|
Name |
Accession |
Description |
Interval |
E-value |
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
1-506 |
7.71e-128 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 380.59 E-value: 7.71e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 1 MHVLMVAAEndALPNAKVGGVADVVRDAPKALAAQGVSVDVVIPDYGF---EQLQREYIGDVTVIFRAQPQVLSLFKISD 77
Cdd:COG0297 1 MKILFVASE--AAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSiddKLKDLEVVASLEVPLGGRTYYARVLEGPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 78 DNTHInqFVISHPLFSQSGSVYCNdePGRPFATDATKYALFSAALCEaLLQGLITRPQALHLHDWHSACVAVLLKFDKRY 157
Cdd:COG0297 79 DGVPV--YFIDNPELFDRPGPYGD--PDRDYPDNAERFAFFSRAALE-LLKGLDWKPDIIHCHDWQTGLIPALLKTRYAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 158 DTLANLHIAYTVHNLALQGIRPFKHDDsslEAWFPSLGYNGQHLcdpRYPHCFNPMRSAINLADKVHLVSPTYSTEVLKP 237
Cdd:COG0297 154 DPFKRIKTVFTIHNLAYQGIFPAEILE---LLGLPPELFTPDGL---EFYGQINFLKAGIVYADRVTTVSPTYAREIQTP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 238 snyqqgfFGGEGLELDLQNQSaqGKVVGILNGCEYPEKNPEqvTLSALYERieHTLFNWMAKHE---QLetsyyvahQRM 314
Cdd:COG0297 228 -------EFGEGLDGLLRARS--GKLSGILNGIDYDVWNPA--TDPYLPAN--YSADDLEGKAAnkaAL--------QEE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 315 LQFKNTPiDGPLVTSIGRLTEQKVLLLCQQygnalALDKVCEIinrfNGRLIILGSGDKALESIFTKAMARNA-NLLFLK 393
Cdd:COG0297 287 LGLPVDP-DAPLIGMVSRLTEQKGLDLLLE-----ALDELLEE----DVQLVVLGSGDPEYEEAFRELAARYPgRVAVYI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 394 GYGQGIGDSLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNN------NGFAFSggslNEQVDGLM 467
Cdd:COG0297 357 GYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYGTVPIVRRTGGLADTVIDYNeatgegTGFVFD----EYTAEALL 432
|
490 500 510
....*....|....*....|....*....|....*....
gi 2233829271 468 TCLTETLTLKqQNPKQWSNITANAKGARFSWETVAADYI 506
Cdd:COG0297 433 AAIRRALALY-RDPEAWRKLQRNAMKQDFSWEKSAKEYL 470
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
2-506 |
1.62e-111 |
|
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: 338.77 E-value: 1.62e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 2 HVLMVAAEndALPNAKVGGVADVVRDAPKALAAQGVSVDVVIPDYGF---EQLQREYIGDVTVIFRAQPQVLSLFKISDD 78
Cdd:cd03791 1 KVLFVTSE--VAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQipdELDGYLRVLGLEVKVGGRGEEVGVFELPVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 79 NTHInqFVISHPLFSQSGSVYcnDEPGRPFATDATKYALFSAALCEALLQGLItRPQALHLHDWHSACVAVLLKFDKRYD 158
Cdd:cd03791 79 GVDY--YFLDNPEFFDRPGLP--GPPGYDYPDNAERFAFFSRAALELLRRLGF-QPDIIHANDWHTALVPAYLKTRYRGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 159 TLANLHIAYTVHNLALQGIRPFKHddssleawFPSLGYNGQHLC--DPRYPHCFNPMRSAINLADKVHLVSPTYSTEVLK 236
Cdd:cd03791 154 GFKKIKTVFTIHNLAYQGLFPLDT--------LAELGLPPELFHidGLEFYGQINFLKAGIVYADRVTTVSPTYAKEILT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 237 PSnyqqgffGGEGLELDLQNQSaqGKVVGILNGCEYPEKNPE-QVTLSALYERiehtlfNWMAKH----EQLetsyyvah 311
Cdd:cd03791 226 PE-------YGEGLDGVLRARA--GKLSGILNGIDYDEWNPAtDKLIPANYSA------NDLEGKaenkAAL-------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 312 QRMLQFKNTPiDGPLVTSIGRLTEQKVLLLcqqygnalaLDKVCEIINRFNGRLIILGSGDKALESIFTKAMARN-ANLL 390
Cdd:cd03791 283 QKELGLPVDP-DAPLFGFVGRLTEQKGVDL---------ILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYpGKVA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 391 FLKGYGQGIGDSLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNN------NGFAFSGGSlneqVD 464
Cdd:cd03791 353 VVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYDpetgegTGFVFEDYD----AE 428
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2233829271 465 GLMTCLTETLTLKqQNPKQWSNITANAKGARFSWETVAADYI 506
Cdd:cd03791 429 ALLAALRRALALY-RNPELWRKLQKNAMKQDFSWDKSAKEYL 469
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
1-510 |
1.18e-88 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 279.70 E-value: 1.18e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 1 MHVLMVAAEndALPNAKVGGVADVVRDAPKALAAQGVSVDVVIPDYGFeqlQREYIGDVTVIFRAQPqvLSLFKISDDNT 80
Cdd:PRK00654 1 MKILFVASE--CAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPA---IREKLRDAQVVGRLDL--FTVLFGHLEGD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 81 HINQFVISHPLFSQSGSVYcndepgrPFATDATKYALFSAALCEaLLQGLITRPQALHLHDWHSACVAVLLKfDKRYDTL 160
