|
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 ... |
84-582 |
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: 553.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 84 NVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYDQYKDAWDTSVVA---EIKVADRYERVRFFHCYKRGV 160
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVlglEVKVGGRGEEVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 161 DRVFIDHPSFLEKVWGKtgekiygPDTGVDYKDNQMRFSLLCQAALEAPRILnlnnnpyfkgtYGEDVVFVCNDWHTGPL 240
Cdd:cd03791 81 DYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRL-----------GFQPDIIHANDWHTALV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 241 ASYLKNNYQPNGiYRNAKVAFCIHNISYQGRFAFEDYPELNLSErfrsSFDFIDGYEYDTpvegrKINWMKAGILEADRV 320
Cdd:cd03791 143 PAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPP----ELFHIDGLEFYG-----QINFLKAGIVYADRV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 321 LTVSPYYAEELISGiARGCELDNI--MRLTGITGIVNGMDVSEWDPSKDKYITAKYDATTaIEAKALNKEALQAEAGLPV 398
Cdd:cd03791 213 TTVSPTYAKEILTP-EYGEGLDGVlrARAGKLSGILNGIDYDEWNPATDKLIPANYSAND-LEGKAENKAALQKELGLPV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 399 DRKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHLIMAGAD 478
Cdd:cd03791 291 DPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGAD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 479 VLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEG------KTGFhmgrlsvdckVVEPSDVKKVAATLKRAIKV 552
Cdd:cd03791 371 FFLMPSRFEPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYdpetgeGTGF----------VFEDYDAEALLAALRRALAL 440
|
490 500 510
....*....|....*....|....*....|.
gi 1002280365 553 VGTP-AYEEMVRNCMNQDLSWKGPAKNWENV 582
Cdd:cd03791 441 YRNPeLWRKLQKNAMKQDFSWDKSAKEYLEL 471
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
83-586 |
2.13e-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: 490.62 E-value: 2.13e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 83 MNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYDQYKDAW----DTSVVAEIKVADRYERVRFFHCYKR 158
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVddqvKVVELVDLSVGPRTLYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 159 GVDRVFIDHPSFLEKvwgktGEKIYGPDtgvdYKDNQMRFSLLCQAALEAPRILNlnnnpyfkgtYGEDVVfVCNDWHTG 238
Cdd:TIGR02095 81 GVPVYFIDNPSLFDR-----PGGIYGDD----YPDNAERFAFFSRAAAELLSGLG----------WQPDVV-HAHDWHTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 239 PLASYLKNNYQPNgiyrNAKVAFCIHNISYQGRFAFEDYPELNLSERFRSSFDFidgyEYDTpvegrKINWMKAGILEAD 318
Cdd:TIGR02095 141 LVPALLKAVYRPN----PIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGL----EFYG-----RVNFLKGGIVYAD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 319 RVLTVSPYYAEELISGiARGCELDNIMRLTG--ITGIVNGMDVSEWDPSKDKYITAKYDATTAiEAKALNKEALQAEAGL 396
Cdd:TIGR02095 208 RVTTVSPTYAREILTP-EFGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 397 PVDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHLIMAG 476
Cdd:TIGR02095 286 PVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 477 ADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGK------TGFHmgrlsvdckvVEPSDVKKVAATLKRAI 550
Cdd:TIGR02095 366 ADFILMPSRFEPCGLTQLYAMRYGTVPIVRRTGGLADTVVDGDpeaesgTGFL----------FEEYDPGALLAALSRAL 435
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1002280365 551 KvvgtpAY-------EEMVRNCMNQDLSWKGPAKNWENVLLGL 586
Cdd:TIGR02095 436 R-----LYrqdpslwEALQKNAMSQDFSWDKSAKQYVELYRSL 473
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
83-582 |
5.44e-161 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 469.19 E-value: 5.44e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 83 MNVVFVGAEMAPWSKTgglgdvlgglPPAMAANGHRVMVISPRYDQYKDAW-DTSVVAEIKV--ADRYERVRFFHCYKRG 159
Cdd:COG0297 1 MKILFVASEAAPFAKTggladvvgalPKALAKLGHDVRVVLPGYPSIDDKLkDLEVVASLEVplGGRTYYARVLEGPDDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 160 VDRVFIDHPSFLEkvwgktGEKIYGpDTGVDYKDNQMRFSLLCQAALEAprILNLNNNPyfkgtygeDVVFvCNDWHTGP 239
Cdd:COG0297 81 VPVYFIDNPELFD------RPGPYG-DPDRDYPDNAERFAFFSRAALEL--LKGLDWKP--------DIIH-CHDWQTGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 240 LASYLKNNYQPNGiYRNAKVAFCIHNISYQGRFAFEDYPELNLSErfrsSFDFIDGYEYDtpveGrKINWMKAGILEADR 319
Cdd:COG0297 143 IPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPP----ELFTPDGLEFY----G-QINFLKAGIVYADR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 320 VLTVSPYYAEELISGIArGCELDNIMRLTG--ITGIVNGMDVSEWDPSKDKYITAKYDATTaIEAKALNKEALQAEAGLP 397
Cdd:COG0297 213 VTTVSPTYAREIQTPEF-GEGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD-LEGKAANKAALQEELGLP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 398 VDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHLIMAGA 477
Cdd:COG0297 291 VDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 478 DVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVI------EGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIK 551
Cdd:COG0297 371 DFFLMPSRFEPCGLNQMYALRYGTVPIVRRTGGLADTVIdyneatGEGTGF----------VFDEYTAEALLAAIRRALA 440
|
490 500 510
....*....|....*....|....*....|..
