|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
2-451 |
0e+00 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 618.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 2 RICMVSDFFYPSIGGVEEHVYNLSQMLLSLGHKIVVLTHAYGDCSGIRYVTGYLKVYYLPIKVCYNQCILPTAVCNVPML 81
Cdd:cd03796 1 RICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVITHAYGNRVGVRYLTNGLKVYYLPFKVFYNQSTLPTLFSTFPLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 82 RAVLLRERVEVVHGHSAFSALAHEALMVGSLLGLKTVFTDHSLFGFADLSAALTNNLLEVNLGMVNHAICVSHIGKENTV 161
Cdd:cd03796 81 RNILIRERIQIVHGHQAFSSLAHEALFHARTLGLKTVFTDHSLFGFADASSILTNKLLRFSLADIDHVICVSHTSKENTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 162 LRARVAKHRVSVIPNAVDTALFTPDPqQRPSNDIINIVVASRLVYRKGIDLLAGIIPRF-KNTPNINFIIVGDGPKRDLL 240
Cdd:cd03796 161 LRASLDPRIVSVIPNAVDSSDFTPDP-SKPDPNKITIVVISRLVYRKGIDLLVGIIPRIcKKHPNVRFIIGGDGPKRIEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 241 EEIREKTNMQERVQMVGAVEHNRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGIPEVLPKSLILLAEPE 320
Cdd:cd03796 240 EEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 321 IDAIYAAILIAIDRHRKSSFKvspsvgnghlasdangkvkrrrrrkvdtpisptqlpavsappadqnsstepvmcPYRCN 400
Cdd:cd03796 320 PEDIVRKLEEAISILRTGKHD------------------------------------------------------PWSFH 345
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 665401714 401 ELVETLYNWEDVALRTVKVYDRVLNERSFTTSELVFAVWQHGSWFLVFFVV 451
Cdd:cd03796 346 NRVKKMYSWEDVARRTEKVYDRILSTPNRPFLERLKRYYNCGPIAGKIFCL 396
|
|
| PIGA |
pfam08288 |
PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol ... |
40-129 |
2.69e-49 |
|
PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol n-acetylglucosaminyltransferase proteins. These proteins are involved in GPI anchor biosynthesis and are associated with disease the paroxysmal nocturnal haemoglobinuria.
Pssm-ID: 400541 Cd Length: 90 Bit Score: 163.58 E-value: 2.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 40 HAYGDCSGIRYVTGYLKVYYLPIKVCYNQCILPTAVCNVPMLRAVLLRERVEVVHGHSAFSALAHEALMVGSLLGLKTVF 119
Cdd:pfam08288 1 HAYGDRTGVRYLTNGLKVYYVPFLVIYRQSTFPTVFGTFPLFRNILLRERIDIVHGHGSFSTLAHEAILHARTMGLKTVF 80
|
90
....*....|
gi 665401714 120 TDHSLFGFAD 129
Cdd:pfam08288 81 TDHSLFGFAD 90
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-310 |
2.27e-47 |
|
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: 167.71 E-value: 2.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 2 RICMVSDFFYPSIGGVEEHVYNLSQMLLSLGHKIVVLTHAYGDCSGIRYVTGYLKVYYLPIKVCYNqcilptavcNVPML 81
Cdd:cd03801 1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLR---------ARRLL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 82 RAV---LLRERVEVVHGHSAFSALAheALMVGSLLGLKTVFTDHSL-FGFADLSAALTNNLL---EVNLGMVNHAICVSH 154
Cdd:cd03801 72 RELrplLRLRKFDVVHAHGLLAALL--AALLALLLGAPLVVTLHGAePGRLLLLLAAERRLLaraEALLRRADAVIAVSE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 155 IGKENTVLRARVAKHRVSVIPNAVDTALFTPDPQQRP--SNDIINIVVASRLVYRKGIDLLAGIIPRFKNT-PNINFIIV 231
Cdd:cd03801 150 ALRDELRALGGIPPEKIVVIPNGVDLERFSPPLRRKLgiPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRgPDVRLVIV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 232 G-DGPKRDLLEEIREKTnmQERVQMVGAVEHNRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGIPEVLP 310
Cdd:cd03801 230 GgDGPLRAELEELELGL--GDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVE 307
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
3-311 |
5.54e-40 |
|
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: 147.12 E-value: 5.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 3 ICMVSDFFYpsIGGVEEHVYNLSQMLLSLGHKIVVLT-------HAYGDCSGIRYVTGYLKVYYLPIKVcynqcilptav 75
Cdd:cd03819 1 ILMLTPALE--IGGAETYILDLARALAERGHRVLVVTaggpllpRLRQIGIGLPGLKVPLLRALLGNVR----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 76 cnvpmLRAVLLRERVEVVHGHSAFSALAheALMVGSLLGLKTVFTDHSL----FGFADLSAALTNNllevnlgmVNHAIC 151
Cdd:cd03819 68 -----LARLIRRERIDLIHAHSRAPAWL--GWLASRLTGVPLVTTVHGSylatYHPKDFALAVRAR--------GDRVIA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 152 VSHIGKENTVLRARVAKHRVSVIPNAVDTALFTPDP------QQRPSNDIINIVVASRLVYRKGIDLLAGIIPRFKNTPN 225
Cdd:cd03819 133 VSELVRDHLIEALGVDPERIRVIPNGVDTDRFPPEAeaeeraQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 226 INFIIVGDGPKRDLLEEIREKTNMQERVQMVGAVEhnRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGI 305
Cdd:cd03819 213 FRLLVAGDGPERDEIRRLVERLGLRDRVTFTGFRE--DVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGA 290
|
....*.
