|
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 ... |
2-237 |
1.41e-103 |
|
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: 307.95 E-value: 1.41e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 2 KGIYKTAKVAFCIHNIAYQGRFSFSDFSLLNLPDQLkssfDFLDGYRKPvkgRKINWMKAGVLESDRVLTVSPYYAQELA 81
Cdd:cd03791 152 GPGFKKIKTVFTIHNLAYQGLFPLDTLAELGLPPEL----FHIDGLEFY---GQINFLKAGIVYADRVTTVSPTYAKEIL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 82 SNEAkGVELDNIIRK--TGITGIVNGMDVQEWNPSTDKYIDVQYDATTVmAAKPLLKETLQAAVGLPVDRDIPLIGFIGR 159
Cdd:cd03791 225 TPEY-GEGLDGVLRAraGKLSGILNGIDYDEWNPATDKLIPANYSANDL-EGKAENKAALQKELGLPVDPDAPLFGFVGR 302
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835737202 160 LEEQKGSDILAAAIPKFIGENVQIVVLGTGKKSMEKQLEELEMKYPNKARGVVKFNVPLAHMITAGADFIIVPSRFEP 237
Cdd:cd03791 303 LTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEP 380
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
8-237 |
8.22e-98 |
|
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: 293.02 E-value: 8.22e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 8 AKVAFCIHNIAYQGRFSFSDFSLLNLPDQLKSSFDFLDGYRkpvkgrkINWMKAGVLESDRVLTVSPYYAQELaSNEAKG 87
Cdd:TIGR02095 155 IKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLEFYGR-------VNFLKGGIVYADRVTTVSPTYAREI-LTPEFG 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 88 VELDNIIRKTG--ITGIVNGMDVQEWNPSTDKYIDVQYDATTvMAAKPLLKETLQAAVGLPVDRDIPLIGFIGRLEEQKG 165
Cdd:TIGR02095 227 YGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKANYSADD-LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKG 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835737202 166 SDILAAAIPKFIGENVQIVVLGTGKKSMEKQLEELEMKYPNKARGVVKFNVPLAHMITAGADFIIVPSRFEP 237
Cdd:TIGR02095 306 VDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEP 377
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
5-237 |
1.29e-86 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 264.65 E-value: 1.29e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 5 YKTAKVAFCIHNIAYQGRFSFSDFSLLNLPDQLkSSFDFLDGYrkpvkGrKINWMKAGVLESDRVLTVSPYYAQELASNE 84
Cdd:COG0297 156 FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL-FTPDGLEFY-----G-QINFLKAGIVYADRVTTVSPTYAREIQTPE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 85 AkGVELDNIIRKTG--ITGIVNGMDVQEWNPSTDKYIDVQYDATTvMAAKPLLKETLQAAVGLPVDRDIPLIGFIGRLEE 162
Cdd:COG0297 229 F-GEGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD-LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTE 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835737202 163 QKGSDILAAAIPKFIGENVQIVVLGTGKKSMEKQLEELEMKYPNKARGVVKFNVPLAHMITAGADFIIVPSRFEP 237
Cdd:COG0297 307 QKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEP 381
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
5-237 |
2.64e-76 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 237.71 E-value: 2.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 5 YKTAKVAFCIHNIAYQGRFSFSDFSLLNLPDqlkSSFDfLDGYRKPvkgRKINWMKAGVLESDRVLTVSPYYAQELaSNE 84
Cdd:PRK00654 144 YPDIKTVFTIHNLAYQGLFPAEILGELGLPA---EAFH-LEGLEFY---GQISFLKAGLYYADRVTTVSPTYAREI-TTP 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 85 AKGVELDNIIRKTG--ITGIVNGMDVQEWNPSTDKYIDVQYDATTvMAAKPLLKETLQAAVGLPVDrDIPLIGFIGRLEE 162
Cdd:PRK00654 216 EFGYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENKRALQERFGLPDD-DAPLFAMVSRLTE 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835737202 163 QKGSDILAAAIPKFIGENVQIVVLGTGKKSMEKQLEELEMKYPNKARGVVKFNVPLAHMITAGADFIIVPSRFEP 237
Cdd:PRK00654 294 QKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEP 368
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
5-96 |
3.21e-24 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 96.63 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 5 YKTAKVAFCIHNIAYQGRFSFSDFSLLNLPDQLKSsfdfLDGYRKPvkgRKINWMKAGVLESDRVLTVSPYYAQELASnE 84
Cdd:pfam08323 156 FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN----LDGLEFY---GQINFLKAGIVYADAVTTVSPTYAEEIQT-P 227
|
90
....*....|..
