|
Name |
Accession |
Description |
Interval |
E-value |
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
1-471 |
0e+00 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 612.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 1 MNILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLYQQIKSRESEMTLKGTSKIRLGDVEKPVSFYELNYEN 80
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIDDKLKDLEVVASLEVPLGGRTYYARVLEGPDDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 81 VQYIFVDNDDFFNRPKLYG-----YEDDAVRFTFFNFSIFEYIKLSNEYPDIIHVNDWQTGMIPFFLDTRYRSQnaGFQK 155
Cdd:COG0297 81 VPVYFIDNPELFDRPGPYGdpdrdYPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADD--PFKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 156 IKSLLSIHNLEKQGSYPIETEKIFG--NKNFTY---IHMDRVNFLKCGIMRANAINTVSESYRNEILTRFYGFTLDGPLK 230
Cdd:COG0297 159 IKTVFTIHNLAYQGIFPAEILELLGlpPELFTPdglEFYGQINFLKAGIVYADRVTTVSPTYAREIQTPEFGEGLDGLLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 231 SRQYDLYGILNGLDQDLYNPSLSKYIVRNYDENNfIEGKNTNKEFLLRTLSLDSINDMPLVSFITRFARQKGIDIMMTSL 310
Cdd:COG0297 239 ARSGKLSGILNGIDYDVWNPATDPYLPANYSADD-LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 311 EDYLKQGkINFIALGSGDALYESFFTQMQTKYPTHVFYQSGFDIELSQKVYAASDLFMLPSLFEPCGLNHMIAMKYGALP 390
Cdd:COG0297 318 DELLEED-VQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYGTVP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 391 IVRETGGLKDTVTPYNKFTGVGVGFAFKNYDATEFKEAIDQALDIYhHDKEAWNNLIHQAMHVNHSLSKMAKQYEDLYQK 470
Cdd:COG0297 397 IVRRTGGLADTVIDYNEATGEGTGFVFDEYTAEALLAAIRRALALY-RDPEAWRKLQRNAMKQDFSWEKSAKEYLELYRE 475
|
.
gi 1088626635 471 I 471
Cdd:COG0297 476 L 476
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
2-470 |
0e+00 |
|
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: 551.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 2 NILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLYQQIKSRESEMTLKGTSKIRLGDVEKPVSFYELNYENV 81
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEVKVGGRGEEVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 82 QYIFVDNDDFFNRPKL-----YGYEDDAVRFTFFNFSIFEYIKLSNEYPDIIHVNDWQTGMIPFFLDTRYRsqNAGFQKI 156
Cdd:cd03791 81 DYYFLDNPEFFDRPGLpgppgYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYR--GPGFKKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 157 KSLLSIHNLEKQGSYPIET-EKIFGNKNF----TYIHMDRVNFLKCGIMRANAINTVSESYRNEILTRFYGFTLDGPLKS 231
Cdd:cd03791 159 KTVFTIHNLAYQGLFPLDTlAELGLPPELfhidGLEFYGQINFLKAGIVYADRVTTVSPTYAKEILTPEYGEGLDGVLRA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 232 RQYDLYGILNGLDQDLYNPSLSKYIVRNYDENNfIEGKNTNKEFLLRTLSLDSINDMPLVSFITRFARQKGIDIMMTSLE 311
Cdd:cd03791 239 RAGKLSGILNGIDYDEWNPATDKLIPANYSAND-LEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 312 DYLKQGkINFIALGSGDALYESFFTQMQTKYPTHVFYQSGFDIELSQKVYAASDLFMLPSLFEPCGLNHMIAMKYGALPI 391
Cdd:cd03791 318 ELLEEG-GQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTLPI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088626635 392 VRETGGLKDTVTPYNKFTGVGVGFAFKNYDATEFKEAIDQALDIYhHDKEAWNNLIHQAMHVNHSLSKMAKQYEDLYQK 470
Cdd:cd03791 397 VRRTGGLADTVFDYDPETGEGTGFVFEDYDAEALLAALRRALALY-RNPELWRKLQKNAMKQDFSWDKSAKEYLELYRS 474
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
1-473 |
0e+00 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 523.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 1 MNILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLYQQIKSRESEMTLKGtskiRLGDVEkpVSFYELNYEN 80
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKLRDAQVVG----RLDLFT--VLFGHLEGDG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 81 VQYIFVDNDDFFNRPKLYGYEDDAVRFTFFNFSIFEYIKLSNEYPDIIHVNDWQTGMIPFFLDTRYRsqnAGFQKIKSLL 160
Cdd:PRK00654 75 VPVYLIDAPHLFDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGLIPALLKEKYW---RGYPDIKTVF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 161 SIHNLEKQGSYPIETEKIFGNKNFTYiHMDR------VNFLKCGIMRANAINTVSESYRNEILTRFYGFTLDGPLKSRQY 234
Cdd:PRK00654 152 TIHNLAYQGLFPAEILGELGLPAEAF-HLEGlefygqISFLKAGLYYADRVTTVSPTYAREITTPEFGYGLEGLLRARSG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 235 DLYGILNGLDQDLYNPSLSKYIVRNYDENNFiEGKNTNKEFLLRTLSLDSiNDMPLVSFITRFARQKGIDIMMTSLEDYL 314
Cdd:PRK00654 231 KLSGILNGIDYDIWNPETDPLLAANYSADDL-EGKAENKRALQERFGLPD-DDAPLFAMVSRLTEQKGLDLVLEALPELL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 315 KQGkINFIALGSGDALYESFFTQMQTKYPTHVFYQSGFDIELSQKVYAASDLFMLPSLFEPCGLNHMIAMKYGALPIVRE 394
