|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
5-360 |
3.05e-83 |
|
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: 258.02 E-value: 3.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 5 RILFVIDSLRVGGAETLLLD-LLDAAKARGDLAHVAYFTPGPLAPEVEKRGIATTRLSRKGLRDPLALWRIWQLMRRWQP 83
Cdd:cd03807 1 KVAHVITGLNVGGAETMLLRlLEHMDKSRFEHVVISLTGDGVLGEELLAAGVPVVCLGLSSGKDPGVLLRLAKLIRKRNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 84 DVVHSHLTKSDLVAQLAARMRGLPRLV-TLHNAAPW-RKKRLPARLYHWVVGKPDALIAVTPLVADHVARYGgVPRENIE 161
Cdd:cd03807 81 DVVHTWMYHADLIGGLAAKLAGGVKVIwSVRSSNIPqRLTRLVRKLCLLLSKFSPATVANSSAVAEFHQEQG-YAKNKIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 162 VIQNGVDLSRFSPENATPLDLSQ-FGVPKDAVVIAKVGRLNVQKDHANFLRAAAILARKDPRAHFLVVGDGELMTQSQEL 240
Cdd:cd03807 160 VIYNGIDLFKLSPDDASRARARRrLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 241 ARQLGLGpDRLTFTGNIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGeNGMLVPASDPA 320
Cdd:cd03807 240 LLELGLE-DRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPAGDPQ 317
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 960397608 321 ALAAAGGMLVSDADLRHRIGAAGQDTVRARFSGKAMTDRI 360
Cdd:cd03807 318 ALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRY 357
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
5-361 |
1.68e-71 |
|
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: 227.86 E-value: 1.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 5 RILFVIdsLRVGGAETLLLDLLDAAKARGDLAHVAYFTPGPLAPEVEKRGIA--TTRLSRKG---LRDPLALWRIWQLMR 79
Cdd:cd03808 1 KILFIV--NVDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKELGVKviDIPILRRGinpLKDLKALFKLYKLLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 80 RWQPDVVHSHLTKSDLVAQLAARMRGLPRLV-TLH-----NAAPWRKKRLPARLYHWVVGKPDALIAVTPLVADHVARYG 153
Cdd:cd03808 79 KEKPDIVHCHTPKPGILGRLAARLAGVPKVIyTVHglgfvFTEGKLLRLLYLLLEKLALLFTDKVIFVNEDDRDLAIKKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 154 GVPRENIEVIQ-NGVDLSRFSPenatpldlSQFGVPKDAVVIAKVGRLNVQKDHANFLRAAAILARKDPRAHFLVVGDGE 232
Cdd:cd03808 159 IIKKKKTVLIPgSGVDLDRFQY--------SPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 233 LMTQSQELARQLGLGpDRLTFTGNIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGM 312
Cdd:cd03808 231 LENPSEILIEKLGLE-GRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGF 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 960397608 313 LVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFSGKAMTDRIW 361
Cdd:cd03808 310 LVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
5-352 |
3.65e-68 |
|
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: 218.77 E-value: 3.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 5 RILFVIDSLRVGGAETLLLDLLDAAKARGDLAHVAYFTPG-----PLAPEVEKRGIATTRLSRKGLRDPLALWRIWQLMR 79
Cdd:cd03811 1 KILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVLLRDEgdldkQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRILK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 80 RWQPDVVHSHLTKSDLVAQLAARmRGLPRLVTLHNAAPWRKKRLPARLYHWVVGKP-DALIAVTPLVADHVARYGGVPRE 158
Cdd:cd03811 81 RAKPDVVISFLGFATYIVAKLAA-ARSKVIAWIHSSLSKLYYLKKKLLLKLKLYKKaDKIVCVSKGIKEDLIRLGPSPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 159 NIEVIQNGVDLSRFSPENATPLDLSQFGVPkdaVVIAkVGRLNVQKDHANFLRAAAILARKDPRAHFLVVGDGELMTQSQ 238
Cdd:cd03811 160 KIEVIYNPIDIDRIRALAKEPILNEPEDGP---VILA-VGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 239 ELARQLGLGpDRLTFTGNIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLVPASD 318
Cdd:cd03811 236 KLAKELGLA-ERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGD 314
|
330 340 350
....*....|....*....|....*....|....*..
gi 960397608 319 PAALAAAGGML---VSDADLRhRIGAAGQDTVRARFS 352
Cdd:cd03811 315 AAALAGILAALlqkKLDAALR-ERLAKAQEAVFREYT 350
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
5-360 |
8.13e-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: 218.56 E-value: 8.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 5 RILFVIDSL--RVGGAETLLLDLLDAAKARGDLAHVAYFTPGPLAPEVEKRGIATTRLSRKGLRDPL--ALWRIWQLMRR 80
Cdd:cd03801 1 KILLLSPELppPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRArrLLRELRPLLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 81 WQPDVVHSHLTKSDLVAQLAARMRGLPRLVTLHNAAPWRKKRLPARLYHWV------VGKPDALIAVTPLVADHVARYGG 154
Cdd:cd03801 81 RKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLaraealLRRADAVIAVSEALRDELRALGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 155 VPRENIEVIQNGVDLSRFSPENATPldlsqFGVPKDAVVIAKVGRLNVQKDHANFLRAAAILARKDPRAHFLVVG-DGEL 233
Cdd:cd03801 161 IPPEKIVVIPNGVDLERFSPPLRRK-----LGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGgDGPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 234 MtqsQELARQLGLGPDRLTFTGNI--RQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENG 311
Cdd:cd03801 236 R---AELEELELGLGDRVRFLGFVpdEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGG 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 960397608 312 MLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFSGKAMTDRI 360
Cdd:cd03801 313 LVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERL 361
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
6-350 |
1.29e-64 |
|
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: 209.52 E-value: 1.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 6 ILFVIDSLRVGGAETLLLDLLDAAKARGdlaHVAYF--TPGPLAPEVEKRGIATTRLSRKGLRDPLALWRIWQLMRRWQP 83
Cdd:cd03819 1 ILMLTPALEIGGAETYILDLARALAERG---HRVLVvtAGGPLLPRLRQIGIGLPGLKVPLLRALLGNVRLARLIRRERI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 84 DVVHSHLTKSDLVAQLAARMRGLPRLVTLHNAAPWRKkrLPARLYHWVVGKPDALIAVTPLVADHVARYGGVPRENIEVI 163
Cdd:cd03819 78 DLIHAHSRAPAWLGWLASRLTGVPLVTTVHGSYLATY--HPKDFALAVRARGDRVIAVSELVRDHLIEALGVDPERIRVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 164 QNGVDLSRFSPENATPlDLSQFGVPKDAVVIAKVGRLNVQKDHANFLRAAAILaRKDPRAHFLVVGDGELMTQSQELARQ 243
Cdd:cd03819 156 PNGVDTDRFPPEAEAE-ERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAGDGPERDEIRRLVER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 244 LGLGpDRLTFTGNIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLVPASDPAALA 323
Cdd:cd03819 234 LGLR-DRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALA 312
|
330 340
....*....|....*....|....*..