gi 835737202 85 AKGVELDNIIRK 96
Cdd:pfam08323 228 EFGGGLDGLLRE 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 ... |
2-237 |
1.41e-103 |
|
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: 307.95 E-value: 1.41e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 2 KGIYKTAKVAFCIHNIAYQGRFSFSDFSLLNLPDQLkssfDFLDGYRKPvkgRKINWMKAGVLESDRVLTVSPYYAQELA 81
Cdd:cd03791 152 GPGFKKIKTVFTIHNLAYQGLFPLDTLAELGLPPEL----FHIDGLEFY---GQINFLKAGIVYADRVTTVSPTYAKEIL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 82 SNEAkGVELDNIIRK--TGITGIVNGMDVQEWNPSTDKYIDVQYDATTVmAAKPLLKETLQAAVGLPVDRDIPLIGFIGR 159
Cdd:cd03791 225 TPEY-GEGLDGVLRAraGKLSGILNGIDYDEWNPATDKLIPANYSANDL-EGKAENKAALQKELGLPVDPDAPLFGFVGR 302
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835737202 160 LEEQKGSDILAAAIPKFIGENVQIVVLGTGKKSMEKQLEELEMKYPNKARGVVKFNVPLAHMITAGADFIIVPSRFEP 237
Cdd:cd03791 303 LTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEP 380
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
8-237 |
8.22e-98 |
|
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: 293.02 E-value: 8.22e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 8 AKVAFCIHNIAYQGRFSFSDFSLLNLPDQLKSSFDFLDGYRkpvkgrkINWMKAGVLESDRVLTVSPYYAQELaSNEAKG 87
Cdd:TIGR02095 155 IKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLEFYGR-------VNFLKGGIVYADRVTTVSPTYAREI-LTPEFG 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 88 VELDNIIRKTG--ITGIVNGMDVQEWNPSTDKYIDVQYDATTvMAAKPLLKETLQAAVGLPVDRDIPLIGFIGRLEEQKG 165
Cdd:TIGR02095 227 YGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKANYSADD-LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKG 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835737202 166 SDILAAAIPKFIGENVQIVVLGTGKKSMEKQLEELEMKYPNKARGVVKFNVPLAHMITAGADFIIVPSRFEP 237
Cdd:TIGR02095 306 VDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEP 377
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
5-237 |
1.29e-86 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 264.65 E-value: 1.29e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 5 YKTAKVAFCIHNIAYQGRFSFSDFSLLNLPDQLkSSFDFLDGYrkpvkGrKINWMKAGVLESDRVLTVSPYYAQELASNE 84
Cdd:COG0297 156 FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL-FTPDGLEFY-----G-QINFLKAGIVYADRVTTVSPTYAREIQTPE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 85 AkGVELDNIIRKTG--ITGIVNGMDVQEWNPSTDKYIDVQYDATTvMAAKPLLKETLQAAVGLPVDRDIPLIGFIGRLEE 162
Cdd:COG0297 229 F-GEGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD-LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTE 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835737202 163 QKGSDILAAAIPKFIGENVQIVVLGTGKKSMEKQLEELEMKYPNKARGVVKFNVPLAHMITAGADFIIVPSRFEP 237
Cdd:COG0297 307 QKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEP 381
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
5-237 |
2.64e-76 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 237.71 E-value: 2.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 5 YKTAKVAFCIHNIAYQGRFSFSDFSLLNLPDqlkSSFDfLDGYRKPvkgRKINWMKAGVLESDRVLTVSPYYAQELaSNE 84
Cdd:PRK00654 144 YPDIKTVFTIHNLAYQGLFPAEILGELGLPA---EAFH-LEGLEFY---GQISFLKAGLYYADRVTTVSPTYAREI-TTP 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 85 AKGVELDNIIRKTG--ITGIVNGMDVQEWNPSTDKYIDVQYDATTvMAAKPLLKETLQAAVGLPVDrDIPLIGFIGRLEE 162
Cdd:PRK00654 216 EFGYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENKRALQERFGLPDD-DAPLFAMVSRLTE 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835737202 163 QKGSDILAAAIPKFIGENVQIVVLGTGKKSMEKQLEELEMKYPNKARGVVKFNVPLAHMITAGADFIIVPSRFEP 237
