|
Name |
Accession |
Description |
Interval |
E-value |
| wcaI |
TIGR04007 |
colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl ... |
1-407 |
0e+00 |
|
colanic acid biosynthesis glycosyl transferase WcaI; This gene is one of the glycosyl transferases involved in the biosynthesis of colanic acid, an exopolysaccharide expressed in Enterobacteraceae species.
Pssm-ID: 188522 [Multi-domain] Cd Length: 407 Bit Score: 871.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKREEGAATVWRCPLYVPKQPST 80
Cdd:TIGR04007 1 MKILVYGINYSPELTGIGKYTGEMVEWMARQGHEVRVITAPPYYPQWKVGENYSAWRYRREEGAATVWRCPLYVPKQPST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 81 LKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVA 160
Cdd:TIGR04007 81 LKRLLHLGSFALSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGMAGKGKGGKVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 161 QLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQHVADADVDALRNQLGLPDNKKIILYSGNI 240
Cdd:TIGR04007 161 RLASAFERSGLHNVDNVSTISRSMMNKAQEKGVAAEKVIFFPNWSEVARFRDVKDADVEALRSQLGLPDDKKIILYSGNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 241 GEKQGLENVIEAADRLRDEPLIFAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAADAV 320
Cdd:TIGR04007 241 GEKQGLENVIDAAARLTDRPWIFAIVGQGGGKARLEKMARERGLTNVKFFPLQPYEALPALLKMGDCHLVVQKRGAADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 321 LPSKLTNILAVGGNAVITAEAHTELGQLCETFPGIAVCVEPESVEALVAGIRQALLLPKYNTVAREYAERTLDKENVLRQ 400
Cdd:TIGR04007 321 LPSKLTNILAVGGNAVITAEPHTELGQLCITYPGIAVCVEPESVDALVAGIVQALAMPKNNTVAREYAERTLEKENVLRQ 400
|
....*..
gi 1730355522 401 FINDIRG 407
Cdd:TIGR04007 401 FIADIRG 407
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
1-407 |
0e+00 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 729.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKRE-EGAATVWRCPLYVPKQPS 79
Cdd:PRK10307 1 MKILVYGINYAPELTGIGKYTGEMAEWLAARGHEVRVITAPPYYPQWRVGEGYSAWRYRREsEGGVTVWRCPLYVPKQPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 80 TLKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMlglGLAGKGKGGKV 159
Cdd:PRK10307 81 GLKRLLHLGSFALSSFFPLLAQRRWRPDRVIGVVPTLFCAPGARLLARLSGARTWLHIQDYEVDAA---FGLGLLKGGKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 160 AQLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQHVADADVDALRNQLGLPDNKKIILYSGN 239
Cdd:PRK10307 158 ARLATAFERSLLRRFDNVSTISRSMMNKAREKGVAAEKVIFFPNWSEVARFQPVADADVDALRAQLGLPDGKKIVLYSGN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 240 IGEKQGLENVIEAADRLRDEP-LIFAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAAD 318
Cdd:PRK10307 238 IGEKQGLELVIDAARRLRDRPdLIFVICGQGGGKARLEKMAQCRGLPNVHFLPLQPYDRLPALLKMADCHLLPQKAGAAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 319 AVLPSKLTNILAVGGNAVITAEAHTELGQLCEtfpGIAVCVEPESVEALVAGI----RQALLLPKYNTVAREYAERTLDK 394
Cdd:PRK10307 318 LVLPSKLTNMLASGRNVVATAEPGTELGQLVE---GIGVCVEPESVEALVAAIaalaRQALLRPKLGTVAREYAERTLDK 394
|
410
....*....|...
gi 1730355522 395 ENVLRQFINDIRG 407
Cdd:PRK10307 395 ENVLRQFIADIRG 407
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-402 |
5.26e-81 |
|
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
Pssm-ID: 340825 [Multi-domain] Cd Length: 391 Bit Score: 254.19 E-value: 5.26e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWqvgenYSAWRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03794 1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLG-----RIFAGATETKDGIRVIRVKLGPIKKNGLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 82 KRLLHLGSFAVSSFFPLMAqRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVAQ 161
Cdd:cd03794 76 RRLLNYLSFALAALLKLLV-REERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKKGSLLKLLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 162 LataFERSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQhvaDADVDALRnQLGLPDNKKIILYSGNIG 241
Cdd:cd03794 155 K---LERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFK---PPPKDELR-KKLGLDDKFVVVYAGNIG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 242 EKQGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAA-DA 319
Cdd:cd03794 228 KAQGLETLLEAAERLKRRPDIrFLFVGDGDEKERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLVPLKDNPAnRG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 320 VLPSKLTNILAVGGNAVITAEAHTELGQLCEtfpGIAVCVEPESVEALVAGIRQALLLP----KYNTVAREYAERTLDKE 395
Cdd:cd03794 308 SSPSKLFEYMAAGKPILASDDGGSDLAVEIN---GCGLVVEPGDPEALADAILELLDDPelrrAMGENGRELAEEKFSRE 384
|
....*..