gi 960397608 324 AAGGMLVSDADLRHRIGAAGQDTVRAR 350
Cdd:cd03819 313 DAIRAAKLLPEAREKLQAAAALTEAVR 339
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
65-360 |
1.89e-58 |
|
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: 194.52 E-value: 1.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 65 LRDPLALWRIWQLM---RRWQPDVVHSHLTKSD-LVAQLAARMRGLPRLVTLH--NAAPWRKKRLPARLYHWVVGKPDAL 138
Cdd:cd03798 75 LLAPLRAPSLAKLLkrrRRGPPDLIHAHFAYPAgFAAALLARLYGVPYVVTEHgsDINVFPPRSLLRKLLRWALRRAARV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 139 IAVTPLVADHVARYGgVPRENIEVIQNGVDLSRFSPENATPldlsqfGVPKDAVVIAKVGRLNVQKDHANFLRAAAILAR 218
Cdd:cd03798 155 IAVSKALAEELVALG-VPRDRVDVIPNGVDPARFQPEDRGL------GLPLDAFVILFVGRLIPRKGIDLLLEAFARLAK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 219 KDPRAHFLVVGDGELMTQSQELARQLGLGpDRLTFTGNI--RQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVST 296
Cdd:cd03798 228 ARPDVVLLIVGDGPLREALRALAEDLGLG-DRVTFTGRLphEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVAT 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 960397608 297 AVGGVPDLIANGENGMLVPASDPAALAAAGGMLVSDADLRhRIGAAGQDTVRARFSGKAMTDRI 360
Cdd:cd03798 307 DVGGIPEVVGDPETGLLVPPGDADALAAALRRALAEPYLR-ELGEAARARVAERFSWVKAADRI 369
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
76-360 |
1.22e-47 |
|
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: 166.65 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 76 QLMRRW-----QPDVVHSHLTKSDLVAQLAARMRGLPRLVTLHNAAPWRKKRLPAR-LYHW---------VVGKPDALIA 140
Cdd:cd03800 90 GLLRFIareggRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHSLGRVKYRHLGAQdTYHPslritaeeqILEAADRVIA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 141 VTPLVADHVARYGGVPRENIEVIQNGVDLSRFSPENATPLDLSQFGVPKDAVVIAKVGRLNVQKDHANFLRAAAILARKD 220
Cdd:cd03800 170 STPQEADELISLYGADPSRINVVPPGVDLERFFPVDRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 221 PRAHFLVVG----DGELMT--QSQELARQLGLGpDRLTFTGNIRQ--MPELLSAIDIFMLASAWEGLPMVLLEAMAMGLP 292
Cdd:cd03800 250 ELANLVLVGgpsdDPLSMDreELAELAEELGLI-DRVRFPGRVSRddLPELYRAADVFVVPSLYEPFGLTAIEAMACGTP 328
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 960397608 293 VVSTAVGGVPDLIANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFSGKAMTDRI 360
Cdd:cd03800 329 VVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQL 396
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
72-359 |
8.07e-47 |
|
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.
Pssm-ID: 132132 [Multi-domain] Cd Length: 374 Bit Score: 163.74 E-value: 8.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 72 WRIWQLMRRWQPDVVHSHlTKSDLVAQLAARMRGLPRlvTLHNAAPW---------RKKRLPARLYHWVVGKpdaLIAVT 142
Cdd:TIGR03088 71 PQLYRLLRQLRPDIVHTR-NLAALEAQLPAALAGVPA--RIHGEHGRdvfdldgsnWKYRWLRRLYRPLIHH---YVAVS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 143 PLVADHVARYGGVPRENIEVIQNGVDLSRFSPENATPLDL--SQFGVPkDAVVIAKVGRLNVQKDHANFLRAAAILARK- 219
Cdd:TIGR03088 145 RDLEDWLRGPVKVPPAKIHQIYNGVDTERFHPSRGDRSPIlpPDFFAD-ESVVVGTVGRLQAVKDQPTLVRAFALLVRQl 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 220 ---DPRAHFLVVGDGELMTQSQELARQLGLGpdRLT-FTGNIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVS 295
Cdd:TIGR03088 224 pegAERLRLVIVGDGPARGACEQMVRAAGLA--HLVwLPGERDDVPALMQALDLFVLPSLAEGISNTILEAMASGLPVIA 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 960397608 296 TAVGGVPDLIANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFSGKAMTDR 359
Cdd:TIGR03088 302 TAVGGNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSINAMVAA 365
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
5-352 |
6.79e-46 |
|
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: 160.87 E-value: 6.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 5 RILFVIDSL-RVGGAEtllldlldaaKARGDLA----------HVAYFTPGPLAP--------EVEKRGIATTRLSRKGL 65
Cdd:cd03820 1 KIAIVIPSIsNAGGAE----------RVAINLAnhlakkgydvTIISLDSAEKPPfyelddniKIKNLGDRKYSHFKLLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 66 RDPLALWRIWQLMRRWQPDVVHSHLTkSDLVAqLAARMRGLPRLVTLHNAAPWRKKRL-PARLYHWVVGKPDALIAVTpl 144
Cdd:cd03820 71 KYFKKVRRLRKYLKNNKPDVVISFRT-SLLTF-LALIGLKSKLIVWEHNNYEAYNKGLrRLLLRRLLYKRADKIVVLT-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 145 vADHVARYGGVPRENIEVIQNGVDLSrfSPENATPLdlsqfgvpKDAVVIAkVGRLNVQKDHANFLRAAAILARKDPRAH 224
Cdd:cd03820 147 -EADKLKKYKQPNSNVVVIPNPLSFP--SEEPSTNL--------KSKRILA-VGRLTYQKGFDLLIEAWALIAKKHPDWK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 225 FLVVGDGELMTQSQELARQLGLGpDRLTFTGNIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTA-VGGVPD 303
Cdd:cd03820 215 LRIYGDGPEREELEKLIDKLGLE-DRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDcPTGPSE 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 960397608 304 LIANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDtVRARFS 352
Cdd:cd03820 294 IIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARK-NAERFS 341
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
5-319 |
2.53e-45 |
|
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: 159.75 E-value: 2.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 5 RILFVIDSL--RVGGAETLLLDLLDAAKARGDLAHVAYFTPGPLAPEVEKRGIattRLSRKGLRD------PLALWRIWQ 76
Cdd:cd03817 1 KIAIFTDTYlpQVNGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEEVVRY---RSFSIPIRKyhrqhiPFPFKKAVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 77 L-MRRWQPDVVHSHLT-KSDLVAQLAARMRGLPRLVTLH--------------NAAPWRKKRLPARLYHWVvgkpDALIA 140
Cdd:cd03817 78 DrIKELGPDIIHTHTPfSLGKLGLRIARKLKIPIVHTYHtmyedylhyipkgkLLVKAVVRKLVRRFYNHT----DAVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 141 VTPLVADHVARYGGvpRENIEVIQNGVDLSRFSPEnATPLDLSQFGVPKDAVVIAKVGRLNVQKDHANFLRAAAILaRKD 220
Cdd:cd03817 154 PSEKIKDTLREYGV--KGPIEVIPNGIDLDKFEKP-LNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAEL-KKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 221 PRAHFLVVGDGELMTQSQELARQLGLGpDRLTFTGNI--RQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAV 298
Cdd:cd03817 230 PNIKLVIVGDGPEREELKELARELGLA-DKVIFTGFVprEELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKD 308
|
330 340
....*....|....*....|.
gi 960397608 299 GGVPDLIANGENGMLVPASDP 319
Cdd:cd03817 309 PAASELVEDGENGFLFEPNDE 329
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
5-319 |
7.63e-42 |
|
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: 150.29 E-value: 7.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 5 RILFVIDSLRVGGAETLLLDLLDAAKARGDLAHVAYFTPGPL-APEVEKRGIATTRLSRKGLRDPLALWRIWQLMRRWQP 83
Cdd:cd04951 1 KILYVITGLGLGGAEKQTVLLADQMFIRGHDVNIVYLTGEVEvKPLNNNIIIYNLGMDKNPRSLLKALLKLKKIISAFKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 84 DVVHSHLTKSDLVAQLAARMRGLPRLV-TLHNAAPWRKKRLpaRLYHWVvgkpDALIAVTPLVADHVARY----GGVPRE 158
Cdd:cd04951 81 DVVHSHMFHANIFARFLRMLYPIPLLIcTAHNKNEGGRIRM--FIYRLT----DFLCDITTNVSREALDEfiakKAFSKN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 159 NIEVIQNGVDLSRFSPENATPLDL-SQFGVPKDAVVIAKVGRLNVQKDHANFLRAAAILARKDPRAHFLVVGDGELMTQS 237
Cdd:cd04951 155 KSVPVYNGIDLNKFKKDINVRLKIrNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPLRNEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 238 QELARQLGLgPDRLTFTGNIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGEngMLVPAS 317
Cdd:cd04951 235 ERLICNLNL-VDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHN--YVVPVS 311
|
..
