|
Name |
Accession |
Description |
Interval |
E-value |
| GT2_RfbF_like |
cd02526 |
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ... |
11-251 |
5.90e-67 |
|
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.
Pssm-ID: 133017 [Multi-domain] Cd Length: 237 Bit Score: 209.45 E-value: 5.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 11 AVVVVFDPD-DRFRQLLLSLVEQVNKIWIIDNQPNSVscNYVKGGQVQqrNNITLVENKKNVGLAAAQNQGIKLALEDGV 89
Cdd:cd02526 1 AVVVTYNPDlSKLKELLAALAEQVDKVVVVDNSSGND--IELRLRLNS--EKIELIHLGENLGIAKALNIGIKAALENGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 90 DWILLLDQDSILDKDFVKNMLDTALKYKNKKNIGFLTPRHEYDDGRPSVP--TYSKGLFLKPRRYHMSLAEIDdtllFGM 167
Cdd:cd02526 77 DYVLLFDQDSVPPPDMVEKLLAYKILSDKNSNIGAVGPRIIDRRTGENSPgvRKSGYKLRIQKEGEEGLKEVD----FLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 168 ASGSFIPRQTLEEVGLMREEFWIDYIDYEFSFRVRKRGLRILGVGGARLNHRLGIANYLKILGKVLSfqVHPAFRRYTIY 247
Cdd:cd02526 153 TSGSLISLEALEKVGGFDEDLFIDYVDTEWCLRARSKGYKIYVVPDAVLKHELGDKRVKRLGGVSVP--LHSPLRRYYLF 230
|
....
gi 2034063478 248 RNRV 251
Cdd:cd02526 231 RNAI 234
|
|
| rhamnosyltran |
TIGR01556 |
L-rhamnosyltransferase; This model subfamily is comprised of gamma proteobacteria whose ... |
14-300 |
2.11e-40 |
|
L-rhamnosyltransferase; This model subfamily is comprised of gamma proteobacteria whose proteins function as L-rhamnosyltransferases in the synthesis of their respective surface polysaccharides. Rhamnolipids are glycolipids containing mono- or di- L-rhamnose molecules. Rhamnolipid synthesis occurs by sequential glycosyltransferase reactions involving two distinct rhamnosyltransferase enzymes. In P.aeruginosa, the synthesis of mono-rhamnolipids is catalyzed by rhamnosyltransferase 1, and proceeds by a glycosyltransfer reaction catalyzed by rhamnosyltransferase 2 to yield di-rhamnolipids. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 130619 [Multi-domain] Cd Length: 281 Bit Score: 142.62 E-value: 2.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 14 VVFDPD-DRFRQLLLSLVEQVNKIWIIDNQPNsvsCNYVKGGQVQQRNNITLVENKKNVGLAAAQNQGIKLALEDGVDWI 92
Cdd:TIGR01556 1 VTFNPDlEHLGELITSLPKQVDRIIAVDNSPH---SDQPLKNARLRGQKIALIHLGDNQGIAGAQNQGLDASFRRGVQGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 93 LLLDQDSILDKDFVKNMLdtALKYKNKKNIGFLTPRH-EYDDGRPSVPTYSKGlFLKPRRYHMSLAEIDDTlLFGMASGS 171
Cdd:TIGR01556 78 LLLDQDSRPGNAFLAAQW--KLLSAENGQACALGPRFfDRGTSRRLPAIHLDG-LLLRQISLDGLTTPQKT-SFLISSGC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 172 FIPRQTLEEVGLMREEFWIDYIDYEFSFRVRKRGLRILGVGGARLNHRLGIANYLKILGKVLSFQVHPAFRRYTIYRNRV 251
Cdd:TIGR01556 154 LITREVYQRLGMMDEELFIDHVDTEWSLRAQNYGIPLYIDPDIVLEHRIGDSKVRILGGLSLSIPNHSPLRRYYLFRNGI 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2034063478 252 TVIKEYSTLFPdFLLFEILSIAKDLLKLVLLEDQKFNKLRSIFIGTMHG 300
Cdd:TIGR01556 234 LVLRRYARSLP-LKLRENLFTLIQFLAVMILEKNKLLKLRCLIKGLWDG 281
|
|
| WcaE |
COG1216 |
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism]; |
7-267 |
1.70e-32 |
|
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
Pssm-ID: 440829 [Multi-domain] Cd Length: 202 Bit Score: 119.33 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 7 PTVAAVVVVFDPDDRFRQLLLSLVEQVN---KIWIIDNQPNSVSCNYVKGgqvQQRNNITLVENKKNVGLAAAQNQGIKL 83
Cdd:COG1216 3 PKVSVVIPTYNRPELLRRCLESLLAQTYppfEVIVVDNGSTDGTAELLAA---LAFPRVRVIRNPENLGFAAARNLGLRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 84 AledGVDWILLLDQDSILDKDFVKNMLDtalkyknkknigfltprheyddgrpsvptyskglflkprryhmslaeiddtl 163
Cdd:COG1216 80 A---GGDYLLFLDDDTVVEPDWLERLLA---------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 164 lfgmASGSFIPRQTLEEVGLMREEFWIDYIDYEFSFRVRKRGLRILGVGGARLNHRLGIANylkilgkvlsfqvHPAFRR 243
Cdd:COG1216 105 ----AACLLIRREVFEEVGGFDERFFLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASS-------------GPLLRA 167
|
250 260
....*....|....*....|....
