|
Name |
Accession |
Description |
Interval |
E-value |
| wcaL |
TIGR04005 |
colanic acid biosynthesis glycosyltransferase WcaL; This gene is one of the glycosyl ... |
1-406 |
0e+00 |
|
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: 849.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 1 MKVGFFLLKFPLSSETFVLNQITAFIDMGYDVEIVALQKGDTKNTHAAYTQYGLEAKTRWLQDEPAGKLSKLRYRASQTL 80
Cdd:TIGR04005 1 MKVSFFLLKFPLSSETFVLNQITAFIDMGYEVEIVALQKGDTQNTHAAWTEYNLAAKTRWLQDEPEGKLAKLRYRASQTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 81 RGIHRASTWRALNVSRYGSESRNLILSAICGQTAQPYRADVFIAHFGPAGVTAAKLRELGVIDGKIATIFHGIDISSREV 160
Cdd:TIGR04005 81 RGLFRASTWKALNMSRYGDESRNLILSAICGQVPQPFKADVFIAHFGPAGVTAAKLRELGVIDGKIATIFHGIDISSREV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 161 LNHYTPEYQQLFRRGDMMLPISDLWAGRLKSMGCPGEKIAVSRMGVDLTRFTRRPVKVPGTPLQIISVARLTEKKGLHVA 240
Cdd:TIGR04005 161 LNHYTPEYQQLFRRGDLMLPISDLWAGRLKAMGCPPEKIAVSRMGVDMTRFTHRPVKAPGTPLEIISVARLTEKKGLHVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 241 IEACRQLKARGVAFHYRILGIGPWERRLRTLIEQYQLDDVVEMPGFKPSHEVKAMLDEADVFLLPSVTGADGDMEGIPVA 320
Cdd:TIGR04005 241 IEACRQLKAQGVAFRYRILGIGPWERRLRTLIEQYQLEDVVEMPGFKPSHEVKAMLDDADVFLLPSVTGTDGDMEGIPVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 321 LMEAMAVGIPVVSTLHSGIPELIKSDHSGWLVPENNAMALADRLAAFSDIDQQALEPVLHNARQKVETDFNQQVINRQLA 400
Cdd:TIGR04005 321 LMEAMAVGIPVVSTVHSGIPELVEAGKSGWLVPENDAHALADRLAAFSRIDTQTLRPVLTRAREKVEADFNQQVINRQLA 400
|
....*.
gi 1452262053 401 SLLQTL 406
Cdd:TIGR04005 401 SLLQTL 406
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
2-399 |
7.60e-126 |
|
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: 367.16 E-value: 7.60e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 2 KVGFFLLKFPLSSETFVLNQITAFIDMGYDVEIVALQKGDTKNTHAAytqygleaktrwlqdepagklsklryrasqtlr 81
Cdd:cd03799 1 KIAFIVDEFPVLSETFILNQITGLIDRGHEVDIYAVNPGDLVKRHPD--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 82 gihrastwralnVSRYGSESRNLiLSAICGQTAQPYrADVFIAHFGPAGVTAAKLRELGVIDGKIATIFHGIDISSReVL 161
Cdd:cd03799 48 ------------VEKYNVPSLNL-LYAIVGLNKKGA-YDIIHCQFGPLGALGALLRRLKVLKGKLVTSFRGYDISMY-VI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 162 NHYTPEYQQLFRRGDMMLPISDLWAGRLKSMGCPGEKIAVSRMGVDLTRFTRRPVKVP-GTPLQIISVARLTEKKGLHVA 240
Cdd:cd03799 113 LEGNKVYPQLFAQGDLFLPNCELFKHRLIALGCDEKKIIVHRSGIDCNKFRFKPRYLPlDGKIRILTVGRLTEKKGLEYA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 241 IEACRQLKARGVAFHYRILGIGPWERRLRTLIEQYQLDDVVEMPGFKPSHEVKAMLDEADVFLLPSVTGADGDMEGIPVA 320
Cdd:cd03799 193 IEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTAADGDQDGPPNT 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1452262053 321 LMEAMAVGIPVVSTLHSGIPELIKSDHSGWLVPENNAMALADRLAAFSDiDQQALEPVLHNARQKVETDFNQQVINRQL 399
Cdd:cd03799 273 LKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIE-HPAIWPEMGKAGRARVEEEYDINKLNDEL 350
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-404 |
5.79e-47 |
|
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: 164.63 E-value: 5.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 2 KVGFFLLKFPLSS---ETFVLNQITAFIDMGYDVEIVALQKGDTKNTHAAYTQYGLEAKTRWLQDEPAGKLSKLRYRASQ 78
Cdd:cd03801 1 KILLLSPELPPPVggaERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 79 tlrgihrastwralnvsrygsesrnlilsaicgqtaqpYRADVFIAHFGPAGVTAAKLRELgvIDGKIATIFHGIDISSR 158
Cdd:cd03801 81 --------------------------------------RKFDVVHAHGLLAALLAALLALL--LGAPLVVTLHGAEPGRL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 159 EVLNHYTP----EYQQLFRRGDMMLPISDLWAGRLKSM-GCPGEKIAVSRMGVDLTRF---TRRPVKVPGTPLQIISVAR 230
Cdd:cd03801 121 LLLLAAERrllaRAEALLRRADAVIAVSEALRDELRALgGIPPEKIVVIPNGVDLERFsppLRRKLGIPPDRPVLLFVGR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 231 LTEKKGLHVAIEACRQLKARGVAFHYRILGI-GPWERRLRTLieQYQLDDVVEMPGFKPSHEVKAMLDEADVFLLPSVtg 309
Cdd:cd03801 201 LSPRKGVDLLLEALAKLLRRGPDVRLVIVGGdGPLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSR-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 310 adgdMEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDHSGWLVPENNAMALADRLAAFSDiDQQALEPVLHNARQKVETD 389
Cdd:cd03801 277 ----YEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLA-DPELRARLGRAARERVAER 351
|
410
....*....|....*
gi 1452262053 390 FNQQVINRQLASLLQ 404
Cdd:cd03801 352 FSWERVAERLLDLYR 366
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
114-366 |
3.79e-46 |
|
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: 162.62 E-value: 3.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 114 AQPYRADVFIAHFGPAGVTAAKL-RELGVidgKIATIFHGIDIS--------SREVLNHYTPEYQQLFRRGDMMLPISDL 184
Cdd:cd05844 77 AAGLAPALVHAHFGRDGVYALPLaRALGV---PLVVTFHGFDITtsrawlaaSPGWPSQFQRHRRALQRPAALFVAVSGF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 185 WAGRLKSMGCPGEKIAVSRMGVDLTRFtrRPVKVPGTPLQIISVARLTEKKGLHVAIEACRQLKARGVAFHYRILGIGPW 264
Cdd:cd05844 154 IRDRLLARGLPAERIHVHYIGIDPAKF--APRDPAERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 265 ERRLRTLIEQYqldDVVEMPGFKPSHEVKAMLDEADVFLLPSVTGADGDMEGIPVALMEAMAVGIPVVSTLHSGIPELIK 344
Cdd:cd05844 232 RPALQALAAAL---GRVRFLGALPHAEVQDWMRRAEIFCLPSVTAASGDSEGLGIVLLEAAACGVPVVSSRHGGIPEAIL 308
|
250 260
....*....|....*....|..