gi 1730355522 396 NVLRQFI 402
Cdd:cd03794 385 KLADRLL 391
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
230-390 |
1.59e-23 |
|
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: 95.80 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 230 NKKIILYSGNIGEKQGLENVIEAADRLR--DEPLIFAIVGQGGGKARLEKMAQQRGLRNMQFFPL-QSYDALPALLKMgd 306
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKekNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGfVSDEDLPELLKI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 307 CHLVVQKrgAADAVLPSKLTNILAVGGnAVITAEAHTELGQLCETFPGiaVCVEPESVEALVAGIRQALLLPKYNTVARE 386
Cdd:pfam00534 79 ADVFVLP--SRYEGFGIVLLEAMACGL-PVIASDVGGPPEVVKDGETG--FLVKPNNAEALAEAIDKLLEDEELRERLGE 153
|
....
gi 1730355522 387 YAER 390
Cdd:pfam00534 154 NARK 157
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
15-204 |
3.68e-20 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 86.69 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 15 TGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQvgenysawrykREEGAATVWRCPL-YVPKQPSTLKRLLHLGSFAvs 93
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPE-----------LVGDGVRVHRLPVpPRPSPLADLAALRRLRRLL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 94 sffplmaqRRWKPDRIIGVVPTLFctPGMRLLAKLSGARTVLHIQDYEVDamlglglagkGKGGKVAQLATAFERSGLHN 173
Cdd:pfam13579 68 --------RAERPDVVHAHSPTAG--LAARLARRRRGVPLVVTVHGLALD----------YGSGWKRRLARALERRLLRR 127
|
170 180 190
....*....|....*....|....*....|.
gi 1730355522 174 VDNVSTISRSMMNKAIEKGVAADNIIFFPNW 204
Cdd:pfam13579 128 ADAVVVVSEAEAELLRALGVPAARVVVVPNG 158
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-406 |
1.35e-19 |
|
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: 89.52 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYypqwqvgenysawRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03801 1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADP-------------GEPPEELEDGVIVPLLPSLAALLRA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 82 KRLLHLGSFAVssffplmaqRRWKPDRIIgvVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKggkvaq 161
Cdd:cd03801 68 RRLLRELRPLL---------RLRKFDVVH--AHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRL------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 162 LATAFERsgLHNVDNVSTISRSMMNKAIEKGVA-ADNIIFFPNWSEIARFQhvadadvDALRNQLGLPDNKKIILYSGNI 240
Cdd:cd03801 131 LARAEAL--LRRADAVIAVSEALRDELRALGGIpPEKIVVIPNGVDLERFS-------PPLRRKLGIPPDRPVLLFVGRL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 241 GEKQGLENVIEAADRLRDE--PLIFAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDChlvvqkrgaad 318
Cdd:cd03801 202 SPRKGVDLLLEALAKLLRRgpDVRLVIVGGDGPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADV----------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 319 AVLPSKLTNIlavgGNAVITAEAH------TELGQLCETFP--GIAVCVEPESVEALVAGIRQAL----LLPKYNTVARE 386
Cdd:cd03801 271 FVLPSRYEGF----GLVVLEAMAAglpvvaTDVGGLPEVVEdgEGGLVVPPDDVEALADALLRLLadpeLRARLGRAARE 346
|
410 420
....*....|....*....|
gi 1730355522 387 YAERTLDKENVLRQFINDIR 406
Cdd:cd03801 347 RVAERFSWERVAERLLDLYR 366
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