Cdd:PRK00654 309 EQG-GQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPIVRR 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088626635 395 TGGLKDTVTPYNKFTGVGVGFAFKNYDATEFKEAIDQALDIYHHDKEaWNNLIHQAMHVNHSLSKMAKQYEDLYQKILN 473
Cdd:PRK00654 388 TGGLADTVIDYNPEDGEATGFVFDDFNAEDLLRALRRALELYRQPPL-WRALQRQAMAQDFSWDKSAEEYLELYRRLLG 465
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
1-471 |
1.52e-168 |
|
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: 482.92 E-value: 1.52e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 1 MNILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLYQQIKSRESEMTLKGTSK-IRLGDVEKPVSFYELNYE 79
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVVELVdLSVGPRTLYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 80 NVQYIFVDNDDFFNRP-KLYG--YEDDAVRFTFFNFSIFEYIKLSNEYPDIIHVNDWQTGMIPFFLDTRYRsqnagFQKI 156
Cdd:TIGR02095 81 GVPVYFIDNPSLFDRPgGIYGddYPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVYR-----PNPI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 157 KSLLSIHNLEKQGSYPIETEKIFGNKNFtYIHM------DRVNFLKCGIMRANAINTVSESYRNEILTRFYGFTLDGPLK 230
Cdd:TIGR02095 156 KTVFTIHNLAYQGVFPADDFSELGLPPE-YFHMeglefyGRVNFLKGGIVYADRVTTVSPTYAREILTPEFGYGLDGVLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 231 SRQYDLYGILNGLDQDLYNPSLSKYIVRNYDENNFiEGKNTNKEFLLRTLSLDSINDMPLVSFITRFARQKGIDIMMTSL 310
Cdd:TIGR02095 235 ARSGKLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 311 EDYLKQGkINFIALGSGDALYESFFTQMQTKYPTHVFYQSGFDIELSQKVYAASDLFMLPSLFEPCGLNHMIAMKYGALP 390
Cdd:TIGR02095 314 PELLELG-GQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTVP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 391 IVRETGGLKDTVTPYNKFTGVGVGFAFKNYDATEFKEAIDQALDIYHHDKEAWNNLIHQAMHVNHSLSKMAKQYEDLYQK 470
Cdd:TIGR02095 393 IVRRTGGLADTVVDGDPEAESGTGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSAKQYVELYRS 472
|
.
gi 1088626635 471 I 471
Cdd:TIGR02095 473 L 473
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
3-230 |
3.45e-83 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 256.49 E-value: 3.45e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 3 ILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLYQQIKSRESEMTLKGTSKIRLGDVEKP--VSFYELNYEN 80
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEERNQLEDVIRLSVAAGVPVRPltVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 81 VQYIFVDNDDFFNRPKLYG-----YEDDAVRFTFFNFSIFEYIKLSNEYPDIIHVNDWQTGMIPFFLDTRYRsqNAGFQK 155
Cdd:pfam08323 81 VDVYFLDNPDYFDRPGLYGddgrdYEDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYA--DDPFKN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 156 IKSLLSIHNLEKQGSYPIETEKIFG--NKNFT---YIHMDRVNFLKCGIMRANAINTVSESYRNEILTRFYGFTLDGPLK 230
Cdd:pfam08323 159 IKTVFTIHNLAYQGRFPADLLDLLGlpPEDFNldgLEFYGQINFLKAGIVYADAVTTVSPTYAEEIQTPEFGGGLDGLLR 238
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
1-471 |
0e+00 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 612.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 1 MNILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLYQQIKSRESEMTLKGTSKIRLGDVEKPVSFYELNYEN 80
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIDDKLKDLEVVASLEVPLGGRTYYARVLEGPDDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 81 VQYIFVDNDDFFNRPKLYG-----YEDDAVRFTFFNFSIFEYIKLSNEYPDIIHVNDWQTGMIPFFLDTRYRSQnaGFQK 155
Cdd:COG0297 81 VPVYFIDNPELFDRPGPYGdpdrdYPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADD--PFKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 156 IKSLLSIHNLEKQGSYPIETEKIFG--NKNFTY---IHMDRVNFLKCGIMRANAINTVSESYRNEILTRFYGFTLDGPLK 230
Cdd:COG0297 159 IKTVFTIHNLAYQGIFPAEILELLGlpPELFTPdglEFYGQINFLKAGIVYADRVTTVSPTYAREIQTPEFGEGLDGLLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 231 SRQYDLYGILNGLDQDLYNPSLSKYIVRNYDENNfIEGKNTNKEFLLRTLSLDSINDMPLVSFITRFARQKGIDIMMTSL 310
Cdd:COG0297 239 ARSGKLSGILNGIDYDVWNPATDPYLPANYSADD-LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 311 EDYLKQGkINFIALGSGDALYESFFTQMQTKYPTHVFYQSGFDIELSQKVYAASDLFMLPSLFEPCGLNHMIAMKYGALP 390
Cdd:COG0297 318 DELLEED-VQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYGTVP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 391 IVRETGGLKDTVTPYNKFTGVGVGFAFKNYDATEFKEAIDQALDIYhHDKEAWNNLIHQAMHVNHSLSKMAKQYEDLYQK 470
Cdd:COG0297 397 IVRRTGGLADTVIDYNEATGEGTGFVFDEYTAEALLAAIRRALALY-RDPEAWRKLQRNAMKQDFSWEKSAKEYLELYRE 475
|
.
