|
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 ... |
84-580 |
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: 549.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 84 NVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYDQYKDAWDTSVVA---EIKVADRYERVRFFHCYKRGV 160
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVlglEVKVGGRGEEVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 161 DRVFIDHPSFLEKVWGKtgekiygPDTGVDYKDNQMRFSLLCQAALEAPRILnlnnnpyfkgtYGEDVVFVCNDWHTGPL 240
Cdd:cd03791 81 DYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRL-----------GFQPDIIHANDWHTALV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 241 ASYLKNNYQPNGiYRNAKVAFCIHNISYQGRFAFEDYPELNLSErfrsSFDFIDGYDtpvEGRKINWMKAGILEADRVLT 320
Cdd:cd03791 143 PAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPP----ELFHIDGLE---FYGQINFLKAGIVYADRVTT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 321 VSPYYAEELISGiARGCELDNI--MRLTGITGIVNGMDVSEWDPSKDKYITAKYDATTaIEAKALNKEALQAEAGLPVDR 398
Cdd:cd03791 215 VSPTYAKEILTP-EYGEGLDGVlrARAGKLSGILNGIDYDEWNPATDKLIPANYSAND-LEGKAENKAALQKELGLPVDP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 399 KIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHLIMAGADVL 478
Cdd:cd03791 293 DAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 479 AVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEG------KTGFhmgrlsvdckVVEPSDVKKVAATLKRAIKVVG 552
Cdd:cd03791 373 LMPSRFEPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYdpetgeGTGF----------VFEDYDAEALLAALRRALALYR 442
|
490 500
....*....|....*....|....*....
gi 1002280373 553 TP-AYEEMVRNCMNQDLSWKGPAKNWENV 580
Cdd:cd03791 443 NPeLWRKLQKNAMKQDFSWDKSAKEYLEL 471
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
83-584 |
1.31e-169 |
|
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: 491.01 E-value: 1.31e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 83 MNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYDQYKDAW----DTSVVAEIKVADRYERVRFFHCYKR 158
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVddqvKVVELVDLSVGPRTLYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 159 GVDRVFIDHPSFLEKvwgktGEKIYGPDtgvdYKDNQMRFSLLCQAALEAPRILNlnnnpyfkgtYGEDVVfVCNDWHTG 238
Cdd:TIGR02095 81 GVPVYFIDNPSLFDR-----PGGIYGDD----YPDNAERFAFFSRAAAELLSGLG----------WQPDVV-HAHDWHTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 239 PLASYLKNNYQPNgiyrNAKVAFCIHNISYQGRFAFEDYPELNLSERFRSSFDFIDGYDtpvegrkINWMKAGILEADRV 318
Cdd:TIGR02095 141 LVPALLKAVYRPN----PIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLEFYGR-------VNFLKGGIVYADRV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 319 LTVSPYYAEELISGiARGCELDNIMRLTG--ITGIVNGMDVSEWDPSKDKYITAKYDATTAiEAKALNKEALQAEAGLPV 396
Cdd:TIGR02095 210 TTVSPTYAREILTP-EFGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 397 DRKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHLIMAGAD 476
Cdd:TIGR02095 288 DDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGAD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 477 VLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGK------TGFHmgrlsvdckvVEPSDVKKVAATLKRAIKv 550
Cdd:TIGR02095 368 FILMPSRFEPCGLTQLYAMRYGTVPIVRRTGGLADTVVDGDpeaesgTGFL----------FEEYDPGALLAALSRALR- 436
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1002280373 551 vgtpAY-------EEMVRNCMNQDLSWKGPAKNWENVLLGL 584
Cdd:TIGR02095 437 ----LYrqdpslwEALQKNAMSQDFSWDKSAKQYVELYRSL 473
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
83-580 |
1.44e-159 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 465.34 E-value: 1.44e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 83 MNVVFVGAEMAPWSKTgglgdvlgglPPAMAANGHRVMVISPRYDQYKDAW-DTSVVAEIKV--ADRYERVRFFHCYKRG 159
Cdd:COG0297 1 MKILFVASEAAPFAKTggladvvgalPKALAKLGHDVRVVLPGYPSIDDKLkDLEVVASLEVplGGRTYYARVLEGPDDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 160 VDRVFIDHPSFLEkvwgktGEKIYGpDTGVDYKDNQMRFSLLCQAALEAprILNLNNNPyfkgtygeDVVFvCNDWHTGP 239
Cdd:COG0297 81 VPVYFIDNPELFD------RPGPYG-DPDRDYPDNAERFAFFSRAALEL--LKGLDWKP--------DIIH-CHDWQTGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 240 LASYLKNNYQPNGiYRNAKVAFCIHNISYQGRFAFEDYPELNLSERFrSSFDFIDGYDtpvegrKINWMKAGILEADRVL 319
Cdd:COG0297 143 IPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL-FTPDGLEFYG------QINFLKAGIVYADRVT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 320 TVSPYYAEELISGIArGCELDNIMRLTG--ITGIVNGMDVSEWDPSKDKYITAKYDATTaIEAKALNKEALQAEAGLPVD 397
Cdd:COG0297 215 TVSPTYAREIQTPEF-GEGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD-LEGKAANKAALQEELGLPVD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 398 RKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHLIMAGADV 477
Cdd:COG0297 293 PDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 478 LAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVI------EGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIKVV 551
