|
Name |
Accession |
Description |
Interval |
E-value |
| mycothiol_MshA |
TIGR03449 |
D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively ... |
24-429 |
0e+00 |
|
D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively in the Actinobacteria, are MshA, the glycosyltransferase of mycothiol biosynthesis. Mycothiol replaces glutathione in these species.
Pssm-ID: 132490 [Multi-domain] Cd Length: 405 Bit Score: 598.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 24 VAMVSMHTSPLEQPGTGDAGGMNVYVLQTARRLADRGVAVEIFTRATSSEQPPALSPSEGITVHYVPAGPFEGLSKGDLP 103
Cdd:TIGR03449 1 VAMISMHTSPLQQPGTGDAGGMNVYILETATELARRGIEVDIFTRATRPSQPPVVEVAPGVRVRNVVAGPYEGLDKEDLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 104 SQLCAFTNGVLRAEAAQPPGYFDVIHSHYWLSGQAAWLAAERWGVPHIHSAHTLAKVKNLHLAAEDTPEPFTRVVGEEQV 183
Cdd:TIGR03449 81 TQLCAFTGGVLRAEARHEPGYYDLIHSHYWLSGQVGWLLRDRWGVPLVHTAHTLAAVKNAALADGDTPEPEARRIGEQQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 184 VAESDALVTNTSSEAEVLVDLYRADPDKVTVTPPGVDPEVFTPGDKLAARRRLGLPDDALVLGFAGRIQPLKAPDVLVRA 263
Cdd:TIGR03449 161 VDNADRLIANTDEEARDLVRHYDADPDRIDVVAPGADLERFRPGDRATERARLGLPLDTKVVAFVGRIQPLKAPDVLLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 264 VARLRALNPElaPRLRLVVVGGPSGNGADNPRWLHDLAAELGIADAVTFLKPRAGHELAEVFRACDVVGVPSYNETFGLV 343
Cdd:TIGR03449 241 VAELLDRDPD--RNLRVIVVGGPSGSGLATPDALIELAAELGIADRVRFLPPRPPEELVHVYRAADVVAVPSYNESFGLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 344 ALEAQACGTPVVAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAARFTWSHTADDLLGA 423
Cdd:TIGR03449 319 AMEAQACGTPVVAARVGGLPVAVADGETGLLVDGHDPADWADALARLLDDPRTRIRMGAAAVEHAAGFSWAATADGLLSS 398
|
....*.
gi 310947090 424 YGDAIQ 429
Cdd:TIGR03449 399 YRDALA 404
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
23-421 |
3.88e-163 |
|
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: 465.18 E-value: 3.88e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 23 RVAMVSMHTSPLEQPGTGDAGGMNVYVLQTARRLADRGVAVEIFTRATSSEQPPALSPSEGITVHYVPAGPFEGLSKGDL 102
Cdd:cd03800 1 RIALISVHGSPLAQPGGADTGGQNVYVLELARALAELGYQVDIFTRRISPADPEVVEIAPGARVIRVPAGPPEYLPKEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 103 PSQLCAFTNGVLRAEAAQPPGYfDVIHSHYWLSGQAAWLAAERWGVPHIHSAHTLAKVKNLHLAAEDTPEPFTRVVGEEQ 182
Cdd:cd03800 81 WPYLEEFADGLLRFIAREGGRY-DLIHSHYWDSGLVGALLARRLGVPLVHTFHSLGRVKYRHLGAQDTYHPSLRITAEEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 183 VVAESDALVTNTSSEAEVLVDLYRADPDKVTVTPPGVDPEVFTPGDKLAARR-RLGLPDDALVLGFAGRIQPLKAPDVLV 261
Cdd:cd03800 160 ILEAADRVIASTPQEADELISLYGADPSRINVVPPGVDLERFFPVDRAEARRaRLLLPPDKPVVLALGRLDPRKGIDTLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 262 RAVARLralnPELAPRLRLVVVGGPSGNGADNPRWLHD-LAAELGIADAVTFLKPRAGHELAEVFRACDVVGVPSYNETF 340
Cdd:cd03800 240 RAFAQL----PELRELANLVLVGGPSDDPLSMDREELAeLAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 341 GLVALEAQACGTPVVAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHA-ARFTWSHTADD 419
Cdd:cd03800 316 GLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERArAHYTWESVADQ 395
|
..
gi 310947090 420 LL 421
Cdd:cd03800 396 LL 397
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
23-424 |
2.16e-68 |
|
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: 221.64 E-value: 2.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 23 RVAMVSMHTSPleqpgtgDAGGMNVYVLQTARRLADRGVAVEIFTRATSSEQPPALSPSEGITVHYVPAgpfeglskgdl 102
Cdd:cd03801 1 KILLLSPELPP-------PVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLA----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 103 psqLCAFTNGVLRAEAAQPPGY-FDVIHSHYWLSGQAAWLAAERWGVPHIHSAHTLAKVKNLHLAAEDTpepftRVVGE- 180
Cdd:cd03801 63 ---ALLRARRLLRELRPLLRLRkFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAER-----RLLARa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 181 EQVVAESDALVTNTSSEAEVLVDLYRADPDKVTVTPPGVDPEVFTPgdklAARRRLGLPDDALVLGFAGRIQPLKAPDVL 260
Cdd:cd03801 135 EALLRRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSP----PLRRKLGIPPDRPVLLFVGRLSPRKGVDLL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 261 VRAVARLRALNPELaprlRLVVVGGpsgnGADNPRWLHDLaaELGIADAVTFLKPRAGHELAEVFRACDVVGVPSYNETF 340
Cdd:cd03801 211 LEALAKLLRRGPDV----RLVIVGG----DGPLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 341 GLVALEAQACGTPVVAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDH-AARFTWSHTADD 419
Cdd:cd03801 281 GLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERvAERFSWERVAER 360
|
....*
gi 310947090 420 LLGAY 424
Cdd:cd03801 361 LLDLY 365
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
43-427 |
1.14e-53 |
|
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: 183.73 E-value: 1.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 43 GGMNVYVLQTARRLADRGVAVEIFtrATSSEQPPALSPSEGITVHYVPAGPFEGLskgdLPSQLCAFTNGVLRAEAAQP- 121
Cdd:cd03798 14 PGRGIFVRRQVRALSRRGVDVEVL--APAPWGPAAARLLRKLLGEAVPPRDGRRL----LPLKPRLRLLAPLRAPSLAKl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 122 -----PGYFDVIHSHY-WLSGQAAWLAAERWGVPHIHSAHT--LAKVKNLHLAAEDtpepftrvvgEEQVVAESDALVTN 193
Cdd:cd03798 88 lkrrrRGPPDLIHAHFaYPAGFAAALLARLYGVPYVVTEHGsdINVFPPRSLLRKL----------LRWALRRAARVIAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 194 TSSEAEVLVDLYrADPDKVTVTPPGVDPEVFTPGDklaarRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLRALNPE 273
Cdd:cd03798 158 SKALAEELVALG-VPRDRVDVIPNGVDPARFQPED-----RGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 274 LapRLRLVvvggpsGNGADNPRwLHDLAAELGIADAVTFLKPRAGHELAEVFRACDVVGVPSYNETFGLVALEAQACGTP 353
Cdd:cd03798 232 V--VLLIV------GDGPLREA-LRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLP 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 310947090 354 VVAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAARFTWSHTADDLLGAYGDA 427
Cdd:cd03798 303 VVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALAEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
41-411 |
2.14e-44 |
|
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: 158.29 E-value: 2.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 41 DAGGMNVYVLQTARRLADRGVAVEIFTRAtsseqPPALSPSEGITVHYvpagpfEGLSKGDLPSQLCAFTNGVLRAEAAq 120
Cdd:cd03819 9 EIGGAETYILDLARALAERGHRVLVVTAG-----GPLLPRLRQIGIGL------PGLKVPLLRALLGNVRLARLIRRER- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 121 ppgyFDVIHSHYWLSGQAAWLAAERWGVPHIHSAHtlakvkNLHLAaedtPEPFTRVVGEEQVVAESDALVTNtsSEAEV 200
Cdd:cd03819 77 ----IDLIHAHSRAPAWLGWLASRLTGVPLVTTVH------GSYLA----TYHPKDFALAVRARGDRVIAVSE--LVRDH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 201 LVDLYRADPDKVTVTPPGVDPEVFTPGDKLAARRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLRAlnpelAPRLRL 280
Cdd:cd03819 141 LIEALGVDPERIRVIPNGVDTDRFPPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKD-----EPDFRL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 281 VVVGGpsgnGADNPRwLHDLAAELGIADAVTFLKPRagHELAEVFRACDVVGVPSYNETFGLVALEAQACGTPVVAAAVG 360
Cdd:cd03819 216 LVAGD----GPERDE-IRRLVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVG 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 310947090 361 GLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARL--AAGALDHAARF 411
Cdd:cd03819 289 GAREIVVHGRTGLLVPPGDAEALADAIRAAKLLPEAREKLqaAAALTEAVREL 341
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
125-411 |
4.59e-44 |
|
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: 157.83 E-value: 4.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 125 FDVIHSHYWLS-GQAAWLAAERWGVPHIHSAHTLAK--VKNLHLaaedtPEPFTRVVGEEQVVA---ESDALVTNTSSEA 198
Cdd:cd03817 85 PDIIHTHTPFSlGKLGLRIARKLKIPIVHTYHTMYEdyLHYIPK-----GKLLVKAVVRKLVRRfynHTDAVIAPSEKIK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 199 EVLVDlyRADPDKVTVTPPGVDPEVFTPGDKLAARRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLRALNPelaprL 278
Cdd:cd03817 160 DTLRE--YGVKGPIEVIPNGIDLDKFEKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEPN-----I 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 279 RLVVVGgpsgNGADNPRwLHDLAAELGIADAVTFLKPRAGHELAEVFRACDVVGVPSYNETFGLVALEAQACGTPVVAAA 358
Cdd:cd03817 233 KLVIVG----DGPEREE-LKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAK 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 310947090 359 VGGLTTAVADGHSGLLIRGHDETdWANALDKLVTDAPRRARLAAGALDHAARF 411
Cdd:cd03817 308 DPAASELVEDGENGFLFEPNDET-LAEKLLHLRENLELLRKLSKNAEISAREF 359
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
244-404 |
2.27e-39 |
|
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: 138.95 E-value: 2.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 244 VLGFAGRIQPLKAPDVLVRAVARLRALNPELaprlRLVVVGGPsgngaDNPRWLHDLAAELGIADAVTFLKPRAGHELAE 323
Cdd:pfam00534 4 IILFVGRLEPEKGLDLLIKAFALLKEKNPNL----KLVIAGDG-----EEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 324 VFRACDVVGVPSYNETFGLVALEAQACGTPVVAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAG 403
Cdd:pfam00534 75 LLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGEN 154
|
.