Cdd:PRK00654 74 GVPVYLIDAPHLFDRPSGY-------GYPDNGERFAFFSWAAAE-FAEGLDPRPDIVHAHDWHTGLIPALLK-EKYWRGY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 161 ANLHIAYTVHNLALQGIRPFKHddssleawFPSLGYNGQ--HLCDPRYPHCFNPMRSAINLADKVHLVSPTYSTEVLKPS 238
Cdd:PRK00654 145 PDIKTVFTIHNLAYQGLFPAEI--------LGELGLPAEafHLEGLEFYGQISFLKAGLYYADRVTTVSPTYAREITTPE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 239 nyqqgffGGEGLELDLQNQSaqGKVVGILNGCEYPEKNPEqvT---LSALYeriehTLFNWMAKHE---QLetsyyvahQ 312
Cdd:PRK00654 217 -------FGYGLEGLLRARS--GKLSGILNGIDYDIWNPE--TdplLAANY-----SADDLEGKAEnkrAL--------Q 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 313 RMLQFKNTpiDGPLVTSIGRLTEQKvlllcqqyGnalaLDKVCEIINRF---NGRLIILGSGDKALESIFTKAMARNANL 389
Cdd:PRK00654 273 ERFGLPDD--DAPLFAMVSRLTEQK--------G----LDLVLEALPELleqGGQLVLLGTGDPELEEAFRALAARYPGK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 390 LFLK-GYGQGIGDSLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNN------NGFAFSggslNEQ 462
Cdd:PRK00654 339 VGVQiGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPIVRRTGGLADTVIDYNpedgeaTGFVFD----DFN 414
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2233829271 463 VDGLMTCLTETLTLKQQnPKQWSNITANAKGARFSWETVAADYIsSMY 510
Cdd:PRK00654 415 AEDLLRALRRALELYRQ-PPLWRALQRQAMAQDFSWDKSAEEYL-ELY 460
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
1-506 |
8.79e-85 |
|
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: 269.91 E-value: 8.79e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 1 MHVLMVAAEndALPNAKVGGVADVVRDAPKALAAQGVSVDVVIPDYGfeQLQREYIGDVTVIFRA------QPQVLSLFK 74
Cdd:TIGR02095 1 MRVLFVAAE--MAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYG--CIEDEVDDQVKVVELVdlsvgpRTLYVKVFE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 75 ISDDNTHInqFVISHP-LFSQSGSVYCNDEPGrpfatDATKYALFSAAlCEALLQGLITRPQALHLHDWHSACVAVLLKf 153
Cdd:TIGR02095 77 GVVEGVPV--YFIDNPsLFDRPGGIYGDDYPD-----NAERFAFFSRA-AAELLSGLGWQPDVVHAHDWHTALVPALLK- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 154 dKRYdtlANLHIA--YTVHNLALQGIRPFkhDDSSLEAWFPSLGyngqHLCDPRYPHCFNPMRSAINLADKVHLVSPTYS 231
Cdd:TIGR02095 148 -AVY---RPNPIKtvFTIHNLAYQGVFPA--DDFSELGLPPEYF----HMEGLEFYGRVNFLKGGIVYADRVTTVSPTYA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 232 TEVLKPSnyqqgffGGEGLELDLQNQSaqGKVVGILNGCEYPEKNPE-QVTLSALYeriehTLFNWMAKHEQLEtsyyvA 310
Cdd:TIGR02095 218 REILTPE-------FGYGLDGVLKARS--GKLRGILNGIDTEVWNPAtDPYLKANY-----SADDLAGKAENKE-----A 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 311 HQRMLQFKNTPiDGPLVTSIGRLTEQKvlllcqqygnalALDKVCEIINRF---NGRLIILGSGDKALESIFTKAMARN- 386
Cdd:TIGR02095 279 LQEELGLPVDD-DVPLFGVISRLTQQK------------GVDLLLAALPELlelGGQLVVLGTGDPELEEALRELAERYp 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 387 ANLLFLKGYGQGIGDSLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNN------NGFAFSGGSLn 460
Cdd:TIGR02095 346 GNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTVPIVRRTGGLADTVVDGDpeaesgTGFLFEEYDP- 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2233829271 461 eqvDGLMTCLTETLTLKQQNPKQWSNITANAKGARFSWETVAADYI 506
Cdd:TIGR02095 425 ---GALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSAKQYV 467
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
3-256 |
9.74e-67 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 215.27 E-value: 9.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 3 VLMVAAENDalPNAKVGGVADVVRDAPKALAAQGVSVDVVIPDYGF---EQLQREYIGDVTVIF--RAQPQVLSLFKISD 77
Cdd:pfam08323 1 ILFVASEVA--PFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNipeERNQLEDVIRLSVAAgvPVRPLTVGVARLEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 78 DNthINQFVISHPLFSQSGSVYCNDepGRPFATDATKYALFSAALCEALlQGLITRPQALHLHDWHSACVAVLLKFDKRY 157
Cdd:pfam08323 79 DG--VDVYFLDNPDYFDRPGLYGDD--GRDYEDNAERFAFFSRAALELA-KKLGWIPDIIHCHDWHTALVPAYLKEAYAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 158 DTLANLHIAYTVHNLALQGIRPFkhdDSSLEAWFPSLGYngqHLCDPRYPHCFNPMRSAINLADKVHLVSPTYSTEVLKP 237
Cdd:pfam08323 154 DPFKNIKTVFTIHNLAYQGRFPA---DLLDLLGLPPEDF---NLDGLEFYGQINFLKAGIVYADAVTTVSPTYAEEIQTP 227
|
250
....*....|....*....
