARLRQQTEHLGMSGDVLMAGALFPALP-VYRIASVVVMPSENEAFGMVLAEAS 282
Cdd:cd01635 129 LEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLElLLAAADVFVLPSRSEGFGLVLLEAM 208
|
250 260
....*....|....*....|....*..
gi 446898486 283 VSGVPVIASETGGIPDVIQKNVTGTLL 309
Cdd:cd01635 209 AAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
3-340 |
5.78e-24 |
|
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: 101.25 E-value: 5.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 3 KILFTESS---SDIGGQELQALAQMTALQKQGHSV--LLACREKSKIAPEARK-----------RGHDVTFIPFRNSL-H 65
Cdd:cd03823 1 KILLVNSLyppQRVGGAEISVHDLAEALVAEGHEVavLTAGVGPPGQATVARSvvryrrapdetLPLALKRRGYELFEtY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 66 LPSILR-LRRIIGEFKPDLVICHsghdsNIAGLS---------RLI-----------CCHRFSIVRQKTyitrktrtfsl 124
Cdd:cd03823 81 NPGLRRlLARLLEDFRPDVVHTH-----NLSGLGaslldaardLGIpvvhtlhdywlLCPRQFLFKKGG----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 125 nylcDFIVVPSSAMMAHLMAEGVRTP-VTVIPPGFDWPalhneamrpLPLHIHAWAASADNVplIVQVGMLRPEKGHEFM 203
Cdd:cd03823 145 ----DAVLAPSRFTANLHEANGLFSArISVIPNAVEPD---------LAPPPRRRPGTERLR--FGYIGRLTEEKGIDLL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 204 LRVLYQLKMEGKSFRwlVVGAGREEYEARL---RQQTEHlgmsGDVLMAgalfPALPVYRIASVVVMPSE-NEAFGMVLA 279
Cdd:cd03823 210 VEAFKRLPREDIELV--IAGHGPLSDERQIeggRRIAFL----GRVPTD----DIKDFYEKIDVLVVPSIwPEPFGLVVR 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446898486 280 EASVSGVPVIASETGGIPDVIQKNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAASARE 340
Cdd:cd03823 280 EAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEP 340
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
59-343 |
2.96e-23 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 100.56 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 59 PFRNSLHLpSILRLRRIIGE---FKPDLVICHSGHDSNIAGL--SRLICchrFSIVRQ-----KTYITRKTRTFSLNYLC 128
Cdd:PLN02871 121 PFYQKVPL-SLALSPRIISEvarFKPDLIHASSPGIMVFGALfyAKLLC---VPLVMSyhthvPVYIPRYTFSWLVKPMW 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 129 DFI----------VVPSSAMMAHLMAEGVRTP--VTVIPPGFDWPALH----NEAMRplplhiHAWAASADNVPLIVQVG 192
Cdd:PLN02871 197 DIIrflhraadltLVTSPALGKELEAAGVTAAnrIRVWNKGVDSESFHprfrSEEMR------ARLSGGEPEKPLIVYVG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 193 MLRPEKGHEFMLRVLYQLKmegkSFRWLVVGAG--REEYEARLR-QQTEHLGM-SGDVLMAGalfpalpvYRIASVVVMP 268
Cdd:PLN02871 271 RLGAEKNLDFLKRVMERLP----GARLAFVGDGpyREELEKMFAgTPTVFTGMlQGDELSQA--------YASGDVFVMP 338
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446898486 269 SENEAFGMVLAEASVSGVPVIASETGGIPDVI---QKNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIE 343
Cdd:PLN02871 339 SESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVE 416
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
129-353 |
5.14e-22 |
|
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.