gi 960397608 318 DP 319
Cdd:cd04951 312 DP 313
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
5-294 |
9.89e-39 |
|
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: 142.04 E-value: 9.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 5 RILFVIDSLRVGGAETLLLDLLDAAKARGDLAHVaYFTPGPLAP---EVEKRGIATTRLSRKGLRDPLALWRIWQLMRRW 81
Cdd:cd03812 1 KILHIVGGMNVGGIETFLMNLYRKLDKSKIEFDF-LATSDDKGEydeELEELGGKIFYIPPKKKNIIKYFIKLLKLIKKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 82 QPDVVHSHLTKSDLVAQLAARMRGLP-RLVTLHNAAPWRKKRLPARLYH--WVVGK-PDALIAVtplvADHVAR--YGGV 155
Cdd:cd03812 80 KYDIVHVHGSSSNGIILLLAAKAGVPvRIAHSHNTKDSSIKLRKIRKNVlkKLIERlSTKYLAC----SEDAGEwlFGEV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 156 PRENIEVIQNGVDLSRFSPENATPLDLSQFGVPKDAVVIAKVGRLNVQKDHANFLRAAAILARKDPRAHFLVVGDGELMT 235
Cdd:cd03812 156 ENGKFKVIPNGIDIEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 960397608 236 QSQELARQLGLgPDRLTFTGNIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVV 294
Cdd:cd03812 236 KIKEKVKELGL-EDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCL 293
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
193-344 |
5.08e-37 |
|
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: 131.63 E-value: 5.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 193 VIAKVGRLNVQKDHANFLRAAAILARKDPRAHFLVVGDGELMTQSQELARQLGLGpDRLTFTGNI--RQMPELLSAIDIF 270
Cdd:pfam00534 4 IILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLG-DNVIFLGFVsdEDLPELLKIADVF 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 960397608 271 MLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQ 344
Cdd:pfam00534 83 VLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENAR 156
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
193-319 |
1.68e-36 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 129.55 E-value: 1.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 193 VIAKVGRLNV-QKDHANFLRAAAILARKDPRAHFLVVGDGELmtqsQELARQLGLGPDRLTFTGNIRQMPELLSAIDIFM 271
Cdd:pfam13692 3 VILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPE----EELEELAAGLEDRVIFTGFVEDLAELLAAADVFV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 960397608 272 LASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIaNGENGMLVPASDP 319
Cdd:pfam13692 79 LPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDP 125
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
5-343 |
3.01e-36 |
|
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: 135.50 E-value: 3.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 5 RILFVIDSL--RVGGAETLLLDLLDAAKARGDLAHVayFTPGPlAPEVEKRGIATTRLS------RKGLRDPLAL-WRIW 75
Cdd:cd03814 1 RIALVTDTYhpQVNGVVRTLERLVDHLRRRGHEVRV--VAPGP-FDEAESAEGRVVSVPsfplpfYPEYRLALPLpRRVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 76 QLMRRWQPDVVHShltkSD-----LVAQLAARMRGLPRLVTLHN-----AAPWRKKRLPARLYHWVV---GKPDALIAVT 142
Cdd:cd03814 78 RLIKEFQPDIIHI----ATpgplgLAALRAARRLGLPVVTSYHTdfpeyLSYYTLGPLSWLAWAYLRwfhNPFDTTLVPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 143 PLVADHVARYGgvpRENIEVIQNGVDLSRFSPENATPLDLSQFGVPKDAVVIAkVGRLNVQKDHANFLRAAAILARKDPr 222
Cdd:cd03814 154 PSIARELEGHG---FERVRLWPRGVDTELFHPSRRDAALRRRLGPPGRPLLLY-VGRLAPEKNLEALLDADLPLAASPP- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 223 AHFLVVGDGElmtQSQELARQlglGPDrLTFTGNIRqmPELLSAI----DIFMLASAWEGLPMVLLEAMAMGLPVVSTAV 298
Cdd:cd03814 229 VRLVVVGDGP---ARAELEAR---GPD-VIFTGFLT--GEELARAyasaDVFVFPSRTETFGLVVLEAMASGLPVVAADA 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 960397608 299 GGVPDLIANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAG 343
Cdd:cd03814 300 GGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARA 344
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
84-358 |
6.48e-35 |
|
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: 132.09 E-value: 6.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 84 DVVHSHLTKSDLVAQLAARM---RGLPRLVTLHNAAPWRKKRLPArLYH---WVVGKPDALIAVTPLVADHVARYGGVPR 157
Cdd:cd04962 86 DVLHAHYAIPHASCAYLAREilgEKIPIVTTLHGTDITLVGYDPS-LQPavrFSINKSDRVTAVSSSLRQETYELFDVDK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 158 EnIEVIQNGVDLSRFSPENATPLDlSQFGVPKDAVVIAKVGRLNVQKDHANFLRAAAILARKDPrAHFLVVGDGELMTQS 237
Cdd:cd04962 165 D-IEVIHNFIDEDVFKRKPAGALK-RRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIP-AKLLLVGDGPERVPA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 238 QELARQLGLGpDRLTFTGNIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLVPAS 317
Cdd:cd04962 242 EELARELGVE-DRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVG 320
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 960397608 318 DPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFSGKAMTD 358
Cdd:cd04962 321 DVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVP 361
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
71-359 |
6.93e-34 |
|
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: 130.92 E-value: 6.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 71 LWRIWQLMRRWqpDVVHSHLTK-SDLVAQLAARMRGLPRLVTLHN-----------AAPWRK---KRLPARLYHwVVGKP 135
Cdd:cd03813 164 LAIAADDLPEA--DLYHSVSTGyAGLLGALARHRRGIPFLLTEHGiytrerkieilQSTWIMgyiKKLWIRFFE-RLGKL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 136 --DALIAVTPLVaDHVARYG---GVPRENIEVIQNGVDLSRFSPenatpldLSQFGVPKDAVVIAKVGRLNVQKDHANFL 210
Cdd:cd03813 241 ayQQADKIISLY-EGNRRRQirlGADPDKTRVIPNGIDIQRFAP-------AREERPEKEPPVVGLVGRVVPIKDVKTFI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 211 RAAAILARKDPRAHFLVVG----DGELMTQSQELARQLGLGpDRLTFTGnIRQMPELLSAIDIFMLASAWEGLPMVLLEA 286
Cdd:cd03813 313 RAFKLVRRAMPDAEGWLIGpedeDPEYAQECKRLVASLGLE-NKVKFLG-FQNIKEYYPKLGLLVLTSISEGQPLVILEA 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 960397608 287 MAMGLPVVSTAVGGVPDLI-----ANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFSGKAMTDR 359
Cdd:cd03813 391 MASGVPVVATDVGSCRELIygaddALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDS 468
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
59-360 |
1.64e-33 |
|
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: 128.61 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 59 RLSRKGLRDPLALWrIWQLMRRWQPDVVHSH---LTKSdLVAQLAARMRGLPRLVTLHN-------AAPWRKKRLP---- 124
Cdd:cd03794 76 RRLLNYLSFALAAL-LKLLVREERPDVIIAYsppITLG-LAALLLKKLRGAPFILDVRDlwpesliALGVLKKGSLlkll 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 125 ARLYHWVVGKPDALIAVTPLVADHVaRYGGVPRENIEVIQNGVDLSRFSPENATPLDlsQFGVPKDAVVIAKVGRLNVQK 204
Cdd:cd03794 154 KKLERKLYRLADAIIVLSPGLKEYL-LRKGVPKEKIIVIPNWADLEEFKPPPKDELR--KKLGLDDKFVVVYAGNIGKAQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 205 DHANFLRAAAILaRKDPRAHFLVVGDGELMTQSQELARQLGLgpDRLTFTGNI--RQMPELLSAIDIFML-----ASAWE 277
Cdd:cd03794 231 GLETLLEAAERL-KRRPDIRFLFVGDGDEKERLKELAKARGL--DNVTFLGRVpkEEVPELLSAADVGLVplkdnPANRG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 278 GLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFSGKAMT 357
Cdd:cd03794 308 SSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLA 387
|
...