gi 1002280365 552 VVGTP-AYEEMVRNCMNQDLSWKGPAKNWENV 582
Cdd:COG0297 441 LYRDPeAWRKLQRNAMKQDFSWEKSAKEYLEL 472
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
83-577 |
1.81e-141 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 418.75 E-value: 1.81e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 83 MNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYDQYKDA-WDTSVVAEIKVAdryeRVRFFHCYKRGVD 161
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKlRDAQVVGRLDLF----TVLFGHLEGDGVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 162 RVFIDHPSFlekvwgktgekiYGPDTGVDYKDNQMRFSLLCQAALEAprILNLNNNPyfkgtygeDVVFvCNDWHTGPLA 241
Cdd:PRK00654 77 VYLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEF--AEGLDPRP--------DIVH-AHDWHTGLIP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 242 SYLKNNYQPNgiYRNAKVAFCIHNISYQGRFAFEDYPELNL-SERFRssfdfIDGYEYDTpvegrKINWMKAGILEADRV 320
Cdd:PRK00654 134 ALLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLpAEAFH-----LEGLEFYG-----QISFLKAGLYYADRV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 321 LTVSPYYAEELISGiARGCELDNIMRLTG--ITGIVNGMDVSEWDPSKDKYITAKYDATTaIEAKALNKEALQAEAGLPV 398
Cdd:PRK00654 202 TTVSPTYAREITTP-EFGYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENKRALQERFGLPD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 399 DrKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHLIMAGAD 478
Cdd:PRK00654 280 D-DAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGAD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 479 VLAVPSRFEPCGLIQLQGMRYGT-PCAcASTGGLVDTVI------EGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIK 551
Cdd:PRK00654 359 MFLMPSRFEPCGLTQLYALRYGTlPIV-RRTGGLADTVIdynpedGEATGF----------VFDDFNAEDLLRALRRALE 427
|
490 500
....*....|....*....|....*..
gi 1002280365 552 VVGTPA-YEEMVRNCMNQDLSWKGPAK 577
Cdd:PRK00654 428 LYRQPPlWRALQRQAMAQDFSWDKSAE 454
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
83-579 |
6.02e-89 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 284.30 E-value: 6.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 83 MNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYdqykdawdTSVVAEIKVADRYERVR-FFHCYKR--- 158
Cdd:PRK14099 4 LRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGY--------PAVLAGIEDAEQVHSFPdLFGGPARlla 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 159 ----GVDRVFIDHPsfleKVWGKTGEKIYGPDtGVDYKDNQMRFSLLCQAALEapriLNLNNNPYFKgtygEDVVFVcND 234
Cdd:PRK14099 76 aragGLDLFVLDAP----HLYDRPGNPYVGPD-GKDWPDNAQRFAALARAAAA----IGQGLVPGFV----PDIVHA-HD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 235 WHTGPLASYLKNNYQPNgiyrnAKVAFCIHNISYQGRFAFEDYPELNLSERfrsSFDfIDGYEYDTpvegrKINWMKAGI 314
Cdd:PRK14099 142 WQAGLAPAYLHYSGRPA-----PGTVFTIHNLAFQGQFPRELLGALGLPPS---AFS-LDGVEYYG-----GIGYLKAGL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 315 LEADRVLTVSPYYAEElISGIARGCELDNIMRLTG--ITGIVNGMDVSEWDPSKDKYITAKYDATTaIEAKALNKEALQA 392
Cdd:PRK14099 208 QLADRITTVSPTYALE-IQGPEAGMGLDGLLRQRAdrLSGILNGIDTAVWNPATDELIAATYDVET-LAARAANKAALQA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 393 EAGLPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHL 472
Cdd:PRK14099 286 RFGLDPDPDALLLGVISRLSWQKGLDLLLEALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 473 IMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGK---------TGFHMGRLSVDCkvvepsdvkkVA 543
Cdd:PRK14099 366 IQAGADALLVPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVDANemaiatgvaTGVQFSPVTADA----------LA 435
|
490 500 510
....*....|....*....|....*....|....*..
