|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
2-399 |
0e+00 |
|
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: 529.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 2 KLTFFTMQFPVSSETFVLNQVTHFIDIGYEVEIIAVFPGDLVNRHAAFDQYNlaakthyllpddkagkvgklaqrlkiil 81
Cdd:cd03799 1 KIAFIVDEFPVLSETFILNQITGLIDRGHEVDIYAVNPGDLVKRHPDVEKYN---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 82 pkiykpgtlksfhigrygaQSSKLLLPAIVAANKKpFVADIFLVHFGYAGALANKLRELNVLQGKQVTVFHGADISRRHI 161
Cdd:cd03799 53 -------------------VPSLNLLYAIVGLNKK-GAYDIIHCQFGPLGALGALLRRLKVLKGKLVTSFRGYDISMYVI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 162 lEEHRDDYPRLFAQNELLLPISRLWEHKLIAMGCPAEKINVTRMGIEPEKFNLKLR-DSLHQPLRILSVARLTEKKGLAV 240
Cdd:cd03799 113 -LEGNKVYPQLFAQGDLFLPNCELFKHRLIALGCDEKKIIVHRSGIDCNKFRFKPRyLPLDGKIRILTVGRLTEKKGLEY 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 241 AIEACKILKEQGGQFEYTIVGYGDLENQLKTGIADGNLEDCVKLVGFKPQEEIKRYLDEADIFLLPSLTAADGDMEGIPV 320
Cdd:cd03799 192 AIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTAADGDQDGPPN 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501912241 321 ALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAKVETEFNQHIAYRQL 399
Cdd:cd03799 272 TLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDINKLNDEL 350
|
|
| wcaL |
TIGR04005 |
colanic acid biosynthesis glycosyltransferase WcaL; This gene is one of the glycosyl ... |
1-406 |
9.81e-175 |
|
colanic acid biosynthesis glycosyltransferase WcaL; This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species.
Pssm-ID: 188520 [Multi-domain] Cd Length: 406 Bit Score: 493.66 E-value: 9.81e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 1 MKLTFFTMQFPVSSETFVLNQVTHFIDIGYEVEIIAVFPGDLVNRHAAFDQYNLAAKTHYLLpDDKAGKVGKLAQRLKII 80
Cdd:TIGR04005 1 MKVSFFLLKFPLSSETFVLNQITAFIDMGYEVEIVALQKGDTQNTHAAWTEYNLAAKTRWLQ-DEPEGKLAKLRYRASQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 81 LPKIYKPGTLKSFHIGRYGAQSSKLLLPAIVAANKKPFVADIFLVHFGYAGALANKLRELNVLQGKQVTVFHGADISRRH 160
Cdd:TIGR04005 80 LRGLFRASTWKALNMSRYGDESRNLILSAICGQVPQPFKADVFIAHFGPAGVTAAKLRELGVIDGKIATIFHGIDISSRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 161 ILEEHRDDYPRLFAQNELLLPISRLWEHKLIAMGCPAEKINVTRMGIEPEKFNLKLRDSLHQPLRILSVARLTEKKGLAV 240
Cdd:TIGR04005 160 VLNHYTPEYQQLFRRGDLMLPISDLWAGRLKAMGCPPEKIAVSRMGVDMTRFTHRPVKAPGTPLEIISVARLTEKKGLHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 241 AIEACKILKEQGGQFEYTIVGYGDLENQLKTGIADGNLEDCVKLVGFKPQEEIKRYLDEADIFLLPSLTAADGDMEGIPV 320
Cdd:TIGR04005 240 AIEACRQLKAQGVAFRYRILGIGPWERRLRTLIEQYQLEDVVEMPGFKPSHEVKAMLDDADVFLLPSVTGTDGDMEGIPV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 321 ALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILLKLSR-GEDDIAQVVLAARAKVETEFNQHIAYRQL 399
Cdd:TIGR04005 320 ALMEAMAVGIPVVSTVHSGIPELVEAGKSGWLVPENDAHALADRLAAFSRiDTQTLRPVLTRAREKVEADFNQQVINRQL 399
|
....*..
gi 501912241 400 AEILERL 406
Cdd:TIGR04005 400 ASLLQTL 406
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
6-404 |
1.23e-52 |
|
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: 179.57 E-value: 1.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 6 FTMQFPVSSETFVLNQVTHFidigyeVEIIAVFPGDLVNRHAAFDqyNLAAKTHYLLPDDKAGKVGKLAQRLKiilpkiy 85
Cdd:cd05844 5 YRTVLLPVSETFIREQASGL------RRYRPTFVGCRRLAPAPFD--GVALRALGGSGPLRWLRQMAQRLLGW------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 86 kpgtlksfhiGRYGAQSSKLLLPAIVAAnkkpfvadiflvHFGYAGALANKL-RELNVlqgKQVTVFHGADIS-RRHILE 163
Cdd:cd05844 70 ----------SAPRLGGAAGLAPALVHA------------HFGRDGVYALPLaRALGV---PLVVTFHGFDITtSRAWLA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 164 EHRD---DYPRLFA----QNELLLPISRLWEHKLIAMGCPAEKINVTRMGIEPEKFnlKLRDSLHQPLRILSVARLTEKK 236
Cdd:cd05844 125 ASPGwpsQFQRHRRalqrPAALFVAVSGFIRDRLLARGLPAERIHVHYIGIDPAKF--APRDPAERAPTILFVGRLVEKK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 237 GLAVAIEACKILKEQGGQFEYTIVGYGDLENQLKTGIADGnleDCVKLVGFKPQEEIKRYLDEADIFLLPSLTAADGDME 316
Cdd:cd05844 203 GCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAAL---GRVRFLGALPHAEVQDWMRRAEIFCLPSVTAASGDSE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 317 GIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAKVETEFNqhiaY 396
Cdd:cd05844 280 GLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFD----I 355
|
....*...
