|
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 ... |
88-585 |
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: 586.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 88 LFVSAEVGPWSKTGGLGDVLGALPPRLAANGHRVMTVSPRYDQYKDAWDTSVLV---EIKVGDRVETVRYFHCFKRGVDR 164
Cdd:cd03791 3 LFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVlglEVKVGGRGEEVGVFELPVDGVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 165 VFVDHPVFLEKVWGKtqsklygPKAGEDYADNQFRFSLLCLAALEAPRVLnlnsnpyfsgpYGEDVVFIANDWHTALLPC 244
Cdd:cd03791 83 YFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRL-----------GFQPDIIHANDWHTALVPA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 245 YLKSMYKSRGiYMNAKVAFCIHNIAYQGRFAFADFPLLGLPDEFrssfDFMDGYDKPvkgRKINWMKAGIIESDRVVTVS 324
Cdd:cd03791 145 YLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPPEL----FHIDGLEFY---GQINFLKAGIVYADRVTTVS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 325 PYYAQELVSGEdRGVELDTII--RSVGITGIRNGMDHREWSPKTDRFISIHYDATTVtEAKCLLKQALQAECGLPVDSNI 402
Cdd:cd03791 217 PTYAKEILTPE-YGEGLDGVLraRAGKLSGILNGIDYDEWNPATDKLIPANYSANDL-EGKAENKAALQKELGLPVDPDA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 403 PVIGFIGRLEEQKGSDILFEAISKFIHLDVQIIVLGTGKKYMEKQIEQLEELYPEKARGIAKFNTPLAHKIIAGADFIVI 482
Cdd:cd03791 295 PLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 483 PSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVIEGY------TGFHagafsvecdaVDPADVEKLTSTVIRALTTFGTP 556
Cdd:cd03791 375 PSRFEPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYDpetgegTGFV----------FEDYDAEALLAALRRALALYRNP 444
|
490 500 510
....*....|....*....|....*....|
gi 1432028620 557 -VWKEIVQNCMAQDFSWKEPAKLWEKMLLS 585
Cdd:cd03791 445 eLWRKLQKNAMKQDFSWDKSAKEYLELYRS 474
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
85-586 |
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: 521.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 85 MTFLFVSAEVGPWSKTGGLGDVLGALPPRLAANGHRVMTVSPRYDQYKDAW----DTSVLVEIKVGDRVETVRYFHCFKR 160
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVddqvKVVELVDLSVGPRTLYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 161 GVDRVFVDHPVFLEKVwgktqSKLYGPkageDYADNQFRFSLLCLAALEAPRVLNlnsnpyfsgpYGEDVVfIANDWHTA 240
Cdd:TIGR02095 81 GVPVYFIDNPSLFDRP-----GGIYGD----DYPDNAERFAFFSRAAAELLSGLG----------WQPDVV-HAHDWHTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 241 LLPCYLKSMYKSRgiymNAKVAFCIHNIAYQGRFAFADFPLLGLPDEFRSSFDfMDGYDKpvkgrkINWMKAGIIESDRV 320
Cdd:TIGR02095 141 LVPALLKAVYRPN----PIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEG-LEFYGR------VNFLKGGIVYADRV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 321 VTVSPYYAQELVSGEdRGVELDTIIRSVG--ITGIRNGMDHREWSPKTDRFISIHYDATTVtEAKCLLKQALQAECGLPV 398
Cdd:TIGR02095 210 TTVSPTYAREILTPE-FGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 399 DSNIPVIGFIGRLEEQKGSDILFEAISKFIHLDVQIIVLGTGKKYMEKQIEQLEELYPEKARGIAKFNTPLAHKIIAGAD 478
Cdd:TIGR02095 288 DDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGAD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 479 FIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVIEGyTGFHAGAFSVECDAVDPADvekLTSTVIRALTTF-GTP- 556
Cdd:TIGR02095 368 FILMPSRFEPCGLTQLYAMRYGTVPIVRRTGGLADTVVDG-DPEAESGTGFLFEEYDPGA---LLAALSRALRLYrQDPs 443
|
490 500 510
....*....|....*....|....*....|
gi 1432028620 557 VWKEIVQNCMAQDFSWKEPAKLWEKMLLSL 586
Cdd:TIGR02095 444 LWEALQKNAMSQDFSWDKSAKQYVELYRSL 473
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
85-577 |
1.31e-170 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 493.84 E-value: 1.31e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 85 MTFLFVSAEVGPWSKTGGLGDVLGALPPRLAANGHRVMTVSPRYDQYKDAWDTSVLV---EIKVGDRVETVRYFHCFKRG 161
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIDDKLKDLEVVaslEVPLGGRTYYARVLEGPDDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 162 VDRVFVDHPVFLEKvwgktqSKLYGPkAGEDYADNQFRFSLLCLAALEAprVLNLNSNPyfsgpygeDVVFiANDWHTAL 241
Cdd:COG0297 81 VPVYFIDNPELFDR------PGPYGD-PDRDYPDNAERFAFFSRAALEL--LKGLDWKP--------DIIH-CHDWQTGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 242 LPCYLKSMYKSRGiYMNAKVAFCIHNIAYQGRFAFADFPLLGLPDEFrSSFDFMDGYDKpvkgrkINWMKAGIIESDRVV 321
Cdd:COG0297 143 IPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL-FTPDGLEFYGQ------INFLKAGIVYADRVT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 322 TVSPYYAQELVSGEdRGVELDTIIRSVG--ITGIRNGMDHREWSPKTDRFISIHYDATTVTE-AKCllKQALQAECGLPV 398
Cdd:COG0297 215 TVSPTYAREIQTPE-FGEGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADDLEGkAAN--KAALQEELGLPV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 399 DSNIPVIGFIGRLEEQKGSDILFEAISKFIHLDVQIIVLGTGKKYMEKQIEQLEELYPEKARGIAKFNTPLAHKIIAGAD 478
Cdd:COG0297 292 DPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGAD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 479 FIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVI------EGYTGFHagaFsvecdavDPADVEKLTSTVIRALTT 552
Cdd:COG0297 372 FFLMPSRFEPCGLNQMYALRYGTVPIVRRTGGLADTVIdyneatGEGTGFV---F-------DEYTAEALLAAIRRALAL 441
|
490 500
....*....|....*....|....*.