gi 2233829271 238 snyqqgfFGGEGLELDLQN 256
Cdd:pfam08323 228 -------EFGGGLDGLLRE 239
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1-505 |
1.87e-45 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 170.85 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 1 MHVLMVAAEndALPNAKVGGVADVVRDAPKALAAQGVSVDVVIPDYGFEQLQReyIGDVTVIfraQPQVLSLFkisDDNT 80
Cdd:PLN02939 482 LHIVHIAAE--MAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQYDQ--IRNLKVL---DVVVESYF---DGNL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 81 HINQFVI-------------SHP-LFSQSGSVYCNDEpgrpfatDATKYALFSAALCEALLQGLiTRPQALHLHDWHSAC 146
Cdd:PLN02939 552 FKNKIWTgtveglpvyfiepQHPsKFFWRAQYYGEHD-------DFKRFSYFSRAALELLYQSG-KKPDIIHCHDWQTAF 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 147 VAVLLkfdkrYDTLANL-----HIAYTVHNLALQGIRPFkhddssleawfPSLGYNG---QHLCDPR----YPHC-FNPM 213
Cdd:PLN02939 624 VAPLY-----WDLYAPKgfnsaRICFTCHNFEYQGTAPA-----------SDLASCGldvHQLDRPDrmqdNAHGrINVV 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 214 RSAINLADKVHLVSPTYSTEVLKPsnyqqgffGGEGLELDLQNQSAqgKVVGILNGCEYPEKNPE-QVTLSALYErieht 292
Cdd:PLN02939 688 KGAIVYSNIVTTVSPTYAQEVRSE--------GGRGLQDTLKFHSK--KFVGILNGIDTDTWNPStDRFLKVQYN----- 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 293 lfnwmAKHEQLETSYYVAHQRMLQFKNTPIDGPLVTSIGRLTEQKVLLLCQQygnalALDKVCEIinrfNGRLIILGSG- 371
Cdd:PLN02939 753 -----ANDLQGKAANKAALRKQLGLSSADASQPLVGCITRLVPQKGVHLIRH-----AIYKTAEL----GGQFVLLGSSp 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 372 ----DKALESIFTKAMARNANLLFLKgYGQGIGDSLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTV-- 445
Cdd:PLN02939 819 vphiQREFEGIADQFQSNNNIRLILK-YDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSVfd 897
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2233829271 446 -------SHNNNGFAFSggSLNEQvdGLMTCLTETLTLKQQNPKQWSNITANAKGARFSWETVAADY 505
Cdd:PLN02939 898 fddetipVELRNGFTFL--TPDEQ--GLNSALERAFNYYKRKPEVWKQLVQKDMNIDFSWDSSASQY 960
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
1-505 |
1.07e-41 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 155.65 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 1 MHVLMVAAEndALPNAKVGGVADVVRDAPKALAAQGVSVDVVIPDY-----GFEQLQ-----REYIGDVTVIFRAQPQVL 70
Cdd:PRK14099 4 LRVLSVASE--IFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYpavlaGIEDAEqvhsfPDLFGGPARLLAARAGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 71 SLFKIsdDNTHinqfvishpLFSQSGSVYCNDEpGRPFATDATKYAlfsaALCEA---LLQGLIT--RPQALHLHDWHSA 145
Cdd:PRK14099 82 DLFVL--DAPH---------LYDRPGNPYVGPD-GKDWPDNAQRFA----ALARAaaaIGQGLVPgfVPDIVHAHDWQAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 146 CVAVLLKFDKRydtlANLHIAYTVHNLALQGirpfkhddssleaWFPS--LGYNGQhlcdPryPHCFNP----------- 212
Cdd:PRK14099 146 LAPAYLHYSGR----PAPGTVFTIHNLAFQG-------------QFPRelLGALGL----P--PSAFSLdgveyyggigy 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 213 MRSAINLADKVHLVSPTYSTEVlkpsnyqQGFFGGEGLELDLQNQSAQgkVVGILNGCEYPEKNPEQVTLSALYERIEHT 292
Cdd:PRK14099 203 LKAGLQLADRITTVSPTYALEI-------QGPEAGMGLDGLLRQRADR--LSGILNGIDTAVWNPATDELIAATYDVETL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 293 LFNWMAKheqletsyyVAHQRMLQFKNTPiDGPLVTSIGRLTEQKVLLLcqqygnalaLDKVCEIINRFNGRLIILGSGD 372
Cdd:PRK14099 274 AARAANK---------AALQARFGLDPDP-DALLLGVISRLSWQKGLDL---------LLEALPTLLGEGAQLALLGSGD 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 373 KALESIFTKAMARN-ANLLFLKGYGQGIGDSLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNN-- 449
Cdd:PRK14099 335 AELEARFRAAAQAYpGQIGVVIGYDEALAHLIQAGADALLVPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVDANem 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2233829271 450 -------NGFAFSGGSlneqVDGLMTCLTETLTLkQQNPKQWSNITANAKGARFSWETVAADY 505
Cdd:PRK14099 415 aiatgvaTGVQFSPVT----ADALAAALRKTAAL-FADPVAWRRLQRNGMTTDVSWRNPAQHY 472
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1-456 |
2.50e-28 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 119.59 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 1 MHVLMVAAEndALPNAKVGGVADVVRDAPKALAAQGVSVDVVIPDYGFEQL--------QREYIGDVTVI--FRAQPQVL 70