gi 501912241 397 RQLAEILE 404
Cdd:cd05844 356 RVQTAKLE 363
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-404 |
4.55e-43 |
|
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: 154.23 E-value: 4.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 2 KLTFFTMQFPVSS---ETFVLNQVTHFIDIGYEVEIIAVFPGDlvnrhAAFDQYNLAAKTHYLLPDDKAGKVGKLAQRLK 78
Cdd:cd03801 1 KILLLSPELPPPVggaERHVRELARALAARGHDVTVLTPADPG-----EPPEELEDGVIVPLLPSLAALLRARRLLRELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 79 IILpkiykpgtlksfhigrygaqssklllpaivaankKPFVADIFLVHFGYAGALANKLRELnvLQGKQVTVFHGADISR 158
Cdd:cd03801 76 PLL----------------------------------RLRKFDVVHAHGLLAALLAALLALL--LGAPLVVTLHGAEPGR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 159 RHILEEHR----DDYPRLFAQNELLLPISRLWEHKLIAM-GCPAEKINVTRMGIEPEKFNLKLRDSLH---QPLRILSVA 230
Cdd:cd03801 120 LLLLLAAErrllARAEALLRRADAVIAVSEALRDELRALgGIPPEKIVVIPNGVDLERFSPPLRRKLGippDRPVLLFVG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 231 RLTEKKGLAVAIEACKILKEQGGQFEYTIVG-YGDLENQLKTgiADGNLEDCVKLVGFKPQEEIKRYLDEADIFLLPSLt 309
Cdd:cd03801 200 RLSPRKGVDLLLEALAKLLRRGPDVRLVIVGgDGPLRAELEE--LELGLGDRVRFLGFVPDEELPALYAAADVFVLPSR- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 310 aadgdMEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAKVETE 389
Cdd:cd03801 277 -----YEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAER 351
|
410
....*....|....*
gi 501912241 390 FNQHIAYRQLAEILE 404
Cdd:cd03801 352 FSWERVAERLLDLYR 366
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
6-406 |
1.10e-41 |
|
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.
Pssm-ID: 340828 [Multi-domain] Cd Length: 376 Bit Score: 150.99 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 6 FTMQFPVS----SETFVLNQVTHFIDIGYEVEIIA-VFPGDLVNRHAAFDQYNLAAKTHYLLPddkagkvgklaqrlkii 80
Cdd:cd03798 4 LTNIYPNAnspgRGIFVRRQVRALSRRGVDVEVLApAPWGPAAARLLRKLLGEAVPPRDGRRL----------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 81 LPKIYKPGTLKSFHIgrygaqssKLLLPAIVAANKKPFvaDIFLVHFGY-AGALANKLRELNvlqGKQVTV-FHGADISR 158
Cdd:cd03798 67 LPLKPRLRLLAPLRA--------PSLAKLLKRRRRGPP--DLIHAHFAYpAGFAAALLARLY---GVPYVVtEHGSDINV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 159 RHILEEHRDDYPRLFAQNELLLPISRLWEHKLIAMGCPAEKINVTRMGIEPEKFNLKLRDsLHQPLR---ILSVARLTEK 235
Cdd:cd03798 134 FPPRSLLRKLLRWALRRAARVIAVSKALAEELVALGVPRDRVDVIPNGVDPARFQPEDRG-LGLPLDafvILFVGRLIPR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 236 KGLAVAIEACKILKEQGGQFEYTIVGYGDLENQLKTGIADGNLEDCVKLVGFKPQEEIKRYLDEADIFLLPSLtaadgdM 315
Cdd:cd03798 213 KGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSR------H 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 316 EGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILLKLSRgEDDIAQVVLAARAKVETEFNQHIA 395
Cdd:cd03798 287 EGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALA-EPYLRELGEAARARVAERFSWVKA 365
|
410
....*....|.
gi 501912241 396 YRQLAEILERL 406
Cdd:cd03798 366 ADRIAAAYRDV 376
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
205-399 |
1.46e-41 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
Pssm-ID: 340837 [Multi-domain] Cd Length: 358 Bit Score: 150.05 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 205 MGIEPEKFNLKLRDSLHQPLRILSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVGYGDLENQLKTGIADGNLEDCVKL 284
Cdd:cd03808 171 SGVDLDRFQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEF 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 285 VGFKpqEEIKRYLDEADIFLLPSltaadgDMEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAI 364
Cdd:cd03808 251 LGFR--SDVPELLAESDVFVLPS------YREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADA 322
|
170 180 190
....*....|....*....|....*....|....*
gi 501912241 365 LLKLSRGEDDIAQVVLAARAKVETEFNQHIAYRQL 399
Cdd:cd03808 323 IEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKL 357
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
226-385 |
2.70e-37 |
|
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: 132.78 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 226 ILSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVGYGDLENQLKTGIADGNLEDCVKLVGFKPQEEIKRYLDEADIFLL 305
Cdd:pfam00534 5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 306 PSLTaadgdmEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILLKLSrgEDDIAQVVLAARAK 385
Cdd:pfam00534 85 PSRY------EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLL--EDEELRERLGENAR 156
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
15-394 |
5.13e-37 |
|
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: 137.87 E-value: 5.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 15 ETFVLNQVTHFIDIGYEVEIIaVFPGDLVNRHAAFDQYNLAAKtHYLLPDDKAGKVGKLAQRLKIILpKIYKPgtlksfh 94
Cdd:cd03811 15 ERVLLNLANALDKRGYDVTLV-LLRDEGDLDKQLNGDVKLIRL-LIRVLKLIKLGLLKAILKLKRIL-KRAKP------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 95 igrygaqssklllpaivaankkpfvaDIFLVHFGYAGALANKLRELNVlqgKQVTVFHGaDISRRHILEEHRDDYPRLFA 174
Cdd:cd03811 85 --------------------------DVVISFLGFATYIVAKLAAARS---KVIAWIHS-SLSKLYYLKKKLLLKLKLYK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 175 QNELLLPISRLWEHKLIA-MGCPAEKINVTRMGIEPEKFNLKLRDSL----HQPLRILSVARLTEKKGLAVAIEACKILK 249
Cdd:cd03811 135 KADKIVCVSKGIKEDLIRlGPSPPEKIEVIYNPIDIDRIRALAKEPIlnepEDGPVILAVGRLDPQKGHDLLIEAFAKLR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 250 EQGGQFEYTIVGYGDLENQLKTGIADGNLEDCVKLVGFKPQeeIKRYLDEADIFLLPSLTaadgdmEGIPVALMEAMAVG 329