Cdd:COG0297 373 FLMPSRFEPCGLNQMYALRYGTVPIVRRTGGLADTVIdyneatGEGTGF----------VFDEYTAEALLAAIRRALALY 442
|
490 500 510
....*....|....*....|....*....|
gi 1002280373 552 GTP-AYEEMVRNCMNQDLSWKGPAKNWENV 580
Cdd:COG0297 443 RDPeAWRKLQRNAMKQDFSWEKSAKEYLEL 472
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
83-575 |
2.61e-139 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 413.36 E-value: 2.61e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 83 MNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYDQYKDA-WDTSVVAEIKVAdryeRVRFFHCYKRGVD 161
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKlRDAQVVGRLDLF----TVLFGHLEGDGVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 162 RVFIDHPSFlekvwgktgekiYGPDTGVDYKDNQMRFSLLCQAALEAprILNLNNNPyfkgtygeDVVFvCNDWHTGPLA 241
Cdd:PRK00654 77 VYLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEF--AEGLDPRP--------DIVH-AHDWHTGLIP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 242 SYLKNNYQPNgiYRNAKVAFCIHNISYQGRFAFEDYPELNL-SERFRSSFDFIDGydtpvegrKINWMKAGILEADRVLT 320
Cdd:PRK00654 134 ALLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLpAEAFHLEGLEFYG--------QISFLKAGLYYADRVTT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 321 VSPYYAEELISGiARGCELDNIMRLTG--ITGIVNGMDVSEWDPSKDKYITAKYDATTaIEAKALNKEALQAEAGLPVDr 398
Cdd:PRK00654 204 VSPTYAREITTP-EFGYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENKRALQERFGLPDD- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 399 KIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHLIMAGADVL 478
Cdd:PRK00654 281 DAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 479 AVPSRFEPCGLIQLQGMRYGT-PCAcASTGGLVDTVI------EGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIKVV 551
Cdd:PRK00654 361 LMPSRFEPCGLTQLYALRYGTlPIV-RRTGGLADTVIdynpedGEATGF----------VFDDFNAEDLLRALRRALELY 429
|
490 500
....*....|....*....|....*
gi 1002280373 552 GTPA-YEEMVRNCMNQDLSWKGPAK 575
Cdd:PRK00654 430 RQPPlWRALQRQAMAQDFSWDKSAE 454
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
83-577 |
3.48e-87 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 279.68 E-value: 3.48e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 83 MNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYdqykdawdTSVVAEIKVADRYERVR-FFHCYKR--- 158
Cdd:PRK14099 4 LRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGY--------PAVLAGIEDAEQVHSFPdLFGGPARlla 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 159 ----GVDRVFIDHPsfleKVWGKTGEKIYGPDtGVDYKDNQMRFSLLCQAALEapriLNLNNNPYFKgtygEDVVFVcND 234
Cdd:PRK14099 76 aragGLDLFVLDAP----HLYDRPGNPYVGPD-GKDWPDNAQRFAALARAAAA----IGQGLVPGFV----PDIVHA-HD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 235 WHTGPLASYLKNNYQPNgiyrnAKVAFCIHNISYQGRFAFEDYPELNLSERfrsSFDfIDGydtpVE--GrKINWMKAGI 312
Cdd:PRK14099 142 WQAGLAPAYLHYSGRPA-----PGTVFTIHNLAFQGQFPRELLGALGLPPS---AFS-LDG----VEyyG-GIGYLKAGL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 313 LEADRVLTVSPYYAEElISGIARGCELDNIMRLTG--ITGIVNGMDVSEWDPSKDKYITAKYDATTaIEAKALNKEALQA 390
Cdd:PRK14099 208 QLADRITTVSPTYALE-IQGPEAGMGLDGLLRQRAdrLSGILNGIDTAVWNPATDELIAATYDVET-LAARAANKAALQA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 391 EAGLPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHL 470
Cdd:PRK14099 286 RFGLDPDPDALLLGVISRLSWQKGLDLLLEALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 471 IMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGK---------TGFHMGRLSVDCkvvepsdvkkVA 541
Cdd:PRK14099 366 IQAGADALLVPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVDANemaiatgvaTGVQFSPVTADA----------LA 435
|
490 500 510
....*....|....*....|....*....|....*..
gi 1002280373 542 ATLKRAIKVVGTPA-YEEMVRNCMNQDLSWKGPAKNW 577
Cdd:PRK14099 436 AALRKTAALFADPVaWRRLQRNGMTTDVSWRNPAQHY 472
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
85-344 |
1.01e-66 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 217.58 E-value: 1.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 85 VVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYD-------QYKDAWDTSVVAEIKVadRYERVRFFHCYK 157
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGnipeernQLEDVIRLSVAAGVPV--RPLTVGVARLEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 158 RGVDRVFIDHPSFLEKvwgktgEKIYGpDTGVDYKDNQMRFSLLCQAALEAPRILNlnnnpyfkgtYGEDVVfVCNDWHT 237
Cdd:pfam08323 79 DGVDVYFLDNPDYFDR------PGLYG-DDGRDYEDNAERFAFFSRAALELAKKLG----------WIPDII-HCHDWHT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 238 GPLASYLKNNYQPNGiYRNAKVAFCIHNISYQGRFAFEDYPELNLSERFRSsfdfIDGYDTPvegRKINWMKAGILEADR 317
Cdd:pfam08323 141 ALVPAYLKEAYADDP-FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN----LDGLEFY---GQINFLKAGIVYADA 212
|
250 260
....*....|....*....|....*..