gi 1088626635 471 I 471
Cdd:COG0297 476 L 476
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
2-470 |
0e+00 |
|
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: 551.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 2 NILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLYQQIKSRESEMTLKGTSKIRLGDVEKPVSFYELNYENV 81
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEVKVGGRGEEVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 82 QYIFVDNDDFFNRPKL-----YGYEDDAVRFTFFNFSIFEYIKLSNEYPDIIHVNDWQTGMIPFFLDTRYRsqNAGFQKI 156
Cdd:cd03791 81 DYYFLDNPEFFDRPGLpgppgYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYR--GPGFKKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 157 KSLLSIHNLEKQGSYPIET-EKIFGNKNF----TYIHMDRVNFLKCGIMRANAINTVSESYRNEILTRFYGFTLDGPLKS 231
Cdd:cd03791 159 KTVFTIHNLAYQGLFPLDTlAELGLPPELfhidGLEFYGQINFLKAGIVYADRVTTVSPTYAKEILTPEYGEGLDGVLRA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 232 RQYDLYGILNGLDQDLYNPSLSKYIVRNYDENNfIEGKNTNKEFLLRTLSLDSINDMPLVSFITRFARQKGIDIMMTSLE 311
Cdd:cd03791 239 RAGKLSGILNGIDYDEWNPATDKLIPANYSAND-LEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 312 DYLKQGkINFIALGSGDALYESFFTQMQTKYPTHVFYQSGFDIELSQKVYAASDLFMLPSLFEPCGLNHMIAMKYGALPI 391
Cdd:cd03791 318 ELLEEG-GQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTLPI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088626635 392 VRETGGLKDTVTPYNKFTGVGVGFAFKNYDATEFKEAIDQALDIYhHDKEAWNNLIHQAMHVNHSLSKMAKQYEDLYQK 470
Cdd:cd03791 397 VRRTGGLADTVFDYDPETGEGTGFVFEDYDAEALLAALRRALALY-RNPELWRKLQKNAMKQDFSWDKSAKEYLELYRS 474
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
1-473 |
0e+00 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 523.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 1 MNILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLYQQIKSRESEMTLKGtskiRLGDVEkpVSFYELNYEN 80
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKLRDAQVVG----RLDLFT--VLFGHLEGDG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 81 VQYIFVDNDDFFNRPKLYGYEDDAVRFTFFNFSIFEYIKLSNEYPDIIHVNDWQTGMIPFFLDTRYRsqnAGFQKIKSLL 160
Cdd:PRK00654 75 VPVYLIDAPHLFDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGLIPALLKEKYW---RGYPDIKTVF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 161 SIHNLEKQGSYPIETEKIFGNKNFTYiHMDR------VNFLKCGIMRANAINTVSESYRNEILTRFYGFTLDGPLKSRQY 234
Cdd:PRK00654 152 TIHNLAYQGLFPAEILGELGLPAEAF-HLEGlefygqISFLKAGLYYADRVTTVSPTYAREITTPEFGYGLEGLLRARSG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 235 DLYGILNGLDQDLYNPSLSKYIVRNYDENNFiEGKNTNKEFLLRTLSLDSiNDMPLVSFITRFARQKGIDIMMTSLEDYL 314
Cdd:PRK00654 231 KLSGILNGIDYDIWNPETDPLLAANYSADDL-EGKAENKRALQERFGLPD-DDAPLFAMVSRLTEQKGLDLVLEALPELL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 315 KQGkINFIALGSGDALYESFFTQMQTKYPTHVFYQSGFDIELSQKVYAASDLFMLPSLFEPCGLNHMIAMKYGALPIVRE 394
Cdd:PRK00654 309 EQG-GQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPIVRR 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088626635 395 TGGLKDTVTPYNKFTGVGVGFAFKNYDATEFKEAIDQALDIYHHDKEaWNNLIHQAMHVNHSLSKMAKQYEDLYQKILN 473
Cdd:PRK00654 388 TGGLADTVIDYNPEDGEATGFVFDDFNAEDLLRALRRALELYRQPPL-WRALQRQAMAQDFSWDKSAEEYLELYRRLLG 465
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
1-471 |
1.52e-168 |
|
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: 482.92 E-value: 1.52e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 1 MNILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLYQQIKSRESEMTLKGTSK-IRLGDVEKPVSFYELNYE 79
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVVELVdLSVGPRTLYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 80 NVQYIFVDNDDFFNRP-KLYG--YEDDAVRFTFFNFSIFEYIKLSNEYPDIIHVNDWQTGMIPFFLDTRYRsqnagFQKI 156
Cdd:TIGR02095 81 GVPVYFIDNPSLFDRPgGIYGddYPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVYR-----PNPI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 157 KSLLSIHNLEKQGSYPIETEKIFGNKNFtYIHM------DRVNFLKCGIMRANAINTVSESYRNEILTRFYGFTLDGPLK 230
Cdd:TIGR02095 156 KTVFTIHNLAYQGVFPADDFSELGLPPE-YFHMeglefyGRVNFLKGGIVYADRVTTVSPTYAREILTPEFGYGLDGVLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 231 SRQYDLYGILNGLDQDLYNPSLSKYIVRNYDENNFiEGKNTNKEFLLRTLSLDSINDMPLVSFITRFARQKGIDIMMTSL 310
Cdd:TIGR02095 235 ARSGKLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 311 EDYLKQGkINFIALGSGDALYESFFTQMQTKYPTHVFYQSGFDIELSQKVYAASDLFMLPSLFEPCGLNHMIAMKYGALP 390
Cdd:TIGR02095 314 PELLELG-GQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTVP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 391 IVRETGGLKDTVTPYNKFTGVGVGFAFKNYDATEFKEAIDQALDIYHHDKEAWNNLIHQAMHVNHSLSKMAKQYEDLYQK 470
Cdd:TIGR02095 393 IVRRTGGLADTVVDGDPEAESGTGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSAKQYVELYRS 472
|
.
