|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
34-433 |
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: 732.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 34 NICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVITVTHAYGNRKGVRYLTNGLKVYYLPLRVMYNQSTATTLFHSLPLL 113
Cdd:cd03796 1 RICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVITHAYGNRVGVRYLTNGLKVYYLPFKVFYNQSTLPTLFSTFPLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 114 RYIFVRERITIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNHIICVSYTSKENTV 193
Cdd:cd03796 81 RNILIRERIQIVHGHQAFSSLAHEALFHARTLGLKTVFTDHSLFGFADASSILTNKLLRFSLADIDHVICVSHTSKENTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 194 LRAALNPEIVSVIPNAVDPTDFTPEPFRRHDSVITVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLIGGEGPKRIILE 273
Cdd:cd03796 161 LRASLDPRIVSVIPNAVDSSDFTPDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 274 EVRERYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLPENLIILCEPSV 353
Cdd:cd03796 241 EMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 354 KSLCEGLEKAIFQVKSGTlPAPENIHNVVKTFYTWRNVAERTEKVYERVSKESVLPMHKRLdRLISHCGPVTGYIFALLA 433
Cdd:cd03796 321 EDIVRKLEEAISILRTGK-HDPWSFHNRVKKMYSWEDVARRTEKVYDRILSTPNRPFLERL-KRYYNCGPIAGKIFCLLA 398
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
34-400 |
4.00e-55 |
|
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: 188.13 E-value: 4.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 34 NICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVITVTHAYGNRKGVRYLTNGLKVYYLPLRVMYnqstatTLFHSLPLL 113
Cdd:cd03801 1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALL------RARRLLREL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 114 RYIFVRERITIIHSHSSFSAMAHDALFHAKtmGLQTVFTDHSLFGF------ADVSSVLTNKLLTVSLCDtnHIICVSYT 187
Cdd:cd03801 75 RPLLRLRKFDVVHAHGLLAALLAALLALLL--GAPLVVTLHGAEPGrlllllAAERRLLARAEALLRRAD--AVIAVSEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 188 SKENTVLRAALNPEIVSVIPNAVDPTDFTPEPFRRH---DSVITVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLI-G 263
Cdd:cd03801 151 LRDELRALGGIPPEKIVVIPNGVDLERFSPPLRRKLgipPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIvG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 264 GEGPKRiilEEVRER-YQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLP 342
Cdd:cd03801 231 GDGPLR---AELEELeLGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVE 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807754 343 --ENLIILCEPSVKSLCEGLEKAIfqvKSGTLPAP--ENIHNVVKTFYTWRNVAERTEKVYE 400
Cdd:cd03801 308 dgEGGLVVPPDDVEALADALLRLL---ADPELRARlgRAARERVAERFSWERVAERLLDLYR 366
|
|
| PIGA |
pfam08288 |
PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol ... |
72-161 |
9.80e-52 |
|
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: 170.13 E-value: 9.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 72 HAYGNRKGVRYLTNGLKVYYLPLRVMYNQSTATTLFHSLPLLRYIFVRERITIIHSHSSFSAMAHDALFHAKTMGLQTVF 151
Cdd:pfam08288 1 HAYGDRTGVRYLTNGLKVYYVPFLVIYRQSTFPTVFGTFPLFRNILLRERIDIVHGHGSFSTLAHEAILHARTMGLKTVF 80
|
90
....*....|
gi 1958807754 152 TDHSLFGFAD 161
Cdd:pfam08288 81 TDHSLFGFAD 90
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
35-351 |
7.11e-39 |
|
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: 144.42 E-value: 7.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 35 ICMVSDFFYpnMGGVESHIYQLSQCLIERGHKVITVTHAYGNRKGVRYLTNGLKVYYLPLRVMYNqstattlfhSLPLLR 114
Cdd:cd03819 1 ILMLTPALE--IGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGIGLPGLKVPLLRALL---------GNVRLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 115 YIFVRERITIIHSHSSFSAMAhdALFHAKTMGLQTVFTDHSLfgfaDVSSVLTNKLLTVSLCDTNHIICVSYTSKENTVL 194
Cdd:cd03819 70 RLIRRERIDLIHAHSRAPAWL--GWLASRLTGVPLVTTVHGS----YLATYHPKDFALAVRARGDRVIAVSELVRDHLIE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 195 RAALNPEIVSVIPNAVDPTDFTPEPFRRH-------DSVITVVVVSRLVYRKGTDLLSGIIPELcQKYQELNFLIGGEGP 267
Cdd:cd03819 144 ALGVDPERIRVIPNGVDTDRFPPEAEAEEraqlglpEGKPVVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAGDGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 268 KRIILEEVRERYQLHDRVQLLGAleHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLPENLII 347
Cdd:cd03819 223 ERDEIRRLVERLGLRDRVTFTGF--REDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTG 300
|
....