15-395 |
5.34e-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: 84.74 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 15 TGIGKYTGEMVEWLAAQGHEVRVITAPPYYPqwqvgenySAWRYKREEGAATVWRCPLYVPKQPStlKRLLHLGSFAVSS 94
Cdd:cd03798 14 PGRGIFVRRQVRALSRRGVDVEVLAPAPWGP--------AAARLLRKLLGEAVPPRDGRRLLPLK--PRLRLLAPLRAPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 95 FFPLMAQ-RRWKPDRI--IGVVPTLFctpGMRLLAKLSGARTVL-----HIQDYEVDamlglglagkgkggkvaQLATAF 166
Cdd:cd03798 84 LAKLLKRrRRGPPDLIhaHFAYPAGF---AAALLARLYGVPYVVtehgsDINVFPPR-----------------SLLRKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 167 ERSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQHVADAdvdalrnqLGLPDNKKIILYSGNIGEKQGL 246
Cdd:cd03798 144 LRWALRRAARVIAVSKALAEELVALGVPRDRVDVIPNGVDPARFQPEDRG--------LGLPLDAFVILFVGRLIPRKGI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 247 ENVIEAADRLRDE--PLIFAIVGQGGGKARLEKMAQQRGLRN-MQFFPLQSYDALPALLKmgdchlvvqkrgAADA-VLP 322
Cdd:cd03798 216 DLLLEAFARLAKArpDVVLLIVGDGPLREALRALAEDLGLGDrVTFTGRLPHEQVPAYYR------------ACDVfVLP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 323 SkltniLAVG-GNAVITAEA------HTELGQLCE--TFPGIAVCVEPESVEALVAGIRQALLLPkYNTVAREYAERTLD 393
Cdd:cd03798 284 S-----RHEGfGLVLLEAMAcglpvvATDVGGIPEvvGDPETGLLVPPGDADALAAALRRALAEP-YLRELGEAARARVA 357
|
..
gi 1730355522 394 KE 395
Cdd:cd03798 358 ER 359
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
26-390 |
6.39e-16 |
|
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: 78.47 E-value: 6.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 26 EWLAAQGHEVRVITapPYYPQWQVGENYSAWRYKREEGAATVWRCpLYVPKQPSTLKRLlhlgsfavssffplmaqRRWK 105
Cdd:cd03817 25 RALEKRGHEVYVIT--PSDPGAEDEEEVVRYRSFSIPIRKYHRQH-IPFPFKKAVIDRI-----------------KELG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 106 PDRI-------IGVVptlfctpGMRLlAKLSGARTV--LHIQdYEVDAmLGLGLAGKGKGGKVAQLATAFersgLHNVDN 176
Cdd:cd03817 85 PDIIhthtpfsLGKL-------GLRI-ARKLKIPIVhtYHTM-YEDYL-HYIPKGKLLVKAVVRKLVRRF----YNHTDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 177 VSTISRSMMNKAIEKGVAaDNIIFFPNWSEIARFQHVADadvDALRNQLGLPDNKKIILYSGNIGEKQGLENVIEAADRL 256
Cdd:cd03817 151 VIAPSEKIKDTLREYGVK-GPIEVIPNGIDLDKFEKPLN---TEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 257 RDEPLIFA-IVGQGGGKARLEKMAQQRGL-RNMQFFPLQSYDALPALLKMGDCH----------LVVQKrgAADAVLPsk 324
Cdd:cd03817 227 KKEPNIKLvIVGDGPEREELKELARELGLaDKVIFTGFVPREELPEYYKAADLFvfasttetqgLVYLE--AMAAGLP-- 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730355522 325 ltnILAVGGNAVITAEAHTELGQLCETfpgiavcvEPESVEALVAGIRQAL-LLPKYNTVAREYAER 390
Cdd:cd03817 303 ---VVAAKDPAASELVEDGENGFLFEP--------NDETLAEKLLHLRENLeLLRKLSKNAEISARE 358
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
7-379 |
2.93e-10 |
|
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: 61.23 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 7 GINYSPE---LTGIGKYTGEMVEWLAAQGHEVRVITAPPYypqwqvgenysawryKREEGAATVWRCPLYVPKQPSTLKR 83
Cdd:cd03809 3 LIDGRSLaqrLTGIGRYTRELLKALAKNDPDESVLAVPPL---------------PGELLRLLREYPELSLGVIKIKLWR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 84 LLHLgsfavssffplmaQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVAQLA 163