gi 1452262053 345 SDHSGWLVPENNAMALADRLAA 366
Cdd:cd05844 309 DGETGFLVPEGDVDALADALQA 330
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
221-367 |
2.63e-41 |
|
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: 143.18 E-value: 2.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 221 TPLQIISVARLTEKKGLHVAIEACRQLKARGVAFHYRILGIGPWERRLRTLIEQYQLDDVVEMPGFKPSHEVKAMLDEAD 300
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIAD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1452262053 301 VFLLPSVTgadgdmEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDHSGWLVPENNAMALADRLAAF 367
Cdd:pfam00534 81 VFVLPSRY------EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKL 141
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
14-365 |
1.67e-39 |
|
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: 144.83 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 14 SETFVLNQITAFIDMGYDVEIVALQKGDTKnthaaytqygLEAKTRWLQDEPagklsklryRASQTLRGIHRASTWRALN 93
Cdd:cd03798 16 RGIFVRRQVRALSRRGVDVEVLAPAPWGPA----------AARLLRKLLGEA---------VPPRDGRRLLPLKPRLRLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 94 VSRYGSESRNLILSAICGqtaqpyRADVFIAHFG-PAGVTAAKLRELGvidGKIATI-FHGIDISSREVLNHYTPEYQQL 171
Cdd:cd03798 77 APLRAPSLAKLLKRRRRG------PPDLIHAHFAyPAGFAAALLARLY---GVPYVVtEHGSDINVFPPRSLLRKLLRWA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 172 FRRGDMMLPISDLWAGRLKSMGCPGEKIAVSRMGVDLTRF---TRRPVKVPGTPLqIISVARLTEKKGLHVAIEACRQLK 248
Cdd:cd03798 148 LRRAARVIAVSKALAEELVALGVPRDRVDVIPNGVDPARFqpeDRGLGLPLDAFV-ILFVGRLIPRKGIDLLLEAFARLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 249 ARGVAFHYRILGIGPWERRLRTLIEQYQLDDVVEMPGFKPSHEVKAMLDEADVFLLPSVtgadgdMEGIPVALMEAMAVG 328
Cdd:cd03798 227 KARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSR------HEGFGLVLLEAMACG 300
|
330 340 350
....*....|....*....|....*....|....*..
gi 1452262053 329 IPVVSTLHSGIPELIKSDHSGWLVPENNAMALADRLA 365
Cdd:cd03798 301 LPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALR 337
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
117-399 |
3.57e-39 |
|
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: 143.50 E-value: 3.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 117 YRADVFIAHFGPAGV---TAAKLreLGVIdgKIATIFHG---IDISSREVLNHYTPEYQQLFRRGDMMLPISDLWAGRLK 190
Cdd:cd03808 80 EKPDIVHCHTPKPGIlgrLAARL--AGVP--KVIYTVHGlgfVFTEGKLLRLLYLLLEKLALLFTDKVIFVNEDDRDLAI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 191 SMG-CPGEKIAVSR-MGVDLTRFTRRPVKVPGTPLQIISVARLTEKKGLHVAIEACRQLKARGVAFHYRILGIGPWERRL 268
Cdd:cd03808 156 KKGiIKKKKTVLIPgSGVDLDRFQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPS 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 269 RTLIEQYQLDDVVEMPGFkpSHEVKAMLDEADVFLLPSvtgadgDMEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDHS 348
Cdd:cd03808 236 EILIEKLGLEGRIEFLGF--RSDVPELLAESDVFVLPS------YREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVN 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1452262053 349 GWLVPENNAMALADRLAAFSDIDQQALEpVLHNARQKVETDFNQQVINRQL 399
Cdd:cd03808 308 GFLVPPGDVEALADAIEKLIEDPELRKE-MGEAARKRVEEKFDEEKVVNKL 357
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
15-392 |
2.89e-34 |
|
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: 130.17 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 15 ETFVLNQITAFIDMGYDVEIVALQKGdtknthaaytqygleaktRWLQDEPAGKLSKLRYRASQTLRGihraSTWRALNV 94
Cdd:cd03811 15 ERVLLNLANALDKRGYDVTLVLLRDE------------------GDLDKQLNGDVKLIRLLIRVLKLI----KLGLLKAI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 95 SRYGSESRNlilsaicgqtAQPyraDVFIAHFGPAGVTAAKLRELGVidgKIATIFHGiDISSREVLNHYTPEYQQLFRR 174
Cdd:cd03811 73 LKLKRILKR----------AKP---DVVISFLGFATYIVAKLAAARS---KVIAWIHS-SLSKLYYLKKKLLLKLKLYKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 175 GDMMLPISDLWAGRL-KSMGCPGEKIAVSRMGVDLTRFTRRPVKV----PGTPLQIISVARLTEKKGLHVAIEACRQLKA 249
Cdd:cd03811 136 ADKIVCVSKGIKEDLiRLGPSPPEKIEVIYNPIDIDRIRALAKEPilnePEDGPVILAVGRLDPQKGHDLLIEAFAKLRK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 250 RGVAFHYRILGIGPWERRLRTLIEQYQLDDVVEMPGFKPshEVKAMLDEADVFLLPSVTgadgdmEGIPVALMEAMAVGI 329
Cdd:cd03811 216 KYPDVKLVILGDGPLREELEKLAKELGLAERVIFLGFQS--NPYPYLKKADLFVLSSRY------EGFPNVLLEAMALGT 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1452262053 330 PVVSTLHSGIPELIKSDHSGWLVPENNAMALADRLAAFSD-IDQQALEPVLHNARQKVETDFNQ 392