gi 1958807754 348 LCEP 351
Cdd:cd03819 301 LLVP 304
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
41-368 |
6.77e-33 |
|
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: 127.86 E-value: 6.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 41 FFYPNM--GGVESHIYQLSQCLIERGHKVITVTHAYGNRKgVRYLTNGLKVYYLPLRVMYNQSTAttLFHSLPLLRYIFV 118
Cdd:cd03811 4 FVIPSLsgGGAERVLLNLANALDKRGYDVTLVLLRDEGDL-DKQLNGDVKLIRLLIRVLKLIKLG--LLKAILKLKRILK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 119 RERITIIHSHSSFSAmahDALFHAKTMGLQTVFTDHSlfgFADVSSVLTNKLLTVSLC--DTNHIICVSYTSKENTVLRA 196
Cdd:cd03811 81 RAKPDVVISFLGFAT---YIVAKLAAARSKVIAWIHS---SLSKLYYLKKKLLLKLKLykKADKIVCVSKGIKEDLIRLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 197 ALNPEIVSVIPNAVDPTDFTPEP----FRRHDSVITVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLIGGEGPKRIIL 272
Cdd:cd03811 155 PSPPEKIEVIYNPIDIDRIRALAkepiLNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 273 EEVRERYQLHDRVQLLGalEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLPENL-IILCEP 351
Cdd:cd03811 235 EKLAKELGLAERVIFLG--FQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGEnGLLVPD 312
|
330
....*....|....*..
gi 1958807754 352 SVKSLCEGLEKAIFQVK 368
Cdd:cd03811 313 GDAAALAGILAALLQKK 329
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
34-402 |
1.88e-32 |
|
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: 127.01 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 34 NICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVITVT----HAYGNRKGVRYLTNGLkvyylPLRVMYNQSTATTLFHS 109
Cdd:cd03817 1 KIAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITpsdpGAEDEEEVVRYRSFSI-----PIRKYHRQHIPFPFKKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 110 LPLlryIFVRERITIIHSHSSFSAMAHdALFHAKTMGLQTVFTDHSL---------FGFADVSSVLtnKLLTVSLCD-TN 179
Cdd:cd03817 76 VID---RIKELGPDIIHTHTPFSLGKL-GLRIARKLKIPIVHTYHTMyedylhyipKGKLLVKAVV--RKLVRRFYNhTD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 180 HIICVSYTSKEntVLRAALNPEIVSVIPNAVDPTDFTPEP---FRRH----DSVITVVVVSRLVYRKGTDLLSGIIPELC 252
Cdd:cd03817 150 AVIAPSEKIKD--TLREYGVKGPIEVIPNGIDLDKFEKPLnteERRKlglpPDEPILLYVGRLAKEKNIDFLLRAFAELK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 253 QKyQELNFLIGGEGPKRIILEEVRERYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVST 332
Cdd:cd03817 228 KE-PNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAA 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807754 333 KVGGIPEVLpENLI--ILCEPSVKSLCEGLEKAIFQVKSGTLPApENIHNVVKTFytwrNVAERTEKVYERV 402
Cdd:cd03817 307 KDPAASELV-EDGEngFLFEPNDETLAEKLLHLRENLELLRKLS-KNAEISAREF----AFAKSVEKLYEEV 372
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
41-402 |
8.32e-32 |
|
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: 125.57 E-value: 8.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 41 FFYPN--MGGVESHIYQLSQCLIERGHKVITVT------HAYGNRKGVRYLTNGLKVYYLPLRVMYNQSTATTLFHSLPL 112
Cdd:cd03798 6 NIYPNanSPGRGIFVRRQVRALSRRGVDVEVLApapwgpAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAPSLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 113 -LRYIFVRERITIIHSHSSFSAMAHDALFHAKTmGLQTVFTDHS--LFGFADVSSVLTNKLLTVSLCDtnhiiCVSYTSK 189
Cdd:cd03798 86 kLLKRRRRGPPDLIHAHFAYPAGFAAALLARLY-GVPYVVTEHGsdINVFPPRSLLRKLLRWALRRAA-----RVIAVSK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 190 E--NTVLRAALNPEIVSVIPNAVDPTDFTPEPFRRH--DSVITVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLIGGE 265
Cdd:cd03798 160 AlaEELVALGVPRDRVDVIPNGVDPARFQPEDRGLGlpLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 266 GPKRIILEEVRERYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVL-PEN 344
Cdd:cd03798 240 GPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVgDPE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807754 345 LIILCEP-SVKSLCEGLEKAIFQVKSGTLPApENIHNVVKTFyTWRNVAERTEKVYERV 402
Cdd:cd03798 320 TGLLVPPgDADALAAALRRALAEPYLRELGE-AARARVAERF-SWVKAADRIAAAYRDV 376
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
45-364 |
8.53e-32 |
|
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: 125.12 E-value: 8.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 45 NMGGVESHIYQL--SQCLIERGHKVITVTH--AYGNRkgvrYLTNGLKVYYLPLrvmynqstatTLFHSLP-LLRYI--F 117
Cdd:cd03807 10 NVGGAETMLLRLleHMDKSRFEHVVISLTGdgVLGEE----LLAAGVPVVCLGL----------SSGKDPGvLLRLAklI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 118 VRERITIIHSHssfsaMAHDALFHAKTMGLQ----TVFTDHSLFGFADVSSVL--TNKLLTVSLCDTnhiICVSYTSKEn 191
Cdd:cd03807 76 RKRNPDVVHTW-----MYHADLIGGLAAKLAggvkVIWSVRSSNIPQRLTRLVrkLCLLLSKFSPAT---VANSSAVAE- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 192 TVLRAALNPEIVSVIPNAVDPTDFTPEPFRRH---------DSVITVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLI 262
Cdd:cd03807 147 FHQEQGYAKNKIVVIYNGIDLFKLSPDDASRArarrrlglaEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 263 GGEGPKRIILEEVRERYQLHDRVQLLGalEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLP 342
Cdd:cd03807 227 VGRGPERPNLERLLLELGLEDRVHLLG--ERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVD 304
|
330 340
....*....|....*....|...
