|
Name |
Accession |
Description |
Interval |
E-value |
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
3-362 |
3.30e-138 |
|
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: 401.56 E-value: 3.30e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 3 TSVAVEVKVADSIEIVRFFHCYKRGVDRVFVDHPIFLEKVWGKtgskiygPKAGQDYLDNELRFSLLCQAALEAPRVLnl 82
Cdd:cd03791 55 RVLGLEVKVGGRGEEVGVFELPVDGVDYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRL-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 83 ncskyfsgpYGEDVLFIVNDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPyefrGSFDFID 162
Cdd:cd03791 126 ---------GFQPDIIHANDWHTALVPAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLP----PELFHID 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 163 GcekPVKGRKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKY 240
Cdd:cd03791 192 G---LEFYGQINFLKAGIVYADRVTTVSPTYAKEILTP-EYGEGLDGVLRARAgkLSGILNGIDYDEWNPATDKLIPANY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 241 DiTTVMDAKPLLKETLQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVL 320
Cdd:cd03791 268 S-ANDLEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAER 346
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 45826397 321 YPNKAKGVAKFNVPLAHMITAGADFMLVPSRFEPCGLIQLHA 362
Cdd:cd03791 347 YPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYA 388
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
2-362 |
6.48e-125 |
|
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273969 [Multi-domain] Cd Length: 473 Bit Score: 367.36 E-value: 6.48e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 2 DTSVAVEVKVADSIEIVRFFHCYKRGVDRVFVDHPIFLEKvwgktGSKIYGPkagqDYLDNELRFSLLCQAALEAPRVLN 81
Cdd:TIGR02095 56 KVVELVDLSVGPRTLYVKVFEGVVEGVPVYFIDNPSLFDR-----PGGIYGD----DYPDNAERFAFFSRAAAELLSGLG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 82 lncskyfsgpYGEDVlFIVNDWHTALIPCYLKSMYQSrgiyLNAKVAFCIHNIAYQGRFAFSDFPLLNLPYEFRGSFDFI 161
Cdd:TIGR02095 127 ----------WQPDV-VHAHDWHTALVPALLKAVYRP----NPIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 162 DGcekpvkgRKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVK 239
Cdd:TIGR02095 192 FY-------GRVNFLKGGIVYADRVTTVSPTYAREILTP-EFGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKAN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 240 YDITTvMDAKPLLKETLQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEV 319
Cdd:TIGR02095 264 YSADD-LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAE 342
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 45826397 320 LYPNKAKGVAKFNVPLAHMITAGADFMLVPSRFEPCGLIQLHA 362
Cdd:TIGR02095 343 RYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYA 385
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
7-362 |
4.22e-111 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 332.44 E-value: 4.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 7 VEVKVADSIEIVRFFHCYKRGVDRVFVDHPIFLEkvwgktGSKIYGPkAGQDYLDNELRFSLLCQAALEAPRVLNLNCsk 86
Cdd:COG0297 60 LEVPLGGRTYYARVLEGPDDGVPVYFIDNPELFD------RPGPYGD-PDRDYPDNAERFAFFSRAALELLKGLDWKP-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 87 yfsgpygeDVLFiVNDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPYEFrgsfDFIDGCEK 166
Cdd:COG0297 131 --------DIIH-CHDWQTGLIPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL----FTPDGLEF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 167 PvkGrKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITT 244
Cdd:COG0297 197 Y--G-QINFLKAGIVYADRVTTVSPTYAREIQTP-EFGEGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 245 vMDAKPLLKETLQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 324
Cdd:COG0297 273 -LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGR 351
|
330 340 350
....*....|....*....|....*....|....*...
gi 45826397 325 AKGVAKFNVPLAHMITAGADFMLVPSRFEPCGLIQLHA 362
Cdd:COG0297 352 VAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYA 389
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
18-362 |
4.61e-96 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 293.56 E-value: 4.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 18 VRFFHCYKRGVDRVFVDHPIFlekvwgktgskiYGPKAGQDYLDNELRFSLLCQAALEAprvlnlnCSKYFSGPygeDVL 97
Cdd:PRK00654 65 VLFGHLEGDGVPVYLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEF-------AEGLDPRP---DIV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 98 FiVNDWHTALIPCYLKSMYQSRgiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPYEFR--GSFDFIDGcekpvkgrkINW 175
Cdd:PRK00654 123 H-AHDWHTGLIPALLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAEAFhlEGLEFYGQ---------ISF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 176 MKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLK 253
Cdd:PRK00654 191 LKAGLYYADRVTTVSPTYAREITTP-EFGYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 254 ETLQAAVGLPVDrKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGVAKFNV 333
Cdd:PRK00654 269 RALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDE 347
|
330 340
....*....|....*....|....*....