gi 2034063478 244 YTIYRNRVTVIKEYSTLFPDFLLF 267
Cdd:COG1216 168 YYLGRNRLLFLRKHGPRPLLRLAL 191
|
|
| Glycos_transf_2 |
pfam00535 |
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ... |
12-180 |
1.51e-07 |
|
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
Pssm-ID: 425738 [Multi-domain] Cd Length: 166 Bit Score: 50.47 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 12 VVVVFDPDDRFRQLLLSLVEQVNK---IWIIDN--QPNSVScnYVKGgQVQQRNNITLVENKKNVGLAAAQNQGIKLAle 86
Cdd:pfam00535 3 IIPTYNEEKYLLETLESLLNQTYPnfeIIVVDDgsTDGTVE--IAEE-YAKKDPRVRVIRLPENRGKAGARNAGLRAA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 87 DGvDWILLLDQDSILDKDFVKNMLDTALKYKNKKNIG--FLTPRHEYDDGRPSVPTYSKGLFLKPRRYhmslaeIDDTLL 164
Cdd:pfam00535 78 TG-DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGsrYVIFGETGEYRRASRITLSRLPFFLGLRL------LGLNLP 150
|
170
....*....|....*.
gi 2034063478 165 FGMASGSFIPRQTLEE 180
Cdd:pfam00535 151 FLIGGFALYRREALEE 166
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GT2_RfbF_like |
cd02526 |
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ... |
11-251 |
5.90e-67 |
|
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.
Pssm-ID: 133017 [Multi-domain] Cd Length: 237 Bit Score: 209.45 E-value: 5.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 11 AVVVVFDPD-DRFRQLLLSLVEQVNKIWIIDNQPNSVscNYVKGGQVQqrNNITLVENKKNVGLAAAQNQGIKLALEDGV 89
Cdd:cd02526 1 AVVVTYNPDlSKLKELLAALAEQVDKVVVVDNSSGND--IELRLRLNS--EKIELIHLGENLGIAKALNIGIKAALENGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 90 DWILLLDQDSILDKDFVKNMLDTALKYKNKKNIGFLTPRHEYDDGRPSVP--TYSKGLFLKPRRYHMSLAEIDdtllFGM 167
Cdd:cd02526 77 DYVLLFDQDSVPPPDMVEKLLAYKILSDKNSNIGAVGPRIIDRRTGENSPgvRKSGYKLRIQKEGEEGLKEVD----FLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 168 ASGSFIPRQTLEEVGLMREEFWIDYIDYEFSFRVRKRGLRILGVGGARLNHRLGIANYLKILGKVLSfqVHPAFRRYTIY 247
Cdd:cd02526 153 TSGSLISLEALEKVGGFDEDLFIDYVDTEWCLRARSKGYKIYVVPDAVLKHELGDKRVKRLGGVSVP--LHSPLRRYYLF 230
|
....