gi 310947090 404 A 404
Cdd:pfam00534 155 A 155
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
182-421 |
3.38e-38 |
|
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: 142.12 E-value: 3.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 182 QVVAESDALVTNTSSEAEVLVDLYRADPDKVTVTPPGVDPEVFTPGDKLAARRRLGLPDDALVlgFAGRIQPLKAPDVLV 261
Cdd:cd03809 134 ISLRRADAIITVSEATRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLPEPYFL--YVGTLEPRKNHERLL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 262 RAVARLRALNPELaprlRLVVVGGpSGNGADNprwLHDLAAELGIADAVTFLkpraGH----ELAEVFRACDVVGVPSYN 337
Cdd:cd03809 212 KAFALLKKQGGDL----KLVIVGG-KGWEDEE---LLDLVKKLGLGGRVRFL----GYvsdeDLPALYRGARAFVFPSLY 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 338 ETFGLVALEAQACGTPVVAAAVGGLTTAVADghSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAARFTWSHTA 417
Cdd:cd03809 280 EGFGLPVLEAMACGTPVIASNISVLPEVAGD--AALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTA 357
|
....
gi 310947090 418 DDLL 421
Cdd:cd03809 358 EKTL 361
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
43-425 |
1.66e-37 |
|
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: 140.12 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 43 GGMNVYVLQTARRLADRGVAVEIFTratsSEQPPALSPSEGiTVHYVPAGPFEGLSKGDLPsqLCAFTNGVLRAEAAQPp 122
Cdd:cd03814 14 NGVVRTLERLVDHLRRRGHEVRVVA----PGPFDEAESAEG-RVVSVPSFPLPFYPEYRLA--LPLPRRVRRLIKEFQP- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 123 gyfDVIHSHYWLS-GQAAWLAAERWGVPHIHSAHTlakvKNLHLAAEDTPEPFTRVVGE--EQVVAESDALVTNTSSeae 199
Cdd:cd03814 86 ---DIIHIATPGPlGLAALRAARRLGLPVVTSYHT----DFPEYLSYYTLGPLSWLAWAylRWFHNPFDTTLVPSPS--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 200 VLVDLYRADPDKVTVTPPGVDPEVFTPGDKLAARRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLRAlnpelAPRLR 279
Cdd:cd03814 156 IARELEGHGFERVRLWPRGVDTELFHPSRRDAALRRRLGPPGRPLLLYVGRLAPEKNLEALLDADLPLAA-----SPPVR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 280 LVVVGgpsgngaDNPRwlhdlAAELGIADA-VTFLKPRAGHELAEVFRACDVVGVPSYNETFGLVALEAQACGTPVVAAA 358
Cdd:cd03814 231 LVVVG-------DGPA-----RAELEARGPdVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAAD 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 310947090 359 VGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAARFTWSHTADDLLGAYG 425
Cdd:cd03814 299 AGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERYSWEAFLDNLLDYYA 365
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
37-402 |
3.72e-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: 3.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 37 PGTGDAGGMNVyVLQTARRLADRGVAVEIFTRATSSEqppALSPSEGITVHYVPAGPFEGLSKGDLPSQLCAFtngvlRA 116
Cdd:cd03811 7 PSLSGGGAERV-LLNLANALDKRGYDVTLVLLRDEGD---LDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKL-----KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 117 EAAQppGYFDVIHSHywlSGQAAWLAAerwgvpHIHSAHTLaKVKNLHLAAEDTPEPFTRVVGEEQVVAESDALVTNTSS 196
Cdd:cd03811 78 ILKR--AKPDVVISF---LGFATYIVA------KLAAARSK-VIAWIHSSLSKLYYLKKKLLLKLKLYKKADKIVCVSKG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 197 EAEVLVDLYRADPDKVTVTPPGVDPEVFTpgdKLAARRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLRALNPELap 276
Cdd:cd03811 146 IKEDLIRLGPSPPEKIEVIYNPIDIDRIR---ALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDV-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 277 rlRLVVVGgpsgNGADNPRwLHDLAAELGIADAVTFLkpraGHE--LAEVFRACDVVGVPSYNETFGLVALEAQACGTPV 354
Cdd:cd03811 221 --KLVILG----DGPLREE-LEKLAKELGLAERVIFL----GFQsnPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPV 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 310947090 355 VAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAA 402
Cdd:cd03811 290 VSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQKKLDAALRER 337
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
126-412 |
1.15e-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: 126.66 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 126 DVIHSH----YWLSGQAAWLAAerwGVPHIHSAHTLakvknlhlaaeDTPEPFTRVVGEEQVVAE--SDALVTNTSSEAE 199
Cdd:cd03807 81 DVVHTWmyhaDLIGGLAAKLAG---GVKVIWSVRSS-----------NIPQRLTRLVRKLCLLLSkfSPATVANSSAVAE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 200 VLVDLYrADPDKVTVTPPGVDPEVFTPGDK--LAARRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLRALNPelapR 277
Cdd:cd03807 147 FHQEQG-YAKNKIVVIYNGIDLFKLSPDDAsrARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHP----D 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 278 LRLVVVGgpSGNGADNPRwlhDLAAELGIADAVTFLKPRagHELAEVFRACDVVGVPSYNETFGLVALEAQACGTPVVAA 357
Cdd:cd03807 222 LRLLLVG--RGPERPNLE---RLLLELGLEDRVHLLGER--SDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVAT 294
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 310947090 358 AVGGLTTAVADGhSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDH-AARFT 412
Cdd:cd03807 295 DVGGAAELVDDG-TGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERiANEFS 349
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
39-421 |
4.80e-31 |
|
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: 122.86 E-value: 4.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 39 TGDAGGMNVYVLQTARRLADRGVAVEI-FTRATSSEQPPALSPSEGITVHYVPAGPFEGLSKGDLPsqLCAFTNGVLRAE 117
Cdd:cd03821 10 SPKAGGPVKVVLRLAAALAALGHEVTIvSTGDGYESLVVEENGRYIPPQDGFASIPLLRQGAGRTD--FSPGLPNWLRRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 118 AAQppgyFDVIHSH-YW--LSGQAAWLAAERwGVPHIHSAHTLakvknLHLAAEDTPEPFTRVVG---EEQVVAESDALV 191