Cdd:cd03811 288 PVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQkKLDAALRERLAKAQEAVFREYTI 351
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
225-366 |
5.89e-30 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 112.60 E-value: 5.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 225 IISVARLTEK-KGLHVAIEACRQLKARGVAFHYRILGIGPwERRLRTLIEQyqLDDVVEMPGFKPshEVKAMLDEADVFL 303
Cdd:pfam13692 4 ILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVGDGP-EEELEELAAG--LEDRVIFTGFVE--DLAELLAAADVFV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1452262053 304 LPSVTgadgdmEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDHsGWLVPENNAMALADRLAA 366
Cdd:pfam13692 79 LPSLY------EGFGLKLLEAMAAGLPVVATDVGGIPELVDGEN-GLLVPPGDPEALAEAILR 134
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
117-362 |
4.57e-26 |
|
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: 107.44 E-value: 4.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 117 YRADVFIAH-FGPAGVTAAKLRELGVidgKIATIFHGIDISSrevlNHYTPEYQQLFRRGDMMLPISDLWAGRL-KSMGC 194
Cdd:cd03819 75 ERIDLIHAHsRAPAWLGWLASRLTGV---PLVTTVHGSYLAT----YHPKDFALAVRARGDRVIAVSELVRDHLiEALGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 195 PGEKIAVSRMGVDLTRFT-------RRPVKVPGTPLQIISVARLTEKKGLHVAIEACRQLKARgVAFHYRILGIGPWERR 267
Cdd:cd03819 148 DPERIRVIPNGVDTDRFPpeaeaeeRAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDE-PDFRLLVAGDGPERDE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 268 LRTLIEQYQLDDVVEMPGFKpsHEVKAMLDEADVFLLPSVTgadgdmEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDH 347
Cdd:cd03819 227 IRRLVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSLH------EEFGRVALEAMACGTPVVATDVGGAREIVVHGR 298
|
250
....*....|....*
gi 1452262053 348 SGWLVPENNAMALAD 362
Cdd:cd03819 299 TGLLVPPGDAEALAD 313
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
171-403 |
4.46e-25 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 105.09 E-value: 4.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 171 LFRRGDMMLPISDLWAGRLKSMGCPGEKIAVSRMGVDLTRF---------TRRPVKVPGTPLQIISVARLTEKKGLHVAI 241
Cdd:cd03807 130 LSKFSPATVANSSAVAEFHQEQGYAKNKIVVIYNGIDLFKLspddasrarARRRLGLAEDRRVIGIVGRLHPVKDHSDLL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 242 EACRQLKARGVAFHYRILGIGPWERRLRTLIEQYQLDDVVEMPGfkPSHEVKAMLDEADVFLLPSVTgadgdmEGIPVAL 321
Cdd:cd03807 210 RAAALLVETHPDLRLLLVGRGPERPNLERLLLELGLEDRVHLLG--ERSDVPALLPAMDIFVLSSRT------EGFPNAL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 322 MEAMAVGIPVVSTLHSGIPELIKsDHSGWLVPENNAMALAD---RLAAFSDIDQQALEpvlhNARQKVETDFNQQVINRQ 398
Cdd:cd03807 282 LEAMACGLPVVATDVGGAAELVD-DGTGFLVPAGDPQALADairALLEDPEKRARLGR----AARERIANEFSIDAMVRR 356
|
....*
gi 1452262053 399 LASLL 403
Cdd:cd03807 357 YETLY 361
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
114-352 |
1.35e-22 |
|
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: 95.55 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 114 AQPYRADVFIAHFGPAGVTAAkLRELGVIDGKIATIFHGIDISSREVLNHYTPEYqqlfrrgdmmlpisdlwagrlksmg 193
Cdd:cd01635 50 LLELKPDVVHAHSPHAAALAA-LLAARLLGIPIVVTVHGPDSLESTRSELLALAR------------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 194 cpgekIAVSRMGVDLtrftrrpvkvpgtplqiISVARLTEKKGLHVAIEACRQLKARGVAFHYRILGIGPWERRLRTLIE 273
Cdd:cd01635 104 -----LLVSLPLADK-----------------VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 274 QYQLDDVVEMPGFKPSHEVKAMLDE-ADVFLLPSVTgadgdmEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDHSGWLV 352
Cdd:cd01635 162 ALGLLERVVIIGGLVDDEVLELLLAaADVFVLPSRS------EGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
205-388 |
2.30e-22 |
|
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: 97.35 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 205 GVDLTRF-------TRRPVKVPGTPLQIISVARLTEKKGLHVAIEACRQLKARgVAFHYRILGIGPWERRLRTLIEQYQL 277
Cdd:cd03817 177 GIDLDKFekplnteERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKE-PNIKLVIVGDGPEREELKELARELGL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 278 DDVVEMPGFKPSHEVKAMLDEADVFLLPSVTgadgdmEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDHSGWLVPENNA 357
Cdd:cd03817 256 ADKVIFTGFVPREELPEYYKAADLFVFASTT------ETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDE 329
|
170 180 190
....*....|....*....|....*....|....*...
