|
Name |
Accession |
Description |
Interval |
E-value |
| glgA |
PRK00654 |
glycogen synthase GlgA; |
45-514 |
0e+00 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 691.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 45 KVLFVTSEIADLVKTGGLGDVSAALPRAMAHL-HDVRLLIPGYRQVMHSENPIHIIGELGGHAALpackIGRMDmPDGLV 123
Cdd:PRK00654 2 KILFVASECAPLIKTGGLGDVVGALPKALAALgHDVRVLLPGYPAIREKLRDAQVVGRLDLFTVL----FGHLE-GDGVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 124 IYVLICPELYEREGtpygannGRDWPDNHIRFARLGLAAADIAAnlaQIHWCPDLVHAHDWPAGLAPAYMH---WRG-QR 199
Cdd:PRK00654 77 VYLIDAPHLFDRPS-------GYGYPDNGERFAFFSWAAAEFAE---GLDPRPDIVHAHDWHTGLIPALLKekyWRGyPD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 200 TPTLFTIHNLAYQGVVSLASCPELGIPEHALQQEGMEFYGKLSFLKAGMAYASHITTVSATYAQEITTPAFGCGLDGFLA 279
Cdd:PRK00654 147 IKTVFTIHNLAYQGLFPAEILGELGLPAEAFHLEGLEFYGQISFLKAGLYYADRVTTVSPTYAREITTPEFGYGLEGLLR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 280 SKTQQglLSGIPNGIDES-WDAATDPHLSTPFAIGDWQGKAANAAHVRQMFGLDPSNGPLFAVVSRLVYQKGLDLTEGVA 358
Cdd:PRK00654 227 ARSGK--LSGILNGIDYDiWNPETDPLLAANYSADDLEGKAENKRALQERFGLPDDDAPLFAMVSRLTEQKGLDLVLEAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 359 EYIVKSGGQIAIIGRGEPEEEQAMRALAARFPGRIGVNIGFNETDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFGSLPV 438
Cdd:PRK00654 305 PELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 439 ARNTGGLADTIENG------VTGFLFDESTVASYEEALSRAFKVFAYPQLLNAMRCRAMAAPFNWCKAVEPYAELYEQLV 512
Cdd:PRK00654 385 VRRTGGLADTVIDYnpedgeATGFVFDDFNAEDLLRALRRALELYRQPPLWRALQRQAMAQDFSWDKSAEEYLELYRRLL 464
|
..
gi 740794015 513 AK 514
Cdd:PRK00654 465 GK 466
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
45-511 |
0e+00 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 627.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 45 KVLFVTSEIADLVKTGGLGDVSAALPRAMAHL-HDVRLLIPGYRQVMHSENPIHIIGELGGHA--ALPACKIGRMDmPDG 121
Cdd:COG0297 2 KILFVASEAAPFAKTGGLADVVGALPKALAKLgHDVRVVLPGYPSIDDKLKDLEVVASLEVPLggRTYYARVLEGP-DDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 122 LVIYVLICPELYEREGtPYGaNNGRDWPDNHIRFARLGLAAADIAAnlaQIHWCPDLVHAHDWPAGLAPAYMHWRGQ--- 198
Cdd:COG0297 81 VPVYFIDNPELFDRPG-PYG-DPDRDYPDNAERFAFFSRAALELLK---GLDWKPDIIHCHDWQTGLIPALLKTRYAddp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 199 --RTPTLFTIHNLAYQGVVSLASCPELGIPEHALQQEGMEFYGKLSFLKAGMAYASHITTVSATYAQEITTPAFGCGLDG 276
Cdd:COG0297 156 fkRIKTVFTIHNLAYQGIFPAEILELLGLPPELFTPDGLEFYGQINFLKAGIVYADRVTTVSPTYAREIQTPEFGEGLDG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 277 FLASKtqQGLLSGIPNGID-ESWDAATDPHLSTPFAIGDWQGKAANAAHVRQMFGLDPS-NGPLFAVVSRLVYQKGLDLT 354
Cdd:COG0297 236 LLRAR--SGKLSGILNGIDyDVWNPATDPYLPANYSADDLEGKAANKAALQEELGLPVDpDAPLIGMVSRLTEQKGLDLL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 355 EGVAEYIVKSGGQIAIIGRGEPEEEQAMRALAARFPGRIGVNIGFNETDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFG 434
Cdd:COG0297 314 LEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 435 SLPVARNTGGLADTIEN------GVTGFLFDESTVASYEEALSRAFKVFAYPQLLNAMRCRAMAAPFNWCKAVEPYAELY 508
Cdd:COG0297 394 TVPIVRRTGGLADTVIDyneatgEGTGFVFDEYTAEALLAAIRRALALYRDPEAWRKLQRNAMKQDFSWEKSAKEYLELY 473
|
...
gi 740794015 509 EQL 511
Cdd:COG0297 474 REL 476
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
45-510 |
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: 576.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 45 KVLFVTSEIADLVKTGGLGDVSAALPRAMAHL-HDVRLLIPGYRQVMHSENPIHIIGELGGHAALPACKIGRMDMP-DGL 122
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLgHDVRVILPRYGQIPDELDGYLRVLGLEVKVGGRGEEVGVFELPvDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 123 VIYVLICPELYEREGTPYgaNNGRDWPDNHIRFARLGLAAADIAAnlaQIHWCPDLVHAHDWPAGLAPAYMHWRG----- 197
Cdd:cd03791 81 DYYFLDNPEFFDRPGLPG--PPGYDYPDNAERFAFFSRAALELLR---RLGFQPDIIHANDWHTALVPAYLKTRYrgpgf 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 198 QRTPTLFTIHNLAYQGVVSLASCPELGIPEHALQQEGMEFYGKLSFLKAGMAYASHITTVSATYAQEITTPAFGCGLDGF 277
Cdd:cd03791 156 KKIKTVFTIHNLAYQGLFPLDTLAELGLPPELFHIDGLEFYGQINFLKAGIVYADRVTTVSPTYAKEILTPEYGEGLDGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 278 LasKTQQGLLSGIPNGID-ESWDAATDPHLSTPFAIGDWQGKAANAAHVRQMFGLD-PSNGPLFAVVSRLVYQKGLDLTE 355
Cdd:cd03791 236 L--RARAGKLSGILNGIDyDEWNPATDKLIPANYSANDLEGKAENKAALQKELGLPvDPDAPLFGFVGRLTEQKGVDLIL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 356 GVAEYIVKSGGQIAIIGRGEPEEEQAMRALAARFPGRIGVNIGFNETDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFGS 435
Cdd:cd03791 314 DALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 436 LPVARNTGGLADTIENGV------TGFLFDESTVASYEEALSRAFKVFAYPQLLNAMRCRAMAAPFNWCKAVEPYAELYE 509
Cdd:cd03791 394 LPIVRRTGGLADTVFDYDpetgegTGFVFEDYDAEALLAALRRALALYRNPELWRKLQKNAMKQDFSWDKSAKEYLELYR 473
|
.