gi 960397608 358 DRI 360
Cdd:cd03794 388 DRL 390
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
60-351 |
1.36e-32 |
|
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: 125.64 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 60 LSRKGLRDPLALWRI-WQLMRRW-----------QPDVVHSHLTKSDLVAQLAARMRGLPRLVTLHN----------AAP 117
Cdd:cd05844 47 LRALGGSGPLRWLRQmAQRLLGWsaprlggaaglAPALVHAHFGRDGVYALPLARALGVPLVVTFHGfdittsrawlAAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 118 WRKKRLPARLYHWVVGKPDALIAVTPLVADHVARyGGVPRENIEVIQNGVDLSRFSPENatpldlsqfgVPKDAVVIAKV 197
Cdd:cd05844 127 PGWPSQFQRHRRALQRPAALFVAVSGFIRDRLLA-RGLPAERIHVHYIGIDPAKFAPRD----------PAERAPTILFV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 198 GRLNVQKDHANFLRAAAILARKDPRAHFLVVGDGELMTQSQELARQLGlgpdRLTFTGNI---RQMPELLSAIdIFMLAS 274
Cdd:cd05844 196 GRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAALG----RVRFLGALphaEVQDWMRRAE-IFCLPS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 275 AW------EGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTVR 348
Cdd:cd05844 271 VTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVC 350
|
...
gi 960397608 349 ARF 351
Cdd:cd05844 351 EQF 353
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
5-358 |
9.88e-31 |
|
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: 120.13 E-value: 9.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 5 RILFVIDS---LRVGGAETLLLDLLDAAKARGdlAHVAYFTPGPLAPEVEKRGIATTRLSR--KGLRDPLALWRIWQLMR 79
Cdd:cd03823 1 KILLVNSLyppQRVGGAEISVHDLAEALVAEG--HEVAVLTAGVGPPGQATVARSVVRYRRapDETLPLALKRRGYELFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 80 RW---------------QPDVVHSHlTKSDLVAQL--AARMRGLPRLVTLHNAAPwrkkrlparLYHWV---VGKPDALI 139
Cdd:cd03823 79 TYnpglrrllarlledfRPDVVHTH-NLSGLGASLldAARDLGIPVVHTLHDYWL---------LCPRQflfKKGGDAVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 140 AVTPLVADhVARYGGVPRENIEVIQNGVDLSRFSPENATPLDlsqfgvpkDAVVIAKVGRLNVQKDHANFLRAAAILARK 219
Cdd:cd03823 149 APSRFTAN-LHEANGLFSARISVIPNAVEPDLAPPPRRRPGT--------ERLRFGYIGRLTEEKGIDLLVEAFKRLPRE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 220 DprAHFLVVGDGelmtqSQELARQLGLGPdRLTFTGNIR--QMPELLSAIDIFMLASAW-EGLPMVLLEAMAMGLPVVST 296
Cdd:cd03823 220 D--IELVIAGHG-----PLSDERQIEGGR-RIAFLGRVPtdDIKDFYEKIDVLVVPSIWpEPFGLVVREAIAAGLPVIAS 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960397608 297 AVGGVPDLIANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFSGKAMTD 358
Cdd:cd03823 292 DLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEEYLK 353
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
68-350 |
4.66e-28 |
|
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: 113.23 E-value: 4.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 68 PLALWRIWQlmrrwQPDVVHSHLTKS--DLVAQLAARMRGLPRLVTLHNA--------APWRKKRLPARLYHWVVGKPDA 137
Cdd:cd03821 81 PNWLRRNLR-----EYDVVHIHGVWTytSLAACKLARRRGIPYVVSPHGMldpwalqqKHWKKRIALHLIERRNLNNAAL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 138 LIAVTPLVADHVARYGgvPRENIEVIQNGVDLSRFSPENAtplDLSQFGVPKDAVVIAKVGRLNVQKDHANFLRAAAILA 217
Cdd:cd03821 156 VHFTSEQEADELRRFG--LEPPIAVIPNGVDIPEFDPGLR---DRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 218 RKDPRAHFLVVG-DGELMTQSQELARQLGLGpDRLTFTGNIRQM--PELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVV 294
Cdd:cd03821 231 EQGRDWHLVIAGpDDGAYPAFLQLQSSLGLG-DRVTFTGPLYGEakWALYASADLFVLPSYSENFGNVVAEALACGLPVV 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 960397608 295 STAVGGVPDLIaNGENGMLVPASDPAALAAAGGMLvSDADLRHRIGAAGQDTVRAR 350
Cdd:cd03821 310 ITDKCGLSELV-EAGCGVVVDPNVSSLAEALAEAL-RDPADRKRLGEMARRARQVE 363
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
96-314 |
7.94e-28 |
|
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: 109.42 E-value: 7.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 96 VAQLAARMRGLPRLVTLHnAAPWRKKRlpARLYHWVVGKPDALIAVTP----LVADHVARYGGVPRenIEVIQNGVDLSR 171
Cdd:cd01635 19 VRALARALAALGHEVTVL-ALLLLALR--RILKKLLELKPDVVHAHSPhaaaLAALLAARLLGIPI--VVTVHGPDSLES 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 172 FSPENATPLDLSQFGVPKDAVViakVGRLNVQKDHANFLRAAAILARKDPRAHFLVVGDGELMTQSQELARQLGLGPDRL 251
Cdd:cd01635 94 TRSELLALARLLVSLPLADKVS---VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 960397608 252 TFTGNIR--QMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLV 314
Cdd:cd01635 171 IIGGLVDdeVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
37-361 |
9.65e-28 |
|
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: 112.07 E-value: 9.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 37 HVAYFTPGPLAPEVEKRGIATTRLSRKGLRDPLA------LWRIWQLMRRWQPDVVHS-HLTksdlvaqLAARMRGLPRL 109
Cdd:cd03809 33 DESVLAVPPLPGELLRLLREYPELSLGVIKIKLWrelallRWLQILLPKKDKPDLLHSpHNT-------APLLLKGCPQV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 110 VTLHNAAP---WRKKRLPARLYH-----WVVGKPDALIAVTPLVADHVARYGGVPRENIEVIQNGVDLSRFSPEnaTPLD 181
Cdd:cd03809 106 VTIHDLIPlryPEFFPKRFRLYYrlllpISLRRADAIITVSEATRDDIIKFYGVPPEKIVVIPLGVDPSFFPPE--SAAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 182 LSQFGVPKDAVVIAkVGRLNVQKDHANFLRAAAILARKDPRAHFLVVGDGELMTQSQELARQLGLGPDRLTFTGNI--RQ 259
Cdd:cd03809 184 LIAKYLLPEPYFLY-VGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEELLDLVKKLGLGGRVRFLGYVsdED 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 260 MPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDlIAnGENGMLVPASDPAALAAAGGMLVSDADLRHRI 339
Cdd:cd03809 263 LPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPE-VA-GDAALYFDPLDPESIADAILRLLEDPSLREEL 340
|
330 340
....*....|....*....|..
gi 960397608 340 GAAGQDTVRaRFSGKAMTDRIW 361
Cdd:cd03809 341 IRKGLERAK-KFSWEKTAEKTL 361
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
43-351 |
3.24e-27 |
|
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: 110.62 E-value: 3.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 43 PGPLA---PEVEKRGIATTRLsrkglrdplaLWRIWQLMRRWQPDVVHSHLTKSDLVAQLAARMRGLP-RLVTLHNAA-- 116
Cdd:cd03799 38 PGDLVkrhPDVEKYNVPSLNL----------LYAIVGLNKKGAYDIIHCQFGPLGALGALLRRLKVLKgKLVTSFRGYdi 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 117 PWRKKRLPARLYHWVVGKPDALIAVTPLVADHVARYGgVPRENIEVIQNGVDLSRFspenatPLDLSQFgvPKDAVV-IA 195
Cdd:cd03799 108 SMYVILEGNKVYPQLFAQGDLFLPNCELFKHRLIALG-CDEKKIIVHRSGIDCNKF------RFKPRYL--PLDGKIrIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 196 KVGRLNVQKDHANFLRAAAILARKDPRAHFLVVGDGELMTQSQELARQLGLGpDRLTFTG--NIRQMPELLSAIDIFMLA 273
Cdd:cd03799 179 TVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIG-DCVKLLGwkPQEEIIEILDEADIFIAP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 274 SA------WEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTV 347
Cdd:cd03799 258 SVtaadgdQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARV 337
|
....