gi 1958807754 343 ENLIILCEP-SVKSLCEGLEKAI 364
Cdd:cd03807 305 DGTGFLVPAgDPQALADAIRALL 327
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
45-364 |
1.19e-28 |
|
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: 116.16 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 45 NMGGVESHIYQLSQCLIERGHKVITVTHAYGNRK------GVRYLTNGLKVyyLPLRVMYNqstattlFHSLPLLRYIFV 118
Cdd:cd03808 8 VDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSdelkelGVKVIDIPILR--RGINPLKD-------LKALFKLYKLLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 119 RERITIIHSHSSFSAM-AHDALFHAKTMglQTVFTDHSLfGFADVSSVLTNKLLTV----SLCDTNHIICVSYTSKENTV 193
Cdd:cd03808 79 KEKPDIVHCHTPKPGIlGRLAARLAGVP--KVIYTVHGL-GFVFTEGKLLRLLYLLleklALLFTDKVIFVNEDDRDLAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 194 -LRAALNPEIVSVIPNAVDPTDFTPEPFRRHDSVITVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLIGGEGPKRIIL 272
Cdd:cd03808 156 kKGIIKKKKTVLIPGSGVDLDRFQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 273 EEVRERYQLHDRVQLLGalEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPE-VLPENLIILCEP 351
Cdd:cd03808 236 EILIEKLGLEGRIEFLG--FRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRElVIDGVNGFLVPP 313
|
330
....*....|....
gi 1958807754 352 -SVKSLCEGLEKAI 364
Cdd:cd03808 314 gDVEALADAIEKLI 327
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
45-331 |
7.23e-26 |
|
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: 108.09 E-value: 7.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 45 NMGGVESHIYQLSQCLIERGHKVITVTHAYGNRKGVRYLTNGLKVYYLPLRVMYNQSTATTLFHSLPLLRYIFVRER--I 122
Cdd:cd03820 11 NAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYELDDNIKIKNLGDRKYSHFKLLLKYFKKVRRLRKYLKNNKpdV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 123 TIIHSHSSFSAMAhdalfhAKTMGLQTVFTDHSLFGFA-DVSSVLTNKLLTVSLCDTnhIICVSYTSKENTVLRAALNpe 201
Cdd:cd03820 91 VISFRTSLLTFLA------LIGLKSKLIVWEHNNYEAYnKGLRRLLLRRLLYKRADK--IVVLTEADKLKKYKQPNSN-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 202 iVSVIPNAVDPTDFTPEPFRRHDSVITVvvvSRLVYRKGTDLLSGIIPELCQKYQELNFLIGGEGPKRIILEEVRERYQL 281
Cdd:cd03820 161 -VVVIPNPLSFPSEEPSTNLKSKRILAV---GRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958807754 282 HDRVQLLGALehKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVS 331
Cdd:cd03820 237 EDRVKLLGPT--KNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIIS 284
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
34-401 |
5.12e-25 |
|
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: 105.87 E-value: 5.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 34 NICMVSDFFYPN-MGGVESHIYQLSQCLIERGHKVITVTHAYGNRKGVRYLTNGLKVYYLPLRVMYNQSTATTLFHS--- 109
Cdd:cd03823 1 KILLVNSLYPPQrVGGAEISVHDLAEALVAEGHEVAVLTAGVGPPGQATVARSVVRYRRAPDETLPLALKRRGYELFety 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 110 ----LPLLRYIFVRERITIIHSHSsFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVslcdtnhiICVS 185
Cdd:cd03823 81 npglRRLLARLLEDFRPDVVHTHN-LSGLGASLLDAARDLGIPVVHTLHDYWLLCPRQFLFKKGGDAV--------LAPS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 186 -YTskENTVLRAALNPEIVSVIPNAVDPTDFTPEPFRRHDSVITVVVVSRLVYRKGTDLLSGIIPELcqKYQELNFLIGG 264
Cdd:cd03823 152 rFT--ANLHEANGLFSARISVIPNAVEPDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRL--PREDIELVIAG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 265 EGPKRIIleevrERYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSL-TEAFCMAIVEAASCGLQVVSTKVGGIPE-VLP 342
Cdd:cd03823 228 HGPLSDE-----RQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAElIQP 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 343 ENLIILCEPSVKslcEGLEKAIFQV-KSGTLPAPENIHNVVKTFYTWRnvAERTEKVYER 401
Cdd:cd03823 303 GVNGLLFAPGDA---EDLAAAMRRLlTDPALLERLRAGAEPPRSTESQ--AEEYLKLYRD 357
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
227-364 |
1.97e-23 |
|
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 96.19 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 227 ITVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLIGGEGPKRIILEEVRERYQLHDRVQLLGALEHKDVRNVLVQGHIF 306
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVF 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 307 LNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLPENLI-ILCEP-SVKSLCEGLEKAI 364
Cdd:pfam00534 83 VLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETgFLVKPnNAEALAEAIDKLL 142
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
228-364 |
5.05e-23 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 94.50 E-value: 5.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 228 TVVVVSRLV-YRKGTDLLSGIIPELCQKYQELNFLIGGEGPKRIILEEVREryqLHDRVQLLGALEhkDVRNVLVQGHIF 306
Cdd:pfam13692 3 VILFVGRLHpNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEELAAG---LEDRVIFTGFVE--DLAELLAAADVF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807754 307 LNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLPENLIILCEP-SVKSLCEGLEKAI 364
Cdd:pfam13692 78 VLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENGLLVPPgDPEALAEAILRLL 136
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
35-344 |
1.61e-22 |
|
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: 95.93 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 35 ICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVITVTHaygnrkgvryltnglkvyylplrvmynqstattLFHSLPLLR 114