gi 1002280373 318 VLTVSPYYAEELISGiARGCELDNIMR 344
Cdd:pfam08323 213 VTTVSPTYAEEIQTP-EFGGGLDGLLR 238
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
232-577 |
1.23e-66 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 225.38 E-value: 1.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 232 CNDWHTGPLASYLKNNYQPNGIYRNAKVAFCIHNISYQGRFAFEDYPELnLSErfrssfDFIDGYDtpVEGRKINWMKAG 311
Cdd:PRK14098 147 CHDWYAGLVPLLLKTVYADHEFFKDIKTVLTIHNVYRQGVLPFKVFQKL-LPE------EVCSGLH--REGDEVNMLYTG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 312 ILEADRVLTVSPYYAEELISGIARGCELDNIM--RLTGITGIVNGMDVSEWDPSKDKYITAKYDATTaIEAKALNKEALQ 389
Cdd:PRK14098 218 VEHADLLTTTSPRYAEEIAGDGEEAFGLDKVLeeRKMRLHGILNGIDTRQWNPSTDKLIKKRYSIER-LDGKLENKKALL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 390 AEAGLPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAH 469
Cdd:PRK14098 297 EEVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFH 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 470 LIMAGADVLAVPSRFEPCGLIQLQGMRYGT-PCACAsTGGLVDTVIE----GKTGFhmgrlsvdckVVEPSDVKKVAATL 544
Cdd:PRK14098 377 LAIAGLDMLLMPGKIESCGMLQMFAMSYGTiPVAYA-GGGIVETIEEvsedKGSGF----------IFHDYTPEALVAKL 445
|
330 340 350
....*....|....*....|....*....|....
gi 1002280373 545 KRAIKVVG-TPAYEEMVRNCMNQDLSWKGPAKNW 577
Cdd:PRK14098 446 GEALALYHdEERWEELVLEAMERDFSWKNSAEEY 479
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
83-574 |
1.24e-52 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 194.70 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 83 MNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYD----------QYKDA--WDTSvvaEIKVAdrYERV 150
Cdd:PLN02316 588 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDclnlshvkdlHYQRSysWGGT---EIKVW--FGKV 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 151 RFFHCYkrgvdrvfidhpsFLEKVWGKTGEK-IYGPdtgvdyKDNQMRFSLLCQAALEAprILNLNNNPyfkgtygeDVV 229
Cdd:PLN02316 663 EGLSVY-------------FLEPQNGMFWAGcVYGC------RNDGERFGFFCHAALEF--LLQSGFHP--------DII 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 230 FvCNDWHTGPLASYLKNNYQPNGIyRNAKVAFCIHNISYqgrfafedypelnlserfrssfdfidgydtpvegrKINWMK 309
Cdd:PLN02316 714 H-CHDWSSAPVAWLFKDHYAHYGL-SKARVVFTIHNLEF-----------------------------------GANHIG 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 310 AGILEADRVLTVSPYYAEElISG---IARgceldnimRLTGITGIVNGMDVSEWDPSKDKYITAKYDATTAIEAKALNKE 386
Cdd:PLN02316 757 KAMAYADKATTVSPTYSRE-VSGnsaIAP--------HLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKE 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 387 ALQAEAGL-PVDrkIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTG-----KKKFEKLLKSMEEKYPGKVRAV 460
Cdd:PLN02316 828 ALQQRLGLkQAD--LPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGSApdpriQNDFVNLANQLHSSHHDRARLC 905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 461 VKFNAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEgktgfhmgrlsVD-------CKVVE 533
Cdd:PLN02316 906 LTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTVFD-----------VDhdkeraqAQGLE 974
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1002280373 534 P-------SDVKKVAATLKRAIKVV--GTPAYEEMVRNCMNQDLSWKGPA 574
Cdd:PLN02316 975 PngfsfdgADAAGVDYALNRAISAWydGRDWFNSLCKRVMEQDWSWNRPA 1024
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
70-580 |
1.13e-50 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 188.57 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 70 RFPSVVVYATGAGMNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYD--QYKDawdtsvVAEIKVADRy 147
Cdd:PLN02939 469 NFLKLTLSGTSSGLHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDcmQYDQ------IRNLKVLDV- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 148 ervrffhcykrgVDRVFIDHPSFLEKVWGKTGE-------------KIYGPDTGVDYKDNQMRFSLLCQAALEAprILNL 214
Cdd:PLN02939 542 ------------VVESYFDGNLFKNKIWTGTVEglpvyfiepqhpsKFFWRAQYYGEHDDFKRFSYFSRAALEL--LYQS 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 215 NNNPyfkgtygeDVVFvCNDWHTGPLASYLKNNYQPNGiYRNAKVAFCIHNISYQGRFAFE-------DYPELNLSERFR 287
Cdd:PLN02939 608 GKKP--------DIIH-CHDWQTAFVAPLYWDLYAPKG-FNSARICFTCHNFEYQGTAPASdlascglDVHQLDRPDRMQ 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 288 SSfdfidgydtpvEGRKINWMKAGILEADRVLTVSPYYAEELISGIARGCELDNIMRLTGITGIVNGMDVSEWDPSKDKY 367
Cdd:PLN02939 678 DN-----------AHGRINVVKGAIVYSNIVTTVSPTYAQEVRSEGGRGLQDTLKFHSKKFVGILNGIDTDTWNPSTDRF 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 368 ITAKYDATTaIEAKALNKEALQAEAGLP-VDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTG-----KKK 441
Cdd:PLN02939 747 LKVQYNAND-LQGKAANKAALRKQLGLSsADASQPLVGCITRLVPQKGVHLIRHAIYKTAELGGQFVLLGSSpvphiQRE 825
