|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
86-492 |
3.62e-60 |
|
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: 202.00 E-value: 3.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 86 KIAVVVKKWPRKSqaGGLERHALTLHLALANRGHELHVFTAASPSFPEYQLKNLMFHLSEPTAAGYLDQASVSQQLQTQN 165
Cdd:cd03801 1 KILLLSPELPPPV--GGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 166 AsGRPFDVIHTES--VGLLHTRAKNLRN--VVASWHGIAYETFhsdiiqellrqadiaaataagteeeqpppssPALTER 241
Cdd:cd03801 79 R-LRKFDVVHAHGllAALLAALLALLLGapLVVTLHGAEPGRL-------------------------------LLLLAA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 242 AKRVVEEVKFFQRYA-HHVATSDHCGDVLKRIYMIPEERVHIILNGVDENVFKPDVSKREsfrekfgvrsgKNKKSPLVL 320
Cdd:cd03801 127 ERRLLARAEALLRRAdAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSPPLRRKL-----------GIPPDRPVL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 321 GIAGRLVRDKGHPLMFSALKRVFEENKEARenvVVLVAGDGPWGNRYKDLG---STNVIVLGPLDQEKLAGFYNAIDVFV 397
Cdd:cd03801 196 LFVGRLSPRKGVDLLLEALAKLLRRGPDVR---LVIVGGDGPLRAELEELElglGDRVRFLGFVPDEELPALYAAADVFV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 398 NPTlRAQGLDHTLLEAMVSGKPVLATRLASITGSVVVGPHlGYTFSP-NVESLTEAILRVVSDGtEELQRKGKEARERSL 476
Cdd:cd03801 273 LPS-RYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEG-GLVVPPdDVEALADALLRLLADP-ELRARLGRAARERVA 349
|
410
....*....|....*.
gi 42568648 477 RLFTATKMADSYERFF 492
Cdd:cd03801 350 ERFSWERVAERLLDLY 365
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
89-486 |
5.71e-31 |
|
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: 123.26 E-value: 5.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 89 VVVKKWPRKSQAGGLERHALTLHLALANRGHELHVFTAASPSFPEYQLK------------NLMFHLSEPTAAGY--LDQ 154
Cdd:cd03798 2 LILTNIYPNANSPGRGIFVRRQVRALSRRGVDVEVLAPAPWGPAAARLLrkllgeavpprdGRRLLPLKPRLRLLapLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 155 ASVSQQLQTQNasGRPFDVIHTE---SVGLLHTRAKNLRNV--VASWHGiayetfhSDIiqellrqadiaaataagteee 229
Cdd:cd03798 82 PSLAKLLKRRR--RGPPDLIHAHfayPAGFAAALLARLYGVpyVVTEHG-------SDI--------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 230 QPPPSSPALTERAKRVVEevkffqRYAHHVATSDHCGDVLKRIYMiPEERVHIILNGVDENVFKPdvskresfrekfGVR 309
Cdd:cd03798 132 NVFPPRSLLRKLLRWALR------RAARVIAVSKALAEELVALGV-PRDRVDVIPNGVDPARFQP------------EDR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 310 SGKNKKSPLVLGIAGRLVRDKGHPLMFSALKRVFEenkeARENVVVLVAGDGPWGNRYKDLGST-----NVIVLGPLDQE 384
Cdd:cd03798 193 GLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAK----ARPDVVLLIVGDGPLREALRALAEDlglgdRVTFTGRLPHE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 385 KLAGFYNAIDVFVNPTlRAQGLDHTLLEAMVSGKPVLATRLASItGSVVVGPHLGYTFSP-NVESLTEAILRVVSDgtEE 463
Cdd:cd03798 269 QVPAYYRACDVFVLPS-RHEGFGLVLLEAMACGLPVVATDVGGI-PEVVGDPETGLLVPPgDADALAAALRRALAE--PY 344
|
410 420
....*....|....*....|...
gi 42568648 464 LQRKGKEARERSLRLFTATKMAD 486
Cdd:cd03798 345 LRELGEAARARVAERFSWVKAAD 367
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
100-490 |
1.89e-27 |
|
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: 113.87 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 100 AGGLERHALTLHLALANRGHELHVFT-AASPSFP-------------------EYQLKNLMFHlseptaagYLDqASVSQ 159
Cdd:cd03800 20 TGGQNVYVLELARALAELGYQVDIFTrRISPADPevveiapgarvirvpagppEYLPKEELWP--------YLE-EFADG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 160 QLQTQNASGRPFDVIHTE-----SVGLLhtraknlrnvVASWHGIAY-ETFHSDIIQELLRQADiaaataagteeeQPPP 233
Cdd:cd03800 91 LLRFIAREGGRYDLIHSHywdsgLVGAL----------LARRLGVPLvHTFHSLGRVKYRHLGA------------QDTY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 234 SSPALTERAKRVVEEVKFFqryahhVATSDHCGDVLKRIYMIPEERVHIILNGVDENVFKPdVSKRESFREKFGVRSGKn 313
Cdd:cd03800 149 HPSLRITAEEQILEAADRV------IASTPQEADELISLYGADPSRINVVPPGVDLERFFP-VDRAEARRARLLLPPDK- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 314 kksPLVLGIaGRLVRDKGhplmFSALKRVFEENKEARENVVVLVAGDGPWGNRYKDLGSTNVIV-----------LGPLD 382
Cdd:cd03800 221 ---PVVLAL-GRLDPRKG----IDTLVRAFAQLPELRELANLVLVGGPSDDPLSMDREELAELAeelglidrvrfPGRVS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 383 QEKLAGFYNAIDVFVNPTL-RAQGLdhTLLEAMVSGKPVLATRLASITGSVVVGPHlGYTFSPN-VESLTEAILRVVSDG 460
Cdd:cd03800 293 RDDLPELYRAADVFVVPSLyEPFGL--TAIEAMACGTPVVATAVGGLQDIVRDGRT-GLLVDPHdPEALAAALRRLLDDP 369
|
410 420 430
....*....|....*....|....*....|
gi 42568648 461 tEELQRKGKEARERSLRLFTATKMADSYER 490
Cdd:cd03800 370 -ALWQRLSRAGLERARAHYTWESVADQLLT 398
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
101-494 |
5.98e-27 |
|
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: 111.29 E-value: 5.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 101 GGLERHALTLHLALANRGHELHVFTAASPSFPEYQL--KNLMFHLSEPTAAGYLdqASVSQQLQTQnasgRPFDVIHTes 178
Cdd:cd03819 11 GGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQigIGLPGLKVPLLRALLG--NVRLARLIRR----ERIDLIHA-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 179 vgllHTRAKN-LRNVVASWHGIAY-ETFHSdiiqellrqadiaaataagteeeqpppsSPALTERAKRVVEEVKFFQRYA 256
Cdd:cd03819 83 ----HSRAPAwLGWLASRLTGVPLvTTVHG----------------------------SYLATYHPKDFALAVRARGDRV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 257 HHVATSDHcgDVLKRIYMIPEERVHIILNGVDENVFKPDVSKREsfREKFGVRSGKnkkspLVLGIAGRLVRDKGHPLMF 336
Cdd:cd03819 131 IAVSELVR--DHLIEALGVDPERIRVIPNGVDTDRFPPEAEAEE--RAQLGLPEGK-----PVVGYVGRLSPEKGWLLLV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 337 SALkrvfEENKEAReNVVVLVAGDGP----WGNRYKDLGSTN-VIVLGPLdqEKLAGFYNAIDVFVNPTLRaQGLDHTLL 411
Cdd:cd03819 202 DAA----AELKDEP-DFRLLVAGDGPerdeIRRLVERLGLRDrVTFTGFR--EDVPAALAASDVVVLPSLH-EEFGRVAL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 412 EAMVSGKPVLATRLASITGSVVVGPHlGYTFSPN-VESLTEAILRVVsdgteeLQRKGKEARERSLRLftatkmADSYER 490
Cdd:cd03819 274 EAMACGTPVVATDVGGAREIVVHGRT-GLLVPPGdAEALADAIRAAK------LLPEAREKLQAAAAL------TEAVRE 340
|
....