gi 665401714 306 PEVLPK 311
Cdd:cd03819 291 REIVVH 296
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
2-309 |
1.62e-36 |
|
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: 138.18 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 2 RICMVSDFFYPSIGGVEEHVYNLSQMLLSLGHKIVVLTHAYGDCSGIRYVTGYLKVYYlPIKVCYNQCILPTavcNVPML 81
Cdd:cd03817 1 KIAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEEVVRYRSFSI-PIRKYHRQHIPFP---FKKAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 82 RAVLLRERVEVVHGHSAFSA-LAheALMVGSLLGLKTVFTDHSL---------FGFADLSAALTNNLLEVnLGMVNHAIC 151
Cdd:cd03817 77 IDRIKELGPDIIHTHTPFSLgKL--GLRIARKLKIPIVHTYHTMyedylhyipKGKLLVKAVVRKLVRRF-YNHTDAVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 152 VSHigKENTVLRARVAKHRVSVIPNAVDTALFTPDPQQR------PSNDIINIVVASRLVYRKGIDLLAGIIPRFKNTPN 225
Cdd:cd03817 154 PSE--KIKDTLREYGVKGPIEVIPNGIDLDKFEKPLNTEerrklgLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEPN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 226 INFIIVGDGPKRDLLEEIREKTNMQERVQMVGAVEHNRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGI 305
Cdd:cd03817 232 IKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAA 311
|
....
gi 665401714 306 PEVL 309
Cdd:cd03817 312 SELV 315
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
9-310 |
1.23e-30 |
|
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: 122.10 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 9 FFYP--SIGGVEEHVYNLSQMLLSLGHKIVVLT-----------------HAYGDCSGIRYVTGYLKVYYLPIKVCynqc 69
Cdd:cd03798 6 NIYPnaNSPGRGIFVRRQVRALSRRGVDVEVLApapwgpaaarllrkllgEAVPPRDGRRLLPLKPRLRLLAPLRA---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 70 ilptavcnvPMLRAVLL---RERVEVVHGHSAFSALAhEALMVGSLLGLKTVFTDHS--LFGFADLSAaltnnLLEVNLG 144
Cdd:cd03798 82 ---------PSLAKLLKrrrRGPPDLIHAHFAYPAGF-AAALLARLYGVPYVVTEHGsdINVFPPRSL-----LRKLLRW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 145 MVNHAICVSHIGKE--NTVLRARVAKHRVSVIPNAVDTALFTP-DPQQRPSNDIINIVVASRLVYRKGIDLLAGIIPR-F 220
Cdd:cd03798 147 ALRRAARVIAVSKAlaEELVALGVPRDRVDVIPNGVDPARFQPeDRGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARlA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 221 KNTPNINFIIVGDGPKRDLLEEIREKTNMQERVQMVGAVEHNRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVST 300
Cdd:cd03798 227 KARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVAT 306
|
330
....*....|
gi 665401714 301 SVGGIPEVLP 310
Cdd:cd03798 307 DVGGIPEVVG 316
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
9-309 |
4.58e-30 |
|
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: 120.16 E-value: 4.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 9 FFYPS--IGGVEEHVYNLSQMLLSLGHKIVVLT-----HAYGDCSGIRYVTGYLKVYYLPIKVcynqcILPTAVcnvPML 81
Cdd:cd03811 4 FVIPSlsGGGAERVLLNLANALDKRGYDVTLVLlrdegDLDKQLNGDVKLIRLLIRVLKLIKL-----GLLKAI---LKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 82 RAVLLRERVEVVHGHSAFSALahealMVGSLL--GLKTVFTDHSLFgFADLSAALTNNLLEVNLGMVNHAICVSHIGKEN 159
Cdd:cd03811 76 KRILKRAKPDVVISFLGFATY-----IVAKLAaaRSKVIAWIHSSL-SKLYYLKKKLLLKLKLYKKADKIVCVSKGIKED 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 160 TVLRARVAKHRVSVIPNAVDTALFTPDPQQRPSN---DIINIVVASRLVYRKGIDLL---AGIIPrfKNTPNINFIIVGD 233
Cdd:cd03811 150 LIRLGPSPPEKIEVIYNPIDIDRIRALAKEPILNepeDGPVILAVGRLDPQKGHDLLieaFAKLR--KKYPDVKLVILGD 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665401714 234 GPKRDLLEEIREKTNMQERVQMVGAVEhNrVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGIPEVL 309
Cdd:cd03811 228 GPLREELEKLAKELGLAERVIFLGFQS-N-PYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREIL 301
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
15-311 |
2.78e-24 |
|
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: 103.94 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 15 GGVEEHVYNLSQMLLSLGHKIVV--LTH--AYGD---CSGIRYVTgylkvyylpIKVCYNqcILPTAVcnvPMLRAVLLR 87
Cdd:cd03807 12 GGAETMLLRLLEHMDKSRFEHVVisLTGdgVLGEellAAGVPVVC---------LGLSSG--KDPGVL---LRLAKLIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 88 ERVEVVHGHSA----FSALAheALMVGsllGLKTVFTDHSLFGFADLSAALT-NNLLEVNLGMVnhAICVSHIGKEnTVL 162
Cdd:cd03807 78 RNPDVVHTWMYhadlIGGLA--AKLAG---GVKVIWSVRSSNIPQRLTRLVRkLCLLLSKFSPA--TVANSSAVAE-FHQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 163 RARVAKHRVSVIPNAVDTALFTPDPQQRPSN--------DIINIVVASRLVYRKGIDLL---AGIIPrfKNTPNINFIIV 231
Cdd:cd03807 150 EQGYAKNKIVVIYNGIDLFKLSPDDASRARArrrlglaeDRRVIGIVGRLHPVKDHSDLlraAALLV--ETHPDLRLLLV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 232 GDGPKRDLLEEIREKTNMQERVQMVGAVEHnrVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGIPEVLPK 311
Cdd:cd03807 228 GRGPERPNLERLLLELGLEDRVHLLGERSD--VPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDD 305
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
2-310 |
1.36e-22 |
|
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: 98.94 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 2 RICMVSDFFYP-SIGGVEEHVYNLSQMLLSLGHKIVVLTHAYGdCSGIRYVTGYLKVYYLPIKVC--------------- 65
Cdd:cd03823 1 KILLVNSLYPPqRVGGAEISVHDLAEALVAEGHEVAVLTAGVG-PPGQATVARSVVRYRRAPDETlplalkrrgyelfet 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 66 YNQCIlptavcnVPMLRAVLLRERVEVVHGHSaFSALAHEALMVGSLLGLKTVFTDHSLFGFADlsaaltNNLLEVNLG- 144
Cdd:cd03823 80 YNPGL-------RRLLARLLEDFRPDVVHTHN-LSGLGASLLDAARDLGIPVVHTLHDYWLLCP------RQFLFKKGGd 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 145 MVnhaICVSHIgKENTVLRARVAKHRVSVIPNAVdTALFTPDPQQRPSNDIINIVVASRLVYRKGIDLL---AGIIPRfk 221
Cdd:cd03823 146 AV---LAPSRF-TANLHEANGLFSARISVIPNAV-EPDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLveaFKRLPR-- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 222 ntPNINFIIVGDGPkrdllEEIREKTNMQERVQMVGAVEHNRVRDFLVRGHIFLNTSL-TEAYCMAIVEAASCGLQVVST 300
Cdd:cd03823 219 --EDIELVIAGHGP-----LSDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIAS 291
|
330
....*....|
gi 665401714 301 SVGGIPEVLP 310
Cdd:cd03823 292 DLGGIAELIQ 301
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
198-309 |
1.39e-22 |
|
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: 93.88 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 198 IVVASRLVYRKGIDLLAGIIPRFK-NTPNINFIIVGDGPKRDLLEEIREKTNMQERVQMVGAVEHNRVRDFLVRGHIFLN 276
Cdd:pfam00534 5 ILFVGRLEPEKGLDLLIKAFALLKeKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVL 84
|
90 100 110
....*....|....*....|....*....|...
