|
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 ... |
143-643 |
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: 623.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 143 NLVFVTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYLNGTAADKNYARAKDLGIRVtvncFGGSQEVSFYHEY 222
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEVKV----GGRGEEVGVFELP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 223 RDGVDWVFVDHKSYHRPGNPYGDSKGAFGDNQFRFTLLCHAACEAPLVLplggftYGEKSLFLVNDWHAGLVPILLAAKY 302
Cdd:cd03791 77 VDGVDYYFLDNPEFFDRPGLPGPPGYDYPDNAERFAFFSRAALELLRRL------GFQPDIIHANDWHTALVPAYLKTRY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 303 RPYGvYKDARSILIIHNLAHQGVEPAATYTNLGLPSEWYgavgwvfptwaRTHALDTGEAVNVLKGAIVTSDRIITVSQG 382
Cdd:cd03791 151 RGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPPELF-----------HIDGLEFYGQINFLKAGIVYADRVTTVSPT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 383 YAWEITTVEGGYGLQDLLSSRKSVINGITNGINVDEWNPSTDEHIPFHYSADDVSEKIKCKMALQKELGLPIRPECPMIG 462
Cdd:cd03791 219 YAKEILTPEYGEGLDGVLRARAGKLSGILNGIDYDEWNPATDKLIPANYSANDLEGKAENKAALQKELGLPVDPDAPLFG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 463 FIGRLDYQKGIDLIQTAGPDLMVDDIQFVMLGSGDPKYESWMRSMEETYRDKFRGWVGFNVPISHRITAGCDILLMPSRF 542
Cdd:cd03791 299 FVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 543 EPCGLNQLYAMRYGTIPVVHGTGGLRDTVENFNPYaeggAGTGTGWVFTPLSKDSMVSALRLAAATYREyKQSWEGLMRR 622
Cdd:cd03791 379 EPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYDPE----TGEGTGFVFEDYDAEALLAALRRALALYRN-PELWRKLQKN 453
|
490 500
....*....|....*....|.
gi 15237934 623 GMTRNYSWENAAVQYEQVFQW 643
Cdd:cd03791 454 AMKQDFSWDKSAKEYLELYRS 474
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
143-644 |
0e+00 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 571.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 143 NLVFVTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYlnGTAADKNYARAKDLGIRVTVNcfGGSQEVSFYHEY 222
Cdd:COG0297 2 KILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGY--PSIDDKLKDLEVVASLEVPLG--GRTYYARVLEGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 223 RDGVDWVFVDHKSY-HRPGnPYGDSKGAFGDNQFRFTLLCHAACEAplvLPLGGFTYGeksLFLVNDWHAGLVPILLAAK 301
Cdd:COG0297 78 DDGVPVYFIDNPELfDRPG-PYGDPDRDYPDNAERFAFFSRAALEL---LKGLDWKPD---IIHCHDWQTGLIPALLKTR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 302 YRPYGvYKDARSILIIHNLAHQGVEPAATYTNLGLPSEWYgavgwvfptwaRTHALDTGEAVNVLKGAIVTSDRIITVSQ 381
Cdd:COG0297 151 YADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPELF-----------TPDGLEFYGQINFLKAGIVYADRVTTVSP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 382 GYAWEITTVEGGYGLQDLLSSRKSVINGITNGINVDEWNPSTDEHIPFHYSADDVSEKIKCKMALQKELGLPIRPECPMI 461
Cdd:COG0297 219 TYAREIQTPEFGEGLDGLLRARSGKLSGILNGIDYDVWNPATDPYLPANYSADDLEGKAANKAALQEELGLPVDPDAPLI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 462 GFIGRLDYQKGIDLIQTAGPDLMVDDIQFVMLGSGDPKYESWMRSMEETYRDKFRGWVGFNVPISHRITAGCDILLMPSR 541
Cdd:COG0297 299 GMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 542 FEPCGLNQLYAMRYGTIPVVHGTGGLRDTVENFNPYAEGgagtgtgwVFTPLSKDSMVSALRLAAATYReYKQSWEGLMR 621
Cdd:COG0297 379 FEPCGLNQMYALRYGTVPIVRRTGGLADTVIDYNEATGEgt----gfVFDEYTAEALLAAIRRALALYR-DPEAWRKLQR 453
|
490 500
....*....|....*....|...
gi 15237934 622 RGMTRNYSWENAAVQYEQVFQWV 644
Cdd:COG0297 454 NAMKQDFSWEKSAKEYLELYREL 476
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
143-642 |
0e+00 |
|
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: 540.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 143 NLVFVTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYlnGTAADKNYaRAKDLGIRVTVNCFGGSQEVSFYHEY 222
Cdd:TIGR02095 2 RVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAY--GCIEDEVD-DQVKVVELVDLSVGPRTLYVKVFEGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 223 RDGVDWVFVDHKSY-HRPGNPYGDskgAFGDNQFRFTLLCHAACEAPLVLplgGFTYGeksLFLVNDWHAGLVPILLAAK 301
Cdd:TIGR02095 79 VEGVPVYFIDNPSLfDRPGGIYGD---DYPDNAERFAFFSRAAAELLSGL---GWQPD---VVHAHDWHTALVPALLKAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 302 YRPYgvykDARSILIIHNLAHQGVEPAATYTNLGLPSEWYGAvgwvfptwartHALDTGEAVNVLKGAIVTSDRIITVSQ 381
Cdd:TIGR02095 150 YRPN----PIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHM-----------EGLEFYGRVNFLKGGIVYADRVTTVSP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 382 GYAWEITTVEGGYGLQDLLSSRKSVINGITNGINVDEWNPSTDEHIPFHYSADDVSEKIKCKMALQKELGLPIRPECPMI 461
Cdd:TIGR02095 215 TYAREILTPEFGYGLDGVLKARSGKLRGILNGIDTEVWNPATDPYLKANYSADDLAGKAENKEALQEELGLPVDDDVPLF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 462 GFIGRLDYQKGIDLIQTAGPDLMVDDIQFVMLGSGDPKYESWMRSMEETYRDKFRGWVGFNVPISHRITAGCDILLMPSR 541
Cdd:TIGR02095 295 GVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 542 FEPCGLNQLYAMRYGTIPVVHGTGGLRDTVENFNPyaegGAGTGTGWVFTPLSKDSMVSALRLAAATYREYKQSWEGLMR 621
Cdd:TIGR02095 375 FEPCGLTQLYAMRYGTVPIVRRTGGLADTVVDGDP----EAESGTGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQK 450
|
490 500
....*....|....*....|.