Cdd:cd01635 1 ILLVTGEYPPLRGGLELHVRALARALAALGHEVTVLAL---------------------------------LLLALRRIL 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 115 YIFVRERITIIHSHSSFSAMAHdALFHAKTMGLQTVFTDHSLFGFAdvssvltnklltvslcdtnhiicvsytskentvl 194
Cdd:cd01635 48 KKLLELKPDVVHAHSPHAAALA-ALLAARLLGIPIVVTVHGPDSLE---------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 195 raalnpeivsvipnAVDPTDFTPEPFRRHDSVITVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLIGGEGPKRIILEE 274
Cdd:cd01635 93 --------------STRSELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEA 158
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958807754 275 VRERYQLHDRVQLLGALEHKDVRNVLVQG-HIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLPEN 344
Cdd:cd01635 159 LAAALGLLERVVIIGGLVDDEVLELLLAAaDVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDG 229
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
47-396 |
7.36e-21 |
|
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: 94.23 E-value: 7.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 47 GGVESHIYQLSQCLIERGHKVITVTHAYGNRKGVR-YLTNGLKVYYLPLR----VMYNQstattLFHSLP-----LLRYI 116
Cdd:cd03800 21 GGQNVYVLELARALAELGYQVDIFTRRISPADPEVvEIAPGARVIRVPAGppeyLPKEE-----LWPYLEefadgLLRFI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 117 fVRERIT--IIHSHSSFSAMAhdALFHAKTMGLQTVFTDHSL-------FGFADVSSV---LTNKLLTVSLCDTnhIICV 184
Cdd:cd03800 96 -AREGGRydLIHSHYWDSGLV--GALLARRLGVPLVHTFHSLgrvkyrhLGAQDTYHPslrITAEEQILEAADR--VIAS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 185 SYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPEPfrRHDSVIT----------VVVVSRLVYRKGTDLL---SGIIPEL 251
Cdd:cd03800 171 TPQEADELISLYGADPSRINVVPPGVDLERFFPVD--RAEARRArlllppdkpvVLALGRLDPRKGIDTLvraFAQLPEL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 252 cqkYQELNFLIGGeGPKRIILEEVRE-------RYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAAS 324
Cdd:cd03800 249 ---RELANLVLVG-GPSDDPLSMDREelaelaeELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMA 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807754 325 CGLQVVSTKVGGIPE-VLPENLIILCEP-SVKSLCEGLEKaIFQVKSGTLPAPENIHNVVKTFYTWRNVAERTE 396
Cdd:cd03800 325 CGTPVVATAVGGLQDiVRDGRTGLLVDPhDPEALAAALRR-LLDDPALWQRLSRAGLERARAHYTWESVADQLL 397
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
38-336 |
4.11e-19 |
|
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: 88.49 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 38 VSDFFYPNMGGVESHIYQLSQCLIERGH--KVITVTHaygNRKGVRYLTNGLKVYYLPLRVMYNqstATTLFHSLPlLRY 115
Cdd:cd03795 5 VFKFYYPDIGGIEQVIYDLAEGLKKKGIevDVLCFSK---EKETPEKEENGIRIHRVKSFLNVA---STPFSPSYI-KRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 116 IFVRERITIIHSHSSFSAMahDALFHAKTMGLQTVFTDHslfgfadvSSVLTNK--------LLTVSLCDTNHIICVSYT 187
Cdd:cd03795 78 KKLAKEYDIIHYHFPNPLA--DLLLFFSGAKKPVVVHWH--------SDIVKQKkllklykpLMTRFLRRADRIIATSPN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 188 SKENT-VLRAALNPeiVSVIPNAVDPTDFTP----EPFRRHDSVIT--VVVVSRLVYRKGTDLlsgiipeLCQKYQELNF 260
Cdd:cd03795 148 YVETSpTLREFKNK--VRVIPLGIDKNVYNIprvdFENIKREKKGKkiFLFIGRLVYYKGLDY-------LIEAAQYLNY 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 261 --LIGGEGPKRIILEEVRErYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSL--TEAFCMAIVEAASCGLQVVSTKVGG 336
Cdd:cd03795 219 piVIGGEGPLKPDLEAQIE-LNLLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVISTNIGT 297
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
35-397 |
7.76e-19 |
|
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: 87.80 E-value: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 35 ICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVITVTHAYGNRKGVRYLTNGLKVYYLPLRVMYNQSTATTLFhslpLLR 114
Cdd:cd03809 2 ILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRW----LQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 115 YIFVRERITIIHSHSSFSAMahdalfhaKTMGLQTVFTDHSLF------GFADVSSVLTNKLLTVSLCDTNHIICVSYTS 188
Cdd:cd03809 78 LLPKKDKPDLLHSPHNTAPL--------LLKGCPQVVTIHDLIplrypeFFPKRFRLYYRLLLPISLRRADAIITVSEAT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 189 KENTVLRAALNPEIVSVIPNAVDPTDFTPEpfrRHDSVI--------TVVVVSRLVYRKGTDLLSGIIPELCQKYQELNF 260
Cdd:cd03809 150 RDDIIKFYGVPPEKIVVIPLGVDPSFFPPE---SAAVLIakyllpepYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 261 LI-GGEGPKRIILEEVRERYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPE 339
Cdd:cd03809 227 VIvGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPE 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807754 340 VLPENlIILCEP-SVKSLCEGLEKAIFQvKSGTLPAPENIHNVVKTFyTWRNVAERTEK 397
Cdd:cd03809 307 VAGDA-ALYFDPlDPESIADAILRLLED-PSLREELIRKGLERAKKF-SWEKTAEKTLE 362
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
47-212 |
8.05e-19 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 83.74 E-value: 8.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 47 GGVESHIYQLSQCLIERGHKVITVTHAYGNRKGVRYLTnglkVYYLPLRVMYNQSTATTLFHSLPLLRYIFVRERITIIH 126
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVR----VVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 127 SHSSFSAMAhDALFHAKTMGLQTVFTDHSLF-------GFADVSSVLTNKLLTVSLCDTNHIICVSYTSKENTVLRAALN 199
Cdd:pfam13439 77 AHSPFPLGL-AALAARLRLGIPLVVTYHGLFpdykrlgARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVP 155
|
170
....*....|...