gi 665401714 277 TSLTEAYCMAIVEAASCGLQVVSTSVGGIPEVL 309
Cdd:pfam00534 85 PSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV 117
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
13-308 |
3.08e-22 |
|
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: 97.67 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 13 SIGGVEEHVYNLSQMLLSLGHKIVVLthaygdCSGIRYVTGYLK---VYYLPIKVCYNQCILPTAVCNVPMLRAVLLRER 89
Cdd:cd03808 8 VDGGFQSFRLPLIKALVKKGYEVHVI------APDGDKLSDELKelgVKVIDIPILRRGINPLKDLKALFKLYKLLKKEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 90 VEVVHGHSAFSALahealmVGSL-----LGLKTVFTDHSLfGFAD----LSAALTNNLLEVNLGMVNHAICVSHiGKENT 160
Cdd:cd03808 82 PDIVHCHTPKPGI------LGRLaarlaGVPKVIYTVHGL-GFVFtegkLLRLLYLLLEKLALLFTDKVIFVNE-DDRDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 161 VLRARVAKHRVSVI--PNAVDTALFTPDPQQRPSNDIInIVVASRLVYRKGIDLL---AGIIprFKNTPNINFIIVGDGP 235
Cdd:cd03808 154 AIKKGIIKKKKTVLipGSGVDLDRFQYSPESLPSEKVV-FLFVARLLKDKGIDELieaAKIL--KKKGPNVRFLLVGDGE 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665401714 236 KRDLLEEIREKTNMQERVQMVGAVEHnrVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGIPEV 308
Cdd:cd03808 231 LENPSEILIEKLGLEGRIEFLGFRSD--VPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCREL 301
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
198-309 |
1.00e-20 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 87.95 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 198 IVVASRLV-YRKGIDLLAGIIPRFKNTPN-INFIIVGDGPKRDLLEEIRektNMQERVQMVGAVEHnrVRDFLVRGHIFL 275
Cdd:pfam13692 4 ILFVGRLHpNVKGVDYLLEAVPLLRKRDNdVRLVIVGDGPEEELEELAA---GLEDRVIFTGFVED--LAELLAAADVFV 78
|
90 100 110
....*....|....*....|....*....|....
gi 665401714 276 NTSLTEAYCMAIVEAASCGLQVVSTSVGGIPEVL 309
Cdd:pfam13692 79 LPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV 112
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
2-299 |
3.78e-20 |
|
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: 91.53 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 2 RICmvsdFFYPSI---GGVEEHVYNLSQMLLSLGHKIVVLTHAYGDCSGIRYVTGYLKVYYLPIKVCYNQCILPTAVCNV 78
Cdd:cd03820 1 KIA----IVIPSIsnaGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYELDDNIKIKNLGDRKYSHFKLLLKYFKKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 79 PMLRAVLLRERVEVV--HGHSAFSALAhealMVGslLGLKTVFTDHSlfgfadlSAALTNNLLEVNLGMVNHAICVSHIg 156
Cdd:cd03820 77 RRLRKYLKNNKPDVVisFRTSLLTFLA----LIG--LKSKLIVWEHN-------NYEAYNKGLRRLLLRRLLYKRADKI- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 157 kenTVLRARVAKH-------RVSVIPNAVDTALFTPDPQqRPSNDIINIvvaSRLVYRKGIDLLAGIIPRFKNT-PNINF 228
Cdd:cd03820 143 ---VVLTEADKLKkykqpnsNVVVIPNPLSFPSEEPSTN-LKSKRILAV---GRLTYQKGFDLLIEAWALIAKKhPDWKL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665401714 229 IIVGDGPKRDLLEEIREKTNMQERVQMVGAVEHnrVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVS 299
Cdd:cd03820 216 RIYGDGPEREELEKLIDKLGLEDRVKLLGPTKN--IAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIIS 284
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
89-307 |
4.39e-20 |
|
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: 91.36 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 89 RVEVVHGHSAFSALahEALMVGSLLGLKTVFTDHSLFGFADLSAALTNNLLEVNLGMVNHA--------ICVSHIGKENt 160
Cdd:cd05844 81 APALVHAHFGRDGV--YALPLARALGVPLVVTFHGFDITTSRAWLAASPGWPSQFQRHRRAlqrpaalfVAVSGFIRDR- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 161 VLRARVAKHRVSVIPNAVDTALFTPDPqqrPSNDIINIVVASRLVYRKGIDLL----AGIIPRfknTPNINFIIVGDGPK 236
Cdd:cd05844 158 LLARGLPAERIHVHYIGIDPAKFAPRD---PAERAPTILFVGRLVEKKGCDVLieafRRLAAR---HPTARLVIAGDGPL 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665401714 237 RDLLEEIREKTNmqeRVQMVGAVEHNRVRDFLVRGHIFLNTSLT------EAYCMAIVEAASCGLQVVSTSVGGIPE 307
Cdd:cd05844 232 RPALQALAAALG---RVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPE 305
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
2-307 |
5.22e-20 |
|
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: 91.53 E-value: 5.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 2 RICMVSDFFYPSI-------GGVEEHVYNLSQMLLSLGHKIVVLTHAYGD--------CSGIRYV-------TGYLKVYY 59