gi 960397608 348 RARF 351
Cdd:cd03799 338 EEEY 341
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
73-318 |
2.29e-25 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 108.20 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 73 RIWQLMRRWQPDVVHSHLTKSDLVAQLAARMRGLPRLVTLHNAAP--WRKKRLPAR---LYHWVVGKPD-ALIAVTPLVA 146
Cdd:PRK15179 391 KLTDVMRSSVPSVVHIWQDGSIFACALAALLAGVPRIVLSVRTMPpvDRPDRYRVEydiIYSELLKMRGvALSSNSQFAA 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 147 DHVARYGGVPRENIEVIQNGV-DLSRFSPENATPLDLSQFGVPKDAV-VIAKVGRLNVQKDHANFLRAAAILARKDPRAH 224
Cdd:PRK15179 471 HRYADWLGVDERRIPVVYNGLaPLKSVQDDACTAMMAQFDARTSDARfTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVR 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 225 FLVVGDGELMTQSQELARQLGLGpDRLTFTGNIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDL 304
Cdd:PRK15179 551 FIMVGGGPLLESVREFAQRLGMG-ERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEA 629
|
250
....*....|....
gi 960397608 305 IANGENGMLVPASD 318
Cdd:PRK15179 630 VQEGVTGLTLPADT 643
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
263-360 |
6.10e-25 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 98.14 E-value: 6.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 263 LLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAA 342
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96
|
90
....*....|....*...
gi 960397608 343 GQDTVRARFSGKAMTDRI 360
Cdd:COG0438 97 ARERAEERFSWEAIAERL 114
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
73-360 |
9.44e-25 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 105.18 E-value: 9.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 73 RIWQLMRRWQPDVVHSHLTKSDLVAQLA-ARMRGLPRLVTLHNAAPwrkKRLPARLYHWVV-----------GKPDALIA 140
Cdd:PLN02871 135 RIISEVARFKPDLIHASSPGIMVFGALFyAKLLCVPLVMSYHTHVP---VYIPRYTFSWLVkpmwdiirflhRAADLTLV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 141 VTPLVADHVARYGGVPRENIEVIQNGVDLSRFSPE---NATPLDLSQfGVPKDAVVIAkVGRLNVQKDhANFLRAaaILA 217
Cdd:PLN02871 212 TSPALGKELEAAGVTAANRIRVWNKGVDSESFHPRfrsEEMRARLSG-GEPEKPLIVY-VGRLGAEKN-LDFLKR--VME 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 218 RKdPRAHFLVVGDGelmTQSQELARQLGLGPdrLTFTGNIrQMPELLSA---IDIFMLASAWEGLPMVLLEAMAMGLPVV 294
Cdd:PLN02871 287 RL-PGARLAFVGDG---PYREELEKMFAGTP--TVFTGML-QGDELSQAyasGDVFVMPSESETLGFVVLEAMASGVPVV 359
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 960397608 295 STAVGGVPDLIAN---GENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTVrARFSGKAMTDRI 360
Cdd:PLN02871 360 AARAGGIPDIIPPdqeGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEV-EKWDWRAATRKL 427
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
118-356 |
2.03e-24 |
|
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: 102.80 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 118 WRKKRlparlYHWVVGKPDaLIAVTPLVADHVARYGGVPRENIEVIQNGVDLSRFSPENAtPLDLSQFGVPKDAVVI--A 195
Cdd:cd03825 127 FRRKR-----EALAKKRLT-IVAPSRWLADMVRRSPLLKGLPVVVIPNGIDTEIFAPVDK-AKARKRLGIPQDKKVIlfG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 196 KVGRLNVQKDHANFLRAAAILARKDpRAHFLVVGDGELMTQSQELA-RQLGlgpdrltFTGNIRQMPELLSAIDIFMLAS 274
Cdd:cd03825 200 AESVTKPRKGFDELIEALKLLATKD-DLLLVVFGKNDPQIVILPFDiISLG-------YIDDDEQLVDIYSAADLFVHPS 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 275 AWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFSGK 354
Cdd:cd03825 272 LADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQR 351
|
..
gi 960397608 355 AM 356
Cdd:cd03825 352 VQ 353
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
16-170 |
4.60e-22 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 91.83 E-value: 4.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 16 GGAETLLLDLLDAAKARGDLAHVAYFTPGPLAPEVEKRGIATTR----LSRKGLRDPLALWRIWQLMRRWQPDVVHSHLT 91
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRvplpLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 92 KSDLVAQLAARMR-GLPRLVTLHN---------AAPWRKKRLPARLYHWVVGKPDALIAVTPLVADHVARYGGVPRENIE 161
Cdd:pfam13439 81 FPLGLAALAARLRlGIPLVVTYHGlfpdykrlgARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVPPEKIR 160
|
....*....
gi 960397608 162 VIQNGVDLS 170
Cdd:pfam13439 161 VIPNGVDLE 169
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
154-359 |
7.89e-22 |
|
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: 96.92 E-value: 7.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 154 GVPRENIEVIQNGVDLSRFSPenatPLDLSQFGVPKdavVIAKVGRLNVQKDHANFLRAAAILARKDPRAHFLVVG---- 229
Cdd:NF038011 276 GAPPERTRVIPNGIDLPRLAP----LRAQRPAGIPP---VVGLIGRVVPIKDIKTFIRAMRTVVRAMPEAEGWIVGpeee 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 230 DGELMTQSQELARQLGLGpDRLTFTGnIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLI---- 305
Cdd:NF038011 349 DPAYAAECRSLVASLGLQ-DKVKFLG-FQKIDDLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLIegld 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 960397608 306 ----ANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFSGKAMTDR 359
Cdd:NF038011 427 eedrALGAAGEVVAIADPQALARAALDLLRDPQRWQAAQAAGLARVERYYTEELMFDR 484
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
16-166 |
7.46e-19 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 82.83 E-value: 7.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 16 GGAETLLLDLLDAAKARGDLAHVAYFTPGPLAPEVEKRGIATTRL----SRKGLRDPLALWRIWQLMRRWQPDVVHSHLT 91
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLpvppRPSPLADLAALRRLRRLLRAERPDVVHAHSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 960397608 92 KSDLVAQLAARMRGLPRLVTLHNAAP----WRKKRLPARLYHWVVGKPDALIAVTPLVADHVARYgGVPRENIEVIQNG 166
Cdd:pfam13579 81 TAGLAARLARRRRGVPLVVTVHGLALdygsGWKRRLARALERRLLRRADAVVVVSEAEAELLRAL-GVPAARVVVVPNG 158
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
95-314 |
8.17e-19 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 88.22 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 95 LVAQLAARMRGLPRL-VTLHNAAPWRKKRL--PAR--LYHWVVGKPDA-LIAVTPLVADHVARYGGVPRENIEVIQNGVD 168
Cdd:PRK15490 293 LMIALAALIAGVPRIqLGLRGLPPVVRKRLfkPEYepLYQALAVVPGVdFMSNNHCVTRHYADWLKLEAKHFQVVYNGVL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 169 LSRFSPENATPLDLSQFGVPK--DA-VVIAKVGRLNVQKDHANFLRAAAILARKDPRAHFLVVGDGELMTQSQELARQLG 245
Cdd:PRK15490 373 PPSTEPSSEVPHKIWQQFTQKtqDAdTTIGGVFRFVGDKNPFAWIDFAARYLQHHPATRFVLVGDGDLRAEAQKRAEQLG 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 960397608 246 LgPDRLTFTGNIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLV 314
Cdd:PRK15490 453 I-LERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGSAECFIEGVSGFIL 520
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
55-357 |
1.04e-18 |
|
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: 86.56 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 55 IATTRLSrkglrdPLALWRIWQLmrRWQPDVVHSHLtkSDLVAQLAARMRGLPRLVTLHnaapW-----RKKRLpARLY- 128
Cdd:cd03795 64 VASTPFS------PSYIKRFKKL--AKEYDIIHYHF--PNPLADLLLFFSGAKKPVVVH----WhsdivKQKKL-LKLYk 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 129 ---HWVVGKPDALIAVTPLVADHVARYGGVpRENIEVIQNGVDlsrfspENATPLDLSQFGVPKDAVVIAK----VGRLN 201
Cdd:cd03795 129 plmTRFLRRADRIIATSPNYVETSPTLREF-KNKVRVIPLGID------KNVYNIPRVDFENIKREKKGKKiflfIGRLV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 202 VQKDHANFLRAAAILarkdpRAHFLVVGDGELMTQSQELARQLGLgpDRLTFTGNI--RQMPELLSAIDIFMLASAW--E 277
Cdd:cd03795 202 YYKGLDYLIEAAQYL-----NYPIVIGGEGPLKPDLEAQIELNLL--DNVKFLGRVddEEKVIYLHLCDVFVFPSVLrsE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 278 GLPMVLLEAMAMGLPVVSTAVG-GVPDLIANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFSGKAM 356
Cdd:cd03795 275 AFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEKM 354
|
.