gi 1432028620 553 FGTP-VWKEIVQNCMAQDFSWKEPAK 577
Cdd:COG0297 442 YRDPeAWRKLQRNAMKQDFSWEKSAK 467
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
85-582 |
1.05e-148 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 437.63 E-value: 1.05e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 85 MTFLFVSAEVGPWSKTGGLGDVLGALPPRLAANGHRVMTVSPRYDQYKDAWDTSVLVEikvGDRVETVRYFHCFKRGVDR 164
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKLRDAQVVG---RLDLFTVLFGHLEGDGVPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 165 VFVDHPVFlekvwgktqsklYGPKAGEDYADNQFRFSLLCLAALEAprVLNLNSNPyfsgpygeDVVFiANDWHTALLPC 244
Cdd:PRK00654 78 YLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEF--AEGLDPRP--------DIVH-AHDWHTGLIPA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 245 YLKSMYKSRgiYMNAKVAFCIHNIAYQGRFAFADFPLLGLPDEfRSSFDFMDGYDKpvkgrkINWMKAGIIESDRVVTVS 324
Cdd:PRK00654 135 LLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAE-AFHLEGLEFYGQ------ISFLKAGLYYADRVTTVS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 325 PYYAQELVSGEDrGVELDTIIRSVG--ITGIRNGMDHREWSPKTDRFISIHYDATTVTE-AKCllKQALQAECGLPvDSN 401
Cdd:PRK00654 206 PTYAREITTPEF-GYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADDLEGkAEN--KRALQERFGLP-DDD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 402 IPVIGFIGRLEEQKGSDILFEAISKFIHLDVQIIVLGTGKKYMEKQIEQLEELYPEKARGIAKFNTPLAHKIIAGADFIV 481
Cdd:PRK00654 282 APLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 482 IPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVI------EGYTGFHagaFsvecdavDPADVEKLTSTVIRALTTFGT 555
Cdd:PRK00654 362 MPSRFEPCGLTQLYALRYGTLPIVRRTGGLADTVIdynpedGEATGFV---F-------DDFNAEDLLRALRRALELYRQ 431
|
490 500
....*....|....*....|....*...
gi 1432028620 556 -PVWKEIVQNCMAQDFSWKEPAKLWEKM 582
Cdd:PRK00654 432 pPLWRALQRQAMAQDFSWDKSAEEYLEL 459
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
83-586 |
1.48e-96 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 303.95 E-value: 1.48e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 83 TGMTFLFVSAEVGPWSKTGGLGDVLGALPPRLAANGHRVMTVSPRYdqykdawdTSVLVEIkvgDRVETVRYFHCFKRGV 162
Cdd:PRK14099 2 TPLRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGY--------PAVLAGI---EDAEQVHSFPDLFGGP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 163 DRV----------FV-DHPvfleKVWGKTQSKLYGPKaGEDYADNQFRFSLLCLAALEaprvLNLNSNPYFSgpygEDVV 231
Cdd:PRK14099 71 ARLlaaraggldlFVlDAP----HLYDRPGNPYVGPD-GKDWPDNAQRFAALARAAAA----IGQGLVPGFV----PDIV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 232 FiANDWHTALLPCYLKSMYKSRgiymnAKVAFCIHNIAYQGRFAFADFPLLGLPDefrSSFDfMDGYDkpVKGrKINWMK 311
Cdd:PRK14099 138 H-AHDWQAGLAPAYLHYSGRPA-----PGTVFTIHNLAFQGQFPRELLGALGLPP---SAFS-LDGVE--YYG-GIGYLK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 312 AGIIESDRVVTVSPYYAQElVSGEDRGVELDTII--RSVGITGIRNGMDHREWSPKTDRFISIHYDATTVtEAKCLLKQA 389
Cdd:PRK14099 205 AGLQLADRITTVSPTYALE-IQGPEAGMGLDGLLrqRADRLSGILNGIDTAVWNPATDELIAATYDVETL-AARAANKAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 390 LQAECGLPVDSNIPVIGFIGRLEEQKGSDILFEAISKFIHLDVQIIVLGTGKKYMEKQIEQLEELYPEKARGIAKFNTPL 469
Cdd:PRK14099 283 LQARFGLDPDPDALLLGVISRLSWQKGLDLLLEALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEAL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 470 AHKIIAGADFIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVI-EGYTGFHAG-AFSVECdavDPADVEKLTSTVI 547
Cdd:PRK14099 363 AHLIQAGADALLVPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVdANEMAIATGvATGVQF---SPVTADALAAALR 439
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1432028620 548 RALTTFGTPV-WKEIVQNCMAQDFSWKEPAKLWEKMLLSL 586
Cdd:PRK14099 440 KTAALFADPVaWRRLQRNGMTTDVSWRNPAQHYAALYRSL 479
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
88-346 |
2.29e-81 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 256.10 E-value: 2.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 88 LFVSAEVGPWSKTGGLGDVLGALPPRLAANGHRVMTVSPRYD-------QYKDAWDTSVLVEIKVgdRVETVRYFHCFKR 160
Cdd:pfam08323 2 LFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGnipeernQLEDVIRLSVAAGVPV--RPLTVGVARLELD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 161 GVDRVFVDHPVFLEKvwgktqSKLYGPKaGEDYADNQFRFSLLCLAALEAPRVLNlnsnpyfsgpYGEDVVfIANDWHTA 240
Cdd:pfam08323 80 GVDVYFLDNPDYFDR------PGLYGDD-GRDYEDNAERFAFFSRAALELAKKLG----------WIPDII-HCHDWHTA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 241 LLPCYLKSMYKSRGIYmNAKVAFCIHNIAYQGRFAFADFPLLGLPDEFRSsfdfMDGYDKPvkgRKINWMKAGIIESDRV 320
Cdd:pfam08323 142 LVPAYLKEAYADDPFK-NIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN----LDGLEFY---GQINFLKAGIVYADAV 213
|
250 260
....*....|....*....|....*.