Cdd:cd03800 1 RIALISVHGSPLAqpggadtGGQNVYVLELARALAELGYQVDIFTRRISPadpevveiAPGARVIrvpagppEYLPKEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 60 LPikvcYnqciLPTAVCNvpMLRAvLLRE--RVEVVHGHSAFSALAheALMVGSLLGLKTVFTDHSLfG---FADLSAAL 134
Cdd:cd03800 81 WP----Y----LEEFADG--LLRF-IAREggRYDLIHSHYWDSGLV--GALLARRLGVPLVHTFHSL-GrvkYRHLGAQD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 135 TNNL---LEVNLGMVNHAICV-SHIGKENTVLRARVAKH--RVSVIPNAVDTALFTPDPQQR--------PSNDIInIVV 200
Cdd:cd03800 147 TYHPslrITAEEQILEAADRViASTPQEADELISLYGADpsRINVVPPGVDLERFFPVDRAEarrarlllPPDKPV-VLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 201 ASRLVYRKGIDLL---AGIIPRFKntPNINFIIVGdGPKRDLL----EEIREKTNM---QERVQMVGAVEHNRVRDFLVR 270
Cdd:cd03800 226 LGRLDPRKGIDTLvraFAQLPELR--ELANLVLVG-GPSDDPLsmdrEELAELAEElglIDRVRFPGRVSRDDLPELYRA 302
|
330 340 350
....*....|....*....|....*....|....*..
gi 665401714 271 GHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGIPE 307
Cdd:cd03800 303 ADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQD 339
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
15-181 |
3.11e-19 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 84.89 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 15 GGVEEHVYNLSQMLLSLGHKIVVLTHAYGDCSGIRYVTGYLKVYYLPIKVCYNQCILPtavcNVPMLRAVLLRERVEVVH 94
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLA----FLRRLRRLLRRERPDVVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 95 GHSAFSALAhEALMVGSLLGLKTVFTDHSLF-------GFADLSAALTNNLLEVNLGMVNHAICVSHIGKENTVLRARVA 167
Cdd:pfam13439 77 AHSPFPLGL-AALAARLRLGIPLVVTYHGLFpdykrlgARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVP 155
|
170
....*....|....
gi 665401714 168 KHRVSVIPNAVDTA 181
Cdd:pfam13439 156 PEKIRVIPNGVDLE 169
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
3-309 |
2.18e-18 |
|
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: 84.38 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 3 ICMVSDFFYPSIGGVEEHVYNLSQMLLSLGHKIVVLthaygdcsgiryvtGYLKVYYLPIkvcynqcilptavcnvpmlR 82
Cdd:cd01635 1 ILLVTGEYPPLRGGLELHVRALARALAALGHEVTVL--------------ALLLLALRRI-------------------L 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 83 AVLLRERVEVVHGHSAFSALAHeALMVGSLLGLKTVFTDHSLFGFADlsaaltnnllevnlgmvnhaiCVSHIGKENTVL 162
Cdd:cd01635 48 KKLLELKPDVVHAHSPHAAALA-ALLAARLLGIPIVVTVHGPDSLES---------------------TRSELLALARLL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 163 RARVAKHRVSVipnavdtalftpdpqqrpsndiinivvaSRLVYRKGIDLLAGIIPR-FKNTPNINFIIVGDGPKRDLLE 241
Cdd:cd01635 106 VSLPLADKVSV----------------------------GRLVPEKGIDLLLEALALlKARLPDLVLVLVGGGGEREEEE 157
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665401714 242 EIREKTNMQERVQMVGAVEHNRVRDFLVRG-HIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGIPEVL 309
Cdd:cd01635 158 ALAAALGLLERVVIIGGLVDDEVLELLLAAaDVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
2-308 |
8.41e-18 |
|
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: 84.73 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 2 RICMVSDFFYPSIGGVEEHVYNLSQMLLSLGHKIVVLThaYGDC----SGIRYVTGYLKVYYLPIKVCYNQCILPTAVCn 77
Cdd:cd03821 1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVS--TGDGyeslVVEENGRYIPPQDGFASIPLLRQGAGRTDFS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 78 vPMLRAVLLRE--RVEVVHGHSAFSALAHEALMVGSLLGLKTVFTDHSLFGFADLSAALTNNLLEVNL---GMVNHAICV 152
Cdd:cd03821 78 -PGLPNWLRRNlrEYDVVHIHGVWTYTSLAACKLARRRGIPYVVSPHGMLDPWALQQKHWKKRIALHLierRNLNNAALV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 153 SHIG-KENTVLRARVAKHRVSVIPNAVDTALFTPDPQQR----PSNDIINIVVASRLVYRKGIDLLAGIIPRFKN-TPNI 226
Cdd:cd03821 157 HFTSeQEADELRRFGLEPPIAVIPNGVDIPEFDPGLRDRrkhnGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEqGRDW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 227 NFIIVG-DGPKRDLLEEIREKTNMQERVQMVGAVEHNRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGI 305
Cdd:cd03821 237 HLVIAGpDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGL 316
|
...