gi 960397608 357 T 357
Cdd:cd03795 355 K 355
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
157-352 |
5.01e-18 |
|
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: 84.72 E-value: 5.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 157 RENIEVIQNGVDLSRFSPE-NATPLDLSQFGVPKDAVVIAKVGR-LNVQKDHANFLRAAAILARKDPRAHFLVVGDGELM 234
Cdd:cd03818 178 RDRISVIHDGVDTDRLAPDpAARLRLLNGTELKAGDPVITYVARnLEPYRGFHVFMRALPRIQARRPDARVVVVGGDGVS 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 235 TQS---------QELARQLGLGPDRLTFTG--NIRQMPELLSAIDI-----FMLASAWEglpmvLLEAMAMGLPVVSTAV 298
Cdd:cd03818 258 YGSpppdggswkQKMLAELGVDLERVHFVGkvPYDQYVRLLQLSDAhvyltYPFVLSWS-----LLEAMACGCPVIGSDT 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 960397608 299 GGVPDLIANGENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFS 352
Cdd:cd03818 333 APVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDS 386
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
84-352 |
5.11e-16 |
|
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: 78.59 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 84 DVVHSHLTKS-DLVAQLAARmRGLPRLV-TLHNAAPWRKKRLpARLYHWVVGKPDALIAVTPLVADHVARYGGVpreNIE 161
Cdd:TIGR04047 88 DVVHAQDCISgNALATLRAE-GLIPGFVrTVHHLDDFDDPRL-AACQERAIVEADAVLCVSAAWAAELRAEWGI---DAT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 162 VIQNGVDLSRFS--PENATPLDLSQFGVPKDAVVIAkVGRLNVQKDHANFLRAAAILARKDPRAHfLVVGDGELM----- 234
Cdd:TIGR04047 163 VVPNGVDAARFSpaADAADAALRRRLGLRGGPYVLA-VGGIEPRKNTIDLLEAFALLRARRPQAQ-LVIAGGATLfdyda 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 235 --TQSQELARQLGLGPDRLTFTGNIRQ--MPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIaNGEN 310
Cdd:TIGR04047 241 yrREFRARAAELGVDPGPVVITGPVPDadLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYL-GRFD 319
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 960397608 311 GMLVPASDPaaLAAAGGMLVS-DADLRHRIGAAGQDTVrARFS 352
Cdd:TIGR04047 320 AAWADPSDP--DSIADALALAlDPARRPALRAAGPELA-ARYT 359
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
65-313 |
1.27e-15 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 77.44 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 65 LRDPLALWRIWQLMRRWQPDVVHSHLTKSDLVAQLAARMRGLP-RLVT-----LHNAAPWRKKRLPARLYHWVVGKP--D 136
Cdd:PRK09922 67 LRRAKHVYNFSKWLKETQPDIVICIDVISCLYANKARKKSGKQfKIFSwphfsLDHKKHAECKKITCADYHLAISSGikE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 137 ALIAVtplvadhvarygGVPRENIEVIQNGVDLSRFS---PENATPLDLsqfgvpkdavviAKVGRLNV--QKDHANFLR 211
Cdd:PRK09922 147 QMMAR------------GISAQRISVIYNPVEIKTIIippPERDKPAVF------------LYVGRLKFegQKNVKELFD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 212 AaaiLARKDPRAHFLVVGDGELMTQSQELARQLGLGpDRLTFTGNIRQMPELL----SAIDIFMLASAWEGLPMVLLEAM 287
Cdd:PRK09922 203 G---LSQTTGEWQLHIIGDGSDFEKCKAYSRELGIE-QRIIWHGWQSQPWEVVqqkiKNVSALLLTSKFEGFPMTLLEAM 278
|
250 260
....*....|....*....|....*..
gi 960397608 288 AMGLPVVST-AVGGVPDLIANGENGML 313
Cdd:PRK09922 279 SYGIPCISSdCMSGPRDIIKPGLNGEL 305
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
76-304 |
1.24e-13 |
|
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: 71.50 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 76 QLMRRWQPDVVHSHLTKSDLV--AQLAARMRGLPRLVTLH------NAAP-WRKKrlparLYHWVVGKPDALIAVTplva 146
Cdd:cd03796 82 NILIRERIQIVHGHQAFSSLAheALFHARTLGLKTVFTDHslfgfaDASSiLTNK-----LLRFSLADIDHVICVS---- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 147 dHVAR-----YGGVPRENIEVIQNGVDLSRFSPENATPldlsqfgvPKDAVVIAKVGRLNVQKDHANFLRAAAILARKDP 221
Cdd:cd03796 153 -HTSKentvlRASLDPRIVSVIPNAVDSSDFTPDPSKP--------DPNKITIVVISRLVYRKGIDLLVGIIPRICKKHP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 222 RAHFLVVGDGELMTQSQELARQLGLgPDRLTFTGNIR--QMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVG 299
Cdd:cd03796 224 NVRFIIGGDGPKRIELEEMREKYQL-QDRVELLGAVPheEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVG 302
|
....*
gi 960397608 300 GVPDL 304
Cdd:cd03796 303 GIPEV 307
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
136-315 |
1.76e-13 |
|
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: 70.79 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 136 DALIAVTPL-VADHVARYGGVPRenIEVIQNGVDLSRFSPENAtpldlsqfgVPKDAVVIAKVGRLNVQKDHANFLRAAA 214
Cdd:cd04949 115 DAIIVSTEQqKQDLSERFNKYPP--IFTIPVGYVDQLDTAESN---------HERKSNKIITISRLAPEKQLDHLIEAVA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 215 ILARKDPRAHFLVVGDGELMTQSQELARQLGLGpDRLTFTGNIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVV 294
Cdd:cd04949 184 KAVKKVPEITLDIYGYGEEREKLKKLIEELHLE-DNVFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVV 262
|
170 180
....*....|....*....|..