gi 1002280365 544 ATLKRAIKVVGTPA-YEEMVRNCMNQDLSWKGPAKNW 579
Cdd:PRK14099 436 AALRKTAALFADPVaWRRLQRNGMTTDVSWRNPAQHY 472
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
85-346 |
2.53e-68 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 221.82 E-value: 2.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 85 VVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYD-------QYKDAWDTSVVAEIKVadRYERVRFFHCYK 157
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGnipeernQLEDVIRLSVAAGVPV--RPLTVGVARLEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 158 RGVDRVFIDHPSFLEKvwgktgEKIYGpDTGVDYKDNQMRFSLLCQAALEAPRILNlnnnpyfkgtYGEDVVfVCNDWHT 237
Cdd:pfam08323 79 DGVDVYFLDNPDYFDR------PGLYG-DDGRDYEDNAERFAFFSRAALELAKKLG----------WIPDII-HCHDWHT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 238 GPLASYLKNNYQPNGiYRNAKVAFCIHNISYQGRFAFEDYPELNLSERFRSsfdfIDGYEYDTpvegrKINWMKAGILEA 317
Cdd:pfam08323 141 ALVPAYLKEAYADDP-FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN----LDGLEFYG-----QINFLKAGIVYA 210
|
250 260
....*....|....*....|....*....
gi 1002280365 318 DRVLTVSPYYAEELISGiARGCELDNIMR 346
Cdd:pfam08323 211 DAVTTVSPTYAEEIQTP-EFGGGLDGLLR 238
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
232-579 |
2.63e-66 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 224.61 E-value: 2.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 232 CNDWHTGPLASYLKNNYQPNGIYRNAKVAFCIHNISYQGRFAFEDYPELnLSErfrssfDFIDGYEydtpVEGRKINWMK 311
Cdd:PRK14098 147 CHDWYAGLVPLLLKTVYADHEFFKDIKTVLTIHNVYRQGVLPFKVFQKL-LPE------EVCSGLH----REGDEVNMLY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 312 AGILEADRVLTVSPYYAEELISGIARGCELDNIM--RLTGITGIVNGMDVSEWDPSKDKYITAKYDATTaIEAKALNKEA 389
Cdd:PRK14098 216 TGVEHADLLTTTSPRYAEEIAGDGEEAFGLDKVLeeRKMRLHGILNGIDTRQWNPSTDKLIKKRYSIER-LDGKLENKKA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 390 LQAEAGLPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPL 469
Cdd:PRK14098 295 LLEEVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAF 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 470 AHLIMAGADVLAVPSRFEPCGLIQLQGMRYGT-PCACAsTGGLVDTVIE----GKTGFhmgrlsvdckVVEPSDVKKVAA 544
Cdd:PRK14098 375 FHLAIAGLDMLLMPGKIESCGMLQMFAMSYGTiPVAYA-GGGIVETIEEvsedKGSGF----------IFHDYTPEALVA 443
|
330 340 350
....*....|....*....|....*....|....*.
gi 1002280365 545 TLKRAIKVVG-TPAYEEMVRNCMNQDLSWKGPAKNW 579
Cdd:PRK14098 444 KLGEALALYHdEERWEELVLEAMERDFSWKNSAEEY 479
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
83-576 |
1.36e-52 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 194.70 E-value: 1.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 83 MNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYD----------QYKDA--WDTSvvaEIKVAdrYERV 150
Cdd:PLN02316 588 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDclnlshvkdlHYQRSysWGGT---EIKVW--FGKV 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 151 RFFHCYkrgvdrvfidhpsFLEKVWGKTGEK-IYGPdtgvdyKDNQMRFSLLCQAALEAprILNLNNNPyfkgtygeDVV 229
Cdd:PLN02316 663 EGLSVY-------------FLEPQNGMFWAGcVYGC------RNDGERFGFFCHAALEF--LLQSGFHP--------DII 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 230 FvCNDWHTGPLASYLKNNYQPNGIyRNAKVAFCIHNIsyqgrfafedypelnlserfrssfdfidgyEYDTPVEGRKINW 309
Cdd:PLN02316 714 H-CHDWSSAPVAWLFKDHYAHYGL-SKARVVFTIHNL------------------------------EFGANHIGKAMAY 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 310 mkagileADRVLTVSPYYAEElISG---IARgceldnimRLTGITGIVNGMDVSEWDPSKDKYITAKYDATTAIEAKALN 386
Cdd:PLN02316 762 -------ADKATTVSPTYSRE-VSGnsaIAP--------HLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAA 825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 387 KEALQAEAGL-PVDrkIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTG-----KKKFEKLLKSMEEKYPGKVR 460
Cdd:PLN02316 826 KEALQQRLGLkQAD--LPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGSApdpriQNDFVNLANQLHSSHHDRAR 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 461 AVVKFNAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEgktgfhmgrlsVD-------CKV 533
Cdd:PLN02316 904 LCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTVFD-----------VDhdkeraqAQG 972
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1002280365 534 VEP-------SDVKKVAATLKRAIKVV--GTPAYEEMVRNCMNQDLSWKGPA 576
Cdd:PLN02316 973 LEPngfsfdgADAAGVDYALNRAISAWydGRDWFNSLCKRVMEQDWSWNRPA 1024
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
70-582 |
2.20e-50 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 187.80 E-value: 2.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 70 RFPSVVVYATGAGMNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYD--QYKDawdtsvVAEIKVADRy 147
Cdd:PLN02939 469 NFLKLTLSGTSSGLHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDcmQYDQ------IRNLKVLDV- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 148 ervrffhcykrgVDRVFIDHPSFLEKVWGKTGE-------------KIYGPDTGVDYKDNQMRFSLLCQAALEAprILNL 214
Cdd:PLN02939 542 ------------VVESYFDGNLFKNKIWTGTVEglpvyfiepqhpsKFFWRAQYYGEHDDFKRFSYFSRAALEL--LYQS 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 215 NNNPyfkgtygeDVVFvCNDWHTGPLASYLKNNYQPNGiYRNAKVAFCIHNISYQGRFAFE-------DYPELNLSERFR 287