gi 45826397 334 PLAHMITAGADFMLVPSRFEPCGLIQLHA 362
Cdd:PRK00654 348 ALAHRIYAGADMFLMPSRFEPCGLTQLYA 376
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
1-213 |
3.68e-54 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 178.29 E-value: 3.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 1 WDTSVAVEVKVADsiEIVRFFHCYKRGVDRVFVDHPIFLEKvwgktgSKIYGPKaGQDYLDNELRFSLLCQAALEAPRVL 80
Cdd:pfam08323 56 IRLSVAAGVPVRP--LTVGVARLELDGVDVYFLDNPDYFDR------PGLYGDD-GRDYEDNAERFAFFSRAALELAKKL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 81 NlncskyfsgpYGEDVLfIVNDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPYEFR--GSF 158
Cdd:pfam08323 127 G----------WIPDII-HCHDWHTALVPAYLKEAYADDP-FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFnlDGL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45826397 159 DFIDgcekpvkgrKINWMKAGILESHRVVTVSPYYAQELVSAVDkGVELDNVLRK 213
Cdd:pfam08323 195 EFYG---------QINFLKAGIVYADAVTTVSPTYAEEIQTPEF-GGGLDGLLRE 239
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
3-362 |
3.30e-138 |
|
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: 401.56 E-value: 3.30e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 3 TSVAVEVKVADSIEIVRFFHCYKRGVDRVFVDHPIFLEKVWGKtgskiygPKAGQDYLDNELRFSLLCQAALEAPRVLnl 82
Cdd:cd03791 55 RVLGLEVKVGGRGEEVGVFELPVDGVDYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRL-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 83 ncskyfsgpYGEDVLFIVNDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPyefrGSFDFID 162
Cdd:cd03791 126 ---------GFQPDIIHANDWHTALVPAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLP----PELFHID 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 163 GcekPVKGRKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKY 240
Cdd:cd03791 192 G---LEFYGQINFLKAGIVYADRVTTVSPTYAKEILTP-EYGEGLDGVLRARAgkLSGILNGIDYDEWNPATDKLIPANY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 241 DiTTVMDAKPLLKETLQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVL 320
Cdd:cd03791 268 S-ANDLEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAER 346
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 45826397 321 YPNKAKGVAKFNVPLAHMITAGADFMLVPSRFEPCGLIQLHA 362
Cdd:cd03791 347 YPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYA 388
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
2-362 |
6.48e-125 |
|
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273969 [Multi-domain] Cd Length: 473 Bit Score: 367.36 E-value: 6.48e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 2 DTSVAVEVKVADSIEIVRFFHCYKRGVDRVFVDHPIFLEKvwgktGSKIYGPkagqDYLDNELRFSLLCQAALEAPRVLN 81
Cdd:TIGR02095 56 KVVELVDLSVGPRTLYVKVFEGVVEGVPVYFIDNPSLFDR-----PGGIYGD----DYPDNAERFAFFSRAAAELLSGLG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 82 lncskyfsgpYGEDVlFIVNDWHTALIPCYLKSMYQSrgiyLNAKVAFCIHNIAYQGRFAFSDFPLLNLPYEFRGSFDFI 161
Cdd:TIGR02095 127 ----------WQPDV-VHAHDWHTALVPALLKAVYRP----NPIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 162 DGcekpvkgRKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVK 239
Cdd:TIGR02095 192 FY-------GRVNFLKGGIVYADRVTTVSPTYAREILTP-EFGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKAN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 240 YDITTvMDAKPLLKETLQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEV 319
Cdd:TIGR02095 264 YSADD-LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAE 342
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 45826397 320 LYPNKAKGVAKFNVPLAHMITAGADFMLVPSRFEPCGLIQLHA 362
Cdd:TIGR02095 343 RYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYA 385
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
7-362 |
4.22e-111 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 332.44 E-value: 4.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 7 VEVKVADSIEIVRFFHCYKRGVDRVFVDHPIFLEkvwgktGSKIYGPkAGQDYLDNELRFSLLCQAALEAPRVLNLNCsk 86
Cdd:COG0297 60 LEVPLGGRTYYARVLEGPDDGVPVYFIDNPELFD------RPGPYGD-PDRDYPDNAERFAFFSRAALELLKGLDWKP-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 87 yfsgpygeDVLFiVNDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPYEFrgsfDFIDGCEK 166
Cdd:COG0297 131 --------DIIH-CHDWQTGLIPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL----FTPDGLEF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 167 PvkGrKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITT 244
Cdd:COG0297 197 Y--G-QINFLKAGIVYADRVTTVSPTYAREIQTP-EFGEGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 245 vMDAKPLLKETLQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 324
Cdd:COG0297 273 -LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGR 351
|
330 340 350
....*....|....*....|....*....|....*...