Pssm-ID: 340848 [Multi-domain] Cd Length: 377 Bit Score: 95.90 E-value: 5.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 129 DFIVVPSSAMMAHLMAEGVRTPVTVIPPGFDWPALHNEAMRPlplhihAWAASADNVPLIVQVGMLRPEKGHEFMLRVLY 208
Cdd:cd03821 154 ALVHFTSEQEADELRRFGLEPPIAVIPNGVDIPEFDPGLRDR------RKHNGLEDRRIILFLGRIHPKKGLDLLIRAAR 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 209 QLKMEGKSFRWLVVGAGREEYEARLRQQTEhLGMSGDVLMAGALFP-ALPV-YRIASVVVMPSENEAFGMVLAEASVSGV 286
Cdd:cd03821 228 KLAEQGRDWHLVIAGPDDGAYPAFLQLQSS-LGLGDRVTFTGPLYGeAKWAlYASADLFVLPSYSENFGNVVAEALACGL 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446898486 287 PVIASETGGIPDVIQKNVTGTLLPvgDVSAWTGALRDFLSRPERFRMMAASARE--DIECRFDINRTAQ 353
Cdd:cd03821 307 PVVITDKCGLSELVEAGCGVVVDP--NVSSLAEALAEALRDPADRKRLGEMARRarQVEENFSWEAVAG 373
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
3-349 |
8.64e-19 |
|
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: 86.57 E-value: 8.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 3 KILFTESSSDIGGQELQALAQMTALQKQGHSVLLACREKSKIA--PEARKRGHDVTFIPFRNSLHLPSILRLRRIIGEFK 80
Cdd:cd03812 1 KILHIVGGMNVGGIETFLMNLYRKLDKSKIEFDFLATSDDKGEydEELEELGGKIFYIPPKKKNIIKYFIKLLKLIKKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 81 PDLVICHSGHDSNI-------AGLSRLICcHRFSIVRQKTYItRKTRTFSL----NYLCDFIVVPSSAMMAHLMAEGVRT 149
Cdd:cd03812 81 YDIVHVHGSSSNGIilllaakAGVPVRIA-HSHNTKDSSIKL-RKIRKNVLkkliERLSTKYLACSEDAGEWLFGEVENG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 150 PVTVIPPGFDWPAL-HNEAMRP--LPLHIhawaasADNVPLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWLVVGAGR 226
Cdd:cd03812 159 KFKVIPNGIDIEKYkFNKEKRRkrRKLLI------LEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 227 EEYEarLRQQTEHLGMSGDVLMAGALFPALPVYRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTG 306
Cdd:cd03812 233 LKEK--IKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITNNVEF 310
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446898486 307 TLLPVGdVSAWTGALRDFLSRPERFRmmaaSAREDIECRFDIN 349
Cdd:cd03812 311 LPLNET-PSTWAEKILKLIKRKRRIN----KEINKEKKELGYD 348
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
12-350 |
1.55e-18 |
|
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: 85.79 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 12 DIGGQE--LQALAQmtALQKQGHSVLLACREKSKIAPEARKRGHDV-----TFIPFRNSLHLPSILRLRRIIGEfkPDLV 84
Cdd:cd03795 12 DIGGIEqvIYDLAE--GLKKKGIEVDVLCFSKEKETPEKEENGIRIhrvksFLNVASTPFSPSYIKRFKKLAKE--YDII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 85 ICHsgHDSNIAGLSRLIC-------CHRFS-IVRQKtYITRKTRTFSLNYL--CDFIVVPSSAMMAH---LmaEGVRTPV 151
Cdd:cd03795 88 HYH--FPNPLADLLLFFSgakkpvvVHWHSdIVKQK-KLLKLYKPLMTRFLrrADRIIATSPNYVETsptL--REFKNKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 152 TVIPPGFDwpalHNEAMRPLPLHIHAWAaSADNVPLIVQVGMLRPEKGHEFMLRVlyqlkMEGKSFRWLVVGAGREEyeA 231
Cdd:cd03795 163 RVIPLGID----KNVYNIPRVDFENIKR-EKKGKKIFLFIGRLVYYKGLDYLIEA-----AQYLNYPIVIGGEGPLK--P 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 232 RLRQQTEhLGMSGDVLMAGALFPA-LPVYRIAS-VVVMPS--ENEAFGMVLAEASVSGVPVIASETG-GIPDVIQKNVTG 306
Cdd:cd03795 231 DLEAQIE-LNLLDNVKFLGRVDDEeKVIYLHLCdVFVFPSvlRSEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETG 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446898486 307 TLLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIECRFDINR 350
Cdd:cd03795 310 LVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEK 353
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
108-358 |
2.05e-18 |
|
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: 85.46 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 108 IVRQKTYITRKTRtfslnylcdFIVVPSSAMMAHlMAEGV----RTPVTVIPPGFD---WPALHNEAMRPlplhihAWAA 180
Cdd:cd03825 126 LFRRKREALAKKR---------LTIVAPSRWLAD-MVRRSpllkGLPVVVIPNGIDteiFAPVDKAKARK------RLGI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 181 SAD-NVPLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFrwLVVGAGREEYEARLRQQTEHLG-MSGDVLMAgalfpalPV 258
Cdd:cd03825 190 PQDkKVILFGAESVTKPRKGFDELIEALKLLATKDDLL--LVVFGKNDPQIVILPFDIISLGyIDDDEQLV-------DI 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 259 YRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAASA 338
Cdd:cd03825 261 YSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERA 340
|
250 260
....*....|....*....|
gi 446898486 339 REDIECRFDINRTAQIIVSL 358
Cdd:cd03825 341 RALAENHFDQRVQAQRYLEL 360
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
51-350 |
2.89e-17 |
|
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: 81.73 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 51 RGHDVTFIPFRN-----------SLHLPSILRLRRIIG---EFKPDLVICHSGHDSNIAGLSR--------LICCHR--- 105
Cdd:cd03799 27 RGHEVDIYAVNPgdlvkrhpdveKYNVPSLNLLYAIVGlnkKGAYDIIHCQFGPLGALGALLRrlkvlkgkLVTSFRgyd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 106 FSIVRQKTYITRKTRTFSLNylcDFIVVPSSAMMAHLMAEGV-RTPVTVIPPGFDwPALHNEAMRPLPLH--IHawaasa 182
Cdd:cd03799 107 ISMYVILEGNKVYPQLFAQG---DLFLPNCELFKHRLIALGCdEKKIIVHRSGID-CNKFRFKPRYLPLDgkIR------ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 183 dnvplIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWLVVGAGreEYEARLRQQTEHLGMSGDVLMAGALfPALPVYRI- 261
Cdd:cd03799 177 -----ILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDG--DLKEQLQQLIQELNIGDCVKLLGWK-PQEEIIEIl 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 262 --ASVVVMPS------ENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLPVGDVSAWTGALRDFLSRPERFRM 333
Cdd:cd03799 249 deADIFIAPSvtaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPE 328
|
330
....*....|....*..