Cdd:cd03809 68 ELAL-------------LRWLQILLPKKDKPDLLHSPHNTAPLLLKGCPQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 164 TafersgLHNVDNVSTISRSMMNKAIEK-GVAADNIIFFPNwsEIARFQHVADADvDALRNQLGLPDnkKIILYSGNIGE 242
Cdd:cd03809 135 S------LRRADAIITVSEATRDDIIKFyGVPPEKIVVIPL--GVDPSFFPPESA-AVLIAKYLLPE--PYFLYVGTLEP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 243 KQGLENVIEAADRLRDE--PLIFAIVGQGGGK-ARLEKMAQQRGLR-NMQFFPLQSYDALPALLKmgdchlvvqkrgAAD 318
Cdd:cd03809 204 RKNHERLLKAFALLKKQggDLKLVIVGGKGWEdEELLDLVKKLGLGgRVRFLGYVSDEDLPALYR------------GAR 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730355522 319 A-VLPSkltniLAVG-----------GNAVITA--EAHTELGqlcetfPGIAVCVEPESVEALVAGIRQALLLPK 379
Cdd:cd03809 272 AfVFPS-----LYEGfglpvleamacGTPVIASniSVLPEVA------GDAALYFDPLDPESIADAILRLLEDPS 335
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
164-395 |
1.06e-09 |
|
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: 59.69 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 164 TAFERSGLHNVDNVSTISRSMMNKAIEKGVAADnIIFFPNWSEIARFqHVADADvdalRNQLGLPDNKKIILYSGNIGEK 243
Cdd:cd03821 143 HLIERRNLNNAALVHFTSEQEADELRRFGLEPP-IAVIPNGVDIPEF-DPGLRD----RRKHNGLEDRRIILFLGRIHPK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 244 QGLENVIEAADRLRDEPL--IFAIVGQGGGkARLEKMAQQR--GLRNMQFFPLQSY-DALPALLKMGDCHlvvqkrgaad 318
Cdd:cd03821 217 KGLDLLIRAARKLAEQGRdwHLVIAGPDDG-AYPAFLQLQSslGLGDRVTFTGPLYgEAKWALYASADLF---------- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 319 aVLPSKLTNI-------LAVGGNAVITAEAHtelgqLCETF-PGIAVCVEPEsVEALVAGIRQALLLPKYNTVAREYAER 390
Cdd:cd03821 286 -VLPSYSENFgnvvaeaLACGLPVVITDKCG-----LSELVeAGCGVVVDPN-VSSLAEALAEALRDPADRKRLGEMARR 358
|
....*
gi 1730355522 391 TLDKE 395
Cdd:cd03821 359 ARQVE 363
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
191-391 |
2.32e-08 |
|
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.
Pssm-ID: 340849 [Multi-domain] Cd Length: 370 Bit Score: 55.47 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 191 KGVAADNIIFFPNWSEIARFQHVADadvdalRNQLGLPDNKKIILYSGNIGEKQGLENVIEAADRLRDE--PLIFAIVG- 267
Cdd:cd03822 153 KLIPAVNIEVIPHGVPEVPQDPTTA------LKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEfpDVRLVIAGe 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 268 ------QGGGKARLEKMAQQRGLRNMQFFPLQSY--DALPALLKMgdCHLVVQ-----KRGAADAVlpskltnILAVG-G 333
Cdd:cd03822 227 lhpslaRYEGERYRKAAIEELGLQDHVDFHNNFLpeEEVPRYISA--ADVVVLpylntEQSSSGTL-------SYAIAcG 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1730355522 334 NAVITaeahTELGQLCETFPGIA-VCVEPESVEALVAGIRQALLLPKYntvAREYAERT 391
Cdd:cd03822 298 KPVIS----TPLRHAEELLADGRgVLVPFDDPSAIAEAILRLLEDDER---RQAIAERA 349
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
2-403 |
3.91e-08 |
|
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: 54.64 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 2 KILVYGINYSPELT-GIGKYTGEMVEWLAAQGHEVRVITAPPYyPQWQVGENYSAWRYKReegaatvwrcPLYVPKQPST 80