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 442 FEKLLKSMEEKypGKVRAVVKFNAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTV-------- 513
Cdd:PLN02939 826 FEGIADQFQSN--NNIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSVfdfddeti 903
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 514 -IEGKTGFHMGRlsvdckvvepSDVKKVAATLKRAIKVV--GTPAYEEMVRNCMNQDLSWKGPAKNWENV 580
Cdd:PLN02939 904 pVELRNGFTFLT----------PDEQGLNSALERAFNYYkrKPEVWKQLVQKDMNIDFSWDSSASQYEEL 963
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
197-581 |
2.29e-23 |
|
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: 102.23 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 197 RFSLLCQAALEAPRILNLNNNPYFKGTYgeDVVfVCNDWHTGPLASYLKnnyqpngIYRNAKVAFCIHNISYQGRFAFED 276
Cdd:cd03801 56 PLLPSLAALLRARRLLRELRPLLRLRKF--DVV-HAHGLLAALLAALLA-------LLLGAPLVVTLHGAEPGRLLLLLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 277 YPElnlserfrssfdfidgydtpvegRKINWMKAGILEADRVLTVSPYYAEELISgiargcelDNIMRLTGITGIVNGMD 356
Cdd:cd03801 126 AER-----------------------RLLARAEALLRRADAVIAVSEALRDELRA--------LGGIPPEKIVVIPNGVD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 357 VSEWDPskdkyitakydattaieakalnkeALQAEAGLPVDRkiPLIAFIGRLEEQKGPDVMAAAIPELMQE--DVQIVL 434
Cdd:cd03801 175 LERFSP------------------------PLRRKLGIPPDR--PVLLFVGRLSPRKGVDLLLEALAKLLRRgpDVRLVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 435 LGTGKKKFEKLlKSMEEKYPGKVRAVVKFNAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVI 514
Cdd:cd03801 229 VGGDGPLRAEL-EELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 515 EGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIKvvGTPAYEEMVRN---CMNQDLSWKGPAKNWENVL 581
Cdd:cd03801 308 DGEGGL----------VVPPDDVEALADALLRLLA--DPELRARLGRAareRVAERFSWERVAERLLDLY 365
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
401-549 |
3.34e-19 |
|
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: 84.63 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 401 PLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHLI--MAGADVL 478
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPelLKIADVF 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002280373 479 AVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIK 549
Cdd:pfam00534 83 VLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGF----------LVKPNNAEALAEAIDKLLE 143
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
401-549 |
3.30e-18 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 81.40 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 401 PLIAFIGRL-EEQKGPDVMAAAIPELMQE--DVQIVLLGTGK-KKFEKLLKSMEEK--YPGKVRAVVKFnaplahliMAG 474
Cdd:pfam13692 2 PVILFVGRLhPNVKGVDYLLEAVPLLRKRdnDVRLVIVGDGPeEELEELAAGLEDRviFTGFVEDLAEL--------LAA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002280373 475 ADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDtVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIK 549
Cdd:pfam13692 74 ADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPE-LVDGENGL----------LVPPGDPEALAEAILRLLE 137
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
385-549 |
1.50e-16 |
|
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: 81.90 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 385 KEALQAEAGLPVDRKIplIAFIGRLEEQKGPDVMAAA---IPELmQEDVQIVLLGTG-----------KKKFEKLLKSME 450
Cdd:cd03800 207 AEARRARLLLPPDKPV--VLALGRLDPRKGIDTLVRAfaqLPEL-RELANLVLVGGPsddplsmdreeLAELAEELGLID 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 451 E-KYPGKVRAVVkfnapLAHLIMAgADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFHmgrlsvdc 529
Cdd:cd03800 284 RvRFPGRVSRDD-----LPELYRA-ADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLL-------- 349
|
170 180
....*....|....*....|
gi 1002280373 530 kvVEPSDVKKVAATLKRAIK 549
Cdd:cd03800 350 --VDPHDPEALAAALRRLLD 367
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
314-548 |
1.02e-13 |
|
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: 73.18 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 314 EADRVLTVSPYYAEELIS-GIARGceldnimrltGITGIVNGMDVSEWDPSkdkyitakydattaieakalnkealQAEA 392
Cdd:cd03798 150 RAARVIAVSKALAEELVAlGVPRD----------RVDVIPNGVDPARFQPE-------------------------DRGL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 393 GLPVDRkiPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLL--GTG--KKKFEKLLKSmeekypGKVRAVVKFNAPLA 468
Cdd:cd03798 195 GLPLDA--FVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLivGDGplREALRALAED------LGLGDRVTFTGRLP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 469 H----LIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATL 544
Cdd:cd03798 267 HeqvpAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGL----------LVPPGDADALAAAL 336
|
....
