|
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: 866.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKREEGAATVWRCPLYVPKQPST 80
Cdd:TIGR04007 1 MKILVYGINYSPELTGIGKYTGEMVEWMARQGHEVRVITAPPYYPQWKVGENYSAWRYRREEGAATVWRCPLYVPKQPST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 81 LKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCAPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVA 160
Cdd:TIGR04007 81 LKRLLHLGSFALSSFFPLMAQRRWKPDRIIGVVPTLFCTPGMRLLAKLSGARTVLHIQDYEVDAMLGLGMAGKGKGGKVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 161 QLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQHVADADVDALRNQLDLPDNKKIILYSGNI 240
Cdd:TIGR04007 161 RLASAFERSGLHNVDNVSTISRSMMNKAQEKGVAAEKVIFFPNWSEVARFRDVKDADVEALRSQLGLPDDKKIILYSGNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 241 GEKQGLENVIEAADRLRDEPLIFAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAADAV 320
Cdd:TIGR04007 241 GEKQGLENVIDAAARLTDRPWIFAIVGQGGGKARLEKMARERGLTNVKFFPLQPYEALPALLKMGDCHLVVQKRGAADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 321 LPSKLTNILAVGGNAVITAEAYTELGQLCETFPGIAVCVEPESVEALVAGIRQALLLPKHNTVAREYAERTLDKENVLRQ 400
Cdd:TIGR04007 321 LPSKLTNILAVGGNAVITAEPHTELGQLCITYPGIAVCVEPESVDALVAGIVQALAMPKNNTVAREYAERTLEKENVLRQ 400
|
....*..
gi 1535758469 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: 728.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 1 MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKRE-EGAATVWRCPLYVPKQPS 79
Cdd:PRK10307 1 MKILVYGINYAPELTGIGKYTGEMAEWLAARGHEVRVITAPPYYPQWRVGEGYSAWRYRREsEGGVTVWRCPLYVPKQPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 80 TLKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCAPGMRLLAKLSGARTVLHIQDYEVDAMlglGLAGKGKGGKV 159
Cdd:PRK10307 81 GLKRLLHLGSFALSSFFPLLAQRRWRPDRVIGVVPTLFCAPGARLLARLSGARTWLHIQDYEVDAA---FGLGLLKGGKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 160 AQLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQHVADADVDALRNQLDLPDNKKIILYSGN 239
Cdd:PRK10307 158 ARLATAFERSLLRRFDNVSTISRSMMNKAREKGVAAEKVIFFPNWSEVARFQPVADADVDALRAQLGLPDGKKIVLYSGN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 240 IGEKQGLENVIEAADRLRDEP-LIFAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAAD 318
Cdd:PRK10307 238 IGEKQGLELVIDAARRLRDRPdLIFVICGQGGGKARLEKMAQCRGLPNVHFLPLQPYDRLPALLKMADCHLLPQKAGAAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 319 AVLPSKLTNILAVGGNAVITAEAYTELGQLCEtfpGIAVCVEPESVEALVAGI----RQALLLPKHNTVAREYAERTLDK 394
Cdd:PRK10307 318 LVLPSKLTNMLASGRNVVATAEPGTELGQLVE---GIGVCVEPESVEALVAAIaalaRQALLRPKLGTVAREYAERTLDK 394
|
410
....*....|...
gi 1535758469 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 |
6.66e-80 |
|
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: 251.11 E-value: 6.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWqvgenYSAWRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03794 1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLG-----RIFAGATETKDGIRVIRVKLGPIKKNGLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 82 KRLLHLGSFAVSSFFPLMAqRRWKPDRIIGVVPTLFCAPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVAQ 161
Cdd:cd03794 76 RRLLNYLSFALAALLKLLV-REERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKKGSLLKLLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 162 LataFERSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQHVADADVDALRNqldlPDNKKIILYSGNIG 241
Cdd:cd03794 155 K---LERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPKDELRKKLG----LDDKFVVVYAGNIG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 242 EKQGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAA-DA 319
Cdd:cd03794 228 KAQGLETLLEAAERLKRRPDIrFLFVGDGDEKERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLVPLKDNPAnRG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 320 VLPSKLTNILAVGGNAVITAEAYTELGQLCEtfpGIAVCVEPESVEALVAGIRQALLlpkhNTV--------AREYAERT 391
Cdd:cd03794 308 SSPSKLFEYMAAGKPILASDDGGSDLAVEIN---GCGLVVEPGDPEALADAILELLD----DPElrramgenGRELAEEK 380
|
410
....*....|.