Cdd:PRK00654 294 QKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEP 368
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
9-237 |
1.88e-58 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 192.24 E-value: 1.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 9 KVAFCIHNIAYQGRFSFSDFSLLNLPdqlKSSFDfLDG--YRKpvkgrKINWMKAGVLESDRVLTVSPYYAQELASNEAk 86
Cdd:PRK14099 160 GTVFTIHNLAFQGQFPRELLGALGLP---PSAFS-LDGveYYG-----GIGYLKAGLQLADRITTVSPTYALEIQGPEA- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 87 GVELDNIIRKTG--ITGIVNGMDVQEWNPSTDKYIDVQYDATTvMAAKPLLKETLQAAVGLPVDRDIPLIGFIGRLEEQK 164
Cdd:PRK14099 230 GMGLDGLLRQRAdrLSGILNGIDTAVWNPATDELIAATYDVET-LAARAANKAALQARFGLDPDPDALLLGVISRLSWQK 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 835737202 165 GSDILAAAIPKFIGENVQIVVLGTGKKSMEKQLEELEMKYPNKARGVVKFNVPLAHMITAGADFIIVPSRFEP 237
Cdd:PRK14099 309 GLDLLLEALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQAGADALLVPSRFEP 381
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
5-236 |
6.24e-42 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 148.73 E-value: 6.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 5 YKTAKVAFCIHNIAYQGRFSFSDFSLLnLPDQLKSSFDfldgyrkpVKGRKINWMKAGVLESDRVLTVSPYYAQELASNE 84
Cdd:PRK14098 169 FKDIKTVLTIHNVYRQGVLPFKVFQKL-LPEEVCSGLH--------REGDEVNMLYTGVEHADLLTTTSPRYAEEIAGDG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 85 AKGVELDNII--RKTGITGIVNGMDVQEWNPSTDKYIDVQYDATTvMAAKPLLKETLQAAVGLPVDRDIPLIGFIGRLEE 162
Cdd:PRK14098 240 EEAFGLDKVLeeRKMRLHGILNGIDTRQWNPSTDKLIKKRYSIER-LDGKLENKKALLEEVGLPFDEETPLVGVIINFDD 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 835737202 163 QKGSDILAAAIPKFIGENVQIVVLGTGKKSMEKQLEELEMKYPNKARGVVKFNVPLAHMITAGADFIIVPSRFE 236
Cdd:PRK14098 319 FQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFHLAIAGLDMLLMPGKIE 392
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
5-237 |
4.88e-33 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 126.17 E-value: 4.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 5 YKTAKVAFCIHNIAYQGRFSFSDFSL-------LNLPDQLKSSfdfldgyrkpvKGRKINWMKAGVLESDRVLTVSPYYA 77
Cdd:PLN02939 637 FNSARICFTCHNFEYQGTAPASDLAScgldvhqLDRPDRMQDN-----------AHGRINVVKGAIVYSNIVTTVSPTYA 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 78 QELASNEAKGVELDNIIRKTGITGIVNGMDVQEWNPSTDKYIDVQYDATTvMAAKPLLKETLQAAVGLP-VDRDIPLIGF 156
Cdd:PLN02939 706 QEVRSEGGRGLQDTLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNAND-LQGKAANKAALRKQLGLSsADASQPLVGC 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 157 IGRLEEQKGSDILAAAIPKFIGENVQIVVLGTGK-KSMEKQLEELEMKYP--NKARGVVKFNVPLAHMITAGADFIIVPS 233
Cdd:PLN02939 785 ITRLVPQKGVHLIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGIADQFQsnNNIRLILKYDEALSHSIYAASDMFIIPS 864
|
....
gi 835737202 234 RFEP 237
Cdd:PLN02939 865 MFEP 868
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
66-237 |
3.90e-31 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 120.75 E-value: 3.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 66 SDRVLTVSPYYAQELASNEAKGVELDNIirktgiTGIVNGMDVQEWNPSTDKYIDVQYDATTVMAAKPLLKETLQAAVGL 145
Cdd:PLN02316 762 ADKATTVSPTYSREVSGNSAIAPHLYKF------HGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGL 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 146 PvDRDIPLIGFIGRLEEQKGSDILAAAIPKFIGENVQIVVLGTG-----KKSMEKQLEELEMKYPNKARGVVKFNVPLAH 220
Cdd:PLN02316 836 K-QADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGSApdpriQNDFVNLANQLHSSHHDRARLCLTYDEPLSH 914
|
170
....*....|....*..