Cdd:cd03821 88 LRE----YDVVHIHgVWtyTSLAACKLARRR-GIPYVVSPHGM-----LDPWALQQKHWKKRIALhliERRNLNNAALVH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 192 TNTSSEAEVLVDLyrADPDKVTVTPPGVDPEVFTPGdkLAARRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLRaln 271
Cdd:cd03821 158 FTSEQEADELRRF--GLEPPIAVIPNGVDIPEFDPG--LRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLA--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 272 pELAPRLRLVVVGGPSGNGadnPRWLHDLAaELGIADAVTFLKPRAGHELAEVFRACDVVGVPSYNETFGLVALEAQACG 351
Cdd:cd03821 231 -EQGRDWHLVIAGPDDGAY---PAFLQLQS-SLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACG 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 310947090 352 TPVVAAAVGGLTTAVADGhSGLLIRGHDEtDWANALDKLVTDAPRRARLAAGAL---DHAARFTWSHTADDLL 421
Cdd:cd03821 306 LPVVITDKCGLSELVEAG-CGVVVDPNVS-SLAEALAEALRDPADRKRLGEMARrarQVEENFSWEAVAGQLG 376
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
23-421 |
2.36e-30 |
|
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: 120.91 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 23 RVAMVSMHTSPleqpgtgDAGGMNVYVLQTARRLADRGVAVEIFT----RATSSEQPPALSPSEGITVHYVPAGPFEGLS 98
Cdd:cd03794 1 KILLISQYYPP-------PKGAAAARVYELAKELVRRGHEVTVLTpspnYPLGRIFAGATETKDGIRVIRVKLGPIKKNG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 99 KGDLPSQLCAFT-NGVLRAEAAQPPgyFDVIHSH--YWLSGQAAWLAAERWGVP---HIHSAHTLAKVKNLHLAAEDTPE 172
Cdd:cd03794 74 LIRRLLNYLSFAlAALLKLLVREER--PDVIIAYspPITLGLAALLLKKLRGAPfilDVRDLWPESLIALGVLKKGSLLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 173 PFTRVvgEEQVVAESDALVTNTSSEAEVLVDLYRaDPDKVTVTPPGVDPEVFTPGDKLAARRRLGLPDDaLVLGFAGRIQ 252
Cdd:cd03794 152 LLKKL--ERKLYRLADAIIVLSPGLKEYLLRKGV-PKEKIIVIPNWADLEEFKPPPKDELRKKLGLDDK-FVVVYAGNIG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 253 PLKAPDVLVRAVARLRALnpelaPRLRLVVVGGpsgnGADNPRwLHDLAAELGIADaVTFLKPRAGHELAEVFRACDV-- 330
Cdd:cd03794 228 KAQGLETLLEAAERLKRR-----PDIRFLFVGD----GDEKER-LKELAKARGLDN-VTFLGRVPKEEVPELLSAADVgl 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 331 ---VGVPSYNETFGLVALEAQACGTPVVAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDH 407
Cdd:cd03794 297 vplKDNPANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGREL 376
|
410
....*....|....*
gi 310947090 408 AA-RFTWSHTADDLL 421
Cdd:cd03794 377 AEeKFSREKLADRLL 391
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
244-393 |
3.22e-29 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 111.06 E-value: 3.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 244 VLGFAGRIQP-LKAPDVLVRAVARLRALNPELaprlRLVVVGGpsgngaDNPRWLHDLAAelGIADAVTFLKPRAghELA 322
Cdd:pfam13692 3 VILFVGRLHPnVKGVDYLLEAVPLLRKRDNDV----RLVIVGD------GPEEELEELAA--GLEDRVIFTGFVE--DLA 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 310947090 323 EVFRACDVVGVPSYNETFGLVALEAQACGTPVVAAAVGGLTTAVaDGHSGLLIRGHDETDWANALDKLVTD 393
Cdd:pfam13692 69 ELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
43-410 |
3.57e-29 |
|
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: 117.04 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 43 GGMNVYVLQTARRLADRGVAVEIFTrATSSEQPPALSPSEgiTVHYVPAGPFEglskgdLPSQLCAFT-------NGVLR 115
Cdd:cd03823 15 GGAEISVHDLAEALVAEGHEVAVLT-AGVGPPGQATVARS--VVRYRRAPDET------LPLALKRRGyelfetyNPGLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 116 AEAAQPPGYF--DVIHSHYwLSG--QAAWLAAERWGVPHIHSAHtlakvkNLHLAAedtPEPFtrvvgeeQVVAESDALV 191
Cdd:cd03823 86 RLLARLLEDFrpDVVHTHN-LSGlgASLLDAARDLGIPVVHTLH------DYWLLC---PRQF-------LFKKGGDAVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 192 TNTsseaEVLVDLYRA---DPDKVTVTPPGVDPEvftpgdkLAARRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLR 268
Cdd:cd03823 149 APS----RFTANLHEAnglFSARISVIPNAVEPD-------LAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 269 ALNPELaprlrlVVVGGpsgngadnpRWLHDlAAELGIADAVTFLKPRAGHELAEVFRACDVVGVPS-YNETFGLVALEA 347
Cdd:cd03823 218 REDIEL------VIAGH---------GPLSD-ERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSiWPEPFGLVVREA 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 310947090 348 QACGTPVVAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAAR 410
Cdd:cd03823 282 IAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRST 344
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
23-424 |
7.69e-29 |
|
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274943 [Multi-domain] Cd Length: 373 Bit Score: 116.34 E-value: 7.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 23 RVAMVSMHTSPleqpgtgdAGGMnVYVLQTARRLADRGVAVEIFTRATSSEQPPALSPsegITVHYVPAGPFEGLSKGDL 102
Cdd:TIGR04047 1 RIALLTYSTKP--------RGGV-VHTLELAEALTALGHDVTVWALAADGFGFFRDPP---CAVRLVPVAPAPGDTDAMV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 103 PSQLCAFTNGVLRAEAAQppgyFDVIHSHYWLSGQAAWLAAERWGVPH-IHSAHtlakvknlHLAAEDTPEpftRVVGEE 181
Cdd:TIGR04047 69 EQRIARSIDHLRAHFARG----FDVVHAQDCISGNALATLRAEGLIPGfVRTVH--------HLDDFDDPR---LAACQE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 182 QVVAESDALVTNTSSEAEVLVDLYRADPdkvTVTPPGVDPEVFTP---GDKLAARRRLGLPDDALVLGFAGrIQPLKAPD 258
Cdd:TIGR04047 134 RAIVEADAVLCVSAAWAAELRAEWGIDA---TVVPNGVDAARFSPaadAADAALRRRLGLRGGPYVLAVGG-IEPRKNTI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 259 VLVRAVARLRALNPELaprlRLVVVGGPS-GNGADNPRWLHDLAAELGIA-DAVTFLKPRAGHELAEVFRACDVVGVPSY 336
Cdd:TIGR04047 210 DLLEAFALLRARRPQA----QLVIAGGATlFDYDAYRREFRARAAELGVDpGPVVITGPVPDADLPALYRCADAFAFPSL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 337 NETFGLVALEAQACGTPVVAAAVGGLTTAVaDGHSGLLIRGHDETDWANALdKLVTDAPRRARLAAGALDHAARFTWSHT 416
Cdd:TIGR04047 286 KEGFGLVVLEALASGIPVVASDIAPFTEYL-GRFDAAWADPSDPDSIADAL-ALALDPARRPALRAAGPELAARYTWDAS 363
|
....*...