Cdd:PLN02316 588 MHIVHIAVE--MAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLshvkdlhyQRSYSWGGTEIkvWFGKVEGL 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 71 SLFKISDDNThinqfvishplFSQSGSVY-CNDepgrpfatDATKYALFSAALCEALLQGLiTRPQALHLHDWHSACVAV 149
Cdd:PLN02316 666 SVYFLEPQNG-----------MFWAGCVYgCRN--------DGERFGFFCHAALEFLLQSG-FHPDIIHCHDWSSAPVAW 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 150 LLKFDKRYDTLANLHIAYTVHNLALqgirpfkhddssleawfpslgynGQHLcdpryphcfnpMRSAINLADKVHLVSPT 229
Cdd:PLN02316 726 LFKDHYAHYGLSKARVVFTIHNLEF-----------------------GANH-----------IGKAMAYADKATTVSPT 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 230 YSTEVlkpsnyqqgffGGEGLEldlqnQSAQGKVVGILNGCEYPEKNPEQVTLSALYERIEHTLFNWMAKHEQLetsyyv 309
Cdd:PLN02316 772 YSREV-----------SGNSAI-----APHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEAL------ 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 310 ahQRMLQFKNTpiDGPLVTSIGRLTEQKVLLLCQQygnalALDKVCEiinrFNGRLIILGSG-DKALESIFTK------- 381
Cdd:PLN02316 830 --QQRLGLKQA--DLPLVGIITRLTHQKGIHLIKH-----AIWRTLE----RNGQVVLLGSApDPRIQNDFVNlanqlhs 896
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 382 ---AMARnanlLFLKgYGQGIGDSLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDT---VSHNN------ 449
Cdd:PLN02316 897 shhDRAR----LCLT-YDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTvfdVDHDKeraqaq 971
|
490
....*....|.
gi 2233829271 450 ----NGFAFSG 456
Cdd:PLN02316 972 glepNGFSFDG 982
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
3-505 |
1.44e-25 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 109.44 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 3 VLMVAAEndALPNAKVGGVADVVRDAPKALAAQGVSVDVVIPDYG------FEQLQREYIGDVTVIFRAQPQVLSLFKIS 76
Cdd:PRK14098 8 VLYVSGE--VSPFVRVSALADFMASFPQALEEEGFEARIMMPKYGtindrkFRLHDVLRLSDIEVPLKEKTDLLHVKVTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 77 DDNTHINQ-FVISHPLFSQSGsVYCNDEPGRPFATDATKYALFSAALCEALlQGLITRPQALHLHDWHSACVAVLLKfdK 155
Cdd:PRK14098 86 LPSSKIQTyFLYNEKYFKRNG-LFTDMSLGGDLKGSAEKVIFFNVGVLETL-QRLGWKPDIIHCHDWYAGLVPLLLK--T 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 156 RY---DTLANLHIAYTVHNLALQGIRPFKHddssLEAWFPSLGYNGQHLCDPRyphcFNPMRSAINLADKVHLVSPTYST 232
Cdd:PRK14098 162 VYadhEFFKDIKTVLTIHNVYRQGVLPFKV----FQKLLPEEVCSGLHREGDE----VNMLYTGVEHADLLTTTSPRYAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 233 EVLkpSNYQQGFFGGEGLEldlqnqSAQGKVVGILNGCEYPEKNPEQVTLSALYERIEHTlfnwmakHEQLETSYYVAHQ 312
Cdd:PRK14098 234 EIA--GDGEEAFGLDKVLE------ERKMRLHGILNGIDTRQWNPSTDKLIKKRYSIERL-------DGKLENKKALLEE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 313 RMLQFKNtpiDGPLVTSIGRLTE-QKVLLLCQQYGNALALDKvceiinrfngRLIILGSGDKALESIFTKamarnanllF 391
Cdd:PRK14098 299 VGLPFDE---ETPLVGVIINFDDfQGAELLAESLEKLVELDI----------QLVICGSGDKEYEKRFQD---------F 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 392 LKGYGQGIG------DSLYELG----DLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTV----SHNNNGFAFSGG 457
Cdd:PRK14098 357 AEEHPEQVSvqteftDAFFHLAiaglDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETIeevsEDKGSGFIFHDY 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2233829271 458 SlneqVDGLMTCLTETLTLkQQNPKQWSNITANAKGARFSWETVAADY 505
Cdd:PRK14098 437 T----PEALVAKLGEALAL-YHDEERWEELVLEAMERDFSWKNSAEEY 479
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
321-507 |
1.04e-15 |
|
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: 78.73 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 321 PIDGPLVTSIGRLTEQK-VLLLCQqygnalALDKVCEIINRFngRLIILGSGDKALESIFTKAMARNANLLFLkGYgQGI 399
Cdd:cd03801 189 PPDRPVLLFVGRLSPRKgVDLLLE------ALAKLLRRGPDV--RLVIVGGDGPLRAELEELELGLGDRVRFL-GF-VPD 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 400 GD--SLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNNGFAFSGGSlneqVDGLMTCLTETLTlk 477
Cdd:cd03801 259 EElpALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDD----VEALADALLRLLA-- 332
|
170 180 190
....*....|....*....|....*....|...