gi 740794015 510 Q 510
Cdd:cd03791 474 S 474
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
45-511 |
0e+00 |
|
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273969 [Multi-domain] Cd Length: 473 Bit Score: 531.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 45 KVLFVTSEIADLVKTGGLGDVSAALPRAMAHL-HDVRLLIPGYRQVMHSENPIHIIGELGGHAALPACKIGRM--DMPDG 121
Cdd:TIGR02095 2 RVLFVAAEMAPFAKTGGLADVVGALPKALAALgHDVRVLLPAYGCIEDEVDDQVKVVELVDLSVGPRTLYVKVfeGVVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 122 LVIYVLICPELYEREGTPYGAnngrDWPDNHIRFARLGLAAADIAAnlaQIHWCPDLVHAHDWPAGLAPAYMHWRG--QR 199
Cdd:TIGR02095 82 VPVYFIDNPSLFDRPGGIYGD----DYPDNAERFAFFSRAAAELLS---GLGWQPDVVHAHDWHTALVPALLKAVYrpNP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 200 TPTLFTIHNLAYQGVVSLASCPELGIPEHALQQEGMEFYGKLSFLKAGMAYASHITTVSATYAQEITTPAFGCGLDGFLA 279
Cdd:TIGR02095 155 IKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLEFYGRVNFLKGGIVYADRVTTVSPTYAREILTPEFGYGLDGVLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 280 SKtqQGLLSGIPNGIDES-WDAATDPHLSTPFAIGDWQGKAANAAHVRQMFGLDPSN-GPLFAVVSRLVYQKGLDLTEGV 357
Cdd:TIGR02095 235 AR--SGKLRGILNGIDTEvWNPATDPYLKANYSADDLAGKAENKEALQEELGLPVDDdVPLFGVISRLTQQKGVDLLLAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 358 AEYIVKSGGQIAIIGRGEPEEEQAMRALAARFPGRIGVNIGFNETDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFGSLP 437
Cdd:TIGR02095 313 LPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTVP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 438 VARNTGGLADTIENG------VTGFLFDESTVASYEEALSRAFKVFA-YPQLLNAMRCRAMAAPFNWCKAVEPYAELYEQ 510
Cdd:TIGR02095 393 IVRRTGGLADTVVDGdpeaesGTGFLFEEYDPGALLAALSRALRLYRqDPSLWEALQKNAMSQDFSWDKSAKQYVELYRS 472
|
.
gi 740794015 511 L 511
Cdd:TIGR02095 473 L 473
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
45-513 |
7.74e-144 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 422.59 E-value: 7.74e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 45 KVLFVTSEIADLVKTGGLGDVSAALPRA-MAHLHDVRLLIPGYRQVM---HSENPIHIIGEL-GGHAALPACKIGRMDMp 119
Cdd:PRK14099 5 RVLSVASEIFPLIKTGGLADVAGALPAAlKAHGVEVRTLVPGYPAVLagiEDAEQVHSFPDLfGGPARLLAARAGGLDL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 120 dglviYVLICPELYEREGTPYGANNGRDWPDNHIRFARLGLAAADIAANLAQiHWCPDLVHAHDWPAGLAPAYMHWRGQR 199
Cdd:PRK14099 84 -----FVLDAPHLYDRPGNPYVGPDGKDWPDNAQRFAALARAAAAIGQGLVP-GFVPDIVHAHDWQAGLAPAYLHYSGRP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 200 TP-TLFTIHNLAYQGVVSLASCPELGIPEHALQQEGMEFYGKLSFLKAGMAYASHITTVSATYAQEITTPAFGCGLDGFL 278
Cdd:PRK14099 158 APgTVFTIHNLAFQGQFPRELLGALGLPPSAFSLDGVEYYGGIGYLKAGLQLADRITTVSPTYALEIQGPEAGMGLDGLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 279 asKTQQGLLSGIPNGIDES-WDAATDPHLSTPFAIGDWQGKAANAAHVRQMFGLDPSNG-PLFAVVSRLVYQKGLDLTEG 356
Cdd:PRK14099 238 --RQRADRLSGILNGIDTAvWNPATDELIAATYDVETLAARAANKAALQARFGLDPDPDaLLLGVISRLSWQKGLDLLLE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 357 VAEYIVKSGGQIAIIGRGEPEEEQAMRALAARFPGRIGVNIGFNETDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFGSL 436
Cdd:PRK14099 316 ALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQAGADALLVPSRFEPCGLTQLCALRYGAV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 437 PVARNTGGLADT--------IENGV-TGFLFDESTVASYEEALSRAFKVFAYPQLLNAMRCRAMAAPFNWCKAVEPYAEL 507
Cdd:PRK14099 396 PVVARVGGLADTvvdanemaIATGVaTGVQFSPVTADALAAALRKTAALFADPVAWRRLQRNGMTTDVSWRNPAQHYAAL 475
|
....*.