gi 1452262053 358 MA------LADRLAAFSDIDQQALEPVLHNAR-QKVET 388
Cdd:cd03817 330 TLaekllhLRENLELLRKLSKNAEISAREFAFaKSVEK 367
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
225-367 |
3.94e-22 |
|
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: 96.54 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 225 IISVARLTEKKGLHVAIEACRQLKARGVAFHYRILGIGPWERRLRTLIEQYQLDDVVEMPGfkPSHEVKAMLDEADVFLL 304
Cdd:cd03820 184 ILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLG--PTKNIAEEYANSSIFVL 261
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1452262053 305 PSvtgadgDMEGIPVALMEAMAVGIPVVST-LHSGIPELIKSDHSGWLVPENNAMALADRLAAF 367
Cdd:cd03820 262 SS------RYEGFPMVLLEAMAYGLPIISFdCPTGPSEIIEDGENGLLVPNGDVDALAEALLRL 319
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
292-406 |
7.10e-22 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 90.05 E-value: 7.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 292 VKAMLDEADVFLLPSVTgadgdmEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDHSGWLVPENNAMALADRLAAFSDiD 371
Cdd:COG0438 14 LEALLAAADVFVLPSRS------EGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLE-D 86
|
90 100 110
....*....|....*....|....*....|....*
gi 1452262053 372 QQALEPVLHNARQKVETDFNQQVINRQLASLLQTL 406
Cdd:COG0438 87 PELRRRLGEAARERAEERFSWEAIAERLLALYEEL 121
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
143-394 |
7.21e-22 |
|
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: 96.38 E-value: 7.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 143 DGKIATIFHGIDISSREVLNHYTPEYQQLFRRGDMMLPISDlwAGRLKSMGC---PGEKIAVSRMGVDLTRFTRRPVKVP 219
Cdd:cd04946 146 RDVVISRAHRYDLYEDQYGSYYLPLREYLVSYLDAVFLISK--EGKDYLQKCypaYKEKIFVSRLGVSDKEQYSKVKKEG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 220 GtpLQIISVARLTEKKGLHVAIEACRQL--KARGVAFHYRILGIGPWERRLRTLIEQYQLDDVVEMPGFKPSHEVKA--M 295
Cdd:cd04946 224 D--LRLVSCSSIVPVKRIDLIIETLNSLcvAHPSICISWTHIGGGPLKERLEKLAENKLENVKVNFTGEVSNKEVKQlyK 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 296 LDEADVFLLPSVTgadgdmEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDHSGWLVPENNA-MALADRLAAFSDIDQQa 374
Cdd:cd04946 302 ENDVDVFVNVSES------EGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLLLDKDPTpNEIVSSIMKFYLDGGD- 374
|
250 260
....*....|....*....|
gi 1452262053 375 LEPVLHNARQKVETDFNQQV 394
Cdd:cd04946 375 YKTMKISARECWEERFNAEV 394
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
194-389 |
4.42e-21 |
|
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.
Pssm-ID: 340848 [Multi-domain] Cd Length: 377 Bit Score: 93.97 E-value: 4.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 194 CPGEKIAVSRMGVDLTRF---TRRPVKVPGTPLQ--IISVARLTEKKGLHVAIEACRQLKARGVAFHYRILGIGP-WERR 267
Cdd:cd03821 171 GLEPPIAVIPNGVDIPEFdpgLRDRRKHNGLEDRriILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDgAYPA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 268 LRTLIEQYQLDDVVEMPGFKPSHEVKAMLDEADVFLLPSVTgadgdmEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDh 347
Cdd:cd03821 251 FLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYS------ENFGNVVAEALACGLPVVITDKCGLSELVEAG- 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1452262053 348 SGWLVpENNAMALADRLAAFSDI--DQQALEPVLHNARQKVETD 389
Cdd:cd03821 324 CGVVV-DPNVSSLAEALAEALRDpaDRKRLGEMARRARQVEENF 366
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
170-389 |
2.12e-19 |
|
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: 88.54 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 170 QLFRRGDMMLPISDLWAGRLKSMGCPGEKIAVSRMGVDLTRFTRRPVKVPGTPLQIISVARLTEKKGLHVAIEACRQLKA 249
Cdd:cd03823 139 LFKKGGDAVLAPSRFTANLHEANGLFSARISVIPNAVEPDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLPR 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 250 RGVAFHyrILGIGPWERrlrtlIEQYQLDDVVEMPGFKPSHEVKAMLDEADVFLLPSVTgadgdMEGIPVALMEAMAVGI 329
Cdd:cd03823 219 EDIELV--IAGHGPLSD-----ERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIW-----PEPFGLVVREAIAAGL 286
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1452262053 330 PVVSTLHSGIPELIKSDHSGWLVPENNAMALADRLAAFsdIDQQALEPVLH-NARQKVETD 389
Cdd:cd03823 287 PVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRL--LTDPALLERLRaGAEPPRSTE 345
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
104-398 |
2.82e-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: 82.78 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 104 LILSAICGQTAQPYRADVFIAHFG-PAGVTAAKLRELGVIDGKIATIFHGIDISsrevLNHYTPEYQQLFR----RGDMM 178
Cdd:cd04962 70 LALASKIVEVAKEHKLDVLHAHYAiPHASCAYLAREILGEKIPIVTTLHGTDIT----LVGYDPSLQPAVRfsinKSDRV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 179 LPISDLWAGRLKSMGCPGEKIAVSRMGVDLTRFTRRPvkvpGTPLQIISVARLTEKKGLHVAieACRQLK---------- 248
Cdd:cd04962 146 TAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKP----AGALKRRLLAPPDEKVVIHVS--NFRPVKriddvvrvfa 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 249 --ARGVAFHYRILGIGPWERRLRTLIEQYQLDDVVEMPGFKPshEVKAMLDEADVFLLPSVTgadgdmEGIPVALMEAMA 326
Cdd:cd04962 220 rvRRKIPAKLLLVGDGPERVPAEELARELGVEDRVLFLGKQD--DVEELLSIADLFLLPSEK------ESFGLAALEAMA 291
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1452262053 327 VGIPVVSTLHSGIPELIKSDHSGWLVPENNAMALADRlaAFSDIDQQALEPVL-HNARQKVETDFNQQVINRQ 398
Cdd:cd04962 292 CGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKS--ALSILEDDELYNRMgRAARKRAAERFDPERIVPQ 362
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
170-406 |
5.96e-17 |
|
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: 81.61 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 170 QLFRRGDMMLPISDLWAGRL--KSMGCPGEKIAVSRMGVDLTRFT-------RRPVKVPGTPLQIISVARLTEK--KGLH 238
Cdd:cd03825 132 EALAKKRLTIVAPSRWLADMvrRSPLLKGLPVVVIPNGIDTEIFApvdkakaRKRLGIPQDKKVILFGAESVTKprKGFD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 239 VAIEACRQLkargvAFHYRILG--IGPWERRLRTL----IEQYQLDDVVEMpgfkpsHEVKAMldeADVFLLPSVtgadg 312
Cdd:cd03825 212 ELIEALKLL-----ATKDDLLLvvFGKNDPQIVILpfdiISLGYIDDDEQL------VDIYSA---ADLFVHPSL----- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 313 dMEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDHSGWLVPENNAMALADRLAAFSDIDQQALEpVLHNARQKVETDFNQ 392
Cdd:cd03825 273 -ADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERES-LGERARALAENHFDQ 350
|
250
....*....|....