gi 1088626635 471 I 471
Cdd:TIGR02095 473 L 473
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
3-474 |
3.26e-89 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 280.47 E-value: 3.26e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 3 ILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLYQQIKSRESEMTlkgtSKIRLGDVEKP---------VSF 73
Cdd:PRK14098 8 VLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYGTINDRKFRLH----DVLRLSDIEVPlkektdllhVKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 74 YELNYENVQYIFVDNDDFFNRPKLYG-------YEDDAVRFTFFNFSIFEYIKLSNEYPDIIHVNDWQTGMIPFFLDTRY 146
Cdd:PRK14098 84 TALPSSKIQTYFLYNEKYFKRNGLFTdmslggdLKGSAEKVIFFNVGVLETLQRLGWKPDIIHCHDWYAGLVPLLLKTVY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 147 RSqNAGFQKIKSLLSIHNLEKQGSYPIET-EKIFGNKNFTYIHM--DRVNFLKCGIMRANAINTVSESYRNEILT-RFYG 222
Cdd:PRK14098 164 AD-HEFFKDIKTVLTIHNVYRQGVLPFKVfQKLLPEEVCSGLHRegDEVNMLYTGVEHADLLTTTSPRYAEEIAGdGEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 223 FTLDGPLKSRQYDLYGILNGLDQDLYNPSLSKYIVRNYDENNfIEGKNTNKEFLLRTLSLDSINDMPLVSFITRFARQKG 302
Cdd:PRK14098 243 FGLDKVLEERKMRLHGILNGIDTRQWNPSTDKLIKKRYSIER-LDGKLENKKALLEEVGLPFDEETPLVGVIINFDDFQG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 303 IDIMMTSLEDYLKQgKINFIALGSGDALYESFFTQMQTKYPTHVFYQSGFDIELSQKVYAASDLFMLPSLFEPCGLNHMI 382
Cdd:PRK14098 322 AELLAESLEKLVEL-DIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFHLAIAGLDMLLMPGKIESCGMLQMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 383 AMKYGALPIVRETGGLKDTVTPYNKftGVGVGFAFKNYDATEFKEAIDQALDIYhHDKEAWNNLIHQAMHVNHSLSKMAK 462
Cdd:PRK14098 401 AMSYGTIPVAYAGGGIVETIEEVSE--DKGSGFIFHDYTPEALVAKLGEALALY-HDEERWEELVLEAMERDFSWKNSAE 477
|
490
....*....|..
gi 1088626635 463 QYEDLYQKILNP 474
Cdd:PRK14098 478 EYAQLYRELLGP 489
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
3-230 |
3.45e-83 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 256.49 E-value: 3.45e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 3 ILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLYQQIKSRESEMTLKGTSKIRLGDVEKP--VSFYELNYEN 80
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEERNQLEDVIRLSVAAGVPVRPltVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 81 VQYIFVDNDDFFNRPKLYG-----YEDDAVRFTFFNFSIFEYIKLSNEYPDIIHVNDWQTGMIPFFLDTRYRsqNAGFQK 155
Cdd:pfam08323 81 VDVYFLDNPDYFDRPGLYGddgrdYEDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYA--DDPFKN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 156 IKSLLSIHNLEKQGSYPIETEKIFG--NKNFT---YIHMDRVNFLKCGIMRANAINTVSESYRNEILTRFYGFTLDGPLK 230
Cdd:pfam08323 159 IKTVFTIHNLAYQGRFPADLLDLLGlpPEDFNldgLEFYGQINFLKAGIVYADAVTTVSPTYAEEIQTPEFGGGLDGLLR 238
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1-470 |
3.16e-82 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 273.70 E-value: 3.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 1 MNILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLY-----QQIKS-RESEMTLKG-------TSKIRLGDV 67
Cdd:PLN02939 482 LHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYdcmqyDQIRNlKVLDVVVESyfdgnlfKNKIWTGTV 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 68 EK-PVSFYELNYENvqyifvdndDFFNRPKLYGYEDDAVRFTFFNFSIFEYIKLSNEYPDIIHVNDWQTGMI-PFFLDTr 145
Cdd:PLN02939 562 EGlPVYFIEPQHPS---------KFFWRAQYYGEHDDFKRFSYFSRAALELLYQSGKKPDIIHCHDWQTAFVaPLYWDL- 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 146 yrSQNAGFQKIKSLLSIHNLEKQGSYP--------IETEKIFGNKNFTYIHMDRVNFLKCGIMRANAINTVSESYRNEIL 217
Cdd:PLN02939 632 --YAPKGFNSARICFTCHNFEYQGTAPasdlascgLDVHQLDRPDRMQDNAHGRINVVKGAIVYSNIVTTVSPTYAQEVR 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 218 TRfYGFTLDGPLKSRQYDLYGILNGLDQDLYNPSLSKYIVRNYDENNfIEGKNTNKEFLLRTLSLDSIN-DMPLVSFITR 296
Cdd:PLN02939 710 SE-GGRGLQDTLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNAND-LQGKAANKAALRKQLGLSSADaSQPLVGCITR 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 297 FARQKGIDIMMTSLEDYLKQGKiNFIALGSGDAL-----YESFFTQMQTKypTHVFYQSGFDIELSQKVYAASDLFMLPS 371
Cdd:PLN02939 788 LVPQKGVHLIRHAIYKTAELGG-QFVLLGSSPVPhiqreFEGIADQFQSN--NNIRLILKYDEALSHSIYAASDMFIIPS 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 372 LFEPCGLNHMIAMKYGALPIVRETGGLKDTVTPYNKFT---GVGVGFAFKNYDATEFKEAIDQALDIYHHDKEAWNNLIH 448
Cdd:PLN02939 865 MFEPCGLTQMIAMRYGSVPIVRKTGGLNDSVFDFDDETipvELRNGFTFLTPDEQGLNSALERAFNYYKRKPEVWKQLVQ 944
|
490 500
....*....|....*....|..