gi 15237934 622 RGMTRNYSWENAAVQYEQVFQ 642
Cdd:TIGR02095 451 NAMSQDFSWDKSAKQYVELYR 471
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
143-642 |
9.92e-173 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 500.42 E-value: 9.92e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 143 NLVFVTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYlngtaaDKNYARAKDLGIRVTVNCFggsqEVSFYHEY 222
Cdd:PRK00654 2 KILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGY------PAIREKLRDAQVVGRLDLF----TVLFGHLE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 223 RDGVDWVFVDHKS-YHRPGNpYGdskgaFGDNQFRFTLLCHAACEaplvlplggftYGEKSLFL-----VNDWHAGLVPI 296
Cdd:PRK00654 72 GDGVPVYLIDAPHlFDRPSG-YG-----YPDNGERFAFFSWAAAE-----------FAEGLDPRpdivhAHDWHTGLIPA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 297 LLAAKYRPYgvYKDARSILIIHNLAHQGVEPAATYTNLGLPS--------EWYGAVGWvfptwarthaldtgeavnvLKG 368
Cdd:PRK00654 135 LLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAeafhleglEFYGQISF-------------------LKA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 369 AIVTSDRIITVSQGYAWEITTVEGGYGLQDLLSSRKSVINGITNGINVDEWNPSTDEHIPFHYSADDVSEKIKCKMALQK 448
Cdd:PRK00654 194 GLYYADRVTTVSPTYAREITTPEFGYGLEGLLRARSGKLSGILNGIDYDIWNPETDPLLAANYSADDLEGKAENKRALQE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 449 ELGLPiRPECPMIGFIGRLDYQKGIDLIQTAGPDLMVDDIQFVMLGSGDPKYESWMRSMEETYRDKFRGWVGFNVPISHR 528
Cdd:PRK00654 274 RFGLP-DDDAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 529 ITAGCDILLMPSRFEPCGLNQLYAMRYGTIPVVHGTGGLRDTVENFNPYaeggAGTGTGWVFTPLSKDSMVSALRLAAAT 608
Cdd:PRK00654 353 IYAGADMFLMPSRFEPCGLTQLYALRYGTLPIVRRTGGLADTVIDYNPE----DGEATGFVFDDFNAEDLLRALRRALEL 428
|
490 500 510
....*....|....*....|....*....|....
gi 15237934 609 YREYKQsWEGLMRRGMTRNYSWENAAVQYEQVFQ 642
Cdd:PRK00654 429 YRQPPL-WRALQRQAMAQDFSWDKSAEEYLELYR 461
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
145-401 |
1.30e-77 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 247.24 E-value: 1.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 145 VFVTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYLNGTAADKNYARAKDLGIRVTVNcfGGSQEVSFYHEYRD 224
Cdd:pfam08323 2 LFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEERNQLEDVIRLSVAAGVP--VRPLTVGVARLELD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 225 GVDWVFVDHKSYHRPGNPYGDSKGAFGDNQFRFTLLCHAACEAPLVLplgGFTYgekSLFLVNDWHAGLVPILLAAKYRP 304
Cdd:pfam08323 80 GVDVYFLDNPDYFDRPGLYGDDGRDYEDNAERFAFFSRAALELAKKL---GWIP---DIIHCHDWHTALVPAYLKEAYAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 305 YGVyKDARSILIIHNLAHQGVEPAATYTNLGLPSEWYgavgwvfptwaRTHALDTGEAVNVLKGAIVTSDRIITVSQGYA 384
Cdd:pfam08323 154 DPF-KNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDF-----------NLDGLEFYGQINFLKAGIVYADAVTTVSPTYA 221
|
250
....*....|....*..