gi 1432028620 321 VTVSPYYAQELVSGEDrGVELDTIIR 346
Cdd:pfam08323 214 TTVSPTYAEEIQTPEF-GGGLDGLLR 238
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
235-577 |
3.87e-73 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 242.72 E-value: 3.87e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 235 NDWHTALLPCYLKSMYKSRGIYMNAKVAFCIHNIAYQGRFAFADFPLLgLPDEFRSSFDfmdgydkpVKGRKINWMKAGI 314
Cdd:PRK14098 148 HDWYAGLVPLLLKTVYADHEFFKDIKTVLTIHNVYRQGVLPFKVFQKL-LPEEVCSGLH--------REGDEVNMLYTGV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 315 IESDRVVTVSPYYAQELVSGEDRGVELDTII--RSVGITGIRNGMDHREWSPKTDRFISIHYDATTVtEAKCLLKQALQA 392
Cdd:PRK14098 219 EHADLLTTTSPRYAEEIAGDGEEAFGLDKVLeeRKMRLHGILNGIDTRQWNPSTDKLIKKRYSIERL-DGKLENKKALLE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 393 ECGLPVDSNIPVIGFIGRLEEQKGSDILFEAISKFIHLDVQIIVLGTGKKYMEKQIEQLEELYPEKARGIAKFNTPLAHK 472
Cdd:PRK14098 298 EVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFHL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 473 IIAGADFIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTvIEGYTGFHAGAFsvecdAVDPADVEKLTSTVIRALTT 552
Cdd:PRK14098 378 AIAGLDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGIVET-IEEVSEDKGSGF-----IFHDYTPEALVAKLGEALAL 451
|
330 340
....*....|....*....|....*.
gi 1432028620 553 FG-TPVWKEIVQNCMAQDFSWKEPAK 577
Cdd:PRK14098 452 YHdEERWEELVLEAMERDFSWKNSAE 477
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
83-585 |
8.63e-63 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 224.01 E-value: 8.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 83 TGMTFLFVSAEVGPWSKTGGLGDVLGALPPRLAANGHRVMTVSPRYD--QYKDAWDTSVLveikvgdRVETVRYFhcfkr 160
Cdd:PLN02939 480 SGLHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDcmQYDQIRNLKVL-------DVVVESYF----- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 161 gvdrvfvDHPVFLEKVWGKT-------------QSKLY--GPKAGEDyaDNQFRFSLLCLAALEaprvLNLNSnpyfsgp 225
Cdd:PLN02939 548 -------DGNLFKNKIWTGTveglpvyfiepqhPSKFFwrAQYYGEH--DDFKRFSYFSRAALE----LLYQS------- 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 226 yGEDVVFI-ANDWHTALL-PCYLkSMYKSRGiYMNAKVAFCIHNIAYQGRFAFADFPLLGL-------PDEFRSSfdfmd 296
Cdd:PLN02939 608 -GKKPDIIhCHDWQTAFVaPLYW-DLYAPKG-FNSARICFTCHNFEYQGTAPASDLASCGLdvhqldrPDRMQDN----- 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 297 gydkpvKGRKINWMKAGIIESDRVVTVSPYYAQELVSGEDRGVELDTIIRSVGITGIRNGMDHREWSPKTDRFISIHYDA 376
Cdd:PLN02939 680 ------AHGRINVVKGAIVYSNIVTTVSPTYAQEVRSEGGRGLQDTLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNA 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 377 TTVtEAKCLLKQALQAECGLP-VDSNIPVIGFIGRLEEQKGSDILFEAISKFIHLDVQIIVLGTGK-KYMEKQIEQLEEL 454
Cdd:PLN02939 754 NDL-QGKAANKAALRKQLGLSsADASQPLVGCITRLVPQKGVHLIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGIADQ 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 455 YP--EKARGIAKFNTPLAHKIIAGADFIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTViegytgfhagaFSVECD 532
Cdd:PLN02939 833 FQsnNNIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSV-----------FDFDDE 901
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1432028620 533 AVDP----------ADVEKLTSTVIRALTTF--GTPVWKEIVQNCMAQDFSWKEPAKLWEKMLLS 585
Cdd:PLN02939 902 TIPVelrngftfltPDEQGLNSALERAFNYYkrKPEVWKQLVQKDMNIDFSWDSSASQYEELYQR 966
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
76-576 |
4.72e-57 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 207.80 E-value: 4.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 76 VGKIVCETGMTFLFVSAEVGPWSKTGGLGDVLGALPPRLAANGHRVMTVSPRYDQYKDAwdtsvlveikvgdRVETVRYF 155