gi 2034063478 248 RNRV 251
Cdd:cd02526 231 RNAI 234
|
|
| rhamnosyltran |
TIGR01556 |
L-rhamnosyltransferase; This model subfamily is comprised of gamma proteobacteria whose ... |
14-300 |
2.11e-40 |
|
L-rhamnosyltransferase; This model subfamily is comprised of gamma proteobacteria whose proteins function as L-rhamnosyltransferases in the synthesis of their respective surface polysaccharides. Rhamnolipids are glycolipids containing mono- or di- L-rhamnose molecules. Rhamnolipid synthesis occurs by sequential glycosyltransferase reactions involving two distinct rhamnosyltransferase enzymes. In P.aeruginosa, the synthesis of mono-rhamnolipids is catalyzed by rhamnosyltransferase 1, and proceeds by a glycosyltransfer reaction catalyzed by rhamnosyltransferase 2 to yield di-rhamnolipids. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 130619 [Multi-domain] Cd Length: 281 Bit Score: 142.62 E-value: 2.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 14 VVFDPD-DRFRQLLLSLVEQVNKIWIIDNQPNsvsCNYVKGGQVQQRNNITLVENKKNVGLAAAQNQGIKLALEDGVDWI 92
Cdd:TIGR01556 1 VTFNPDlEHLGELITSLPKQVDRIIAVDNSPH---SDQPLKNARLRGQKIALIHLGDNQGIAGAQNQGLDASFRRGVQGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 93 LLLDQDSILDKDFVKNMLdtALKYKNKKNIGFLTPRH-EYDDGRPSVPTYSKGlFLKPRRYHMSLAEIDDTlLFGMASGS 171
Cdd:TIGR01556 78 LLLDQDSRPGNAFLAAQW--KLLSAENGQACALGPRFfDRGTSRRLPAIHLDG-LLLRQISLDGLTTPQKT-SFLISSGC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 172 FIPRQTLEEVGLMREEFWIDYIDYEFSFRVRKRGLRILGVGGARLNHRLGIANYLKILGKVLSFQVHPAFRRYTIYRNRV 251
Cdd:TIGR01556 154 LITREVYQRLGMMDEELFIDHVDTEWSLRAQNYGIPLYIDPDIVLEHRIGDSKVRILGGLSLSIPNHSPLRRYYLFRNGI 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2034063478 252 TVIKEYSTLFPdFLLFEILSIAKDLLKLVLLEDQKFNKLRSIFIGTMHG 300
Cdd:TIGR01556 234 LVLRRYARSLP-LKLRENLFTLIQFLAVMILEKNKLLKLRCLIKGLWDG 281
|
|
| WcaE |
COG1216 |
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism]; |
7-267 |
1.70e-32 |
|
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
Pssm-ID: 440829 [Multi-domain] Cd Length: 202 Bit Score: 119.33 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 7 PTVAAVVVVFDPDDRFRQLLLSLVEQVN---KIWIIDNQPNSVSCNYVKGgqvQQRNNITLVENKKNVGLAAAQNQGIKL 83
Cdd:COG1216 3 PKVSVVIPTYNRPELLRRCLESLLAQTYppfEVIVVDNGSTDGTAELLAA---LAFPRVRVIRNPENLGFAAARNLGLRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 84 AledGVDWILLLDQDSILDKDFVKNMLDtalkyknkknigfltprheyddgrpsvptyskglflkprryhmslaeiddtl 163
Cdd:COG1216 80 A---GGDYLLFLDDDTVVEPDWLERLLA---------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 164 lfgmASGSFIPRQTLEEVGLMREEFWIDYIDYEFSFRVRKRGLRILGVGGARLNHRLGIANylkilgkvlsfqvHPAFRR 243
Cdd:COG1216 105 ----AACLLIRREVFEEVGGFDERFFLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASS-------------GPLLRA 167
|
250 260
....*....|....*....|....