gi 1535758469 392 LDKENVLRQFI 402
Cdd:cd03794 381 FSREKLADRLL 391
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
230-390 |
1.47e-24 |
|
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: 98.50 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 230 NKKIILYSGNIGEKQGLENVIEAADRLR--DEPLIFAIVGQGGGKARLEKMAQQRGLRNMQFFPL-QSYDALPALLKMgd 306
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKekNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGfVSDEDLPELLKI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 307 CHLVVQKrgAADAVLPSKLTNILAVGGnAVITAEAYTELGQLCETFPGiaVCVEPESVEALVAGIRQALLLPKHNTVARE 386
Cdd:pfam00534 79 ADVFVLP--SRYEGFGIVLLEAMACGL-PVIASDVGGPPEVVKDGETG--FLVKPNNAEALAEAIDKLLEDEELRERLGE 153
|
....
gi 1535758469 387 YAER 390
Cdd:pfam00534 154 NARK 157
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
15-204 |
2.37e-20 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 87.07 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 15 TGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQvgenysawrykREEGAATVWRCPL-YVPKQPSTLKRLLHLGSFAvs 93
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPE-----------LVGDGVRVHRLPVpPRPSPLADLAALRRLRRLL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 94 sffplmaqRRWKPDRIIGVVPTLfcAPGMRLLAKLSGARTVLHIQDYEVDamlglglagkGKGGKVAQLATAFERSGLHN 173
Cdd:pfam13579 68 --------RAERPDVVHAHSPTA--GLAARLARRRRGVPLVVTVHGLALD----------YGSGWKRRLARALERRLLRR 127
|
170 180 190
....*....|....*....|....*....|.
gi 1535758469 174 VDNVSTISRSMMNKAIEKGVAAENVIFFPNW 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 |
5.58e-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: 87.59 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYypqwqvgenysawRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03801 1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADP-------------GEPPEELEDGVIVPLLPSLAALLRA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 82 KRLLHLGSFAVssffplmaqRRWKPDRIIgvVPTLFCAPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKggkvaq 161
Cdd:cd03801 68 RRLLRELRPLL---------RLRKFDVVH--AHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRL------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 162 LATAFERsgLHNVDNVSTISRSMMNKAIEKGVA-AENVIFFPNWSEIARFQhvadadvDALRNQLDLPDNKKIILYSGNI 240
Cdd:cd03801 131 LARAEAL--LRRADAVIAVSEALRDELRALGGIpPEKIVVIPNGVDLERFS-------PPLRRKLGIPPDRPVLLFVGRL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 241 GEKQGLENVIEAADRLRDE--PLIFAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDChlvvqkrgaad 318
Cdd:cd03801 202 SPRKGVDLLLEALAKLLRRgpDVRLVIVGGDGPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADV----------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 319 AVLPSKLTNIlavgGNAVITAEAY------TELGQLCETFP--GIAVCVEPESVEALVAGIRQAL----LLPKHNTVARE 386
Cdd:cd03801 271 FVLPSRYEGF----GLVVLEAMAAglpvvaTDVGGLPEVVEdgEGGLVVPPDDVEALADALLRLLadpeLRARLGRAARE 346
|
410 420
....*....|....*....|
gi 1535758469 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 ... |