gi 1002280373 545 KRAI 548
Cdd:cd03798 337 RRAL 340
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
405-520 |
2.58e-13 |
|
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: 69.74 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 405 FIGRLEEQKGPDVMAAAIPELMQE--DVQIVLLGTGKKKfEKLLKSMEEKYPGKVRAVVKF--NAPLAHLIMAGADVLAV 480
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLKARlpDLVLVLVGGGGER-EEEEALAAALGLLERVVIIGGlvDDEVLELLLAAADVFVL 193
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1002280373 481 PSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGF 520
Cdd:cd01635 194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
467-584 |
6.10e-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: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 467 LAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKR 546
Cdd:COG0438 13 LLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGL----------LVPPGDPEALAEAILR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1002280373 547 AIKvvGTPAYEEMVRNC---MNQDLSWKGPAKNWENVLLGL 584
Cdd:COG0438 83 LLE--DPELRRRLGEAArerAEERFSWEAIAERLLALYEEL 121
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
297-561 |
1.20e-11 |
|
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: 66.22 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 297 DTPVEGRKINWMKAGILEADRVLTVSPYYAEELISGIARGCELdnimrltgITGIVNGMDvsewdpskdkyiTAKYDATT 376
Cdd:cd03819 109 SYLATYHPKDFALAVRARGDRVIAVSELVRDHLIEALGVDPER--------IRVIPNGVD------------TDRFPPEA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 377 AIEAKAlnkealqaeaGLPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELmQEDVQIVLLGTGKKKFEKLLKSMEEKYPGK 456
Cdd:cd03819 169 EAEERA----------QLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAGDGPERDEIRRLVERLGLR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 457 VRAVVKFNAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrLSVDCKVVEPSD 536
Cdd:cd03819 238 DRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGL----LVPPGDAEALAD 313
|
250 260
....*....|....*....|....*.
gi 1002280373 537 VKK-VAATLKRAIKVVGTPAYEEMVR 561
Cdd:cd03819 314 AIRaAKLLPEAREKLQAAAALTEAVR 339
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
403-548 |
5.72e-11 |
|
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: 64.27 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 403 IAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEE-KYPGKVRavvkfNAPLAHLiMAGADVLAVP 481
Cdd:cd03823 194 FGYIGRLTEEKGIDLLVEAFKRLPREDIELVIAGHGPLSDERQIEGGRRiAFLGRVP-----TDDIKDF-YEKIDVLVVP 267
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002280373 482 SRF-EPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFHmgrlsvdckvVEPSDVKKVAATLKRAI 548
Cdd:cd03823 268 SIWpEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLL----------FAPGDAEDLAAAMRRLL 325
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
384-581 |
8.02e-11 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 64.04 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 384 NKEALQAEAGLPVDRKIplIAFIGRLEEQKGPDVMAAAIPELM--QEDVQIVLLG--TGKKKFEKllksmeEKYPGKVRA 459
Cdd:PRK15484 179 PQPNLRQQLNISPDETV--LLYAGRISPDKGILLLMQAFEKLAtaHSNLKLVVVGdpTASSKGEK------AAYQKKVLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 460 VVKfnAPLAHLIMAG-------------ADVLAVPSRF-EPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFHMGrl 525
Cdd:PRK15484 251 AAK--RIGDRCIMLGgqppekmhnyyplADLVVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLA-- 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002280373 526 svdckvvEPSDVKKVAATLKRAIKVVGTPAYEEMVRNCMNQDLSWKGPAKNWENVL 581
Cdd:PRK15484 327 -------EPMTSDSIISDINRTLADPELTQIAEQAKDFVFSKYSWEGVTQRFEEQI 375
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
303-549 |
2.64e-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: 62.23 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 303 RKINWMKAGILE------ADRVLTVSPYYAEELISgiARGCELDNIMRLTGitgivNGMDVSEWDPSKDKYITAKydatt 376
Cdd:cd03808 122 GKLLRLLYLLLEklallfTDKVIFVNEDDRDLAIK--KGIIKKKKTVLIPG-----SGVDLDRFQYSPESLPSEK----- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 377 aieakalnkealqaeaglpvdrkiPLIAFIGRLEEQKGPD--VMAAAIPELMQEDVQIVLLGTG------KKKFEKLLKS 448
Cdd:cd03808 190 ------------------------VVFLFVARLLKDKGIDelIEAAKILKKKGPNVRFLLVGDGelenpsEILIEKLGLE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 449 MEEKYPGKVRAVVKFnaplahliMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvd 528
Cdd:cd03808 246 GRIEFLGFRSDVPEL--------LAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGF-------- 309
|
250 260
....*....|....*....|.