gi 665401714 306 PEV 308
Cdd:cd03821 317 SEL 319
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
84-308 |
8.69e-18 |
|
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: 84.71 E-value: 8.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 84 VLLRERVEVVHGHSAFSAlAHEALMVGSLLG--LKTVFTDH----SLFGfADLSAAltnnllevnlGMVNHAI------- 150
Cdd:cd04962 79 VAKEHKLDVLHAHYAIPH-ASCAYLAREILGekIPIVTTLHgtdiTLVG-YDPSLQ----------PAVRFSInksdrvt 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 151 CVSHIGKENTVLRARVAKhRVSVIPNAVDTALFTPDPQQR--------PSNDIINIVVASRLVyrKGIDLLAGIIPRFKN 222
Cdd:cd04962 147 AVSSSLRQETYELFDVDK-DIEVIHNFIDEDVFKRKPAGAlkrrllapPDEKVVIHVSNFRPV--KRIDDVVRVFARVRR 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 223 TPNINFIIVGDGPKRDLLEEIREKTNMQERVQMVGAVEHnrVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSV 302
Cdd:cd04962 224 KIPAKLLLVGDGPERVPAEELARELGVEDRVLFLGKQDD--VEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNA 301
|
....*.
gi 665401714 303 GGIPEV 308
Cdd:cd04962 302 GGIPEV 307
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
2-310 |
1.86e-17 |
|
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: 83.88 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 2 RICMVSDFFYPSIGGVEEHVYNLSQMLLSLGHKIVVLT--HAYGDCSGIRYVTGylkVYYLPIKVcYNQCILptAVCNVP 79
Cdd:cd03814 1 RIALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVApgPFDEAESAEGRVVS---VPSFPLPF-YPEYRL--ALPLPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 80 MLRAVLLRERVEVVHGHSAFSaLAHEALMVGSLLGLKTVFTDHSLF-------GFADLSAALTNNLLEVNlGMVNHAICV 152
Cdd:cd03814 75 RVRRLIKEFQPDIIHIATPGP-LGLAALRAARRLGLPVVTSYHTDFpeylsyyTLGPLSWLAWAYLRWFH-NPFDTTLVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 153 SH-IGKEntvLRARVAKhRVSVIPNAVDTALFTPDPQQR-------PSNDIInIVVASRLVYRKGIDLLAGIIPRFKNTP 224
Cdd:cd03814 153 SPsIARE---LEGHGFE-RVRLWPRGVDTELFHPSRRDAalrrrlgPPGRPL-LLYVGRLAPEKNLEALLDADLPLAASP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 225 NINFIIVGDGPKRDLLEEirekTNMQerVQMVGAvehnRVRDFLVR----GHIFLNTSLTEAYCMAIVEAASCGLQVVST 300
Cdd:cd03814 228 PVRLVVVGDGPARAELEA----RGPD--VIFTGF----LTGEELARayasADVFVFPSRTETFGLVVLEAMASGLPVVAA 297
|
330
....*....|
gi 665401714 301 SVGGIPEVLP 310
Cdd:cd03814 298 DAGGPRDIVR 307
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-309 |
3.63e-16 |
|
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: 80.08 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 2 RICMVSDFFYPSIGGVEEHVYNLSQMLLSLGHKIVVLTHAYGDCSGIRYVTGY-----LKVYYLPIKVCYNQCILPTAVC 76
Cdd:cd03794 1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGATetkdgIRVIRVKLGPIKKNGLIRRLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 77 NVP-----MLRAVLLRERVEVVHGHS--AFSALAheALMVGSLLGLKTVFTDHSLFGFADLSA-ALTNNLL--------E 140
Cdd:cd03794 81 YLSfalaaLLKLLVREERPDVIIAYSppITLGLA--ALLLKKLRGAPFILDVRDLWPESLIALgVLKKGSLlkllkkleR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 141 VNLGMVNHAICVSHIGKENtVLRARVAKHRVSVIPNAVDTALFTPDPQQ-----RPSNDIINIVVASRLVYRKGIDLLAG 215
Cdd:cd03794 159 KLYRLADAIIVLSPGLKEY-LLRKGVPKEKIIVIPNWADLEEFKPPPKDelrkkLGLDDKFVVVYAGNIGKAQGLETLLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 216 IIPRFKNTPNINFIIVGDGPKRDLLEEIREKTNMQeRVQMVGAVEHNRVRDFLVRGHIFLNTSLTEAYCMAIV-----EA 290
Cdd:cd03794 238 AAERLKRRPDIRFLFVGDGDEKERLKELAKARGLD-NVTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGSSpsklfEY 316
|
330
....*....|....*....
gi 665401714 291 ASCGLQVVSTSVGGIPEVL 309
Cdd:cd03794 317 MAAGKPILASDDGGSDLAV 335
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
178-309 |
8.48e-16 |
|
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.
Pssm-ID: 340829 [Multi-domain] Cd Length: 350 Bit Score: 78.65 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 178 VDTALFTPDPQQRPSNDIINIVVASRLVYRKGIDLLAGIIPRFKNT-PNINFIIVGDGPKRDLLEEIREKTNMQERVQMV 256
Cdd:cd03799 157 IDCNKFRFKPRYLPLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKyPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLL 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 665401714 257 GAVEHNRVRDFLVRGHIFLNTSLT------EAYCMAIVEAASCGLQVVSTSVGGIPEVL 309
Cdd:cd03799 237 GWKPQEEIIEILDEADIFIAPSVTaadgdqDGPPNTLKEAMAMGLPVISTEHGGIPELV 295
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
168-309 |
3.85e-14 |
|
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general 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 in bacteria.