gi 960397608 295 STAVG-GVPDLIANGENGMLVP 315
Cdd:cd04949 263 SYDVKyGPSELIEDGENGYLIE 284
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
155-359 |
2.82e-11 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 64.43 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 155 VPRENIEVIQNGVDLSRFSpENATPLDLSQFGVPKDAVVIAKVGRLNVQKDHANFLRAAAILARKDPRAHFLVVGD---- 230
Cdd:PRK15484 158 LPNADISIVPNGFCLETYQ-SNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGDptas 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 231 -----GELMTQSQELARQLGlgpDRLTFTGNI--RQMPELLSAIDIFMLASAW-EGLPMVLLEAMAMGLPVVSTAVGGVP 302
Cdd:PRK15484 237 skgekAAYQKKVLEAAKRIG---DRCIMLGGQppEKMHNYYPLADLVVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGIT 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 960397608 303 DLIANGENGM-LVPASDPAALAAAGGMLVSDADlRHRIGAAGQDTVRARFSGKAMTDR 359
Cdd:PRK15484 314 EFVLEGITGYhLAEPMTSDSIISDINRTLADPE-LTQIAEQAKDFVFSKYSWEGVTQR 370
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
41-359 |
6.55e-10 |
|
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: 59.99 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 41 FTPGPLAPEVEKRGIATTRLSRKGLRDPLALWRIWQlmRRWQPDVVHSHltkSDLVAQLAARMRGLPRLVTLHNAApwRK 120
Cdd:cd03802 47 HTSAPLVAVIPRALRLDPIPQESKLAELLEALEVQL--RASDFDVIHNH---SYDWLPPFAPLIGTPFVTTLHGPS--IP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 121 KRLPARLYHwvvgKPDALIAVTplvadHVARYGGVPRENIEVIQNGVDLSRFSPENATPLDLSQFGV------PKDAVVI 194
Cdd:cd03802 120 PSLAIYAAE----PPVNYVSIS-----DAQRAATPPIDYLTVVHNGLDPADYRFQPDPEDYLAFLGRiapekgLEDAIRV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 195 AKvgRLNVQ---------KDHANFLRAAAILarkdPRAHFLvvgdGELMTQsqELARQLGlgpdrltftgNIRQMpells 265
Cdd:cd03802 191 AR--RAGLPlkiagkvrdEDYFYYLQEPLPG----PRIEFI----GEVGHD--EKQELLG----------GARAL----- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 266 aidIFMlaSAWE---GLPMVllEAMAMGLPVVSTAVGGVPDLIANGENGMLVPAsdpaalaaAGGMlvsdADLRHRIG-- 340
Cdd:cd03802 244 ---LFP--INWDepfGLVMI--EAMACGTPVIAYRRGGLPEVIQHGETGFLVDS--------VEEM----AEAIANIDri 304
|
330 340
....*....|....*....|.
gi 960397608 341 --AAGQDTVRARFSGKAMTDR 359
Cdd:cd03802 305 drAACRRYAEDRFSAARMADR 325
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
266-319 |
8.71e-10 |
|
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.
Pssm-ID: 340854 [Multi-domain] Cd Length: 401 Bit Score: 59.78 E-value: 8.71e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 960397608 266 AIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLvPASDP 319
Cdd:cd04946 304 DVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLL-LDKDP 356
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
79-343 |
8.04e-09 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 56.91 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 79 RRWQPDVVHShLTKSDLVAQLAARMRGLPRLVT-LH------NAA-------PWRKKRLPARLYHWVVGKPDALIAVTPL 144
Cdd:PRK10307 103 RRWRPDRVIG-VVPTLFCAPGARLLARLSGARTwLHiqdyevDAAfglgllkGGKVARLATAFERSLLRRFDNVSTISRS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 145 VADHvARYGGVPRENIEVIQNGVDLSRFSP--ENATPLDLSQFGVPKDAVVIAKVGRLNVQKDHANFLRAAAILARKdPR 222
Cdd:PRK10307 182 MMNK-AREKGVAAEKVIFFPNWSEVARFQPvaDADVDALRAQLGLPDGKKIVLYSGNIGEKQGLELVIDAARRLRDR-PD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 223 AHFLVVGDGELMTQSQELARQLGLGPDRLTFTGNIRQMPELLSAIDIFML---ASAWEG-LPMVLLEAMAMGLPVVSTAV 298
Cdd:PRK10307 260 LIFVICGQGGGKARLEKMAQCRGLPNVHFLPLQPYDRLPALLKMADCHLLpqkAGAADLvLPSKLTNMLASGRNVVATAE 339
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 960397608 299 GG--VPDLIAngENGMLVPASDPAALAAAGGMLVSDADLRHRIGAAG 343
Cdd:PRK10307 340 PGteLGQLVE--GIGVCVEPESVEALVAAIAALARQALLRPKLGTVA 384
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
71-339 |
1.09e-08 |
|
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: 56.24 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 71 LWRIWQLMRRWQPDVVHSHL------TKSDLVAQLAARMRGLPRLVTLHNA----APWRKKR----LPARLYHWVVgkpd 136
Cdd:cd03822 64 YFRLLDHLNFKKPDVVHIQHefgifgGKYGLYALGLLLHLRIPVITTLHTVldlsDPGKQALkvlfRIATLSERVV---- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 137 alIAVTPLVADHVaRYGGVPRENIEVIQNGVDLSRFSPENAtpldLSQFGVPKDAVVIAKVGRLNVQKDHANFLRAAAIL 216
Cdd:cd03822 140 --VMAPISRFLLV-RIKLIPAVNIEVIPHGVPEVPQDPTTA----LKRLLLPEGKKVILTFGFIGPGKGLEILLEALPEL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 217 ARKDPRAHFLVVGDGELMTQSQELARQLGLGPDRLTFTGNIR---------QMPELLSAIDIFMLA--SAWEGLPMVLLE 285
Cdd:cd03822 213 KAEFPDVRLVIAGELHPSLARYEGERYRKAAIEELGLQDHVDfhnnflpeeEVPRYISAADVVVLPylNTEQSSSGTLSY 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 960397608 286 AMAMGLPVVSTAVGGVPDLIAnGENGMLVPASDPAALAAAGGMLVSDADLRHRI 339
Cdd:cd03822 293 AIACGKPVISTPLRHAEELLA-DGRGVLVPFDDPSAIAEAILRLLEDDERRQAI 345
|
|
| stp1 |
TIGR03087 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
78-360 |
5.62e-08 |
|
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.
Pssm-ID: 274425 [Multi-domain] Cd Length: 397 Bit Score: 54.32 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 78 MRRWQPDVVHSHLTK-----SDLVAQ-LAARMRGLPRLVTL--HNAAPW----RKKRLPARLYHWVVGKP---------- 135
Cdd:TIGR03087 92 LQRWVNALLAAEPVDaivvfSSAMAQyVTHHVRGIPRIIDFvdVDSDKWaqyaRTKRWPLSWIYQREGRLllayerriaa 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 136 --DALIAVTPLVADHVARYGGVPRENIEVIQNGVDLSRFSPENATPldlSQFGVPKDAVVIakVGRLNV---QKDHANFL 210
Cdd:TIGR03087 172 lfDAATFVSEAEAELFRRLAPEAAVRIDAFPNGVDADFFSPDRDYP---NPYPPGKRVLVF--TGAMDYwpnIDAVSWFA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 211 RAA--AILARKdPRAHFLVVGdgelmTQSQELARQLGLGPDrLTFTGNIRQM-PELL-SAIDIFMLASAwEGLPMVLLEA 286
Cdd:TIGR03087 247 ERVfpAVRAAR-PAAQFYIVG-----AKPSDAVQALAALPG-VTVTGSVADVrPYLAhAAAAVAPLRIA-RGIQNKVLEA 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 960397608 287 MAMGLPVVST--AVGGVpdlIANGENGMLVpASDPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFSGKAMTDRI 360
Cdd:TIGR03087 319 MAMGRPVVASpeAAEGI---DALAEAELLV-AADPAEFAAAILAVLANPAEAEGAGQAGRRRVLSHYAWPRNLARL 390
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
185-351 |
6.86e-08 |
|
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: 53.86 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 185 FGVPKDAVVIAKVGRLNVQKDHANFLRAAAILARKDPRAHFLVVG-------DGELMTQsqELARQLGLGPD--RLTFTG 255
Cdd:cd03792 191 FVIDPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGhgavddpEGSVVYE--EVMEYAGDDHDihVLRLPP 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 256 NIRQMPELLSAIDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLVPASDPAALAAAggMLVSDADL 335
Cdd:cd03792 269 SDQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAVRIL--RLLTDPEL 346
|
170
....*....|....*.
gi 960397608 336 RHRIGAAGQDTVRARF 351
Cdd:cd03792 347 RRKMGLAAREHVRDNF 362
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
204-360 |
1.32e-07 |
|
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: 52.98 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 204 KDHANFLRAAAILARKDP-RAHF-LVVGDG-------------ELmtqsQELARQLGLGPDRLTFTGNI--RQMPELLSA 266
Cdd:cd03805 224 KNIALAIEAFAKLKQKLPeFENVrLVIAGGydprvaenveyleEL----QRLAEELLNVEDQVLFLRSIsdSQKEQLLSS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 267 IDIFMLASAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLVpasDPAALAAAGGML--VSDADLRHRIGAAGQ 344
Cdd:cd03805 300 ALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLC---EPTPEAFAEAMLklANDPDLADRMGAAGR 376
|
170
....*....|....*.