Cdd:PLN02939 608 GKKP--------DIIH-CHDWQTAFVAPLYWDLYAPKG-FNSARICFTCHNFEYQGTAPASdlascglDVHQLDRPDRMQ 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 288 SSfdfidgyeydtpvEGRKINWMKAGILEADRVLTVSPYYAEELISGIARGCELDNIMRLTGITGIVNGMDVSEWDPSKD 367
Cdd:PLN02939 678 DN-------------AHGRINVVKGAIVYSNIVTTVSPTYAQEVRSEGGRGLQDTLKFHSKKFVGILNGIDTDTWNPSTD 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 368 KYITAKYDATTaIEAKALNKEALQAEAGLP-VDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTG-----K 441
Cdd:PLN02939 745 RFLKVQYNAND-LQGKAANKAALRKQLGLSsADASQPLVGCITRLVPQKGVHLIRHAIYKTAELGGQFVLLGSSpvphiQ 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 442 KKFEKLLKSMEEKypGKVRAVVKFNAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTV------ 515
Cdd:PLN02939 824 REFEGIADQFQSN--NNIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSVfdfdde 901
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002280365 516 ---IEGKTGFHMGRlsvdckvvepSDVKKVAATLKRAIKVV--GTPAYEEMVRNCMNQDLSWKGPAKNWENV 582
Cdd:PLN02939 902 tipVELRNGFTFLT----------PDEQGLNSALERAFNYYkrKPEVWKQLVQKDMNIDFSWDSSASQYEEL 963
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
197-583 |
4.14e-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: 101.46 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 197 RFSLLCQAALEAPRILNLNNNPYFKGTYgeDVVfVCNDWHTGPLASYLKnnyqpngIYRNAKVAFCIHNISYQGRFAFED 276
Cdd:cd03801 56 PLLPSLAALLRARRLLRELRPLLRLRKF--DVV-HAHGLLAALLAALLA-------LLLGAPLVVTLHGAEPGRLLLLLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 277 YPElnlserfrssfdfidgyeydtpvegRKINWMKAGILEADRVLTVSPYYAEELISgiargcelDNIMRLTGITGIVNG 356
Cdd:cd03801 126 AER-------------------------RLLARAEALLRRADAVIAVSEALRDELRA--------LGGIPPEKIVVIPNG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 357 MDVSEWDPskdkyitakydattaieakalnkeALQAEAGLPVDRkiPLIAFIGRLEEQKGPDVMAAAIPELMQE--DVQI 434
Cdd:cd03801 173 VDLERFSP------------------------PLRRKLGIPPDR--PVLLFVGRLSPRKGVDLLLEALAKLLRRgpDVRL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 435 VLLGTGKKKFEKLlKSMEEKYPGKVRAVVKFNAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDT 514
Cdd:cd03801 227 VIVGGDGPLRAEL-EELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEV 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002280365 515 VIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIKvvGTPAYEEMVRN---CMNQDLSWKGPAKNWENVL 583
Cdd:cd03801 306 VEDGEGGL----------VVPPDDVEALADALLRLLA--DPELRARLGRAareRVAERFSWERVAERLLDLY 365
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
403-551 |
3.52e-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: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 403 PLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHLI--MAGADVL 480
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPelLKIADVF 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002280365 481 AVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIK 551
Cdd:pfam00534 83 VLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGF----------LVKPNNAEALAEAIDKLLE 143
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
403-551 |
3.16e-18 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 81.40 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 403 PLIAFIGRL-EEQKGPDVMAAAIPELMQE--DVQIVLLGTGK-KKFEKLLKSMEEK--YPGKVRAVVKFnaplahliMAG 476
Cdd:pfam13692 2 PVILFVGRLhPNVKGVDYLLEAVPLLRKRdnDVRLVIVGDGPeEELEELAAGLEDRviFTGFVEDLAEL--------LAA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002280365 477 ADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDtVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIK 551
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 ... |
387-551 |
1.49e-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: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 387 KEALQAEAGLPVDRKIplIAFIGRLEEQKGPDVMAAA---IPELmQEDVQIVLLGTG-----------KKKFEKLLKSME 452
Cdd:cd03800 207 AEARRARLLLPPDKPV--VLALGRLDPRKGIDTLVRAfaqLPEL-RELANLVLVGGPsddplsmdreeLAELAEELGLID 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 453 E-KYPGKVRAVVkfnapLAHLIMAgADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFHmgrlsvdc 531
Cdd:cd03800 284 RvRFPGRVSRDD-----LPELYRA-ADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLL-------- 349
|
170 180
....*....|....*....|
gi 1002280365 532 kvVEPSDVKKVAATLKRAIK 551
Cdd:cd03800 350 --VDPHDPEALAAALRRLLD 367
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
316-550 |
1.01e-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: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 316 EADRVLTVSPYYAEELIS-GIARGceldnimrltGITGIVNGMDVSEWDPSkdkyitakydattaieakalnkealQAEA 394
Cdd:cd03798 150 RAARVIAVSKALAEELVAlGVPRD----------RVDVIPNGVDPARFQPE-------------------------DRGL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 395 GLPVDRkiPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLL--GTG--KKKFEKLLKSmeekypGKVRAVVKFNAPLA 470
Cdd:cd03798 195 GLPLDA--FVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLivGDGplREALRALAED------LGLGDRVTFTGRLP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 471 H----LIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATL 546
Cdd:cd03798 267 HeqvpAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGL----------LVPPGDADALAAAL 336
|
....
