NCBI Conserved Domain Search

Conserved domains on [gi|808669993|emb|CQD05163|]

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group 1 glycosyl transferase [Mycolicibacterium conceptionense]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

Glycosyltransferase_GTB-type super family

cl10013

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...

13-378

3.92e-71

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.

The actual alignment was detected with superfamily member cd03821:

Pssm-ID: 471961 [Multi-domain] Cd Length: 377 Bit Score: 227.25 E-value: 3.92e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  13 VLHVVTLITPdgAYGGPVRVAFNQSRQLRAAGHRTLVAGAVRGYPQIPTVLDGV--PVRLAKARSIIPRLGFS-GLLAPA 89
Cdd:cd03821    2 ILHVTPSISP--KAGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEENGRyiPPQDGFASIPLLRQGAGrTDFSPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  90 LLVWMVRNRRSFDVVHVHLARDLITLPAAAIALILRKRVIVQTHGMITDSSHPIAPILDRVLTRPILRR----AAAVLYL 165
Cdd:cd03821   80 LPNWLRRNLREYDVVHIHGVWTYTSLAACKLARRRGIPYVVSPHGMLDPWALQQKHWKKRIALHLIERRnlnnAALVHFT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 166 TEDERAALLRVQPEAAVRHLRNGV--PGYEGTPAAARADPTA-GRVEVLYLARLQVRKRPALFVKAAARLLAAGCDARFT 242
Cdd:cd03821  160 SEQEADELRRFGLEPPIAVIPNGVdiPEFDPGLRDRRKHNGLeDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 243 LVGPDEGEGPEVLDTIMRSDIRfDEIRWEGALPPDRTVLRMAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLAD 322
Cdd:cd03821  240 IAGPDDGAYPAFLQLQSSLGLG-DRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSE 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 808669993 323 TVRAsGSGLVVDESEDALMEAMRTLIIDQRLREKMSAAARQTAAAV--FSMEAIARDL 378
Cdd:cd03821  319 LVEA-GCGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRARQVEenFSWEAVAGQL 375

Name

Accession

Description

Interval

E-value

GT4_Bme6-like

cd03821

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...

13-378

3.92e-71

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: 227.25 E-value: 3.92e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  13 VLHVVTLITPdgAYGGPVRVAFNQSRQLRAAGHRTLVAGAVRGYPQIPTVLDGV--PVRLAKARSIIPRLGFS-GLLAPA 89
Cdd:cd03821    2 ILHVTPSISP--KAGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEENGRyiPPQDGFASIPLLRQGAGrTDFSPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  90 LLVWMVRNRRSFDVVHVHLARDLITLPAAAIALILRKRVIVQTHGMITDSSHPIAPILDRVLTRPILRR----AAAVLYL 165
Cdd:cd03821   80 LPNWLRRNLREYDVVHIHGVWTYTSLAACKLARRRGIPYVVSPHGMLDPWALQQKHWKKRIALHLIERRnlnnAALVHFT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 166 TEDERAALLRVQPEAAVRHLRNGV--PGYEGTPAAARADPTA-GRVEVLYLARLQVRKRPALFVKAAARLLAAGCDARFT 242
Cdd:cd03821  160 SEQEADELRRFGLEPPIAVIPNGVdiPEFDPGLRDRRKHNGLeDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 243 LVGPDEGEGPEVLDTIMRSDIRfDEIRWEGALPPDRTVLRMAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLAD 322
Cdd:cd03821  240 IAGPDDGAYPAFLQLQSSLGLG-DRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSE 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 808669993 323 TVRAsGSGLVVDESEDALMEAMRTLIIDQRLREKMSAAARQTAAAV--FSMEAIARDL 378
Cdd:cd03821  319 LVEA-GCGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRARQVEenFSWEAVAGQL 375

Glycos_transf_1

pfam00534

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...

210-358

1.26e-27

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: 106.59 E-value: 1.26e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  210 VLYLARLQVRKRPALFVKAAARLLAAGCDARFTLVGpdEGEGPEVLDTIMRSDIRFDEIRWEGALPPDRTVLRMAAASIY 289
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAG--DGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVF 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  290 VLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVDE-SEDALMEAMRTLIIDQRLREKMS 358
Cdd:pfam00534  83 VLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPnNAEALAEAIDKLLEDEELRERLG 152

RfaB

COG0438

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...

283-383

8.39e-21

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 86.97 E-value: 8.39e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 283 MAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVD-ESEDALMEAMRTLIIDQRLREKMSAAA 361
Cdd:COG0438   18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPpGDPEALAEAILRLLEDPELRRRLGEAA 97

                         90       100
                 ....*....|....*....|..
gi 808669993 362 RQTAAAVFSMEAIARDLTAVYA 383
Cdd:COG0438   98 RERAEERFSWEAIAERLLALYE 119

stp2

TIGR03088

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...

149-382

1.93e-11

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: 64.74 E-value: 1.93e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  149 RVLTRPILRRAAAVLYLTEDERAALLRVQPeAAVRHLRNGV------PGYEGTPAAARADPTAGR-VEVLYLARLQVRKR 221
Cdd:TIGR03088 130 RRLYRPLIHHYVAVSRDLEDWLRGPVKVPP-AKIHQIYNGVdterfhPSRGDRSPILPPDFFADEsVVVGTVGRLQAVKD 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  222 PALFVKAAARLLAAGCD----ARFTLVGpdEGEGPEVLDTIMRSDiRFDEIRWegaLPPDRTVLR--MAAASIYVLPSVD 295
Cdd:TIGR03088 209 QPTLVRAFALLVRQLPEgaerLRLVIVG--DGPARGACEQMVRAA-GLAHLVW---LPGERDDVPalMQALDLFVLPSLA 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  296 EPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVDESE-DALMEAMRTLIIDQRLREKMSAAARQTAAAVFSMEAI 374
Cdd:TIGR03088 283 EGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPGDaVALARALQPYVSDPAARRAHGAAGRARAEQQFSINAM 362