gi 310947090 417 ADDLLGAY 424
Cdd:TIGR04047 364 ARAHLEFY 371
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
125-412 |
8.72e-29 |
|
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: 8.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 125 FDVIHSHYWLSGQAAWLAAERWGVPH-IHSAHTLA-------KVKNLHLAAEDTPEPFTrvvgeeqvvaesDALVTNTSS 196
Cdd:cd03808 82 PDIVHCHTPKPGILGRLAARLAGVPKvIYTVHGLGfvftegkLLRLLYLLLEKLALLFT------------DKVIFVNED 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 197 EAEVLVDLYRADPDKVTVTPP-GVDPEVFTPgdklaarRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLRALNPELa 275
Cdd:cd03808 150 DRDLAIKKGIIKKKKTVLIPGsGVDLDRFQY-------SPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNV- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 276 prlRLVVVG-GPSGNGADnprwlhDLAAELGIADAVTFLKPRagHELAEVFRACDVVGVPSYNETFGLVALEAQACGTPV 354
Cdd:cd03808 222 ---RFLLVGdGELENPSE------ILIEKLGLEGRIEFLGFR--SDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPV 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 310947090 355 VAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLA-AGALDHAARFT 412
Cdd:cd03808 291 ITTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGeAARKRVEEKFD 349
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
211-426 |
5.23e-28 |
|
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: 113.97 E-value: 5.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 211 KVTVTPPGVDPEVFTPGDKLAARRRLGLPDDALVLGFAGR--IQPLKAPDVLVRAvarLRALNPElaPRLRLVVVGGPSG 288
Cdd:cd03825 162 PVVVIPNGIDTEIFAPVDKAKARKRLGIPQDKKVILFGAEsvTKPRKGFDELIEA---LKLLATK--DDLLLVVFGKNDP 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 289 NGADNP------RWLHDlaaelgiadavtflkpraGHELAEVFRACDVVGVPSYNETFGLVALEAQACGTPVVAAAVGGL 362
Cdd:cd03825 237 QIVILPfdiislGYIDD------------------DEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGS 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 310947090 363 TTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHA-ARFTWSHTADDLLGAYGD 426
Cdd:cd03825 299 PEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAeNHFDQRVQAQRYLELYKD 363
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
313-429 |
9.13e-27 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 103.92 E-value: 9.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 313 LKPRAGHE--LAEVFRACDVVGVPSYNETFGLVALEAQACGTPVVAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKL 390
Cdd:COG0438 4 LVPRKGLDllLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 310947090 391 VTDAPRRARLAAGALDHAA-RFTWSHTADDLLGAYGDAIQ 429
Cdd:COG0438 84 LEDPELRRRLGEAARERAEeRFSWEAIAERLLALYEELLA 123
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
126-409 |
1.25e-25 |
|
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: 107.44 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 126 DVIHSHYwlsgqaawlaaerwGVPHIHSAHtLAK---------VKNLH------LAAEDTPEPFTRVVgeeqvVAESDAL 190
Cdd:cd04962 86 DVLHAHY--------------AIPHASCAY-LAReilgekipiVTTLHgtditlVGYDPSLQPAVRFS-----INKSDRV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 191 VTNTSSEAEVLVDLYraDPDK-VTVTPPGVDPEVFTPGDKLAARRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLRA 269
Cdd:cd04962 146 TAVSSSLRQETYELF--DVDKdIEVIHNFIDEDVFKRKPAGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRR 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 270 LNPElaprlRLVVVG-GPSGNGADNprwlhdLAAELGIADAVTFLKPRagHELAEVFRACDVVGVPSYNETFGLVALEAQ 348
Cdd:cd04962 224 KIPA-----KLLLVGdGPERVPAEE------LARELGVEDRVLFLGKQ--DDVEELLSIADLFLLPSEKESFGLAALEAM 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 310947090 349 ACGTPVVAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAA 409
Cdd:cd04962 291 ACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAA 351
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
37-415 |
2.34e-24 |
|
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: 103.47 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 37 PGTGDAGGMNVYVLQTARRLADRGVAVEIFTrATSSEQPPALSPSEGITVHYVPAGPFEGLSKG-DLPSQLCAFTNgVLR 115
Cdd:cd03820 7 PSISNAGGAERVAINLANHLAKKGYDVTIIS-LDSAEKPPFYELDDNIKIKNLGDRKYSHFKLLlKYFKKVRRLRK-YLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 116 AEAAqppgyfDVIHSHywLSGQAAWLAAERWGVPHIHSAHTlakvkNLHLaaedTPEPFTRVVGEEQVVAESDALVTNTS 195
Cdd:cd03820 85 NNKP------DVVISF--RTSLLTFLALIGLKSKLIVWEHN-----NYEA----YNKGLRRLLLRRLLYKRADKIVVLTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 196 SEAEvlvDLYRADPDKVTVTPPGVDPEVFTPGDKLAARRRLglpddalvlgFAGRIQPLKAPDVLVRAVARLRALNPELa 275
Cdd:cd03820 148 ADKL---KKYKQPNSNVVVIPNPLSFPSEEPSTNLKSKRIL----------AVGRLTYQKGFDLLIEAWALIAKKHPDW- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 276 pRLRLVvvggpsGNGADNPRwLHDLAAELGIADAVtFLKPRAGHeLAEVFRACDVVGVPSYNETFGLVALEAQACGTPVV 355
Cdd:cd03820 214 -KLRIY------GDGPEREE-LEKLIDKLGLEDRV-KLLGPTKN-IAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPII 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 310947090 356 A-AAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAARFTWSH 415
Cdd:cd03820 284 SfDCPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAERFSIEK 344
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
126-410 |
1.52e-23 |
|
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: 101.38 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 126 DVIHSHYWLSGQAAWLAAERWGVPHIHSAHTLAKVKNLHLAAEDTPEPFTRVVGEEQVVAESDALVTNTSSEAEVLVDLy 205
Cdd:cd05844 83 ALVHAHFGRDGVYALPLARALGVPLVVTFHGFDITTSRAWLAASPGWPSQFQRHRRALQRPAALFVAVSGFIRDRLLAR- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 206 RADPDKVTVTPPGVDPEVFTPGDKlaarrrlglPDDALVLGFAGRIQPLKAPDVLVRAVARLRALNPElaprLRLVVVgg 285
Cdd:cd05844 162 GLPAERIHVHYIGIDPAKFAPRDP---------AERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPT----ARLVIA-- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 286 psGNGADNPRwLHDLAAELGiadAVTFLKPRAGHELAEVFRACDVVGVPSY------NETFGLVALEAQACGTPVVAAAV 359
Cdd:cd05844 227 --GDGPLRPA-LQALAAALG---RVRFLGALPHAEVQDWMRRAEIFCLPSVtaasgdSEGLGIVLLEAAACGVPVVSSRH 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 310947090 360 GGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAAR 410
Cdd:cd05844 301 GGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCE 351
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
125-418 |
3.74e-22 |
|
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.
Pssm-ID: 340849 [Multi-domain] Cd Length: 370 Bit Score: 97.46 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 125 FDVIHSHYWLSgqaawLAAERWGVPHIHSAH--TLAKVKNLH-LAAEDTPEPFTRVVGEEqVVAESDALVTNTSSEAEVL 201
Cdd:cd03822 76 PDVVHIQHEFG-----IFGGKYGLYALGLLLhlRIPVITTLHtVLDLSDPGKQALKVLFR-IATLSERVVVMAPISRFLL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 202 VDLYRADPDKVTVTPPGVdPEVftPGDKLAARRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLRALNpelaPRLRLV 281
Cdd:cd03822 150 VRIKLIPAVNIEVIPHGV-PEV--PQDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEF----PDVRLV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 282 VVGGPSGNGADNP--RWLHDLAAELGIADAVTFlkPRAGHELAEVFR---ACDVVGVPSYNE---TFGLVALeAQACGTP 353
Cdd:cd03822 223 IAGELHPSLARYEgeRYRKAAIEELGLQDHVDF--HNNFLPEEEVPRyisAADVVVLPYLNTeqsSSGTLSY-AIACGKP 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 310947090 354 VVAAAVGGLTTAVADGhSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAARFTWSHTAD 418
Cdd:cd03822 300 VISTPLRHAEELLADG-RGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIAD 363
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
207-424 |
6.32e-22 |
|
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: 97.79 E-value: 6.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 207 ADPDKVTVTPPGVDPEVFTPgdklAARRRLglPDDALVLGFAGRIQPLKAPDVLVRAVARLRALNPELaprlRLVVVGGP 286
Cdd:cd03813 264 ADPDKTRVIPNGIDIQRFAP----AREERP--EKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDA----EGWLIGPE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 287 SgngaDNPRWLH---DLAAELGIADAVTFLKPRaghELAEVFRACDVVGVPSYNETFGLVALEAQACGTPVVAAAVGGLT 363
Cdd:cd03813 334 D----EDPEYAQeckRLVASLGLENKVKFLGFQ---NIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCR 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 310947090 364 TAV-----ADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAARFtwsHTADDLLGAY 424
Cdd:cd03813 407 ELIygaddALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKY---YTLEGMIDSY 469
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
43-222 |
1.92e-21 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 90.67 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 43 GGMNVYVLQTARRLADRGVAVEIFTRAtsseqPPALSPSEGITVHYVPAGPFeglSKGDLPSQLCAFTNGVLRAEAAQPP 122
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPG-----GPGPLAEEVVRVVRVPRVPL---PLPPRLLRSLAFLRRLRRLLRRERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 123 gyfDVIHSHYWLSGQAAWLAA-ERWGVPHIHSAHTLAKVKNLHLAAEDTPEPFTRVVgEEQVVAESDALVTNTSSEAEVL 201
Cdd:pfam13439 73 ---DVVHAHSPFPLGLAALAArLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRRL-ERRLLRRADRVIAVSEAVADEL 148
|
170 180
....*....|....*....|.
