|
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 ... |
5-353 |
6.47e-130 |
|
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: 379.99 E-value: 6.47e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 5 TSVAIEVKVGDSIEIVRFFHCYKRGVDRVFVDHPMFLEKVWGKtgskiygPKAGQDYLDNELRFSLLCQAALKAPRVLnl 84
Cdd:cd03791 55 RVLGLEVKVGGRGEEVGVFELPVDGVDYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRL-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 85 ncskyfsgpYGEDVLFIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFID 164
Cdd:cd03791 126 ---------GFQPDIIHANDWHTALVPAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPPEL----FHID 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 165 GHEKPvkgRKINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKY 242
Cdd:cd03791 192 GLEFY---GQINFLKAGIVYADRVTTVSPTYAKEILTP-EYGEGLDGVLRARAgkLSGILNGIDYDEWNPATDKLIPANY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 243 DiTTVMDAKPLLKEALQAAVGLPVDRRIPLIGFIGRLEEQKGSDILVAAIHQFIGLDVQIVVLGTGKKKFEQEIEQLEVL 322
Cdd:cd03791 268 S-ANDLEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAER 346
|
330 340 350
....*....|....*....|....*....|.
gi 67037828 323 YPNKAKGVAKFNVPLAHMITAGADFMLVPSR 353
Cdd:cd03791 347 YPGKVAVVIGFDEALAHRIYAGADFFLMPSR 377
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
4-353 |
2.93e-117 |
|
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: 347.72 E-value: 2.93e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 4 DTSVAIEVKVGDSIEIVRFFHCYKRGVDRVFVDHPMFLEKvwgktGSKIYGPkagqDYLDNELRFSLLCQAALKAPRVLN 83
Cdd:TIGR02095 56 KVVELVDLSVGPRTLYVKVFEGVVEGVPVYFIDNPSLFDR-----PGGIYGD----DYPDNAERFAFFSRAAAELLSGLG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 84 lncskyfsgpYGEDVlFIANDWHTALIPCYLKSMYQSrgiyLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFRGSFDFI 163
Cdd:TIGR02095 127 ----------WQPDV-VHAHDWHTALVPALLKAVYRP----NPIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 164 DGHEkpvkgrkINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVK 241
Cdd:TIGR02095 192 FYGR-------VNFLKGGIVYADRVTTVSPTYAREILTP-EFGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKAN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 242 YDITTvMDAKPLLKEALQAAVGLPVDRRIPLIGFIGRLEEQKGSDILVAAIHQFIGLDVQIVVLGTGKKKFEQEIEQLEV 321
Cdd:TIGR02095 264 YSADD-LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAE 342
|
330 340 350
....*....|....*....|....*....|..
gi 67037828 322 LYPNKAKGVAKFNVPLAHMITAGADFMLVPSR 353
Cdd:TIGR02095 343 RYPGNVRVIIGYDEALAHLIYAGADFILMPSR 374
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
9-353 |
2.77e-102 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 309.33 E-value: 2.77e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 9 IEVKVGDSIEIVRFFHCYKRGVDRVFVDHPMFLEkvwgktGSKIYGPkAGQDYLDNELRFSLLCQAALKAPRVLNLNCsk 88
Cdd:COG0297 60 LEVPLGGRTYYARVLEGPDDGVPVYFIDNPELFD------RPGPYGD-PDRDYPDNAERFAFFSRAALELLKGLDWKP-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 89 yfsgpygeDVLFiANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFIDGHEK 168
Cdd:COG0297 131 --------DIIH-CHDWQTGLIPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL----FTPDGLEF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 169 PvkGrKINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITT 246
Cdd:COG0297 197 Y--G-QINFLKAGIVYADRVTTVSPTYAREIQTP-EFGEGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 247 vMDAKPLLKEALQAAVGLPVDRRIPLIGFIGRLEEQKGSDILVAAIHQFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 326
Cdd:COG0297 273 -LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGR 351
|
330 340
....*....|....*....|....*..