gi 42568648 491 FFLC 494
Cdd:cd03819 341 LLLR 344
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
259-492 |
8.38e-27 |
|
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: 111.25 E-value: 8.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 259 VATSDHCGDVLKRIYmIPEERVHIILNGVDENVFKPDVSKRESFREKFGVrsgknKKSPLVLGIAGRLVRDKGHPLMFSA 338
Cdd:cd03807 138 VANSSAVAEFHQEQG-YAKNKIVVIYNGIDLFKLSPDDASRARARRRLGL-----AEDRRVIGIVGRLHPVKDHSDLLRA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 339 LKRVfeenKEARENVVVLVAGDGPwgnRYKDLGST--------NVIVLGPldQEKLAGFYNAIDVFVNPTlRAQGLDHTL 410
Cdd:cd03807 212 AALL----VETHPDLRLLLVGRGP---ERPNLERLllelgledRVHLLGE--RSDVPALLPAMDIFVLSS-RTEGFPNAL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 411 LEAMVSGKPVLATRLASItgSVVVGPHLGYTFSP-NVESLTEAILRVVSDgTEELQRKGKEARERSLRLFTATKMADSYE 489
Cdd:cd03807 282 LEAMACGLPVVATDVGGA--AELVDDGTGFLVPAgDPQALADAIRALLED-PEKRARLGRAARERIANEFSIDAMVRRYE 358
|
...
gi 42568648 490 RFF 492
Cdd:cd03807 359 TLY 361
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
109-490 |
5.96e-25 |
|
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: 106.21 E-value: 5.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 109 TLHLALANRGHELHVFTaasPSFPEYQ---------------LKNLMFHLSEPTAAGYLDQASVsqqlqtqnasgRPFDV 173
Cdd:cd03817 22 NLARALEKRGHEVYVIT---PSDPGAEdeeevvryrsfsipiRKYHRQHIPFPFKKAVIDRIKE-----------LGPDI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 174 IHTE---SVGLLHTR-AKNLR-NVVASWHGIAYETFHSDIIQELLRQADIAAataagteeeqpppsspalterakrvveE 248
Cdd:cd03817 88 IHTHtpfSLGKLGLRiARKLKiPIVHTYHTMYEDYLHYIPKGKLLVKAVVRK---------------------------L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 249 VKFFQRYAHHVAT-SDHCGDVLKRiYMIpEERVHIILNGVDENVFKPDVSKREsfREKFGVRSGKNkksplVLGIAGRLV 327
Cdd:cd03817 141 VRRFYNHTDAVIApSEKIKDTLRE-YGV-KGPIEVIPNGIDLDKFEKPLNTEE--RRKLGLPPDEP-----ILLYVGRLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 328 RDKGHPLMFSALKRVFEENkeareNVVVLVAGDGPWGNRYKDLGST-----NVIVLGPLDQEKLAGFYNAIDVFVNP-TL 401
Cdd:cd03817 212 KEKNIDFLLRAFAELKKEP-----NIKLVIVGDGPEREELKELARElgladKVIFTGFVPREELPEYYKAADLFVFAsTT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 402 RAQGLdhTLLEAMVSGKPVLATRLASITGSVVVGpHLGYTFSPNVESLTEAILRVVSDgTEELQRKGKEARERSLRLFTA 481
Cdd:cd03817 287 ETQGL--VYLEAMAAGLPVVAAKDPAASELVEDG-ENGFLFEPNDETLAEKLLHLREN-LELLRKLSKNAEISAREFAFA 362
|
....*....
gi 42568648 482 TKMADSYER 490
Cdd:cd03817 363 KSVEKLYEE 371
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
250-489 |
5.49e-24 |
|
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: 103.06 E-value: 5.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 250 KFFQRYAHHVAT-SDHCGDVLKRIYMIPEERVHIIL-NGVDENVFKPdvskresfrekfgvRSGKNKKSPLVLGIAGRLV 327
Cdd:cd03808 134 KLALLFTDKVIFvNEDDRDLAIKKGIIKKKKTVLIPgSGVDLDRFQY--------------SPESLPSEKVVFLFVARLL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 328 RDKGHPLMFSALKRVfeenKEARENVVVLVAGDGPWGNRYKDLGST-----NVIVLGPLDQekLAGFYNAIDVFVNPTLR 402
Cdd:cd03808 200 KDKGIDELIEAAKIL----KKKGPNVRFLLVGDGELENPSEILIEKlglegRIEFLGFRSD--VPELLAESDVFVLPSYR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 403 aQGLDHTLLEAMVSGKPVLATrlaSITG--SVVVGPHLGYTFSP-NVESLTEAILRVVSDgtEELQRK-GKEARERSLRL 478
Cdd:cd03808 274 -EGLPRSLLEAMAAGRPVITT---DVPGcrELVIDGVNGFLVPPgDVEALADAIEKLIED--PELRKEmGEAARKRVEEK 347
|
250
....*....|.
gi 42568648 479 FTATKMADSYE 489
Cdd:cd03808 348 FDEEKVVNKLL 358
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
254-489 |
2.21e-23 |
|
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: 101.29 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 254 RYAHHVAT-SDHCGDVLKRIYMIPEERVHIILNGVDENVFKPDVSKResfrekfgVRSGKNKKSPLVLgIAGRLVRDKGH 332
Cdd:cd03809 137 RRADAIITvSEATRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESAAV--------LIAKYLLPEPYFL-YVGTLEPRKNH 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 333 PLMFSALKRVFEENKeareNVVVLVAGDGPWGNRY------KDLGSTNVIVLGPLDQEKLAGFYNAIDVFVNPTLRAQ-G 405
Cdd:cd03809 208 ERLLKAFALLKKQGG----DLKLVIVGGKGWEDEElldlvkKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGfG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 406 LdhTLLEAMVSGKPVLATRLASItgSVVVGPHlGYTFSP-NVESLTEAILRVVSDGT--EELQRKGKEarerSLRLFTAT 482
Cdd:cd03809 284 L--PVLEAMACGTPVIASNISVL--PEVAGDA-ALYFDPlDPESIADAILRLLEDPSlrEELIRKGLE----RAKKFSWE 354
|
....*..