Pssm-ID: 340857 [Multi-domain] Cd Length: 360 Bit Score: 73.63 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 168 KHRVSVIPNAVDTALFTPDPQQRP--------SNDIINIVVASRLVYRKG-IDLLAGIIPRFKNTPNINFIIVGDGPKRD 238
Cdd:cd04951 153 KNKSVPVYNGIDLNKFKKDINVRLkirnklnlKNDEFVILNVGRLTEAKDyPNLLLAISELILSKNDFKLLIAGDGPLRN 232
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665401714 239 LLEEIREKTNMQERVQMVGAveHNRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGIPEVL 309
Cdd:cd04951 233 ELERLICNLNLVDRVILLGQ--ISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVV 301
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
2-304 |
3.09e-13 |
|
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: 70.77 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 2 RICMVSDFFYPSIGGVEEHVYNLSQMLLSLGHKIVVLThAYGDCSGIRYVTGYLKVyylpIKVCYNQCILPTAVCNVPML 81
Cdd:cd03795 1 KVLHVFKFYYPDIGGIEQVIYDLAEGLKKKGIEVDVLC-FSKEKETPEKEENGIRI----HRVKSFLNVASTPFSPSYIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 82 RAVLLRERVEVVHGHSAFSaLAHEALMVGSLLGlKTVFTDHSLF----GFADLSAALTNNLLEvnlgMVNHAICVSHIGK 157
Cdd:cd03795 76 RFKKLAKEYDIIHYHFPNP-LADLLLFFSGAKK-PVVVHWHSDIvkqkKLLKLYKPLMTRFLR----RADRIIATSPNYV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 158 ENT-VLRArvAKHRVSVIPNAVDTALFTPDPQQRPS----NDIINIVVA-SRLVYRKGIDLL---AGIIprfkntpNINF 228
Cdd:cd03795 150 ETSpTLRE--FKNKVRVIPLGIDKNVYNIPRVDFENikreKKGKKIFLFiGRLVYYKGLDYLieaAQYL-------NYPI 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665401714 229 IIVGDGPKRDLLEEIREKtNMQERVQMVGAVEHNRVRDFLVRGHIFLNTSL--TEAYCMAIVEAASCGLQVVSTSVGG 304
Cdd:cd03795 221 VIGGEGPLKPDLEAQIEL-NLLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVISTNIGT 297
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
15-310 |
2.79e-11 |
|
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.
Pssm-ID: 340832 [Multi-domain] Cd Length: 333 Bit Score: 64.62 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 15 GGVEEHVYNLSQMLLSLGHKIVVLTHA--YGDCSGIRYVTGYLKVyylpikvcyNQCILPTAVCNVP-MLRAVLLRERVE 91
Cdd:cd03802 18 GGTELVVSALTEGLVRRGHEVTLFAPGdsHTSAPLVAVIPRALRL---------DPIPQESKLAELLeALEVQLRASDFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 92 VVHGHSAfsalaHEALMVGSLLGLKTVFTDHSLFGFADLSAALTNNLlevnlgmvNHAICVSHIGKentvlRARVAKHRV 171
Cdd:cd03802 89 VIHNHSY-----DWLPPFAPLIGTPFVTTLHGPSIPPSLAIYAAEPP--------VNYVSISDAQR-----AATPPIDYL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 172 SVIPNAVDTALFTPDPQQRPsndiiNIVVASRLVYRKGIDLLAgiipRFKNTPNINFIIVGDGPKRDLLEEIREKtNMQE 251
Cdd:cd03802 151 TVVHNGLDPADYRFQPDPED-----YLAFLGRIAPEKGLEDAI----RVARRAGLPLKIAGKVRDEDYFYYLQEP-LPGP 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 252 RVQMVGAVEHNRVRDFLVRGHIFLNTSL-TEAYCMAIVEAASCGLQVVSTSVGGIPEVLP 310
Cdd:cd03802 221 RIEFIGEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQ 280
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
14-298 |
1.23e-10 |
|
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: 62.69 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 14 IGGVEEHVYNLSQMLLSLGHKIVVLTHAYGDCSGIRYV--TGyLKVYYLPIKVCYNqcilPTAVCNVPMLRAVllrERVE 91
Cdd:cd03812 11 VGGIETFLMNLYRKLDKSKIEFDFLATSDDKGEYDEELeeLG-GKIFYIPPKKKNI----IKYFIKLLKLIKK---EKYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 92 VVHGHSAFSALAHEALMVgsLLGLKT-VFTDH-----SLFGFADLSAALTNnLLEVNlgmVNHAICVSHIGKENtvLRAR 165
Cdd:cd03812 83 IVHVHGSSSNGIILLLAA--KAGVPVrIAHSHntkdsSIKLRKIRKNVLKK-LIERL---STKYLACSEDAGEW--LFGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 166 VAKHRVSVIPNAVDTALFTPDPQQR--------PSNDIINIVVAsRLVYRKG----IDLLAGIIprfKNTPNINFIIVGD 233
Cdd:cd03812 155 VENGKFKVIPNGIDIEKYKFNKEKRrkrrklliLEDKLVLGHVG-RFNEQKNhsflIDIFEELK---KKNPNVKLVLVGE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665401714 234 GPkrdLLEEIREKTNM---QERVQMVGAVehNRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVV 298
Cdd:cd03812 231 GE---LKEKIKEKVKElglEDKVIFLGFR--NDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCL 293
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
82-246 |
2.26e-10 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 62.42 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 82 RAVL-----LRERVEVVHGH---SAF-SALAHEALMVGSLLGLKTVFTDHSL-----FGFADLSA------ALTNNLLE- 140
Cdd:COG0297 117 RAALellkgLDWKPDIIHCHdwqTGLiPALLKTRYADDPFKRIKTVFTIHNLayqgiFPAEILELlglppeLFTPDGLEf 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 141 ---VNL--GMVNHAicvSHIgkeNTV--------------------LRARvaKHRVSVIPNAVDTALFTP--DP------ 187
Cdd:COG0297 197 ygqINFlkAGIVYA---DRV---TTVsptyareiqtpefgegldglLRAR--SGKLSGILNGIDYDVWNPatDPylpany 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 188 ---------------QQR----PSNDIINIVVASRLVYRKGIDLLAGIIPRFKNTpNINFIIVGDGPKR--DLLEEIREK 246
Cdd:COG0297 269 saddlegkaankaalQEElglpVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEE-DVQLVVLGSGDPEyeEAFRELAAR 347
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
169-309 |
5.28e-10 |
|
glycosyltransferase family 4 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, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340841 [Multi-domain] Cd Length: 474 Bit Score: 61.58 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 169 HRVSVIPNAVDTALFTPDPQQRPSNDIINIVVASRLVYRKGIDLLagiIPRFK----NTPNINFIIVG---DGPkrDLLE 241
Cdd:cd03813 267 DKTRVIPNGIDIQRFAPAREERPEKEPPVVGLVGRVVPIKDVKTF---IRAFKlvrrAMPDAEGWLIGpedEDP--EYAQ 341
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665401714 242 EIRE---KTNMQERVQMVGAVehnRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGIPEVL 309
Cdd:cd03813 342 ECKRlvaSLGLENKVKFLGFQ---NIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELI 409
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
170-299 |
1.55e-09 |
|
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general 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 in bacteria.