15-375 |
6.94e-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: 84.35 E-value: 6.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 15 TGIGKYTGEMVEWLAAQGHEVRVITAPPYYPqwqvgenySAWRYKREEGAATVWRCPLYVPKQPStlKRLLHLGSFAVSS 94
Cdd:cd03798 14 PGRGIFVRRQVRALSRRGVDVEVLAPAPWGP--------AAARLLRKLLGEAVPPRDGRRLLPLK--PRLRLLAPLRAPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 95 FFPLMAQ-RRWKPDRI--IGVVPTLFCApgmRLLAKLSGARTVL-----HIQDYEVDamlglglagkgkggkvaQLATAF 166
Cdd:cd03798 84 LAKLLKRrRRGPPDLIhaHFAYPAGFAA---ALLARLYGVPYVVtehgsDINVFPPR-----------------SLLRKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 167 ERSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQHVADAdvdalrnqLDLPDNKKIILYSGNIGEKQGL 246
Cdd:cd03798 144 LRWALRRAARVIAVSKALAEELVALGVPRDRVDVIPNGVDPARFQPEDRG--------LGLPLDAFVILFVGRLIPRKGI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 247 ENVIEAADRLRDE--PLIFAIVGQGGGKARLEKMAQQRGLRN-MQFFPLQSYDALPALLKmgdchlvvqkrgAADA-VLP 322
Cdd:cd03798 216 DLLLEAFARLAKArpDVVLLIVGDGPLREALRALAEDLGLGDrVTFTGRLPHEQVPAYYR------------ACDVfVLP 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1535758469 323 SkltniLAVG-GNAVITAEA------YTELGQLCE--TFPGIAVCVEPESVEALVAGIRQAL 375
Cdd:cd03798 284 S-----RHEGfGLVLLEAMAcglpvvATDVGGIPEvvGDPETGLLVPPGDADALAAALRRAL 340
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
26-307 |
3.56e-13 |
|
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: 70.39 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 26 EWLAAQGHEVRVITapPYYPQWQVGENYSAWRYKREEGAATVWRCpLYVPKQPSTLKRLlhlgsfavssffplmaqRRWK 105
Cdd:cd03817 25 RALEKRGHEVYVIT--PSDPGAEDEEEVVRYRSFSIPIRKYHRQH-IPFPFKKAVIDRI-----------------KELG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 106 PDRI-------IGVVptlfcapGMRLlAKLSGARTV--LHIQdYEVDAmLGLGLAGKGKGGKVAQLATAFersgLHNVDN 176
Cdd:cd03817 85 PDIIhthtpfsLGKL-------GLRI-ARKLKIPIVhtYHTM-YEDYL-HYIPKGKLLVKAVVRKLVRRF----YNHTDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 177 VSTISRSMMNKAIEKGVAAE-NVIffPNWSEIARFQHVADadvDALRNQLDLPDNKKIILYSGNIGEKQGLENVIEAADR 255
Cdd:cd03817 151 VIAPSEKIKDTLREYGVKGPiEVI--PNGIDLDKFEKPLN---TEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAE 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1535758469 256 LRDEPLIFA-IVGQGGGKARLEKMAQQRGL-RNMQFFPLQSYDALPALLKMGDC 307
Cdd:cd03817 226 LKKEPNIKLvIVGDGPEREELKELARELGLaDKVIFTGFVPREELPEYYKAADL 279
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
7-379 |
4.96e-09 |
|
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 57.37 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 7 GINYSPE---LTGIGKYTGEMVEWLAAQGHEVRVITAPPYypqwqvgenysawryKREEGAATVWRCPLYVPKQPSTLKR 83
Cdd:cd03809 3 LIDGRSLaqrLTGIGRYTRELLKALAKNDPDESVLAVPPL---------------PGELLRLLREYPELSLGVIKIKLWR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 84 LLHLgsfavssffplmaQRRWKPDRIIGVVPTLFCAPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVAQLA 163
Cdd:cd03809 68 ELAL-------------LRWLQILLPKKDKPDLLHSPHNTAPLLLKGCPQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 164 TafersgLHNVDNVSTISRSMMNKAIEK-GVAAENVIFFPNWSEIARFQHVADADVDALRNQLDlpdnkKIILYSGNIGE 242