gi 310947090 202 VDLYRADPDKVTVTPPGVDPE 222
Cdd:pfam13439 149 RRLYGVPPEKIRVIPNGVDLE 169
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
23-424 |
1.96e-21 |
|
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: 94.66 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 23 RVAMVSmhtSPLEQPGTGDAGGMNVYVLQTARRLADRGVAVEIFTRATSseqppalspsegitvhyVPAGPFEGLSKGDL 102
Cdd:cd03802 1 RIAQVS---PPRGPVPPGKYGGTELVVSALTEGLVRRGHEVTLFAPGDS-----------------HTSAPLVAVIPRAL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 103 PSQLCAFTNGV----LRAEAAQPPGYFDVIHSHywlSGQAAWLAAERWGVPHIHSAHTLAKVKNLHLAAEDTPEPFtrvv 178
Cdd:cd03802 61 RLDPIPQESKLaellEALEVQLRASDFDVIHNH---SYDWLPPFAPLIGTPFVTTLHGPSIPPSLAIYAAEPPVNY---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 179 geeqvVAESDAlvtntsseaevlvdlYRA---DPDKVTVTPPGVDPEVFTPGDKlaarrrlglPDDalVLGFAGRIQPLK 255
Cdd:cd03802 134 -----VSISDA---------------QRAatpPIDYLTVVHNGLDPADYRFQPD---------PED--YLAFLGRIAPEK 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 256 APDVLVRAVARLRalnpelaprLRLVVVGGpsgngADNPRWlHDLAAELGIADAVTFLKPRAGHELAEVFRACDVVGVPS 335
Cdd:cd03802 183 GLEDAIRVARRAG---------LPLKIAGK-----VRDEDY-FYYLQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 336 -YNETFGLVALEAQACGTPVVAAAVGGLTTAVADGHSGLLIrgHDETDWANALDKLvtDAPRRARLAAGALDhaaRFTWS 414
Cdd:cd03802 248 nWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLV--DSVEEMAEAIANI--DRIDRAACRRYAED---RFSAA 320
|
410
....*....|
gi 310947090 415 HTADDLLGAY 424
Cdd:cd03802 321 RMADRYEALY 330
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
43-218 |
6.00e-21 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 89.00 E-value: 6.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 43 GGMNVYVLQTARRLADRGVAVEIFTRATSSEQPPAlsPSEGITVHYVPAGPFEGLSKgdlpsqLCAFTNGVLRAEAAQPP 122
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPEL--VGDGVRVHRLPVPPRPSPLA------DLAALRRLRRLLRAERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 123 gyfDVIHSHYWLSGQAAWLAAERWGVPHIHSAHTLAkvknlhLAAEDTPEPFTRVVGEEQVVAESDALVTNTSSEAEVLV 202
Cdd:pfam13579 73 ---DVVHAHSPTAGLAARLARRRRGVPLVVTVHGLA------LDYGSGWKRRLARALERRLLRRADAVVVVSEAEAELLR 143
|
170
....*....|....*.
gi 310947090 203 DLYrADPDKVTVTPPG 218
Cdd:pfam13579 144 ALG-VPAARVVVVPNG 158
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
41-404 |
6.37e-21 |
|
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: 93.49 E-value: 6.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 41 DAGGMNVYVLQTARRLADRGVAVEIFTRATSSEQPPalSPSEGITVHYVPagpfeglSKGDLPSQLCAFTN-GVLRAEAA 119
Cdd:cd03795 12 DIGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPE--KEENGIRIHRVK-------SFLNVASTPFSPSYiKRFKKLAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 120 QPpgyfDVIHSHY-WLSGQAA--WLAAERWGVPHIHS----------------AHTLAKVKnlhlaaedtpepftrvvge 180
Cdd:cd03795 83 EY----DIIHYHFpNPLADLLlfFSGAKKPVVVHWHSdivkqkkllklykplmTRFLRRAD------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 181 eQVVAESDALVTNTsseaEVLVDlYRadpDKVTVTPPGVDPEVFTPGDKLAARRRLGLPDDALVLgFAGRIQPLKAPDVL 260
Cdd:cd03795 140 -RIIATSPNYVETS----PTLRE-FK---NKVRVIPLGIDKNVYNIPRVDFENIKREKKGKKIFL-FIGRLVYYKGLDYL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 261 VRAVarlRALNPELaprlrlVVVG-GPSGNgadnprwlhDL--AAELGIADAVTFLKPRAGHELAEVFRACDVVGVPSY- 336
Cdd:cd03795 210 IEAA---QYLNYPI------VIGGeGPLKP---------DLeaQIELNLLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVl 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 337 -NETFGLVALEAQACGTPVVAAAVGGLTTAVA-DGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGA 404
Cdd:cd03795 272 rSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNnNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENA 341
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
247-375 |
1.14e-19 |
|
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: 87.46 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 247 FAGRIQPLKAPDVLVRAVARLRALNPelapRLRLVVVGGpsgnGADNPRWLHDLAAELGIADAVTFLKPRAGHELAEVFR 326
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLKARLP----DLVLVLVGG----GGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLA 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 310947090 327 ACDVVGVPSYNETFGLVALEAQACGTPVVAAAVGGLTTAVADGHSGLLI 375
Cdd:cd01635 187 AADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
211-413 |
1.75e-17 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 84.38 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 211 KVTVTPPGVDPEVFTPGDKLAA-RRRL--GLPDDALVlGFAGRIQPLKAPDVLVRAVARLralnpelaPRLRLVVVGgps 287
Cdd:PLN02871 230 RIRVWNKGVDSESFHPRFRSEEmRARLsgGEPEKPLI-VYVGRLGAEKNLDFLKRVMERL--------PGARLAFVG--- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 288 gNGADNPRwLHDLAAELgiadAVTFLKPRAGHELAEVFRACDVVGVPSYNETFGLVALEAQACGTPVVAAAVGGLTTAVA 367
Cdd:PLN02871 298 -DGPYREE-LEKMFAGT----PTVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIP 371
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 310947090 368 D---GHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAARFTW 413
Cdd:PLN02871 372 PdqeGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEKWDW 420
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
125-397 |
3.05e-17 |
|
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: 82.72 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 125 FDVIHSHYWLSGQAAWLAAERWGVPH--IHSAHTLAKVKNLHLAAEDTPEPFTRVVgeeqvvaeSDALVTNTSSEAEVLV 202
Cdd:cd03812 81 YDIVHVHGSSSNGIILLLAAKAGVPVriAHSHNTKDSSIKLRKIRKNVLKKLIERL--------STKYLACSEDAGEWLF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 203 DLyrADPDKVTVTPPGVDPEVFTPGDKLAARRR-LGLPDDALVLGFAGRIQPLKAPDVLVRAVARLRALNPelapRLRLV 281
Cdd:cd03812 153 GE--VENGKFKVIPNGIDIEKYKFNKEKRRKRRkLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNP----NVKLV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 282 VVG-GPSGNGadnprwLHDLAAELGIADAVTFLkpraGHE--LAEVFRACDVVGVPSYNETFGLVALEAQACGTPVVAAA 358
Cdd:cd03812 227 LVGeGELKEK------IKEKVKELGLEDKVIFL----GFRndVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSD 296
|
250 260 270
....*....|....*....|....*....|....*....