Pssm-ID: 340855 [Multi-domain] Cd Length: 328 Bit Score: 59.24 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 170 RVSVIPNA-VDTALFTPDPQQRPSNDIINIvvaSRLVYRKGIDLLAGIIPRFKNT-PNINFIIVGDGPKRDLLEEIREKT 247
Cdd:cd04949 137 PIFTIPVGyVDQLDTAESNHERKSNKIITI---SRLAPEKQLDHLIEAVAKAVKKvPEITLDIYGYGEEREKLKKLIEEL 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 665401714 248 NMQERVQMVGAveHNRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVS 299
Cdd:cd04949 214 HLEDNVFLKGY--HSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVS 263
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
151-309 |
3.24e-09 |
|
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.
Pssm-ID: 340854 [Multi-domain] Cd Length: 401 Bit Score: 58.63 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 151 CVSHIGKENTVLRARVAKHRVSVIpnavdtALFTPDPQQRPS---NDIINIVVASRLVYRKGIDLLAGIIPRF---KNTP 224
Cdd:cd04946 183 LISKEGKDYLQKCYPAYKEKIFVS------RLGVSDKEQYSKvkkEGDLRLVSCSSIVPVKRIDLIIETLNSLcvaHPSI 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 225 NINFIIVGDGP-KRDLLEEIREKTNMQeRVQMVGAVEHNRVRDFLVRG--HIFLNTSLTEAYCMAIVEAASCGLQVVSTS 301
Cdd:cd04946 257 CISWTHIGGGPlKERLEKLAENKLENV-KVNFTGEVSNKEVKQLYKENdvDVFVNVSESEGIPVSIMEAISFGIPVIATN 335
|
....*...
gi 665401714 302 VGGIPEVL 309
Cdd:cd04946 336 VGGTREIV 343
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
2-320 |
5.94e-09 |
|
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 57.76 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 2 RICMVSDFFYPSIGGVEEHVYNLSQMLLSLGHKIVVLTHAYGDCSGIRYVTGYLKVYYLPIKVCYNQCILPTAVcnvpML 81
Cdd:cd03809 1 KILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRW----LQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 82 RAVLLRERVEVVHGHSafsalaHEALMvgSLLGLKTVFTDHSL--FGFADLSAALTNNLLEVNLGMV----NHAICVSHI 155
Cdd:cd03809 77 ILLPKKDKPDLLHSPH------NTAPL--LLKGCPQVVTIHDLipLRYPEFFPKRFRLYYRLLLPISlrraDAIITVSEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 156 GKENTVLRARVAKHRVSVIPNAVDTALFTPDPQQRPSNDII----NIVVASRLVYRKGIDLLAGIIPRFK-NTPNINFII 230
Cdd:cd03809 149 TRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLlpepYFLYVGTLEPRKNHERLLKAFALLKkQGGDLKLVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 231 VG-DGPKRDLLEEIREKTNMQERVQMVGAVEHNRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGIPEVL 309
Cdd:cd03809 229 VGgKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVA 308
|
330
....*....|.
gi 665401714 310 PKSlILLAEPE 320
Cdd:cd03809 309 GDA-ALYFDPL 318
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
170-309 |
9.73e-09 |
|
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: 56.96 E-value: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 170 RVSVIPNAVDTALFTPDPQQ--RPSNDII---NIVVASRLVY---RKGIDLLAGIIPRFKNTPNINFIIVGDGPKRDL-- 239
Cdd:cd03825 162 PVVVIPNGIDTEIFAPVDKAkaRKRLGIPqdkKVILFGAESVtkpRKGFDELIEALKLLATKDDLLLVVFGKNDPQIVil 241
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665401714 240 ------LEEIREKTnmqervqmvgavehnRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGIPEVL 309
Cdd:cd03825 242 pfdiisLGYIDDDE---------------QLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIV 302
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
15-177 |
4.38e-08 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 52.40 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 15 GGVEEHVYNLSQMLLSLGHKIVVLTHAYGDCSGIRYVTGyLKVYYLPikVCYNQcILPTAVCNVPMLRAVLLRERVEVVH 94
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDG-VRVHRLP--VPPRP-SPLADLAALRRLRRLLRAERPDVVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 95 GHSAFSALAheALMVGSLLGLKTVFTDHSLfGFADLSAALTNNLLEVNLGMVNHA---ICVSHIGKEnTVLRARVAKHRV 171
Cdd:pfam13579 77 AHSPTAGLA--ARLARRRRGVPLVVTVHGL-ALDYGSGWKRRLARALERRLLRRAdavVVVSEAEAE-LLRALGVPAARV 152
|
....*.
gi 665401714 172 SVIPNA 177
Cdd:pfam13579 153 VVVPNG 158
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
155-311 |
1.63e-07 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 53.56 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 155 IGKENTVLRARVAKhRVSVIPNAVDTALFTP-----DPQQRPSN---DIINIVVASRLVYRKGIDLLAGIIPRFkntPNI 226
Cdd:PLN02871 216 LGKELEAAGVTAAN-RIRVWNKGVDSESFHPrfrseEMRARLSGgepEKPLIVYVGRLGAEKNLDFLKRVMERL---PGA 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 227 NFIIVGDGPKRDLLEEIREKTNmqerVQMVGAVEHNRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGIP 306
Cdd:PLN02871 292 RLAFVGDGPYREELEKMFAGTP----TVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIP 367
|
....*
gi 665401714 307 EVLPK 311
Cdd:PLN02871 368 DIIPP 372
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
76-309 |
7.98e-07 |
|
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).