gi 1002280373 529 ckVVEPSDVKKVAATLKRAIK 549
Cdd:cd03808 310 --LVPPGDVEALADAIEKLIE 328
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
403-549 |
5.53e-10 |
|
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: 61.48 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 403 IAFIGRLEEQKGPDVM--AAAIPELMQEDVQIVLLGTG--KKKFEKLLKS--MEE--KYPGKVRAVvkfnaplaHLIMAG 474
Cdd:cd03820 184 ILAVGRLTYQKGFDLLieAWALIAKKHPDWKLRIYGDGpeREELEKLIDKlgLEDrvKLLGPTKNI--------AEEYAN 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002280373 475 ADVLAVPSRFEPCGLIQLQGMRYGTPCAC-ASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIK 549
Cdd:cd03820 256 SSIFVLSSRYEGFPMVLLEAMAYGLPIISfDCPTGPSEIIEDGENGL----------LVPNGDVDALAEALLRLME 321
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
303-520 |
3.56e-09 |
|
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: 58.91 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 303 RKINWMKAGILEADRVLTVSPYYAEELIS-GIARGCELDNIMrltgitgivNGMDVSEwdpskdkyitakydattaieAK 381
Cdd:cd03811 124 KKLLLKLKLYKKADKIVCVSKGIKEDLIRlGPSPPEKIEVIY---------NPIDIDR--------------------IR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 382 ALNKEALQAEaglpvDRKIPLIAFIGRLEEQKGPDVM--AAAIPELMQEDVQIVLLGTGKKKfEKLLKSMEE-------K 452
Cdd:cd03811 175 ALAKEPILNE-----PEDGPVILAVGRLDPQKGHDLLieAFAKLRKKYPDVKLVILGDGPLR-EELEKLAKElglaervI 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002280373 453 YPGKVRAVVKFnaplahliMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGF 520
Cdd:cd03811 249 FLGFQSNPYPY--------LKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGL 308
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
401-563 |
1.61e-08 |
|
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: 56.90 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 401 PLIAFIGRLEEQKGPDVMAAAIPELmqeDVQIVLLGTGKKKfEKLLKSMEEKYPGKVRAVVKF-NAPLAHLIMAgADVLA 479
Cdd:cd03795 192 KIFLFIGRLVYYKGLDYLIEAAQYL---NYPIVIGGEGPLK-PDLEAQIELNLLDNVKFLGRVdDEEKVIYLHL-CDVFV 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 480 VPS--RFEPCGLIQLQGMRYGTP-CACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIKvvGTPAY 556
Cdd:cd03795 267 FPSvlRSEAFGIVLLEAMMCGKPvISTNIGTGVPYVNNNGETGL----------VVPPKDPDALAEAIDKLLS--DEELR 334
|
....*..
gi 1002280373 557 EEMVRNC 563
Cdd:cd03795 335 ESYGENA 341
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
255-507 |
2.88e-08 |
|
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: 56.22 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 255 RNAKVAFCIHNisyqgrFAFEDYPELnlserfrSSFDFIDGYDTpvegrkinWMKAGILEADRVLTVSPYYAEELIsgia 334
Cdd:cd03809 100 KGCPQVVTIHD------LIPLRYPEF-------FPKRFRLYYRL--------LLPISLRRADAIITVSEATRDDII---- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 335 rgceldnimRLTGItgivngmdvsewdpSKDKYITAkYDATTAIEAKALNKEALQAEAGLPVdrkiPLIAFIGRLEEQKG 414
Cdd:cd03809 155 ---------KFYGV--------------PPEKIVVI-PLGVDPSFFPPESAAVLIAKYLLPE----PYFLYVGTLEPRKN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 415 PDVMAAA---IPELMQeDVQIVLLGTGKKKFEKLLKSMEEKY-PGKVRAVVKFNAP-LAHLImAGADVLAVPSRFEPCGL 489
Cdd:cd03809 207 HERLLKAfalLKKQGG-DLKLVIVGGKGWEDEELLDLVKKLGlGGRVRFLGYVSDEdLPALY-RGARAFVFPSLYEGFGL 284
|
250
....*....|....*...