gi 740794015 508 YEQLVA 513
Cdd:PRK14099 476 YRSLVA 481
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
46-278 |
4.40e-86 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 265.35 E-value: 4.40e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 46 VLFVTSEIADLVKTGGLGDVSAALPRAMAHL-HDVRLLIPGYRQVMHSENPIHIIGELGGHAALPA----CKIGRMdMPD 120
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALgHDVRVIMPRYGNIPEERNQLEDVIRLSVAAGVPVrpltVGVARL-ELD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 121 GLVIYVLICPELYEREGtPYGaNNGRDWPDNHIRFARLGLAAADIAAnlaQIHWCPDLVHAHDWPAGLAPAYMHWRGQ-- 198
Cdd:pfam08323 80 GVDVYFLDNPDYFDRPG-LYG-DDGRDYEDNAERFAFFSRAALELAK---KLGWIPDIIHCHDWHTALVPAYLKEAYAdd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 199 ---RTPTLFTIHNLAYQGVVSLASCPELGIPEHALQQEGMEFYGKLSFLKAGMAYASHITTVSATYAQEITTPAFGCGLD 275
Cdd:pfam08323 155 pfkNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFNLDGLEFYGQINFLKAGIVYADAVTTVSPTYAEEIQTPEFGGGLD 234
|
...
gi 740794015 276 GFL 278
Cdd:pfam08323 235 GLL 237
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
45-514 |
6.34e-62 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 210.75 E-value: 6.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 45 KVLFVTSEIADLVKTGGLGDVSAALPRAMAHL-HDVRLLIPGYRQVMHSENPIHIIGELGG------------H---AAL 108
Cdd:PRK14098 7 KVLYVSGEVSPFVRVSALADFMASFPQALEEEgFEARIMMPKYGTINDRKFRLHDVLRLSDievplkektdllHvkvTAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 109 PACKIGrmdmpdglvIYVLICPELYEREGTPYGANNGRDWPDN--HIRFARLGLAAADIaanlaQIHWCPDLVHAHDWPA 186
Cdd:PRK14098 87 PSSKIQ---------TYFLYNEKYFKRNGLFTDMSLGGDLKGSaeKVIFFNVGVLETLQ-----RLGWKPDIIHCHDWYA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 187 GLAPAYM------HWRGQRTPTLFTIHNLAYQGVVSLASCPELGIPE--HALQQEGmefyGKLSFLKAGMAYASHITTVS 258
Cdd:PRK14098 153 GLVPLLLktvyadHEFFKDIKTVLTIHNVYRQGVLPFKVFQKLLPEEvcSGLHREG----DEVNMLYTGVEHADLLTTTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 259 ATYAQEITT-PAFGCGLDGFLASktQQGLLSGIPNGID-ESWDAATDPHLSTPFAIGDWQGKAANAAHVRQMFGLDPSNG 336
Cdd:PRK14098 229 PRYAEEIAGdGEEAFGLDKVLEE--RKMRLHGILNGIDtRQWNPSTDKLIKKRYSIERLDGKLENKKALLEEVGLPFDEE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 337 -PLFAVVSRLVYQKGLDLTEGVAEYIVKSGGQIAIIGRGEPEEEQAMRALAARFPGRIGVNIGFNETDARRMFAGSDFLL 415
Cdd:PRK14098 307 tPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFHLAIAGLDMLL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 416 MPSRYEPCGLSQMYAQRFGSLPVARNTGGLADTI----ENGVTGFLFDESTVASYEEALSRAFKVFAYPQLLNAMRCRAM 491
Cdd:PRK14098 387 MPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETIeevsEDKGSGFIFHDYTPEALVAKLGEALALYHDEERWEELVLEAM 466
|
490 500
....*....|....*....|...
gi 740794015 492 AAPFNWCKAVEPYAELYEQLVAK 514
Cdd:PRK14098 467 ERDFSWKNSAEEYAQLYRELLGP 489
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
25-515 |
9.90e-58 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 207.06 E-value: 9.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 25 ILAPGGKTSLPLIHhnpnrkkvlfVTSEIADLVKTGGLGDVSAALPRAM---AHLhdVRLLIPGYRQVMHSE----NPIH 97
Cdd:PLN02939 473 LTLSGTSSGLHIVH----------IAAEMAPVAKVGGLADVVSGLGKALqkkGHL--VEIVLPKYDCMQYDQirnlKVLD 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 98 IIGELGGHAALPACKI--GRMDmpdGLVIYvLICPELYER---EGTPYGanngrdwpdNHIRFARLGLAAADIAANLAQI 172
Cdd:PLN02939 541 VVVESYFDGNLFKNKIwtGTVE---GLPVY-FIEPQHPSKffwRAQYYG---------EHDDFKRFSYFSRAALELLYQS 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 173 HWCPDLVHAHDW-PAGLAPAYmhW-----RGQRTPTL-FTIHNLAYQGVVS---LASCpelGIPEHALQQEG-ME--FYG 239
Cdd:PLN02939 608 GKKPDIIHCHDWqTAFVAPLY--WdlyapKGFNSARIcFTCHNFEYQGTAPasdLASC---GLDVHQLDRPDrMQdnAHG 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 240 KLSFLKAGMAYASHITTVSATYAQEITTPAfGCGLDGFLASKTQQglLSGIPNGID-ESWDAATDPHLSTPFAIGDWQGK 318
Cdd:PLN02939 683 RINVVKGAIVYSNIVTTVSPTYAQEVRSEG-GRGLQDTLKFHSKK--FVGILNGIDtDTWNPSTDRFLKVQYNANDLQGK 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 319 AANAAHVRQMFGLDPSNG--PLFAVVSRLVYQKGLDLTEGVAEYIVKSGGQIAIIGRGE-PEEEQAMRALAARFPG--RI 393
Cdd:PLN02939 760 AANKAALRKQLGLSSADAsqPLVGCITRLVPQKGVHLIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGIADQFQSnnNI 839
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 394 GVNIGFNETDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFGSLPVARNTGGLADTI------------ENGVTGFLFDES 461
Cdd:PLN02939 840 RLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSVfdfddetipvelRNGFTFLTPDEQ 919
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 740794015 462 TVASyeeALSRAFKVFAY-PQLLNAMRCRAMAAPFNWCKAVEPYAELYEQLVAKA 515
Cdd:PLN02939 920 GLNS---ALERAFNYYKRkPEVWKQLVQKDMNIDFSWDSSASQYEELYQRAVARA 971
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
46-508 |
7.26e-47 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 175.44 E-value: 7.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 46 VLFVTSEIADLVKTGGLGDVSAALPRAMAHL-HDVRLLIPGYRQVMHSE-NPIHIIGELGGHAALPACKIGRMDmpdGLV 123