Pssm-ID: 340845 [Multi-domain] Cd Length: 396 Bit Score: 51.21 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 76 CNVPMLRAVLLRE--RVEVVHGHSAFsalahealmvGSLLGLKTVFTDHSLFGFADL----SAALTNNLLE--------V 141
Cdd:cd03818 74 QAVLRALLALKREgfRPDVVVGHPGW----------GEALFVKDVFPDVPLIGYCEYyyraEGADVGFDPEfpldlmirC 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 142 NLGMVNHAICVSHIGKENTVLRAR--------VAKHRVSVIPNAVDTALFTPDPQQRPSNDIINIVVASRLV-------- 205
Cdd:cd03818 144 RLRNRNIALLLSLEQADLGVTPTRwqrslfpaAYRDRISVIHDGVDTDRLAPDPAARLRLLNGTELKAGDPVityvarnl 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 206 --YRkGIDLLAGIIPRFKNT-PNINFIIVGD------GPKRD-------LLEEIREKtnmQERVQMVGAVEHNRVRDFLV 269
Cdd:cd03818 224 epYR-GFHVFMRALPRIQARrPDARVVVVGGdgvsygSPPPDggswkqkMLAELGVD---LERVHFVGKVPYDQYVRLLQ 299
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 665401714 270 RG--HIFlntsLTEAYCM--AIVEAASCGLQVVSTSVGGIPEVL 309
Cdd:cd03818 300 LSdaHVY----LTYPFVLswSLLEAMACGCPVIGSDTAPVREVI 339
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
163-319 |
1.07e-06 |
|
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: 50.75 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 163 RARVAK--HRVS-VIPNAVDTALFTPDPqqrPSNDIIniVVASRLVYRKGIDLlagIIPRFKNTPNiNFIIVGDGPKrdl 239
Cdd:cd03804 169 ARRIKKfyGREStVIYPPVDTDAFAPAA---DKEDYY--LTASRLVPYKRIDL---AVEAFNELPK-RLVVIGDGPD--- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 240 LEEIREKTnmQERVQMVGAVEHNRVRDFLVRGHIFLNTSlTEAYCMAIVEAASCGLQVVSTSVGGIPEVLP--KSLILLA 317
Cdd:cd03804 237 LDRLRAMA--SPNVEFLGYQPDEVLKELLSKARAFVFAA-EEDFGIVPVEAQACGTPVIAFGKGGALETVRpgPTGILFG 313
|
..
gi 665401714 318 EP 319
Cdd:cd03804 314 EQ 315
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
267-309 |
1.68e-06 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 46.91 E-value: 1.68e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 665401714 267 FLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVSTSVGGIPEVL 309
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVI 59
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
221-307 |
8.37e-06 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 48.49 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 221 KNTPNINFIIVGDGPKRDLLEEIREKTNMQERVQMVGAveHNRVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVST 300
Cdd:PRK15179 544 ASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGL--SRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTT 621
|
....*..
gi 665401714 301 SVGGIPE 307
Cdd:PRK15179 622 LAGGAGE 628
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
161-246 |
1.29e-05 |
|
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: 47.56 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 161 VLRARvaKHRVSVIPNAVDTALFTP--DP---------------------QQR----PSNDIINIVVASRLVYRKGIDLL 213
Cdd:cd03791 235 VLRAR--AGKLSGILNGIDYDEWNPatDKlipanysandlegkaenkaalQKElglpVDPDAPLFGFVGRLTEQKGVDLI 312
|
90 100 110
....*....|....*....|....*....|....*....
gi 665401714 214 AGIIPRFKNTpNINFIIVGDGPK------RDLLEEIREK 246
Cdd:cd03791 313 LDALPELLEE-GGQLVVLGSGDPeyeqafRELAERYPGK 350
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
163-319 |
1.81e-05 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 46.71 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 163 RARVAKHRVSVIPNAVDTALFTPDPQQR-------PSNDIInIVVASRLVYRKGIDLLAGIIPRF-KNTPNINFIIVGD- 233
Cdd:PRK15484 155 EERLPNADISIVPNGFCLETYQSNPQPNlrqqlniSPDETV-LLYAGRISPDKGILLLMQAFEKLaTAHSNLKLVVVGDp 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 234 -----GPKRDLLEEIREKTN-MQERVQMVGAVE----HN--RVRDFLVrghifLNTSLTEAYCMAIVEAASCGLQVVSTS 301
Cdd:PRK15484 234 tasskGEKAAYQKKVLEAAKrIGDRCIMLGGQPpekmHNyyPLADLVV-----VPSQVEEAFCMVAVEAMAAGKPVLAST 308
|
170 180
....*....|....*....|
gi 665401714 302 VGGIPE-VLPKSL-ILLAEP 319
Cdd:PRK15484 309 KGGITEfVLEGITgYHLAEP 328
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
161-234 |
1.58e-03 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 40.87 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 161 VLRARVAKhrVSVIPNAVDTALFTP--DP---------------------QQR---PSNDIINIVVASRLVYRKGIDLLA 214
Cdd:PRK00654 224 LLRARSGK--LSGILNGIDYDIWNPetDPllaanysaddlegkaenkralQERfglPDDDAPLFAMVSRLTEQKGLDLVL 301
|
90 100
....*....|....*....|.
gi 665401714 215 GIIPRF-KNtpNINFIIVGDG 234
Cdd:PRK00654 302 EALPELlEQ--GGQLVLLGTG 320
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
161-242 |
1.60e-03 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 40.73 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 161 VLRAR---VAKHRVSVIPNAVDTALFTPDPQQR----------PSNDIInIVVASRLVYRKGIDLLAGIIPRFKNTPNIN 227
Cdd:PRK10307 183 MNKARekgVAAEKVIFFPNWSEVARFQPVADADvdalraqlglPDGKKI-VLYSGNIGEKQGLELVIDAARRLRDRPDLI 261
|
90
....*....|....*
gi 665401714 228 FIIVGDGPKRDLLEE 242
Cdd:PRK10307 262 FVICGQGGGKARLEK 276
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
220-307 |
3.75e-03 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 39.68 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665401714 220 FKNTPNINFIIVGDGPKRDLLEEIREKTNMQERVQMVGAVEHnrVRDFLVRGHIFLNTSLTEAYCMAIVEAASCGLQVVS 299
Cdd:PRK15490 424 LQHHPATRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRD--VGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVIS 501
|
....*...
gi 665401714 300 TSVGGIPE 307
Cdd:PRK15490 502 TPAGGSAE 509
|
|
| |