gi 1088626635 449 QAMHVNHSLSKMAKQYEDLYQK 470
Cdd:PLN02939 945 KDMNIDFSWDSSASQYEELYQR 966
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
1-472 |
8.03e-77 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 248.48 E-value: 8.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 1 MNILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLYQQIksresemtLKGtskirLGDVEKPVSFYELNYEN 80
Cdd:PRK14099 4 LRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYPAV--------LAG-----IEDAEQVHSFPDLFGGP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 81 VQYIFVDND--DFF--NRPKLYG-------------YEDDAVRFTFFNfSIFEYIK---LSNEYPDIIHVNDWQTGMIPF 140
Cdd:PRK14099 71 ARLLAARAGglDLFvlDAPHLYDrpgnpyvgpdgkdWPDNAQRFAALA-RAAAAIGqglVPGFVPDIVHAHDWQAGLAPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 141 FLdtRYrsqnAGFQKIKSLLSIHNLEKQGSYPIE-------TEKIFGNKNFTYIHMdrVNFLKCGIMRANAINTVSESYR 213
Cdd:PRK14099 150 YL--HY----SGRPAPGTVFTIHNLAFQGQFPREllgalglPPSAFSLDGVEYYGG--IGYLKAGLQLADRITTVSPTYA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 214 NEILTRFYGFTLDGPLKSRQYDLYGILNGLDQDLYNPSLSKYIVRNYDENNfIEGKNTNKEFLLRTLSLDSINDMPLVSF 293
Cdd:PRK14099 222 LEIQGPEAGMGLDGLLRQRADRLSGILNGIDTAVWNPATDELIAATYDVET-LAARAANKAALQARFGLDPDPDALLLGV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 294 ITRFARQKGIDIMMTSLEDYLKQGkINFIALGSGDALYESFFTQMQTKYPTHVFYQSGFDIELSQKVYAASDLFMLPSLF 373
Cdd:PRK14099 301 ISRLSWQKGLDLLLEALPTLLGEG-AQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQAGADALLVPSRF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 374 EPCGLNHMIAMKYGALPIVRETGGLKDTVTPYNKF---TGVGVGFAFKNYDAtefkEAIDQALD---IYHHDKEAWNNLI 447
Cdd:PRK14099 380 EPCGLTQLCALRYGAVPVVARVGGLADTVVDANEMaiaTGVATGVQFSPVTA----DALAAALRktaALFADPVAWRRLQ 455
|
490 500
....*....|....*....|....*
gi 1088626635 448 HQAMHVNHSLSKMAKQYEDLYQKIL 472
Cdd:PRK14099 456 RNGMTTDVSWRNPAQHYAALYRSLV 480
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1-468 |
1.06e-65 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 228.60 E-value: 1.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 1 MNILFCSGEVYPFSKTGGLADVAASLPKALKGLGHDVKVITPLY--------QQIKSRESeMTLKGTS-KIRLGDVEKpV 71
Cdd:PLN02316 588 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYdclnlshvKDLHYQRS-YSWGGTEiKVWFGKVEG-L 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 72 SFYELNYENvqyifvdndDFFNRPKLYGYEDDAVRFTFFNFSIFEYIKLSNEYPDIIHVNDWQTGMIPFFLDTRYRsqNA 151
Cdd:PLN02316 666 SVYFLEPQN---------GMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYA--HY 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 152 GFQKIKSLLSIHNLEkqgsypietekiFGnknftyihmdrVNFLKCGIMRANAINTVSESYRNEIltrfygfTLDGPLKS 231
Cdd:PLN02316 735 GLSKARVVFTIHNLE------------FG-----------ANHIGKAMAYADKATTVSPTYSREV-------SGNSAIAP 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 232 RQYDLYGILNGLDQDLYNPSLSKYIVRNYDENNFIEGKNTNKEFLLRTLSLDSInDMPLVSFITRFARQKGIDIMMTSLE 311
Cdd:PLN02316 785 HLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLKQA-DLPLVGIITRLTHQKGIHLIKHAIW 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 312 DYLKQGKiNFIALGSG-DALYESFFT----QMQTKYPTHVFYQSGFDIELSQKVYAASDLFMLPSLFEPCGLNHMIAMKY 386
Cdd:PLN02316 864 RTLERNG-QVVLLGSApDPRIQNDFVnlanQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRY 942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 387 GALPIVRETGGLKDTVTPYN----KFTGVGV---GFAFKNYDATEFKEAIDQALDIYHHDKEAWNNLIHQAMHVNHSLSK 459
Cdd:PLN02316 943 GSIPVVRKTGGLFDTVFDVDhdkeRAQAQGLepnGFSFDGADAAGVDYALNRAISAWYDGRDWFNSLCKRVMEQDWSWNR 1022
|
....*....