gi 1002280373 490 IQLQGMRYGTPCACASTG 507
Cdd:cd03809 285 PVLEAMACGTPVIASNIS 302
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
267-563 |
2.93e-08 |
|
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: 56.15 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 267 SYQGRFafedyPELnLSERFRSsfdfidgydtPVEGRKINWMKAGILEADRVLTVSPYYAEELIsgiARGCEldNIMRLT 346
Cdd:cd03814 114 SYHTDF-----PEY-LSYYTLG----------PLSWLAWAYLRWFHNPFDTTLVPSPSIARELE---GHGFE--RVRLWP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 347 gitgivNGMDVSEWDPS-KDKyitakydattaieakALNKEALQAEAglpvdrkiPLIAFIGRLEEQKGPDVMAAAIPEL 425
Cdd:cd03814 173 ------RGVDTELFHPSrRDA---------------ALRRRLGPPGR--------PLLLYVGRLAPEKNLEALLDADLPL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 426 MQED-VQIVLLGTGKKKfekllKSMEEKYPGKVRAVVKFNAPLAHlIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACA 504
Cdd:cd03814 224 AASPpVRLVVVGDGPAR-----AELEARGPDVIFTGFLTGEELAR-AYASADVFVFPSRTETFGLVVLEAMASGLPVVAA 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002280373 505 STGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATL------KRAIKVVGTPAYEEMVRNC 563
Cdd:cd03814 298 DAGGPRDIVRPGGTGA----------LVEPGDAAAFAAALralledPELRRRMAARARAEAERYS 352
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
381-521 |
4.99e-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: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 381 KALNKEALQaEAGLPVDRKIplIAFIGRLEEQKGPDVMAAAIPEL-MQEDVQIVLLGTG--KKKFEKLLKSMeekypgKV 457
Cdd:cd03817 185 KPLNTEERR-KLGLPPDEPI--LLYVGRLAKEKNIDFLLRAFAELkKEPNIKLVIVGDGpeREELKELAREL------GL 255
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002280373 458 RAVVKF-----NAPLAHLiMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFH 521
Cdd:cd03817 256 ADKVIFtgfvpREELPEY-YKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFL 323
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
401-546 |
6.36e-08 |
|
glycosyltransferase family 4 proteins; 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 glycosyltransferase family 4 (GT4). 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.
Pssm-ID: 340860 [Multi-domain] Cd Length: 365 Bit Score: 55.15 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 401 PLIAFIGRLEEQKGPDVMAAAIPELMQE--DVQIVLLGTGKkkfekLLKSMEEKYPGKVRavVKFNAPLAHL----IMAG 474
Cdd:cd05844 190 PTILFVGRLVEKKGCDVLIEAFRRLAARhpTARLVIAGDGP-----LRPALQALAAALGR--VRFLGALPHAevqdWMRR 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002280373 475 ADVLAVPSRF------EPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKR 546
Cdd:cd05844 263 AEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGF----------LVPEGDVDALADALQA 330
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
389-579 |
3.40e-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: 52.76 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 389 QAEAGLPvDRKIplIAFIGRLEEQKGPDVMAAAIPELMQE--DVQIVLLGTGKKKFEKLLKSMEEK-------YPGKVRA 459
Cdd:cd03821 196 RKHNGLE-DRRI--ILFLGRIHPKKGLDLLIRAARKLAEQgrDWHLVIAGPDDGAYPAFLQLQSSLglgdrvtFTGPLYG 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 460 VVKFNAplahliMAGADVLAVPSRFEPCGLIQLQGMRYGTPcacastgglvdTVIEGKTGFHMGRlSVDCKVVEPSDVKK 539
Cdd:cd03821 273 EAKWAL------YASADLFVLPSYSENFGNVVAEALACGLP-----------VVITDKCGLSELV-EAGCGVVVDPNVSS 334
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1002280373 540 VAATLKRAIKVVGTP-AYEEMVRNC--MNQDLSWKGPAKNWEN 579
Cdd:cd03821 335 LAEALAEALRDPADRkRLGEMARRArqVEENFSWEAVAGQLGE 377
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
401-545 |
8.50e-07 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 51.64 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 401 PLIAFIGRLEEQKGPDvmaaAIPELMQE--DVQIVLLGTG--KKKFEKLLKSMEEKYPGKVRAVVKFNAplahliMAGAD 476
Cdd:PLN02871 264 PLIVYVGRLGAEKNLD----FLKRVMERlpGARLAFVGDGpyREELEKMFAGTPTVFTGMLQGDELSQA------YASGD 333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002280373 477 VLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTV---IEGKTGFhmgrlsvdckVVEPSDVKKVAATLK 545
Cdd:PLN02871 334 VFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGF----------LYTPGDVDDCVEKLE 395
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
315-549 |
3.69e-06 |
|
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
Pssm-ID: 340825 [Multi-domain] Cd Length: 391 Bit Score: 49.65 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 315 ADRVLTVSPYYAEELisgIARGCELDNImrltgitgIV--NGMDVSEWDPSKDKYITAKYdattaieakalnkealqaea 392
Cdd:cd03794 164 ADAIIVLSPGLKEYL---LRKGVPKEKI--------IVipNWADLEEFKPPPKDELRKKL-------------------- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 393 gLPVDRKIplIAFIGRLEEQKGPDVMAAAIPEL-MQEDVQIVLLGTGKKKfeKLLKSMEEKypgKVRAVVKFNAPLAH-- 469
Cdd:cd03794 213 -GLDDKFV--VVYAGNIGKAQGLETLLEAAERLkRRPDIRFLFVGDGDEK--ERLKELAKA---RGLDNVTFLGRVPKee 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 470 --LIMAGADVLAVPSRFEPCGL----IQLQG-MRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAA 542
Cdd:cd03794 285 vpELLSAADVGLVPLKDNPANRgsspSKLFEyMAAGKPILASDDGGSDLAVEINGCGL----------VVEPGDPEALAD 354
|
....*..