gi 1452262053 393 QVINRQLASLLQTL 406
Cdd:cd03825 351 RVQAQRYLELYKDL 364
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
24-400 |
9.53e-17 |
|
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: 81.23 E-value: 9.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 24 AFIDMGYDVEIVALQ-KGDTKNTHAAYTQYGLEAKTRWLqdepagklsKLRYRASQTLRGihrastwRALNVSRYGSESR 102
Cdd:cd03794 26 ELVRRGHEVTVLTPSpNYPLGRIFAGATETKDGIRVIRV---------KLGPIKKNGLIR-------RLLNYLSFALAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 103 NLILSAIcgqtaqpYRADVFIAH-----FGPAGVTAAKLRelgvidgKIATIFH--------GID---ISSREVLNHYTP 166
Cdd:cd03794 90 LKLLVRE-------ERPDVIIAYsppitLGLAALLLKKLR-------GAPFILDvrdlwpesLIAlgvLKKGSLLKLLKK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 167 EYQQLFRRGDMMLPISDLWAGRLKSMGCPGEKIAVSRMGVDLTRFTR------RPVKVPGTPLQIISVARLTEKKGLHVA 240
Cdd:cd03794 156 LERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPppkdelRKKLGLDDKFVVVYAGNIGKAQGLETL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 241 IEACRQLKAR-GVAFHyrILGIGPWERRLRTLIEQYQLDDVVEMPgFKPSHEVKAMLDEADVFLLPSVTGADGDMeGIPV 319
Cdd:cd03794 236 LEAAERLKRRpDIRFL--FVGDGDEKERLKELAKARGLDNVTFLG-RVPKEEVPELLSAADVGLVPLKDNPANRG-SSPS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 320 ALMEAMAVGIPVVSTLHSGIPELIKSDHSGWLVPENNAMALADRLAAFSDiDQQALEPVLHNARQKVETDFNQQVINRQL 399
Cdd:cd03794 312 KLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLD-DPELRRAMGENGRELAEEKFSREKLADRL 390
|
.
gi 1452262053 400 A 400
Cdd:cd03794 391 L 391
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
114-401 |
9.75e-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: 81.13 E-value: 9.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 114 AQPYRADVFIAHFGPAGVTAAKLRE-LGVidgKIATIFHGIDISSREVLNHY-TPEY-------QQLFRRGDMMLP---- 180
Cdd:cd03800 97 REGGRYDLIHSHYWDSGLVGALLARrLGV---PLVHTFHSLGRVKYRHLGAQdTYHPslritaeEQILEAADRVIAstpq 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 181 -ISDLWAgrlkSMGCPGEKIAVSRMGVDLTRFT--------RRPVKVPGTPLQIISVARLTEKKGLHVAIEACRQLKARG 251
Cdd:cd03800 174 eADELIS----LYGADPSRINVVPPGVDLERFFpvdraearRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 252 vAFHYRILGIGPW-------ERRLRTLIEQYQLDDVVEMPGFKPSHEVKAMLDEADVFLLPSVTGADGdmegipVALMEA 324
Cdd:cd03800 250 -ELANLVLVGGPSddplsmdREELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFG------LTAIEA 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1452262053 325 MAVGIPVVSTLHSGIPELIKSDHSGWLVPENNAMALADRLAAFsdIDQQALEPVL-HNARQKVETDFNQQVINRQLAS 401
Cdd:cd03800 323 MACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRL--LDDPALWQRLsRAGLERARAHYTWESVADQLLT 398
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
197-346 |
1.06e-15 |
|
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: 78.05 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 197 EKIAVSRMGVDLTRFTRRPVKVPGTPLQIISVARLTEKKGLHVAIEACRQLKARGVAFHYRILGIGPWERRLRTLIEQYQ 276
Cdd:cd03796 168 RIVSVIPNAVDSSDFTPDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMREKYQ 247
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 277 LDDVVEMPGFKPSHEVKAMLDEADVFLLPSVTgadgdmEGIPVALMEAMAVGIPVVSTLHSGIPELIKSD 346
Cdd:cd03796 248 LQDRVELLGAVPHEEVRDVLVQGHIFLNTSLT------EAFCIAIVEAASCGLLVVSTRVGGIPEVLPPD 311
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
225-364 |
1.29e-15 |
|
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: 77.34 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 225 IISVARLTEKKGLHVAIEACRQLKAR--GVAFHyrILGIGPWERRLRTLIEQYQLDDVVEMPGF--KPSHEVKamldEAD 300
Cdd:cd04949 163 IITISRLAPEKQLDHLIEAVAKAVKKvpEITLD--IYGYGEEREKLKKLIEELHLEDNVFLKGYhsNLDQEYQ----DAY 236
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1452262053 301 VFLLPSvtgadgDMEGIPVALMEAMAVGIPVVS-TLHSGIPELIKSDHSGWLVPENNAMALADRL 364
Cdd:cd04949 237 LSLLTS------QMEGFGLTLMEAIGHGLPVVSyDVKYGPSELIEDGENGYLIEKNNIDALADKI 295
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
217-390 |
6.77e-14 |
|
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: 72.31 E-value: 6.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 217 KVPGTPLqIISVARLTEKKGLHVAIEACRQLKARGVafhyrILGIGPWERRLRTLIEQYQLDDvVEMPGFKPSHEVKAML 296
Cdd:cd03795 187 EKKGKKI-FLFIGRLVYYKGLDYLIEAAQYLNYPIV-----IGGEGPLKPDLEAQIELNLLDN-VKFLGRVDDEEKVIYL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 297 DEADVFLLPSVTGAdgdmEGIPVALMEAMAVGIPVVST-LHSGIPELIKSDHSGWLVPENNAMALADRLAAFSDiDQQAL 375
Cdd:cd03795 260 HLCDVFVFPSVLRS----EAFGIVLLEAMMCGKPVISTnIGTGVPYVNNNGETGLVVPPKDPDALAEAIDKLLS-DEELR 334
|
170
....*....|....*
gi 1452262053 376 EPVLHNARQKVETDF 390
Cdd:cd03795 335 ESYGENAKKRFEELF 349
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
193-397 |
3.03e-13 |
|