gi 45826397 325 AKGVAKFNVPLAHMITAGADFMLVPSRFEPCGLIQLHA 362
Cdd:COG0297 352 VAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYA 389
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
18-362 |
4.61e-96 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 293.56 E-value: 4.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 18 VRFFHCYKRGVDRVFVDHPIFlekvwgktgskiYGPKAGQDYLDNELRFSLLCQAALEAprvlnlnCSKYFSGPygeDVL 97
Cdd:PRK00654 65 VLFGHLEGDGVPVYLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEF-------AEGLDPRP---DIV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 98 FiVNDWHTALIPCYLKSMYQSRgiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPYEFR--GSFDFIDGcekpvkgrkINW 175
Cdd:PRK00654 123 H-AHDWHTGLIPALLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAEAFhlEGLEFYGQ---------ISF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 176 MKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLK 253
Cdd:PRK00654 191 LKAGLYYADRVTTVSPTYAREITTP-EFGYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 254 ETLQAAVGLPVDrKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGVAKFNV 333
Cdd:PRK00654 269 RALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDE 347
|
330 340
....*....|....*....|....*....
gi 45826397 334 PLAHMITAGADFMLVPSRFEPCGLIQLHA 362
Cdd:PRK00654 348 ALAHRIYAGADMFLMPSRFEPCGLTQLYA 376
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
47-362 |
1.16e-66 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 218.05 E-value: 1.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 47 GSKIYGPKaGQDYLDNELRFSLLCQAALEAPRVLnlncskyfSGPYGEDVLFiVNDWHTALIPCYLKsmYQSRGiylNAK 126
Cdd:PRK14099 96 GNPYVGPD-GKDWPDNAQRFAALARAAAAIGQGL--------VPGFVPDIVH-AHDWQAGLAPAYLH--YSGRP---APG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 127 VAFCIHNIAYQGRFAFSDFPLLNLPYEfrgSFDfIDGCEkpVKGrKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVE 206
Cdd:PRK14099 161 TVFTIHNLAFQGQFPRELLGALGLPPS---AFS-LDGVE--YYG-GIGYLKAGLQLADRITTVSPTYALEIQGP-EAGMG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 207 LDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKETLQAAVGLPVDRKIPLIGFIGRLEEQKGSD 284
Cdd:PRK14099 233 LDGLLRQRAdrLSGILNGIDTAVWNPATDELIAATYDVET-LAARAANKAALQARFGLDPDPDALLLGVISRLSWQKGLD 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45826397 285 ILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGVAKFNVPLAHMITAGADFMLVPSRFEPCGLIQLHA 362
Cdd:PRK14099 312 LLLEALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQAGADALLVPSRFEPCGLTQLCA 389
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
101-362 |
1.78e-54 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 186.09 E-value: 1.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 101 NDWHTALIPCYLKSMYQSRGIYLNAKVAFCIHNIAYQGRFAFSDFPLLnLPYEFrgsfdfIDGCEkpVKGRKINWMKAGI 180
Cdd:PRK14098 148 HDWYAGLVPLLLKTVYADHEFFKDIKTVLTIHNVYRQGVLPFKVFQKL-LPEEV------CSGLH--REGDEVNMLYTGV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 181 LESHRVVTVSPYYAQELVSAVDKGVELDNVL--RKTSITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKETLQA 258
Cdd:PRK14098 219 EHADLLTTTSPRYAEEIAGDGEEAFGLDKVLeeRKMRLHGILNGIDTRQWNPSTDKLIKKRYSIER-LDGKLENKKALLE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 259 AVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGVAKFNVPLAHM 338
Cdd:PRK14098 298 EVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFHL 377
|
250 260
....*....|....*....|....