gi 1088626635 460 MAKQYEDLY 468
Cdd:PLN02316 1023 PALDYMELY 1031
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-469 |
4.43e-18 |
|
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: 85.67 E-value: 4.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 2 NILFCSGEVYPFSktGGLADVAASLPKALKGLGHDVKVITPlyqqiksresemtlkgtskirlGDVEKPVSFYELNYENV 81
Cdd:cd03801 1 KILLLSPELPPPV--GGAERHVRELARALAARGHDVTVLTP----------------------ADPGEPPEELEDGVIVP 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 82 QYIFVDNDDFFNRpklygyeddavrftffnfSIFEY-IKLSNEYPDIIHVNDWQTGMIPFFLdtryrsqnAGFQKIKSLL 160
Cdd:cd03801 57 LLPSLAALLRARR------------------LLRELrPLLRLRKFDVVHAHGLLAALLAALL--------ALLLGAPLVV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 161 SIHNLEKQGSYPIETekifgnknftyIHMDRVNFLKCGIMRANAINTVSESYRNEILTRFygftldGPLKSRqydLYGIL 240
Cdd:cd03801 111 TLHGAEPGRLLLLLA-----------AERRLLARAEALLRRADAVIAVSEALRDELRALG------GIPPEK---IVVIP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 241 NGLDQDLYNPSLSKyivrnydENNFIEGKntnkefllrtlsldsindmPLVSFITRFARQKGIDIM---MTSLEDYLKQG 317
Cdd:cd03801 171 NGVDLERFSPPLRR-------KLGIPPDR-------------------PVLLFVGRLSPRKGVDLLleaLAKLLRRGPDV 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 318 KINFIalGSGDALYESFFtQMQTKYPTHVFYQSGFDIELSQKVYAASDLFMLPSLFEPCGLNHMIAMKYGALPIVRETGG 397
Cdd:cd03801 225 RLVIV--GGDGPLRAELE-ELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGG 301
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1088626635 398 LKDTVTPynkftgVGVGFAFKNYDATEFKEAIDQALDiyhhDKE-----AWNNLIHQAMHvnHSLSKMAKQYEDLYQ 469
Cdd:cd03801 302 LPEVVED------GEGGLVVPPDDVEALADALLRLLA----DPElrarlGRAARERVAER--FSWERVAERLLDLYR 366
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
361-473 |
1.27e-14 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 70.02 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 361 YAASDLFMLPSLFEPCGLNHMIAMKYGALPIVRETGGLKDTVTPYnkftgvGVGFAFKNYDATEFKEAIDQALDiyhhDK 440
Cdd:COG0438 18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDG------ETGLLVPPGDPEALAEAILRLLE----DP 87
|
90 100 110
....*....|....*....|....*....|....*.
gi 1088626635 441 EAWNNLIHQA---MHVNHSLSKMAKQYEDLYQKILN 473
Cdd:COG0438 88 ELRRRLGEAArerAEERFSWEAIAERLLALYEELLA 123
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
289-450 |
1.49e-13 |
|
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: 68.07 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 289 PLVSFITRFARQKGIDIMMTSLEDYLKQG-KINFIALGSGDALYESFFTQMQTKYPTHVF---YQSGFDIElsqKVYAAS 364
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKEKNpNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIflgFVSDEDLP---ELLKIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 365 DLFMLPSLFEPCGLNHMIAMKYGALPIVRETGGLKDTVTPYNKftgvgvGFAFKNYDATEFKEAIDQALdiyhHDKEAWN 444
Cdd:pfam00534 80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGET------GFLVKPNNAEALAEAIDKLL----EDEELRE 149
|
....*.