gi 310947090 359 VGGLTTAVADGHSGLLIRGHDETdWANALDKLVTDAPRR 397
Cdd:cd03812 297 TITKECDITNNVEFLPLNETPST-WAEKILKLIKRKRRI 334
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
198-417 |
3.86e-17 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 82.53 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 198 AEVLVDLYRAD-PD-KVTVTPPGVDPEVFTPGDKLAARRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLRALNPEla 275
Cdd:PRK15484 147 SQFLKKFYEERlPNaDISIVPNGFCLETYQSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSN-- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 276 prLRLVVVGGP----SGNGADNPRWLHDLAAELGiaDAVTFLKPRAGHELAEVFRACDVVGVPS-YNETFGLVALEAQAC 350
Cdd:PRK15484 225 --LKLVVVGDPtassKGEKAAYQKKVLEAAKRIG--DRCIMLGGQPPEKMHNYYPLADLVVVPSqVEEAFCMVAVEAMAA 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 310947090 351 GTPVVAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHA-ARFTWSHTA 417
Cdd:PRK15484 301 GKPVLASTKGGITEFVLEGITGYHLAEPMTSDSIISDINRTLADPELTQIAEQAKDFVfSKYSWEGVT 368
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
150-412 |
2.17e-15 |
|
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: 76.96 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 150 HIHSAHTLAKVKNLHLAAEDTPEPFTRVVGEEQVVAES---DALVTNTSSEAEVLVDLYRADPdKVTVTPPGVDPEVFTP 226
Cdd:cd04949 74 TKGPAKKGAVLHNEHVKNNDDPEHSLIKNFYKYVFENLnkyDAIIVSTEQQKQDLSERFNKYP-PIFTIPVGYVDQLDTA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 227 GDKLAARRRLglpddalvLGFAGRIQPLKAPDVLVRAVARLRALNPELaprlRLVVVGgpSGNGADNPRwlhDLAAELGI 306
Cdd:cd04949 153 ESNHERKSNK--------IITISRLAPEKQLDHLIEAVAKAVKKVPEI----TLDIYG--YGEEREKLK---KLIEELHL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 307 ADAVTFlkpRAGH-ELAEVFRACDVVGVPSYNETFGLVALEAQACGTPVVAAAVG-GLTTAVADGHSGLLIRGHDETDWA 384
Cdd:cd04949 216 EDNVFL---KGYHsNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALA 292
|
250 260
....*....|....*....|....*...
gi 310947090 385 NALDKLVTDAPRRARLAAGALDHAARFT 412
Cdd:cd04949 293 DKIIELLNDPEKLQQFSEESYKIAEKYS 320
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
126-424 |
1.83e-14 |
|
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: 74.91 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 126 DVIHSHYWLSGQAAWLAAERW------GVPHIHSAHTLAK--VKNLHLAAEDT--PEPFTRVVGE--EQV------VAES 187
Cdd:cd03791 130 DIIHANDWHTALVPAYLKTRYrgpgfkKIKTVFTIHNLAYqgLFPLDTLAELGlpPELFHIDGLEfyGQInflkagIVYA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 188 DALVT--NTSSEaEVLVDLY--------RADPDKVTVTPPGVDPEVFTPG-------------------DKLAARRRLGL 238
Cdd:cd03791 210 DRVTTvsPTYAK-EILTPEYgegldgvlRARAGKLSGILNGIDYDEWNPAtdklipanysandlegkaeNKAALQKELGL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 239 P--DDALVLGFAGRIQPLKAPDVLVRAVARLRALNpelaprLRLVVVGgpSGngadnPRWLHDLAAELgiadAVTFLKPR 316
Cdd:cd03791 289 PvdPDAPLFGFVGRLTEQKGVDLILDALPELLEEG------GQLVVLG--SG-----DPEYEQAFREL----AERYPGKV 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 317 AGH-----ELA-EVFRACDVVGVPSYNETFGLVALEAQACGTPVVAAAVGGLTTAVADGH------SGLLIRGHDETDWA 384
Cdd:cd03791 352 AVVigfdeALAhRIYAGADFFLMPSRFEPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYDpetgegTGFVFEDYDAEALL 431
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 310947090 385 NALDK---LVTDAPRRARLAAGALdhAARFTWSHTADDLLGAY 424
Cdd:cd03791 432 AALRRalaLYRNPELWRKLQKNAM--KQDFSWDKSAKEYLELY 472
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
192-395 |
1.05e-13 |
|
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: 72.09 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 192 TNTSSEAEVLVDLYRADPD-KVTVTPPGVDPEVF--TPGDKLAARRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLr 268
Cdd:cd04951 135 TNVSREALDEFIAKKAFSKnKSVPVYNGIDLNKFkkDINVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISEL- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 269 alnPELAPRLRLVVVG-GPSGNGadnprwLHDLAAELGIADAVTFLKPRAghELAEVFRACDVVGVPSYNETFGLVALEA 347
Cdd:cd04951 214 ---ILSKNDFKLLIAGdGPLRNE------LERLICNLNLVDRVILLGQIS--NISEYYNAADLFVLSSEWEGFGLVVAEA 282
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 310947090 348 QACGTPVVAAAVGGLTTAVADghSGLLIRGHDETDWANALDKLVTDAP 395
Cdd:cd04951 283 MACERPVVATDAGGVAEVVGD--HNYVVPVSDPQLLAEKIKEIFDMSD 328
|
|
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
41-415 |
1.99e-13 |
|
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.
Pssm-ID: 274147 [Multi-domain] Cd Length: 1050 Bit Score: 72.51 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 41 DAGGMNVYVLQTARRLADR-GV-AVEIFTRATSS--------EQPPALSP------------SEGITVHYVPAGPFEG-L 97
Cdd:TIGR02468 193 DTGGQVKYVVELARALGSMpGVyRVDLLTRQVSSpdvdwsygEPTEMLTPrssendgdemgeSSGAYIIRIPFGPRDKyI 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 98 SKGDLPSQLCAFTNGVLR---------AEAAQP--PGYFDVIHSHYWLSGQAAWLAAERWGVPHIHSAHTLAK------V 160
Cdd:TIGR02468 273 PKEELWPYIPEFVDGALShivnmskvlGEQIGSghPVWPYVIHGHYADAGDSAALLSGALNVPMVLTGHSLGRdkleqlL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 161 KNLHLAAED---TPEPFTRVVGEEQVVAESDALVTNTSSEAEVLVDLYRA-DP---------------------DKVTVT 215
Cdd:TIGR02468 353 KQGRMSKEEinsTYKIMRRIEAEELSLDASEIVITSTRQEIEEQWGLYDGfDVilerklrararrgvscygrfmPRMAVI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 216 PPGVDPEVFTPGDKLAARRRLGLPDDA---------------------LVLGFAgRIQPLKAPDVLVRAVARLRALNpEL 274
Cdd:TIGR02468 433 PPGMEFSHIVPHDGDMDGETEGNEEHPakpdppiwseimrfftnprkpMILALA-RPDPKKNITTLVKAFGECRPLR-EL 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 275 AprlRLVVVGG--------PSGNGADnprwlhdLAAELGIAD------AVTFLKPRAGHELAEVFR-ACDVVGV---PSY 336
Cdd:TIGR02468 511 A---NLTLIMGnrddidemSSGSSSV-------LTSVLKLIDkydlygQVAYPKHHKQSDVPDIYRlAAKTKGVfinPAF 580
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 310947090 337 NETFGLVALEAQACGTPVVAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAARFTWSH 415
Cdd:TIGR02468 581 IEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKLVADKQLWAECRQNGLKNIHLFSWPE 659
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
184-410 |
7.47e-13 |
|
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: 69.70 E-value: 7.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 184 VAESDALVTNTSSEAEVLVDLYRadpDKVTVTPPGVDPEVFTPGDklAARRRLG----LPDDALVLGFAGR-IQPLKAPD 258
Cdd:cd03818 156 LEQADLGVTPTRWQRSLFPAAYR---DRISVIHDGVDTDRLAPDP--AARLRLLngteLKAGDPVITYVARnLEPYRGFH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 259 VLVRAVARLRALNPELaprlRLVVVGGPS----GNGADNPRWLHDLAAELGIADA-VTFLKPRAGHELAEVFRACDVVGV 333
Cdd:cd03818 231 VFMRALPRIQARRPDA----RVVVVGGDGvsygSPPPDGGSWKQKMLAELGVDLErVHFVGKVPYDQYVRLLQLSDAHVY 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 310947090 334 PSYNETFGLVALEAQACGTPVVAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAAR 410
Cdd:cd03818 307 LTYPFVLSWSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVER 383
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
261-412 |
1.83e-12 |
|
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.