gi 42568648 483 KMADSYE 489
Cdd:cd03809 355 KTAEKTL 361
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
172-485 |
6.50e-23 |
|
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: 100.04 E-value: 6.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 172 DVIHTES----VGLLHTRAKNLRNVVASWHgiayetfhSDII-QELLRQadiaaataagteEEQPPPSSpaLTERAKRVV 246
Cdd:cd03795 85 DIIHYHFpnplADLLLFFSGAKKPVVVHWH--------SDIVkQKKLLK------------LYKPLMTR--FLRRADRII 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 247 eevkffqryahhvATSD---HCGDVLKRIymipEERVHIILNGVDENVFKPDVSKRESFREKfgvrsgkNKKSPLVLGIa 323
Cdd:cd03795 143 -------------ATSPnyvETSPTLREF----KNKVRVIPLGIDKNVYNIPRVDFENIKRE-------KKGKKIFLFI- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 324 GRLVRDKGHPLMFSALKRVfeenkeareNVVVLVAGDGPWGNRYKDL----GSTNVIVLGPLDQEKLAGFYNAIDVFVNP 399
Cdd:cd03795 198 GRLVYYKGLDYLIEAAQYL---------NYPIVIGGEGPLKPDLEAQielnLLDNVKFLGRVDDEEKVIYLHLCDVFVFP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 400 T-LRAQGLDHTLLEAMVSGKPVLATRLASITGSVVVGPHLGYTFSP-NVESLTEAILRVVSDgTEELQRKGKEARERSLR 477
Cdd:cd03795 269 SvLRSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNNGETGLVVPPkDPDALAEAIDKLLSD-EELRESYGENAKKRFEE 347
|
....*...
gi 42568648 478 LFTATKMA 485
Cdd:cd03795 348 LFTAEKMK 355
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
251-488 |
1.18e-21 |
|
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: 96.25 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 251 FFQRYAHHVATSDHCGDVLKRIYMIPEERVHIILNGVDENVFKPdVSKRESfREKFGVrsGKNKKSPLVLGIAGRLVRdK 330
Cdd:cd03825 134 LAKKRLTIVAPSRWLADMVRRSPLLKGLPVVVIPNGIDTEIFAP-VDKAKA-RKRLGI--PQDKKVILFGAESVTKPR-K 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 331 GHPLMFSALKRVfeenkEARENVVVLVAG-----DGPWGNRYKDLGSTNvivlgplDQEKLAGFYNAIDVFVNPTlRAQG 405
Cdd:cd03825 209 GFDELIEALKLL-----ATKDDLLLVVFGkndpqIVILPFDIISLGYID-------DDEQLVDIYSAADLFVHPS-LADN 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 406 LDHTLLEAMVSGKPVLATrlaSITGS--VVVGPHLGYTFSP-NVESLTEAILRVVSDGTEELQRkGKEARERSLRLFTAT 482
Cdd:cd03825 276 LPNTLLEAMACGTPVVAF---DTGGSpeIVQHGVTGYLVPPgDVQALAEAIEWLLANPKERESL-GERARALAENHFDQR 351
|
....*.
gi 42568648 483 KMADSY 488
Cdd:cd03825 352 VQAQRY 357
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
99-480 |
1.39e-21 |
|
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: 95.89 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 99 QAGGLERHALTLHLALANRGHELHVFT----AASPSFPEYQLKNLMFHLSEPTAAGYLDQASVSQQLQtqNASGRPFDVI 174
Cdd:cd03811 10 SGGGAERVLLNLANALDKRGYDVTLVLlrdeGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKR--ILKRAKPDVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 175 HTesvglLHTRAKNLRNVVASWHGIAYETFHSDIIQELLRQadiaaataagteeeqpppsspalteraKRVVEEVKFFQR 254
Cdd:cd03811 88 IS-----FLGFATYIVAKLAAARSKVIAWIHSSLSKLYYLK---------------------------KKLLLKLKLYKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 255 YAHHVATSDHCGDVLKRIYMIPEERVHIILNGVDenvfkpdvskRESFREKFGVRSGKNKKSPLVLGIAGRLVRDKGHPL 334
Cdd:cd03811 136 ADKIVCVSKGIKEDLIRLGPSPPEKIEVIYNPID----------IDRIRALAKEPILNEPEDGPVILAVGRLDPQKGHDL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 335 MFSALKRVFEENKEARenvvVLVAGDGPWGNRY----KDLGSTN-VIVLGPldQEKLAGFYNAIDVFVNPTlRAQGLDHT 409
Cdd:cd03811 206 LIEAFAKLRKKYPDVK----LVILGDGPLREELeklaKELGLAErVIFLGF--QSNPYPYLKKADLFVLSS-RYEGFPNV 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42568648 410 LLEAMVSGKPVLATRlasITGS--VVVGPHLGYTFSPNVESLTEAILRVVSDG--TEELQRKGKEARERSLRLFT 480
Cdd:cd03811 279 LLEAMALGTPVVSTD---CPGPreILDDGENGLLVPDGDAAALAGILAALLQKklDAALRERLAKAQEAVFREYT 350
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
317-474 |
4.60e-21 |
|
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: 89.64 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 317 PLVLGIAGRLVRDKGHPLMFSALKRVfeenKEARENVVVLVAGDGPWGNRYKDL-----GSTNVIVLGPLDQEKLAGFYN 391
Cdd:pfam00534 2 KKIILFVGRLEPEKGLDLLIKAFALL----KEKNPNLKLVIAGDGEEEKRLKKLaeklgLGDNVIFLGFVSDEDLPELLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 392 AIDVFVNPTLRAqGLDHTLLEAMVSGKPVLATRLASItgSVVVGPHL-GYTF-SPNVESLTEAILRVVSDGtEELQRKGK 469
Cdd:pfam00534 78 IADVFVLPSRYE-GFGIVLLEAMACGLPVIASDVGGP--PEVVKDGEtGFLVkPNNAEALAEAIDKLLEDE-ELRERLGE 153
|
....*
gi 42568648 470 EARER 474
Cdd:pfam00534 154 NARKR 158
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
86-489 |
2.66e-20 |
|
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: 92.79 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 86 KIAVVVKKWPRKSQAGGlerhALTLHLA--LANRGHELHVFTaaspSFPEYQLKNLMFHLSE--------PTAAGYLDQA 155
Cdd:cd03794 1 KILLISQYYPPPKGAAA----ARVYELAkeLVRRGHEVTVLT----PSPNYPLGRIFAGATEtkdgirviRVKLGPIKKN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 156 SVSQQLQTQN-----------ASGRPFDVIHTES----VGLLHTRAKNLRNVVASWHgiayetfhsdiIQELLRQADIAA 220
Cdd:cd03794 73 GLIRRLLNYLsfalaallkllVREERPDVIIAYSppitLGLAALLLKKLRGAPFILD-----------VRDLWPESLIAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 221 ATaagteeeqpppsspaltERAKRVVEEVKFFQRYAhhVATSDHCG-------DVLKRIYmIPEERVHIILNGVDENVFK 293