Cdd:cd03811 215 KKYPDVKLVILGDGPLREELEKLAKELGLAERVIFLGFQSN--PYPYLKKADLFVLSSRY------EGFPNVLLEAMALG 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501912241 330 LPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAKVETEFNQHI 394
Cdd:cd03811 287 TPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEAVFREYTI 351
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
223-368 |
7.36e-34 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 123.01 E-value: 7.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 223 PLRILSVARLTEK-KGLAVAIEACKILKEQGGQFEYTIVGYGDLEnQLKTGIAdgNLEDCVKLVGFkpQEEIKRYLDEAD 301
Cdd:pfam13692 1 RPVILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEE-ELEELAA--GLEDRVIFTGF--VEDLAELLAAAD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501912241 302 IFLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRHSGIPELIeHNVSGWLAPEGDAQALAAILLKL 368
Cdd:pfam13692 76 VFVLPSLY------EGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRL 135
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
15-399 |
3.69e-31 |
|
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: 122.05 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 15 ETFVLNQVTHFIDIGYEVeiiAVFPGDlvNRHAAFDQYNLAAKTHYLLPDdkagkvgklaqrlkiilPKIYKPGTLKSFH 94
Cdd:cd03823 18 EISVHDLAEALVAEGHEV---AVLTAG--VGPPGQATVARSVVRYRRAPD-----------------ETLPLALKRRGYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 95 IGRYgaqssklLLPAIvaankKPFVADIF------LVHF----GYAGALANKLRELNVlqgKQVTVFHGAD-ISRRHILE 163
Cdd:cd03823 76 LFET-------YNPGL-----RRLLARLLedfrpdVVHThnlsGLGASLLDAARDLGI---PVVHTLHDYWlLCPRQFLF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 164 EHRDDyprlfaqneLLLPISRLWEHKLIAMGCPAEKINVTRMGIEPEKFNLKLRDSLHQPLRILSVARLTEKKGLAVAIE 243
Cdd:cd03823 141 KKGGD---------AVLAPSRFTANLHEANGLFSARISVIPNAVEPDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 244 ACKILKEqgGQFEYTIVGYGDLEnqlktGIADGNLEDCVKLVGFKPQEEIKRYLDEADIFLLPSLTAadgdmEGIPVALM 323
Cdd:cd03823 212 AFKRLPR--EDIELVIAGHGPLS-----DERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWP-----EPFGLVVR 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501912241 324 EAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAKVETEfNQHIAYRQL 399
Cdd:cd03823 280 EAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTE-SQAEEYLKL 354
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
190-390 |
1.50e-29 |
|
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: 117.42 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 190 LIAMGCPAEKINVTRMGIEPEKFN--LKLRDSLHQPL-------RILSVARLTEKKGLAVAIEACKILKEQGGQFEYTIV 260
Cdd:cd03807 148 HQEQGYAKNKIVVIYNGIDLFKLSpdDASRARARRRLglaedrrVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLV 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 261 GYGDLENQLKTGIADGNLEDCVKLVGfkPQEEIKRYLDEADIFLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRHSGI 340
Cdd:cd03807 228 GRGPERPNLERLLLELGLEDRVHLLG--ERSDVPALLPAMDIFVLSSRT------EGFPNALLEAMACGLPVVATDVGGA 299
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501912241 341 PELIEhNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAKVETEF 390
Cdd:cd03807 300 AELVD-DGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEF 348
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
225-387 |
4.64e-28 |
|
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: 113.10 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 225 RILSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVGYGDLENQLKTGIADGNLEDCVKLVGfkPQEEIKRYLDEADIFL 304
Cdd:cd03820 183 RILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLG--PTKNIAEEYANSSIFV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 305 LPSltaadgDMEGIPVALMEAMAVGLPVVSS-RHSGIPELIEHNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAAR 383
Cdd:cd03820 261 LSS------RYEGFPMVLLEAMAYGLPIISFdCPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNAR 334
|
....
gi 501912241 384 AKVE 387
Cdd:cd03820 335 KNAE 338
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
195-388 |
8.05e-26 |
|
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.
Pssm-ID: 340848 [Multi-domain] Cd Length: 377 Bit Score: 107.45 E-value: 8.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 195 CPAEKINVTRMGIEPEKFNLKLRDSLHQPLR-----ILSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVGYGDLENQL 269
Cdd:cd03821 171 GLEPPIAVIPNGVDIPEFDPGLRDRRKHNGLedrriILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDGAYPA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 270 KTG-IADGNLEDCVKLVGFKPQEEIKRYLDEADIFLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNV 348
Cdd:cd03821 251 FLQlQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYS------ENFGNVVAEALACGLPVVITDKCGLSELVEAGC 324
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 501912241 349 SGWLAPegDAQALAAIL---LKLSRGEDDIAQVVLAARAKVET 388
Cdd:cd03821 325 GVVVDP--NVSSLAEALaeaLRDPADRKRLGEMARRARQVEEN 365
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
293-406 |
5.63e-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: 5.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 293 IKRYLDEADIFLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILLKLSRGE 372
Cdd:COG0438 14 LEALLAAADVFVLPSRS------EGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDP 87
|
90 100 110
....*....|....*....|....*....|....