gi 45826397 339 ITAGADFMLVPSRFEPCGLIQLHA 362
Cdd:PRK14098 378 AIAGLDMLLMPGKIESCGMLQMFA 401
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
1-213 |
3.68e-54 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 178.29 E-value: 3.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 1 WDTSVAVEVKVADsiEIVRFFHCYKRGVDRVFVDHPIFLEKvwgktgSKIYGPKaGQDYLDNELRFSLLCQAALEAPRVL 80
Cdd:pfam08323 56 IRLSVAAGVPVRP--LTVGVARLELDGVDVYFLDNPDYFDR------PGLYGDD-GRDYEDNAERFAFFSRAALELAKKL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 81 NlncskyfsgpYGEDVLfIVNDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPYEFR--GSF 158
Cdd:pfam08323 127 G----------WIPDII-HCHDWHTALVPAYLKEAYADDP-FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFnlDGL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45826397 159 DFIDgcekpvkgrKINWMKAGILESHRVVTVSPYYAQELVSAVDkGVELDNVLRK 213
Cdd:pfam08323 195 EFYG---------QINFLKAGIVYADAVTTVSPTYAEEIQTPEF-GGGLDGLLRE 239
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
61-362 |
5.17e-37 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 141.96 E-value: 5.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 61 DNELRFSLLCQAALEaprvLNLNCSKYFsgpygeDVLFiVNDWHTALI-PCYLkSMYQSRGIYlNAKVAFCIHNIAYQGR 139
Cdd:PLN02939 588 DDFKRFSYFSRAALE----LLYQSGKKP------DIIH-CHDWQTAFVaPLYW-DLYAPKGFN-SARICFTCHNFEYQGT 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 140 FAFSDFPLLNLPYEfrgSFDFIDGCEKPVKGRkINWMKAGILESHRVVTVSPYYAQELVSAVDKGVELDNVLRKTSITGI 219
Cdd:PLN02939 655 APASDLASCGLDVH---QLDRPDRMQDNAHGR-INVVKGAIVYSNIVTTVSPTYAQEVRSEGGRGLQDTLKFHSKKFVGI 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 220 VNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKETLQAAVGLP-VDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDV 298
Cdd:PLN02939 731 LNGIDTDTWNPSTDRFLKVQYNAND-LQGKAANKAALRKQLGLSsADASQPLVGCITRLVPQKGVHLIRHAIYKTAELGG 809
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45826397 299 QIVVLGTG-----KKKFEQEIEQLEvlYPNKAKGVAKFNVPLAHMITAGADFMLVPSRFEPCGLIQLHA 362
Cdd:PLN02939 810 QFVLLGSSpvphiQREFEGIADQFQ--SNNNIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIA 876
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
50-362 |
4.44e-33 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 130.38 E-value: 4.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 50 IYGPKagqdylDNELRFSLLCQAALEAPRvlnlncskyfSGPYGEDVLFiVNDWHTALIPCYLKSMYQSRGIyLNAKVAF 129
Cdd:PLN02316 682 VYGCR------NDGERFGFFCHAALEFLL----------QSGFHPDIIH-CHDWSSAPVAWLFKDHYAHYGL-SKARVVF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 130 CIHNIayqgrfafsdfpllnlpyEFrgsfdfidgcekpvkgrKINWMKAGILESHRVVTVSPYYAQELV--SAVdkgvel 207
Cdd:PLN02316 744 TIHNL------------------EF-----------------GANHIGKAMAYADKATTVSPTYSREVSgnSAI------ 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 208 dnVLRKTSITGIVNGMDTQEWNPATDKYTDVKYDITTVMDAKPLLKETLQAAVGL-PVDrkIPLIGFIGRLEEQKGSDIL 286
Cdd:PLN02316 783 --APHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLkQAD--LPLVGIITRLTHQKGIHLI 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 287 VAAIHKFIGLDVQIVVLGTG-----KKKFEQEIEQLEVLYPNKAKGVAKFNVPLAHMITAGADFMLVPSRFEPCGLIQLH 361
Cdd:PLN02316 859 KHAIWRTLERNGQVVLLGSApdpriQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLT 938
|
.