gi 15237934 385 WEITTVEGGYGLQDLLS 401
Cdd:pfam08323 222 EEIQTPEFGGGLDGLLR 238
|
|
| |
|
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 ... |
143-643 |
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: 623.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 143 NLVFVTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYLNGTAADKNYARAKDLGIRVtvncFGGSQEVSFYHEY 222
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEVKV----GGRGEEVGVFELP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 223 RDGVDWVFVDHKSYHRPGNPYGDSKGAFGDNQFRFTLLCHAACEAPLVLplggftYGEKSLFLVNDWHAGLVPILLAAKY 302
Cdd:cd03791 77 VDGVDYYFLDNPEFFDRPGLPGPPGYDYPDNAERFAFFSRAALELLRRL------GFQPDIIHANDWHTALVPAYLKTRY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 303 RPYGvYKDARSILIIHNLAHQGVEPAATYTNLGLPSEWYgavgwvfptwaRTHALDTGEAVNVLKGAIVTSDRIITVSQG 382
Cdd:cd03791 151 RGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPPELF-----------HIDGLEFYGQINFLKAGIVYADRVTTVSPT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 383 YAWEITTVEGGYGLQDLLSSRKSVINGITNGINVDEWNPSTDEHIPFHYSADDVSEKIKCKMALQKELGLPIRPECPMIG 462
Cdd:cd03791 219 YAKEILTPEYGEGLDGVLRARAGKLSGILNGIDYDEWNPATDKLIPANYSANDLEGKAENKAALQKELGLPVDPDAPLFG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 463 FIGRLDYQKGIDLIQTAGPDLMVDDIQFVMLGSGDPKYESWMRSMEETYRDKFRGWVGFNVPISHRITAGCDILLMPSRF 542
Cdd:cd03791 299 FVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 543 EPCGLNQLYAMRYGTIPVVHGTGGLRDTVENFNPYaeggAGTGTGWVFTPLSKDSMVSALRLAAATYREyKQSWEGLMRR 622
Cdd:cd03791 379 EPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYDPE----TGEGTGFVFEDYDAEALLAALRRALALYRN-PELWRKLQKN 453
|
490 500
....*....|....*....|.
gi 15237934 623 GMTRNYSWENAAVQYEQVFQW 643
Cdd:cd03791 454 AMKQDFSWDKSAKEYLELYRS 474
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
143-644 |
0e+00 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 571.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 143 NLVFVTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYlnGTAADKNYARAKDLGIRVTVNcfGGSQEVSFYHEY 222
Cdd:COG0297 2 KILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGY--PSIDDKLKDLEVVASLEVPLG--GRTYYARVLEGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 223 RDGVDWVFVDHKSY-HRPGnPYGDSKGAFGDNQFRFTLLCHAACEAplvLPLGGFTYGeksLFLVNDWHAGLVPILLAAK 301
Cdd:COG0297 78 DDGVPVYFIDNPELfDRPG-PYGDPDRDYPDNAERFAFFSRAALEL---LKGLDWKPD---IIHCHDWQTGLIPALLKTR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 302 YRPYGvYKDARSILIIHNLAHQGVEPAATYTNLGLPSEWYgavgwvfptwaRTHALDTGEAVNVLKGAIVTSDRIITVSQ 381
Cdd:COG0297 151 YADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPELF-----------TPDGLEFYGQINFLKAGIVYADRVTTVSP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 382 GYAWEITTVEGGYGLQDLLSSRKSVINGITNGINVDEWNPSTDEHIPFHYSADDVSEKIKCKMALQKELGLPIRPECPMI 461
Cdd:COG0297 219 TYAREIQTPEFGEGLDGLLRARSGKLSGILNGIDYDVWNPATDPYLPANYSADDLEGKAANKAALQEELGLPVDPDAPLI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 462 GFIGRLDYQKGIDLIQTAGPDLMVDDIQFVMLGSGDPKYESWMRSMEETYRDKFRGWVGFNVPISHRITAGCDILLMPSR 541
Cdd:COG0297 299 GMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 542 FEPCGLNQLYAMRYGTIPVVHGTGGLRDTVENFNPYAEGgagtgtgwVFTPLSKDSMVSALRLAAATYReYKQSWEGLMR 621
Cdd:COG0297 379 FEPCGLNQMYALRYGTVPIVRRTGGLADTVIDYNEATGEgt----gfVFDEYTAEALLAAIRRALALYR-DPEAWRKLQR 453
|
490 500
....*....|....*....|...
gi 15237934 622 RGMTRNYSWENAAVQYEQVFQWV 644
Cdd:COG0297 454 NAMKQDFSWEKSAKEYLELYREL 476
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
143-642 |
0e+00 |
|
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: 540.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 143 NLVFVTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYlnGTAADKNYaRAKDLGIRVTVNCFGGSQEVSFYHEY 222
Cdd:TIGR02095 2 RVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAY--GCIEDEVD-DQVKVVELVDLSVGPRTLYVKVFEGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 223 RDGVDWVFVDHKSY-HRPGNPYGDskgAFGDNQFRFTLLCHAACEAPLVLplgGFTYGeksLFLVNDWHAGLVPILLAAK 301
Cdd:TIGR02095 79 VEGVPVYFIDNPSLfDRPGGIYGD---DYPDNAERFAFFSRAAAELLSGL---GWQPD---VVHAHDWHTALVPALLKAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 302 YRPYgvykDARSILIIHNLAHQGVEPAATYTNLGLPSEWYGAvgwvfptwartHALDTGEAVNVLKGAIVTSDRIITVSQ 381
Cdd:TIGR02095 150 YRPN----PIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHM-----------EGLEFYGRVNFLKGGIVYADRVTTVSP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 382 GYAWEITTVEGGYGLQDLLSSRKSVINGITNGINVDEWNPSTDEHIPFHYSADDVSEKIKCKMALQKELGLPIRPECPMI 461
Cdd:TIGR02095 215 TYAREILTPEFGYGLDGVLKARSGKLRGILNGIDTEVWNPATDPYLKANYSADDLAGKAENKEALQEELGLPVDDDVPLF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 462 GFIGRLDYQKGIDLIQTAGPDLMVDDIQFVMLGSGDPKYESWMRSMEETYRDKFRGWVGFNVPISHRITAGCDILLMPSR 541
Cdd:TIGR02095 295 GVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 542 FEPCGLNQLYAMRYGTIPVVHGTGGLRDTVENFNPyaegGAGTGTGWVFTPLSKDSMVSALRLAAATYREYKQSWEGLMR 621
Cdd:TIGR02095 375 FEPCGLTQLYAMRYGTVPIVRRTGGLADTVVDGDP----EAESGTGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQK 450
|
490 500
....*....|....*....|.