Cdd:cd03794 142 GV-----------------LKKGSLLKLLKKLERKL--YRLADAIIvlspglkEYLLRKG-VPKEKIIVIPNWADLEEFK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 294 PdvSKRESFREKFGvrsgknKKSPLVLGIAGRLvrdkGHPLMFSALKRVFEENKEaRENVVVLVAGDGPWGNRYK----D 369
Cdd:cd03794 202 P--PPKDELRKKLG------LDDKFVVVYAGNI----GKAQGLETLLEAAERLKR-RPDIRFLFVGDGDEKERLKelakA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 370 LGSTNVIVLGPLDQEKLAGFYNAIDVFVNPtLRAQGLDHT-----LLEAMVSGKPVLATRLASITGSVVVGPhLGYTFSP 444
Cdd:cd03794 269 RGLDNVTFLGRVPKEEVPELLSAADVGLVP-LKDNPANRGsspskLFEYMAAGKPILASDDGGSDLAVEING-CGLVVEP 346
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 42568648 445 -NVESLTEAILRVVSDgTEELQRKGKEARERSLRLFTATKMADSYE 489
Cdd:cd03794 347 gDPEALADAILELLDD-PELRRAMGENGRELAEEKFSREKLADRLL 391
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
317-459 |
5.24e-19 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 83.33 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 317 PLVLGIAGRLV-RDKGHPLMFSALKRVfeenKEARENVVVLVAGDGPWgNRYKDL---GSTNVIVLGPLDQekLAGFYNA 392
Cdd:pfam13692 1 RPVILFVGRLHpNVKGVDYLLEAVPLL----RKRDNDVRLVIVGDGPE-EELEELaagLEDRVIFTGFVED--LAELLAA 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42568648 393 IDVFVNPtLRAQGLDHTLLEAMVSGKPVLATRLASItGSVVVGPHlGYTFSP-NVESLTEAILRVVSD 459
Cdd:pfam13692 74 ADVFVLP-SLYEGFGLKLLEAMAAGLPVVATDVGGI-PELVDGEN-GLLVPPgDPEALAEAILRLLED 138
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
386-492 |
6.14e-17 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 76.95 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 386 LAGFYNAIDVFVNPTlRAQGLDHTLLEAMVSGKPVLATRLASItGSVVVGPHLGYTFSP-NVESLTEAILRVVSDgTEEL 464
Cdd:COG0438 14 LEALLAAADVFVLPS-RSEGFGLVLLEAMAAGLPVIATDVGGL-PEVIEDGETGLLVPPgDPEALAEAILRLLED-PELR 90
|
90 100
....*....|....*....|....*...
gi 42568648 465 QRKGKEARERSLRLFTATKMADSYERFF 492
Cdd:COG0438 91 RRLGEAARERAEERFSWEAIAERLLALY 118
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
275-490 |
6.36e-17 |
|
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: 81.99 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 275 IPEERVHIILNGVdenvfKPDVSKRESfrekfgvrsGKNKKSPLVLGIAGRLVRDKGHPLmfsaLKRVFEENKeaRENVV 354
Cdd:cd03823 163 LFSARISVIPNAV-----EPDLAPPPR---------RRPGTERLRFGYIGRLTEEKGIDL----LVEAFKRLP--REDIE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 355 VLVAGDGPWGNRYKDLGSTNVIVLGPLDQEKLAGFYNAIDVFVNPTLRAQGLDHTLLEAMVSGKPVLATRLASITGSVVV 434
Cdd:cd03823 223 LVIAGHGPLSDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPFGLVVREAIAAGLPVIASDLGGIAELIQP 302
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 42568648 435 GPHlGYTFSP-NVESLTEAILRVVSDGtEELQRKGKEARERSLRLFTATKMADSYER 490
Cdd:cd03823 303 GVN-GLLFAPgDAEDLAAAMRRLLTDP-ALLERLRAGAEPPRSTESQAEEYLKLYRD 357
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
86-477 |
1.01e-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: 81.57 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 86 KIAVVVKKWPrkSQAGGLERHALTLHLALANRGHELHVFTAASPSFPEYQLKNLMFHLSE--PTAAGY----LDQASVSQ 159
Cdd:cd03814 1 RIALVTDTYH--PQVNGVVRTLERLVDHLRRRGHEVRVVAPGPFDEAESAEGRVVSVPSFplPFYPEYrlalPLPRRVRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 160 QLQTQNasgrpFDVIH--TESV----GLLHTRAKNLRnVVASwhgiayetFHSDIIqELLRQadiaaataagteEEQPPP 233
Cdd:cd03814 79 LIKEFQ-----PDIIHiaTPGPlglaALRAARRLGLP-VVTS--------YHTDFP-EYLSY------------YTLGPL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 234 SspalteraKRVVEEVKFFQRYAHHV-ATSDHCGDVLKRIymiPEERVHIILNGVDENVFKPdvSKR-ESFREKFGVRSG 311
Cdd:cd03814 132 S--------WLAWAYLRWFHNPFDTTlVPSPSIARELEGH---GFERVRLWPRGVDTELFHP--SRRdAALRRRLGPPGR 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 312 KnkksplVLGIAGRLVRDKGhplmFSALKRVFEENKEAREnVVVLVAGDGPwgNRYK-DLGSTNVIVLGPLDQEKLAGFY 390
Cdd:cd03814 199 P------LLLYVGRLAPEKN----LEALLDADLPLAASPP-VRLVVVGDGP--ARAElEARGPDVIFTGFLTGEELARAY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 391 NAIDVFVNP----TLraqGLdhTLLEAMVSGKPVLATRlASITGSVVVGPHLGYTFSP-NVESLTEAILRVVSDGtEELQ 465
Cdd:cd03814 266 ASADVFVFPsrteTF---GL--VVLEAMASGLPVVAAD-AGGPRDIVRPGGTGALVEPgDAAAFAAALRALLEDP-ELRR 338
|
410
....*....|..
gi 42568648 466 RKGKEARERSLR 477
Cdd:cd03814 339 RMAARARAEAER 350
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
250-432 |
1.22e-15 |
|
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: 78.10 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 250 KFFQRYA-HHVATSDHCGDVLkrIYMIPEERVHIILNGVDENVFKPDVSKRESFREKfgvrsgKNKKSPLVLGIAGRLVR 328
Cdd:cd03812 131 KLIERLStKYLACSEDAGEWL--FGEVENGKFKVIPNGIDIEKYKFNKEKRRKRRKL------LILEDKLVLGHVGRFNE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 329 DKGHPLMFsalkRVFEENKEARENVVVLVAGDGPWGNRYKDLGS-----TNVIVLGplDQEKLAGFYNAIDVFVNPTLrA 403
Cdd:cd03812 203 QKNHSFLI----DIFEELKKKNPNVKLVLVGEGELKEKIKEKVKelgleDKVIFLG--FRNDVSEILSAMDVFLFPSL-Y 275
|
170 180 190
....*....|....*....|....*....|...