gi 446898486 334 MAASAREDIECRFDINR 350
Cdd:cd03799 329 MGKAGRARVEEEYDINK 345
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
3-357 |
2.98e-17 |
|
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: 82.11 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 3 KILFTESSSDIGGQELQALAQMTALQKQGHSVLLAC----------REKSKIapeaRKRGHDVTFIPFrnslhLPSILRL 72
Cdd:cd04951 1 KILYVITGLGLGGAEKQTVLLADQMFIRGHDVNIVYltgevevkplNNNIII----YNLGMDKNPRSL-----LKALLKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 73 RRIIGEFKPDLVICHSGHdSNIagLSRLICCHRFSI--------------VRQKTYitRKTrtfslNYLCDFIVVPSSAM 138
Cdd:cd04951 72 KKIISAFKPDVVHSHMFH-ANI--FARFLRMLYPIPllictahnkneggrIRMFIY--RLT-----DFLCDITTNVSREA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 139 MAHLMAEGV--RTPVTVIPPGFDWPALHNEAMRPLPLHiHAWAASaDNVPLIVQVGMLRPEKGHEFMLRVLYQLKMEGKS 216
Cdd:cd04951 142 LDEFIAKKAfsKNKSVPVYNGIDLNKFKKDINVRLKIR-NKLNLK-NDEFVILNVGRLTEAKDYPNLLLAISELILSKND 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 217 FRWLVVGAG--REEYEARLRQqtehLGMSGDVLMAGALFPALPVYRIASVVVMPSENEAFGMVLAEASVSGVPVIASETG 294
Cdd:cd04951 220 FKLLIAGDGplRNELERLICN----LNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAG 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446898486 295 GIPDVIQKnvTGTLLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIECRFDINrtaqIIVS 357
Cdd:cd04951 296 GVAEVVGD--HNYVVPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFSIN----TIVN 352
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
20-353 |
5.60e-17 |
|
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: 81.26 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 20 ALAQMTALQK--QGHSVLLACREKSKIAPEARKRGHDVTFIPFRNSLHLPS--ILRLRRIIGEFKPDLVICHSGHDS-NI 94
Cdd:cd03809 20 TRELLKALAKndPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELAllRWLQILLPKKDKPDLLHSPHNTAPlLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 95 AGLSRLICCHRFSIVRQK-TYITRKTRTFSLNYL-----CDFIVVPSSAM---MAHLMAEgVRTPVTVIPPGFDwpalhn 165
Cdd:cd03809 100 KGCPQVVTIHDLIPLRYPeFFPKRFRLYYRLLLPislrrADAIITVSEATrddIIKFYGV-PPEKIVVIPLGVD------ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 166 EAMRPLPLHIHAWAASADNVPLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWLVVGAGREEYEaRLRQQTEHLGMSGD 245
Cdd:cd03809 173 PSFFPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDE-ELLDLVKKLGLGGR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 246 VLMAGAL-FPALP-VYRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNvtGTLLPVGDVSAWTGALRD 323
Cdd:cd03809 252 VRFLGYVsDEDLPaLYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDA--ALYFDPLDPESIADAILR 329
|
330 340 350
....*....|....*....|....*....|
gi 446898486 324 FLSRPERFRMMAASAREDIEcRFDINRTAQ 353
Cdd:cd03809 330 LLEDPSLREELIRKGLERAK-KFSWEKTAE 358
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
186-355 |
3.33e-16 |
|
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: 79.03 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 186 PLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWLVVGAGREEyeARLRQQTEHLGmsgDVLMAGALFPA--LPVYRIAS 263
Cdd:cd05844 190 PTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLR--PALQALAAALG---RVRFLGALPHAevQDWMRRAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 264 VVVMPS------ENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAAS 337
Cdd:cd05844 265 IFCLPSvtaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGA 344
|
170
....*....|....*...