gi 15237934 622 RGMTRNYSWENAAVQYEQVFQ 642
Cdd:TIGR02095 451 NAMSQDFSWDKSAKQYVELYR 471
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
143-642 |
9.92e-173 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 500.42 E-value: 9.92e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 143 NLVFVTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYlngtaaDKNYARAKDLGIRVTVNCFggsqEVSFYHEY 222
Cdd:PRK00654 2 KILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGY------PAIREKLRDAQVVGRLDLF----TVLFGHLE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 223 RDGVDWVFVDHKS-YHRPGNpYGdskgaFGDNQFRFTLLCHAACEaplvlplggftYGEKSLFL-----VNDWHAGLVPI 296
Cdd:PRK00654 72 GDGVPVYLIDAPHlFDRPSG-YG-----YPDNGERFAFFSWAAAE-----------FAEGLDPRpdivhAHDWHTGLIPA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 297 LLAAKYRPYgvYKDARSILIIHNLAHQGVEPAATYTNLGLPS--------EWYGAVGWvfptwarthaldtgeavnvLKG 368
Cdd:PRK00654 135 LLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAeafhleglEFYGQISF-------------------LKA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 369 AIVTSDRIITVSQGYAWEITTVEGGYGLQDLLSSRKSVINGITNGINVDEWNPSTDEHIPFHYSADDVSEKIKCKMALQK 448
Cdd:PRK00654 194 GLYYADRVTTVSPTYAREITTPEFGYGLEGLLRARSGKLSGILNGIDYDIWNPETDPLLAANYSADDLEGKAENKRALQE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 449 ELGLPiRPECPMIGFIGRLDYQKGIDLIQTAGPDLMVDDIQFVMLGSGDPKYESWMRSMEETYRDKFRGWVGFNVPISHR 528
Cdd:PRK00654 274 RFGLP-DDDAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 529 ITAGCDILLMPSRFEPCGLNQLYAMRYGTIPVVHGTGGLRDTVENFNPYaeggAGTGTGWVFTPLSKDSMVSALRLAAAT 608
Cdd:PRK00654 353 IYAGADMFLMPSRFEPCGLTQLYALRYGTLPIVRRTGGLADTVIDYNPE----DGEATGFVFDDFNAEDLLRALRRALEL 428
|
490 500 510
....*....|....*....|....*....|....
gi 15237934 609 YREYKQsWEGLMRRGMTRNYSWENAAVQYEQVFQ 642
Cdd:PRK00654 429 YRQPPL-WRALQRQAMAQDFSWDKSAEEYLELYR 461
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
147-642 |
9.02e-107 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 331.68 E-value: 9.02e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 147 VTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYLNGTAADKNYARakdlgIRVTVNCFGGSQEVsfYHEYRDGV 226
Cdd:PRK14099 9 VASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYPAVLAGIEDAEQ-----VHSFPDLFGGPARL--LAARAGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 227 DWVFVDHKS-YHRPGNPYGDSKGA-FGDNQFRFTLLCHAACEAPLVLpLGGFTygeKSLFLVNDWHAGLVPILLAAKYRP 304
Cdd:PRK14099 82 DLFVLDAPHlYDRPGNPYVGPDGKdWPDNAQRFAALARAAAAIGQGL-VPGFV---PDIVHAHDWQAGLAPAYLHYSGRP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 305 YgvykdARSILIIHNLAHQGVEPAATYTNLGLPS--------EWYGAVGWvfptwarthaldtgeavnvLKGAIVTSDRI 376
Cdd:PRK14099 158 A-----PGTVFTIHNLAFQGQFPRELLGALGLPPsafsldgvEYYGGIGY-------------------LKAGLQLADRI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 377 ITVSQGYAWEITTVEGGYGLQDLLSSRKSVINGITNGINVDEWNPSTDEHIPFHYSADDVSEKIKCKMALQKELGLPIRP 456
Cdd:PRK14099 214 TTVSPTYALEIQGPEAGMGLDGLLRQRADRLSGILNGIDTAVWNPATDELIAATYDVETLAARAANKAALQARFGLDPDP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 457 ECPMIGFIGRLDYQKGIDLIQTAGPDLMVDDIQFVMLGSGDPKYESWMRSMEETYRDKFRGWVGFNVPISHRITAGCDIL 536
Cdd:PRK14099 294 DALLLGVISRLSWQKGLDLLLEALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQAGADAL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 537 LMPSRFEPCGLNQLYAMRYGTIPVVHGTGGLRDTVENFNPyAEGGAGTGTGWVFTPLSKDSMVSALRLAAATYREyKQSW 616
Cdd:PRK14099 374 LVPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVDANE-MAIATGVATGVQFSPVTADALAAALRKTAALFAD-PVAW 451
|
490 500
....*....|....*....|....*.