gi 501912241 373 DDIAQVVLAARAKVETEFNQHIAYRQLAEILERL 406
Cdd:COG0438 88 ELRRRLGEAARERAEERFSWEAIAERLLALYEEL 121
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
120-352 |
2.99e-24 |
|
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: 100.17 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 120 ADIFLVHFGYAGALANKLRELNVLQgKQVTVFHGADISRrhileehrddYPRLFAQNELLLPISRLWEHKLiamgcpaek 199
Cdd:cd01635 55 PDVVHAHSPHAAALAALLAARLLGI-PIVVTVHGPDSLE----------STRSELLALARLLVSLPLADKV--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 200 invtrmgiepekfnlklrdslhqplrilSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVGYGDLENQLKTGIADGNLE 279
Cdd:cd01635 115 ----------------------------SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501912241 280 DCVKLVGFKPQEEIKRYLDE-ADIFLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWL 352
Cdd:cd01635 167 ERVVIIGGLVDDEVLELLLAaADVFVLPSRS------EGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLL 234
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
24-400 |
5.06e-24 |
|
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: 102.42 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 24 HFIDIGYEVEIIAVFPgdlvnrhaafdqynlaaktHYLLPDDKAGKVGKLAqRLKIILPKIYKPGTLKSFHIGRYGAQSS 103
Cdd:cd03794 26 ELVRRGHEVTVLTPSP-------------------NYPLGRIFAGATETKD-GIRVIRVKLGPIKKNGLIRRLLNYLSFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 104 KLLLPAIVAANKKPfvaDIFLVH-----FGYAGALANKLRelnvlqGKQVtvfhgadisrrhILEeHRDDYPRLFA---- 174
Cdd:cd03794 86 LAALLKLLVREERP---DVIIAYsppitLGLAALLLKKLR------GAPF------------ILD-VRDLWPESLIalgv 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 175 -QNELLLPISRLWEHK------------------LIAMGCPAEKINVTRMGIEPEKFNLKLRDSLHQ------PLRILSV 229
Cdd:cd03794 144 lKKGSLLKLLKKLERKlyrladaiivlspglkeyLLRKGVPKEKIIVIPNWADLEEFKPPPKDELRKklglddKFVVVYA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 230 ARLTEKKGLAVAIEACKILKEQGgQFEYTIVGYGDLENQLKTGIADGNLEDcVKLVGFKPQEEIKRYLDEADIFLLPsLT 309
Cdd:cd03794 224 GNIGKAQGLETLLEAAERLKRRP-DIRFLFVGDGDEKERLKELAKARGLDN-VTFLGRVPKEEVPELLSAADVGLVP-LK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 310 AADGDMEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAKVETE 389
Cdd:cd03794 301 DNPANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEK 380
|
410
....*....|.
gi 501912241 390 FNQHIAYRQLA 400
Cdd:cd03794 381 FSREKLADRLL 391
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
121-363 |
8.73e-23 |
|
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: 98.20 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 121 DIFLVHF-----GYAGALANKLRELnvlqgKQVTVFHGadisrRHILEEHRDDY---PRLFAQNELLlpISRLWEHKLI- 191
Cdd:cd03819 76 RIDLIHAhsrapAWLGWLASRLTGV-----PLVTTVHG-----SYLATYHPKDFalaVRARGDRVIA--VSELVRDHLIe 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 192 AMGCPAEKINVTRMGIEPEKF--------NLKLRDSLHQPLrILSVARLTEKKGLAVAIEACKILKEQGGqFEYTIVGYG 263
Cdd:cd03819 144 ALGVDPERIRVIPNGVDTDRFppeaeaeeRAQLGLPEGKPV-VGYVGRLSPEKGWLLLVDAAAELKDEPD-FRLLVAGDG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 264 DLENQLKTGIADGNLEDCVKLVGFKpqEEIKRYLDEADIFLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRHSGIPEL 343
Cdd:cd03819 222 PERDEIRRLVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSLH------EEFGRVALEAMACGTPVVATDVGGAREI 293
|
250 260
....*....|....*....|
gi 501912241 344 IEHNVSGWLAPEGDAQALAA 363
Cdd:cd03819 294 VVHGRTGLLVPPGDAEALAD 313
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
170-394 |
4.95e-22 |
|
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: 96.19 E-value: 4.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 170 PRLFAQNELLLPISRlwEHKLIAMGCPAEKINVTRMGIE-PEKFNLKLRDslhqplrILSVARLTEKKGLAVAIEACKIL 248
Cdd:cd03795 146 PNYVETSPTLREFKN--KVRVIPLGIDKNVYNIPRVDFEnIKREKKGKKI-------FLFIGRLVYYKGLDYLIEAAQYL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 249 KeqggqFEYTIVGYGDLENQLKTGIADGNLEDcVKLVGFKPQEEIKRYLDEADIFLLPSLTAAdgdmEGIPVALMEAMAV 328
Cdd:cd03795 217 N-----YPIVIGGEGPLKPDLEAQIELNLLDN-VKFLGRVDDEEKVIYLHLCDVFVFPSVLRS----EAFGIVLLEAMMC 286
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501912241 329 GLPVVSSR-HSGIPELIEHNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAKVETEFNQHI 394
Cdd:cd03795 287 GKPVISTNiGTGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEK 353
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
207-387 |
4.67e-21 |
|
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: 93.13 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 207 IEPEKFNLKLRDSlhQPLRILSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVGYGDLENQLKTGIADGNLEDCVKLVG 286
Cdd:cd04949 146 VDQLDTAESNHER--KSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 287 F--KPQEEIKRYldeaDIFLLPSLtaadgdMEGIPVALMEAMAVGLPVVSSR-HSGIPELIEHNVSGWLAPEGDAQALAA 363
Cdd:cd04949 224 YhsNLDQEYQDA----YLSLLTSQ------MEGFGLTLMEAIGHGLPVVSYDvKYGPSELIEDGENGYLIEKNNIDALAD 293
|
170 180
....*....|....*....|....
gi 501912241 364 ILLKLSRGEDDIAQVVLAARAKVE 387
Cdd:cd04949 294 KIIELLNDPEKLQQFSEESYKIAE 317
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
206-387 |
1.27e-20 |
|
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: 92.34 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 206 GIEPEKFNLKLRDSLHQPL-------RILSVARLTEKKGLAVAIEACKILKEQGgQFEYTIVGYGDLENQLKTGIADGNL 278
Cdd:cd03817 177 GIDLDKFEKPLNTEERRKLglppdepILLYVGRLAKEKNIDFLLRAFAELKKEP-NIKLVIVGDGPEREELKELARELGL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 279 EDCVKLVGFKPQEEIKRYLDEADIFLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDA 358
Cdd:cd03817 256 ADKVIFTGFVPREELPEYYKAADLFVFASTT------ETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDE 329
|
170 180
....*....|....*....|....*....