gi 835737202 221 MITAGADFIIVPSRFEP 237
Cdd:PLN02316 915 LIYAGADFILVPSIFEP 931
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
5-96 |
3.21e-24 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 96.63 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 5 YKTAKVAFCIHNIAYQGRFSFSDFSLLNLPDQLKSsfdfLDGYRKPvkgRKINWMKAGVLESDRVLTVSPYYAQELASnE 84
Cdd:pfam08323 156 FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN----LDGLEFY---GQINFLKAGIVYADAVTTVSPTYAEEIQT-P 227
|
90
....*....|..
gi 835737202 85 AKGVELDNIIRK 96
Cdd:pfam08323 228 EFGGGLDGLLRE 239
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
39-237 |
1.36e-12 |
|
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: 66.02 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 39 SSFDFLDGYRKPVKGRKINWMKAGVLESDRVLTVSPYYAQELAsnEAKGVELDNIIRktgitgIVNGMDVQEWNPSTDKy 118
Cdd:cd03801 114 GAEPGRLLLLLAAERRLLARAEALLRRADAVIAVSEALRDELR--ALGGIPPEKIVV------IPNGVDLERFSPPLRR- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 119 idvqydattvmaakpllketlqaavGLPVDRDIPLIGFIGRLEEQKGSDILAAAIPKFI--GENVQIVVLGtGKKSMEKQ 196
Cdd:cd03801 185 -------------------------KLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLrrGPDVRLVIVG-GDGPLRAE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 835737202 197 LEELEMKYPNKargvVKF--NVPLAHM--ITAGADFIIVPSRFEP 237
Cdd:cd03801 239 LEELELGLGDR----VRFlgFVPDEELpaLYAAADVFVLPSRYEG 279
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
152-237 |
1.95e-05 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 43.27 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 152 PLIGFIGRL-EEQKGSDILAAAIPKFIGE--NVQIVVLGTGKksmEKQLEELEMKYPNKAR--GVVKfNVPlAHMitAGA 226
Cdd:pfam13692 2 PVILFVGRLhPNVKGVDYLLEAVPLLRKRdnDVRLVIVGDGP---EEELEELAAGLEDRVIftGFVE-DLA-ELL--AAA 74
|
90
....*....|.
gi 835737202 227 DFIIVPSRFEP 237
Cdd:pfam13692 75 DVFVLPSLYEG 85
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
152-237 |
2.69e-05 |
|
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: 43.03 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 152 PLIGFIGRLEEQKGSDILAAAIPKFIGENVQIVVLGTGKKSMEKQLEELEMKYPNKARGVVKFNVP---LAHMITAgADF 228
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSdedLPELLKI-ADV 81
|
....*....
gi 835737202 229 IIVPSRFEP 237
Cdd:pfam00534 82 FVLPSRYEG 90
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
154-236 |
3.10e-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: 44.24 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 154 IGFIGRLEEQKGSDILAAAIPKFIGENVQIVVLGtgkKSMEKQLEELEMKYPNKARGVVKFNVPLAHMitAGADFIIVPS 233
Cdd:cd03823 194 FGYIGRLTEEKGIDLLVEAFKRLPREDIELVIAG---HGPLSDERQIEGGRRIAFLGRVPTDDIKDFY--EKIDVLVVPS 268
|
...
gi 835737202 234 RFE 236
Cdd:cd03823 269 IWP 271
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
156-237 |
1.44e-04 |
|
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: 41.62 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 156 FIGRLEEQKGSDILAAAIPKF--IGENVQIVVLGTGK-KSMEKQLEELEMKYPNKARGVVKFNVPLAHMITAGADFIIVP 232
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLkaRLPDLVLVLVGGGGeREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLP 194
|
....*
gi 835737202 233 SRFEP 237
Cdd:cd01635 195 SRSEG 199
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
65-237 |
3.19e-04 |
|
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: 41.07 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 65 ESDRVLTVSPYYAQELASN-EAKGVEldniirktgITGIVNGMDVQEWNPSTDKyidvqydattvmaakpllkETLQAAV 143
Cdd:cd03800 163 AADRVIASTPQEADELISLyGADPSR---------INVVPPGVDLERFFPVDRA-------------------EARRARL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 144 GLPVDRDIPLigFIGRLEEQKGSDIL--AAAIPKFIGENVQIVVLG---TGKKSMEKQLEElEMKYPNKARGVVKFNVPL 218
Cdd:cd03800 215 LLPPDKPVVL--ALGRLDPRKGIDTLvrAFAQLPELRELANLVLVGgpsDDPLSMDREELA-ELAEELGLIDRVRFPGRV 291
|
170 180
....*....|....*....|...