Pssm-ID: 340834 [Multi-domain] Cd Length: 392 Bit Score: 68.38 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 261 VRAVARLRALNPElAPRLRLVVVGGPSGNGADNP---RWLHDLAAEL-GIADAVTFLKPRAGHELAEVFRACD-VVGVPS 335
Cdd:cd03805 230 IEAFAKLKQKLPE-FENVRLVIAGGYDPRVAENVeylEELQRLAEELlNVEDQVLFLRSISDSQKEQLLSSALaLLYTPS 308
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 310947090 336 yNETFGLVALEAQACGTPVVAAAVGGLTTAVADGHSGLLIRGHDEtDWANALDKLVTDAPRRARL-AAGALDHAARFT 412
Cdd:cd03805 309 -NEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPE-AFAEAMLKLANDPDLADRMgAAGRKRVKEKFS 384
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
207-424 |
2.60e-12 |
|
GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.
Pssm-ID: 411604 [Multi-domain] Cd Length: 489 Bit Score: 68.42 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 207 ADPDKVTVTPPGVDPEVFTPgdkLAARRRLGLPDdalVLGFAGRIQPLKAPDVLVRAVARLRALNPELAPRlrlvvVGGP 286
Cdd:NF038011 277 APPERTRVIPNGIDLPRLAP---LRAQRPAGIPP---VVGLIGRVVPIKDIKTFIRAMRTVVRAMPEAEGW-----IVGP 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 287 SGNGADNPRWLHDLAAELGIADAVTFLKPRaghELAEVFRACDVVGVPSYNETFGLVALEAQACGTPVVAAAVG------ 360
Cdd:NF038011 346 EEEDPAYAAECRSLVASLGLQDKVKFLGFQ---KIDDLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVGscrqli 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 310947090 361 -GLTTAVAD-GHSGLLIRGHDETDWANALDKLVTDAPR-RARLAAGaldhAARFTWSHTADDLLGAY 424
Cdd:NF038011 423 eGLDEEDRAlGAAGEVVAIADPQALARAALDLLRDPQRwQAAQAAG----LARVERYYTEELMFDRY 485
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
188-374 |
4.09e-12 |
|
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: 67.31 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 188 DALVTNTSSEAEVLVDLYRADPdkvTVTPPGVDPEVFTPgdklAARRRlglpDDALVlgfAGRIQPLKAPDVLVRAVARL 267
Cdd:cd03804 159 DLFIANSQFVARRIKKFYGRES---TVIYPPVDTDAFAP----AADKE----DYYLT---ASRLVPYKRIDLAVEAFNEL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 268 ralnpelaPRlRLVVVG-GPsgngadnprwlhDLAAELGIADA-VTFLKPRAGHELAEVFRACDVVGVPSyNETFGLVAL 345
Cdd:cd03804 225 --------PK-RLVVIGdGP------------DLDRLRAMASPnVEFLGYQPDEVLKELLSKARAFVFAA-EEDFGIVPV 282
|
170 180
....*....|....*....|....*....
gi 310947090 346 EAQACGTPVVAAAVGGLTTAVADGHSGLL 374
Cdd:cd03804 283 EAQACGTPVIAFGKGGALETVRPGPTGIL 311
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
216-407 |
4.06e-11 |
|
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: 64.26 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 216 PPGVDP-----EVFTPGDKLAARRRLGL--PDDALVLGFAgRIQPLKAPDVLVRAVARLRALNPELaprlRLVVVGGPSG 288
Cdd:cd03792 165 PPSIDPlsgknKDLSPADIRYYLEKPFVidPERPYILQVA-RFDPSKDPLGVIDAYKLFKRRAEEP----QLVICGHGAV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 289 NGADNPRWLHDLAAELGIADAVTFLKPRAGHELAEVF-RACDVVGVPSYNETFGLVALEAQACGTPVVAAAVGGLTTAVA 367
Cdd:cd03792 240 DDPEGSVVYEEVMEYAGDDHDIHVLRLPPSDQEINALqRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVI 319
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 310947090 368 DGHSGLLIRGHDETdwANALDKLVTDAPRRARLAAGALDH 407
Cdd:cd03792 320 DGETGFLVNSVEGA--AVRILRLLTDPELRRKMGLAAREH 357
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
24-412 |
4.47e-11 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 65.06 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 24 VAMVSMHTSPLEQPGTGDAGGMNVYVLQTARR---------LADRGVAVEIFTRATS---SEQPPALSPSEGItVHYVPA 91
Cdd:PRK15179 305 VALQSAIQQGQSIAGYGVLGPVQVVCRSLRSRegadffaatLADAGIPVSVYSDMQAwggCEFSSLLAPYREY-LRFLPK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 92 GPFEGLSKgdlpsqlcafTNGVLRAEAaqppgyFDVIHshYWLSGQ--AAWLAAERWGVPHIH-SAHTLAKVKNLHLAAE 168
Cdd:PRK15179 384 QIIEGTTK----------LTDVMRSSV------PSVVH--IWQDGSifACALAALLAGVPRIVlSVRTMPPVDRPDRYRV 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 169 DTPEPFTRVVGEEQVvaesdALVTNTSSEAEVLVDLYRADPDKVTVTPPGVDP--EVFTPGDK-LAARRRLGLPDDALVL 245
Cdd:PRK15179 446 EYDIIYSELLKMRGV-----ALSSNSQFAAHRYADWLGVDERRIPVVYNGLAPlkSVQDDACTaMMAQFDARTSDARFTV 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 246 GFAGRIQPLKAPDVLVRAVARLRALNPelapRLRLVVVGGpsGNGADNPRwlhDLAAELGIADAVTF--LKPRAGHELAE 323
Cdd:PRK15179 521 GTVMRVDDNKRPFLWVEAAQRFAASHP----KVRFIMVGG--GPLLESVR---EFAQRLGMGERILFtgLSRRVGYWLTQ 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 324 VfracDVVGVPSYNETFGLVALEAQACGTPVVAAAVGGLTTAVADGHSGLLIRGHDET--DWANALDKLVTDAPRRARLA 401
Cdd:PRK15179 592 F----NAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTapDVAEALARIHDMCAADPGIA 667
|
410
....*....|..
gi 310947090 402 AGALDHA-ARFT 412
Cdd:PRK15179 668 RKAADWAsARFS 679
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
23-361 |
1.15e-10 |
|
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: 63.03 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 23 RVAMVSMHTSPLeqpgtgdAGGMNVYVLQTARRLADRGVAVEIFTRATSSEQP-PALSPseGITVHYVPAGPFegLSKGD 101
Cdd:cd03796 1 RICMVSDFFYPN-------LGGVETHIYQLSQCLIKRGHKVIVITHAYGNRVGvRYLTN--GLKVYYLPFKVF--YNQST 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 102 LPSQLCAFT---NGVLRAEAaqppgyfDVIHSHYWLSGQA--AWLAAERWGVPHI---HSAHTLAKVKNLHLAAedtpep 173
Cdd:cd03796 70 LPTLFSTFPllrNILIRERI-------QIVHGHQAFSSLAheALFHARTLGLKTVftdHSLFGFADASSILTNK------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 174 FTRVVgeeqvVAESDAL--VTNTSSEAEVLvdlyRA--DPDKVTVTPPGVDPEVFTPGDKLAarrrlglPDDALVLGFAG 249
Cdd:cd03796 137 LLRFS-----LADIDHVicVSHTSKENTVL----RAslDPRIVSVIPNAVDSSDFTPDPSKP-------DPNKITIVVIS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 250 RIQPLKAPDVLVRAVARLRALNPELaprlRLVVVGgpsgngaDNPRW--LHDLAAELGIADAVTFLKPRAGHELAEVFRA 327
Cdd:cd03796 201 RLVYRKGIDLLVGIIPRICKKHPNV----RFIIGG-------DGPKRieLEEMREKYQLQDRVELLGAVPHEEVRDVLVQ 269
|
330 340 350
....*....|....*....|....*....|....
gi 310947090 328 CDVVGVPSYNETFGLVALEAQACGTPVVAAAVGG 361
Cdd:cd03796 270 GHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGG 303
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
330-422 |
1.43e-09 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 54.92 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 330 VVGVPSYNETFGLVALEAQACGTPVVAAAVGGLTTAVADGHSGLLIRghDETDWANALDKLVTDAPRRARLAAGALDHA- 408
Cdd:pfam13524 2 VLNPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERVl 79
|
90
....*....|....