gi 1958807754 200 PEIVSVIPNAVDP 212
Cdd:pfam13439 156 PEKIRVIPNGVDL 168
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
181-339 |
5.12e-18 |
|
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: 85.58 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 181 IICVSYTSKENtVLRAALNPEIVSVIPNAVDPTDFTPEPFRRHDSVItvVVVSRLVYRKGTDLLSGIIPELCQKYQELNF 260
Cdd:cd05844 147 FVAVSGFIRDR-LLARGLPAERIHVHYIGIDPAKFAPRDPAERAPTI--LFVGRLVEKKGCDVLIEAFRRLAARHPTARL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 261 LIGGEGPKRIILEEVRERYqlhDRVQLLGALEHKDVRNVLVQGHIFLNTSLT------EAFCMAIVEAASCGLQVVSTKV 334
Cdd:cd05844 224 VIAGDGPLRPALQALAAAL---GRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRH 300
|
....*
gi 1958807754 335 GGIPE 339
Cdd:cd05844 301 GGIPE 305
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
34-396 |
1.90e-17 |
|
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: 83.93 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 34 NICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVITVTHAYGNRKGVRYLT-----NGLKVYYLPLRVMYNQSTATTLFH 108
Cdd:cd03794 1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGatetkDGIRVIRVKLGPIKKNGLIRRLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 109 --SLP---LLRYIFVRERITIIHSHSS--FSAMAhdALFHAKTMGLQTVFTDHSLFGFADVS-SVLTNKLL--------- 171
Cdd:cd03794 81 ylSFAlaaLLKLLVREERPDVIIAYSPpiTLGLA--ALLLKKLRGAPFILDVRDLWPESLIAlGVLKKGSLlkllkkler 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 172 -TVSLCDtnHIICVSYTSKENtVLRAALNPEIVSVIPNAVDPTDFTPEPFRRHDSVITVVVVSRLVY------RKGTDLL 244
Cdd:cd03794 159 kLYRLAD--AIIVLSPGLKEY-LLRKGVPKEKIIVIPNWADLEEFKPPPKDELRKKLGLDDKFVVVYagnigkAQGLETL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 245 SGIIPELcQKYQELNFLIGGEGPKRIILEEVRERYQLhDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIV---- 320
Cdd:cd03794 236 LEAAERL-KRRPDIRFLFVGDGDEKERLKELAKARGL-DNVTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGSSpskl 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807754 321 -EAASCGLQVVSTKVGGIPE-VLPENLIILCEP-SVKSLCEGLEKAIFQVKSGTLPApENIHNVVKTFYTWRNVAERTE 396
Cdd:cd03794 314 fEYMAAGKPILASDDGGSDLaVEINGCGLVVEPgDPEALADAILELLDDPELRRAMG-ENGRELAEEKFSREKLADRLL 391
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
34-396 |
2.77e-17 |
|
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: 83.19 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 34 NICMVSDFFYPNMGGVESHIYQLSQCLIERGHKV--ITVTHAYGNRKGVRYLTNGLKVYYLPLRVMYNQS---TATTLFH 108
Cdd:cd03821 1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVtiVSTGDGYESLVVEENGRYIPPQDGFASIPLLRQGagrTDFSPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 109 SLPLLRYIfvRE-RITIIHSHSSFSAMAhdALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNHI---ICV 184
Cdd:cd03821 81 PNWLRRNL--REyDVVHIHGVWTYTSLA--ACKLARRRGIPYVVSPHGMLDPWALQQKHWKKRIALHLIERRNLnnaALV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 185 SYTS-KENTVLRAALNPEIVSVIPNAVDPTDFTPEPFRR------HDSVItVVVVSRLVYRKGTDLLSGIIPELCQKYQE 257
Cdd:cd03821 157 HFTSeQEADELRRFGLEPPIAVIPNGVDIPEFDPGLRDRrkhnglEDRRI-ILFLGRIHPKKGLDLLIRAARKLAEQGRD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 258 LNFLIGGEGPKriiLEEVRERYQ----LHDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTK 333
Cdd:cd03821 236 WHLVIAGPDDG---AYPAFLQLQsslgLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITD 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807754 334 VGGIPEVLPENLIILCEPSVKSLCEGLEKAIfQVKSGTLPAPENIHNVVKT--FYTWRNVAERTE 396
Cdd:cd03821 313 KCGLSELVEAGCGVVVDPNVSSLAEALAEAL-RDPADRKRLGEMARRARQVeeNFSWEAVAGQLG 376
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
35-343 |
4.29e-16 |
|
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: 79.65 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 35 ICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVITVT----HAYGNRKGVRYLTNGLKvyyLPLRVMYnqstattlfhSL 110
Cdd:cd03814 2 IALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVApgpfDEAESAEGRVVSVPSFP---LPFYPEY----------RL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 111 PLLRYIFVRERI-----TIIHSHSSFSaMAHDALFHAKTMGLQTVFTDHSLF-------GFADVSSVLTNKLLTVS-LCD 177