gi 1002280365 547 KRAI 550
Cdd:cd03798 337 RRAL 340
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
407-522 |
2.62e-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: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 407 FIGRLEEQKGPDVMAAAIPELMQE--DVQIVLLGTGKKKfEKLLKSMEEKYPGKVRAVVKF--NAPLAHLIMAGADVLAV 482
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLKARlpDLVLVLVGGGGER-EEEEALAAALGLLERVVIIGGlvDDEVLELLLAAADVFVL 193
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1002280365 483 PSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGF 522
Cdd:cd01635 194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
469-586 |
6.30e-12 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 62.70 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 469 LAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKR 548
Cdd:COG0438 13 LLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGL----------LVPPGDPEALAEAILR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1002280365 549 AIKvvGTPAYEEMVRNC---MNQDLSWKGPAKNWENVLLGL 586
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 ... |
299-563 |
1.21e-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: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 299 DTPVEGRKINWMKAGILEADRVLTVSPYYAEELISGIARGCELdnimrltgITGIVNGMDvsewdpskdkyiTAKYDATT 378
Cdd:cd03819 109 SYLATYHPKDFALAVRARGDRVIAVSELVRDHLIEALGVDPER--------IRVIPNGVD------------TDRFPPEA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 379 AIEAKAlnkealqaeaGLPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELmQEDVQIVLLGTGKKKFEKLLKSMEEKYPGK 458
Cdd:cd03819 169 EAEERA----------QLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAGDGPERDEIRRLVERLGLR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 459 VRAVVKFNAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrLSVDCKVVEPSD 538
Cdd:cd03819 238 DRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGL----LVPPGDAEALAD 313
|
250 260
....*....|....*....|....*.
gi 1002280365 539 VKK-VAATLKRAIKVVGTPAYEEMVR 563
Cdd:cd03819 314 AIRaAKLLPEAREKLQAAAALTEAVR 339
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
405-550 |
5.75e-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: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 405 IAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEE-KYPGKVRavvkfNAPLAHLiMAGADVLAVP 483
Cdd:cd03823 194 FGYIGRLTEEKGIDLLVEAFKRLPREDIELVIAGHGPLSDERQIEGGRRiAFLGRVP-----TDDIKDF-YEKIDVLVVP 267
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002280365 484 SRF-EPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFHmgrlsvdckvVEPSDVKKVAATLKRAI 550
Cdd:cd03823 268 SIWpEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLL----------FAPGDAEDLAAAMRRLL 325
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
386-583 |
7.92e-11 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 64.04 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 386 NKEALQAEAGLPVDRKIplIAFIGRLEEQKGPDVMAAAIPELM--QEDVQIVLLG--TGKKKFEKllksmeEKYPGKVRA 461
Cdd:PRK15484 179 PQPNLRQQLNISPDETV--LLYAGRISPDKGILLLMQAFEKLAtaHSNLKLVVVGdpTASSKGEK------AAYQKKVLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 462 VVKfnAPLAHLIMAG-------------ADVLAVPSRF-EPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFHMGrl 527
Cdd:PRK15484 251 AAK--RIGDRCIMLGgqppekmhnyyplADLVVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLA-- 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002280365 528 svdckvvEPSDVKKVAATLKRAIKVVGTPAYEEMVRNCMNQDLSWKGPAKNWENVL 583
Cdd:PRK15484 327 -------EPMTSDSIISDINRTLADPELTQIAEQAKDFVFSKYSWEGVTQRFEEQI 375
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
305-551 |
2.65e-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: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 305 RKINWMKAGILE------ADRVLTVSPYYAEELISgiARGCELDNIMRLTGitgivNGMDVSEWDPSKDKYITAKydatt 378
Cdd:cd03808 122 GKLLRLLYLLLEklallfTDKVIFVNEDDRDLAIK--KGIIKKKKTVLIPG-----SGVDLDRFQYSPESLPSEK----- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 379 aieakalnkealqaeaglpvdrkiPLIAFIGRLEEQKGPD--VMAAAIPELMQEDVQIVLLGTG------KKKFEKLLKS 450
Cdd:cd03808 190 ------------------------VVFLFVARLLKDKGIDelIEAAKILKKKGPNVRFLLVGDGelenpsEILIEKLGLE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 451 MEEKYPGKVRAVVKFnaplahliMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvd 530
Cdd:cd03808 246 GRIEFLGFRSDVPEL--------LAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGF-------- 309
|
250 260
....*....|....*....|.