gi 45826397 362 A 362
Cdd:PLN02316 939 A 939
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
78-360 |
2.44e-11 |
|
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: 64.10 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 78 RVLNLNCSKYFSGPYGEDVLFIVNDWHTALIPCYLKSMYQSRGIYLNAKVAFCIHniaYQGRFAFSDFPLLNLPYE---- 153
Cdd:cd03801 33 DVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVH---AHGLLAALLAALLALLLGaplv 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 154 --FRGSFDFIDGCEKPVKGRKINWMKAGILESHRVVTVSPYYAQELVSAvdkgveldNVLRKTSITGIVNGMDTQEWNPA 231
Cdd:cd03801 110 vtLHGAEPGRLLLLLAAERRLLARAEALLRRADAVIAVSEALRDELRAL--------GGIPPEKIVVIPNGVDLERFSPP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 232 TDKytdvkydittvmdakpllketlqaavGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTGkkk 309
Cdd:cd03801 182 LRR--------------------------KLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLrrGPDVRLVIVGGD--- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 45826397 310 fEQEIEQLEVLYPNKAKGVaKF--NVPLAHM--ITAGADFMLVPSRFEPCGLIQL 360
Cdd:cd03801 233 -GPLRAELEELELGLGDRV-RFlgFVPDEELpaLYAAADVFVLPSRYEGFGLVVL 285
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
185-362 |
3.70e-06 |
|
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: 48.53 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 185 RVVTVSPYYAQELVSAvdkGVELDNVlrktsiTGIVNGMDTQEWNPATdkytdvkydittvmdakpllketlqAAVGLPV 264
Cdd:cd03798 153 RVIAVSKALAEELVAL---GVPRDRV------DVIPNGVDPARFQPED-------------------------RGLGLPL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 265 DRkiPLIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTG--KKKFEQEIEQLevlypNKAKGVaKFNVPL----- 335
Cdd:cd03798 199 DA--FVILFVGRLIPRKGIDLLLEAFARLAkaRPDVVLLIVGDGplREALRALAEDL-----GLGDRV-TFTGRLpheqv 270
|
170 180
....*....|....*....|....*...
gi 45826397 336 -AHMitAGADFMLVPSRFEPCGLIQLHA 362
Cdd:cd03798 271 pAYY--RACDVFVLPSRHEGFGLVLLEA 296
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
182-362 |
8.21e-06 |
|
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: 47.24 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 182 ESHRVVTVSPYYAQELVSAVDKGVELDNVlrktsitgIVNGMDTQEWNPATDKytdvkydittvmdakpllkETLQAAVG 261
Cdd:cd03800 163 AADRVIASTPQEADELISLYGADPSRINV--------VPPGVDLERFFPVDRA-------------------EARRARLL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 262 LPVDRKIPLigFIGRLEEQKGSDILVAAIHKFIGLDVQ---IVVLGT---GKKKFEQEIEQLEVLYpnkaKGVAKFNVP- 334
Cdd:cd03800 216 LPPDKPVVL--ALGRLDPRKGIDTLVRAFAQLPELRELanlVLVGGPsddPLSMDREELAELAEEL----GLIDRVRFPg 289
|
170 180 190
....*....|....*....|....*....|....
gi 45826397 335 ------LAHMITAgADFMLVPSRFEPCGLIQLHA 362
Cdd:cd03800 290 rvsrddLPELYRA-ADVFVVPSLYEPFGLTAIEA 322
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
269-362 |
2.54e-05 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 43.65 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 269 PLIGFIGRL-EEQKGSDILVAAIHKFI--GLDVQIVVLGTGkkkfeqEIEQLEVLYPNKAKGVaKF--NVPLAHMITAGA 343
Cdd:pfam13692 2 PVILFVGRLhPNVKGVDYLLEAVPLLRkrDNDVRLVIVGDG------PEEELEELAAGLEDRV-IFtgFVEDLAELLAAA 74
|
90
....*....|....*....
gi 45826397 344 DFMLVPSRFEPCGLIQLHA 362
Cdd:pfam13692 75 DVFVLPSLYEGFGLKLLEA 93
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
273-360 |
7.05e-05 |
|
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: 43.55 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 273 FIGRLEEQKGSDILVAAIHK----FIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGvAKFNVPLAHMITAGADFMLV 348
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALlkarLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIG-GLVDDEVLELLLAAADVFVL 193
|
90
....*....|..