Cdd:cd03809 135 S------LRRADAIITVSEATRDDIIKFyGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLPE-----PYFLYVGTLEP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 243 KQGLENVIEAADRLRDE--PLIFAIVGQGGGK-ARLEKMAQQRGLR-NMQFFPLQSYDALPALLKmgdchlvvqkrgAAD 318
Cdd:cd03809 204 RKNHERLLKAFALLKKQggDLKLVIVGGKGWEdEELLDLVKKLGLGgRVRFLGYVSDEDLPALYR------------GAR 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1535758469 319 A-VLPSkltniLAVG-----------GNAVITAEAYTelgqLCETFPGIAVCVEPESVEALVAGIRQALLLPK 379
Cdd:cd03809 272 AfVFPS-----LYEGfglpvleamacGTPVIASNISV----LPEVAGDAALYFDPLDPESIADAILRLLEDPS 335
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
2-278 |
2.01e-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: 55.76 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 2 KILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVIT-APPYYPQWQVGENYSAWRykreegaatvWRCPLY------V 74
Cdd:cd03814 1 RIALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVApGPFDEAESAEGRVVSVPS----------FPLPFYpeyrlaL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 75 PKQPSTLKR-------LLHLGSFAVSSFFPLMAQRRWKPDrIIGVVPTLFCAPGM-RLLAKLSGartvlhiqdyevdaml 146
Cdd:cd03814 71 PLPRRVRRLikefqpdIIHIATPGPLGLAALRAARRLGLP-VVTSYHTDFPEYLSyYTLGPLSW---------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 147 glglagkgkggkvaqLATAFERSgLHN-VDNVSTISRSMMNKAIEKGvaAENVIFFPNWSEIARFqHVADADVDALRNQl 225
Cdd:cd03814 134 ---------------LAWAYLRW-FHNpFDTTLVPSPSIARELEGHG--FERVRLWPRGVDTELF-HPSRRDAALRRRL- 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1535758469 226 dLPDNKKIILYSGNIGEKQGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKM 278
Cdd:cd03814 194 -GPPGRPLLLYVGRLAPEKNLEALLDADLPLAASPPVrLVVVGDGPARAELEAR 246
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
164-395 |
2.42e-08 |
|
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: 55.45 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 164 TAFERSGLHNVDNVSTISrSMMNKAIEKGVAAENVIFFPNWSEIARFqHVADADvdalRNQLDLPDNKKIILYSGNIGEK 243
Cdd:cd03821 143 HLIERRNLNNAALVHFTS-EQEADELRRFGLEPPIAVIPNGVDIPEF-DPGLRD----RRKHNGLEDRRIILFLGRIHPK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 244 QGLENVIEAADRLRDEPL--IFAIVGQGGGkARLEKMAQQR--GLRNMQFFPLQSY-DALPALLKMGDCHlvvqkrgaad 318
Cdd:cd03821 217 KGLDLLIRAARKLAEQGRdwHLVIAGPDDG-AYPAFLQLQSslGLGDRVTFTGPLYgEAKWALYASADLF---------- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 319 aVLPSKLTNI-------LAVGGNAVITAEAytelgQLCETF-PGIAVCVEPEsVEALVAGIRQALLLPKHNTVAREYAER 390
Cdd:cd03821 286 -VLPSYSENFgnvvaeaLACGLPVVITDKC-----GLSELVeAGCGVVVDPN-VSSLAEALAEALRDPADRKRLGEMARR 358
|
....*
gi 1535758469 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 |
2.10e-07 |
|
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: 52.39 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 191 KGVAAENVIFFPNWSEIARFQHVADadvdalRNQLDLPDNKKIILYSGNIGEKQGLENVIEAADRLRDE--PLIFAIVG- 267