gi 310947090 409 ARFTWSHTADDLLG 422
Cdd:pfam13524 80 AEHTYAHRAEQLLD 93
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
181-391 |
2.30e-08 |
|
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: 55.53 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 181 EQVVAESDALVTNTSSEAEVLVDLyRADPDKVTVTPPGVDPEVFTPGDklaarRRLGlPDDALVLGFAGRIQPLKAPDVL 260
Cdd:cd03799 120 PQLFAQGDLFLPNCELFKHRLIAL-GCDEKKIIVHRSGIDCNKFRFKP-----RYLP-LDGKIRILTVGRLTEKKGLEYA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 261 VRAVARLRalnpELAPRLRLVVVG-GPSGNGadnprwLHDLAAELGIADAVTFLKPRAGHELAEVFRACDVVGVPSYNET 339
Cdd:cd03799 193 IEAVAKLA----QKYPNIEYQIIGdGDLKEQ------LQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTAA 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 310947090 340 FG-----LVAL-EAQACGTPVVAAAVGGLTTAVADGHSGLLIRGHDETDWANALDKLV 391
Cdd:cd03799 263 DGdqdgpPNTLkEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLI 320
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
249-423 |
1.24e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 50.51 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 249 GRIQPLKAPDVLVRAVARLRALNPELAPRLRLVVVGGPSGNgADNPRW--LHDLAAELGIADAVTFLKPRAGHELAEVFR 326
Cdd:PLN02949 275 AQFRPEKAHALQLEAFALALEKLDADVPRPKLQFVGSCRNK-EDEERLqkLKDRAKELGLDGDVEFHKNVSYRDLVRLLG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 327 ACdVVGVPSY-NETFGLVALEAQACGTPVVAAAVGG----LTTAVADGHSGLLIRGHDEtdWANALDKLVT-DAPRRARL 400
Cdd:PLN02949 354 GA-VAGLHSMiDEHFGISVVEYMAAGAVPIAHNSAGpkmdIVLDEDGQQTGFLATTVEE--YADAILEVLRmRETERLEI 430
|
170 180
....*....|....*....|...
gi 310947090 401 AAGALDHAARFTWSHTADDLLGA 423
Cdd:PLN02949 431 AAAARKRANRFSEQRFNEDFKDA 453
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
203-412 |
1.46e-06 |
|
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.
Pssm-ID: 340835 [Multi-domain] Cd Length: 419 Bit Score: 50.30 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 203 DLYRADPDKVTVTPPgVDPEVFTPGDKLAARRrlglPDDALVLGfagRIQPLKAPDVLVRAVARLRALNPELAPR-LRLV 281
Cdd:cd03806 206 QLWKRNIKPSIVYPP-CDTEELTKLPIDEKTR----ENQILSIA---QFRPEKNHPLQLRAFAELLKRLPESIRSnPKLV 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 282 VVGGpSGNGADNPR--WLHDLAAELGIADAVTFLKPRAGHELAEVFRACdVVGVPS-YNETFGLVALEAQACGTPVVAAA 358
Cdd:cd03806 278 LIGS-CRNEEDKERveALKLLAKELILEDSVEFVVDAPYEELKELLSTA-SIGLHTmWNEHFGIGVVEYMAAGLIPLAHA 355
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 310947090 359 VGG----LTTAVADGHSGLLIRghDETDWANALDKLVTDAPR-RARLAAGALDHAARFT 412
Cdd:cd03806 356 SAGplldIVVPWDGGPTGFLAS--TPEEYAEAIEKILTLSEEeRLQRREAARSSAERFS 412
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
208-435 |
5.17e-06 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 48.43 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 208 DPDKVTVTPPGVDPEVFTP---GDKLAARRRLGLPDDALVLGFAGRIQPLKAPDVLVRAVARLRAlnpelAPRLRLVVVG 284
Cdd:PRK10307 192 AAEKVIFFPNWSEVARFQPvadADVDALRAQLGLPDGKKIVLYSGNIGEKQGLELVIDAARRLRD-----RPDLIFVICG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 285 gpSGNGADNprwLHDLAAELGIADaVTFLKPRAGHELAEVFRACDVVGVPSYNETFGLVaLEAQ-----ACGTPVVAAAV 359
Cdd:PRK10307 267 --QGGGKAR---LEKMAQCRGLPN-VHFLPLQPYDRLPALLKMADCHLLPQKAGAADLV-LPSKltnmlASGRNVVATAE 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 310947090 360 GGLTTAVADGHSGLLIRGHDETDWANALDKLVTDAPRRARLAAGALDHAARfTWSHtaDDLLGAYGDAIQRRAVSP 435
Cdd:PRK10307 340 PGTELGQLVEGIGVCVEPESVEALVAAIAALARQALLRPKLGTVAREYAER-TLDK--ENVLRQFIADIRGLVAER 412
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
228-369 |
9.59e-05 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 44.72 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 228 DKLAARRRLGLPD-DALVLGFAGRIQPLKAPDVLVRAVARLRALNPelaprlRLVVVGgpSGNGADNpRWLHDLAAELgi 306
Cdd:PRK00654 267 NKRALQERFGLPDdDAPLFAMVSRLTEQKGLDLVLEALPELLEQGG------QLVLLG--TGDPELE-EAFRALAARY-- 335
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 310947090 307 ADAVTFlkpRAGH--ELA-EVFRACDVVGVPSYNETFGLVALEAQACGTPVVAAAVGGLTTAVADG 369
Cdd:PRK00654 336 PGKVGV---QIGYdeALAhRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPIVRRTGGLADTVIDY 398
|
|
| LpxB |
COG0763 |
Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide ... |
222-410 |
1.04e-04 |
|
Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 440526 Cd Length: 378 Bit Score: 44.29 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 222 EVFTPGDKLAARRRLGLPDDALVLG-FAG-RIQPLK--APdVLVRAVARLRALNPELaprlRLVVVGGPSgngaDNPRWL 297
Cdd:COG0763 165 EIPLEPDRAAARARLGLDPDKPVIAlLPGsRRSEIKrlLP-VFLEAAKLLAARRPDL----QFVVPLAPS----LRRELI 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 298 HDLAAELGIAdaVTFLKPRAghelAEVFRACDVVGVPSynetfGLVALEAQACGTP-VVAAAVGGLTTAVAdghsGLLIR 376
Cdd:COG0763 236 EAALADWPLP--VTLVDGQT----YDAMAAADAALVAS-----GTATLEAALLGVPmVVAYKVSPLTYWIA----KRLVK 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 310947090 377 ghdeTDW--------------------------ANALDKLVTDAPRRARLAA------------GALDHAAR 410
Cdd:COG0763 301 ----VPYislpnllagrevvpellqddatpenlAAALLRLLDDPAARAAQLAafaelrqllgegGASERAAE 368
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
218-362 |
3.56e-04 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 42.77 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 218 GVDPEVFTPG-------------------DKLAARRRLGLP--DDALVLGFAGRIQPLKAPDVLVRAVARLRALNpelap 276
Cdd:COG0297 250 GIDYDVWNPAtdpylpanysaddlegkaaNKAALQEELGLPvdPDAPLIGMVSRLTEQKGLDLLLEALDELLEED----- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 277 rLRLVVVGgpSGNgadnPR---WLHDLAAELgiadavtflKPRAG------HELA-EVFRACDVVGVPSYNETFGLVALE 346
Cdd:COG0297 325 -VQLVVLG--SGD----PEyeeAFRELAARY---------PGRVAvyigydEALAhRIYAGADFFLMPSRFEPCGLNQMY 388
|
170
....*....|....*.
gi 310947090 347 AQACGTPVVAAAVGGL 362
Cdd:COG0297 389 ALRYGTVPIVRRTGGL 404
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
323-432 |
3.25e-03 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 39.96 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310947090 323 EVFRA-CDVVGV---PSYNETFGLVALEAQACGTPVVAAAVGGLTTAVADGHSGLLIRGHDETDWANAL----DKLVTDA 394
Cdd:PLN00142 658 ELYRYiADTKGAfvqPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDEAANKIadffEKCKEDP 737
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 310947090 395 PRRARLAAGALDHA-ARFTWSHTADDLL---GAYG-----DAIQRRA 432
Cdd:PLN00142 738 SYWNKISDAGLQRIyECYTWKIYAERLLtlgGVYGfwkyvSKLERRE 784
|
|
| |