gi 15237934 617 EGLMRRGMTRNYSWENAAVQYEQVFQ 642
Cdd:PRK14099 452 RRLQRNGMTTDVSWRNPAQHYAALYR 477
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
287-642 |
1.69e-79 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 260.82 E-value: 1.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 287 NDWHAGLVPILLAAKYRPYGVYKDARSILIIHNLAHQGVEPAATYTNLgLPSEWYGAVgwvfptwartHAldTGEAVNVL 366
Cdd:PRK14098 148 HDWYAGLVPLLLKTVYADHEFFKDIKTVLTIHNVYRQGVLPFKVFQKL-LPEEVCSGL----------HR--EGDEVNML 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 367 KGAIVTSDRIITVSQGYAWEITT-VEGGYGLQDLLSSRKSVINGITNGINVDEWNPSTDEHIPFHYSADDVSEKIKCKMA 445
Cdd:PRK14098 215 YTGVEHADLLTTTSPRYAEEIAGdGEEAFGLDKVLEERKMRLHGILNGIDTRQWNPSTDKLIKKRYSIERLDGKLENKKA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 446 LQKELGLPIRPECPMIGFIGRLDYQKGIDLIQTAGPDLMVDDIQFVMLGSGDPKYESWMRSMEETYRDKFRGWVGFNVPI 525
Cdd:PRK14098 295 LLEEVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAF 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 526 SHRITAGCDILLMPSRFEPCGLNQLYAMRYGTIPVVHGTGGLRDTVENFNpyaeggAGTGTGWVFTPLSKDSMVSALRLA 605
Cdd:PRK14098 375 FHLAIAGLDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETIEEVS------EDKGSGFIFHDYTPEALVAKLGEA 448
|
330 340 350
....*....|....*....|....*....|....*..
gi 15237934 606 AATYREyKQSWEGLMRRGMTRNYSWENAAVQYEQVFQ 642
Cdd:PRK14098 449 LALYHD-EERWEELVLEAMERDFSWKNSAEEYAQLYR 484
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
145-401 |
1.30e-77 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 247.24 E-value: 1.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 145 VFVTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYLNGTAADKNYARAKDLGIRVTVNcfGGSQEVSFYHEYRD 224
Cdd:pfam08323 2 LFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEERNQLEDVIRLSVAAGVP--VRPLTVGVARLELD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 225 GVDWVFVDHKSYHRPGNPYGDSKGAFGDNQFRFTLLCHAACEAPLVLplgGFTYgekSLFLVNDWHAGLVPILLAAKYRP 304
Cdd:pfam08323 80 GVDVYFLDNPDYFDRPGLYGDDGRDYEDNAERFAFFSRAALELAKKL---GWIP---DIIHCHDWHTALVPAYLKEAYAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 305 YGVyKDARSILIIHNLAHQGVEPAATYTNLGLPSEWYgavgwvfptwaRTHALDTGEAVNVLKGAIVTSDRIITVSQGYA 384
Cdd:pfam08323 154 DPF-KNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDF-----------NLDGLEFYGQINFLKAGIVYADAVTTVSPTYA 221
|
250
....*....|....*..
gi 15237934 385 WEITTVEGGYGLQDLLS 401
Cdd:pfam08323 222 EEIQTPEFGGGLDGLLR 238
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
144-642 |
1.05e-67 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 239.03 E-value: 1.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 144 LVFVTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYlngtaaD-KNYARAKDLGIRVTVncfggsqeVSFYHE- 221
Cdd:PLN02939 484 IVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKY------DcMQYDQIRNLKVLDVV--------VESYFDg 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 222 --YRDGVdWV---------FVD--H--KSYHRpGNPYGDSkgafgDNQFRFTLLCHAACEapLVLPLGGftygEKSLFLV 286
Cdd:PLN02939 550 nlFKNKI-WTgtveglpvyFIEpqHpsKFFWR-AQYYGEH-----DDFKRFSYFSRAALE--LLYQSGK----KPDIIHC 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 287 NDWHAGLVPILLAAKYRPYGvYKDARSILIIHNLAHQGVEPAATYTNLGLPSEWYGAvgwvfPTWARTHALDTgeaVNVL 366
Cdd:PLN02939 617 HDWQTAFVAPLYWDLYAPKG-FNSARICFTCHNFEYQGTAPASDLASCGLDVHQLDR-----PDRMQDNAHGR---INVV 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 367 KGAIVTSDRIITVSQGYAWEITTvEGGYGLQDLLS--SRKSVinGITNGINVDEWNPSTDEHIPFHYSADDVSEKIKCKM 444
Cdd:PLN02939 688 KGAIVYSNIVTTVSPTYAQEVRS-EGGRGLQDTLKfhSKKFV--GILNGIDTDTWNPSTDRFLKVQYNANDLQGKAANKA 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 445 ALQKELGLP-IRPECPMIGFIGRLDYQKGIDLIQTAGPDLMVDDIQFVMLGSGD-PKYESWMRSMEETYR--DKFRGWVG 520
Cdd:PLN02939 765 ALRKQLGLSsADASQPLVGCITRLVPQKGVHLIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGIADQFQsnNNIRLILK 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 521 FNVPISHRITAGCDILLMPSRFEPCGLNQLYAMRYGTIPVVHGTGGLRDTVENFNPyAEGGAGTGTGWVFTPLSKDSMVS 600
Cdd:PLN02939 845 YDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSVFDFDD-ETIPVELRNGFTFLTPDEQGLNS 923
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15237934 601 ALRLAAATYREYKQSWEGLMRRGMTRNYSWENAAVQYEQVFQ 642
Cdd:PLN02939 924 ALERAFNYYKRKPEVWKQLVQKDMNIDFSWDSSASQYEELYQ 965
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
144-641 |
1.01e-56 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 207.80 E-value: 1.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 144 LVFVTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYlngtaaD-KNYARAKDLGIRvtvNCFG-GSQEVSFYHE 221