gi 1088626635 445 NLIHQA 450
Cdd:pfam00534 150 RLGENA 155
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
92-434 |
5.96e-09 |
|
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: 57.36 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 92 FNRPKLYGYEDDAVRFTFFN-FSIFE-----YIKLSNEYPDIIHVNDWQTGMIPFFLdtryrsqnAGFQKIKSLLSIHNL 165
Cdd:cd03819 38 GPLLPRLRQIGIGLPGLKVPlLRALLgnvrlARLIRRERIDLIHAHSRAPAWLGWLA--------SRLTGVPLVTTVHGS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 166 EkqgsypietekifgnkNFTYIHMDRVNFLKCGIMRANAintVSESYRnEILTRFYGFtldGPLKSRQydlygILNGLDQ 245
Cdd:cd03819 110 Y----------------LATYHPKDFALAVRARGDRVIA---VSELVR-DHLIEALGV---DPERIRV-----IPNGVDT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 246 DLYNPslskyivrnydennfiegknTNKEFLLRTLSLDSinDMPLVSFITRFARQKGIDIMMTSLEDyLKQGKiNFIALG 325
Cdd:cd03819 162 DRFPP--------------------EAEAEERAQLGLPE--GKPVVGYVGRLSPEKGWLLLVDAAAE-LKDEP-DFRLLV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 326 SGDALYESFFTQMQTKYP-THVFYQSGFDiELSQKVYAASDLFMLPSLFEPCGLNHMIAMKYGALPIVRETGGLKDTVTP 404
Cdd:cd03819 218 AGDGPERDEIRRLVERLGlRDRVTFTGFR-EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVH 296
|
330 340 350
....*....|....*....|....*....|
gi 1088626635 405 YNKftgvgvGFAFKNYDATEFKEAIDQALD 434
Cdd:cd03819 297 GRT------GLLVPPGDAEALADAIRAAKL 320
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
289-434 |
6.43e-08 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 51.36 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 289 PLVSFITRFA-RQKGIDIMMTSLEDYLKQ-GKINFIALGSGDALYesfFTQMQTKYPTHVFYQsGFDIELsQKVYAASDL 366
Cdd:pfam13692 2 PVILFVGRLHpNVKGVDYLLEAVPLLRKRdNDVRLVIVGDGPEEE---LEELAAGLEDRVIFT-GFVEDL-AELLAAADV 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088626635 367 FMLPSLFEPCGLNHMIAMKYGaLPIV-RETGGLKDTVTPYNkftgvgvGFAFKNYDATEFKEAIDQALD 434
Cdd:pfam13692 77 FVLPSLYEGFGLKLLEAMAAG-LPVVaTDVGGIPELVDGEN-------GLLVPPGDPEALAEAILRLLE 137
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
284-429 |
1.07e-07 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340842 [Multi-domain] Cd Length: 365 Bit Score: 53.84 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 284 SINDMPLVSFITRFARQKGIDIMMTSLEDYLKQGKINFIALGSGDALYEsfftqMQTKYPTHVF--YQSGfdIELSQkVY 361
Cdd:cd03814 194 GPPGRPLLLYVGRLAPEKNLEALLDADLPLAASPPVRLVVVGDGPARAE-----LEARGPDVIFtgFLTG--EELAR-AY 265
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088626635 362 AASDLFMLPSLFEPCGLNHMIAMKYGaLP-IVRETGGLKDTVTPYnkftgvGVGFAFKNYDATEFKEAI 429
Cdd:cd03814 266 ASADVFVFPSRTETFGLVVLEAMASG-LPvVAADAGGPRDIVRPG------GTGALVEPGDAAAFAAAL 327
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
287-434 |
8.15e-07 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 51.25 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 287 DMPLVSFITRFARQKGIDIMMTSLEDyLKQGKINFIalgsGDALYESFFTQMQTKYPTHVFYQSGFDiELSQkVYAASDL 366
Cdd:PLN02871 262 EKPLIVYVGRLGAEKNLDFLKRVMER-LPGARLAFV----GDGPYREELEKMFAGTPTVFTGMLQGD-ELSQ-AYASGDV 334
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088626635 367 FMLPSLFEPCGLNHMIAMKYGaLPIVR-ETGGLKDTVTPYNkfTGVgVGFAFKNYDATEFKEAIDQALD 434
Cdd:PLN02871 335 FVMPSESETLGFVVLEAMASG-VPVVAaRAGGIPDIIPPDQ--EGK-TGFLYTPGDVDDCVEKLETLLA 399
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
254-406 |
1.12e-06 |
|
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: 49.71 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 254 KYIVRNYDENNFIEGKNTNKEFLLRTLSLDSINDMplvsFITRFARQKGIDIMMTSLEDYLKQG-KINFIALGSGDALYE 332
Cdd:cd01635 80 PIVVTVHGPDSLESTRSELLALARLLVSLPLADKV----SVGRLVPEKGIDLLLEALALLKARLpDLVLVLVGGGGEREE 155
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1088626635 333 SFFTQMQTKYPTHVFYQSGFDI-ELSQKVYAASDLFMLPSLFEPCGLNHMIAMKYGALPIVRETGGLKDTVTPYN 406
Cdd:cd01635 156 EEALAAALGLLERVVIIGGLVDdEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGE 230
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
358-471 |
5.89e-06 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340859 [Multi-domain] Cd Length: 370 Bit Score: 48.50 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 358 QKVYAASDLFMLPSLFEPCGLNHMIAMKYGALPIVRETGGLKDTVTpynkfTGVgVGFAFKNYDATEFKEAIDQALdiyh 437
Cdd:cd04962 264 EELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVK-----HGE-TGFLSDVGDVDAMAKSALSIL---- 333
|
90 100 110
....*....|....*....|....*....|....*..
gi 1088626635 438 HDKEAWNNLIHQA--MHVNH-SLSKMAKQYEDLYQKI 471
Cdd:cd04962 334 EDDELYNRMGRAArkRAAERfDPERIVPQYEAYYRRL 370
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
260-466 |
7.02e-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: 48.01 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 260 YDENNFIEGknTNKEFLLRTLSLDSinDMPLVSFITRFARQKGIDIMMTSL-EDYLKQGKINF-IALG------SGDALY 331
Cdd:cd03800 196 VDLERFFPV--DRAEARRARLLLPP--DKPVVLALGRLDPRKGIDTLVRAFaQLPELRELANLvLVGGpsddplSMDREE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 332 ESFFTQM-----QTKYPTHVfyqsgfdielSQ----KVYAASDLFMLPSLFEPCGLNHMIAMKYGaLPIV-RETGGLKDT 401
Cdd:cd03800 272 LAELAEElglidRVRFPGRV----------SRddlpELYRAADVFVVPSLYEPFGLTAIEAMACG-TPVVaTAVGGLQDI 340
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088626635 402 VTPynkftgvGV-GFAFKNYDATEFKEAIDQALDiyhhDKEAWNNLIHQAM-HVNHSLS--KMAKQYED 466
Cdd:cd03800 341 VRD-------GRtGLLVDPHDPEALAAALRRLLD----DPALWQRLSRAGLeRARAHYTweSVADQLLT 398
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
16-471 |
8.33e-06 |
|
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.