Cdd:PLN02316 579 FGGIAKEPPMHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLS-------------HVKDLHYQ 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 156 HCFKRGVDRVFV------DHPV-FLEKVWGKTQSK-LYGPKagedyaDNQFRFSLLCLAALEAprVLNLNSNPyfsgpyg 227
Cdd:PLN02316 646 RSYSWGGTEIKVwfgkveGLSVyFLEPQNGMFWAGcVYGCR------NDGERFGFFCHAALEF--LLQSGFHP------- 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 228 eDVVFiANDWHTALLPCYLKSMYKSRGIyMNAKVAFCIHNIayqgrfafadfpllglpdEFrssfdfmdgydkpvkgrKI 307
Cdd:PLN02316 711 -DIIH-CHDWSSAPVAWLFKDHYAHYGL-SKARVVFTIHNL------------------EF-----------------GA 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 308 NWMKAGIIESDRVVTVSPYYAQElVSGEDrgveldTIIRSVG-ITGIRNGMDHREWSPKTDRFISIHYDATTVTEAKCLL 386
Cdd:PLN02316 753 NHIGKAMAYADKATTVSPTYSRE-VSGNS------AIAPHLYkFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAA 825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 387 KQALQAECGLPvDSNIPVIGFIGRLEEQKGSDILFEAISKFIHLDVQIIVLGTGKkymEKQIE--------QLEELYPEK 458
Cdd:PLN02316 826 KEALQQRLGLK-QADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGSAP---DPRIQndfvnlanQLHSSHHDR 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 459 ARGIAKFNTPLAHKIIAGADFIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVIE--------GYTGFHAGAFSVe 530
Cdd:PLN02316 902 ARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTVFDvdhdkeraQAQGLEPNGFSF- 980
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1432028620 531 cDAVDPADVEKLTStviRALTTF--GTPVWKEIVQNCMAQDFSWKEPA 576
Cdd:PLN02316 981 -DGADAAGVDYALN---RAISAWydGRDWFNSLCKRVMEQDWSWNRPA 1024
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
199-583 |
1.27e-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: 105.70 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 199 RFSLLCLAALEAPRVLNLNSNPYFSGPYgeDVVfIANDWHTALLPCYLKSMYKsrgiymnAKVAFCIHNIAYQGRFAFAD 278
Cdd:cd03801 56 PLLPSLAALLRARRLLRELRPLLRLRKF--DVV-HAHGLLAALLAALLALLLG-------APLVVTLHGAEPGRLLLLLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 279 FPLlglpdefrssfdfmdgydkpvkgRKINWMKAGIIESDRVVTVSPYYAQELVsgEDRGVELDTIIRsvgitgIRNGMD 358
Cdd:cd03801 126 AER-----------------------RLLARAEALLRRADAVIAVSEALRDELR--ALGGIPPEKIVV------IPNGVD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 359 HREWSPKTDRfisihydattvteakcllkqalqaecGLPVDSNIPVIGFIGRLEEQKGSDILFEAISKFI--HLDVQIIV 436
Cdd:cd03801 175 LERFSPPLRR--------------------------KLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLrrGPDVRLVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 437 LGTGKKYMEkQIEQLEELYPEKARGIAKFNTPLAHKIIAGADFIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVI 516
Cdd:cd03801 229 VGGDGPLRA-ELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 517 EGYTGFHagafsvecdaVDPADVEKLTSTVIRALTtfGTPVWKEIVQN---CMAQDFSWKEPAKLWEKML 583
Cdd:cd03801 308 DGEGGLV----------VPPDDVEALADALLRLLA--DPELRARLGRAareRVAERFSWERVAERLLDLY 365
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
316-583 |
5.08e-18 |
|
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: 86.28 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 316 ESDRVVTVSPYYAQELVS-GEDRGveldtiirsvGITGIRNGMDhrewspkTDRFisihydattvteakcllkQALQAEC 394
Cdd:cd03798 150 RAARVIAVSKALAEELVAlGVPRD----------RVDVIPNGVD-------PARF------------------QPEDRGL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 395 GLPVDSniPVIGFIGRLEEQKGSDILFEAISKFI--HLDVQIIVLGTG--KKYMEKQIEQLeelypeKARGIAKFNTPLA 470
Cdd:cd03798 195 GLPLDA--FVILFVGRLIPRKGIDLLLEAFARLAkaRPDVVLLIVGDGplREALRALAEDL------GLGDRVTFTGRLP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 471 HKIIAG----ADFIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVIEGYTGFhagafsvecdAVDPADVEKLTSTV 546
Cdd:cd03798 267 HEQVPAyyraCDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGL----------LVPPGDADALAAAL 336
|
250 260 270
....*....|....*....|....*....|....*...