gi 2233829271 478 qqNPKQWSNITANAKG---ARFSWETVAADYIS 507
Cdd:cd03801 333 --DPELRARLGRAARErvaERFSWERVAERLLD 363
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
323-484 |
5.98e-14 |
|
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: 69.61 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 323 DGPLVTSIGRLTEQK--VLLLcqqygnaLALDKVCEIINRFngRLIILGSGD--KALESIFTKAMARNaNLLFLKGYGQG 398
Cdd:pfam00534 1 KKKIILFVGRLEPEKglDLLI-------KAFALLKEKNPNL--KLVIAGDGEeeKRLKKLAEKLGLGD-NVIFLGFVSDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 399 IGDSLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNNGFAFSGGSLNEQVDGLMTCLTETLTLKQ 478
Cdd:pfam00534 71 DLPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRER 150
|
....*...
gi 2233829271 479 --QNPKQW 484
Cdd:pfam00534 151 lgENARKR 158
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
401-507 |
1.46e-13 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 67.32 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 401 DSLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNNGFAFSGGSLNEQVDGLMTCLtetltlkqQN 480
Cdd:COG0438 15 EALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLL--------ED 86
|
90 100 110
....*....|....*....|....*....|
gi 2233829271 481 PKQWSNITANAKG---ARFSWETVAADYIS 507
Cdd:COG0438 87 PELRRRLGEAAREraeERFSWEAIAERLLA 116
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
310-507 |
2.18e-11 |
|
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: 65.72 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 310 AHQRMLQfkNTPIDGPLVTSIGRLTEQK-VLLLCQQYGNALALdkvceiinRFNGRLIILGSGDKALESIFTKAMARNAN 388
Cdd:cd03800 208 EARRARL--LLPPDKPVVLALGRLDPRKgIDTLVRAFAQLPEL--------RELANLVLVGGPSDDPLSMDREELAELAE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 389 LL-------FLKGYGQG-IGDsLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNNGFAFSGGSLN 460
Cdd:cd03800 278 ELglidrvrFPGRVSRDdLPE-LYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPE 356
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2233829271 461 EqvdgLMTCLTETLTLKQQNPKQWSNITANAKgARFSWETVAADYIS 507
Cdd:cd03800 357 A----LAAALRRLLDDPALWQRLSRAGLERAR-AHYTWESVADQLLT 398
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
329-454 |
4.48e-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: 62.81 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 329 SIGRLTEQKvlllcqqyGNALALDKVCEIINRF-NGRLIILGSGD-KALESIFTKAMARNANLLFLKGYGQG-IGDSLYE 405
Cdd:cd01635 115 SVGRLVPEK--------GIDLLLEALALLKARLpDLVLVLVGGGGeREEEEALAAALGLLERVVIIGGLVDDeVLELLLA 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2233829271 406 LGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNNGFAF 454
Cdd:cd01635 187 AADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
318-464 |
8.57e-10 |
|
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: 60.30 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 318 KNTPIDGPLVTSIGRLTEQK-VLLLCQqygnalALDKVCEIINRFngRLIILGSGDKALESIFTKAMARNANLLFLKGYG 396
Cdd:cd03808 183 ESLPSEKVVFLFVARLLKDKgIDELIE------AAKILKKKGPNV--RFLLVGDGELENPSEILIEKLGLEGRIEFLGFR 254
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2233829271 397 QGIgDSLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNNGFAFSGGSLNEQVD 464
Cdd:cd03808 255 SDV-PELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALAD 321
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
324-461 |
5.25e-09 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 54.82 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 324 GPLVTSIGRLTEQK--VLLLcqqygnalaLDKVCEIINRFNG-RLIILGSGDkaLESIFTKAMARNANLLFLkGYgqgIG 400
Cdd:pfam13692 1 RPVILFVGRLHPNVkgVDYL---------LEAVPLLRKRDNDvRLVIVGDGP--EEELEELAAGLEDRVIFT-GF---VE 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2233829271 401 D--SLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVsHNNNGFAFSGGSLNE 461
Cdd:pfam13692 66 DlaELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEA 127
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
356-457 |
2.57e-08 |
|
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: 55.82 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 356 EIINRFNGRLIILGSGDkalESIFTKAMARNANLLflkGYGQGIGDS-----LYELGDLFLMPSSFEPCGISQMLAMRAG 430
Cdd:cd04962 220 RVRRKIPAKLLLVGDGP---ERVPAEELARELGVE---DRVLFLGKQddveeLLSIADLFLLPSEKESFGLAALEAMACG 293
|
90 100
....*....|....*....|....*..