gi 2034063478 244 YTIYRNRVTVIKEYSTLFPDFLLF 267
Cdd:COG1216 168 YYLGRNRLLFLRKHGPRPLLRLAL 191
|
|
| GT_2_like_c |
cd04186 |
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ... |
12-219 |
3.15e-23 |
|
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133029 [Multi-domain] Cd Length: 166 Bit Score: 93.78 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 12 VVVVFDPDDRFRQLLLSLVEQVN---KIWIIDNQPNSVSCNYVKggqvQQRNNITLVENKKNVGLAAAQNQGIKLAledG 88
Cdd:cd04186 2 IIVNYNSLEYLKACLDSLLAQTYpdfEVIVVDNASTDGSVELLR----ELFPEVRLIRNGENLGFGAGNNQGIREA---K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 89 VDWILLLDQDSILDKDFVKNMLDTALKYknkKNIGFLTPRheyddgrpsvptyskglflkprryhmslaeiddtllfgmA 168
Cdd:cd04186 75 GDYVLLLNPDTVVEPGALLELLDAAEQD---PDVGIVGPK---------------------------------------V 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2034063478 169 SGSF--IPRQTLEEVGLMREEFWIDYIDYEFSFRVRKRGLRILGVGGARLNHR 219
Cdd:cd04186 113 SGAFllVRREVFEEVGGFDEDFFLYYEDVDLCLRARLAGYRVLYVPQAVIYHH 165
|
|
| GT_2_like_b |
cd04185 |
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ... |
11-250 |
8.46e-18 |
|
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133028 [Multi-domain] Cd Length: 202 Bit Score: 79.99 E-value: 8.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 11 AVVVVFDPDDRFRQLLLSLVEQ---VNKIWIIDNQPNSVSCNYVKggQVQQRNNITLVENKKNVGLAAAQNQGIKLALED 87
Cdd:cd04185 1 AVVVTYNRLDLLKECLDALLAQtrpPDHIIVIDNASTDGTAEWLT--SLGDLDNIVYLRLPENLGGAGGFYEGVRRAYEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 88 GVDWILLLDQDSILDKDfvknMLDTALKYKNKKNIGFLTPRHEYDDGrPSVptyskglflkprryhmslaeiddtllfgm 167
Cdd:cd04185 79 GYDWIWLMDDDAIPDPD----ALEKLLAYADKDNPQFLAPLVLDPDG-SFV----------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 168 asGSFIPRQTLEEVGLMREEFWIDYIDYEFSFRVRKRGLRILgVGGARLNHrlgianYLKILGKVLSFQVH-PAFRRYTI 246
Cdd:cd04185 125 --GVLISRRVVEKIGLPDKEFFIWGDDTEYTLRASKAGPGIY-VPDAVVVH------KTAINKGSSAVVNIdPPWKLYYG 195
|
....
gi 2034063478 247 YRNR 250
Cdd:cd04185 196 VRNR 199
|
|
| BcsA |
COG1215 |
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ... |
7-208 |
1.61e-10 |
|
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];
Pssm-ID: 440828 [Multi-domain] Cd Length: 303 Bit Score: 60.91 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 7 PTVAAVVVVFDPDDRFRQLLLSLVEQ-----VNKIWIIDNQPNSVSCNYVKGGQvQQRNNITLVENKKNVGLAAAQNQGI 81
Cdd:COG1215 29 PRVSVIIPAYNEEAVIEETLRSLLAQdypkeKLEVIVVDDGSTDETAEIARELA-AEYPRVRVIERPENGGKAAALNAGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 82 KLAleDGvDWILLLDQDSILDKDFVKNMLdtalkyknkknigfltprheyddgrpsvptyskGLFLKPrryhmslaeidD 161
Cdd:COG1215 108 KAA--RG-DIVVFLDADTVLDPDWLRRLV---------------------------------AAFADP-----------G 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2034063478 162 TLLFGmaSGSFIPRQTLEEVGLMREEFWIDyiDYEFSFRVRKRGLRI 208
Cdd:COG1215 141 VGASG--ANLAFRREALEEVGGFDEDTLGE--DLDLSLRLLRAGYRI 183
|
|
| WcaA |
COG0463 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
7-208 |
2.68e-09 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440231 [Multi-domain] Cd Length: 208 Bit Score: 56.25 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 7 PTVAAVVVVFDPDDRFRQLLLSLVEQVNK---IWIIDNQPNSVSCNYVKGGQvQQRNNITLVENKKNVGLAAAQNQGIKL 83
Cdd:COG0463 2 PLVSVVIPTYNEEEYLEEALESLLAQTYPdfeIIVVDDGSTDGTAEILRELA-AKDPRIRVIRLERNRGKGAARNAGLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 84 AleDGvDWILLLDQDSILDKDFVKNMLDTALKYKnkknIGFLTPRHEYDDGRpsvpTYSKGLFLKPRRYHMSLAEIDDTl 163
Cdd:COG0463 81 A--RG-DYIAFLDADDQLDPEKLEELVAALEEGP----ADLVYGSRLIREGE----SDLRRLGSRLFNLVRLLTNLPDS- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2034063478 164 lfgMASGSFIPRQTLEEVGLmREEFwidYIDYEFsFRVRKRGLRI 208
Cdd:COG0463 149 ---TSGFRLFRREVLEELGF-DEGF---LEDTEL-LRALRHGFRI 185
|
|
| Glyco_tranf_GTA_type |
cd00761 |
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ... |
11-118 |
5.26e-08 |
|
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.