Cdd:cd03814 69 ALPLPRRVRRLIkefqpDIIHIATPGP-LGLAALRAARRLGLPVVTSYHTDFpeylsyyTLGPLSWLAWAYLRWFHnPFD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 178 TnhIICVSYTSKEntvLRAALNPEIVSVIPNAVDPTDFTPEP----FRRHDSV---ITVVVVSRLVYRKGTDLLSGIIPE 250
Cdd:cd03814 148 T--TLVPSPSIAR---ELEGHGFERVRLWPRGVDTELFHPSRrdaaLRRRLGPpgrPLLLYVGRLAPEKNLEALLDADLP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 251 LCQKyQELNFLIGGEGPKRiilEEVRERYqlhDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVV 330
Cdd:cd03814 223 LAAS-PPVRLVVVGDGPAR---AELEARG---PDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVV 295
|
330
....*....|...
gi 1958807754 331 STKVGGIPEVLPE 343
Cdd:cd03814 296 AADAGGPRDIVRP 308
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
49-345 |
1.37e-15 |
|
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: 77.88 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 49 VESHIYQLSQC--LIERGHKViTVTHAYGNRKGVRYltnglkvyylPLRVMYNQSTATTLFHSLPLLRyifvRERITIIH 126
Cdd:cd03799 11 VLSETFILNQItgLIDRGHEV-DIYAVNPGDLVKRH----------PDVEKYNVPSLNLLYAIVGLNK----KGAYDIIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 127 SHSSFSAMAHDALFHAKTMGLQTVFTDHSlfgfADVSSVLTNKLLTV--SLCDTNHI---ICVSYTSKentVLRAALNPE 201
Cdd:cd03799 76 CQFGPLGALGALLRRLKVLKGKLVTSFRG----YDISMYVILEGNKVypQLFAQGDLflpNCELFKHR---LIALGCDEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 202 IVSVIPNAVDPTDFTPEPFRRH-DSVITVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLIGGEGPKRIILEEVRERYQ 280
Cdd:cd03799 149 KIIVHRSGIDCNKFRFKPRYLPlDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELN 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958807754 281 LHDRVQLLGALEHKDVRNVLVQGHIFLNTSLT------EAFCMAIVEAASCGLQVVSTKVGGIPEVLPENL 345
Cdd:cd03799 229 IGDCVKLLGWKPQEEIIEILDEADIFIAPSVTaadgdqDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGV 299
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
43-344 |
2.22e-15 |
|
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: 77.39 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 43 YPNMGGVESHIYQLSQCLIERGHKVITVTHAYGNRKGvRYLTNglkVYYLPLRVMyNQSTATTLFHSLPL---LRYIFVR 119
Cdd:cd04962 8 YPSYGGSGVVATELGLELAERGHEVHFISSAIPFRLN-LYSGN---IFFHEVEVP-NYPLFEYPPYTLALaskIVEVAKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 120 ERITIIHSHSsfsAMAHD-ALFHAKTM---GLQTVFTDHSlfgfADVSSVLTNK----LLTVSLCDTNHIICVSYTSKEN 191
Cdd:cd04962 83 HKLDVLHAHY---AIPHAsCAYLAREIlgeKIPIVTTLHG----TDITLVGYDPslqpAVRFSINKSDRVTAVSSSLRQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 192 TVLRAALNPEIvSVIPNAVDPTDFTPEP----------------------FRRHDSVITVVVVSRLVYRKgtdllsgiIP 249
Cdd:cd04962 156 TYELFDVDKDI-EVIHNFIDEDVFKRKPagalkrrllappdekvvihvsnFRPVKRIDDVVRVFARVRRK--------IP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 250 ElcqkyqelNFLIGGEGPKRIILEEVRERYQLHDRVQLLGALEHkdVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQV 329
Cdd:cd04962 227 A--------KLLLVGDGPERVPAEELARELGVEDRVLFLGKQDD--VEELLSIADLFLLPSEKESFGLAALEAMACGVPV 296
|
330
....*....|....*
gi 1958807754 330 VSTKVGGIPEVLPEN 344
Cdd:cd04962 297 VSSNAGGIPEVVKHG 311
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
46-347 |
3.16e-15 |
|
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: 77.10 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 46 MGGVESHIYQLSQCLIERGHKViTVTHAYGNRKgVRYLTNGLKVYYLPLrvmynQSTATTLFHSLPLLRYIFVRERITII 125
Cdd:cd04951 11 LGGAEKQTVLLADQMFIRGHDV-NIVYLTGEVE-VKPLNNNIIIYNLGM-----DKNPRSLLKALLKLKKIISAFKPDVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 126 HSHssfsaMAHDALF------HAKTMGLqtVFTDHSlfgfADVSSVLTNKL--LTVSLCD--TNhiicVSYTSKENTVLR 195
Cdd:cd04951 84 HSH-----MFHANIFarflrmLYPIPLL--ICTAHN----KNEGGRIRMFIyrLTDFLCDitTN----VSREALDEFIAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 196 AALNPEIVSVIPNAVDPTDFTPEPFRR---------HDSVITVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLIGGEG 266
Cdd:cd04951 149 KAFSKNKSVPVYNGIDLNKFKKDINVRlkirnklnlKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 267 PKRIILEEVRERYQLHDRVQLLGAleHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVL-PENL 345
Cdd:cd04951 229 PLRNELERLICNLNLVDRVILLGQ--ISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVgDHNY 306
|
..