Cdd:PLN02316 590 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKY------DcLNLSHVKDLHYQ---RSYSwGGTEIKVWFG 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 222 YRDGVDWVFVD-HKSYHRPGNPYGDSkgafgDNQFRFTLLCHAACEaplVLPLGGFTygeKSLFLVNDWHAGLVPILLAA 300
Cdd:PLN02316 661 KVEGLSVYFLEpQNGMFWAGCVYGCR-----NDGERFGFFCHAALE---FLLQSGFH---PDIIHCHDWSSAPVAWLFKD 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 301 KYRPYGVYKdARSILIIHNLAhqgvepaatytnlglpsewYGAvgwvfptwarthaldtgeavNVLKGAIVTSDRIITVS 380
Cdd:PLN02316 730 HYAHYGLSK-ARVVFTIHNLE-------------------FGA--------------------NHIGKAMAYADKATTVS 769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 381 QGYAWEITtvegGYGLqdlLSSRKSVINGITNGINVDEWNPSTDEHIPFHYSADDVSE-KIKCKMALQKELGLPiRPECP 459
Cdd:PLN02316 770 PTYSREVS----GNSA---IAPHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEgKRAAKEALQQRLGLK-QADLP 841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 460 MIGFIGRLDYQKGIDLIQTAGPDLMVDDIQFVMLGSG-DPK----YESWMRSMEETYRDKFRGWVGFNVPISHRITAGCD 534
Cdd:PLN02316 842 LVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGSApDPRiqndFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGAD 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 535 ILLMPSRFEPCGLNQLYAMRYGTIPVVHGTGGLRDT---VENFNPYAEGGAGTGTGWVFTPLSKDSMVSALRLAAATYRE 611
Cdd:PLN02316 922 FILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTvfdVDHDKERAQAQGLEPNGFSFDGADAAGVDYALNRAISAWYD 1001
|
490 500 510
....*....|....*....|....*....|
gi 15237934 612 YKQSWEGLMRRGMTRNYSWENAAVQYEQVF 641
Cdd:PLN02316 1002 GRDWFNSLCKRVMEQDWSWNRPALDYMELY 1031
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
255-642 |
1.75e-17 |
|
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: 84.51 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 255 FRFTLLCHAACEAPLvlplgGFTYGEKSLFLVNDWHAGLVPILLAAKYRPYGVYKDArSILIIHNLAH-QGVEPAATYTN 333
Cdd:cd03801 32 HDVTVLTPADPGEPP-----EELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKF-DVVHAHGLLAaLLAALLALLLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 334 LGLPSEWYGAVGWVFPTWARTHAldtgEAVNVLKGAIVTSDRIITVSQGYAWEITTVEGgyglqdlLSSRKSVIngITNG 413
Cdd:cd03801 106 APLVVTLHGAEPGRLLLLLAAER----RLLARAEALLRRADAVIAVSEALRDELRALGG-------IPPEKIVV--IPNG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 414 INVDEWNPSTDEHipfhysaddvsekikckmalqkelgLPIRPECPMIGFIGRLDYQKGIDLIQTAGPDL--MVDDIQFV 491
Cdd:cd03801 173 VDLERFSPPLRRK-------------------------LGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLlrRGPDVRLV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 492 MLGSGDPkYESWMRSMEETYRDKFRgWVGFnVPIS--HRITAGCDILLMPSRFEPCGLNQLYAMRYGTIPVVHGTGGLRD 569
Cdd:cd03801 228 IVGGDGP-LRAELEELELGLGDRVR-FLGF-VPDEelPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPE 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15237934 570 TVENfnpyaeggagTGTGWVFTPLSKDSMVSALRlAAATYREYKQSWEGLMRRGMTRNYSWENAAVQYEQVFQ 642
Cdd:cd03801 305 VVED----------GEGGLVVPPDDVEALADALL-RLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
459-608 |
5.14e-13 |
|
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: 70.85 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 459 PMIGFIGRLDYQKGIDLIQTAGPDL-MVDDIQFVMLGSGDPKYEswMRSMEETY--RDKFRgWVGFNVPISHRITAgCDI 535
Cdd:cd03819 183 PVVGYVGRLSPEKGWLLLVDAAAELkDEPDFRLLVAGDGPERDE--IRRLVERLglRDRVT-FTGFREDVPAALAA-SDV 258
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15237934 536 LLMPSRFEPCGLNQLYAMRYGTIPVVHGTGGLRDTVENFNPyaeggagtgtGWVFTPLSKDSMVSALRLAAAT 608
Cdd:cd03819 259 VVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRT----------GLLVPPGDAEALADAIRAAKLL 321
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
459-574 |
1.25e-12 |
|
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: 66.14 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 459 PMIGFIGRLDYQKGIDLIQTAGPDLMVDDIQFVMLGSGDPKYESWMRSMEETY--RDKFRgWVGF----NVPISHRItag 532
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLglGDNVI-FLGFvsdeDLPELLKI--- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15237934 533 CDILLMPSRFEPCGLNQLYAMRYGTIPVVHGTGGLRDTVENF 574
Cdd:pfam00534 79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDG 120
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
531-644 |
4.92e-12 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 63.09 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 531 AGCDILLMPSRFEPCGLNQLYAMRYGTIPVVHGTGGLRDTVENfnpyaeggagTGTGWVFTPLSKDSMVSALRLAAATYR 610
Cdd:COG0438 19 AAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIED----------GETGLLVPPGDPEALAEAILRLLEDPE 88
|
90 100 110
....*....|....*....|....*....|....*..