gi 42568648 404 QGLDHTLLEAMVSGKPVLA----TRLASITGSV 432
Cdd:cd03812 276 EGLPLVAVEAQASGLPCLLsdtiTKECDITNNV 308
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
323-437 |
6.22e-15 |
|
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: 74.36 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 323 AGRLVRDKGHPLMFSALKRVFEEnkeaRENVVVLVAGDGPWGNRYK------DLGSTNVIVLGPLDQEKLAGFYNAIDVF 396
Cdd:cd01635 116 VGRLVPEKGIDLLLEALALLKAR----LPDLVLVLVGGGGEREEEEalaaalGLLERVVIIGGLVDDEVLELLLAAADVF 191
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 42568648 397 VNPTlRAQGLDHTLLEAMVSGKPVLATRLASITGSVVVGPH 437
Cdd:cd01635 192 VLPS-RSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGEN 231
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
86-489 |
2.26e-14 |
|
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: 74.71 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 86 KIAVVVkkWPRKSQAGGLERHALTLHLALANRGHELHVFTAASPSfpEYQLKNLMFHLSEPTAAGYLDQASVSQQLQTQN 165
Cdd:cd03821 1 KILHVT--PSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGDGY--ESLVVEENGRYIPPQDGFASIPLLRQGAGRTDF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 166 ASG---------RPFDVIHTESVGLLHTRAknlrnvVASWH---GIAY-ETFHSDIIQELLRQADIAAATAAGTEEEQPP 232
Cdd:cd03821 77 SPGlpnwlrrnlREYDVVHIHGVWTYTSLA------ACKLArrrGIPYvVSPHGMLDPWALQQKHWKKRIALHLIERRNL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 233 PSSPALTERAKRVVEEVKFFQryahhvatsdhcgdvlkriymiPEERVHIILNGVDENVFKPdvskRESFREKFGVRSGK 312
Cdd:cd03821 151 NNAALVHFTSEQEADELRRFG----------------------LEPPIAVIPNGVDIPEFDP----GLRDRRKHNGLEDR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 313 nkksPLVLgIAGRLVRDKGHPLMFSALKRVfeenKEARENVVVLVAGDGPWGNRYKD------LGSTNVIVLGPLDQEKL 386
Cdd:cd03821 205 ----RIIL-FLGRIHPKKGLDLLIRAARKL----AEQGRDWHLVIAGPDDGAYPAFLqlqsslGLGDRVTFTGPLYGEAK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 387 AGFYNAIDVFVNPTlRAQGLDHTLLEAMVSGKPVLATRLASITGSVVVGphLGYTFSPNVESLTEAILRVVSDGTEElQR 466
Cdd:cd03821 276 WALYASADLFVLPS-YSENFGNVVAEALACGLPVVITDKCGLSELVEAG--CGVVVDPNVSSLAEALAEALRDPADR-KR 351
|
410 420
....*....|....*....|....*
gi 42568648 467 KGKEARE--RSLRLFTATKMADSYE 489
Cdd:cd03821 352 LGEMARRarQVEENFSWEAVAGQLG 376
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
276-493 |
2.69e-14 |
|
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: 75.06 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 276 PEERVHIILNGVDENVFKPDVSKREsfrekfgvrsgknKKSPLVLGIAGRLVRDKGHPLMFSALKRVFEENKEARENVVV 355
Cdd:cd03813 265 DPDKTRVIPNGIDIQRFAPAREERP-------------EKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIG 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 356 LVAGDGPWGNRYKDLgstnVIVLGPLDQEKLAGFYNAIDVF-----VNPTLRAQGLDHTLLEAMVSGKPVLATRLAS--- 427
Cdd:cd03813 332 PEDEDPEYAQECKRL----VASLGLENKVKFLGFQNIKEYYpklglLVLTSISEGQPLVILEAMASGVPVVATDVGScre 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42568648 428 -ITGSVVVGPHLGYTFSP-NVESLTEAILRVVSDgTEELQRKGKEARERSLRLFTATKMADSYERFFL 493
Cdd:cd03813 408 lIYGADDALGQAGLVVPPaDPEALAEALIKLLRD-PELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
231-489 |
3.61e-14 |
|
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: 74.03 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 231 PPPSSPALTERAKRvveevkffQRYAHHVATSDHCGDVLKRIyMIPEERVHIILNGVDENVFKP-DVSKREsfrekfgvr 309
Cdd:cd05844 128 GWPSQFQRHRRALQ--------RPAALFVAVSGFIRDRLLAR-GLPAERIHVHYIGIDPAKFAPrDPAERA--------- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 310 sgknkksPLVLgIAGRLVRDKGHPLMFSALKRVFEENKEARenvvVLVAGDGPWGNRYKDL--GSTNVIVLGPLDQEKLA 387
Cdd:cd05844 190 -------PTIL-FVGRLVEKKGCDVLIEAFRRLAARHPTAR----LVIAGDGPLRPALQALaaALGRVRFLGALPHAEVQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 388 GFYNAIDVFVNPTL-----RAQGLDHTLLEAMVSGKPVLATRLASITGSVVVGpHLGYTFSP-NVESLTEAILRVVSDGT 461
Cdd:cd05844 258 DWMRRAEIFCLPSVtaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDG-ETGFLVPEgDVDALADALQALLADRA 336
|
250 260
....*....|....*....|....*...
gi 42568648 462 EElQRKGKEARERSLRLFTATKMADSYE 489
Cdd:cd05844 337 LA-DRMGGAARAFVCEQFDIRVQTAKLE 363
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
249-473 |
4.03e-14 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 74.36 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 249 VKFFQRYAH-HVATSDHCGDVLKRIYMIPEERVHIILNGVDENVFKPDVsKRESFREKFgvrSGKNKKSPLVLGIaGRLV 327
Cdd:PLN02871 199 IRFLHRAADlTLVTSPALGKELEAAGVTAANRIRVWNKGVDSESFHPRF-RSEEMRARL---SGGEPEKPLIVYV-GRLG 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 328 RDKGhplmFSALKRVFEENKEARENVVvlvaGDGPWGNRYKDLGS-TNVIVLGPLDQEKLAGFYNAIDVFVNPTlRAQGL 406
Cdd:PLN02871 274 AEKN----LDFLKRVMERLPGARLAFV----GDGPYREELEKMFAgTPTVFTGMLQGDELSQAYASGDVFVMPS-ESETL 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42568648 407 DHTLLEAMVSGKPVLATRLASITGSV--VVGPHLGYTFSP-NVE---SLTEAILrvvsDGTEELQRKGKEARE 473
Cdd:PLN02871 345 GFVVLEAMASGVPVVAARAGGIPDIIppDQEGKTGFLYTPgDVDdcvEKLETLL----ADPELRERMGAAARE 413
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
283-493 |
3.66e-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: 70.94 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 283 ILNGVDENVFKPDVSKRESFREKFGVrsgknKKSPLVLGIAGRLVRDKGHPLMFSALKrvfeENKEARENVVVLVAGDGP 362
Cdd:cd04951 159 VYNGIDLNKFKKDINVRLKIRNKLNL-----KNDEFVILNVGRLTEAKDYPNLLLAIS----ELILSKNDFKLLIAGDGP 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 363 WGNRYKDLG-----STNVIVLGPLDQekLAGFYNAIDVFVNPTlRAQGLDHTLLEAMVSGKPVLATRlasiTGSV--VVG 435
Cdd:cd04951 230 LRNELERLIcnlnlVDRVILLGQISN--ISEYYNAADLFVLSS-EWEGFGLVVAEAMACERPVVATD----AGGVaeVVG 302
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 42568648 436 PHLGYTFSPNVESLTEAILRVVSDGTEELQRKGKEaRERSLRLFTATKMADSYERFFL 493
Cdd:cd04951 303 DHNYVVPVSDPQLLAEKIKEIFDMSDEERDILGNK-NEYIAKNFSINTIVNEWERLYS 359
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
101-288 |
7.65e-13 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 66.40 E-value: 7.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 101 GGLERHALTLHLALANRGHELHVFTAASPSFPEYQLKNL-----MFHLSEPTAAGYLDQASVSQQLQTQNasgrPFDVIH 175
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVvrvprVPLPLPPRLLRSLAFLRRLRRLLRRE----RPDVVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 176 TES-----VGLLHTRAKNLRNVVASWHGIAYETFHSDIIQELLRQADIAAataagteeeqpppsspalterakrvveEVK 250
Cdd:pfam13439 77 AHSpfplgLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRRL---------------------------ERR 129
|
170 180 190
....*....|....*....|....*....|....*...