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: 70.83 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 193 GCPGEKIAVSRMGVDLTRFT----RRPvkvPGTPLQIISVARLTEKKGLHVAIEACRQLKARGVAFHYRIlgIGP----- 263
Cdd:cd03813 263 GADPDKTRVIPNGIDIQRFApareERP---EKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWL--IGPededp 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 264 -WERRLRTLIEQYQLDDVVEMPGFKpshEVKAMLDEADVFLLPSVTgadgdmEGIPVALMEAMAVGIPVVSTLHSGIPEL 342
Cdd:cd03813 338 eYAQECKRLVASLGLENKVKFLGFQ---NIKEYYPKLGLLVLTSIS------EGQPLVILEAMASGVPVVATDVGSCREL 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1452262053 343 I-----KSDHSGWLVPENNAMALADRLAAFSDiDQQALEPVLHNARQKVETDFN-QQVINR 397
Cdd:cd03813 409 IygaddALGQAGLVVPPADPEALAEALIKLLR-DPELRQAFGEAGRKRVEKYYTlEGMIDS 468
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
205-400 |
1.12e-12 |
|
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: 68.86 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 205 GVDLTRFT--------RRPVKVPGTPLqIISVARLTEKKGLHVAIEACRQLKARgVAFHYRILGIGPWERRLRTlieqyQ 276
Cdd:cd03814 174 GVDTELFHpsrrdaalRRRLGPPGRPL-LLYVGRLAPEKNLEALLDADLPLAAS-PPVRLVVVGDGPARAELEA-----R 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 277 LDDVVeMPGFKPSHEVKAMLDEADVFLLPSVTGADGdmegipVALMEAMAVGIPVVSTLHSGIPELIKSDHSGWLVPENN 356
Cdd:cd03814 247 GPDVI-FTGFLTGEELARAYASADVFVFPSRTETFG------LVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGD 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1452262053 357 AMALADRLAAFsDIDQQALEPVLHNARQKVEtDFNQQVINRQLA 400
Cdd:cd03814 320 AAAFAAALRAL-LEDPELRRRMAARARAEAE-RYSWEAFLDNLL 361
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
187-395 |
3.78e-12 |
|
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: 67.08 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 187 GRLKSMGCPGekiavsrmGVDLTRFTRRPVKVPGTPLQ---------IISVARLTEKKGLHVAIEACRQLKARGVAFHYR 257
Cdd:cd04951 152 SKNKSVPVYN--------GIDLNKFKKDINVRLKIRNKlnlkndefvILNVGRLTEAKDYPNLLLAISELILSKNDFKLL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 258 ILGIGPWERRLRTLIEQYQLDDVVEMPGFKpSHeVKAMLDEADVFLLPSvtgadgDMEGIPVALMEAMAVGIPVVSTLHS 337
Cdd:cd04951 224 IAGDGPLRNELERLICNLNLVDRVILLGQI-SN-ISEYYNAADLFVLSS------EWEGFGLVVAEAMACERPVVATDAG 295
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1452262053 338 GIPELIkSDHSgWLVPENNAMALADRLAAFSDIDQQAlEPVLHNARQKVETDFNQQVI 395
Cdd:cd04951 296 GVAEVV-GDHN-YVVPVSDPQLLAEKIKEIFDMSDEE-RDILGNKNEYIAKNFSINTI 350
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
189-365 |
2.71e-11 |
|
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: 64.31 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 189 LKSMGCPGEKIAVSRMGVDLtRFTRRPVKVPGTPLQ------IISVARLTEKKGLHVAIEACRQLKARGVAFHYRILGIG 262
Cdd:cd03809 154 IKFYGVPPEKIVVIPLGVDP-SFFPPESAAVLIAKYllpepyFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 263 PWE-RRLRTLIEQYQLDDVVEMPGFKPSHEVKAMLDEADVFLLPSVtgadgdME--GIPVAlmEAMAVGIPVV-STLHSg 338
Cdd:cd03809 233 GWEdEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSL------YEgfGLPVL--EAMACGTPVIaSNISV- 303
|
170 180
....*....|....*....|....*..
gi 1452262053 339 IPElIKSDHsGWLVPENNAMALADRLA 365
Cdd:cd03809 304 LPE-VAGDA-ALYFDPLDPESIADAIL 328
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
105-366 |
1.27e-10 |
|
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: 62.41 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 105 ILSAICGQTAQPYRA-DVFIAHFGPAGVTAAKLRELGVIDGKIATIFHgidissrevLNHY-TPEYQQL----FRRGDMM 178
Cdd:TIGR04047 72 IARSIDHLRAHFARGfDVVHAQDCISGNALATLRAEGLIPGFVRTVHH---------LDDFdDPRLAACqeraIVEADAV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 179 LPISDLWAGRLKSmgcpGEKIAVSRM--GVDLTRFTRRPVKVP----------GTPLqIISVARLTEKKGLHVAIEACRQ 246
Cdd:TIGR04047 143 LCVSAAWAAELRA----EWGIDATVVpnGVDAARFSPAADAADaalrrrlglrGGPY-VLAVGGIEPRKNTIDLLEAFAL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 247 LKAR---------GVA--FHYRilgigPWERRLRTLIEQYQLD-DVVEMPGFKPSHEVKAMLDEADVFLLPSVTgadgdm 314
Cdd:TIGR04047 218 LRARrpqaqlviaGGAtlFDYD-----AYRREFRARAAELGVDpGPVVITGPVPDADLPALYRCADAFAFPSLK------ 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1452262053 315 EGIPVALMEAMAVGIPVVSTLHSGIPELIKSDHSGW---LVPENNAMALADRLAA 366
Cdd:TIGR04047 287 EGFGLVVLEALASGIPVVASDIAPFTEYLGRFDAAWadpSDPDSIADALALALDP 341
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
171-388 |
5.46e-09 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 57.80 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 171 LFRRGDMMLPISDLWAGRLKSMGC-PGEKIAVSRMGVDLTRF----------TRRPVKVPGTPLqIISVARLTEKKGLHV 239
Cdd:PLN02871 202 LHRAADLTLVTSPALGKELEAAGVtAANRIRVWNKGVDSESFhprfrseemrARLSGGEPEKPL-IVYVGRLGAEKNLDF 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 240 AIEACRQLKARGVAFhyriLGIGPWERRLrtliEQYQLDDVVEMPGFKPSHEVKAMLDEADVFLLPSvtgadgDMEGIPV 319