gi 446898486 338 AREDIECRFDINRTAQII 355
Cdd:cd05844 345 ARAFVCEQFDIRVQTAKL 362
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
14-159 |
2.83e-15 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 72.95 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 14 GGQELQALAQMTALQKQGHSVLLACREKSKIAPEARKRGHDVTFIPF----RNSLHLPSILRLRRIIGEFKPDLVICHSG 89
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLplppRLLRSLAFLRRLRRLLRRERPDVVHAHSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 90 HDSNIAGLS-------RLIC-CHRFSIVRQKTYITRKTRTFSLNYL-------CDFIVVPSSAMMAHLMAE-GV-RTPVT 152
Cdd:pfam13439 81 FPLGLAALAarlrlgiPLVVtYHGLFPDYKRLGARLSPLRRLLRRLerrllrrADRVIAVSEAVADELRRLyGVpPEKIR 160
|
....*..
gi 446898486 153 VIPPGFD 159
Cdd:pfam13439 161 VIPNGVD 167
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
137-353 |
5.81e-15 |
|
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: 75.44 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 137 AMMAHL---MAEGVRTPVTVIPPGFDWPALHNEAMRP------LPLHIHAWAASadnvPLIVQVGMLRPEKGHEFMLRVL 207
Cdd:cd03792 144 LFVFHPpefVPPQVPPPKFYIPPSIDPLSGKNKDLSPadiryyLEKPFVIDPER----PYILQVARFDPSKDPLGVIDAY 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 208 YQLKMEGKSFRWLVVGAGRE---EYEARLRQQTEHLGMSGD--VLMAG---ALFPALpvYRIASVVVMPSENEAFGMVLA 279
Cdd:cd03792 220 KLFKRRAEEPQLVICGHGAVddpEGSVVYEEVMEYAGDDHDihVLRLPpsdQEINAL--QRAATVVLQLSTREGFGLTVS 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446898486 280 EASVSGVPVIASETGGIPDVIQKNVTGTLLPVGDVSAwtGALRDFLSRPERFRMMAASAREDIECRFDINRTAQ 353
Cdd:cd03792 298 EALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAA--VRILRLLTDPELRRKMGLAAREHVRDNFLITGNLR 369
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
26-356 |
5.54e-14 |
|
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: 72.37 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 26 ALQKQGHSVLLAC----REKSKIAPEARKRGHDVTFIPFR--------------NSLHLPSILRLRRIIGEFKPDLVICH 87
Cdd:cd03794 26 ELVRRGHEVTVLTpspnYPLGRIFAGATETKDGIRVIRVKlgpikknglirrllNYLSFALAALLKLLVREERPDVIIAY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 88 SghDSNIAGLSRLICCHRFSI-------------VRQKTYITRKTRTFSLNYL-------CDFIVVPSSAMMAHLMAEGV 147
Cdd:cd03794 106 S--PPITLGLAALLLKKLRGApfildvrdlwpesLIALGVLKKGSLLKLLKKLerklyrlADAIIVLSPGLKEYLLRKGV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 148 R-TPVTVIPPGFD---WPALHNEAMRPLPLhihawaasADNVPLIVQVGMLRPEKGHEFMLRVLYQLKMEgKSFRWLVVG 223
Cdd:cd03794 184 PkEKIIVIPNWADleeFKPPPKDELRKKLG--------LDDKFVVVYAGNIGKAQGLETLLEAAERLKRR-PDIRFLFVG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 224 AGREEyeARLRQQTEHLGMSGDVLmagalFPALP------VYRIASVVVMP-SENEAFGMV----LAEASVSGVPVIASE 292
Cdd:cd03794 255 DGDEK--ERLKELAKARGLDNVTF-----LGRVPkeevpeLLSAADVGLVPlKDNPANRGSspskLFEYMAAGKPILASD 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446898486 293 TGGIPDVIQKNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIECRFDINRTAQIIV 356
Cdd:cd03794 328 DGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRLL 391
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
2-326 |
8.39e-13 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 68.58 E-value: 8.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 2 MKILF-TESSSDIGGQELQALAQMTALQKQGHS--VLLACREK-------SKIAPEARKRGHDVTFIPFRNSLHlpsilR 71
Cdd:PRK09922 1 MKIAFiGEAVSGFGGMETVISNVINTFEESKINceMFFFCRNDkmdkawlKEIKYAQSFSNIKLSFLRRAKHVY-----N 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 72 LRRIIGEFKPDLVICHSGHDSNIAGLSRLICCHRFSIVRQKTYITRKTRTFSLNYLC--DFIVVPSSAMMAHLMAEGVRT 149
Cdd:PRK09922 76 FSKWLKETQPDIVICIDVISCLYANKARKKSGKQFKIFSWPHFSLDHKKHAECKKITcaDYHLAISSGIKEQMMARGISA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 150 P-VTVIppgFDwPALHNEAMRPLPLHihawaasaDNVPLIVQVGMLRPE--KGHEFMLRVLYQLKMEgksfrWL--VVGA 224
Cdd:PRK09922 156 QrISVI---YN-PVEIKTIIIPPPER--------DKPAVFLYVGRLKFEgqKNVKELFDGLSQTTGE-----WQlhIIGD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 225 GrEEYEaRLRQQTEHLGMSGDVLMAG---ALFPALPVyRIASV--VVMPSENEAFGMVLAEASVSGVPVIASE-TGGIPD 298
Cdd:PRK09922 219 G-SDFE-KCKAYSRELGIEQRIIWHGwqsQPWEVVQQ-KIKNVsaLLLTSKFEGFPMTLLEAMSYGIPCISSDcMSGPRD 295
|
330 340
....*....|....*....|....*...