gi 15237934 611 EYKQswegLMRRGMTR---NYSWENAAVQYEQVFQWV 644
Cdd:COG0438 89 LRRR----LGEAARERaeeRFSWEAIAERLLALYEEL 121
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
426-572 |
1.95e-11 |
|
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: 64.35 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 426 HIPFHYSADDVSEKIKCKMALQKELgLPIRPECPMIgFIGRLDYQKGID-LIQT---AGPDLmvDDIQFVMLGSGDPKYE 501
Cdd:cd01635 80 PIVVTVHGPDSLESTRSELLALARL-LVSLPLADKV-SVGRLVPEKGIDlLLEAlalLKARL--PDLVLVLVGGGGEREE 155
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15237934 502 sWMRSMEETYRDKFRGWVGFNVPISHR--ITAGCDILLMPSRFEPCGLNQLYAMRYGTIPVVHGTGGLRDTVE 572
Cdd:cd01635 156 -EEALAAALGLLERVVIIGGLVDDEVLelLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVV 227
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
373-573 |
4.32e-09 |
|
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: 58.76 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 373 SDRIITVSQGYAWEITTveggYGLQDllSSRKSVINGitNGINVDEWNPStDEHIPfhysaddvSEKIKckmalqkelgl 452
Cdd:cd03808 140 TDKVIFVNEDDRDLAIK----KGIIK--KKKTVLIPG--SGVDLDRFQYS-PESLP--------SEKVV----------- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 453 pirpecpmIGFIGRLDYQKGID-LIQTA------GPDLMvddiqFVMLGSGDPKYESWMRSMEETYRDKFRgWVGFNVPI 525
Cdd:cd03808 192 --------FLFVARLLKDKGIDeLIEAAkilkkkGPNVR-----FLLVGDGELENPSEILIEKLGLEGRIE-FLGFRSDV 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15237934 526 SHRITAgCDILLMPSRFEPCGLNQLYAMRYGtIPVV-HGTGGLRDTVEN 573
Cdd:cd03808 258 PELLAE-SDVFVLPSYREGLPRSLLEAMAAG-RPVItTDVPGCRELVID 304
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
459-575 |
6.38e-09 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 54.82 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 459 PMIGFIGRLD-YQKGID-LIQTAgPDLM--VDDIQFVMLGSGDP-KYESWMRSMEEtyRDKFRGWVGfNVPishRITAGC 533
Cdd:pfam13692 2 PVILFVGRLHpNVKGVDyLLEAV-PLLRkrDNDVRLVIVGDGPEeELEELAAGLED--RVIFTGFVE-DLA---ELLAAA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15237934 534 DILLMPSRFEPCGLNQLYAMRYGTiPVV-HGTGGLRDTVENFN 575
Cdd:pfam13692 75 DVFVLPSLYEGFGLKLLEAMAAGL-PVVaTDVGGIPELVDGEN 116
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
369-639 |
9.98e-09 |
|
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: 57.64 E-value: 9.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 369 AIVTSDRIITvsqgyaweiTTVEGGYGLQDLLSSRKSVINGITNGINVDEWNPSTDehipfhysaddvsekikcKMALQK 448
Cdd:cd03800 160 ILEAADRVIA---------STPQEADELISLYGADPSRINVVPPGVDLERFFPVDR------------------AEARRA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 449 ELGLPirPECPMIGFIGRLDYQKGID-LIQTAG--PDLMVD-DIQFVMLGSGDPKYESWMRSMEETYRDKFRGWVGFNVP 524
Cdd:cd03800 213 RLLLP--PDKPVVLALGRLDPRKGIDtLVRAFAqlPELRELaNLVLVGGPSDDPLSMDREELAELAEELGLIDRVRFPGR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 525 ISHR----ITAGCDILLMPSRFEPCGLNQLYAMRYGTiPVVhGT--GGLRDTVENfnpyaeggagTGTGWVFTPLSKDSM 598
Cdd:cd03800 291 VSRDdlpeLYRAADVFVVPSLYEPFGLTAIEAMACGT-PVV-ATavGGLQDIVRD----------GRTGLLVDPHDPEAL 358
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15237934 599 VSALRLAAATYREYKQSWEGLMRRGmTRNYSWENAAVQYEQ 639
Cdd:cd03800 359 AAALRRLLDDPALWQRLSRAGLERA-RAHYTWESVADQLLT 398
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
444-642 |
3.84e-07 |
|
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: 52.77 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 444 MALQKELGLPirPECPMIGFIGRLDYQKGIDLIQTAGPDLMVD--DIQFVMLGSG-DPKYESWMRSmEETYRDKFRgwvg 520
Cdd:cd03798 188 QPEDRGLGLP--LDAFVILFVGRLIPRKGIDLLLEAFARLAKArpDVVLLIVGDGpLREALRALAE-DLGLGDRVT---- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 521 FNVPISH----RITAGCDILLMPSRFEPCGLNQLYAMRYGTiPVVhGT--GGLRDTVENFNPyaeggagtgtgwVFTPLS 594
Cdd:cd03798 261 FTGRLPHeqvpAYYRACDVFVLPSRHEGFGLVLLEAMACGL-PVV-ATdvGGIPEVVGDPET------------GLLVPP 326
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15237934 595 KDSMVSALRLAAATYREYK-QSWEGLMRRGMTRnYSWENAAVQYEQVFQ 642
Cdd:cd03798 327 GDADALAAALRRALAEPYLrELGEAARARVAER-FSWVKAADRIAAAYR 374
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
373-561 |
8.58e-07 |
|
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: 51.59 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 373 SDRIITVSQGYAWEittveggygLQDLLSSRKSVINGITNGINVDEWNPSTDEHIPFhysaddvsekikckmalqkelgl 452
Cdd:cd03811 136 ADKIVCVSKGIKED---------LIRLGPSPPEKIEVIYNPIDIDRIRALAKEPILN----------------------- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 453 pIRPECPMIGFIGRLDYQKGID-LIQTAG--PDLMvDDIQFVMLGSGDPK--YESWMRSMEETYRDKFRGWVgFNVPish 527
Cdd:cd03811 184 -EPEDGPVILAVGRLDPQKGHDlLIEAFAklRKKY-PDVKLVILGDGPLReeLEKLAKELGLAERVIFLGFQ-SNPY--- 257
|
170 180 190
....*....|....*....|....*....|....