gi 501912241 359 qALAAILLKLSRGEDDIAQVVLAARAKVE 387
Cdd:cd03817 330 -TLAEKLLHLRENLELLRKLSKNAEISAR 357
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
184-399 |
2.68e-20 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340841 [Multi-domain] Cd Length: 474 Bit Score: 92.40 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 184 RLWEhklIAMGCPAEKINVTRMGIEPEKF-NLKLRDSLHQPLRILSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVGy 262
Cdd:cd03813 256 RRRQ---IRLGADPDKTRVIPNGIDIQRFaPAREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIG- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 263 GDLENQL-----KTGIADGNLEDCVKLVGFkpqEEIKRYLDEADIFLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRH 337
Cdd:cd03813 332 PEDEDPEyaqecKRLVASLGLENKVKFLGF---QNIKEYYPKLGLLVLTSIS------EGQPLVILEAMASGVPVVATDV 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 338 SGIPELIE-----HNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAKVETEFNQHI---AYRQL 399
Cdd:cd03813 403 GSCRELIYgaddaLGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGmidSYRKL 472
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
192-406 |
2.93e-19 |
|
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.
Pssm-ID: 132132 [Multi-domain] Cd Length: 374 Bit Score: 88.63 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 192 AMGCPAEKINVTRMGIEPEKFNLKLRD---------SLHQPLRILSVARLTEKKGLAVAIEACKILKEQGGQFE----YT 258
Cdd:TIGR03088 154 PVKVPPAKIHQIYNGVDTERFHPSRGDrspilppdfFADESVVVGTVGRLQAVKDQPTLVRAFALLVRQLPEGAerlrLV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 259 IVGYGDLENQLKTGIADGNLEDCVKLVGfkPQEEIKRYLDEADIFLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRHS 338
Cdd:TIGR03088 234 IVGDGPARGACEQMVRAAGLAHLVWLPG--ERDDVPALMQALDLFVLPSLA------EGISNTILEAMASGLPVIATAVG 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501912241 339 GIPELIEHNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAKVETEFNQHIAYRQLAEILERL 406
Cdd:TIGR03088 306 GNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSINAMVAAYAGLYDQL 373
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
277-400 |
1.78e-17 |
|
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: 83.17 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 277 NLEDCVKLVGfkPQEEIKRYLDEADIFLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEG 356
Cdd:cd04962 249 GVEDRVLFLG--KQDDVEELLSIADLFLLPSEK------ESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVG 320
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 501912241 357 DAQALAAILLKLSRGEDDIAQVVLAARAKVETEFN------QHIAYRQLA 400
Cdd:cd04962 321 DVDAMAKSALSILEDDELYNRMGRAARKRAAERFDperivpQYEAYYRRL 370
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
77-368 |
2.76e-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: 82.41 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 77 LKIILPKIYKPGTLKSFHIGRYGAQSSKLLLPAIVAANKKPFVADIFLVHFGYAGalanklreLNVLQGKQVTVFHgaDI 156
Cdd:cd03809 42 LPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKPDLLHSPHNTAP--------LLLKGCPQVVTIH--DL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 157 SRRHILEEHRDDY--------PRLFAQNELLLPISRLWEHKLIA-MGCPAEKINVTRMGIEPEKFNL--KLRDSLHQPLR 225
Cdd:cd03809 112 IPLRYPEFFPKRFrlyyrlllPISLRRADAIITVSEATRDDIIKfYGVPPEKIVVIPLGVDPSFFPPesAAVLIAKYLLP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 226 ---ILSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVGYGDLEN-QLKTGIADGNLEDCVKLVGFKPQEEIKRYLDEAD 301
Cdd:cd03809 192 epyFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDeELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGAR 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501912241 302 IFLLPSLtaadgdME--GIPVAlmEAMAVGLPVVSSRHSGIPELIEHnvSGWLAPEGDAQALAAILLKL 368
Cdd:cd03809 272 AFVFPSL------YEgfGLPVL--EAMACGTPVIASNISVLPEVAGD--AALYFDPLDPESIADAILRL 330
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
221-368 |
3.65e-17 |
|
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: 82.67 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 221 HQPLRILSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVG-----YGDLENQLKTGIADGN-LEDCVKLVGFKPQEEIK 294
Cdd:cd03800 218 PDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGgpsddPLSMDREELAELAEELgLIDRVRFPGRVSRDDLP 297
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501912241 295 RYLDEADIFLLPSLTAADGdmegipVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILLKL 368
Cdd:cd03800 298 ELYRAADVFVVPSLYEPFG------LTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRL 365
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
68-400 |
8.29e-17 |
|
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: 81.35 E-value: 8.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 68 GKVGKLAQRLKIIL------------PKIYKPGTLKSFHIGRYGAQSSKLLLPAIVAAN-KKPFVA---DIFLVHFGYAG 131
Cdd:cd04946 54 SNSLKITSFLKKIFralslfslvfykEIWIKDKPRSGSFLLLYYFLIASFLSKHRVLALlQFVSIFgqgTVVYSYWLNHT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 132 ALANKLRELNVLQGKQVTVFHGADISRRHILEEHRDDYPRLFAQNELLLPISrlwEHKLIAM-GC-PA--EKINVTRMGI 207
Cdd:cd04946 134 ALGLGLLKDEYYRDVVISRAHRYDLYEDQYGSYYLPLREYLVSYLDAVFLIS---KEGKDYLqKCyPAykEKIFVSRLGV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 208 EPEKFNLKLrdSLHQPLRILSVARLTEKKGLAVAIEACKIL--KEQGGQFEYTIVGYGDLENQLKTgIADGNLEDC-VKL 284
Cdd:cd04946 211 SDKEQYSKV--KKEGDLRLVSCSSIVPVKRIDLIIETLNSLcvAHPSICISWTHIGGGPLKERLEK-LAENKLENVkVNF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 285 VGFKPQEEIKRYLDE--ADIFLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLaPEGDA--QA 360
Cdd:cd04946 288 TGEVSNKEVKQLYKEndVDVFVNVSES------EGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLL-LDKDPtpNE 360
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 501912241 361 LAAILLKLSRGEDDIAQVVLAARAKVETEFNQHIAYRQLA 400
Cdd:cd04946 361 IVSSIMKFYLDGGDYKTMKISARECWEERFNAEVNYSKFA 400
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
226-406 |
2.15e-16 |
|
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: 80.07 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 226 ILSVARLTEK--KGLAVAIEACKILkEQGGQFEYTIVGYGDLENQLKTG--IADGNLEDCVKLVgfkpqeeikRYLDEAD 301
Cdd:cd03825 196 ILFGAESVTKprKGFDELIEALKLL-ATKDDLLLVVFGKNDPQIVILPFdiISLGYIDDDEQLV---------DIYSAAD 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 302 IFLLPSLtaadgdMEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALA-AILLKLSRGED--DIAQv 378
Cdd:cd03825 266 LFVHPSL------ADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAeAIEWLLANPKEreSLGE- 338
|
170 180
....*....|....*....|....*...