gi 2233829271 431 QPCLVHSVGGLKDTVSHNNNGFAFSGG 457
Cdd:cd04962 294 VPVVSSNAGGIPEVVKHGETGFLSDVG 320
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
323-505 |
3.55e-08 |
|
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: 55.36 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 323 DGPLVTSIGRLTEQK---VLLlcqqygNALAldkvcEIINRFNGRLIILGSGdKALESIftKAMARNANLL----FLkGY 395
Cdd:cd03817 200 DEPILLYVGRLAKEKnidFLL------RAFA-----ELKKEPNIKLVIVGDG-PEREEL--KELARELGLAdkviFT-GF 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 396 gqgIGDS----LYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNNGFAFSGGslNEQVDGLMTCLT 471
Cdd:cd03817 265 ---VPREelpeYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPN--DETLAEKLLHLR 339
|
170 180 190
....*....|....*....|....*....|....
gi 2233829271 472 ETLTLKQQNPKQWSNITANAKGARfSWETVAADY 505
Cdd:cd03817 340 ENLELLRKLSKNAEISAREFAFAK-SVEKLYEEV 372
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
321-506 |
1.95e-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: 53.15 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 321 PIDGPLVTSIGRLTEQK-VLLLCQQYgnALALDKVCEIinrfngRLIILGSGdKALESIftKAMARNANL---LFLKGY- 395
Cdd:cd03798 197 PLDAFVILFVGRLIPRKgIDLLLEAF--ARLAKARPDV------VLLIVGDG-PLREAL--RALAEDLGLgdrVTFTGRl 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 396 -GQGIGDsLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNNGFAFSGGSlneqVDGLMTCLTETL 474
Cdd:cd03798 266 pHEQVPA-YYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGD----ADALAAALRRAL 340
|
170 180 190
....*....|....*....|....*....|...
gi 2233829271 475 tlkQQNPKQWSNITANAKGA-RFSWETVAADYI 506
Cdd:cd03798 341 ---AEPYLRELGEAARARVAeRFSWVKAADRIA 370
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
323-499 |
3.65e-07 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 52.41 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 323 DGPLVTSIGRLTEQKvlllcqqygnalALDKVCEIINRFNG-RLIILGSG--DKALESIFTkamarNANLLFLkgyGQGI 399
Cdd:PLN02871 262 EKPLIVYVGRLGAEK------------NLDFLKRVMERLPGaRLAFVGDGpyREELEKMFA-----GTPTVFT---GMLQ 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 400 GDSL---YELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTV---SHNNNGFAFSGGSlneqVDGLMTCLTET 473
Cdd:PLN02871 322 GDELsqaYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGD----VDDCVEKLETL 397
|
170 180
....*....|....*....|....*...
gi 2233829271 474 LTlkqqNPKQWSNI--TANAKGARFSWE 499
Cdd:PLN02871 398 LA----DPELRERMgaAAREEVEKWDWR 421
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
329-506 |
3.92e-07 |
|
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.
Pssm-ID: 340847 [Multi-domain] Cd Length: 351 Bit Score: 52.24 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 329 SIGRLTEQKvlllcqQYGnaLALDKVCEIINRFNG-RLIILGSGDKaLESIFTKAMARN-ANLLFLKGYGQGIgDSLYEL 406
Cdd:cd03820 186 AVGRLTYQK------GFD--LLIEAWALIAKKHPDwKLRIYGDGPE-REELEKLIDKLGlEDRVKLLGPTKNI-AEEYAN 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 407 GDLFLMPSSFEPCGISQMLAMRAGQPCLVH-SVGGLKDTVSHNNNGFAFSGGSLNEQVDGLMTcLTETLTLKQQnpkqws 485
Cdd:cd03820 256 SSIFVLSSRYEGFPMVLLEAMAYGLPIISFdCPTGPSEIIEDGENGLLVPNGDVDALAEALLR-LMEDEELRKK------ 328
|
170 180
....*....|....*....|...