gi 67037828 327 AKGVAKFNVPLAHMITAGADFMLVPSR 353
Cdd:COG0297 352 VAVYIGYDEALAHRIYAGADFFLMPSR 378
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
20-353 |
3.09e-88 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 273.15 E-value: 3.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 20 VRFFHCYKRGVDRVFVDHPMFlekvwgktgskiYGPKAGQDYLDNELRFSLLCQAALKAprvlnlnCSKYFSGPygeDVL 99
Cdd:PRK00654 65 VLFGHLEGDGVPVYLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEF-------AEGLDPRP---DIV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 100 FiANDWHTALIPCYLKSMYQSRgiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFR--GSFDFiDGHekpvkgrkINW 177
Cdd:PRK00654 123 H-AHDWHTGLIPALLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAEAFhlEGLEF-YGQ--------ISF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 178 MKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLK 255
Cdd:PRK00654 191 LKAGLYYADRVTTVSPTYAREITTP-EFGYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 256 EALQAAVGLPVDRrIPLIGFIGRLEEQKGSDILVAAIHQFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGVAKFNV 335
Cdd:PRK00654 269 RALQERFGLPDDD-APLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDE 347
|
330
....*....|....*...
gi 67037828 336 PLAHMITAGADFMLVPSR 353
Cdd:PRK00654 348 ALAHRIYAGADMFLMPSR 365
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
1-215 |
1.17e-55 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 181.76 E-value: 1.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 1 DAWDTSVAIEVKVGDsiEIVRFFHCYKRGVDRVFVDHPMFLEKvwgktgSKIYGPKaGQDYLDNELRFSLLCQAALKAPR 80
Cdd:pfam08323 54 DVIRLSVAAGVPVRP--LTVGVARLELDGVDVYFLDNPDYFDR------PGLYGDD-GRDYEDNAERFAFFSRAALELAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 81 VLNlncskyfsgpYGEDVLfIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFRGsf 160
Cdd:pfam08323 125 KLG----------WIPDII-HCHDWHTALVPAYLKEAYADDP-FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN-- 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 67037828 161 dfIDGHEKPvkgRKINWMKAGILESDRVVTVSPYYAQELVSAVDkGVELDNVLRK 215
Cdd:pfam08323 191 --LDGLEFY---GQINFLKAGIVYADAVTTVSPTYAEEIQTPEF-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 ... |
5-353 |
6.47e-130 |
|
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: 379.99 E-value: 6.47e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 5 TSVAIEVKVGDSIEIVRFFHCYKRGVDRVFVDHPMFLEKVWGKtgskiygPKAGQDYLDNELRFSLLCQAALKAPRVLnl 84
Cdd:cd03791 55 RVLGLEVKVGGRGEEVGVFELPVDGVDYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRL-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 85 ncskyfsgpYGEDVLFIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFID 164
Cdd:cd03791 126 ---------GFQPDIIHANDWHTALVPAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPPEL----FHID 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 165 GHEKPvkgRKINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKY 242
Cdd:cd03791 192 GLEFY---GQINFLKAGIVYADRVTTVSPTYAKEILTP-EYGEGLDGVLRARAgkLSGILNGIDYDEWNPATDKLIPANY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 243 DiTTVMDAKPLLKEALQAAVGLPVDRRIPLIGFIGRLEEQKGSDILVAAIHQFIGLDVQIVVLGTGKKKFEQEIEQLEVL 322
Cdd:cd03791 268 S-ANDLEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAER 346
|
330 340 350
....*....|....*....|....*....|.
gi 67037828 323 YPNKAKGVAKFNVPLAHMITAGADFMLVPSR 353
Cdd:cd03791 347 YPGKVAVVIGFDEALAHRIYAGADFFLMPSR 377
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
4-353 |
2.93e-117 |
|
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: 347.72 E-value: 2.93e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 4 DTSVAIEVKVGDSIEIVRFFHCYKRGVDRVFVDHPMFLEKvwgktGSKIYGPkagqDYLDNELRFSLLCQAALKAPRVLN 83
Cdd:TIGR02095 56 KVVELVDLSVGPRTLYVKVFEGVVEGVPVYFIDNPSLFDR-----PGGIYGD----DYPDNAERFAFFSRAAAELLSGLG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 84 lncskyfsgpYGEDVlFIANDWHTALIPCYLKSMYQSrgiyLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFRGSFDFI 163
Cdd:TIGR02095 127 ----------WQPDV-VHAHDWHTALVPALLKAVYRP----NPIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 164 DGHEkpvkgrkINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVK 241
Cdd:TIGR02095 192 FYGR-------VNFLKGGIVYADRVTTVSPTYAREILTP-EFGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKAN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 242 YDITTvMDAKPLLKEALQAAVGLPVDRRIPLIGFIGRLEEQKGSDILVAAIHQFIGLDVQIVVLGTGKKKFEQEIEQLEV 321
Cdd:TIGR02095 264 YSADD-LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAE 342
|
330 340 350
....*....|....*....|....*....|..