gi 446898486 299 VIQKNVTGTLLPVGDVSAWTGALRDFLS 326
Cdd:PRK09922 296 IIKPGLNGELYTPGNIDEFVGKLNKVIS 323
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
14-353 |
4.28e-12 |
|
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.
Pssm-ID: 340832 [Multi-domain] Cd Length: 333 Bit Score: 66.54 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 14 GGQELQALAQMTALQKQGHSVLLacrekskIAPEARK-RGHDVTFIPFRNSL----------HLPSILRLRRIIGEFkpD 82
Cdd:cd03802 18 GGTELVVSALTEGLVRRGHEVTL-------FAPGDSHtSAPLVAVIPRALRLdpipqesklaELLEALEVQLRASDF--D 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 83 LVICHSGH-DSNIAGL--SRLICCHRFsivrqkTYITRKTRTFSLNYLCDFIVVPSSAMMAHLMAEgvrtPVTVIPPGFD 159
Cdd:cd03802 89 VIHNHSYDwLPPFAPLigTPFVTTLHG------PSIPPSLAIYAAEPPVNYVSISDAQRAATPPID----YLTVVHNGLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 160 WPALHNEAMRPLPLHihaWaasadnvplivqVGMLRPEKGHEFMLRVLYQLKmegksfrWLVVGAGREEYEA-------- 231
Cdd:cd03802 159 PADYRFQPDPEDYLA---F------------LGRIAPEKGLEDAIRVARRAG-------LPLKIAGKVRDEDyfyylqep 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 232 RLRQQTEHLGMSGDVLMAGALFPAlpvyriASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLlpV 311
Cdd:cd03802 217 LPGPRIEFIGEVGHDEKQELLGGA------RALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFL--V 288
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446898486 312 GDVSAWTGALRDfLSRPERfrmmaASAREDIECRFDINRTAQ 353
Cdd:cd03802 289 DSVEEMAEAIAN-IDRIDR-----AACRRYAEDRFSAARMAD 324
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
141-343 |
6.38e-12 |
|
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: 66.59 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 141 HLMAEGVRTpvTVIPPGFDwPALHNEAMRPLPLHIhawaasadnVPLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWL 220
Cdd:cd03813 261 RLGADPDKT--RVIPNGID-IQRFAPAREERPEKE---------PPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGW 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 221 VVGA--GREEYEARLRQQTEHLGMSGDVLMAGalFP-ALPVYRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIP 297
Cdd:cd03813 329 LIGPedEDPEYAQECKRLVASLGLENKVKFLG--FQnIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCR 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446898486 298 DVI-----QKNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIE 343
Cdd:cd03813 407 ELIygaddALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVE 457
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
131-306 |
7.56e-12 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 65.97 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 131 IVVPSSAMMAHLMAEGVRTPVTVIPPGFDWPAL--HNEAMRPLPLHIhawaASADNVplIVQVGMLRPEKGHEFMLRVLY 208
Cdd:PRK15484 143 IIVPSQFLKKFYEERLPNADISIVPNGFCLETYqsNPQPNLRQQLNI----SPDETV--LLYAGRISPDKGILLLMQAFE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 209 QLKMEGKSFRWLVVG-------AGREEYEARLRQQTEHLGmsGDVLMAGALFPAL--PVYRIASVVVMPSE-NEAFGMVL 278
Cdd:PRK15484 217 KLATAHSNLKLVVVGdptasskGEKAAYQKKVLEAAKRIG--DRCIMLGGQPPEKmhNYYPLADLVVVPSQvEEAFCMVA 294
|
170 180
....*....|....*....|....*...
gi 446898486 279 AEASVSGVPVIASETGGIPDVIQKNVTG 306
Cdd:PRK15484 295 VEAMAAGKPVLASTKGGITEFVLEGITG 322
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
151-335 |
1.38e-10 |
|
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.