Cdd:cd03822 153 KLIPAVNIEVIPHGVPEVPQDPTTA------LKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEfpDVRLVIAGe 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 268 ------QGGGKARLEKMAQQRGLRNMQFFPLQSY--DALPALLKMgdCHLVVQ-----KRGAADAVlpskltnILAVG-G 333
Cdd:cd03822 227 lhpslaRYEGERYRKAAIEELGLQDHVDFHNNFLpeEEVPRYISA--ADVVVLpylntEQSSSGTL-------SYAIAcG 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1535758469 334 NAVITaeayTELGQLCETFPGIA-VCVEPESVEALVAGIRQALLLPKHntvAREYAERT 391
Cdd:cd03822 298 KPVIS----TPLRHAEELLADGRgVLVPFDDPSAIAEAILRLLEDDER---RQAIAERA 349
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
8-379 |
2.36e-07 |
|
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: 52.36 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 8 INYSPELTGIGKYTGEMVEWLAAQGHEVRVITAppyypqwqvgenysawrykreeGAATVWRCPLYVPKQPSTLKRLLHL 87
Cdd:cd03819 4 LTPALEIGGAETYILDLARALAERGHRVLVVTA----------------------GGPLLPRLRQIGIGLPGLKVPLLRA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 88 GSFAVSSFFPLmaqRRWKPDrIIGV---VPTLFCApgmrLLAKLSGARTVLHIQDyevdamlglglagkgkGGKVAQLAT 164
Cdd:cd03819 62 LLGNVRLARLI---RRERID-LIHAhsrAPAWLGW----LASRLTGVPLVTTVHG----------------SYLATYHPK 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 165 AFERSGLHNVDNVSTISRSMMNKAIEK-GVAAENVIFFPNWSEIARFQHVADAdvdALRNQLDLPDNKKIILYSGNIGEK 243
Cdd:cd03819 118 DFALAVRARGDRVIAVSELVRDHLIEAlGVDPERIRVIPNGVDTDRFPPEAEA---EERAQLGLPEGKPVVGYVGRLSPE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 244 QGLENVIEAADRLRDEPLI-FAIVGQGGGKARLEKMAQQRGLRNmQFFPLQSYDALPALlkMGDCHLVVqkrGAA-DAVL 321
Cdd:cd03819 195 KGWLLLVDAAAELKDEPDFrLLVAGDGPERDEIRRLVERLGLRD-RVTFTGFREDVPAA--LAASDVVV---LPSlHEEF 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 322 PSKLTNILAVgGNAVITaeayTELGQLCETFPG--IAVCVEPESVEALVAGIRQALLLPK 379
Cdd:cd03819 269 GRVALEAMAC-GTPVVA----TDVGGAREIVVHgrTGLLVPPGDAEALADAIRAAKLLPE 323
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
2-310 |
3.67e-07 |
|
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: 51.56 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 2 KILVYGINYSPELT-GIGKYTGEMVEWLAAQGHEVRVITAPPYyPQWQVGENYSAWRYKReegaatvwrcPLYVPKQPST 80
Cdd:cd03823 1 KILLVNSLYPPQRVgGAEISVHDLAEALVAEGHEVAVLTAGVG-PPGQATVARSVVRYRR----------APDETLPLAL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 81 LKRLLHLGSFAVSSFFPLMAQ--RRWKPDRI-----IGVvptlfcapGMRLL--AKLSGARTVLHIQDYEVDAMlglgla 151
Cdd:cd03823 70 KRRGYELFETYNPGLRRLLARllEDFRPDVVhthnlSGL--------GASLLdaARDLGIPVVHTLHDYWLLCP------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 152 gkgkggkvaqlatafeRSGL--HNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARfqhvadadvdALRNQLDLPD 229
Cdd:cd03823 136 ----------------RQFLfkKGGDAVLAPSRFTANLHEANGLFSARISVIPNAVEPDL----------APPPRRRPGT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 230 NKKIILYSGNIGEKQGLENVIEAADRLRDEPLIFAIVgqggGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHL 309
Cdd:cd03823 190 ERLRFGYIGRLTEEKGIDLLVEAFKRLPREDIELVIA----GHGPLSDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLV 265
|
.