gi 67037828 322 LYPNKAKGVAKFNVPLAHMITAGADFMLVPSR 353
Cdd:TIGR02095 343 RYPGNVRVIIGYDEALAHLIYAGADFILMPSR 374
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
9-353 |
2.77e-102 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 309.33 E-value: 2.77e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 9 IEVKVGDSIEIVRFFHCYKRGVDRVFVDHPMFLEkvwgktGSKIYGPkAGQDYLDNELRFSLLCQAALKAPRVLNLNCsk 88
Cdd:COG0297 60 LEVPLGGRTYYARVLEGPDDGVPVYFIDNPELFD------RPGPYGD-PDRDYPDNAERFAFFSRAALELLKGLDWKP-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 89 yfsgpygeDVLFiANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFIDGHEK 168
Cdd:COG0297 131 --------DIIH-CHDWQTGLIPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL----FTPDGLEF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 169 PvkGrKINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITT 246
Cdd:COG0297 197 Y--G-QINFLKAGIVYADRVTTVSPTYAREIQTP-EFGEGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 247 vMDAKPLLKEALQAAVGLPVDRRIPLIGFIGRLEEQKGSDILVAAIHQFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 326
Cdd:COG0297 273 -LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGR 351
|
330 340
....*....|....*....|....*..
gi 67037828 327 AKGVAKFNVPLAHMITAGADFMLVPSR 353
Cdd:COG0297 352 VAVYIGYDEALAHRIYAGADFFLMPSR 378
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
20-353 |
3.09e-88 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 273.15 E-value: 3.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 20 VRFFHCYKRGVDRVFVDHPMFlekvwgktgskiYGPKAGQDYLDNELRFSLLCQAALKAprvlnlnCSKYFSGPygeDVL 99
Cdd:PRK00654 65 VLFGHLEGDGVPVYLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEF-------AEGLDPRP---DIV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 100 FiANDWHTALIPCYLKSMYQSRgiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFR--GSFDFiDGHekpvkgrkINW 177
Cdd:PRK00654 123 H-AHDWHTGLIPALLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAEAFhlEGLEF-YGQ--------ISF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 178 MKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLK 255
Cdd:PRK00654 191 LKAGLYYADRVTTVSPTYAREITTP-EFGYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 256 EALQAAVGLPVDRrIPLIGFIGRLEEQKGSDILVAAIHQFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGVAKFNV 335
Cdd:PRK00654 269 RALQERFGLPDDD-APLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDE 347
|
330
....*....|....*...
gi 67037828 336 PLAHMITAGADFMLVPSR 353
Cdd:PRK00654 348 ALAHRIYAGADMFLMPSR 365
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
49-353 |
2.81e-61 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 203.80 E-value: 2.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 49 GSKIYGPKaGQDYLDNELRFSLLCQAALKAPRVLnlncskyfSGPYGEDVLFiANDWHTALIPCYLKsmYQSRGiylNAK 128
Cdd:PRK14099 96 GNPYVGPD-GKDWPDNAQRFAALARAAAAIGQGL--------VPGFVPDIVH-AHDWQAGLAPAYLH--YSGRP---APG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 129 VAFCIHNIAYQGRFAFSDFPLLNLPDEfrgSFDfIDGHEkpVKGrKINWMKAGILESDRVVTVSPYYAQELVSAvDKGVE 208
Cdd:PRK14099 161 TVFTIHNLAFQGQFPRELLGALGLPPS---AFS-LDGVE--YYG-GIGYLKAGLQLADRITTVSPTYALEIQGP-EAGMG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 209 LDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKEALQAAVGLPVDRRIPLIGFIGRLEEQKGSD 286
Cdd:PRK14099 233 LDGLLRQRAdrLSGILNGIDTAVWNPATDELIAATYDVET-LAARAANKAALQARFGLDPDPDALLLGVISRLSWQKGLD 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67037828 287 ILVAAIHQFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGVAKFNVPLAHMITAGADFMLVPSR 353
Cdd:PRK14099 312 LLLEALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQAGADALLVPSR 378
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
1-215 |
1.17e-55 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 181.76 E-value: 1.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 1 DAWDTSVAIEVKVGDsiEIVRFFHCYKRGVDRVFVDHPMFLEKvwgktgSKIYGPKaGQDYLDNELRFSLLCQAALKAPR 80