Cdd:PLN02316 590 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLnHNVDIILPKYDCLNLSHvKDLHYQRSYSWGGTEIKVWFGKVE---GLS 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 124 IYVLICPELYEREGTPYGANNgrdwpDNHirfaRLGLAAADIAANLAQIHWCPDLVHAHDWPAglAPA-------YMHWR 196
Cdd:PLN02316 667 VYFLEPQNGMFWAGCVYGCRN-----DGE----RFGFFCHAALEFLLQSGFHPDIIHCHDWSS--APVawlfkdhYAHYG 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 197 GQRTPTLFTIHNLayqgvvslascpELGIPEhalqqegmefYGKlsflkaGMAYASHITTVSATYAQEITtpafgcgldG 276
Cdd:PLN02316 736 LSKARVVFTIHNL------------EFGANH----------IGK------AMAYADKATTVSPTYSREVS---------G 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 277 FLASKTQQGLLSGIPNGID-ESWDAATDPHLSTPFAIGD-WQGKAANAAHVRQMFGLDPSNGPLFAVVSRLVYQKGLDLT 354
Cdd:PLN02316 779 NSAIAPHLYKFHGILNGIDpDIWDPYNDNFIPVPYTSENvVEGKRAAKEALQQRLGLKQADLPLVGIITRLTHQKGIHLI 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 355 EGVAEYIVKSGGQIAIIGRG-EPEEEQAMRALAARFP----GRIGVNIGFNETDARRMFAGSDFLLMPSRYEPCGLSQMY 429
Cdd:PLN02316 859 KHAIWRTLERNGQVVLLGSApDPRIQNDFVNLANQLHsshhDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLT 938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 430 AQRFGSLPVARNTGGLADTI-----------ENGV--TGFLFDESTVASYEEALSRAFKVFaYP--QLLNAMRCRAMAAP 494
Cdd:PLN02316 939 AMRYGSIPVVRKTGGLFDTVfdvdhdkeraqAQGLepNGFSFDGADAAGVDYALNRAISAW-YDgrDWFNSLCKRVMEQD 1017
|
490
....*....|....
gi 740794015 495 FNWCKAVEPYAELY 508
Cdd:PLN02316 1018 WSWNRPALDYMELY 1031
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
126-509 |
5.02e-24 |
|
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: 103.39 E-value: 5.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 126 VLICPELYEREgtPYGANNGRDWPDNHIRFARLGLAAADIAANLAQIHWCPDLVHAHDWPAGLApAYMHWRGQRTPTLFT 205
Cdd:cd03801 35 TVLTPADPGEP--PEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVHAHGLLAALL-AALLALLLGAPLVVT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 206 IHNLAYQGVVSLASCPelgipehalqqegmefYGKLSFLKAGMAYASHITTVSATYAQEITTpAFGCGLDGFLAsktqqg 285
Cdd:cd03801 112 LHGAEPGRLLLLLAAE----------------RRLLARAEALLRRADAVIAVSEALRDELRA-LGGIPPEKIVV------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 286 llsgIPNGIDESwdaatdphlstpfaigdwqgkaANAAHVRQMFGLDPsNGPLFAVVSRLVYQKGLDLTEGVAEYIVKSG 365
Cdd:cd03801 169 ----IPNGVDLE----------------------RFSPPLRRKLGIPP-DRPVLLFVGRLSPRKGVDLLLEALAKLLRRG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 366 GQIA--IIGRGEPEEEQAMRALAA-----RFPGRIgvnigfNETDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFGSLPV 438
Cdd:cd03801 222 PDVRlvIVGGDGPLRAELEELELGlgdrvRFLGFV------PDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVV 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740794015 439 ARNTGGLADTIENGVTGFLFDESTVASYEEALSRAFKvfaYPQLLNAMR--CRAMAAP-FNWCKAVEPYAELYE 509
Cdd:cd03801 296 ATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLA---DPELRARLGraARERVAErFSWERVAERLLDLYR 366
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
335-475 |
2.29e-15 |
|
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: 73.46 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 335 NGPLFAVVSRLVYQKGLDLTEGVAEYIVKSGGQIAIIGRGEPEEEQAMRALAARFPGRIGVN-IGFNETDA-RRMFAGSD 412
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIfLGFVSDEDlPELLKIAD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740794015 413 FLLMPSRYEPCGLSQMYAQRFGSLPVARNTGGLADTIENGVTGFLFDESTVASYEEALSRAFK 475
Cdd:pfam00534 81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLE 143
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
408-513 |
2.31e-15 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 72.33 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 408 FAGSDFLLMPSRYEPCGLSQMYAQRFGSLPVARNTGGLADTIENGVTGFLFDESTVASYEEALSRAfkvFAYPQLLNAMR 487
Cdd:COG0438 18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRL---LEDPELRRRLG 94
|
90 100
....*....|....*....|....*....
gi 740794015 488 CRA---MAAPFNWCKAVEPYAELYEQLVA 513
Cdd:COG0438 95 EAArerAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
148-496 |
5.30e-15 |
|
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: 76.24 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 148 WPDNHIRFARLGLaaadiaanlaqiHWCPDLVHAH----DWPAGLApaymhWRGQRTPTLFTIHNLayqgvvslascpel 223
Cdd:cd03819 61 ALLGNVRLARLIR------------RERIDLIHAHsrapAWLGWLA-----SRLTGVPLVTTVHGS-------------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 224 gipeHALQQEGMEFYgklsflKAGMAYASHITTVSATYAQEITtpafgcGLDGFLASKtqqglLSGIPNGIDESwdaatd 303
Cdd:cd03819 110 ----YLATYHPKDFA------LAVRARGDRVIAVSELVRDHLI------EALGVDPER-----IRVIPNGVDTD------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 304 phlstPFaigDWQGKAANAAhvrqmFGLDPSNGPLFAVVSRLVYQKGLDLTEGVAEYIVKSGGQ-IAIIGRGEPEEEQAM 382
Cdd:cd03819 163 -----RF---PPEAEAEERA-----QLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFrLLVAGDGPERDEIRR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 383 RALAARFPGRIGVnIGFNEtDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFGSLPVARNTGGLADTIENGVTGFLFDEST 462
Cdd:cd03819 230 LVERLGLRDRVTF-TGFRE-DVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGD 307
|
330 340 350
....*....|....*....|....*....|....