Cdd:PLN02871 281 LKRVMERLPGARLAF----VGDGPYREEL----EKMFAGTPTVFTGMLQGDELSQAYASGDVFVMPS------ESETLGF 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1452262053 320 ALMEAMAVGIPVVSTLHSGIPELIKSDH---SGWLVPENNAMALADRLAAFSDiDQQALEPVLHNARQKVET 388
Cdd:PLN02871 347 VVLEAMASGVPVVAARAGGIPDIIPPDQegkTGFLYTPGDVDDCVEKLETLLA-DPELRERMGAAAREEVEK 417
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
170-406 |
2.03e-08 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 55.75 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 170 QLFRRGDMMLPISDLWAGRLKSMGCPGEKIAVSRMGVDLTRFTRRPVK----------VPGTPLQIISVARLTEKKGLHV 239
Cdd:PRK10307 167 SLLRRFDNVSTISRSMMNKAREKGVAAEKVIFFPNWSEVARFQPVADAdvdalraqlgLPDGKKIVLYSGNIGEKQGLEL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 240 AIEACRQLKARGvAFHYRILGIGPWERRLRTLIEQYQLDDVVEMPgFKPSHEVKAMLDEADVFLLPSVTG-ADGDMegiP 318
Cdd:PRK10307 247 VIDAARRLRDRP-DLIFVICGQGGGKARLEKMAQCRGLPNVHFLP-LQPYDRLPALLKMADCHLLPQKAGaADLVL---P 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 319 VALMEAMAVGIPVVST--LHSGIPELIKSdhSGWLVPENNAMALADRLAAFSdiDQQALEPVLHN-ARQKVETDFNQQVI 395
Cdd:PRK10307 322 SKLTNMLASGRNVVATaePGTELGQLVEG--IGVCVEPESVEALVAAIAALA--RQALLRPKLGTvAREYAERTLDKENV 397
|
250
....*....|.
gi 1452262053 396 NRQLASLLQTL 406
Cdd:PRK10307 398 LRQFIADIRGL 408
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
195-406 |
2.62e-08 |
|
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: 54.99 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 195 PGEKIAVSRMGVDLTRFtrRPVKVPGTPLqiISVARLTEKKGLHVAIEACRQLKArgvafHYRILGIGPWERRLRTLIEQ 274
Cdd:cd03802 146 PIDYLTVVHNGLDPADY--RFQPDPEDYL--AFLGRIAPEKGLEDAIRVARRAGL-----PLKIAGKVRDEDYFYYLQEP 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 275 YQLDDVVEMpGFKPSHEVKAMLDEADVFLLPSV-TGADGdmegipVALMEAMAVGIPVVSTLHSGIPELIKSDHSGWLVP 353
Cdd:cd03802 217 LPGPRIEFI-GEVGHDEKQELLGGARALLFPINwDEPFG------LVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVD 289
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1452262053 354 enNAMALADRLAAFSDIDQQAlepvlhnARQKVETDFNQQVINRQLASLLQTL 406
Cdd:cd03802 290 --SVEEMAEAIANIDRIDRAA-------CRRYAEDRFSAARMADRYEALYRKV 333
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
227-404 |
7.81e-08 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 54.27 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 227 SVARLTEKKGLHVAIEACRQLKARGVAFHYRILGIGPWERRLRTLIEQYQLDDVVEMPGFkpSHEVKAMLDEADVFLLPS 306
Cdd:PRK15179 522 TVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGL--SRRVGYWLTQFNAFLLLS 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 307 vtgadgDMEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDHSGWLVPENNAMA--LADRLAafSDIDQQALEPVL-HNAR 383
Cdd:PRK15179 600 ------RFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTApdVAEALA--RIHDMCAADPGIaRKAA 671
|
170 180
....*....|....*....|.
gi 1452262053 384 QKVETDFNqqvINRQLASLLQ 404
Cdd:PRK15179 672 DWASARFS---LNQMIASTVR 689
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
207-403 |
7.87e-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: 53.86 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 207 DLTRFTRRPVKVPGTPLQIISVARLTEKKGLHVAIEACRQLKARGVAFHYRILGIGP-----WERRLRTLIEqYQLDD-- 279
Cdd:cd03792 182 DIRYYLEKPFVIDPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGAvddpeGSVVYEEVME-YAGDDhd 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 280 --VVEMPgfkPSH-EVKAMLDEADVFLLPSVTgadgdmEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDHSGWLV--PE 354
Cdd:cd03792 261 ihVLRLP---PSDqEINALQRAATVVLQLSTR------EGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVnsVE 331
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1452262053 355 NNAMALADRLAafsdiDQQALEPVLHNARQKVETDFnqqVINRQLASLL 403
Cdd:cd03792 332 GAAVRILRLLT-----DPELRRKMGLAAREHVRDNF---LITGNLRAWL 372
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
178-376 |
2.11e-07 |
|
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: 52.39 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 178 MLPISDLWAGRLKsmGCPGEKIAVSRMGVDLTRFTRRPVK-----VPGTPLqIISVARLTEKKGLHVAIEACRQLKARGV 252
Cdd:cd03822 141 MAPISRFLLVRIK--LIPAVNIEVIPHGVPEVPQDPTTALkrlllPEGKKV-ILTFGFIGPGKGLEILLEALPELKAEFP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 253 AFHYRILGiGPWERRLRTLIEQYQ--------LDDVVEMP-GFKPSHEVKAMLDEADVFLLP---SVTGADGdmegipvA 320
Cdd:cd03822 218 DVRLVIAG-ELHPSLARYEGERYRkaaieelgLQDHVDFHnNFLPEEEVPRYISAADVVVLPylnTEQSSSG-------T 289
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1452262053 321 LMEAMAVGIPVVSTLHSGIPELIKSDhSGWLVPENNAMALADRLAAF--SDIDQQALE 376
Cdd:cd03822 290 LSYAIACGKPVISTPLRHAEELLADG-RGVLVPFDDPSAIAEAILRLleDDERRQAIA 346
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
198-400 |
2.96e-07 |
|