gi 2233829271 486 nITANAK--GARFSWETVAADYI 506
Cdd:cd03820 329 -MGKNARknAERFSIEKIIKQWE 350
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
312-507 |
6.00e-07 |
|
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: 51.60 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 312 QRMLQFKNTPIDGPLVTSIGRLTEQKVLLLCQQygnalALDKVCEIINRFngRLIILGSGDKALEsiftKAMARNANL-- 389
Cdd:cd03821 192 LRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIR-----AARKLAEQGRDW--HLVIAGPDDGAYP----AFLQLQSSLgl 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 390 ----LFLKGYGQGIGDSLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNngfafsGGSLNEQVDG 465
Cdd:cd03821 261 gdrvTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAGC------GVVVDPNVSS 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2233829271 466 LMTCLTETLtlkqQNPKQWSNITANAKGAR-----FSWETVAADYIS 507
Cdd:cd03821 335 LAEALAEAL----RDPADRKRLGEMARRARqveenFSWEAVAGQLGE 377
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
323-454 |
1.25e-06 |
|
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: 50.43 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 323 DGPLVTSIGRLTEQKvlllcqqygNALALDKVCEIINRFNG-RLIILGSGDKALEsiftkaMARNANLLFLKGYGQGIG- 400
Cdd:cd03819 181 GKPVVGYVGRLSPEK---------GWLLLVDAAAELKDEPDfRLLVAGDGPERDE------IRRLVERLGLRDRVTFTGf 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2233829271 401 ----DSLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNNGFAF 454
Cdd:cd03819 246 redvPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLV 303
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
326-449 |
1.75e-05 |
|
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general 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 in bacteria.
Pssm-ID: 340857 [Multi-domain] Cd Length: 360 Bit Score: 47.05 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 326 LVTSIGRLTEQKvlllcqQYGNAL-ALDKVCEIINRFngRLIILGSG---DKALESIFTKAMARNanlLFLKGYGQGIGD 401
Cdd:cd04951 190 VILNVGRLTEAK------DYPNLLlAISELILSKNDF--KLLIAGDGplrNELERLICNLNLVDR---VILLGQISNISE 258
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2233829271 402 sLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNN 449
Cdd:cd04951 259 -YYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHN 305
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
402-507 |
2.54e-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: 46.56 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 402 SLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNNGFAFSGGSLNEQVDGLMTCLtetltlkqQNP 481
Cdd:cd03825 259 DIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLL--------ANP 330
|
90 100
....*....|....*....|....*....
gi 2233829271 482 KQWSNITANAK---GARFSWETVAADYIS 507
Cdd:cd03825 331 KERESLGERARalaENHFDQRVQAQRYLE 359
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
364-503 |
5.01e-05 |
|
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: 45.36 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 364 RLIILGSG--DKALEsiftkamARNANLLFLkGYGQGigDSL---YELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSV 438
Cdd:cd03814 230 RLVVVGDGpaRAELE-------ARGPDVIFT-GFLTG--EELaraYASADVFVFPSRTETFGLVVLEAMASGLPVVAADA 299
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2233829271 439 GGLKDTVSHNNNGFAFSGGSlneqvDGLMTCLTETLTlkqQNPKQWSNITANAKGA--RFSWETVAA 503
Cdd:cd03814 300 GGPRDIVRPGGTGALVEPGD-----AAAFAAALRALL---EDPELRRRMAARARAEaeRYSWEAFLD 358
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
306-502 |
2.14e-04 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 43.63 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 306 SYYVAHQRMLQFK-NTPIDGPLVTSIGRLTEQK-VLLLCQqygnalALDKVCEIinRFNGRLIILG------SGDKAL-- 375
Cdd:PRK15484 174 TYQSNPQPNLRQQlNISPDETVLLYAGRISPDKgILLLMQ------AFEKLATA--HSNLKLVVVGdptassKGEKAAyq 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 376 ESIFTKAMARNANLLFLKGYGQGIGDSLYELGDLFLMPSSF-EPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNNGFaf 454
Cdd:PRK15484 246 KKVLEAAKRIGDRCIMLGGQPPEKMHNYYPLADLVVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGY-- 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2233829271 455 sggSLNE--QVDGLMTCLTETLTlkqqNPKQwSNITANAKG---ARFSWETVA 502
Cdd:PRK15484 324 ---HLAEpmTSDSIISDINRTLA----DPEL-TQIAEQAKDfvfSKYSWEGVT 368
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
351-497 |
4.60e-04 |
|
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.
Pssm-ID: 340833 [Multi-domain] Cd Length: 356 Bit Score: 42.27 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 351 LDKVCEIINRFNGRLIILGSGdKALESIftKAMARNaNLLFLkGYgqgIGDSlyELGDL------FLMPSSfEPCGISQM 424
Cdd:cd03804 214 IDLAVEAFNELPKRLVVIGDG-PDLDRL--RAMASP-NVEFL-GY---QPDE--VLKELlskaraFVFAAE-EDFGIVPV 282
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2233829271 425 LAMRAGQPCLVHSVGGLKDTVSHNNNGFAFSggslnEQ-VDglmtCLTETLTLKQQNPKQW--SNITANAKgaRFS 497
Cdd:cd03804 283 EAQACGTPVIAFGKGGALETVRPGPTGILFG-----EQtVE----SLKAAVEEFEQNFDRFkpQAIRANAE--RFS 347
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
330-506 |
1.02e-03 |
|
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).