gi 740794015 463 VASYEEALSRAfkvfaypQLLNAMRCRAMAAPFN 496
Cdd:cd03819 308 AEALADAIRAA-------KLLPEAREKLQAAAAL 334
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
176-505 |
1.73e-13 |
|
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: 72.27 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 176 PDLVHAHDWPAGLAPAYM-HWRGqrTPTLFTIHNLayqGVVSLAscpelgipeHALQQEGMEFYGKLSFLKAGMAYASHI 254
Cdd:cd03800 102 YDLIHSHYWDSGLVGALLaRRLG--VPLVHTFHSL---GRVKYR---------HLGAQDTYHPSLRITAEEQILEAADRV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 255 TtvsATYAQEIttpAFGCGLDGFLASKTQQgllsgIPNGideswdaaTDPHLSTPFAigdwqgkaaNAAHVRQMFGLDPS 334
Cdd:cd03800 168 I---ASTPQEA---DELISLYGADPSRINV-----VPPG--------VDLERFFPVD---------RAEARRARLLLPPD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 335 NGPLFAVvSRLVYQKGLD-LTEGVAE----------YIVksGGQIaiiGRGEPEEEQAMRALAA--------RFPGRIgv 395
Cdd:cd03800 220 KPVVLAL-GRLDPRKGIDtLVRAFAQlpelrelanlVLV--GGPS---DDPLSMDREELAELAEelglidrvRFPGRV-- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 396 nigfNETDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFGsLPV-ARNTGGLADTIENGVTGFLFDESTVASYEEALSRAf 474
Cdd:cd03800 292 ----SRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACG-TPVvATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRL- 365
|
330 340 350
....*....|....*....|....*....|....
gi 740794015 475 kvFAYPQLLNAMRCRAM---AAPFNWCKAVEPYA 505
Cdd:cd03800 366 --LDDPALWQRLSRAGLeraRAHYTWESVADQLL 397
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
333-472 |
3.32e-13 |
|
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: 71.09 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 333 PSNGPLFAVVSRLVYQKGLDLTEGVAEYIVKSGGQIA--IIGRGEPEEEQAMRALAARFPGRIgVNIGFnETDARRMFAG 410
Cdd:cd03808 186 PSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRflLVGDGELENPSEILIEKLGLEGRI-EFLGF-RSDVPELLAE 263
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740794015 411 SDFLLMPSRYEPCGLSQMYAQRFGsLPV-ARNTGGLADTIENGVTGFLFDESTVASYEEALSR 472
Cdd:cd03808 264 SDVFVLPSYREGLPRSLLEAMAAG-RPViTTDVPGCRELVIDGVNGFLVPPGDVEALADAIEK 325
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
341-458 |
3.51e-12 |
|
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: 66.27 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 341 VVSRLVYQKGLDLT-EGVAEYIVK-SGGQIAIIGRGEPEEEQAMRALAARFPGRIGVNIGFNETDARRMF-AGSDFLLMP 417
Cdd:cd01635 115 SVGRLVPEKGIDLLlEALALLKARlPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLlAAADVFVLP 194
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 740794015 418 SRYEPCGLSQMYAQRFGSLPVARNTGGLADTIENGVTGFLF 458
Cdd:cd01635 195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
336-472 |
1.10e-11 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 62.53 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 336 GPLFAVVSRLV-YQKGLD-LTEGVAEyIVKSGG--QIAIIGRGEPEE-EQAMRALAAR--FPGRIgvnigfneTDARRMF 408
Cdd:pfam13692 1 RPVILFVGRLHpNVKGVDyLLEAVPL-LRKRDNdvRLVIVGDGPEEElEELAAGLEDRviFTGFV--------EDLAELL 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740794015 409 AGSDFLLMPSRYEPCGLSQMYAQRFGsLP-VARNTGGLADTIEnGVTGFLFDESTVASYEEALSR 472
Cdd:pfam13692 72 AAADVFVLPSLYEGFGLKLLEAMAAG-LPvVATDVGGIPELVD-GENGLLVPPGDPEALAEAILR 134
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
330-490 |
1.96e-11 |
|
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: 65.39 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 330 GLDPSNGPLFAVVSRLVYQKGLD-LTEGVAEYIVKSGGQIAIIGRGEPEEEQAMRALAARFPGRIGvnigfNETDARrMF 408
Cdd:cd03814 192 RLGPPGRPLLLYVGRLAPEKNLEaLLDADLPLAASPPVRLVVVGDGPARAELEARGPDVIFTGFLT-----GEELAR-AY 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 409 AGSDFLLMPSRYEPCGLSQMYAQRFGsLPV-ARNTGGLADTIENGVTGFLFDESTVASYEEALSRafkVFAYPQLLNAMR 487
Cdd:cd03814 266 ASADVFVFPSRTETFGLVVLEAMASG-LPVvAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRA---LLEDPELRRRMA 341
|
...
gi 740794015 488 CRA 490
Cdd:cd03814 342 ARA 344
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
172-511 |
1.25e-10 |
|
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: 63.17 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 172 IHWCPDLVHAH-DWPAGLAPAYMHWRGQrTPTLFTIHNLAYQgvvslascpelgipehalqqEGMEFYGKLSFLKAGMAY 250
Cdd:cd03798 92 RRGPPDLIHAHfAYPAGFAAALLARLYG-VPYVVTEHGSDIN--------------------VFPPRSLLRKLLRWALRR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 251 ASHITTVSATYAQEittpAFGCGLDGFLASKtqqgllsgIPNGIDESWdaatdphlstpFAIGDWQGKAanaahvrqmfg 330
Cdd:cd03798 151 AARVIAVSKALAEE----LVALGVPRDRVDV--------IPNGVDPAR-----------FQPEDRGLGL----------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 331 ldPSNGPLFAVVSRLVYQKGLD-LTEGVAEYIVKSGG-QIAIIGRGEpeEEQAMRALAA--------RFPGRIgvnigfN 400
Cdd:cd03798 197 --PLDAFVILFVGRLIPRKGIDlLLEAFARLAKARPDvVLLIVGDGP--LREALRALAEdlglgdrvTFTGRL------P 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 401 ETDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFGsLPV-ARNTGGLADTIENGVTGFLFDESTVASYEEALSRAFKVfAY 479
Cdd:cd03798 267 HEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACG-LPVvATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALAE-PY 344
|
330 340 350
....*....|....*....|....*....|..