gi 1535758469 310 V 310
Cdd:cd03823 266 V 266
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
2-291 |
4.63e-06 |
|
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: 48.12 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 2 KILVygINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAppyypqwqvgeNYSAWRYKREEGAATVWRCPLYVPKQPSTL 81
Cdd:cd03811 1 KILF--VIPSLSGGGAERVLLNLANALDKRGYDVTLVLL-----------RDEGDLDKQLNGDVKLIRLLIRVLKLIKLG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 82 KRLLHLgsfavssFFPLMAQRRwKPDRIIGvvptlFCAPGMRLLAKLSGARTVLHIqdYEVDAMLGLGLAgkgkggkvaQ 161
Cdd:cd03811 68 LLKAIL-------KLKRILKRA-KPDVVIS-----FLGFATYIVAKLAAARSKVIA--WIHSSLSKLYYL---------K 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 162 LATAFERSGLHNVDNVSTISRSMMNKAIEKG-VAAENVIFFPNwseiarFQHVADADVDALRNQLDLPDNKKIILYSGNI 240
Cdd:cd03811 124 KKLLLKLKLYKKADKIVCVSKGIKEDLIRLGpSPPEKIEVIYN------PIDIDRIRALAKEPILNEPEDGPVILAVGRL 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1535758469 241 GEKQGLENVIEAADRLRDE--PLIFAIVGQGGGKARLEKMAQQRGLRNMQFFP 291
Cdd:cd03811 198 DPQKGHDLLIEAFAKLRKKypDVKLVILGDGPLREELEKLAKELGLAERVIFL 250
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
16-203 |
7.68e-06 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 45.99 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 16 GIGKYTGEMVEWLAAQGHEVRVIT---APPYYPQWQVGENYSAWRYKREEGaatvwrcPLYVPKQPSTLKRLLhlgsfav 92
Cdd:pfam13439 2 GVERYVLELARALARRGHEVTVVTpggPGPLAEEVVRVVRVPRVPLPLPPR-------LLRSLAFLRRLRRLL------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 93 ssffplmaqRRWKPDRIIGVVPTLFCApGMRLLAKLSGARTV--LHiqdyevdAMLGLGLAGKGKGGKVAQLATAFERSG 170
Cdd:pfam13439 68 ---------RRERPDVVHAHSPFPLGL-AALAARLRLGIPLVvtYH-------GLFPDYKRLGARLSPLRRLLRRLERRL 130
|
170 180 190
....*....|....*....|....*....|....
gi 1535758469 171 LHNVDNVSTISRSMMNKAIEK-GVAAENVIFFPN 203
Cdd:pfam13439 131 LRRADRVIAVSEAVADELRRLyGVPPEKIRVIPN 164
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
180-335 |
3.11e-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: 45.52 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 180 ISRSMMNKAIEKGVAAENVIFFPNWSEIARFqHVADADVDALRnqldlpdnkkiILYSGNIGEKQGLENVIEA----ADR 255
Cdd:cd05844 150 VSGFIRDRLLARGLPAERIHVHYIGIDPAKF-APRDPAERAPT-----------ILFVGRLVEKKGCDVLIEAfrrlAAR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 256 LRDEPLIfaIVGQGGGKARLEKMAqqRGLRNMQFFPLQSYDALPALLkmgdchlvvqkRGAADAVLPSkltnILAVGGNA 335
Cdd:cd05844 218 HPTARLV--IAGDGPLRPALQALA--AALGRVRFLGALPHAEVQDWM-----------RRAEIFCLPS----VTAASGDS 278
|
|
| 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 1535758469 231 KKIILYSGNIGEKQGLENVIEAADRLrDEPLIfaIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDC 307
Cdd:cd03795 191 KKIFLFIGRLVYYKGLDYLIEAAQYL-NYPIV--IGGEGPLKPDLEAQIELNLLDNVKFLGRVDDEEKVIYLHLCDV 264
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
159-401 |
1.77e-04 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 43.24 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 159 VAQLATAFERSGLHNvdNVSTISRSMMNKAI-EKGVAAENVIFFPNWSEIARFQHvadADVDALRNQLDLPDNKKIILYS 237
Cdd:PRK15484 125 VMHMHNAFEPELLDK--NAKIIVPSQFLKKFyEERLPNADISIVPNGFCLETYQS---NPQPNLRQQLNISPDETVLLYA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 238 GNIGEKQGLENVIEAADRLRDEP--LIFAIVGQGGGKARLEKMAQQRGLRNM--------------------QFFPLQSY 295
Cdd:PRK15484 200 GRISPDKGILLLMQAFEKLATAHsnLKLVVVGDPTASSKGEKAAYQKKVLEAakrigdrcimlggqppekmhNYYPLADL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 296 DALPALLKMGDCHLVVQKRGAADAVLPSKLTNIlavggnavitaeayTELGQLCETFPGIAvcvEPESVEALVAGIRQAL 375
Cdd:PRK15484 280 VVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGI--------------TEFVLEGITGYHLA---EPMTSDSIISDINRTL 342
|
250 260
....*....|....*....|....*....