gi 42568648 251 FFQRYAHHVATSDHCGDVLKRIYMIPEERVHIILNGVD 288
Cdd:pfam13439 130 LLRRADRVIAVSEAVADELRRLYGVPPEKIRVIPNGVD 167
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
269-472 |
5.18e-11 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 64.43 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 269 LKRIY--MIPEERVHIILNGVDENVFKPDvsKRESFREKFGVRSGKNkksplVLGIAGRLVRDKGHPLMFSAlkrvFEEN 346
Cdd:PRK15484 150 LKKFYeeRLPNADISIVPNGFCLETYQSN--PQPNLRQQLNISPDET-----VLLYAGRISPDKGILLLMQA----FEKL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 347 KEARENVVVLVAGD---------GPWGNRYKDLGS---TNVIVLGPLDQEKLAGFYNAIDVFVNPTLRAQGLDHTLLEAM 414
Cdd:PRK15484 219 ATAHSNLKLVVVGDptasskgekAAYQKKVLEAAKrigDRCIMLGGQPPEKMHNYYPLADLVVVPSQVEEAFCMVAVEAM 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42568648 415 VSGKPVLATRLASITGSV---VVGPHLGYTFSPnvESLTEAILRVVSDgtEELQRKGKEAR 472
Cdd:PRK15484 299 AAGKPVLASTKGGITEFVlegITGYHLAEPMTS--DSIISDINRTLAD--PELTQIAEQAK 355
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
107-492 |
1.04e-10 |
|
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: 63.14 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 107 ALTLHLALANRGHELHVFTAASPSFPEYQLKNLMFHlsEPTAAGYldqASVSQQLQTQNASGRPFDVIHTESVGLLHTRA 186
Cdd:cd04962 18 ATELGLELAERGHEVHFISSAIPFRLNLYSGNIFFH--EVEVPNY---PLFEYPPYTLALASKIVEVAKEHKLDVLHAHY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 187 KnLRNVVASWHgiAYETFHSDI-IQELLRQADIaaataagTEEEQPPPSSPALT---ERAKRVVEEVKFFQRYAHHVATs 262
Cdd:cd04962 93 A-IPHASCAYL--AREILGEKIpIVTTLHGTDI-------TLVGYDPSLQPAVRfsiNKSDRVTAVSSSLRQETYELFD- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 263 dhcgdvlkriymiPEERVHIILNGVDENVFKPDvSKRESFREKFGVRSGKnkkspLVLGIAGrlvrdkghplmFSALKR- 341
Cdd:cd04962 162 -------------VDKDIEVIHNFIDEDVFKRK-PAGALKRRLLAPPDEK-----VVIHVSN-----------FRPVKRi 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 342 -----VFEENKEaRENVVVLVAGDGP----WGNRYKDLGSTN-VIVLGplDQEKLAGFYNAIDVFVNPTLRAQ-GLdhTL 410
Cdd:cd04962 212 ddvvrVFARVRR-KIPAKLLLVGDGPervpAEELARELGVEDrVLFLG--KQDDVEELLSIADLFLLPSEKESfGL--AA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 411 LEAMVSGKPVLATRLASITgSVVVGPHLGYTFSP-NVESLTEAILRVVSDGtEELQRKGKEARERSLRLFTATKMADSYE 489
Cdd:cd04962 287 LEAMACGVPVVSSNAGGIP-EVVKHGETGFLSDVgDVDAMAKSALSILEDD-ELYNRMGRAARKRAAERFDPERIVPQYE 364
|
...
gi 42568648 490 RFF 492
Cdd:cd04962 365 AYY 367
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
100-477 |
2.05e-10 |
|
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: 62.25 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 100 AGGLERHALTLHLALANRGHELHVFTAASPSFPEY-------QLKNLmFHLSEPTAAGYLDQASVSQQLQTQNASGRPfD 172
Cdd:cd03820 12 AGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFyelddniKIKNL-GDRKYSHFKLLLKYFKKVRRLRKYLKNNKP-D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 173 VI---HTESVGLLHTRAKNLRnVVASWHgIAYETFHSDIIQELLRQ-----ADIAAataagteeeqpppsspALTERakr 244
Cdd:cd03820 90 VVisfRTSLLTFLALIGLKSK-LIVWEH-NNYEAYNKGLRRLLLRRllykrADKIV----------------VLTEA--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 245 vvEEVKFFQRYahhvatsdhcgdvLKRIYMIPeervhiilngvdeNvFKPDVSKRESFrekfgvrsgkNKKSPLVLGIaG 324
Cdd:cd03820 149 --DKLKKYKQP-------------NSNVVVIP-------------N-PLSFPSEEPST----------NLKSKRILAV-G 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 325 RLVRDKGHPLMFSALKRVFEENKEARenvvVLVAGDGPWG----NRYKDLGSTNVIVLGPLDQEkLAGFYNAIDVFVNPT 400
Cdd:cd03820 189 RLTYQKGFDLLIEAWALIAKKHPDWK----LRIYGDGPEReeleKLIDKLGLEDRVKLLGPTKN-IAEEYANSSIFVLSS 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 401 lRAQGLDHTLLEAMVSGKPVLA----TRLASIT-----GsVVVGPHlgytfspNVESLTEAILRVVSDgtEELQRK-GKE 470
Cdd:cd03820 264 -RYEGFPMVLLEAMAYGLPIISfdcpTGPSEIIedgenG-LLVPNG-------DVDALAEALLRLMED--EELRKKmGKN 332
|
....*..
gi 42568648 471 ARERSLR 477
Cdd:cd03820 333 ARKNAER 339
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
269-492 |
8.44e-10 |
|
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: 60.48 E-value: 8.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 269 LKRIYMIPEERVHIILNGVdenvfkPDVSKRESFREK--FGVrsgknkKSPLVLGIAGRLVRDKGHPLMFSALKRVFEEN 346
Cdd:cd03822 149 LVRIKLIPAVNIEVIPHGV------PEVPQDPTTALKrlLLP------EGKKVILTFGFIGPGKGLEILLEALPELKAEF 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 347 KEARenvVVLVAGDGP-----WGNRYKD-----LGSTNVI--VLGPLDQEKLAGFYNAIDVFVNPTL-RAQGLDHTLLEA 413
Cdd:cd03822 217 PDVR---LVIAGELHPslaryEGERYRKaaieeLGLQDHVdfHNNFLPEEEVPRYISAADVVVLPYLnTEQSSSGTLSYA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 414 MVSGKPVLATRLAS-----ITGSVVVGPHlgytfsPNVESLTEAILRVVSDgtEELQRKGKEARERSLRLFTATKMADSY 488
Cdd:cd03822 294 IACGKPVISTPLRHaeellADGRGVLVPF------DDPSAIAEAILRLLED--DERRQAIAERAYAYARAMTWESIADRY 365
|
....
gi 42568648 489 ERFF 492
Cdd:cd03822 366 LRLF 369
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
252-455 |
3.01e-06 |
|
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.