Pssm-ID: 340849 [Multi-domain] Cd Length: 370 Bit Score: 62.02 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 151 VTVIPPG-FDWPALHNEAMRPLPLHihawaasaDNVPLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWLVVGA----- 224
Cdd:cd03822 160 IEVIPHGvPEVPQDPTTALKRLLLP--------EGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGElhpsl 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 225 GREEYEARLRQQTEHLGMSGDVLMAGALFPALPVYRIAS---VVVMPSENEafgmvlaEASVSGV---------PVIASE 292
Cdd:cd03822 232 ARYEGERYRKAAIEELGLQDHVDFHNNFLPEEEVPRYISaadVVVLPYLNT-------EQSSSGTlsyaiacgkPVISTP 304
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446898486 293 TGGIpDVIQKNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMA 335
Cdd:cd03822 305 LRHA-EELLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIA 346
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
270-346 |
7.27e-10 |
|
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: 59.91 E-value: 7.27e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446898486 270 ENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLPvGDVSAWTGALRDFLSRPERFRMMAASAREDIECRF 346
Cdd:cd03805 308 SNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCE-PTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKF 383
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
183-353 |
5.82e-09 |
|
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: 57.19 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 183 DNVPLIVQVGMLRPEKGHEFMLRVLYQLkMEgKSFRWLVVGAGREEYEARLRQQTE--------HLGMSGDV---LMAGA 251
Cdd:cd03791 292 PDAPLFGFVGRLTEQKGVDLILDALPEL-LE-EGGQLVVLGSGDPEYEQAFRELAErypgkvavVIGFDEALahrIYAGA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 252 LFpalpvyriasvVVMPSENEAFGMVLAEASVSGVPVIASETGG----IPDVIQKNVTGTLLPVGDVSAwtGALRDFLSR 327
Cdd:cd03791 370 DF-----------FLMPSRFEPCGLVQMYAMRYGTLPIVRRTGGladtVFDYDPETGEGTGFVFEDYDA--EALLAALRR 436
|
170 180 190
....*....|....*....|....*....|...
gi 446898486 328 -------PERFRMMAASAredIECRFDINRTAQ 353
Cdd:cd03791 437 alalyrnPELWRKLQKNA---MKQDFSWDKSAK 466
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
48-354 |
7.23e-09 |
|
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: 56.99 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 48 ARKRGHDVTFIPFRNSLHLPSILRLR-----------------------RIIGE-------------FKPDLVICHSGHD 91
Cdd:cd03818 21 ARQPGNEVTFLTRRNDQGIPGVRPVRyrpfrgvaspleghryvrdfeegVLRGQavlrallalkregFRPDVVVGHPGWG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 92 sniAGL--------SRLICCHRF--------------------SIVRQKTYITRKTRTFSLnylCDFIVVPSsAMMAHLM 143
Cdd:cd03818 101 ---EALfvkdvfpdVPLIGYCEYyyraegadvgfdpefpldlmIRCRLRNRNIALLLSLEQ---ADLGVTPT-RWQRSLF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 144 AEGVRTPVTVIPPGFDWPALH--NEAMRPLPlhihaWAA--SADNvPLIVQVGM-LRPEKG-HEFMlRVLYQLKMEGKSF 217
Cdd:cd03818 174 PAAYRDRISVIHDGVDTDRLApdPAARLRLL-----NGTelKAGD-PVITYVARnLEPYRGfHVFM-RALPRIQARRPDA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 218 RWLVVGAGREEYEARLR-------QQTEHLGMSGDVLMAGALFPA---LPVYRIASVVVMPSENEAFGMVLAEASVSGVP 287
Cdd:cd03818 247 RVVVVGGDGVSYGSPPPdggswkqKMLAELGVDLERVHFVGKVPYdqyVRLLQLSDAHVYLTYPFVLSWSLLEAMACGCP 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446898486 288 VIASETGGIPDVIQKNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIECRFDINRTAQI 354
Cdd:cd03818 327 VIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCLAR 393
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
14-157 |
1.00e-08 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 53.94 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 14 GGQELQALAQMTALQKQGHSVLLACREKSKIAPEARKRGHDVTFIPFRNSLHLP----SILRLRRIIGEFKPDLVICHSG 89
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPVPPRPSPLadlaALRRLRRLLRAERPDVVHAHSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446898486 90 -------HDSNIAGLSRLICCHRFSIVRQKTyITRKTRTFSLNYLC---DFIVVPSSAMMAHLMAEGV-RTPVTVIPPG 157
Cdd:pfam13579 81 taglaarLARRRRGVPLVVTVHGLALDYGSG-WKRRLARALERRLLrraDAVVVVSEAEAELLRALGVpAARVVVVPNG 158
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
180-301 |
1.33e-07 |
|
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273969 [Multi-domain] Cd Length: 473 Bit Score: 53.04 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 180 ASADNVPLIVQVGMLRPEKGHEFMLRVLYQLkMEgKSFRWLVVGAGREEYEARLRQQTE--------HLGMsgDVLMAGA 251