gi 1958807754 346 II 347
Cdd:cd04951 307 VV 308
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
304-404 |
1.16e-14 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 70.40 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 304 HIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLPENLI-ILCEP-SVKSLCEGLEKAIfqvKSGTLPA--PENIH 379
Cdd:COG0438 22 DVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETgLLVPPgDPEALAEAILRLL---EDPELRRrlGEAAR 98
|
90 100
....*....|....*....|....*
gi 1958807754 380 NVVKTFYTWRNVAERTEKVYERVSK 404
Cdd:COG0438 99 ERAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
47-402 |
6.08e-14 |
|
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: 72.71 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 47 GGVESHIYQLSQCLIERGHKVITVThAYGNRKGVRyltnGLKVYYLPLRVMYNQSTATTLFHSLPLLRYIfVRERITIIH 126
Cdd:cd03802 18 GGTELVVSALTEGLVRRGHEVTLFA-PGDSHTSAP----LVAVIPRALRLDPIPQESKLAELLEALEVQL-RASDFDVIH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 127 SHSSFSamahdALFHAKTMGLQTVFTDHslfGFADVSSvltnkLLTVSLCDTNHIICVSYTSkentvlRAALNP-EIVSV 205
Cdd:cd03802 92 NHSYDW-----LPPFAPLIGTPFVTTLH---GPSIPPS-----LAIYAAEPPVNYVSISDAQ------RAATPPiDYLTV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 206 IPNAVDPTDFTPEPFRRHDsvitVVVVSRLVYRKGTDLlsGIipELCQKyqeLNFLIGGEGPKRiilEEVRERYQ----L 281
Cdd:cd03802 153 VHNGLDPADYRFQPDPEDY----LAFLGRIAPEKGLED--AI--RVARR---AGLPLKIAGKVR---DEDYFYYLqeplP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 282 HDRVQLLGALEHKDVRNVLVQGHIFLNTSL-TEAFCMAIVEAASCGLQVVSTKVGGIPEVLPENLI-ILCEPSvkslcEG 359
Cdd:cd03802 219 GPRIEFIGEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETgFLVDSV-----EE 293
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958807754 360 LEKAIFQVksGTLPaPENIHNVVKTFYTWRNVAERTEKVYERV 402
Cdd:cd03802 294 MAEAIANI--DRID-RAACRRYAEDRFSAARMADRYEALYRKV 333
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
187-334 |
1.09e-10 |
|
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: 62.70 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 187 TSKENTVLRAALNPEI-VSVIPNAVDPTDFTPEPFRRHDSVItVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLIGGE 265
Cdd:cd04949 121 TEQQKQDLSERFNKYPpIFTIPVGYVDQLDTAESNHERKSNK-IITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGY 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807754 266 GPKRIILEEVRERYQLHDRVQLLGAleHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKV 334
Cdd:cd04949 200 GEEREKLKKLIEELHLEDNVFLKGY--HSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDV 266
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
45-330 |
2.68e-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: 61.92 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 45 NMGGVESHIYQLSQCLIERGHKVITVthAYGNRKGVRY---LTNGLKVYYLPLRVMYNqstattLFHSLPLLRYIFVrER 121
Cdd:cd03812 10 NVGGIETFLMNLYRKLDKSKIEFDFL--ATSDDKGEYDeelEELGGKIFYIPPKKKNI------IKYFIKLLKLIKK-EK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 122 ITIIHSHSSFSAMAhdALFHAKTMGLQT-VFTDH-----SLFGFADVSSVLTNKLLTVSlcdTNHIICvsyTSKENTVLR 195
Cdd:cd03812 81 YDIVHVHGSSSNGI--ILLLAAKAGVPVrIAHSHntkdsSIKLRKIRKNVLKKLIERLS---TKYLAC---SEDAGEWLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 196 AALNPEIVSVIPNAVDPTDFTPEPFRRH--------DSVITVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLIGGEGP 267
Cdd:cd03812 153 GEVENGKFKVIPNGIDIEKYKFNKEKRRkrrkllilEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807754 268 KRI-ILEEVRERyQLHDRVQLLGalEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVV 330
Cdd:cd03812 233 LKEkIKEKVKEL-GLEDKVIFLG--FRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCL 293
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
200-341 |
3.57e-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: 61.97 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 200 PEIVSVIPNAVDPTDFTPEPFRRHDS-VITVVVVSRLVYRKgtDLLSGI--IPELCQKYQELNF-LIGGEGPKRIILEEV 275
Cdd:cd03813 266 PDKTRVIPNGIDIQRFAPAREERPEKePPVVGLVGRVVPIK--DVKTFIraFKLVRRAMPDAEGwLIGPEDEDPEYAQEC 343
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807754 276 RERYQ---LHDRVQLLGaleHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVL 341
Cdd:cd03813 344 KRLVAslgLENKVKFLG---FQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELI 409
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
224-364 |
3.92e-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: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 224 DSVITVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFL---IGGeGPKRIILEEVRERYQLHDRVQLLGALEHKDVRNVL 300