gi 1432028620 547 IRAL-TTFGTPVWKEIVQNcMAQDFSWKepaKLWEKML 583
Cdd:cd03798 337 RRALaEPYLRELGEAARAR-VAERFSWV---KAADRIA 370
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
403-551 |
4.75e-17 |
|
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: 78.47 E-value: 4.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 403 PVIGFIGRLEEQKGSDILFEAISKFI--HLDVQIIVLGTG--KKYMEKQIEQLEelYPEKARGIAKFNTPLAHKIIAGAD 478
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKekNPNLKLVIAGDGeeEKRLKKLAEKLG--LGDNVIFLGFVSDEDLPELLKIAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1432028620 479 FIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVIEGYTGFHagafsvecdaVDPADVEKLTSTVIRALT 551
Cdd:pfam00534 81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFL----------VKPNNAEALAEAIDKLLE 143
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
294-551 |
1.23e-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: 82.29 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 294 FMDGYDKPVKGRKINWMKAGIIESDRVVTVSPYYAQELVS--GEDRgveldtiirsVGITGIRNGMDHREWSPKTDrfis 371
Cdd:cd03800 141 HLGAQDTYHPSLRITAEEQILEAADRVIASTPQEADELISlyGADP----------SRINVVPPGVDLERFFPVDR---- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 372 ihydattvteakcllKQALQAECGLPVDSniPVIGFIGRLEEQKGSDILFEAISKFIHLDVQ---IIVLGTGKKYMEKQI 448
Cdd:cd03800 207 ---------------AEARRARLLLPPDK--PVVLALGRLDPRKGIDTLVRAFAQLPELRELanlVLVGGPSDDPLSMDR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 449 EQLEELyPEKARGIAKFNTPLAHK------IIAGADFIVIPSRFEPCGLVQLHAMPYGTvPIVSS-TGGLVDTVIEGYTG 521
Cdd:cd03800 270 EELAEL-AEELGLIDRVRFPGRVSrddlpeLYRAADVFVVPSLYEPFGLTAIEAMACGT-PVVATaVGGLQDIVRDGRTG 347
|
250 260 270
....*....|....*....|....*....|
gi 1432028620 522 FHagafsvecdaVDPADVEKLTSTVIRALT 551
Cdd:cd03800 348 LL----------VDPHDPEALAAALRRLLD 367
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
403-551 |
5.25e-16 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 74.86 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 403 PVIGFIGRL-EEQKGSDILFEAISKFI--HLDVQIIVLGTGKKymekqiEQLEELYPEKARGIaKFNTPLA--HKIIAGA 477
Cdd:pfam13692 2 PVILFVGRLhPNVKGVDYLLEAVPLLRkrDNDVRLVIVGDGPE------EELEELAAGLEDRV-IFTGFVEdlAELLAAA 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1432028620 478 DFIVIPSRFEPCGLVQLHAMPYGtVPIVSST-GGLVDtVIEGYTGFHagafsvecdaVDPADVEKLTSTVIRALT 551
Cdd:pfam13692 75 DVFVLPSLYEGFGLKLLEAMAAG-LPVVATDvGGIPE-LVDGENGLL----------VPPGDPEALAEAILRLLE 137
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
352-522 |
1.36e-14 |
|
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: 75.47 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 352 GIRNGMDHREWSPKtDRFISIhYDATTVTEAKCLLKQALQAECGlpvdsNIPVIGFIGRLEEQKGSDILFEAISKFI--H 429
Cdd:cd03811 145 GIKEDLIRLGPSPP-EKIEVI-YNPIDIDRIRALAKEPILNEPE-----DGPVILAVGRLDPQKGHDLLIEAFAKLRkkY 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 430 LDVQIIVLGTG--KKYMEKQIEQLeelypekarGIAK------FNTPLAhKIIAGADFIVIPSRFEPCGLVQLHAMPYGT 501
Cdd:cd03811 218 PDVKLVILGDGplREELEKLAKEL---------GLAErviflgFQSNPY-PYLKKADLFVLSSRYEGFPNVLLEAMALGT 287
|
170 180
....*....|....*....|..
gi 1432028620 502 vPIVSS-TGGLVDTVIEGYTGF 522
Cdd:cd03811 288 -PVVSTdCPGPREILDDGENGL 308
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
318-552 |
2.42e-14 |
|
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: 74.70 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 318 DRVVTVSPYYAqelvsgedrgvelDTIIRSVG-----ITGIRNGMDhrewspkTDRFisihyDATTVTEAKCLLKqalqa 392
Cdd:cd03819 128 DRVIAVSELVR-------------DHLIEALGvdperIRVIPNGVD-------TDRF-----PPEAEAEERAQLG----- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 393 ecglpVDSNIPVIGFIGRLEEQKGSDILFEAISKFIH-LDVQIIVLGTG--KKYMEKQIEQLeelypekarGIAKF---- 465
Cdd:cd03819 178 -----LPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDePDFRLLVAGDGpeRDEIRRLVERL---------GLRDRvtft 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 466 -NTPLAHKIIAGADFIVIPSRFEPCGLVQLHAMPYGTvPIVSST-GGLVDTVIEGYTGFhagafsvecdAVDPADVEKLT 543
Cdd:cd03819 244 gFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGT-PVVATDvGGAREIVVHGRTGL----------LVPPGDAEALA 312
|
....*....