Pssm-ID: 340833 [Multi-domain] Cd Length: 356 Bit Score: 49.21 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 252 FQRYAHHVATSDHCGDVLKRIYMIPEErvhIILNGVDENVFKPDVSKRESFRekfgvrsgknkksplvlgIAGRLVRDKG 331
Cdd:cd03804 155 AQRVDLFIANSQFVARRIKKFYGREST---VIYPPVDTDAFAPAADKEDYYL------------------TASRLVPYKR 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 332 HPLMFSALkrvfeeNKEARENVVVlvaGDGPWGNRYKDLGSTNVIVLGPLDQEKLAGFYNAIDVFVNPTLRAQGLdhTLL 411
Cdd:cd03804 214 IDLAVEAF------NELPKRLVVI---GDGPDLDRLRAMASPNVEFLGYQPDEVLKELLSKARAFVFAAEEDFGI--VPV 282
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 42568648 412 EAMVSGKPVLATRLASITGSVVVGPhLGYTFS-PNVESLTEAILR 455
Cdd:cd03804 283 EAQACGTPVIAFGKGGALETVRPGP-TGILFGeQTVESLKAAVEE 326
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
86-490 |
1.03e-05 |
|
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: 47.67 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 86 KIAVVVK-KWPRKSQ-AGGLERHALTLHLALANRGHELHVFtAASPSFPeyQLKnlmfHLSEPTAAGYLDQASVSQQLQT 163
Cdd:cd03802 1 RIAQVSPpRGPVPPGkYGGTELVVSALTEGLVRRGHEVTLF-APGDSHT--SAP----LVAVIPRALRLDPIPQESKLAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 164 QNASGR------PFDVIHtesvgllhtraknlrnvvaswhgiayetFHSDIiqellrqadiaaataaGTEEEQPPPSSPA 237
Cdd:cd03802 74 LLEALEvqlrasDFDVIH----------------------------NHSYD----------------WLPPFAPLIGTPF 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 238 LTE---RAKRVVEEVKFFQRYAHHVATSDHcgdvlKRIYMIPEERVHIILNGVDENVFKPDVSKREsfrekfgvrsgknk 314
Cdd:cd03802 110 VTTlhgPSIPPSLAIYAAEPPVNYVSISDA-----QRAATPPIDYLTVVHNGLDPADYRFQPDPED-------------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 315 ksplVLGIAGRLVRDKGHPLMFSALKRVfeenkeareNVVVLVAGDGPWGNRYKDLGS----TNVIVLGPLD-QEKLAGF 389
Cdd:cd03802 171 ----YLAFLGRIAPEKGLEDAIRVARRA---------GLPLKIAGKVRDEDYFYYLQEplpgPRIEFIGEVGhDEKQELL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 390 YNAIDVFVNPTLR-AQGLdhTLLEAMVSGKPVLATRLasitGSV--VVGPHL-GYtFSPNVESLTEAILRVvsdgtEELQ 465
Cdd:cd03802 238 GGARALLFPINWDePFGL--VMIEAMACGTPVIAYRR----GGLpeVIQHGEtGF-LVDSVEEMAEAIANI-----DRID 305
|
410 420
....*....|....*....|....*
gi 42568648 466 RkgKEARERSLRLFTATKMADSYER 490
Cdd:cd03802 306 R--AACRRYAEDRFSAARMADRYEA 328
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
324-474 |
1.98e-05 |
|
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: 46.67 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 324 GRLVRDKGHPLMFSALKRVFEENKEARENVVvlvaGDGPWGNRYKDL-----GSTNVIVLGPLDQEKLAGFYNAIDVFVN 398
Cdd:cd03799 181 GRLTEKKGLEYAIEAVAKLAQKYPNIEYQII----GDGDLKEQLQQLiqelnIGDCVKLLGWKPQEEIIEILDEADIFIA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 399 PTLRAQ-----GLDHTLLEAMVSGKPVLATRLASITGSVVVGPHLGYTFSPNVESLTEAILRVVSdGTEELQRKGKEARE 473
Cdd:cd03799 257 PSVTAAdgdqdGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIE-HPAIWPEMGKAGRA 335
|
.
gi 42568648 474 R 474
Cdd:cd03799 336 R 336
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
283-490 |
4.20e-05 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 46.02 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 283 ILNGVDENVFKPDVSKRESFREKFGVRSGK--NKKS-------------PLvLGIAGRLVRDKGHPLMFSALKRVFEENk 347
Cdd:cd03791 246 ILNGIDYDEWNPATDKLIPANYSANDLEGKaeNKAAlqkelglpvdpdaPL-FGFVGRLTEQKGVDLILDALPELLEEG- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 348 eARenVVVLVAGDGPWGNRYKDLGSTN----VIVLGPLdqEKLAGF-YNAIDVFVNPTL-RAQGLdhTLLEAMVSGKPVL 421
Cdd:cd03791 324 -GQ--LVVLGSGDPEYEQAFRELAERYpgkvAVVIGFD--EALAHRiYAGADFFLMPSRfEPCGL--VQMYAMRYGTLPI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 422 ATRlasiTG----SVVVGPHL-----GYTF-SPNVESLTEAILRVVS-----DGTEELQRKGKEARerslrlFTATKMAD 486
Cdd:cd03791 397 VRR----TGgladTVFDYDPEtgegtGFVFeDYDAEALLAALRRALAlyrnpELWRKLQKNAMKQD------FSWDKSAK 466
|
....