Cdd:pfam08323 54 DVIRLSVAAGVPVRP--LTVGVARLELDGVDVYFLDNPDYFDR------PGLYGDD-GRDYEDNAERFAFFSRAALELAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 81 VLNlncskyfsgpYGEDVLfIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFRGsf 160
Cdd:pfam08323 125 KLG----------WIPDII-HCHDWHTALVPAYLKEAYADDP-FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN-- 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 67037828 161 dfIDGHEKPvkgRKINWMKAGILESDRVVTVSPYYAQELVSAVDkGVELDNVLRK 215
Cdd:pfam08323 191 --LDGLEFY---GQINFLKAGIVYADAVTTVSPTYAEEIQTPEF-GGGLDGLLRE 239
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
103-353 |
3.80e-51 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 177.23 E-value: 3.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 103 NDWHTALIPCYLKSMYQSRGIYLNAKVAFCIHNIAYQGRFAFSDFPLLnLPDEFRGSFDfidghekpVKGRKINWMKAGI 182
Cdd:PRK14098 148 HDWYAGLVPLLLKTVYADHEFFKDIKTVLTIHNVYRQGVLPFKVFQKL-LPEEVCSGLH--------REGDEVNMLYTGV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 183 LESDRVVTVSPYYAQELVSAVDKGVELDNVL--RKTSITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKEALQA 260
Cdd:PRK14098 219 EHADLLTTTSPRYAEEIAGDGEEAFGLDKVLeeRKMRLHGILNGIDTRQWNPSTDKLIKKRYSIER-LDGKLENKKALLE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 261 AVGLPVDRRIPLIGFIGRLEEQKGSDILVAAIHQFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGVAKFNVPLAHM 340
Cdd:PRK14098 298 EVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFHL 377
|
250
....*....|...
gi 67037828 341 ITAGADFMLVPSR 353
Cdd:PRK14098 378 AIAGLDMLLMPGK 390
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
103-352 |
1.56e-31 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 125.78 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 103 NDWHTALI-PCYLkSMYQSRGIYlNAKVAFCIHNIAYQGRFAFSDFPL-------LNLPDEFRgsfDFIDGHEKPVKGrk 174
Cdd:PLN02939 617 HDWQTAFVaPLYW-DLYAPKGFN-SARICFTCHNFEYQGTAPASDLAScgldvhqLDRPDRMQ---DNAHGRINVVKG-- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 175 inwmkaGILESDRVVTVSPYYAQELVSAVDKGVELDNVLRKTSITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLL 254
Cdd:PLN02939 690 ------AIVYSNIVTTVSPTYAQEVRSEGGRGLQDTLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNAND-LQGKAAN 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 255 KEALQAAVGLP-VDRRIPLIGFIGRLEEQKGSDILVAAIHQFIGLDVQIVVLGTG-----KKKFEQEIEQLEvlYPNKAK 328
Cdd:PLN02939 763 KAALRKQLGLSsADASQPLVGCITRLVPQKGVHLIRHAIYKTAELGGQFVLLGSSpvphiQREFEGIADQFQ--SNNNIR 840
|
250 260
....*....|....*....|....
gi 67037828 329 GVAKFNVPLAHMITAGADFMLVPS 352
Cdd:PLN02939 841 LILKYDEALSHSIYAASDMFIIPS 864
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
52-352 |
6.66e-27 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 111.89 E-value: 6.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 52 IYGPKagqdylDNELRFSLLCQAALKAPRvlnlncskyfSGPYGEDVLFiANDWHTALIPCYLKSMYQSRGIyLNAKVAF 131
Cdd:PLN02316 682 VYGCR------NDGERFGFFCHAALEFLL----------QSGFHPDIIH-CHDWSSAPVAWLFKDHYAHYGL-SKARVVF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 132 CIHNIayqgrfafsdfpllnlpdEFrgsfdfidghekpvkgrKINWMKAGILESDRVVTVSPYYAQELV--SAVdkgvel 209
Cdd:PLN02316 744 TIHNL------------------EF-----------------GANHIGKAMAYADKATTVSPTYSREVSgnSAI------ 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 210 dnVLRKTSITGIVNGMDTQEWNPATDKYTDVKYDITTVMDAKPLLKEALQAAVGL-PVDrrIPLIGFIGRLEEQKGSDIL 288
Cdd:PLN02316 783 --APHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLkQAD--LPLVGIITRLTHQKGIHLI 858
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67037828 289 VAAIHQFIGLDVQIVVLGTG-----KKKFEQEIEQLEVLYPNKAKGVAKFNVPLAHMITAGADFMLVPS 352
Cdd:PLN02316 859 KHAIWRTLERNGQVVLLGSApdpriQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPS 927
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