gi 1432028620 544 STVIRALTT 552
Cdd:cd03819 313 DAIRAAKLL 321
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
407-522 |
3.39e-14 |
|
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: 72.44 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 407 FIGRLEEQKGSDILFEAISKF--IHLDVQIIVLGTGKKYMEKQIEQLEELYPEKARGIAKF-NTPLAHKIIAGADFIVIP 483
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLkaRLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLvDDEVLELLLAAADVFVLP 194
|
90 100 110
....*....|....*....|....*....|....*....
gi 1432028620 484 SRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVIEGYTGF 522
Cdd:cd01635 195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
469-586 |
2.29e-13 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 66.94 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 469 LAHKIIAGADFIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVIEGYTGFHagafsvecdaVDPADVEKLTSTVIR 548
Cdd:COG0438 13 LLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLL----------VPPGDPEALAEAILR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1432028620 549 ALTTfgTPVWKEIVQNC---MAQDFSWKEPAKLWEKMLLSL 586
Cdd:COG0438 83 LLED--PELRRRLGEAArerAEERFSWEAIAERLLALYEEL 121
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
359-551 |
6.22e-13 |
|
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: 70.44 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 359 HREWSPKTDRFISIHYdATTVTEAKCllkqalqaECGLPVDSNIpVIGFIGRLEEQKGSDILFEAISKFIHLDVQIIVLG 438
Cdd:cd03823 158 HEANGLFSARISVIPN-AVEPDLAPP--------PRRRPGTERL-RFGYIGRLTEEKGIDLLVEAFKRLPREDIELVIAG 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 439 TGkkyMEKQIEQLEELYPEKARGIAKFNTPLAHkiIAGADFIVIPSRF-EPCGLVQLHAMPYGTVPIVSSTGGLVDTVIE 517
Cdd:cd03823 228 HG---PLSDERQIEGGRRIAFLGRVPTDDIKDF--YEKIDVLVVPSIWpEPFGLVVREAIAAGLPVIASDLGGIAELIQP 302
|
170 180 190
....*....|....*....|....*....|....
gi 1432028620 518 GYTGFHagafsvecdaVDPADVEKLTSTVIRALT 551
Cdd:cd03823 303 GVNGLL----------FAPGDAEDLAAAMRRLLT 326
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
396-583 |
3.08e-11 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 65.58 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 396 LPVDSNIPVIGFIGRLEEQKGSDILFEAISKF--IHLDVQIIVLG--TGKKYMEKQIEQLEELYPEKARGiakfntplAH 471
Cdd:PRK15484 187 LNISPDETVLLYAGRISPDKGILLLMQAFEKLatAHSNLKLVVVGdpTASSKGEKAAYQKKVLEAAKRIG--------DR 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 472 KIIAG-------------ADFIVIPSRF-EPCGLVQLHAMPYGTVPIVSSTGGLVDTVIEGYTGFHAGafsvecdavDPA 537
Cdd:PRK15484 259 CIMLGgqppekmhnyyplADLVVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLA---------EPM 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1432028620 538 DVEKLTSTVIRALttfGTPVWKEIVQNcmAQDF-----SWKEPAKLWEKML 583
Cdd:PRK15484 330 TSDSIISDINRTL---ADPELTQIAEQ--AKDFvfskySWEGVTQRFEEQI 375
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
363-548 |
5.64e-11 |
|
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: 64.54 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 363 SPKTDRFISIHYDATTVTEAKCLLKQALQAE---CGLPVD----------SNIPVIGFIGRLEEQKGSDILFEAIS--KF 427
Cdd:cd03808 137 LLFTDKVIFVNEDDRDLAIKKGIIKKKKTVLipgSGVDLDrfqyspeslpSEKVVFLFVARLLKDKGIDELIEAAKilKK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 428 IHLDVQIIVLGTG--KKYMEKQIEQLEelypekARGIAKF-----NTPlahKIIAGADFIVIPSRFEPCGLVQLHAMPYG 500
Cdd:cd03808 217 KGPNVRFLLVGDGelENPSEILIEKLG------LEGRIEFlgfrsDVP---ELLAESDVFVLPSYREGLPRSLLEAMAAG 287
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1432028620 501 TVPIVSSTGGLVDTVIEGYTGFhagafsvecdAVDPADVEKLTSTVIR 548
Cdd:cd03808 288 RPVITTDVPGCRELVIDGVNGF----------LVPPGDVEALADAIEK 325
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
403-544 |
2.56e-10 |
|
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: 62.29 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 403 PVIGFIGRLEEQKGSDILFEAISKfihLDVQIIVLGTG--KKYMEKQIeqlEELYPEKARGIAKF-NTPLAHKIIAgADF 479
Cdd:cd03795 192 KIFLFIGRLVYYKGLDYLIEAAQY---LNYPIVIGGEGplKPDLEAQI---ELNLLDNVKFLGRVdDEEKVIYLHL-CDV 264
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1432028620 480 IVIPS--RFEPCGLVQLHAMPYGtVPIVSST--GGLVDTVIEGYTGFhagafsvecdAVDPADVEKLTS 544