gi 501912241 379 vlAARAKVETEFNQHIAYRQLAEILERL 406
Cdd:cd03825 339 --RARALAENHFDQRVQAQRYLELYKDL 364
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
209-389 |
3.64e-16 |
|
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: 79.26 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 209 PEKFNLKLRDSLHQPLR--ILSVARLTEKKGLAVAIEACKILKEQGGqFEYTIVGYGDLENQLKTGIadgnleDCVKLVG 286
Cdd:cd03814 182 PSRRDAALRRRLGPPGRplLLYVGRLAPEKNLEALLDADLPLAASPP-VRLVVVGDGPARAELEARG------PDVIFTG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 287 FKPQEEIKRYLDEADIFLLPSLTAADGdmegipVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILL 366
Cdd:cd03814 255 FLTGEELARAYASADVFVFPSRTETFG------LVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALR 328
|
170 180
....*....|....*....|...
gi 501912241 367 KLSrgEDDIAQVVLAARAKVETE 389
Cdd:cd03814 329 ALL--EDPELRRRMAARARAEAE 349
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
206-362 |
5.98e-14 |
|
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: 72.48 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 206 GIEPEKFN------LKLRDSL---HQPLRILSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVGYGDLENQLKTGIADG 276
Cdd:cd04951 162 GIDLNKFKkdinvrLKIRNKLnlkNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPLRNELERLICNL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 277 NLEDCVKLVGFkpQEEIKRYLDEADIFLLPSLtaadgdMEGIPVALMEAMAVGLPVVSSRHSGIPELIEHnvSGWLAPEG 356
Cdd:cd04951 242 NLVDRVILLGQ--ISNISEYYNAADLFVLSSE------WEGFGLVVAEAMACERPVVATDAGGVAEVVGD--HNYVVPVS 311
|
....*.
gi 501912241 357 DAQALA 362
Cdd:cd04951 312 DPQLLA 317
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
206-335 |
2.88e-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: 70.40 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 206 GIEPEK--FNLKLRDSLHQPLrILS-------VARLTEKKGLAVAIEACKILKEQGGQFEYTIVGYGDLENQLKTGIADG 276
Cdd:cd03812 166 GIDIEKykFNKEKRRKRRKLL-ILEdklvlghVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKIKEKVKEL 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 501912241 277 NLEDCVKLVGFkpQEEIKRYLDEADIFLLPSLtaadgdMEGIPVALMEAMAVGLPVVSS 335
Cdd:cd03812 245 GLEDKVIFLGF--RNDVSEILSAMDVFLFPSL------YEGLPLVAVEAQASGLPCLLS 295
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
223-347 |
3.14e-12 |
|
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: 67.65 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 223 PLRILSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVGYGDLENQLKTGIADGNLEDCVKLVGFKPQEEIKRYLDEADI 302
Cdd:cd03796 193 KITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHI 272
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 501912241 303 FLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRHSGIPELIEHN 347
Cdd:cd03796 273 FLNTSLT------EAFCIAIVEAASCGLLVVSTRVGGIPEVLPPD 311
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
196-388 |
3.79e-12 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 67.43 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 196 PAEKINVTRMGIEPEKFNLKLR-DSLHQPLR--------ILSVARLTEKKGLavaiEACKILKEQGGQFEYTIVGYGDLE 266
Cdd:PLN02871 227 AANRIRVWNKGVDSESFHPRFRsEEMRARLSggepekplIVYVGRLGAEKNL----DFLKRVMERLPGARLAFVGDGPYR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 267 NQLKTGIADGNledcVKLVGFKPQEEIKRYLDEADIFLLPSltaadgDMEGIPVALMEAMAVGLPVVSSRHSGIPELI-- 344
Cdd:PLN02871 303 EELEKMFAGTP----TVFTGMLQGDELSQAYASGDVFVMPS------ESETLGFVVLEAMASGVPVVAARAGGIPDIIpp 372
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 501912241 345 -EHNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAKVET 388
Cdd:PLN02871 373 dQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEK 417
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
35-368 |
7.44e-12 |
|
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: 66.25 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 35 IAVFPGDLVNrhaafdqyNLAAKTHYLLPDDKAgkvgklAQRLKIILPKIYKPGTLKSFHIGRYGAqsskllLPAIVAAN 114
Cdd:cd03822 15 IATYTDDLVE--------GLRKGGPVVIVVIVS------PQDEILKDDDFEVPNEIKSWNSNEYFR------LLDHLNFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 115 KkpFVADIFLVHFGYAG--ALANKLRELNVLQGKQVTVFHGADISRrHILEEHRDDYPRLFAQNELLLPISRLWEHKLIA 192
Cdd:cd03822 75 K--PDVVHIQHEFGIFGgkYGLYALGLLLHLRIPVITTLHTVLDLS-DPGKQALKVLFRIATLSERVVVMAPISRFLLVR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 193 M-GCPAEKINVTRMGI----EPEKFNLKLRDSLHQPLRILSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVG------ 261
Cdd:cd03822 152 IkLIPAVNIEVIPHGVpevpQDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGelhpsl 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 262 -YGDLENQLKTGIADGNLEDCVKLV-GFKPQEEIKRYLDEADIFLLP---SLTAADGdmegipvALMEAMAVGLPVVSSR 336
Cdd:cd03822 232 aRYEGERYRKAAIEELGLQDHVDFHnNFLPEEEVPRYISAADVVVLPylnTEQSSSG-------TLSYAIACGKPVISTP 304
|
330 340 350
....*....|....*....|....*....|..