gi 740794015 480 PQLLNAMRCRAMAAPFNWCKAVEPYAELYEQL 511
Cdd:cd03798 345 LRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
176-470 |
4.24e-10 |
|
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: 61.22 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 176 PDLVHAHDWPAGLAPAYMhwRGQRTPTLFTIHNlayqgvvslascpelgIPEHALQQEGMEFYGKLSFLKAgmayaSHIT 255
Cdd:cd03811 84 PDVVISFLGFATYIVAKL--AAARSKVIAWIHS----------------SLSKLYYLKKKLLLKLKLYKKA-----DKIV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 256 TVSATYAQEITtpafgcGLDGFLASKTQQgllsgIPNGIDesWDAATdphlstpfaigdwqgKAANAAHVRqmfglDPSN 335
Cdd:cd03811 141 CVSKGIKEDLI------RLGPSPPEKIEV-----IYNPID--IDRIR---------------ALAKEPILN-----EPED 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 336 GPLFAVVSRLVYQKGLDLT-EGVAEyIVKSGGQI--AIIGRGEPEEEQamRALAA--------RFPGRIgvnigfneTDA 404
Cdd:cd03811 188 GPVILAVGRLDPQKGHDLLiEAFAK-LRKKYPDVklVILGDGPLREEL--EKLAKelglaervIFLGFQ--------SNP 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740794015 405 RRMFAGSDFLLMPSRYEPCGLSQMYAQRFGSLPVARNTGGLADTIENGVTGFLFDESTVASYEEAL 470
Cdd:cd03811 257 YPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGIL 322
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
332-509 |
1.63e-09 |
|
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: 59.65 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 332 DPSNGPL-FAVVSRLVYQKGLDLTEGVAEYIVKSGGQIAIIGRG-EPEEEQAMRALAARFPGRigvnigFNETDARRMFA 409
Cdd:cd03823 186 RPGTERLrFGYIGRLTEEKGIDLLVEAFKRLPREDIELVIAGHGpLSDERQIEGGRRIAFLGR------VPTDDIKDFYE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 410 GSDFLLMPSR-YEPCGLSQMYAQRFGsLPV-ARNTGGLADTIENGVTGFLFDESTVASYEEALSRafkVFAYPQLLNAMR 487
Cdd:cd03823 260 KIDVLVVPSIwPEPFGLVVREAIAAG-LPViASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRR---LLTDPALLERLR 335
|
170 180
....*....|....*....|..
gi 740794015 488 CRAMaAPFNWCKAVEPYAELYE 509
Cdd:cd03823 336 AGAE-PPRSTESQAEEYLKLYR 356
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
174-511 |
7.30e-09 |
|
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: 57.67 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 174 WCPDLVHAHDwP--AGLAPAYMHwRGQRTPTLFTIHnLAYQGVVSLASCPELGIPEHALQQEGmEFYGklsflkagmaYA 251
Cdd:cd03817 83 LGPDIIHTHT-PfsLGKLGLRIA-RKLKIPIVHTYH-TMYEDYLHYIPKGKLLVKAVVRKLVR-RFYN----------HT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 252 SHITTVS---ATYAQE--ITTPAFGcgldgflasktqqgllsgIPNGIDeswDAATDPHLSTPFaigdwqgkaanaahvR 326
Cdd:cd03817 149 DAVIAPSekiKDTLREygVKGPIEV------------------IPNGID---LDKFEKPLNTEE---------------R 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 327 QMFGLDPsNGPLFAVVSRLVYQKGLD-LTEGVAEYIVKSGGQIAIIGRGePEEEQaMRALAARFPGRIGVN-IGF---NE 401
Cdd:cd03817 193 RKLGLPP-DEPILLYVGRLAKEKNIDfLLRAFAELKKEPNIKLVIVGDG-PEREE-LKELARELGLADKVIfTGFvprEE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 402 TDARrmFAGSDFLLMPSRYEPCGLSQMYAQRFGsLPV-ARNTGGLADTIENGVTGFLFDEstvasYEEALSRAF-KVFAY 479
Cdd:cd03817 270 LPEY--YKAADLFVFASTTETQGLVYLEAMAAG-LPVvAAKDPAASELVEDGENGFLFEP-----NDETLAEKLlHLREN 341
|
330 340 350
....*....|....*....|....*....|....
gi 740794015 480 PQLLNAM--RCRAMAAPFNWCKAVEpyaELYEQL 511
Cdd:cd03817 342 LELLRKLskNAEISAREFAFAKSVE---KLYEEV 372
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
336-497 |
1.11e-08 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 57.41 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 336 GPLFAVVSRLVYQKGLDLTEGVAEYIvkSGGQIAIIGRG--EPEEEQAMRALAARFPGRIGVNigfnetDARRMFAGSDF 413
Cdd:PLN02871 263 KPLIVYVGRLGAEKNLDFLKRVMERL--PGARLAFVGDGpyREELEKMFAGTPTVFTGMLQGD------ELSQAYASGDV 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 414 LLMPSRYEPCGLSQMYAQRFGSLPVARNTGGLADTIEN---GVTGFLFDEstvASYEEALSRAFKVFAYPQLLNAM--RC 488
Cdd:PLN02871 335 FVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTP---GDVDDCVEKLETLLADPELRERMgaAA 411
|
....*....