Cdd:cd03823 1 KILLVNSLYPPQRVgGAEISVHDLAEALVAEGHEVAVLTAGVG-PPGQATVARSVVRYRR----------APDETLPLAL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 81 LKRLLHLGSFAVSSFFPLMAQ--RRWKPDRI-----IGVvptlfctpGMRLL--AKLSGARTVLHIQDYEVDAMlglgla 151
Cdd:cd03823 70 KRRGYELFETYNPGLRRLLARllEDFRPDVVhthnlSGL--------GASLLdaARDLGIPVVHTLHDYWLLCP------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 152 gkgkggkvaqlatafeRSGL--HNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARfqhvadadvdALRNQLGLPD 229
Cdd:cd03823 136 ----------------RQFLfkKGGDAVLAPSRFTANLHEANGLFSARISVIPNAVEPDL----------APPPRRRPGT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 230 NKKIILYSGNIGEKQGLENVIEAADRLRDEPLIFAIVgqggGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDChl 309
Cdd:cd03823 190 ERLRFGYIGRLTEEKGIDLLVEAFKRLPREDIELVIA----GHGPLSDERQIEGGRRIAFLGRVPTDDIKDFYEKIDV-- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 310 vvqkrgaadAVLPSK--------LTNILAVGGNaVIT------AEA--HTELGQLCetfpgiavcvEPESVEALVAGIRQ 373
Cdd:cd03823 264 ---------LVVPSIwpepfglvVREAIAAGLP-VIAsdlggiAELiqPGVNGLLF----------APGDAEDLAAAMRR 323
|
410 420 430
....*....|....*....|....*....|
gi 1730355522 374 ALLLPKYNTVAREYAERTLDKENVLRQFIN 403
Cdd:cd03823 324 LLTDPALLERLRAGAEPPRSTESQAEEYLK 353
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
8-379 |
4.24e-08 |
|
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: 54.67 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 8 INYSPELTGIGKYTGEMVEWLAAQGHEVRVITAppyypqwqvgenysawrykreeGAATVWRCPLYVPKQPSTLKRLLHL 87
Cdd:cd03819 4 LTPALEIGGAETYILDLARALAERGHRVLVVTA----------------------GGPLLPRLRQIGIGLPGLKVPLLRA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 88 GSFAVSSFFPLmaqRRWKPDrIIGV---VPTLFCtpgmRLLAKLSGARTVLHIQDyevdamlglglagkgkGGKVAQLAT 164
Cdd:cd03819 62 LLGNVRLARLI---RRERID-LIHAhsrAPAWLG----WLASRLTGVPLVTTVHG----------------SYLATYHPK 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 165 AFERSGLHNVDNVSTISRSMMNKAIEK-GVAADNIIFFPNWSEIARFQHVADAdvdALRNQLGLPDNKKIILYSGNIGEK 243
Cdd:cd03819 118 DFALAVRARGDRVIAVSELVRDHLIEAlGVDPERIRVIPNGVDTDRFPPEAEA---EERAQLGLPEGKPVVGYVGRLSPE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 244 QGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKMAQQRGLRNmQFFPLQSYDALPALlkMGDCHLVvqkrgaadaVLP 322
Cdd:cd03819 195 KGWLLLVDAAAELKDEPDFrLLVAGDGPERDEIRRLVERLGLRD-RVTFTGFREDVPAA--LAASDVV---------VLP 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730355522 323 SkLTNILavgGNAVITAEAH------TELGQLCETFPG--IAVCVEPESVEALVAGIRQALLLPK 379
Cdd:cd03819 263 S-LHEEF---GRVALEAMACgtpvvaTDVGGAREIVVHgrTGLLVPPGDAEALADAIRAAKLLPE 323
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
2-278 |
5.33e-08 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340842 [Multi-domain] Cd Length: 365 Bit Score: 54.22 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVIT-APPYYPQWQVGENYSAWRykreegaatvWRCPLY------V 74
Cdd:cd03814 1 RIALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVApGPFDEAESAEGRVVSVPS----------FPLPFYpeyrlaL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 75 PKQPSTLKR-------LLHLGSFAVSSFFPLMAQRRWKPDrIIGVVPTLFCTPGM-RLLAKLSGartvlhiqdyevdaml 146