gi 1002280365 531 ckVVEPSDVKKVAATLKRAIK 551
Cdd:cd03808 310 --LVPPGDVEALADAIEKLIE 328
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
405-551 |
5.55e-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: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 405 IAFIGRLEEQKGPDVM--AAAIPELMQEDVQIVLLGTG--KKKFEKLLKS--MEE--KYPGKVRAVvkfnaplaHLIMAG 476
Cdd:cd03820 184 ILAVGRLTYQKGFDLLieAWALIAKKHPDWKLRIYGDGpeREELEKLIDKlgLEDrvKLLGPTKNI--------AEEYAN 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002280365 477 ADVLAVPSRFEPCGLIQLQGMRYGTPCAC-ASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIK 551
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 ... |
305-522 |
3.68e-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: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 305 RKINWMKAGILEADRVLTVSPYYAEELIS-GIARGCELDNIMrltgitgivNGMDVSEwdpskdkyitakydattaieAK 383
Cdd:cd03811 124 KKLLLKLKLYKKADKIVCVSKGIKEDLIRlGPSPPEKIEVIY---------NPIDIDR--------------------IR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 384 ALNKEALQAEaglpvDRKIPLIAFIGRLEEQKGPDVM--AAAIPELMQEDVQIVLLGTGKKKfEKLLKSMEE-------K 454
Cdd:cd03811 175 ALAKEPILNE-----PEDGPVILAVGRLDPQKGHDLLieAFAKLRKKYPDVKLVILGDGPLR-EELEKLAKElglaervI 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002280365 455 YPGKVRAVVKFnaplahliMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGF 522
Cdd:cd03811 249 FLGFQSNPYPY--------LKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGL 308
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
255-509 |
8.59e-09 |
|
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: 57.76 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 255 RNAKVAFCIHNisyqgrFAFEDYPELnlserfrSSFDFIDGYEYdtpvegrkinWMKAGILEADRVLTVSPYYAEELIsg 334
Cdd:cd03809 100 KGCPQVVTIHD------LIPLRYPEF-------FPKRFRLYYRL----------LLPISLRRADAIITVSEATRDDII-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 335 iargceldnimRLTGItgivngmdvsewdpSKDKYITAkYDATTAIEAKALNKEALQAEAGLPVdrkiPLIAFIGRLEEQ 414
Cdd:cd03809 155 -----------KFYGV--------------PPEKIVVI-PLGVDPSFFPPESAAVLIAKYLLPE----PYFLYVGTLEPR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 415 KGPDVMAAA---IPELMQeDVQIVLLGTGKKKFEKLLKSMEEKY-PGKVRAVVKFNAP-LAHLImAGADVLAVPSRFEPC 489
Cdd:cd03809 205 KNHERLLKAfalLKKQGG-DLKLVIVGGKGWEDEELLDLVKKLGlGGRVRFLGYVSDEdLPALY-RGARAFVFPSLYEGF 282
|
250 260
....*....|....*....|
gi 1002280365 490 GLIQLQGMRYGTPCACASTG 509
Cdd:cd03809 283 GLPVLEAMACGTPVIASNIS 302
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
403-565 |
1.62e-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: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 403 PLIAFIGRLEEQKGPDVMAAAIPELmqeDVQIVLLGTGKKKfEKLLKSMEEKYPGKVRAVVKF-NAPLAHLIMAgADVLA 481
Cdd:cd03795 192 KIFLFIGRLVYYKGLDYLIEAAQYL---NYPIVIGGEGPLK-PDLEAQIELNLLDNVKFLGRVdDEEKVIYLHL-CDVFV 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 482 VPS--RFEPCGLIQLQGMRYGTP-CACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKRAIKvvGTPAY 558
Cdd:cd03795 267 FPSvlRSEAFGIVLLEAMMCGKPvISTNIGTGVPYVNNNGETGL----------VVPPKDPDALAEAIDKLLS--DEELR 334
|
....*..