gi 740794015 489 RAMAAPFNW 497
Cdd:PLN02871 412 REEVEKWDW 420
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
342-472 |
1.58e-08 |
|
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: 56.48 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 342 VSRLVYQKGLDLTEGVAEYIVKS--GGQIAIIGRGEPEEEQamRALAA--------RFPGRIGvNIgfnetdaRRMFAGS 411
Cdd:cd03820 187 VGRLTYQKGFDLLIEAWALIAKKhpDWKLRIYGDGPEREEL--EKLIDklgledrvKLLGPTK-NI-------AEEYANS 256
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740794015 412 DFLLMPSRYEPCGLSQMYAQRFGsLPVA--RNTGGLADTIENGVTGFLFDESTVASYEEALSR 472
Cdd:cd03820 257 SIFVLSSRYEGFPMVLLEAMAYG-LPIIsfDCPTGPSEIIEDGENGLLVPNGDVDALAEALLR 318
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
400-511 |
2.28e-08 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340859 [Multi-domain] Cd Length: 370 Bit Score: 56.21 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 400 NETDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFGSLPVARNTGGLADTIENGVTGFLFDestVASYEEALSRAFKVFAY 479
Cdd:cd04962 259 KQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSD---VGDVDAMAKSALSILED 335
|
90 100 110
....*....|....*....|....*....|....*
gi 740794015 480 PQLLNAMR--CRAMAAP-FNWCKAVEPYAELYEQL 511
Cdd:cd04962 336 DELYNRMGraARKRAAErFDPERIVPQYEAYYRRL 370
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
329-495 |
5.02e-07 |
|
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: 51.90 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 329 FGLDPSNGPLFAVVSRLVYQKGLDLtegVAEYIVKSGGQIAIIGRGEpeEEQAMRALAA---RFPGRIGVNIgFNE--TD 403
Cdd:cd03804 192 FAPAADKEDYYLTASRLVPYKRIDL---AVEAFNELPKRLVVIGDGP--DLDRLRAMASpnvEFLGYQPDEV-LKEllSK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 404 ARRM-FAGS-DFllmpsryepcGLSQMYAQRFGSLPVARNTGGLADTIENGVTGFLFDESTVASYEEALSRAFKVFAY-- 479
Cdd:cd03804 266 ARAFvFAAEeDF----------GIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEFEQNFDRfk 335
|
170
....*....|....*.
gi 740794015 480 PQllnamRCRAMAAPF 495
Cdd:cd03804 336 PQ-----AIRANAERF 346
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
290-509 |
3.04e-06 |
|
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: 49.24 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 290 IPNGIDeswdaatdphlSTPFAIGDwqgkaANAAHVRQMFGLdPSNGPLFAVVSRLVYQKGLDLTEGVAEYIVKSGGQI- 368
Cdd:cd03807 161 IYNGID-----------LFKLSPDD-----ASRARARRRLGL-AEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLr 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 369 -AIIGRGePEEEQAMRALAA-------RFPGRIGvnigfnetDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFGsLP-VA 439
Cdd:cd03807 224 lLLVGRG-PERPNLERLLLElgledrvHLLGERS--------DVPALLPAMDIFVLSSRTEGFPNALLEAMACG-LPvVA 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740794015 440 RNTGGLADTIENGvTGFLFDESTVASYEEALSRAFKVFA-YPQLLNAMRCRAMAApFNWCKAVEPYAELYE 509
Cdd:cd03807 294 TDVGGAAELVDDG-TGFLVPAGDPQALADAIRALLEDPEkRARLGRAARERIANE-FSIDAMVRRYETLYY 362
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
176-295 |
4.40e-06 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 47.14 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 176 PDLVHAHDWPAGLAPAYMHWRGQRTPTLFTIHNLAYQGVVSLASCPELGIPEHALqqegmefygklsfLKAGMAYASHIT 255
Cdd:pfam13439 72 PDVVHAHSPFPLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRRL-------------ERRLLRRADRVI 138
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 740794015 256 TVSATYAQEITTpafgcgLDGFLASKTQQgllsgIPNGID 295
Cdd:pfam13439 139 AVSEAVADELRR------LYGVPPEKIRV-----IPNGVD 167
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
124-497 |
1.05e-05 |
|
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: 47.74 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 124 IYVLICPELYEREGTPYGANNGRDWPDNHIRFARLGLAAADIAANLAQIHWCPDLVHAHDWPAGLapaymhwRGQRTPTL 203
Cdd:cd03809 33 DESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKPDLLHSPHNTAPL-------LLKGCPQV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 204 FTIHNLAYqgvvslASCPELGIPEHALqqegmeFYGKLsfLKAGMAYASHITTVSATYAQEITTpAFGCGLDGFLAsktq 283
Cdd:cd03809 106 VTIHDLIP------LRYPEFFPKRFRL------YYRLL--LPISLRRADAIITVSEATRDDIIK-FYGVPPEKIVV---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 284 qgllsgIPNGIDESWDaatdphlstpfaigdwqgKAANAAHVRQMFGLDPsngPLFAVVSRLVYQKGLDLTEGVAEYIVK 363
Cdd:cd03809 167 ------IPLGVDPSFF------------------PPESAAVLIAKYLLPE---PYFLYVGTLEPRKNHERLLKAFALLKK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 364 SGG--QIAIIGRGEPEEEQAMRALAA-------RFPGRIgvnigfNETDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFG 434
Cdd:cd03809 220 QGGdlKLVIVGGKGWEDEELLDLVKKlglggrvRFLGYV------SDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACG 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740794015 435 sLPV-ARNTGGLADTIENgvTGFLFDESTVASYEEALSRafkVFAYPQLLNAMR--CRAMAAPFNW 497
Cdd:cd03809 294 -TPViASNISVLPEVAGD--AALYFDPLDPESIADAILR---LLEDPSLREELIrkGLERAKKFSW 353
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
329-470 |
3.37e-05 |
|
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: 46.13 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 329 FGLDPSN-------GPLFAVVSRLVYQKGLDLTEGVAEyivKSGGQIAIIGRGEPEEEqaMRALAARFPGRIGVNIGF-N 400
Cdd:cd03802 155 NGLDPADyrfqpdpEDYLAFLGRIAPEKGLEDAIRVAR---RAGLPLKIAGKVRDEDY--FYYLQEPLPGPRIEFIGEvG 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740794015 401 ETDARRMFAGSDFLLMPSRY-EPCGLSQMYAQRFGSLPVARNTGGLADTIENGVTGFLfdestVASYEEAL 470
Cdd:cd03802 230 HDEKQELLGGARALLFPINWdEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFL-----VDSVEEMA 295
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
290-511 |
3.75e-05 |
|
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.