gi 15237934 528 RITAGCDILLMPSRFEPCGLNQLYAMRYGTiPVV 561
Cdd:cd03811 258 PYLKKADLFVLSSRYEGFPNVLLEAMALGT-PVV 290
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
302-639 |
1.37e-06 |
|
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 50.82 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 302 YRPYGVYKDARSILIIHNLAHqgvepaatytnLGLPsEWYGAVGWVFPTWArthaldtgeavnvLKGAIVTSDRIITVSQ 381
Cdd:cd03809 93 NTAPLLLKGCPQVVTIHDLIP-----------LRYP-EFFPKRFRLYYRLL-------------LPISLRRADAIITVSE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 382 gyaweittveggYGLQDLL------SSRKSVINgitNGInvdewnpstdEHIPFHYSADDVsekikckmaLQKELGLPir 455
Cdd:cd03809 148 ------------ATRDDIIkfygvpPEKIVVIP---LGV----------DPSFFPPESAAV---------LIAKYLLP-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 456 peCPMIGFIGRLDYQKGID-LIQTAG--PDLmVDDIQFVMLGSGDPKYESWMRSMEETYRDKFRGWVGFnvpISHR---- 528
Cdd:cd03809 192 --EPYFLYVGTLEPRKNHErLLKAFAllKKQ-GGDLKLVIVGGKGWEDEELLDLVKKLGLGGRVRFLGY---VSDEdlpa 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 529 ITAGCDILLMPSRFEPCGLNQLYAMRYGTiPVVHGTGG-LRDTVENFNPYaeggagtgtgwvFTPLSKDSMVSAL-RLAA 606
Cdd:cd03809 266 LYRGARAFVFPSLYEGFGLPVLEAMACGT-PVIASNISvLPEVAGDAALY------------FDPLDPESIADAIlRLLE 332
|
330 340 350
....*....|....*....|....*....|...
gi 15237934 607 ATYREYKQSWEGLMRrgmTRNYSWENAAVQYEQ 639
Cdd:cd03809 333 DPSLREELIRKGLER---AKKFSWEKTAEKTLE 362
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
452-561 |
9.62e-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: 48.43 E-value: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 452 LPIRPECPMIGFIGRLDYQKGIDLIQTAGPDL-MVDDIQFVMLGSGD--PKYESWMRSMEETYRDKFRGWVgFNVPISHR 528
Cdd:cd03817 195 LGLPPDEPILLYVGRLAKEKNIDFLLRAFAELkKEPNIKLVIVGDGPerEELKELARELGLADKVIFTGFV-PREELPEY 273
|
90 100 110
....*....|....*....|....*....|...
gi 15237934 529 ITAgCDILLMPSRFEPCGLNQLYAMRYGTiPVV 561
Cdd:cd03817 274 YKA-ADLFVFASTTETQGLVYLEAMAAGL-PVV 304
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
453-639 |
3.85e-05 |
|
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: 46.21 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 453 PIRPECPMIGFIGRLDYQKGIDL-------IQTAGPdlmvdDIQFVMLGSGDPKYESWMRSMEETYRDKFRGWVGFNVP- 524
Cdd:cd03821 199 NGLEDRRIILFLGRIHPKKGLDLliraarkLAEQGR-----DWHLVIAGPDDGAYPAFLQLQSSLGLGDRVTFTGPLYGe 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 525 ISHRITAGCDILLMPSRFEPCGLNQLYAMRYGTIPVVHGTGGLRDTVEnfnpyaeggagTGTGWVFTPlsKDSMVSALRL 604
Cdd:cd03821 274 AKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVE-----------AGCGVVVDP--NVSSLAEALA 340
|
170 180 190
....*....|....*....|....*....|....*...
gi 15237934 605 AAATYREYKQSWeGLMRRG---MTRNYSWENAAVQYEQ 639
Cdd:cd03821 341 EALRDPADRKRL-GEMARRarqVEENFSWEAVAGQLGE 377
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
445-622 |
2.43e-04 |
|
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: 43.82 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 445 ALQKELGLPIRPecpMIGFIGRLDYQKGID-LIQTAGPDLMVDDIQFVMLGSGDPKYESWMRSMEETYrdkfrgwVGFN- 522
Cdd:cd03814 188 ALRRRLGPPGRP---LLLYVGRLAPEKNLEaLLDADLPLAASPPVRLVVVGDGPARAELEARGPDVIF-------TGFLt 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237934 523 -VPIShRITAGCDILLMPSRFEPCGLNQLYAMRYGTIPVVHGTGGLRDTVEN------FNPYAEGGAGTGTGWVftpLSK 595
Cdd:cd03814 258 gEELA-RAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPggtgalVEPGDAAAFAAALRAL---LED 333
|
170 180
....*....|....*....|....*..
gi 15237934 596 DSMVSALRLAAATYREyKQSWEGLMRR 622
Cdd:cd03814 334 PELRRRMAARARAEAE-RYSWEAFLDN 359
|
|
| |