Cdd:cd03795 265 FVFPSvlRSEAFGIVLLEAMMCG-KPVISTNigTGVPYVNNNGETGL----------VVPPKDPDALAE 322
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
408-581 |
9.58e-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: 60.71 E-value: 9.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 408 IGRLEEQKGSDILFEAISKF--IHLDVQIIVLGTG--KKYMEKQIE--QLEE--LYPEKARGIAkfntplahKIIAGADF 479
Cdd:cd03820 187 VGRLTYQKGFDLLIEAWALIakKHPDWKLRIYGDGpeREELEKLIDklGLEDrvKLLGPTKNIA--------EEYANSSI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 480 IVIPSRFEPCGLVQLHAMPYGtVPIVSS--TGGLVDTVIEGYTGFhagafsvecdAVDPADVEKLTSTVIRALTTfgtpv 557
Cdd:cd03820 259 FVLSSRYEGFPMVLLEAMAYG-LPIISFdcPTGPSEIIEDGENGL----------LVPNGDVDALAEALLRLMED----- 322
|
170 180 190
....*....|....*....|....*....|
gi 1432028620 558 wKEIVQNC------MAQDFSWKEPAKLWEK 581
Cdd:cd03820 323 -EELRKKMgknarkNAERFSIEKIIKQWEE 351
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
403-534 |
5.41e-09 |
|
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: 58.46 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 403 PVIGFIGRLEEQKGSDILFEAISKFI-HLDVQIIVLGTGKkymekQIEQLEELYPEKARGIAKFNTPLAhKIIAGADFIV 481
Cdd:cd03814 199 PLLLYVGRLAPEKNLEALLDADLPLAaSPPVRLVVVGDGP-----ARAELEARGPDVIFTGFLTGEELA-RAYASADVFV 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1432028620 482 IPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVIEGYTGF--HAGAFSVECDAV 534
Cdd:cd03814 273 FPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGAlvEPGDAAAFAAAL 327
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
403-550 |
1.31e-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: 57.08 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 403 PVIGFIGRLEEQKGSDILFEAISKFI--HLDVQIIVLGTGkkymeKQIEQLEELypekARGIA--KFNTPLAHKIIA--- 475
Cdd:cd05844 190 PTILFVGRLVEKKGCDVLIEAFRRLAarHPTARLVIAGDG-----PLRPALQAL----AAALGrvRFLGALPHAEVQdwm 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 476 -GADFIVIPSRF------EPCGLVQLHAMPYGtVPIVSST-GGLVDTVIEGYTGFhagafsvecdAVDPADVEKLTSTVI 547
Cdd:cd05844 261 rRAEIFCLPSVTaasgdsEGLGIVLLEAAACG-VPVVSSRhGGIPEAILDGETGF----------LVPEGDVDALADALQ 329
|
...
gi 1432028620 548 RAL 550
Cdd:cd05844 330 ALL 332
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
258-581 |
8.02e-08 |
|
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 54.68 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 258 NAKVAFCIHNIAYqgrFAFADFPLLGLPDEFRSsfdfmdgydkpvkgrkinWMKAGIIESDRVVTVSPYYAQELVSGedR 337
Cdd:cd03809 101 GCPQVVTIHDLIP---LRYPEFFPKRFRLYYRL------------------LLPISLRRADAIITVSEATRDDIIKF--Y 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 338 GVELDTIIrsVgitgIRNGMDHREWSPKTDRFISIHYdattvteakcLLKQalqaecglpvdsniPVIGFIGRLEEQKGS 417
Cdd:cd03809 158 GVPPEKIV--V----IPLGVDPSFFPPESAAVLIAKY----------LLPE--------------PYFLYVGTLEPRKNH 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 418 DILFEAISKFI--HLDVQIIVLGTGKKYMEKQIEQLEELY-PEKARGIAKFNTPLAHKIIAGADFIVIPSRFEPCGLVQL 494
Cdd:cd03809 208 ERLLKAFALLKkqGGDLKLVIVGGKGWEDEELLDLVKKLGlGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 495 HAMPYGTvPIVSSTGGLVDTViegyTGFHAgafsvecDAVDPADVEKLTSTVIRALTTfgTPVWKEIVQNCM--AQDFSW 572
Cdd:cd03809 288 EAMACGT-PVIASNISVLPEV----AGDAA-------LYFDPLDPESIADAILRLLED--PSLREELIRKGLerAKKFSW 353
|
....*....
gi 1432028620 573 KEPAKLWEK 581
Cdd:cd03809 354 EKTAEKTLE 362
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
297-550 |
3.60e-07 |
|
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: 52.74 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 297 GYDKPVKGrKINWmkaGIIESDRVVTVSPYYAQELVS--GEDRGVELdtiirsvgitgIRNGMDHREWSPKTDRfiSIHY 374
Cdd:cd04962 126 GYDPSLQP-AVRF---SINKSDRVTAVSSSLRQETYElfDVDKDIEV-----------IHNFIDEDVFKRKPAG--ALKR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 375 DATTVTEAKCLLKQalqaecglpvdSNI-PVigfigrleeQKGSDIL--FEAISKFIhlDVQIIVLGTG--KKYMEKQIE 449
Cdd:cd04962 189 RLLAPPDEKVVIHV-----------SNFrPV---------KRIDDVVrvFARVRRKI--PAKLLLVGDGpeRVPAEELAR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 450 QLEELypEKARGIAKFNtPLAHkIIAGADFIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVIEGYTGFhagafsv 529
Cdd:cd04962 247 ELGVE--DRVLFLGKQD-DVEE-LLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGF------- 315
|
250 260
....*....|....*....|.