Cdd:cd03814 71 PLPRRVRRLikefqpdIIHIATPGPLGLAALRAARRLGLP-VVTSYHTDFPEYLSyYTLGPLSW---------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 147 glglagkgkggkvaqLATAFERSgLHN-VDNVSTISRSMMNKAIEKGVAadNIIFFPNWSEIARFqHVADADvDALRNQL 225
Cdd:cd03814 134 ---------------LAWAYLRW-FHNpFDTTLVPSPSIARELEGHGFE--RVRLWPRGVDTELF-HPSRRD-AALRRRL 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1730355522 226 GlPDNKKIILYSGNIGEKQGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKM 278
Cdd:cd03814 194 G-PPGRPLLLYVGRLAPEKNLEALLDADLPLAASPPVrLVVVGDGPARAELEAR 246
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
190-388 |
7.23e-08 |
|
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: 53.86 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 190 EKGVAADNIIFFPNWSEIARFqHVADADVDALRNQLGLPDNKKIILYSGNIGEKQGLENVIEAADRLRDEP--LIFAIVG 267
Cdd:cd03807 150 EQGYAKNKIVVIYNGIDLFKL-SPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHpdLRLLLVG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 268 QGGGKARLEKMAQQRGLRNMQFFPLQSYDaLPALLKmgdchlvvqkrgAADA-VLPSK---LTNILA------------- 330
Cdd:cd03807 229 RGPERPNLERLLLELGLEDRVHLLGERSD-VPALLP------------AMDIfVLSSRtegFPNALLeamacglpvvatd 295
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1730355522 331 VGGNAVItaeahtelgqLCetfPGIAVCVEPESVEALVAGIRQALLLPKYNTVAREYA 388
Cdd:cd03807 296 VGGAAEL----------VD---DGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAA 340
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
2-291 |
8.39e-07 |
|
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: 50.43 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 2 KILVygINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAppyypqwqvgeNYSAWRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03811 1 KILF--VIPSLSGGGAERVLLNLANALDKRGYDVTLVLL-----------RDEGDLDKQLNGDVKLIRLLIRVLKLIKLG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 82 KRLLHLgsfavssFFPLMAQRRwKPDRIIGvvptlFCTPGMRLLAKLSGARTVLHIqdYEVDAMLGLGLAgkgkggkvaQ 161
Cdd:cd03811 68 LLKAIL-------KLKRILKRA-KPDVVIS-----FLGFATYIVAKLAAARSKVIA--WIHSSLSKLYYL---------K 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 162 LATAFERSGLHNVDNVSTISRSMMNKAIEKG-VAADNIIFFPNwseiarFQHVADADVDALRNQLGLPDNKKIILYSGNI 240
Cdd:cd03811 124 KKLLLKLKLYKKADKIVCVSKGIKEDLIRLGpSPPEKIEVIYN------PIDIDRIRALAKEPILNEPEDGPVILAVGRL 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1730355522 241 GEKQGLENVIEAADRLRDE--PLIFAIVGQGGGKARLEKMAQQRGLRNMQFFP 291
Cdd:cd03811 198 DPQKGHDLLIEAFAKLRKKypDVKLVILGDGPLREELEKLAKELGLAERVIFL 250
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
16-203 |
6.18e-06 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 45.99 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 16 GIGKYTGEMVEWLAAQGHEVRVIT---APPYYPQWQVGENYSAWRYKREEGaatvwrcPLYVPKQPSTLKRLLhlgsfav 92
Cdd:pfam13439 2 GVERYVLELARALARRGHEVTVVTpggPGPLAEEVVRVVRVPRVPLPLPPR-------LLRSLAFLRRLRRLL------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 93 ssffplmaqRRWKPDRIIGVVPTLFCTpGMRLLAKLSGARTV--LHiqdyevdAMLGLGLAGKGKGGKVAQLATAFERSG 170
Cdd:pfam13439 68 ---------RRERPDVVHAHSPFPLGL-AALAARLRLGIPLVvtYH-------GLFPDYKRLGARLSPLRRLLRRLERRL 130
|
170 180 190
....*....|....*....|....*....|....