gi 960397608 345 DTVRARFSGKAMTDRI 360
Cdd:cd03805 377 KRVKEKFSREAFAERL 392
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
277-352 |
2.81e-07 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 47.98 E-value: 2.81e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 960397608 277 EGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGMLvpASDPAALAAAGGMLVSDADLRHRIGAAGQDTVRARFS 352
Cdd:pfam13524 10 DSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILL--YRDPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHT 83
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
173-309 |
9.82e-07 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 50.76 E-value: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 173 SPENATPLDLSQFGVPKDAVVIAKVGRLnvQKDHANFLRA-AAILARkDPRAHFLVVGDGELMTQS--QELARQLGLGPD 249
Cdd:COG3914 452 APEVAPLPTRADLGLPEGAVVFGSFNNL--YKITPEVFALwARILKA-VPNSVLLLKGGGLPEARErlRAAAAARGVDPD 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 250 RLTFTG--NIRQMPELLSAIDIFmLASawegLP----MVLLEAMAMGLPVVsTAVG---------------GVPDLIANG 308
Cdd:COG3914 529 RLIFLPrlPRAEHLARYALADLF-LDT----FPynggTTTLEALWMGVPVV-TLAGetfasrvgaslltalGLPELIATS 602
|
.
gi 960397608 309 E 309
Cdd:COG3914 603 E 603
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
38-111 |
3.36e-06 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 46.16 E-value: 3.36e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 960397608 38 VAYFTPGPLAPEVEKR-GIA--TTRLSRKGLRDPLALWRIWQLMRRWQPDVVHSHLTKS-DLVAQLAARMRGLPRLVT 111
Cdd:pfam13477 27 VHVISSKGPAKDELIAeGIHvhRLKVPRKGPLGYLKAFRLKKLIKKIKPDVVHVHYAKPyGLLAGLAARLSGFPPVVL 104
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
117-313 |
1.06e-05 |
|
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: 46.89 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 117 PWRKKRLPARL-YH----WVV---GKPDALIAVTPLVADHVARYGGvpRENIeVIQNGVDLSRFSPENatpldlsqfgvP 188
Cdd:cd03804 132 GKGIKSLLASLfLHylrlWDVrtaQRVDLFIANSQFVARRIKKFYG--REST-VIYPPVDTDAFAPAA-----------D 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 189 KDAVVIAkVGRLNVQKDHANFLRAAAILARKdprahFLVVGDGElmtqsqELARQLGLGPDRLTFTGNIRQM--PELLSA 266
Cdd:cd03804 198 KEDYYLT-ASRLVPYKRIDLAVEAFNELPKR-----LVVIGDGP------DLDRLRAMASPNVEFLGYQPDEvlKELLSK 265
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 960397608 267 IDIFMLAsAWEGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGENGML 313
Cdd:cd03804 266 ARAFVFA-AEEDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGIL 311
|
|
| COG4641 |
COG4641 |
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]; |
39-352 |
9.65e-04 |
|
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443679 [Multi-domain] Cd Length: 303 Bit Score: 40.68 E-value: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 39 AYFTPGpLAPEVEKRGIATTRLSRK-GLRDPLALWRiwqLMRRWQPDVVHSHLTKSDLVAqlaARMRGLPRLvtLHNA-A 116
Cdd:COG4641 9 ATYYRG-LLRALAALGHEVTFLEPDdPWHDPLYAAE---LLDAFRPDLVLVISGVELVAA---LRARGIPTV--FWDTdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 117 PWRKKRLPARLYHWvvgkpDALIAVTPlvaDHVARYGGVPRENIEVIQNGVDLSRFSPENAtpldlsQFGVPKDAVVIAk 196
Cdd:COG4641 80 PVTLDRFRELLPLY-----DLVFTFDG---DCVEEYRALGARRVFYLPFAADPELHRPVPP------EARFRYDVAFVG- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 197 vgrlNVQKDHANFLRAaaiLARKDPRAHFLVVGDG---ELMTQSQELARQLGLgpdrltftgniRQMPELLSAIDIF--- 270
Cdd:COG4641 145 ----NYYPDRRARLEE---LLLAPAGLRLKIYGPGwpkLALPANVRRGGHLPG-----------EEHPAAYASSKITlnv 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 271 --MLASAWeGLPMVLLEAMAMGLPVVSTAVGGVPDLIANGEnGMLVpASDPAALAAAGGMLVSDADLRHRIGAAGQDTVR 348
Cdd:COG4641 207 nrMAASPD-SPTRRTFEAAACGAFLLSDPWEGLEELFEPGE-EVLV-FRDGEELAEKLRYLLADPEERRAIAEAGRRRVL 283
|
....
gi 960397608 349 ARFS 352
Cdd:COG4641 284 AEHT 287
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
81-308 |
5.06e-03 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 38.95 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 81 WQPDVVHSHltksD--------LVAQLAARMRGLPRLV-TLHNAA---PWRKK-----RLPARLYH-----------WVV 132
Cdd:PRK00654 117 PRPDIVHAH----DwhtglipaLLKEKYWRGYPDIKTVfTIHNLAyqgLFPAEilgelGLPAEAFHleglefygqisFLK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 133 GkpdALIAvtplvADHV-------AR------YG----GVPRENIEV---IQNGVDLSRFSPE-------NATPLDLS-- 183
Cdd:PRK00654 193 A---GLYY-----ADRVttvsptyAReittpeFGygleGLLRARSGKlsgILNGIDYDIWNPEtdpllaaNYSADDLEgk 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 184 ---------QFGVPK-DAVVIAKVGRLNVQKDhANFLRAAA--ILARkDPRahfLVV---GDGELMTQSQELARQLglgP 248
Cdd:PRK00654 265 aenkralqeRFGLPDdDAPLFAMVSRLTEQKG-LDLVLEALpeLLEQ-GGQ---LVLlgtGDPELEEAFRALAARY---P 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 960397608 249 DR----LTFTgnirqmpELLS-----AIDIFMLASAWE--GL-PMVlleAMAMG-LPVVStAVGGVPDLIANG 308
Cdd:PRK00654 337 GKvgvqIGYD-------EALAhriyaGADMFLMPSRFEpcGLtQLY---ALRYGtLPIVR-RTGGLADTVIDY 398
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
76-300 |
5.24e-03 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 38.92 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 76 QLMRR--WQPDVVHSHltksD----LVAQLAA------RMRGLPRLVTLHNAA-----PWRKKR---LPARLYHwvvgkP 135
Cdd:COG0297 121 ELLKGldWKPDIIHCH----DwqtgLIPALLKtryaddPFKRIKTVFTIHNLAyqgifPAEILEllgLPPELFT-----P 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 136 DALI---AVTPL-----VADHV-------AR------YG----GVPRENIEV---IQNGVDLSRFSPE-------NATPL 180
Cdd:COG0297 192 DGLEfygQINFLkagivYADRVttvsptyAReiqtpeFGegldGLLRARSGKlsgILNGIDYDVWNPAtdpylpaNYSAD 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960397608 181 DLS-----------QFGVP--KDAVVIAKVGRLNVQK--DhanfLRAAAI--LARKDprAHFLVVGDGE--LMTQSQELA 241
Cdd:COG0297 272 DLEgkaankaalqeELGLPvdPDAPLIGMVSRLTEQKglD----LLLEALdeLLEED--VQLVVLGSGDpeYEEAFRELA 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 960397608 242 RQLglgPDRLTFtgNIRQMPEL----LSAIDIFMLASAWE--GLPMvlLEAMAMG-LPVVStAVGG 300
Cdd:COG0297 346 ARY---PGRVAV--YIGYDEALahriYAGADFFLMPSRFEpcGLNQ--MYALRYGtVPIVR-RTGG 403
|
|
| |