Pssm-ID: 132997 [Multi-domain] Cd Length: 156 Bit Score: 51.35 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 11 AVVVVFDPDDRFRQLLLSLVEQVNKIW---IIDNQPNSVSCNYVKGGQvQQRNNITLVENKKNVGLAAAQNQGIKLAled 87
Cdd:cd00761 1 VIIPAYNEEPYLERCLESLLAQTYPNFeviVVDDGSTDGTLEILEEYA-KKDPRVIRVINEENQGLAAARNAGLKAA--- 76
|
90 100 110
....*....|....*....|....*....|.
gi 2034063478 88 GVDWILLLDQDSILDKDFVKNMLDTALKYKN 118
Cdd:cd00761 77 RGEYILFLDADDLLLPDWLERLVAELLADPE 107
|
|
| Glycos_transf_2 |
pfam00535 |
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ... |
12-180 |
1.51e-07 |
|
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
Pssm-ID: 425738 [Multi-domain] Cd Length: 166 Bit Score: 50.47 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 12 VVVVFDPDDRFRQLLLSLVEQVNK---IWIIDN--QPNSVScnYVKGgQVQQRNNITLVENKKNVGLAAAQNQGIKLAle 86
Cdd:pfam00535 3 IIPTYNEEKYLLETLESLLNQTYPnfeIIVVDDgsTDGTVE--IAEE-YAKKDPRVRVIRLPENRGKAGARNAGLRAA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 87 DGvDWILLLDQDSILDKDFVKNMLDTALKYKNKKNIG--FLTPRHEYDDGRPSVPTYSKGLFLKPRRYhmslaeIDDTLL 164
Cdd:pfam00535 78 TG-DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGsrYVIFGETGEYRRASRITLSRLPFFLGLRL------LGLNLP 150
|
170
....*....|....*.
gi 2034063478 165 FGMASGSFIPRQTLEE 180
Cdd:pfam00535 151 FLIGGFALYRREALEE 166
|
|
| Succinoglycan_BP_ExoA |
cd02525 |
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ... |
57-208 |
1.03e-05 |
|
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.
Pssm-ID: 133016 [Multi-domain] Cd Length: 249 Bit Score: 46.07 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 57 QQRNNITLVENKKNVgLAAAQNQGIKLAleDGvDWILLLDQDSILDKDFVKNMLDTALKYKNKKNIGFLTPRHEYDDGRP 136
Cdd:cd02525 54 AKDPRIRLIDNPKRI-QSAGLNIGIRNS--RG-DIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKA 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2034063478 137 SVPTYSKGLFLKPRRYHMSLAEID--DTLLFGMasgsfIPRQTLEEVGLMREEFwIDYIDYEFSFRVRKRGLRI 208
Cdd:cd02525 130 IAVAQSSPLGSGGSAYRGGAVKIGyvDTVHHGA-----YRREVFEKVGGFDESL-VRNEDAELNYRLRKAGYKI 197
|
|
| CESA_like |
cd06423 |
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ... |
55-118 |
3.61e-04 |
|
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.
Pssm-ID: 133045 [Multi-domain] Cd Length: 180 Bit Score: 40.67 E-value: 3.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2034063478 55 QVQQRNNITLVENKKNVGLAAAQNQGIKLAleDGvDWILLLDQDSILDKDFVKNMLDTALKYKN 118
Cdd:cd06423 48 AALYIRRVLVVRDKENGGKAGALNAGLRHA--KG-DIVVVLDADTILEPDALKRLVVPFFADPK 108
|
|
| Glyco_tranf_2_3 |
pfam13641 |
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ... |
7-218 |
4.98e-04 |
|
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.