Pssm-ID: 340850 [Multi-domain] Cd Length: 357 Bit Score: 41.55 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 330 IGRLTEQKvlllcqqyGNALALDKVCEIInRFNGRLIILGSGDKALESiFTKAMARNANLLFlkgYGQGIGDSLYELGDL 409
Cdd:cd03823 197 IGRLTEEK--------GIDLLVEAFKRLP-REDIELVIAGHGPLSDER-QIEGGRRIAFLGR---VPTDDIKDFYEKIDV 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 410 FLMPSSF-EPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNNGFAFSGGSLNEqvdglmtcLTETLTLKQQNPKQWSNIT 488
Cdd:cd03823 264 LVVPSIWpEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAED--------LAAAMRRLLTDPALLERLR 335
|
170
....*....|....*...
gi 2233829271 489 ANAKgARFSWETVAADYI 506
Cdd:cd03823 336 AGAE-PPRSTESQAEEYL 352
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
316-452 |
2.08e-03 |
|
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.
Pssm-ID: 340839 [Multi-domain] Cd Length: 351 Bit Score: 40.42 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 316 QFKNTPIDGPLVTSIGRLTEQK--VLLLcqqygNALA-LDKvceiiNRFNGRLIILGSGD--KALESIftkamARNANL- 389
Cdd:cd03811 180 PILNEPEDGPVILAVGRLDPQKghDLLI-----EAFAkLRK-----KYPDVKLVILGDGPlrEELEKL-----AKELGLa 244
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2233829271 390 --LFLKGYGQGIGDsLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVSHNNNGF 452
Cdd:cd03811 245 erVIFLGFQSNPYP-YLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGL 308
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
321-445 |
3.22e-03 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 39.99 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 321 PIDGPLVTSIGRLTEQK-VLLLCQqygnalALDKVCEiiNRFNGRLIILGSGdkaLESIFTKAMARNANL---LFLKGYG 396
Cdd:cd03807 187 AEDRRVIGIVGRLHPVKdHSDLLR------AAALLVE--THPDLRLLLVGRG---PERPNLERLLLELGLedrVHLLGER 255
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2233829271 397 QGIGdSLYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTV 445
Cdd:cd03807 256 SDVP-ALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELV 303
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
330-502 |
3.62e-03 |
|
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: 39.65 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 330 IGRLTEQK-VLLLCQQYGNALALDKVCeiinrfngRLIILGSGDKALESIFTKAMARNA--NLLFLkGYgqgIGD----S 402
Cdd:cd03809 198 VGTLEPRKnHERLLKAFALLKKQGGDL--------KLVIVGGKGWEDEELLDLVKKLGLggRVRFL-GY---VSDedlpA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 403 LYELGDLFLMPSSFEPCGISQMLAMRAGQPCLVHSVGGLKDTVShnNNGFAFSggslNEQVDGLMTCLTETLT---LKQQ 479
Cdd:cd03809 266 LYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAG--DAALYFD----PLDPESIADAILRLLEdpsLREE 339
|
170 180
....*....|....*....|...
gi 2233829271 480 NPkqwSNITANAKgaRFSWETVA 502
Cdd:cd03809 340 LI---RKGLERAK--KFSWEKTA 357
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
326-435 |
6.78e-03 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).
Pssm-ID: 340840 [Multi-domain] Cd Length: 357 Bit Score: 38.81 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 326 LVTSIGRLTEQKvlllcqqygNALALDKVCEII--NRFNGRLIILGSGDKaLESIftKAMARnanllflkgyGQGIGDSL 403
Cdd:cd03812 193 VLGHVGRFNEQK---------NHSFLIDIFEELkkKNPNVKLVLVGEGEL-KEKI--KEKVK----------ELGLEDKV 250
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2233829271 404 YELG------------DLFLMPSSFEPCGISQMLAMRAGQPCLV 435
Cdd:cd03812 251 IFLGfrndvseilsamDVFLFPSLYEGLPLVAVEAQASGLPCLL 294
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
324-452 |
8.07e-03 |
|
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 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 and eukaryotes.
Pssm-ID: 340826 [Multi-domain] Cd Length: 355 Bit Score: 38.41 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 324 GPLVTSIGRLTEQK---VLLLCQQYGNalaldkvCEIInrfngrliILGSGD--KALESIFTKAMARNANLLflkGYgqg 398
Cdd:cd03795 191 KKIFLFIGRLVYYKgldYLIEAAQYLN-------YPIV--------IGGEGPlkPDLEAQIELNLLDNVKFL---GR--- 249
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2233829271 399 IGD----SLYELGDLFLMPSSF--EPCGISQMLAMRAGQPCLVHSVGGlkDTVSHNNNGF 452
Cdd:cd03795 250 VDDeekvIYLHLCDVFVFPSVLrsEAFGIVLLEAMMCGKPVISTNIGT--GVPYVNNNGE 307
|
|
| |