gi 501912241 337 HsGIPELIEHNVSGWLAPEGDAQALAAILLKL 368
Cdd:cd03822 305 L-RHAEELLADGRGVLVPFDDPSAIAEAILRL 335
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
133-372 |
6.31e-10 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 60.11 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 133 LANKLRELNvlqGKQVTVFHGADISRRHilEEHRDDYPRLFAQNELLlpISRLWEHKLIAMGCPAEKINVTRMGIEPeKF 212
Cdd:PRK09922 98 YANKARKKS---GKQFKIFSWPHFSLDH--KKHAECKKITCADYHLA--ISSGIKEQMMARGISAQRISVIYNPVEI-KT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 213 NLKLRDSLHQPLRILSVARLTEKKGLAVAiEACKILKEQGGQFEYTIVGYGDLENQLKTGIADGNLEDCVKLVGFK--PQ 290
Cdd:PRK09922 170 IIIPPPERDKPAVFLYVGRLKFEGQKNVK-ELFDGLSQTTGEWQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQsqPW 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 291 EEIKRYLDEADIFLLPSltaadgDMEGIPVALMEAMAVGLPVVSSRH-SGIPELIEHNVSGWLAPEGDAQALAAILLKLS 369
Cdd:PRK09922 249 EVVQQKIKNVSALLLTS------KFEGFPMTLLEAMSYGIPCISSDCmSGPRDIIKPGLNGELYTPGNIDEFVGKLNKVI 322
|
...
gi 501912241 370 RGE 372
Cdd:PRK09922 323 SGE 325
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
322-390 |
4.39e-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: 57.76 E-value: 4.39e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501912241 322 LMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAKVETEF 390
Cdd:cd03818 317 LLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSD 385
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
226-390 |
1.93e-08 |
|
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: 55.79 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 226 ILSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVGYG---DLENQL---KTGIADGNLEDCVKLVGFKPQEEIKRYLDE 299
Cdd:cd03792 200 ILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGavdDPEGSVvyeEVMEYAGDDHDIHVLRLPPSDQEINALQRA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 300 ADIFLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAaiLLKLSRGEDDIAQVV 379
Cdd:cd03792 280 ATVVLQLSTR------EGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAVR--ILRLLTDPELRRKMG 351
|
170
....*....|.
gi 501912241 380 LAARAKVETEF 390
Cdd:cd03792 352 LAAREHVRDNF 362
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
227-385 |
2.35e-07 |
|
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: 52.29 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 227 LSVARLTEKKGLAVAIEACKILKEQggqfeYTIVGYGDLENQLKtGIADGNledcVKLVGFKPQEEIKRYLDEADIFLLP 306
Cdd:cd03804 203 LTASRLVPYKRIDLAVEAFNELPKR-----LVVIGDGPDLDRLR-AMASPN----VEFLGYQPDEVLKELLSKARAFVFA 272
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501912241 307 sltaADGDMEGIPValmEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAK 385
Cdd:cd03804 273 ----AEEDFGIVPV---EAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEFEQNFDRFKPQAIRANAE 344
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
207-393 |
2.98e-07 |
|
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: 52.21 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 207 IEPEKFNLKLRDSLHQPLR--ILSVARLTEKKGLAVAIEACKILKEQGGQFE--YTIV--GYGD--LEN-----QLKtGI 273
Cdd:cd03805 193 FDSTSEDPDPGDLIAKSNKkfFLSINRFERKKNIALAIEAFAKLKQKLPEFEnvRLVIagGYDPrvAENveyleELQ-RL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 274 ADGNLEDCVKlVGFKPQ--EEIKRYLDEADIFLL--PSltaadgdME--GI-PValmEAMAVGLPVVSSrHSGIP-ELIE 345
Cdd:cd03805 272 AEELLNVEDQ-VLFLRSisDSQKEQLLSSALALLytPS-------NEhfGIvPL---EAMYAGKPVIAC-NSGGPlETVV 339
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501912241 346 HNVSGWLApEGDAQALAAILLKLSRGEDDIAQVVLAARAKVETEFNQH 393
Cdd:cd03805 340 EGVTGFLC-EPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSRE 386
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
324-391 |
1.98e-06 |
|
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: 49.21 E-value: 1.98e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 324 EAMAVGLPVVSSRHSGIPELIEHNVSGWLAP--EGDAQALAAIlLKLSRgeddiaqvvLAARAKVETEFN 391
Cdd:cd03802 259 EAMACGTPVIAYRRGGLPEVIQHGETGFLVDsvEEMAEAIANI-DRIDR---------AACRRYAEDRFS 318
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
234-407 |
3.31e-05 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 45.74 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 234 EKKGLAVAIEACKILKEQGgQFEYTIVGYGDLENQLKTGIADGNLEDCvKLVGFKPQEEIKRYLDEADIFLLPSLT-AAD 312
Cdd:PRK10307 240 EKQGLELVIDAARRLRDRP-DLIFVICGQGGGKARLEKMAQCRGLPNV-HFLPLQPYDRLPALLKMADCHLLPQKAgAAD 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 313 GDMegiPVALMEAMAVGLPVV--SSRHSGIPELIEHNvsGWLAPEGDAQALAAILLKLSRGEDDIAQVVLAARAKVETEF 390
Cdd:PRK10307 318 LVL---PSKLTNMLASGRNVVatAEPGTELGQLVEGI--GVCVEPESVEALVAAIAALARQALLRPKLGTVAREYAERTL 392
|
170
....*....|....*..