gi 1002280365 559 EEMVRNC 565
Cdd:cd03795 335 ESYGENA 341
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
301-565 |
2.89e-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: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 301 PVEGRKINWMKAGILEADRVLTVSPYYAEELIsgiARGCEldNIMRLTgitgivNGMDVSEWDPS-KDKyitakydatta 379
Cdd:cd03814 130 PLSWLAWAYLRWFHNPFDTTLVPSPSIARELE---GHGFE--RVRLWP------RGVDTELFHPSrRDA----------- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 380 ieakALNKEALQAEAglpvdrkiPLIAFIGRLEEQKGPDVMAAAIPELMQED-VQIVLLGTGKKKfekllKSMEEKYPGK 458
Cdd:cd03814 188 ----ALRRRLGPPGR--------PLLLYVGRLAPEKNLEALLDADLPLAASPpVRLVVVGDGPAR-----AELEARGPDV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 459 VRAVVKFNAPLAHlIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSD 538
Cdd:cd03814 251 IFTGFLTGEELAR-AYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGA----------LVEPGD 319
|
250 260 270
....*....|....*....|....*....|...
gi 1002280365 539 VKKVAATL------KRAIKVVGTPAYEEMVRNC 565
Cdd:cd03814 320 AAAFAAALralledPELRRRMAARARAEAERYS 352
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
383-523 |
5.33e-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: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 383 KALNKEALQaEAGLPVDRKIplIAFIGRLEEQKGPDVMAAAIPEL-MQEDVQIVLLGTG--KKKFEKLLKSMeekypgKV 459
Cdd:cd03817 185 KPLNTEERR-KLGLPPDEPI--LLYVGRLAKEKNIDFLLRAFAELkKEPNIKLVIVGDGpeREELKELAREL------GL 255
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002280365 460 RAVVKFNAPLAH----LIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFH 523
Cdd:cd03817 256 ADKVIFTGFVPReelpEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFL 323
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
403-548 |
5.85e-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: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 403 PLIAFIGRLEEQKGPDVMAAAIPELMQE--DVQIVLLGTGKkkfekLLKSMEEKYPGKVRavVKFNAPLAHL----IMAG 476
Cdd:cd05844 190 PTILFVGRLVEKKGCDVLIEAFRRLAARhpTARLVIAGDGP-----LRPALQALAAALGR--VRFLGALPHAevqdWMRR 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002280365 477 ADVLAVPSRF------EPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKR 548
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 ... |
391-581 |
3.48e-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: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 391 QAEAGLPvDRKIplIAFIGRLEEQKGPDVMAAAIPELMQE--DVQIVLLGTGKKKFEKLLKSMEEK-------YPGKVRA 461
Cdd:cd03821 196 RKHNGLE-DRRI--ILFLGRIHPKKGLDLLIRAARKLAEQgrDWHLVIAGPDDGAYPAFLQLQSSLglgdrvtFTGPLYG 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 462 VVKFNAplahliMAGADVLAVPSRFEPCGLIQLQGMRYGTPcacastgglvdTVIEGKTGFHMGRlSVDCKVVEPSDVKK 541
Cdd:cd03821 273 EAKWAL------YASADLFVLPSYSENFGNVVAEALACGLP-----------VVITDKCGLSELV-EAGCGVVVDPNVSS 334
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1002280365 542 VAATLKRAIKVVGTP-AYEEMVRNC--MNQDLSWKGPAKNWEN 581
Cdd:cd03821 335 LAEALAEALRDPADRkRLGEMARRArqVEENFSWEAVAGQLGE 377
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
403-547 |
8.54e-07 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 51.64 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 403 PLIAFIGRLEEQKGPDvmaaAIPELMQE--DVQIVLLGTG--KKKFEKLLKSMEEKYPGKVRAVVKFNAplahliMAGAD 478
Cdd:PLN02871 264 PLIVYVGRLGAEKNLD----FLKRVMERlpGARLAFVGDGpyREELEKMFAGTPTVFTGMLQGDELSQA------YASGD 333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002280365 479 VLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTV---IEGKTGFhmgrlsvdckVVEPSDVKKVAATLK 547
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 ... |
317-551 |
4.01e-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: 49.26 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 317 ADRVLTVSPYYAEELisgIARGCELDNImrltgitgIV--NGMDVSEWDPSKDKYITAKYdattaieakalnkealqaea 394
Cdd:cd03794 164 ADAIIVLSPGLKEYL---LRKGVPKEKI--------IVipNWADLEEFKPPPKDELRKKL-------------------- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 395 gLPVDRKIplIAFIGRLEEQKGPDVMAAAIPEL-MQEDVQIVLLGTGKKKfeKLLKSMEEKypgKVRAVVKFNAPLAH-- 471
Cdd:cd03794 213 -GLDDKFV--VVYAGNIGKAQGLETLLEAAERLkRRPDIRFLFVGDGDEK--ERLKELAKA---RGLDNVTFLGRVPKee 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 472 --LIMAGADVLAVPSRFEPCGL----IQLQG-MRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAA 544
Cdd:cd03794 285 vpELLSAADVGLVPLKDNPANRgsspSKLFEyMAAGKPILASDDGGSDLAVEINGCGL----------VVEPGDPEALAD 354
|
....*..