Pssm-ID: 340851 [Multi-domain] Cd Length: 364 Bit Score: 45.79 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 290 IPNGIDeswdaaTDphLSTPFaigdwqgkaaNAAHVRQMFGLD-PSNGPLFAVVSRLVYQKGLD-LTEGVAEYIVKSGGQ 367
Cdd:cd03825 166 IPNGID------TE--IFAPV----------DKAKARKRLGIPqDKKVILFGAESVTKPRKGFDeLIEALKLLATKDDLL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 368 IAIIGRGEPEEeqamralaARFPGRIgVNIGF--NETDARRMFAGSDFLLMPSRYEPCGLSQMYAQRFGSLPVARNTGGL 445
Cdd:cd03825 228 LVVFGKNDPQI--------VILPFDI-ISLGYidDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGS 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740794015 446 ADTIENGVTGFLFDESTVasyeEALSRAFK-VFAYPQLLNAMRCRAMAAPFNwCKA----VEPYAELYEQL 511
Cdd:cd03825 299 PEIVQHGVTGYLVPPGDV----QALAEAIEwLLANPKERESLGERARALAEN-HFDqrvqAQRYLELYKDL 364
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
290-497 |
6.55e-05 |
|
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.
Pssm-ID: 340848 [Multi-domain] Cd Length: 377 Bit Score: 45.05 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 290 IPNGIDeswdaatdphlSTPFAIGDWQGKAANaahvrqmfglDPSNGPLFAVVSRLVYQKGLDLTEGVAEYIVKSGG--Q 367
Cdd:cd03821 179 IPNGVD-----------IPEFDPGLRDRRKHN----------GLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRdwH 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 368 IAIIGRGEPEEEQAMRALAA-------RFPGRIgvnigFNETDARRMfAGSDFLLMPSRYEPCGLSQMYAQRFGsLPVAR 440
Cdd:cd03821 238 LVIAGPDDGAYPAFLQLQSSlglgdrvTFTGPL-----YGEAKWALY-ASADLFVLPSYSENFGNVVAEALACG-LPVVI 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 441 NTG-GLADTIENGVTGFLFDEstVASYEEALSRAFKVFAYPQLLNAM--RCRAMAAPFNW 497
Cdd:cd03821 311 TDKcGLSELVEAGCGVVVDPN--VSSLAEALAEALRDPADRKRLGEMarRARQVEENFSW 368
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
337-492 |
1.22e-04 |
|
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: 44.37 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 337 PLFAVVSRLVYQKGLD-LTEGVAEyIVKSGGQIAIIGRGEPEEEQAMRALAARFpGRIGVNIGFNETDARRMFAGSDFLL 415
Cdd:cd05844 190 PTILFVGRLVEKKGCDvLIEAFRR-LAARHPTARLVIAGDGPLRPALQALAAAL-GRVRFLGALPHAEVQDWMRRAEIFC 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 416 MPSRYEPCGLSQ------MYAQRFGSLPVARNTGGLADTIENGVTGFLFDESTVASYEEALSRafkVFAYPQLLNAMRCR 489
Cdd:cd05844 268 LPSVTAASGDSEglgivlLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQA---LLADRALADRMGGA 344
|
...
gi 740794015 490 AMA 492
Cdd:cd05844 345 ARA 347
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
332-472 |
4.93e-04 |
|
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.
Pssm-ID: 340829 [Multi-domain] Cd Length: 350 Bit Score: 42.44 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 332 DPSNGPL-FAVVSRLVYQKGLDLTEGVAEYIVKSGGQI--AIIGRGePEEEQAMRALAARFPGRIGVNIGF-NETDARRM 407
Cdd:cd03799 169 LPLDGKIrILTVGRLTEKKGLEYAIEAVAKLAQKYPNIeyQIIGDG-DLKEQLQQLIQELNIGDCVKLLGWkPQEEIIEI 247
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740794015 408 FAGSDFLLMPSRYEPCG------LSQMYAQRFGsLPVARNT-GGLADTIENGVTGFLFDESTVASYEEALSR 472
Cdd:cd03799 248 LDEADIFIAPSVTAADGdqdgppNTLKEAMAMG-LPVISTEhGGIPELVEDGVSGFLVPERDAEAIAEKLTY 318
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
173-218 |
5.59e-03 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 37.77 E-value: 5.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 740794015 173 HWCPDLVHAHDWPAGLAPAYMHWRgQRTPTLFTIHNLAYQGVVSLA 218
Cdd:pfam13579 69 AERPDVVHAHSPTAGLAARLARRR-RGVPLVVTVHGLALDYGSGWK 113
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
428-486 |
8.76e-03 |
|
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.
Pssm-ID: 340834 [Multi-domain] Cd Length: 392 Bit Score: 38.34 E-value: 8.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 428 MYAQRfgslPV-ARNTGGLADTIENGVTGFLFdESTVASYEEALSRAFKVfayPQLLNAM 486
Cdd:cd03805 320 MYAGK----PViACNSGGPLETVVEGVTGFLC-EPTPEAFAEAMLKLAND---PDLADRM 371
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
336-470 |
9.14e-03 |
|
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340826 [Multi-domain] Cd Length: 355 Bit Score: 38.41 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 336 GPLFAVVSRLVYQKGLD-LTEGVAE--YIvksggqIAIIGRGepEEEQAMRALAA-------RFPGRIgvnigfNETDAR 405
Cdd:cd03795 191 KKIFLFIGRLVYYKGLDyLIEAAQYlnYP------IVIGGEG--PLKPDLEAQIElnlldnvKFLGRV------DDEEKV 256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740794015 406 RMFAGSDFLLMPS--RYEPCGLSQMYAQRFGsLPV---ARNTGGLADTIeNGVTGFLFDESTVASYEEAL 470
Cdd:cd03795 257 IYLHLCDVFVFPSvlRSEAFGIVLLEAMMCG-KPVistNIGTGVPYVNN-NGETGLVVPPKDPDALAEAI 324
|
|
| |