Cdd:cd04946 222 EGDLRLVSCSSIVPVKRIDLIIETLNSLCVAHPSICISwthIGG-GPLKERLEKLAENKLENVKVNFTGEVSNKEVKQLY 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 301 VQG--HIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLpEN----LIILCEPSVKSLCEGLEKAI 364
Cdd:cd04946 301 KENdvDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIV-ENetngLLLDKDPTPNEIVSSIMKFY 369
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
203-361 |
2.83e-07 |
|
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: 52.33 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 203 VSVIPNAVDPTDFTP---EPFRR------HDSVITVVVVSRLVYRKGTDLLsgiIPELCQ--KYQELNFLIGGEGPKRII 271
Cdd:cd03825 163 VVVIPNGIDTEIFAPvdkAKARKrlgipqDKKVILFGAESVTKPRKGFDEL---IEALKLlaTKDDLLLVVFGKNDPQIV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 272 LEEVRERY--QLHDRVQLlgalehkdvRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVL--PENLII 347
Cdd:cd03825 240 ILPFDIISlgYIDDDEQL---------VDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVqhGVTGYL 310
|
170
....*....|....
gi 1958807754 348 LCEPSVKSLCEGLE 361
Cdd:cd03825 311 VPPGDVQALAEAIE 324
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
203-400 |
2.11e-06 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 49.79 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 203 VSVIPNAVDPTDFT--PEPFRRHDSVI----TVVVVS-RLVYRKGTDLLSGIIPELCQKYQELNFLIGGE------GPKR 269
Cdd:PRK15484 163 ISIVPNGFCLETYQsnPQPNLRQQLNIspdeTVLLYAgRISPDKGILLLMQAFEKLATAHSNLKLVVVGDptasskGEKA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 270 IILEEVRE-RYQLHDRVQLLGALEHKDVRNVL-VQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLPENLI- 346
Cdd:PRK15484 243 AYQKKVLEaAKRIGDRCIMLGGQPPEKMHNYYpLADLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITg 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807754 347 -ILCEP-SVKSLCEGLEKAIFQVKSGTLpaPENIHNVVKTFYTWRNVAERTEKVYE 400
Cdd:PRK15484 323 yHLAEPmTSDSIISDINRTLADPELTQI--AEQAKDFVFSKYSWEGVTQRFEEQIH 376
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
47-156 |
3.73e-06 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 47.01 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 47 GGVESHIYQLSQCLIERGHKVITVTHAYGNRkGVRYLTNGLKVYYLPLRvmYNQSTATTLFHSLPLLRYIfVRERITIIH 126
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPG-RPELVGDGVRVHRLPVP--PRPSPLADLAALRRLRRLL-RAERPDVVH 76
|
90 100 110
....*....|....*....|....*....|
gi 1958807754 127 SHSSFSAMAhdALFHAKTMGLQTVFTDHSL 156
Cdd:pfam13579 77 AHSPTAGLA--ARLARRRRGVPLVVTVHGL 104
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
229-285 |
7.68e-05 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 45.08 E-value: 7.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807754 229 VVVVSRLVYRKGTDLLSGIIPELCQkyQELNFLIGGEGPKRI--ILEEVRERYqlHDRV 285
Cdd:COG0297 298 IGMVSRLTEQKGLDLLLEALDELLE--EDVQLVVLGSGDPEYeeAFRELAARY--PGRV 352
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
229-285 |
1.04e-03 |
|
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: 41.39 E-value: 1.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807754 229 VVVVSRLVYRKGTDLLSGIIPELCQKyqELNFLIGGEGPKRII--LEEVRERYqlHDRV 285
Cdd:cd03791 297 FGFVGRLTEQKGVDLILDALPELLEE--GGQLVVLGSGDPEYEqaFRELAERY--PGKV 351
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
229-338 |
1.59e-03 |
|
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.
Pssm-ID: 340823 [Multi-domain] Cd Length: 378 Bit Score: 40.77 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 229 VVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLIGGEGPKR-----IILEEVRERYQLHDRVQLLGALEHKDVRNVLVQG 303
Cdd:cd03792 200 ILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDdpegsVVYEEVMEYAGDDHDIHVLRLPPSDQEINALQRA 279
|
90 100 110
....*....|....*....|....*....|....*.
gi 1958807754 304 -HIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIP 338
Cdd:cd03792 280 aTVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIP 315
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
221-345 |
3.30e-03 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 40.02 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807754 221 RRHDSVITVVVVSRLVYRKGTDLLSGIIPELCQKYQELNFLIGGEGPkriILEEVRE---RYQLHDRVQLLGALEHkdVR 297
Cdd:PRK15179 512 RTSDARFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGP---LLESVREfaqRLGMGERILFTGLSRR--VG 586
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958807754 298 NVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLPENL 345
Cdd:PRK15179 587 YWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGV 634
|
|
| |