156-353 |
1.70e-08 |
|
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: 55.62 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 156 FRGSFDFIDGHEKPVKGRKINWMKAGILESDRVVTVSPYYAQELVSAvdkgveldNVLRKTSITGIVNGMDTQEWNPATD 235
Cdd:cd03801 112 LHGAEPGRLLLLLAAERRLLARAEALLRRADAVIAVSEALRDELRAL--------GGIPPEKIVVIPNGVDLERFSPPLR 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 236 KytdvkydittvmdakpllkealqaAVGLPVDRriPLIGFIGRLEEQKGSDILVAAIHQFI--GLDVQIVVLGTGkkkfE 313
Cdd:cd03801 184 R------------------------KLGIPPDR--PVLLFVGRLSPRKGVDLLLEALAKLLrrGPDVRLVIVGGD----G 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 67037828 314 QEIEQLEVLYPNKAKGVaKF--NVPLAHM--ITAGADFMLVPSR 353
Cdd:cd03801 234 PLRAELEELELGLGDRV-RFlgFVPDEELpaLYAAADVFVLPSR 276
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
184-323 |
8.15e-05 |
|
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: 44.15 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 184 ESDRVVTVSPYYAQELVSAVDKGVELDNVlrktsitgIVNGMDTQEWNPATDKytdvkydittvmdakpllkEALQAAVG 263
Cdd:cd03800 163 AADRVIASTPQEADELISLYGADPSRINV--------VPPGVDLERFFPVDRA-------------------EARRARLL 215
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67037828 264 LPVDRRIPLigFIGRLEEQKGSDILVAAIHQFIGLDVQ---IVVLGT---GKKKFEQEIEQLEVLY 323
Cdd:cd03800 216 LPPDKPVVL--ALGRLDPRKGIDTLVRAFAQLPELRELanlVLVGGPsddPLSMDREELAELAEEL 279
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
273-353 |
6.91e-04 |
|
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: 41.16 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 273 IGFIGRLEEQKGSDILVAAIHQFIGLDVQIVVLGTGKkkfEQEIEQLEVLYPNKAKGVAKFNVPLAHMitAGADFMLVPS 352
Cdd:cd03823 194 FGYIGRLTEEKGIDLLVEAFKRLPREDIELVIAGHGP---LSDERQIEGGRRIAFLGRVPTDDIKDFY--EKIDVLVVPS 268
|
.
gi 67037828 353 R 353
Cdd:cd03823 269 I 269
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
271-319 |
1.92e-03 |
|
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: 39.65 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 67037828 271 PLIGFIGRLEEQKGSDILVAAIHQFI--GLDVQIVVLGTG--KKKFEQEIEQL 319
Cdd:cd03811 189 PVILAVGRLDPQKGHDLLIEAFAKLRkkYPDVKLVILGDGplREELEKLAKEL 241
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
184-353 |
3.86e-03 |
|
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: 38.90 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 184 ESDRVVTVSPYYAQELVSAvdkGVELDNVlrktsiTGIVNGMDTQEWNPATdkytdvkydittvmdakpllkealqAAVG 263
Cdd:cd03798 150 RAARVIAVSKALAEELVAL---GVPRDRV------DVIPNGVDPARFQPED-------------------------RGLG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 264 LPVDRRIplIGFIGRLEEQKGSDILVAAIHQFI--GLDVQIVVLGTG--KKKFEQEIEQLevlypNKAKGVaKFNVPL-- 337
Cdd:cd03798 196 LPLDAFV--ILFVGRLIPRKGIDLLLEAFARLAkaRPDVVLLIVGDGplREALRALAEDL-----GLGDRV-TFTGRLph 267
|
170 180
....*....|....*....|
gi 67037828 338 ----AHMitAGADFMLVPSR 353
Cdd:cd03798 268 eqvpAYY--RACDVFVLPSR 285
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
275-353 |
4.52e-03 |
|
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: 38.15 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 275 FIGRLEEQKGSDILVAAI----HQFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGvAKFNVPLAHMITAGADFMLV 350
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALallkARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIG-GLVDDEVLELLLAAADVFVL 193
|
...
gi 67037828 351 PSR 353
Cdd:cd01635 194 PSR 196
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
271-353 |
6.00e-03 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 36.72 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037828 271 PLIGFIGRL-EEQKGSDILVAAIHQFI--GLDVQIVVLGTGkkkfeqEIEQLEVLYPNKAKGVaKF--NVPLAHMITAGA 345
Cdd:pfam13692 2 PVILFVGRLhPNVKGVDYLLEAVPLLRkrDNDVRLVIVGDG------PEEELEELAAGLEDRV-IFtgFVEDLAELLAAA 74
|
....*...
gi 67037828 346 DFMLVPSR 353
Cdd:pfam13692 75 DVFVLPSL 82
|
|
| |