gi 1002280373 543 TLKRAIK 549
Cdd:cd03794 355 AILELLD 361
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
351-548 |
2.69e-05 |
|
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: 46.54 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 351 IVNGMDVSEWDPSKDKYITAKydattaieakalnkealqAEAGLPVDRKIplIAFIGRLEEQKGPDVMAAAIPELMQEDV 430
Cdd:cd03807 161 IYNGIDLFKLSPDDASRARAR------------------RRLGLAEDRRV--IGIVGRLHPVKDHSDLLRAAALLVETHP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 431 QIVLLGTGKKKFEKLLKSMEEKYpgKVRAVVKFNAPLAHL--IMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGG 508
Cdd:cd03807 221 DLRLLLVGRGPERPNLERLLLEL--GLEDRVHLLGERSDVpaLLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGG 298
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002280373 509 LVDTVIEGkTGFhmgrlsvdckVVEPSDVkkvaATLKRAI 548
Cdd:cd03807 299 AAELVDDG-TGF----------LVPAGDP----QALADAI 323
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
311-566 |
1.16e-04 |
|
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: 44.65 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 311 GILEADRVLTVSPYYAEELISGIargcELDNimrltGITGIVNGMDVSEWdpskdkyitakydattaieaKALNKEALQA 390
Cdd:cd04962 138 SINKSDRVTAVSSSLRQETYELF----DVDK-----DIEVIHNFIDEDVF--------------------KRKPAGALKR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 391 EAGLPVDRKIplIAFIGRLEEQKGPDVMAAAIPELMQE-DVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNaPLAH 469
Cdd:cd04962 189 RLLAPPDEKV--VIHVSNFRPVKRIDDVVRVFARVRRKiPAKLLLVGDGPERVPAEELARELGVEDRVLFLGKQD-DVEE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 470 LIMAgADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAatlKRAIK 549
Cdd:cd04962 266 LLSI-ADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGF----------LSDVGDVDAMA---KSALS 331
|
250
....*....|....*...
gi 1002280373 550 VVGTPA-YEEMVRNCMNQ 566
Cdd:cd04962 332 ILEDDElYNRMGRAARKR 349
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
351-546 |
1.20e-04 |
|
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: 44.63 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 351 IVNGMDVSEWDPskdkyitakydattaieakaLNKEALQAEAGLPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQ-ED 429
Cdd:cd03825 166 IPNGIDTEIFAP--------------------VDKAKARKRLGIPQDKKVILFGAESVTKPRKGFDELIEALKLLATkDD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 430 VQIVLLGTGKKKFEKLlksmeekyPGKVRAVVKF-NAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGG 508
Cdd:cd03825 226 LLLVVFGKNDPQIVIL--------PFDIISLGYIdDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGG 297
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002280373 509 LVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKR 546
Cdd:cd03825 298 SPEIVQHGVTGY----------LVPPGDVQALAEAIEW 325
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
395-520 |
8.40e-04 |
|
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.
Pssm-ID: 340832 [Multi-domain] Cd Length: 333 Bit Score: 41.89 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 395 PVDRKIPLIAFIGRLEEQKGPDVmAAAIPElmQEDVQIVLLGTGKKK--FEKLlksmEEKYPGkvrAVVKFNAPLAHL-- 470
Cdd:cd03802 164 FQPDPEDYLAFLGRIAPEKGLED-AIRVAR--RAGLPLKIAGKVRDEdyFYYL----QEPLPG---PRIEFIGEVGHDek 233
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1002280373 471 --IMAGADVLAVPSRF-EPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGF 520
Cdd:cd03802 234 qeLLGGARALLFPINWdEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGF 286
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
402-501 |
1.02e-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: 41.51 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 402 LIAFIGRLEEQKGPDVMAAAIPEL--MQEDVQIVLLGTG----KKKFEKLLKSMEEKypgkvravVKF---NAPLAHLIM 472
Cdd:cd03812 193 VLGHVGRFNEQKNHSFLIDIFEELkkKNPNVKLVLVGEGelkeKIKEKVKELGLEDK--------VIFlgfRNDVSEILS 264
|
90 100
....*....|....*....|....*....
gi 1002280373 473 AgADVLAVPSRFEPCGLIQLQGMRYGTPC 501
Cdd:cd03812 265 A-MDVFLFPSLYEGLPLVAVEAQASGLPC 292
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
394-529 |
2.70e-03 |
|
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: 40.35 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280373 394 LPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELmqeDVQIVLLGTGKKkfEKLLKSMEE---KYPGKVRAVVKfnapLAHL 470
Cdd:cd03804 193 APAADKEDYYLTASRLVPYKRIDLAVEAFNEL---PKRLVVIGDGPD--LDRLRAMASpnvEFLGYQPDEVL----KELL 263
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002280373 471 IMAGADVLAVPSRFepcGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFHMGRLSVDC 529
Cdd:cd03804 264 SKARAFVFAAEEDF---GIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVES 319
|
|
| |