gi 501912241 391 NQHIAYRQLAEILERLA 407
Cdd:PRK10307 393 DKENVLRQFIADIRGLV 409
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
228-395 |
6.08e-05 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 45.41 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 228 SVARLTEKKGLAVAIEACKILKEQGGQFEYTIVGYGDLENQLKTGIADGNLEDCVKLVGFkpQEEIKRYLDEADIFLLPS 307
Cdd:PRK15179 522 TVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGL--SRRVGYWLTQFNAFLLLS 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 308 ltaadgDMEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPEGD------AQALAAIlLKLSRGEDDIAQVVlA 381
Cdd:PRK15179 600 ------RFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTvtapdvAEALARI-HDMCAADPGIARKA-A 671
|
170
....*....|....
gi 501912241 382 ARAKVETEFNQHIA 395
Cdd:PRK15179 672 DWASARFSLNQMIA 685
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
196-351 |
1.44e-04 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 43.63 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 196 PAEKINVTRMGIEPEKFNLKLRDSLHQPLRI-------LSVARLTEKKGLAVAIEACKILKEQGGQFEYTIVG------- 261
Cdd:PRK15484 159 PNADISIVPNGFCLETYQSNPQPNLRQQLNIspdetvlLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGdptassk 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 262 --YGDLENQLKTgIADGNLEDCVkLVGFKPQEEIKRYLDEADIFLLPSLTAadgdmEGIPVALMEAMAVGLPVVSSRHSG 339
Cdd:PRK15484 239 geKAAYQKKVLE-AAKRIGDRCI-MLGGQPPEKMHNYYPLADLVVVPSQVE-----EAFCMVAVEAMAAGKPVLASTKGG 311
|
170
....*....|..
gi 501912241 340 IPELIEHNVSGW 351
Cdd:PRK15484 312 ITEFVLEGITGY 323
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
206-365 |
1.68e-04 |
|
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274943 [Multi-domain] Cd Length: 373 Bit Score: 43.54 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 206 GIEPEKFNLKLRDSLHQPLRILSVARLTekkglaVAieackilkeqGGQfeyTIVGYGDLENQLKTGIADGNLE-DCVKL 284
Cdd:TIGR04047 201 GIEPRKNTIDLLEAFALLRARRPQAQLV------IA----------GGA---TLFDYDAYRREFRARAAELGVDpGPVVI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 285 VGFKPQEEIKRYLDEADIFLLPSLTaadgdmEGIPVALMEAMAVGLPVVSSRHSGIPELIEHNVSGW---LAPEGDAQAL 361
Cdd:TIGR04047 262 TGPVPDADLPALYRCADAFAFPSLK------EGFGLVVLEALASGIPVVASDIAPFTEYLGRFDAAWadpSDPDSIADAL 335
|
....
gi 501912241 362 AAIL 365
Cdd:TIGR04047 336 ALAL 339
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
322-404 |
2.22e-04 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 39.89 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 322 LMEAMAVGLPVVSSRHSGIPELIEHNVSGWLAPegDAQALAAILLKLSRGEDDIAQVVLAARAKVETEFNqhiaYRQ-LA 400
Cdd:pfam13524 16 VFEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHT----YAHrAE 89
|
....
gi 501912241 401 EILE 404
Cdd:pfam13524 90 QLLD 93
|
|
| GT4_TuaH-like |
cd04950 |
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this ... |
282-388 |
4.00e-04 |
|
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. 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.
Pssm-ID: 340856 [Multi-domain] Cd Length: 373 Bit Score: 42.36 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 282 VKLVGFKPQEEIKRYLDEADIFLLP-SLTAADGDMEgiPVALMEAMAVGLPVVSSRhsgIPELIEHNVSGWLApEGDAQA 360
Cdd:cd04950 255 IHWLGPKPYKELPAYLAGFDVALLPfALNEYTRFIS--PLKLFEYLAAGKPVVATS---IPSVVRFYGEAVLC-GDDPDE 328
|
90 100
....*....|....*....|....*....
gi 501912241 361 L-AAILLKLSRGEDDIAQVVLAARAKVET 388
Cdd:cd04950 329 FsAAIEKALALKGDARDKRLARALARQES 357
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
257-361 |
3.60e-03 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 39.68 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 257 YTIVGYGDLENQLKTGIADGNLEDCVKLVGFkpQEEIKRYLDEADIFLLPSltaadgDMEGIPVALMEAMAVGLPVVSSR 336
Cdd:PRK15490 432 FVLVGDGDLRAEAQKRAEQLGILERILFVGA--SRDVGYWLQKMNVFILFS------RYEGLPNVLIEAQMVGVPVISTP 503
|
90 100
....*....|....*....|....*
gi 501912241 337 HSGIPELIEHNVSGWLApeGDAQAL 361
Cdd:PRK15490 504 AGGSAECFIEGVSGFIL--DDAQTV 526
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
210-382 |
8.51e-03 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 38.31 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 210 EKFNLKLRDSlhQPLrILSVARLTEKKGLAVAIEACKILKEQGGQFeyTIVGYGD--LENQLKTgIADGNLEDCVKLVGF 287
Cdd:cd03791 284 KELGLPVDPD--APL-FGFVGRLTEQKGVDLILDALPELLEEGGQL--VVLGSGDpeYEQAFRE-LAERYPGKVAVVIGF 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501912241 288 KpqEEIKRYLDE-ADIFLLPS------LTAadgdmegipvalMEAMAVG-LPVVSS----RHSGIPE-LIEHNVSGWLAP 354
Cdd:cd03791 358 D--EALAHRIYAgADFFLMPSrfepcgLVQ------------MYAMRYGtLPIVRRtgglADTVFDYdPETGEGTGFVFE 423
|
170 180 190
....*....|....*....|....*....|.
gi 501912241 355 EGDAQALAAIL---LKLSRGEDDIAQVVLAA 382
Cdd:cd03791 424 DYDAEALLAALrraLALYRNPELWRKLQKNA 454
|
|
| |