Pssm-ID: 433372 [Multi-domain] Cd Length: 230 Bit Score: 40.82 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 7 PTVAAVVVVFDPDDRFRQLLLSLVEQVN---KIWIIDNQPNSVSCNYVKGGQVQ-QRNNITLVENKKNVGL---AAAQNQ 79
Cdd:pfam13641 2 PDVSVVVPAFNEDSVLGRVLEAILAQPYppvEVVVVVNPSDAETLDVAEEIAARfPDVRLRVIRNARLLGPtgkSRGLNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 80 GIKLALEDgvdWILLLDQDSILDKDFVKnMLDTALKYKNKKNIGflTPRHEYDDGRPSVPTYSkgLFLKPRRYHMSLAEI 159
Cdd:pfam13641 82 GFRAVKSD---LVVLHDDDSVLHPGTLK-KYVQYFDSPKVGAVG--TPVFSLNRSTMLSALGA--LEFALRHLRMMSLRL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2034063478 160 DDTLLFGMASGSFIPRQTLEEVGLMREEFWIDYiDYEFSFRVRKRGLRILGVGGARLNH 218
Cdd:pfam13641 154 ALGVLPLSGAGSAIRREVLKELGLFDPFFLLGD-DKSLGRRLRRHGWRVAYAPDAAVRT 211
|
|
| Glyco_trans_2_3 |
pfam13632 |
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ... |
91-208 |
7.84e-04 |
|
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.
Pssm-ID: 433365 [Multi-domain] Cd Length: 192 Bit Score: 40.01 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 91 WILLLDQDSILDKDFVK---NMLDTAlkyknkkNIGFLTPrHEYDDGRPSVPTYSKGLFLkpRRYHMSLAEIDDTL---L 164
Cdd:pfam13632 1 WILLLDADTVLPPDCLLgiaNEMASP-------EVAIIQG-PILPMNVGNYLEELAALFF--ADDHGKSIPVRMALgrvL 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2034063478 165 FGMASGSFIPRQTLEEVGlmreeFWIDYI---DYEFSFRVRKRGLRI 208
Cdd:pfam13632 71 PFVGSGAFLRRSALQEVG-----GWDDGSvseDFDFGLRLQRAGYRV 112
|
|
| Glyco_transf_21 |
pfam13506 |
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ... |
67-227 |
9.85e-04 |
|
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.
Pssm-ID: 433264 [Multi-domain] Cd Length: 173 Bit Score: 39.19 E-value: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 67 NKKNVGLAAAQNqgiklaledgvDWILLLDQDSILDKDFVKNMLdtalKYKNKKNIGFLTprheyddgrpSVPTYSK--- 143
Cdd:pfam13506 20 NNLLQGLEAAKY-----------DLLVISDSDIRVPPDYLRDLL----APLADPKVGLVT----------SPPVGSDpkg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 144 --GLFLK------PRRYHMSLAEIDDtlLFGMASgsFIPRQTLEEVGLMREefWIDYI--DYEFSFRVRKRGLRILGVGG 213
Cdd:pfam13506 75 laAALEAaffntlAGVLQAALSGIGF--AVGMSM--AFRRADLERIGGFEA--LADYLaeDYALGKLLRAAGLKVVLSPR 148
|
170
....*....|....
gi 2034063478 214 ARLNHRLGIANYLK 227
Cdd:pfam13506 149 PILQTSGPRRTSFR 162
|
|
| GT2_RfbC_Mx_like |
cd04184 |
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ... |
7-208 |
3.22e-03 |
|
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.
Pssm-ID: 133027 [Multi-domain] Cd Length: 202 Bit Score: 37.95 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 7 PTVAAVVVVFDPDDRF-RQLLLSLVEQVNKIW---IIDNQPNSVSCNYVKGGQVQQRNNITLVENKKNVGLAAAQNQGIK 82
Cdd:cd04184 1 PLISIVMPVYNTPEKYlREAIESVRAQTYPNWelcIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034063478 83 LAledGVDWILLLDQDSILDKDfvkNMLDTALKYKNKKNIGFLTPRHEY--DDGRPSVPtyskglFLKPrryhmslAEID 160
Cdd:cd04184 81 LA---TGEFVALLDHDDELAPH---ALYEVVKALNEHPDADLIYSDEDKidEGGKRSEP------FFKP-------DWSP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2034063478 161 DTLLFGMASGSF--IPRQTLEEVGLMREEFWIDYiDYEFSFRVRKRGLRI 208
Cdd:cd04184 142 DLLLSQNYIGHLlvYRRSLVRQVGGFREGFEGAQ-DYDLVLRVSEHTDRI 190
|
|
| |