gi 1432028620 530 ecdAVDPADVEKLTSTVIRAL 550
Cdd:cd04962 316 ---LSDVGDVDAMAKSALSIL 333
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
353-551 |
1.08e-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: 51.16 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 353 IRNGMDHrewspktDRFiSIHYDATTVTEAKcllkqalqaecgLPVDSNIPVIGFIGRLEEQKGSDILFEAISKFIHLDV 432
Cdd:cd03807 161 IYNGIDL-------FKL-SPDDASRARARRR------------LGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 433 QIIVLGTGKKYMEKQIEQLEElypekargiakfNTPLAHKII-AG-----------ADFIVIPSRFEPCGLVQLHAMPYG 500
Cdd:cd03807 221 DLRLLLVGRGPERPNLERLLL------------ELGLEDRVHlLGersdvpallpaMDIFVLSSRTEGFPNALLEAMACG 288
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1432028620 501 TVPIVSSTGGLVDTVIEGyTGFhagafsvecdAVDPADVEKLtSTVIRALT 551
Cdd:cd03807 289 LPVVATDVGGAAELVDDG-TGF----------LVPAGDPQAL-ADAIRALL 327
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
401-518 |
1.22e-06 |
|
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: 50.83 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 401 NIPVIGFIGRLEEQKGSDILFEAISKFI--HLDVQIIVLGTGkkymekqieqlEELYPEKARGIAKFNtpLAHKI----- 473
Cdd:cd03821 203 DRRIILFLGRIHPKKGLDLLIRAARKLAeqGRDWHLVIAGPD-----------DGAYPAFLQLQSSLG--LGDRVtftgp 269
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1432028620 474 ---------IAGADFIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVIEG 518
Cdd:cd03821 270 lygeakwalYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG 323
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
404-516 |
3.16e-05 |
|
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: 46.51 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 404 VIGFIGRLEEQKGSDILFEAISKFI--HLDVQIIVLGTGKKyMEKQIEQLEELypekarGIAK------FNTPLaHKIIA 475
Cdd:cd03812 193 VLGHVGRFNEQKNHSFLIDIFEELKkkNPNVKLVLVGEGEL-KEKIKEKVKEL------GLEDkviflgFRNDV-SEILS 264
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1432028620 476 GADFIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLvDTVI 516
Cdd:cd03812 265 AMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITK-ECDI 304
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
396-523 |
4.08e-05 |
|
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: 46.12 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 396 LPVDSNIPVIGFIGRLEEQKGSDILFEAISKFIHL-DVQIIVLGTG--KKYMEKQIEQLeelypeKARGIAKFNTPLAHK 472
Cdd:cd03817 195 LGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEpNIKLVIVGDGpeREELKELAREL------GLADKVIFTGFVPRE 268
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1432028620 473 II----AGADFIVIPSRFEPCGLVQLHAMPYGtVPIVS-STGGLVDTVIEGYTGFH 523
Cdd:cd03817 269 ELpeyyKAADLFVFASTTETQGLVYLEAMAAG-LPVVAaKDPAASELVEDGENGFL 323
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
387-530 |
1.75e-03 |
|
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: 41.16 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 387 KQALQAECGLPVDSNIPVIGFIGRLEEQKGSDILFEAISKFIHLD-VQIIVLGtgkkYMEKQIEQLeelyPEKARGIAKF 465
Cdd:cd03825 180 KAKARKRLGIPQDKKVILFGAESVTKPRKGFDELIEALKLLATKDdLLLVVFG----KNDPQIVIL----PFDIISLGYI 251
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1432028620 466 -NTPLAHKIIAGADFIVIPSRFEPCGLVQLHAMPYGTVPIVSSTGGLVDTVIEGYTGFHAGAFSVE 530
Cdd:cd03825 252 dDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQ 317
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
403-541 |
2.19e-03 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 40.85 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 403 PVIGFIGRLEEQKGSDILFEAISKFIhlDVQIIVLGTGKkymekQIEQLEELYpekaRGIAKFNTPLAH-----KIIAGA 477
Cdd:PLN02871 264 PLIVYVGRLGAEKNLDFLKRVMERLP--GARLAFVGDGP-----YREELEKMF----AGTPTVFTGMLQgdelsQAYASG 332
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1432028620 478 DFIVIPSRFEPCGLVQLHAMPYGtVPIVSS-TGGLVDTV---IEGYTGFhagafsvecdAVDPADVEK 541
Cdd:PLN02871 333 DVFVMPSESETLGFVVLEAMASG-VPVVAArAGGIPDIIppdQEGKTGF----------LYTPGDVDD 389
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
409-531 |
4.19e-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: 39.58 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432028620 409 GRLEEQKGSDILFEAISKfihLDVQIIVLGTGkkymekqiEQLEELypekaRGIAKFNTPLA--------HKIIAGADFI 480
Cdd:cd03804 206 SRLVPYKRIDLAVEAFNE---LPKRLVVIGDG--------PDLDRL-----RAMASPNVEFLgyqpdevlKELLSKARAF 269
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1432028620 481 VIPSRfEPCGLVQLHAMPYGTVPIVSSTGGLVDTVIEGYTGFHAGAFSVEC 531
Cdd:cd03804 270 VFAAE-EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVES 319
|
|
| |