Pssm-ID: 340844 [Multi-domain] Cd Length: 372 Bit Score: 47.66 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 16 TGGLADVAASLPKALKGLGHDVKVITPLYQQIKSRESEmtlkgtSKIRLgdvekPVSFYELNYenvqyifvdnddffnrp 95
Cdd:cd03817 13 VNGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEEV------VRYRS-----FSIPIRKYH----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 96 klygyeddavRFTFFNFSIFEYIKLSNEY-PDIIHVndwQTgmiPFFLdtryrsqnaGF-----QKIKSLLSIHnlekqg 169
Cdd:cd03817 65 ----------RQHIPFPFKKAVIDRIKELgPDIIHT---HT---PFSL---------GKlglriARKLKIPIVH------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 170 SYPIETEKIFGN--KNFT----YIHMDRVNFLKcgimRANAINTVSESYRNEIltRFYGFTldGPLKSrqydlygILNGL 243
Cdd:cd03817 114 TYHTMYEDYLHYipKGKLlvkaVVRKLVRRFYN----HTDAVIAPSEKIKDTL--REYGVK--GPIEV-------IPNGI 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 244 DQDLYNPSLSKYIVRnydENNFIEGKntnkefllrtlsldsindmPLVSFITRFARQKGIDIMMTSLEDYLKQGKINFIA 323
Cdd:cd03817 179 DLDKFEKPLNTEERR---KLGLPPDE-------------------PILLYVGRLAKEKNIDFLLRAFAELKKEPNIKLVI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 324 LGSGDAL--YESFFTQMQ-TKYPTHVfyqsGF--DIELSqKVYAASDLFMLPSLFEPCGLNHMIAMKYGaLPIV-RETGG 397
Cdd:cd03817 237 VGDGPEReeLKELARELGlADKVIFT----GFvpREELP-EYYKAADLFVFASTTETQGLVYLEAMAAG-LPVVaAKDPA 310
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1088626635 398 LKDTVtpynkftGVGV-GFAFKNYDATeFKEAIDQALDiyhhDKEAWNNLIHQAmhVNHSLSK-MAKQYEDLYQKI 471
Cdd:cd03817 311 ASELV-------EDGEnGFLFEPNDET-LAEKLLHLRE----NLELLRKLSKNA--EISAREFaFAKSVEKLYEEV 372
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
353-471 |
6.65e-05 |
|
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: 45.02 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 353 DIELSQkVYAASDLFMLPSLFEPCGLNHMIAMKYGALPIVRETGGLKDTVTPynkftGVGvGFAFKNYDATEFKEAIDQA 432
Cdd:cd03825 254 DEQLVD-IYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQH-----GVT-GYLVPPGDVQALAEAIEWL 326
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1088626635 433 LDiyhHDKEAWNNLIHQAMHV-NH-SLSKMAKQYEDLYQKI 471
Cdd:cd03825 327 LA---NPKERESLGERARALAeNHfDQRVQAQRYLELYKDL 364
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
287-466 |
4.93e-04 |
|
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: 42.36 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 287 DMPLVSFITRFARQKGIDIMMTSLEDYLKQGK-INFIALGSGDALYESFFTQMQTKYPTHVFYQSGFdieLSQKV----Y 361
Cdd:cd03821 203 DRRIILFLGRIHPKKGLDLLIRAARKLAEQGRdWHLVIAGPDDGAYPAFLQLQSSLGLGDRVTFTGP---LYGEAkwalY 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 362 AASDLFMLPSLFEPCGLNHMIAMKYGaLPIVRETG-GLKDTVTPynkftGVGVGFAFknyDATEFKEAIDQALDIYHHDK 440
Cdd:cd03821 280 ASADLFVLPSYSENFGNVVAEALACG-LPVVITDKcGLSELVEA-----GCGVVVDP---NVSSLAEALAEALRDPADRK 350
|
170 180
....*....|....*....|....*...
gi 1088626635 441 EAwNNLIHQAMHV--NHSLSKMAKQYED 466
Cdd:cd03821 351 RL-GEMARRARQVeeNFSWEAVAGQLGE 377
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
360-468 |
7.85e-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: 41.53 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088626635 360 VYAASDLFMLPSLFEPCGLNHMIAMKYGaLPIV-RETGGLKDTVTPynkftgvGVGFAFKNYDATEFKEAIDQALdiyhH 438
Cdd:cd03807 261 LLPAMDIFVLSSRTEGFPNALLEAMACG-LPVVaTDVGGAAELVDD-------GTGFLVPAGDPQALADAIRALL----E 328
|
90 100 110
....*....|....*....|....*....|...
gi 1088626635 439 DKEAWN-NLIHQAMHV--NHSLSKMAKQYEDLY 468
Cdd:cd03807 329 DPEKRArLGRAARERIanEFSIDAMVRRYETLY 361
|
|
| |