gi 1730355522 171 LHNVDNVSTISRSMMNKAIEK-GVAADNIIFFPN 203
Cdd:pfam13439 131 LRRADRVIAVSEAVADELRRLyGVPPEKIRVIPN 164
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
180-335 |
2.84e-05 |
|
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: 45.91 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 180 ISRSMMNKAIEKGVAADNIIFFPNWSEIARFqHVADADVDALRnqlglpdnkkiILYSGNIGEKQGLENVIEA----ADR 255
Cdd:cd05844 150 VSGFIRDRLLARGLPAERIHVHYIGIDPAKF-APRDPAERAPT-----------ILFVGRLVEKKGCDVLIEAfrrlAAR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 256 LRDEPLIfaIVGQGGGKARLEKMAqqRGLRNMQFFPLQSYDALPALLkmgdchlvvqkRGAADAVLPSkltnILAVGGNA 335
Cdd:cd05844 218 HPTARLV--IAGDGPLRPALQALA--AALGRVRFLGALPHAEVQDWM-----------RRAEIFCLPS----VTAASGDS 278
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
159-324 |
6.14e-05 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 44.78 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 159 VAQLATAFERSGLHNvdNVSTISRSMMNKAIEKGVAAD-NIIFFPNWSEIARFQHvadADVDALRNQLGLPDNKKIILYS 237
Cdd:PRK15484 125 VMHMHNAFEPELLDK--NAKIIVPSQFLKKFYEERLPNaDISIVPNGFCLETYQS---NPQPNLRQQLNISPDETVLLYA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 238 GNIGEKQGLENVIEAADRLRDEP--LIFAIVGQGGGKARLEKMAQQRGLRNM--------------------QFFPLQSY 295
Cdd:PRK15484 200 GRISPDKGILLLMQAFEKLATAHsnLKLVVVGDPTASSKGEKAAYQKKVLEAakrigdrcimlggqppekmhNYYPLADL 279
|
170 180
....*....|....*....|....*....
gi 1730355522 296 DALPALLKMGDCHLVVQKRGAADAVLPSK 324
Cdd:PRK15484 280 VVVPSQVEEAFCMVAVEAMAAGKPVLAST 308
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
231-307 |
1.48e-04 |
|
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: 43.42 E-value: 1.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730355522 231 KKIILYSGNIGEKQGLENVIEAADRLrDEPLIfaIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDC 307
Cdd:cd03795 191 KKIFLFIGRLVYYKGLDYLIEAAQYL-NYPIV--IGGEGPLKPDLEAQIELNLLDNVKFLGRVDDEEKVIYLHLCDV 264
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
231-375 |
6.43e-04 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 39.80 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 231 KKIILYSGNIGEKQ-GLENVIEAADRLRDEP--LIFAIVGqGGGKARLEKMAqqRGLRNmQFFPLQSYDALPALLKMGDC 307
Cdd:pfam13692 1 RPVILFVGRLHPNVkGVDYLLEAVPLLRKRDndVRLVIVG-DGPEEELEELA--AGLED-RVIFTGFVEDLAELLAAADV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730355522 308 hlvvqkrgaadAVLPSKLTNIlavgGNAVITAEAH------TELGQLCETFPGIA-VCVEPESVEALVAGIRQAL 375
Cdd:pfam13692 77 -----------FVLPSLYEGF----GLKLLEAMAAglpvvaTDVGGIPELVDGENgLLVPPGDPEALAEAILRLL 136
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
168-309 |
1.36e-03 |
|
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: 40.41 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 168 RSGLHNVDNVSTISRSMMNKAIEKGVAADNIIFFPNWSEIARFQHVADadvDALRNQLGLPDNKKIILYSGNIGEKQGLE 247
Cdd:cd04962 136 RFSINKSDRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKPA---GALKRRLLAPPDEKVVIHVSNFRPVKRID 212
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730355522 248 NVIEAADRLRDE-PLIFAIVGQGGGKARLEKMAQQRGLRNMQFFpLQSYDALPALLKMGDCHL 309
Cdd:cd04962 213 DVVRVFARVRRKiPAKLLLVGDGPERVPAEELARELGVEDRVLF-LGKQDDVEELLSIADLFL 274
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| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
216-386 |
2.75e-03 |
|
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: 39.53 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 216 ADVDALRNQLGLPDNKKIILYSGNIGEKQGLENVIEAA--DRLRDEPLIFAIVG--QGGGKAR----LEKMAQQRGLRNM 287
Cdd:cd03800 205 DRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFaqLPELRELANLVLVGgpSDDPLSMdreeLAELAEELGLIDR 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730355522 288 -QFFPLQSYDALPALLKmgdchlvvqkrgAADA-VLPSK-----LTNILA-----------VGGNAVITAEAHTelGQLc 349
Cdd:cd03800 285 vRFPGRVSRDDLPELYR------------AADVfVVPSLyepfgLTAIEAmacgtpvvataVGGLQDIVRDGRT--GLL- 349
|
170 180 190
....*....|....*....|....*....|....*..
gi 1730355522 350 etfpgiavcVEPESVEALVAGIRQALLLPKYNTVARE 386
Cdd:cd03800 350 ---------VDPHDPEALAAALRRLLDDPALWQRLSR 377
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