Cdd:TIGR02095 286 PVDDDVPLFGVISRLTQQKGVDLLLAALPEL-LE-LGGQLVVLGTGDPELEEALRELAErypgnvrvIIGY--DEALAHL 361
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446898486 252 LFPAlpvyriASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQ 301
Cdd:TIGR02095 362 IYAG------ADFILMPSRFEPCGLTQLYAMRYGTVPIVRRTGGLADTVV 405
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
179-316 |
2.12e-07 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 52.73 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 179 AASADNVPLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWLVVGAGReeYEARLRQQTEHLGMSGDVLMAGALFPALPV 258
Cdd:PRK15179 511 ARTSDARFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGP--LLESVREFAQRLGMGERILFTGLSRRVGYW 588
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446898486 259 YRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLPVGDVSA 316
Cdd:PRK15179 589 LTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTA 646
|
|
| COG4641 |
COG4641 |
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]; |
44-340 |
2.25e-07 |
|
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443679 [Multi-domain] Cd Length: 303 Bit Score: 51.86 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 44 IAPEARKRGHDVTFIPFRNSLHLPsiLRLRRIIGEFKPDLVICHSGHDsniaglsrlicchRFSIVRQKTYIT------- 116
Cdd:COG4641 15 LLRALAALGHEVTFLEPDDPWHDP--LYAAELLDAFRPDLVLVISGVE-------------LVAALRARGIPTvfwdtdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 117 RKTRTFSLNYL--CDFIVVPSSAMMAHLMAEGVRtPVTVIPPGFDwPALHneamRPLPlhiHAWAASADnvplIVQVGML 194
Cdd:COG4641 80 PVTLDRFRELLplYDLVFTFDGDCVEEYRALGAR-RVFYLPFAAD-PELH----RPVP---PEARFRYD----VAFVGNY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 195 RPEKGhEFMLRVLyqLKMEGKSFRwlVVGAGREEYEARLRqqtehlgmsgdVLMAGALFPA-LP-VYRIASVVV-MPSEN 271
Cdd:COG4641 147 YPDRR-ARLEELL--LAPAGLRLK--IYGPGWPKLALPAN-----------VRRGGHLPGEeHPaAYASSKITLnVNRMA 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446898486 272 EAFGMV---LAEASVSGVPVIASETGGIPDVIQknvTGTLLPV----GDVSAwtgALRDFLSRPERFRMMAASARE 340
Cdd:COG4641 211 ASPDSPtrrTFEAAACGAFLLSDPWEGLEELFE---PGEEVLVfrdgEELAE---KLRYLLADPEERRAIAEAGRR 280
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
26-87 |
1.02e-06 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 47.70 E-value: 1.02e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446898486 26 ALQKQGHSVLLACREKSKiapEARKRGHDVTFIPFRNSLHLP----SILRLRRIIGEFKPDLVICH 87
Cdd:pfam13477 19 ALADRGYDVHVISSKGPA---KDELIAEGIHVHRLKVPRKGPlgylKAFRLKKLIKKIKPDVVHVH 81
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
120-339 |
1.86e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 46.27 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 120 RTFSLNY-----LCDFIVVPSSAMMAHLMA--EGVRTPVTVIPPgfdwpaLHNEAMRPLPLHihawaaSADNVPLIVQVG 192
Cdd:PLN02949 208 RAFAWMYglvgrCAHLAMVNSSWTKSHIEAlwRIPERIKRVYPP------CDTSGLQALPLE------RSEDPPYIISVA 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 193 MLRPEKGHEFMLR----VLYQLKMEGKSFRWLVVGAGREEYEAR----LRQQTEHLGMSGDV-------------LMAGA 251
Cdd:PLN02949 276 QFRPEKAHALQLEafalALEKLDADVPRPKLQFVGSCRNKEDEErlqkLKDRAKELGLDGDVefhknvsyrdlvrLLGGA 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 252 lfpalpvyrIASVVVMPSENeaFGMVLAEASVSGVPVIASETGG------IPDVIQKnvTGTLlpVGDVSAWTGALRDFL 325
Cdd:PLN02949 356 ---------VAGLHSMIDEH--FGISVVEYMAAGAVPIAHNSAGpkmdivLDEDGQQ--TGFL--ATTVEEYADAILEVL 420
|
250
....*....|....*
gi 446898486 326 SRPERFRM-MAASAR 339
Cdd:PLN02949 421 RMRETERLeIAAAAR 435
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
122-343 |
3.09e-05 |
|
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: 45.37 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 122 FSLNYLcDFIVVpSSAMMAHLMAE--GVRTPVTVIPPGFDWPALHNEAMrplplhihawaaSADNVPLIVQVGMLRPEKG 199
Cdd:cd04949 109 ENLNKY-DAIIV-STEQQKQDLSErfNKYPPIFTIPVGYVDQLDTAESN------------HERKSNKIITISRLAPEKQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 200 HEFMLRVLYQLKMEGKSFRWLVVGAGREEYeaRLRQQTEHLGMSGDVLMAGALFPALPVYRIASVVVMPSENEAFGMVLA 279
Cdd:cd04949 175 LDHLIEAVAKAVKKVPEITLDIYGYGEERE--KLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLM 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446898486 280 EASVSGVPVIASETG-GIPDVIQKNVTGTLLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIE 343
Cdd:cd04949 253 EAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAE 317
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
188-305 |