gi 42568648 487 SYER 490
Cdd:cd03791 467 EYLE 470
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
275-492 |
4.86e-05 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 46.18 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 275 IPEERVHIILNGVdenvfkPDVSKRES--FREKFGVRSGKNKKSPLVLGIAGRLVRDKGHPLMFSALKRVFEENKEARen 352
Cdd:PRK15179 479 VDERRIPVVYNGL------APLKSVQDdaCTAMMAQFDARTSDARFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVR-- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 353 vvVLVAGDGPWGNRY----KDLGSTNVIVLGPLDQeKLAGFYNAIDVFVNPTlRAQGLDHTLLEAMVSGKPVLATrLASI 428
Cdd:PRK15179 551 --FIMVGGGPLLESVrefaQRLGMGERILFTGLSR-RVGYWLTQFNAFLLLS-RFEGLPNVLIEAQFSGVPVVTT-LAGG 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42568648 429 TGSVVVGPHLGYTF-SPNVES--LTEAILRVVSD--GTEELQRKgkeARERSLRLFTATKMADSYERFF 492
Cdd:PRK15179 626 AGEAVQEGVTGLTLpADTVTApdVAEALARIHDMcaADPGIARK---AADWASARFSLNQMIASTVRCY 691
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
411-487 |
5.40e-05 |
|
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: 45.66 E-value: 5.40e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42568648 411 LEAMVSGKPVLATRLASITGSVVVGpHLGYTFSPNVESLTEAILRVVSDGtEELQRKGKEARERSLRLFTATKMADS 487
Cdd:cd03805 317 LEAMYAGKPVIACNSGGPLETVVEG-VTGFLCEPTPEAFAEAMLKLANDP-DLADRMGAAGRKRVKEKFSREAFAER 391
|
|
| GT20_TPS |
cd03788 |
trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a ... |
251-477 |
5.48e-05 |
|
trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a glycosyltransferase that catalyses the synthesis of alpha,alpha-1,1-trehalose-6-phosphate from glucose-6-phosphate using a UDP-glucose donor. It is a key enzyme in the trehalose synthesis pathway. Trehalose is a nonreducing disaccharide present in a wide variety of organisms and may serve as a source of energy and carbon. It is characterized most notably in insect, plant, and microbial cells. Its production is often associated with a variety of stress conditions, including desiccation, dehydration, heat, cold, and oxidation. This family represents the catalytic domain of the TPS. Some members of this domain family coexist with a C-terminal trehalose phosphatase domain.
Pssm-ID: 340820 [Multi-domain] Cd Length: 463 Bit Score: 45.66 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 251 FFQRYAHHVATSdhCGDVLK----------------RIYMIPeerVHIILNGVDENVFKPDVSKR-ESFREKFgvrsgKN 313
Cdd:cd03788 197 QTFEYARHFLSC--CSRLLGlettsaggveyggrrvRVGAFP---IGIDPDRFRRLAASPEVQERaRELRERY-----KG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 314 KKspLVLGIaGRLVRDKGHPLMFSALKRVFEENKEARENVV-VLVA----GDGPWGNRYK---------------DLGST 373
Cdd:cd03788 267 KK--LIVGV-DRLDYTKGIPEKLLAFERFLERYPEWRGKVVlVQVAvpsrTDVEEYQELRreveelvgringrfgTLDWT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 374 NVIVL-GPLDQEKLAGFYNAIDVF-VNPTlrAQGLDHTLLEAMVS---GKPVL--------ATRLasiTGSVVVGPHlgy 440
Cdd:cd03788 344 PVVYLhQSLDREELLALYRAADVAlVTSL--RDGMNLVAKEYVACqrdNPGVLilsefagaASEL---DGAILVNPW--- 415
|
250 260 270
....*....|....*....|....*....|....*..
gi 42568648 441 tfspNVESLTEAILRVVSDGTEElqrkgKEARERSLR 477
Cdd:cd03788 416 ----DIEEVAEAINRALTMSPEE-----RKERHQKLR 443
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
101-202 |
1.64e-04 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 42.00 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 101 GGLERHALTLHLALANRGHELHVFTAASP--SFPEYQLKNLMFHLSEPTAAGYLDQASVSQQLQTQNASGRPfDVIHTES 178
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPpgRPELVGDGVRVHRLPVPPRPSPLADLAALRRLRRLLRAERP-DVVHAHS 79
|
90 100
....*....|....*....|....*...
gi 42568648 179 --VGLLHTRAKNLRNV--VASWHGIAYE 202
Cdd:pfam13579 80 ptAGLAARLARRRRGVplVVTVHGLALD 107
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
317-488 |
2.47e-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: 40.00 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 317 PLVLGIAgRLVRDKGHPLMFSALKRVfeenKEARENVVVLVAG----DGPWGN-------RYKDL-GSTNVIVLGPLDQE 384
Cdd:cd03792 198 PYILQVA-RFDPSKDPLGVIDAYKLF----KRRAEEPQLVICGhgavDDPEGSvvyeevmEYAGDdHDIHVLRLPPSDQE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 385 kLAGFYNAIDVFVNPTLRaQGLDHTLLEAMVSGKPVLATRLASITGSVVVGpHLGYTFSPnVESLTEAILRVVSDgtEEL 464
Cdd:cd03792 273 -INALQRAATVVLQLSTR-EGFGLTVSEALWKGKPVIATPAGGIPLQVIDG-ETGFLVNS-VEGAAVRILRLLTD--PEL 346
|
170 180
....*....|....*....|....*
gi 42568648 465 QRK-GKEARERSLRLFTATKMADSY 488
Cdd:cd03792 347 RRKmGLAAREHVRDNFLITGNLRAW 371
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
283-360 |
2.66e-03 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 40.08 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 283 ILNGVDENVFKP-------------DVSKR----ESFREKFGVRSGKNKksPLVlGIAGRLVRDKGHPLMFSALKRVFEE 345
Cdd:COG0297 247 ILNGIDYDVWNPatdpylpanysadDLEGKaankAALQEELGLPVDPDA--PLI-GMVSRLTEQKGLDLLLEALDELLEE 323
|
90
....*....|....*
gi 42568648 346 NkeAreNVVVLVAGD 360
Cdd:COG0297 324 D--V--QLVVLGSGD 334
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
395-486 |
3.12e-03 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 36.81 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 395 VFVNPTLRAQGLDHTLLEAMVSGKPVLATRLASITGSVVVGPHLgyTFSPNVESLTEAILRVVSDgTEELQRKGKEARER 474
Cdd:pfam13524 1 IVLNPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEI--LLYRDPEELAEKIRYLLEH-PEERRAIAAAGRER 77
|
90
....*....|..
gi 42568648 475 SLRLFTATKMAD 486
Cdd:pfam13524 78 VLAEHTYAHRAE 89
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
279-488 |
8.45e-03 |
|
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: 38.50 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 279 RVHIILNGVDENVFKPDvskRESFREKFGVRSGKnKKSPLVLGIAGRLVRDKGHPLMFSALKRVFEENKEARenvVVLVA 358
Cdd:cd03818 180 RISVIHDGVDTDRLAPD---PAARLRLLNGTELK-AGDPVITYVARNLEPYRGFHVFMRALPRIQARRPDAR---VVVVG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568648 359 GDG-PWGNRYKDLGS-------------TNVIVLGPLDQEKLAGFYNAIDVFVNPTlRAQGLDHTLLEAMVSGKPVLATR 424
Cdd:cd03818 253 GDGvSYGSPPPDGGSwkqkmlaelgvdlERVHFVGKVPYDQYVRLLQLSDAHVYLT-YPFVLSWSLLEAMACGCPVIGSD 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42568648 425 LASI--------TGSVVvgphlGYtFSPnvESLTEAILRVVSDgTEELQRKGKEARERSLRLFTATKMADSY 488
Cdd:cd03818 332 TAPVrevirdgrNGLLV-----DF-FDP--DALAAAVLELLED-PDRAAALRRAARRTVERSDSLDVCLARY 394
|
|
| |