gi 45826397 349 PSRFEPCGLIQL 360
Cdd:cd01635 194 PSRSEGFGLVLL 205
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
271-358 |
8.88e-05 |
|
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: 43.86 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 271 IGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKkkfEQEIEQLEVLYPNKAKGVAKFNVPLAHMitAGADFMLVPS 350
Cdd:cd03823 194 FGYIGRLTEEKGIDLLVEAFKRLPREDIELVIAGHGP---LSDERQIEGGRRIAFLGRVPTDDIKDFY--EKIDVLVVPS 268
|
....*....
gi 45826397 351 RF-EPCGLI 358
Cdd:cd03823 269 IWpEPFGLV 277
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
265-354 |
9.73e-05 |
|
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: 43.89 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 265 DRKIPLIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTG--KKKFEQEIEQLEVlypnkAKGV----AKFNvPLA 336
Cdd:cd03811 185 PEDGPVILAVGRLDPQKGHDLLIEAFAKLRkkYPDVKLVILGDGplREELEKLAKELGL-----AERViflgFQSN-PYP 258
|
90
....*....|....*...
gi 45826397 337 HMitAGADFMLVPSRFEP 354
Cdd:cd03811 259 YL--KKADLFVLSSRYEG 274
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
270-362 |
5.98e-04 |
|
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: 41.51 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 270 LIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTG--KKKFEQEIEQLE----VLYPNKAKGVAKFnvpLAHMita 341
Cdd:cd03812 193 VLGHVGRFNEQKNHSFLIDIFEELKkkNPNVKLVLVGEGelKEKIKEKVKELGledkVIFLGFRNDVSEI---LSAM--- 266
|
90 100
....*....|....*....|.
gi 45826397 342 gaDFMLVPSRFEPCGLIQLHA 362
Cdd:cd03812 267 --DVFLFPSLYEGLPLVAVEA 285
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
259-362 |
2.25e-03 |
|
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: 39.66 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 259 AVGLPVDRKIPLigFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTGKKKFEQEIEQL-------EVLYPNKAKGVA 329
Cdd:cd03821 197 KHNGLEDRRIIL--FLGRIHPKKGLDLLIRAARKLAeqGRDWHLVIAGPDDGAYPAFLQLQsslglgdRVTFTGPLYGEA 274
|
90 100 110
....*....|....*....|....*....|...
gi 45826397 330 KfnvpLAHMitAGADFMLVPSRFEPCGLIQLHA 362
Cdd:cd03821 275 K----WALY--ASADLFVLPSYSENFGNVVAEA 301
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
269-357 |
2.54e-03 |
|
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: 38.02 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 269 PLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVL----GTGKKKFEQEIEQLEvlypNKAKGVAKFNVP---LAHMITA 341
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLViagdGEEEKRLKKLAEKLG----LGDNVIFLGFVSdedLPELLKI 78
|
90
....*....|....*.
gi 45826397 342 gADFMLVPSRFEPCGL 357
Cdd:pfam00534 79 -ADVFVLPSRYEGFGI 93
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
171-362 |
5.71e-03 |
|
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: 38.47 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 171 RKINWMKAGILEshrVVTVSPYYAQELVSAVdkgveldnVLRKTSITGIVNGMDTQEWNPAtDKytdvkydittvMDAKP 250
Cdd:cd03825 129 RKREALAKKRLT---IVAPSRWLADMVRRSP--------LLKGLPVVVIPNGIDTEIFAPV-DK-----------AKARK 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45826397 251 LLketlqaavGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLD-VQIVVLG-TGKKKFEQEIEQLEVLYPNkakgv 328
Cdd:cd03825 186 RL--------GIPQDKKVILFGAESVTKPRKGFDELIEALKLLATKDdLLLVVFGkNDPQIVILPFDIISLGYID----- 252
|
170 180 190
....*....|....*....|....*....|....
gi 45826397 329 akfNVPLAHMITAGADFMLVPSRFEPCGLIQLHA 362
Cdd:cd03825 253 ---DDEQLVDIYSAADLFVHPSLADNLPNTLLEA 283
|
|
| |