gi 1535758469 376 LLPKHNTVAREYAERTLDK---ENVLRQF 401
Cdd:PRK15484 343 ADPELTQIAEQAKDFVFSKyswEGVTQRF 371
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
231-375 |
9.08e-04 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 39.03 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 231 KKIILYSGNIGEKQ-GLENVIEAADRLRDEP--LIFAIVGqGGGKARLEKMAqqRGLRNmQFFPLQSYDALPALLKMGDC 307
Cdd:pfam13692 1 RPVILFVGRLHPNVkGVDYLLEAVPLLRKRDndVRLVIVG-DGPEEELEELA--AGLED-RVIFTGFVEDLAELLAAADV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1535758469 308 hlvvqkrgaadAVLPSKLTNIlavgGNAVITAEAY------TELGQLCETFPGIA-VCVEPESVEALVAGIRQAL 375
Cdd:pfam13692 77 -----------FVLPSLYEGF----GLKLLEAMAAglpvvaTDVGGIPELVDGENgLLVPPGDPEALAEAILRLL 136
|
|
| GT4_TuaH-like |
cd04950 |
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this ... |
28-390 |
2.39e-03 |
|
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. 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.
Pssm-ID: 340856 [Multi-domain] Cd Length: 373 Bit Score: 39.66 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 28 LAAQGHEVRVITAPPYyPQWQVGENYSAWRYKReegaatVWRCPlyvPKQPSTLKRLLHLGSFAVSSFFPLMAQRRWKPD 107
Cdd:cd04950 29 LAKLGHRVLFVEEPGN-RDESRTISPTGRIWDR------VWKFL---VKKLGRPARVGLTPDFSAFLLRSLLDALLADSR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 108 RIIGVVPTLFCAPGMRLLAKLSGARTVLHiqdyevDAMLGLGLAGKGKGGKVAQLATAFERsglhnVDNVSTISRsmmnk 187
Cdd:cd04950 99 LGFRRVVLWYYTPMTLLFSDHLQASLVVY------DCMDELAAFPGMPPELIEQERRLIKR-----ADVVFTTSP----- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 188 AIEKGVAA--ENVIFFPNWSEIARFQhvadADVDALRNQLDLPDNKKIIL-YSGNIGEKQGLENVIEAAdRLRDEpLIFA 264
Cdd:cd04950 163 ALYEAKRPlhENVHPIPNGVDVEHFA----AARQPLDDPIDLREIPGPVLgFFGAIDEKLDFDLIEELA-KARPQ-WNFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 265 IVGQGG--GKARLEKMAqqrglrNMQFFPLQSYDALPALLKMGDCHLV-VQKRGAADAVLPSKLTNILAVGGNAVITaeA 341
Cdd:cd04950 237 FIGPVVkiDPSSLPRAP------NIHWLGPKPYKELPAYLAGFDVALLpFALNEYTRFISPLKLFEYLAAGKPVVAT--S 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1535758469 342 YTELGQLCEtfpgiAVCVEPESVEALVAGIRQALLLPKHNTVAREYAER 390
Cdd:cd04950 309 IPSVVRFYG-----EAVLCGDDPDEFSAAIEKALALKGDARDKRLARAL 352
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| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
168-309 |
8.83e-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: 38.10 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1535758469 168 RSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQHVADadvDALRNQLDLPDNKKIILYSGNIGEKQGLE 247
Cdd:cd04962 136 RFSINKSDRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKPA---GALKRRLLAPPDEKVVIHVSNFRPVKRID 212
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1535758469 248 NVIEAADRLRDE-PLIFAIVGQGGGKARLEKMAQQRGLRNMQFFpLQSYDALPALLKMGDCHL 309
Cdd:cd04962 213 DVVRVFARVRRKiPAKLLLVGDGPERVPAEELARELGVEDRVLF-LGKQDDVEELLSIADLFL 274
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