gi 835737202 219 AH----MITAGADFIIVPSRFEP 237
Cdd:cd03800 292 SRddlpELYRAADVFVVPSLYEP 314
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
54-237 |
3.64e-04 |
|
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: 40.80 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 54 RKINWMKAGVLESDRVLTVSPYYAQELASNeakgveldNIIRKTGITGIVNGMDVqewnpstdkyidvqyDATTVMAAKP 133
Cdd:cd03811 124 KKLLLKLKLYKKADKIVCVSKGIKEDLIRL--------GPSPPEKIEVIYNPIDI---------------DRIRALAKEP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 134 LLKEtlqaavglpvDRDIPLIGFIGRLEEQKGSDIL--AAAIPKFIGENVQIVVLGTG--KKSMEKQLEELEMKypnkar 209
Cdd:cd03811 181 ILNE----------PEDGPVILAVGRLDPQKGHDLLieAFAKLRKKYPDVKLVILGDGplREELEKLAKELGLA------ 244
|
170 180 190
....*....|....*....|....*....|...
gi 835737202 210 GVVKF-----NvPLAHMitAGADFIIVPSRFEP 237
Cdd:cd03811 245 ERVIFlgfqsN-PYPYL--KKADLFVLSSRYEG 274
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
81-236 |
8.63e-04 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 39.99 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 81 ASNEAKGVELDNIIRKTGITGIVNGMDVQEWNPSTDKyidvqydattvmaakpllkeTLQAAVGLPVDRDIPLIGFIGRL 160
Cdd:cd03807 140 NSSAVAEFHQEQGYAKNKIVVIYNGIDLFKLSPDDAS--------------------RARARRRLGLAEDRRVIGIVGRL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 161 EEQKGSDILAAAIPKFIGENVQIVVLGTGKKSMEKQLEELEMKYPNKARgvVKF-----NVP--LAHMitagaDFIIVPS 233
Cdd:cd03807 200 HPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERLLLELGLEDR--VHLlgersDVPalLPAM-----DIFVLSS 272
|
...
gi 835737202 234 RFE 236
Cdd:cd03807 273 RTE 275
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
54-236 |
1.01e-03 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
Pssm-ID: 340837 [Multi-domain] Cd Length: 358 Bit Score: 39.50 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 54 RKINWMKAGVLE------SDRVLTVSPYYAQELasneakgveLDNIIRKTGITGIV--NGMDVQEWNPSTDKYIDvqyda 125
Cdd:cd03808 122 GKLLRLLYLLLEklallfTDKVIFVNEDDRDLA---------IKKGIIKKKKTVLIpgSGVDLDRFQYSPESLPS----- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 126 ttvmaakpllketlqaavglpvdrDIPLIGFIGRLEEQKGSDIL--AAAIPKFIGENVQIVVLGTG--KKSMEKQLEELE 201
Cdd:cd03808 188 ------------------------EKVVFLFVARLLKDKGIDELieAAKILKKKGPNVRFLLVGDGelENPSEILIEKLG 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 835737202 202 mkypnkARGVVKF-----NVPlaHMITAgADFIIVPSRFE 236
Cdd:cd03808 244 ------LEGRIEFlgfrsDVP--ELLAE-SDVFVLPSYRE 274
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
146-204 |
2.33e-03 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 38.37 E-value: 2.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835737202 146 PVDRDIPLIGFIGRLEEQKGSDILAAAIPKFIG--ENVQIVVLGTGKKsmEKQLEELEMKY 204
Cdd:cd03796 188 KPDPNKITIVVISRLVYRKGIDLLVGIIPRICKkhPNVRFIIGGDGPK--RIELEEMREKY 246
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
119-237 |
9.25e-03 |
|
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.
Pssm-ID: 340846 [Multi-domain] Cd Length: 345 Bit Score: 36.56 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835737202 119 IDVQYDATTVMAAKPLLKETLQAAVGLPvdRDIPLIGFIGRLEEQKGSDILAAAIPKFIGE-NVQIVVLGTG--KKSMEK 195
Cdd:cd03819 152 IRVIPNGVDTDRFPPEAEAEERAQLGLP--EGKPVVGYVGRLSPEKGWLLLVDAAAELKDEpDFRLLVAGDGpeRDEIRR 229
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 835737202 196 QLEELemkypnKARGVVKF-----NVPLAHmitAGADFIIVPSRFEP 237
Cdd:cd03819 230 LVERL------GLRDRVTFtgfreDVPAAL---AASDVVVLPSLHEE 267
|
|
| |