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: 51.98 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 198 KIAVSRMGVDLTRF----TRRPVKVPGTPLQ-----IISVARLTEK-KGLHVAIEACRQLKARGVAFHYRILG------- 260
Cdd:cd03818 180 RISVIHDGVDTDRLapdpAARLRLLNGTELKagdpvITYVARNLEPyRGFHVFMRALPRIQARRPDARVVVVGgdgvsyg 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 261 -----IGPWERRLrtlIEQYQLDDV-VEMPGFKPSHEVKAMLDEADV---FLLPSVTGAdgdmegipvALMEAMAVGIPV 331
Cdd:cd03818 260 spppdGGSWKQKM---LAELGVDLErVHFVGKVPYDQYVRLLQLSDAhvyLTYPFVLSW---------SLLEAMACGCPV 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 332 VSTLHSGIPELIKSDHSGWLVPENNAMALADRLAAFSDiDQQALEPVLHNARQKVE-TDFNQQVINRQLA 400
Cdd:cd03818 328 IGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLE-DPDRAAALRRAARRTVErSDSLDVCLARYLA 396
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
226-377 |
6.42e-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: 50.75 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 226 ISVARLTEKKGLHVAIEACRQLKARGVafhyrILGIGPWERRLRTLieqyqLDDVVEMPGFKPSHEVKAMLDEADVFLLP 305
Cdd:cd03804 203 LTASRLVPYKRIDLAVEAFNELPKRLV-----VIGDGPDLDRLRAM-----ASPNVEFLGYQPDEVLKELLSKARAFVFA 272
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1452262053 306 SVtgadgdmEGIPVALMEAMAVGIPVVSTLHSGIPELIKSDHSGWLVPENNAMALADRLAAFSDIdQQALEP 377
Cdd:cd03804 273 AE-------EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEFEQN-FDRFKP 336
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
206-399 |
1.70e-06 |
|
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: 49.89 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 206 VDLTRFT--------RRPVKVPGTPLqIISVARLTEKKGLHVAIEACRQLKARGVAF-HYRILGIGPWERRLRTLIEQYQ 276
Cdd:cd03805 188 VDTDSFDstsedpdpGDLIAKSNKKF-FLSINRFERKKNIALAIEAFAKLKQKLPEFeNVRLVIAGGYDPRVAENVEYLE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 277 -LDDVVEmpgfkpshevKAMLDEADVFLLPSVTGADGDM--------------E--GI-PValmEAMAVGIPVVSTlHSG 338
Cdd:cd03805 267 eLQRLAE----------ELLNVEDQVLFLRSISDSQKEQllssalallytpsnEhfGIvPL---EAMYAGKPVIAC-NSG 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1452262053 339 IP-ELIKSDHSGWLVpENNAMALADRLAAFSdIDQQALEPVLHNARQKVETDFNQQVINRQL 399
Cdd:cd03805 333 GPlETVVEGVTGFLC-EPTPEAFAEAMLKLA-NDPDLADRMGAAGRKRVKEKFSREAFAERL 392
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
210-332 |
8.23e-06 |
|
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: 47.28 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 210 RFTRRPVKVPGTPLQIISVARLTEKKGLHVAIEACRQLKARGVAFHYRILGIGPWERRLRTLIEQYQLDDVVEMPGFK-- 287
Cdd:cd03812 179 RRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLEDKVIFLGFRnd 258
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1452262053 288 PSHEVKAMldeaDVFLLPSVtgadgdMEGIPVALMEAMAVGIPVV 332
Cdd:cd03812 259 VSEILSAM----DVFLFPSL------YEGLPLVAVEAQASGLPCL 293
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
133-369 |
1.08e-04 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 43.93 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 133 AAKLRELGVIDGKIATIFHgidissREVLNHYTPEYQQLfRRGDMMLPISDLWAGRLKSMGCPGEKIAVSRMGVDLTRFT 212
Cdd:PRK09922 99 ANKARKKSGKQFKIFSWPH------FSLDHKKHAECKKI-TCADYHLAISSGIKEQMMARGISAQRISVIYNPVEIKTII 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 213 RRPVKvPGTPLQIISVARLTEK--KGLHVAIEACRQLKARgvaFHYRILGIGPWERRLRTLIEQYQLDDVVEMPGFK--P 288
Cdd:PRK09922 172 IPPPE-RDKPAVFLYVGRLKFEgqKNVKELFDGLSQTTGE---WQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQsqP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 289 SHEVKAMLDEADVFLLPSvtgadgDMEGIPVALMEAMAVGIPVVST-LHSGIPELIKSDHSGWLVPENNAMALADRLAAF 367
Cdd:PRK09922 248 WEVVQQKIKNVSALLLTS------KFEGFPMTLLEAMSYGIPCISSdCMSGPRDIIKPGLNGELYTPGNIDEFVGKLNKV 321
|
..
gi 1452262053 368 SD 369
Cdd:PRK09922 322 IS 323
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
219-333 |
9.48e-04 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 41.39 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 219 PGTPLqIISVARLTEKKGLHVAIEACRQLKARGVAFhyRILGIGPW--ERRLRTLIEQYQlDDVVEMPGFKP--SHEVKA 294
Cdd:cd03791 292 PDAPL-FGFVGRLTEQKGVDLILDALPELLEEGGQL--VVLGSGDPeyEQAFRELAERYP-GKVAVVIGFDEalAHRIYA 367
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1452262053 295 MldeADVFLLPSVtgadgdMEgiPVAL--MEAMAVG-IPVVS 333
Cdd:cd03791 368 G---ADFFLMPSR------FE--PCGLvqMYAMRYGtLPIVR 398
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
219-306 |
2.14e-03 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 40.08 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452262053 219 PGTPLqIISVARLTEKKGLHVAIEACRQLKARGVAFhyRILGIG-PW-ERRLRTLIEQYQlDDVVEMPGFkpsHEVKAML 296
Cdd:COG0297 293 PDAPL-IGMVSRLTEQKGLDLLLEALDELLEEDVQL--VVLGSGdPEyEEAFRELAARYP-GRVAVYIGY---DEALAHR 365
|
90
....*....|..
gi 1452262053 297 DEA--DVFLLPS 306
Cdd:COG0297 366 IYAgaDFFLMPS 377
|
|
| |