5.95e-05 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 44.54 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 188 IVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRWLVVGAG---------REEYEarLRQQTEHLGM-----SGDVLMAGALF 253
Cdd:cd03796 196 IVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGpkrieleemREKYQ--LQDRVELLGAvpheeVRDVLVQGHIF 273
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446898486 254 palpvyriasvvVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVT 305
Cdd:cd03796 274 ------------LNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMI 313
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
266-331 |
6.08e-05 |
|
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: 44.58 E-value: 6.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446898486 266 VMPSEnEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLPVGDVSAWTGALRDFLSRPERF 331
Cdd:cd03804 270 VFAAE-EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEFEQNFDRF 334
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
262-347 |
5.91e-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: 41.68 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 262 ASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQkNVTGTLLPVGD--VSAWTGALRDFLSRPERFRMMAASAR 339
Cdd:cd04946 305 VDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVE-NETNGLLLDKDptPNEIVSSIMKFYLDGGDYKTMKISAR 383
|
....*...
gi 446898486 340 EDIECRFD 347
Cdd:cd04946 384 ECWEERFN 391
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
274-357 |
6.29e-04 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 38.35 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 274 FGMVLAEASVSGVPVIASETGGIPDVIQKNVTgtLLPVGDVSAWTGALRDFLSRPERFRMMAASAREDIECRFDINRTAQ 353
Cdd:pfam13524 12 PNMRVFEAAACGAPLLTDRTPGLEELFEPGEE--ILLYRDPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHTYAHRAE 89
|
....
gi 446898486 354 IIVS 357
Cdd:pfam13524 90 QLLD 93
|
|
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
258-326 |
6.67e-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: 41.69 E-value: 6.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446898486 258 VYRIAS----VVVMPSENEAFGMVLAEASVSGVPVIASETGGIPDVIQKNVTGTLLPVGDVSAWTGALRDFLS 326
Cdd:TIGR02468 564 IYRLAAktkgVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKLVA 636
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
186-295 |
1.24e-03 |
|
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.
Pssm-ID: 340835 [Multi-domain] Cd Length: 419 Bit Score: 40.67 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 186 PLIVQVGMLRPEKGHEFMLRVLYQLKMEGKSFRW----LV-VGAGR----EEYEARLRQQTEHLGMSGDVLMA-GALFPA 255
Cdd:cd03806 238 NQILSIAQFRPEKNHPLQLRAFAELLKRLPESIRsnpkLVlIGSCRneedKERVEALKLLAKELILEDSVEFVvDAPYEE 317
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446898486 256 LPVY-RIASVVVMPSENEAFGMVLAEASVSGVPVIASETGG 295
Cdd:cd03806 318 LKELlSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAG 358
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
20-86 |
2.26e-03 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic 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: 340818 [Multi-domain] Cd Length: 350 Bit Score: 39.51 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 20 ALAQmtALQKQGHSVLLACREKS---KIAPEARKRGHDVTFIPFRN--SLHLP--------SILRLRRIIGEFKPDLVIC 86
Cdd:cd03785 18 ALAE--ELRKRGAEILFIGTKRGleaKLVPEAGIPFHTIPISGLRRkgSLKNLkapfkllkGLRQARKILRKFKPDVVIG 95
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
218-309 |
3.89e-03 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 39.30 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 218 RWLVVGAGREEYEARLRqqTEHLGMSGDVLMAGALFPALPVYRIASVVVMPSENEAFGMVLAEASVSGVPVIASETGGIP 297
Cdd:PRK15490 431 RFVLVGDGDLRAEAQKR--AEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGSA 508
|
90
....*....|..
gi 446898486 298 DVIQKNVTGTLL 309
Cdd:PRK15490 509 ECFIEGVSGFIL 520
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
20-85 |
4.00e-03 |
|
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440471 [Multi-domain] Cd Length: 363 Bit Score: 38.96 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446898486 20 ALAQmtALQKQGHSVLLACREK---SKIAPEArkrGHDVTFIP---FRNSLHLP----------SILRLRRIIGEFKPDL 83
Cdd:COG0707 21 ALAE--ELRERGAEVLFIGTKRgleARLVPAA---GYPLHTIPvggLRRKGSLKnlkapfrllkALLQARKILKRFKPDV 95
|
..
gi 446898486 84 VI 85
Cdd:COG0707 96 VV 97
|
|
| |