gi 1002280365 545 TLKRAIK 551
Cdd:cd03794 355 AILELLD 361
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
353-550 |
2.52e-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: 46.93 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 353 IVNGMDVSEWDPSKDKYITAKydattaieakalnkealqAEAGLPVDRKIplIAFIGRLEEQKGPDVMAAAIPELMQEDV 432
Cdd:cd03807 161 IYNGIDLFKLSPDDASRARAR------------------RRLGLAEDRRV--IGIVGRLHPVKDHSDLLRAAALLVETHP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 433 QIVLLGTGKKKFEKLLKSMEEKYpgKVRAVVKFNAPLAHL--IMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGG 510
Cdd:cd03807 221 DLRLLLVGRGPERPNLERLLLEL--GLEDRVHLLGERSDVpaLLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGG 298
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002280365 511 LVDTVIEGkTGFhmgrlsvdckVVEPSDVkkvaATLKRAI 550
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 ... |
313-568 |
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 1002280365 313 GILEADRVLTVSPYYAEELISGIargcELDNimrltGITGIVNGMDVSEWdpskdkyitakydattaieaKALNKEALQA 392
Cdd:cd04962 138 SINKSDRVTAVSSSLRQETYELF----DVDK-----DIEVIHNFIDEDVF--------------------KRKPAGALKR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 393 EAGLPVDRKIplIAFIGRLEEQKGPDVMAAAIPELMQE-DVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNaPLAH 471
Cdd:cd04962 189 RLLAPPDEKV--VIHVSNFRPVKRIDDVVRVFARVRRKiPAKLLLVGDGPERVPAEELARELGVEDRVLFLGKQD-DVEE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 472 LIMAgADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAatlKRAIK 551
Cdd:cd04962 266 LLSI-ADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGF----------LSDVGDVDAMA---KSALS 331
|
250
....*....|....*...
gi 1002280365 552 VVGTPA-YEEMVRNCMNQ 568
Cdd:cd04962 332 ILEDDElYNRMGRAARKR 349
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
353-548 |
1.21e-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: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 353 IVNGMDVSEWDPskdkyitakydattaieakaLNKEALQAEAGLPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQ-ED 431
Cdd:cd03825 166 IPNGIDTEIFAP--------------------VDKAKARKRLGIPQDKKVILFGAESVTKPRKGFDELIEALKLLATkDD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 432 VQIVLLGTGKKKFEKLlksmeekyPGKVRAVVKF-NAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGG 510
Cdd:cd03825 226 LLLVVFGKNDPQIVIL--------PFDIISLGYIdDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGG 297
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002280365 511 LVDTVIEGKTGFhmgrlsvdckVVEPSDVKKVAATLKR 548
Cdd:cd03825 298 SPEIVQHGVTGY----------LVPPGDVQALAEAIEW 325
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
397-522 |
8.37e-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: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 397 PVDRKIPLIAFIGRLEEQKGPDVmAAAIPElmQEDVQIVLLGTGKKK--FEKLlksmEEKYPGkvrAVVKFNAPLAHL-- 472
Cdd:cd03802 164 FQPDPEDYLAFLGRIAPEKGLED-AIRVAR--RAGLPLKIAGKVRDEdyFYYL----QEPLPG---PRIEFIGEVGHDek 233
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1002280365 473 --IMAGADVLAVPSRF-EPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGF 522
Cdd:cd03802 234 qeLLGGARALLFPINWdEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGF 286
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
404-503 |
1.03e-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: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 404 LIAFIGRLEEQKGPDVMAAAIPEL--MQEDVQIVLLGTG----KKKFEKLLKSMEEKypgkvravVKF---NAPLAHLIM 474
Cdd:cd03812 193 VLGHVGRFNEQKNHSFLIDIFEELkkKNPNVKLVLVGEGelkeKIKEKVKELGLEDK--------VIFlgfRNDVSEILS 264
|
90 100
....*....|....*....|....*....
gi 1002280365 475 AgADVLAVPSRFEPCGLIQLQGMRYGTPC 503
Cdd:cd03812 265 A-MDVFLFPSLYEGLPLVAVEAQASGLPC 292
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
396-531 |
2.81e-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: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280365 396 LPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELmqeDVQIVLLGTGKKkfEKLLKSMEE---KYPGKVRAVVKfnapLAHL 472
Cdd:cd03804 193 APAADKEDYYLTASRLVPYKRIDLAVEAFNEL---PKRLVVIGDGPD--LDRLRAMASpnvEFLGYQPDEVL----KELL 263
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002280365 473 IMAGADVLAVPSRFepcGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFHMGRLSVDC 531
Cdd:cd03804 264 SKARAFVFAAEEDF---GIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVES 319
|
|
| |