                  ....*...
gi 808669993  375 ARDLTAVY 382
Cdd:TIGR03088 363 VAAYAGLY 370

PLN02871

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase

77-357

1.02e-06

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase

Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 50.48 E-value: 1.02e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  77 IPRLGFSGLLAPallVWMVrnrrsfdVVHVHLARDLITLPAAAIALILR-------KRVIVQTHGMITDSSHPiapildr 149
Cdd:PLN02871 183 IPRYTFSWLVKP---MWDI-------IRFLHRAADLTLVTSPALGKELEaagvtaaNRIRVWNKGVDSESFHP------- 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 150 vltrpilrraaavlyltederaallRVQPEAAVRHLRNGVPGyegtpaaaraDPTagrveVLYLARLQVRKRpalfVKAA 229
Cdd:PLN02871 246 -------------------------RFRSEEMRARLSGGEPE----------KPL-----IVYVGRLGAEKN----LDFL 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 230 ARLLAAGCDARFTLVGpdegEGPEvldtimRSDIR--FDEIR--WEGALPPDRTVLRMAAASIYVLPSVDEPFPMSVLEA 305
Cdd:PLN02871 282 KRVMERLPGARLAFVG----DGPY------REELEkmFAGTPtvFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEA 351

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 808669993 306 MSVGLPVVITESCGLADTV---RASGSGLVVDESE-DALMEAMRTLIIDQRLREKM 357
Cdd:PLN02871 352 MASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDvDDCVEKLETLLADPELRERM 407

Name

Accession

Description

Interval

E-value

GT4_Bme6-like

cd03821

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...

13-378

3.92e-71

Pssm-ID: 340848 [Multi-domain] Cd Length: 377 Bit Score: 227.25 E-value: 3.92e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  13 VLHVVTLITPdgAYGGPVRVAFNQSRQLRAAGHRTLVAGAVRGYPQIPTVLDGV--PVRLAKARSIIPRLGFS-GLLAPA 89
Cdd:cd03821    2 ILHVTPSISP--KAGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEENGRyiPPQDGFASIPLLRQGAGrTDFSPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  90 LLVWMVRNRRSFDVVHVHLARDLITLPAAAIALILRKRVIVQTHGMITDSSHPIAPILDRVLTRPILRR----AAAVLYL 165
Cdd:cd03821   80 LPNWLRRNLREYDVVHIHGVWTYTSLAACKLARRRGIPYVVSPHGMLDPWALQQKHWKKRIALHLIERRnlnnAALVHFT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 166 TEDERAALLRVQPEAAVRHLRNGV--PGYEGTPAAARADPTA-GRVEVLYLARLQVRKRPALFVKAAARLLAAGCDARFT 242
Cdd:cd03821  160 SEQEADELRRFGLEPPIAVIPNGVdiPEFDPGLRDRRKHNGLeDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 243 LVGPDEGEGPEVLDTIMRSDIRfDEIRWEGALPPDRTVLRMAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLAD 322
Cdd:cd03821  240 IAGPDDGAYPAFLQLQSSLGLG-DRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSE 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 808669993 323 TVRAsGSGLVVDESEDALMEAMRTLIIDQRLREKMSAAARQTAAAV--FSMEAIARDL 378
Cdd:cd03821  319 LVEA-GCGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRARQVEenFSWEAVAGQL 375

GT4_PimA-like

cd03801

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...

17-382

2.52e-46

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: 162.32 E-value: 2.52e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  17 VTLITPDG--AYGGPVRVAFNQSRQLRAAGHRTLVAGAVRGYPQIPTVLDGVPVRLAKARSIIPRlgfsgllAPALL--V 92
Cdd:cd03801    2 ILLLSPELppPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLR-------ARRLLreL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  93 WMVRNRRSFDVVHVHLARDLitLPAAAIALILRKRVIVQTHGMITDSSHPIAPILDRVLTR--PILRRAAAVLYLTEDER 170
Cdd:cd03801   75 RPLLRLRKFDVVHAHGLLAA--LLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLARaeALLRRADAVIAVSEALR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 171 AALLR--VQPEAAVRHLRNGV-PGYEGTPAAARADPTAGRVEVLYLARLQVRKRPALFVKAAARLLAAGCDARFTLVGPD 247
Cdd:cd03801  153 DELRAlgGIPPEKIVVIPNGVdLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 248 EGEGPEVLDTIMRSDirfDEIRWEGALPPDRTVLRMAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRAS 327
Cdd:cd03801  233 GPLRAELEELELGLG---DRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDG 309

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 808669993 328 GSGLVVD-ESEDALMEAMRTLIIDQRLREKMSAAARQTAAAVFSMEAIARDLTAVY 382
Cdd:cd03801  310 EGGLVVPpDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365

GT4_WlbH-like

cd03798

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...

16-357

5.08e-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: 121.33 E-value: 5.08e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  16 VVTLITPDGAYGGPVRVAFNQSRQLRAAGHRTLVAGAVRGYPQI-----PTVLDGVPVRLAKARSI--IPRLGFSGLLAP 88
Cdd:cd03798    3 ILTNIYPNANSPGRGIFVRRQVRALSRRGVDVEVLAPAPWGPAAarllrKLLGEAVPPRDGRRLLPlkPRLRLLAPLRAP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  89 ALL-VWMVRNRRSFDVVHVHLArdlitLPAAAIALILRKR----VIVQTHGmiTD-SSHPIAPILdRVLTRPILRRAAAV 162
Cdd:cd03798   83 SLAkLLKRRRRGPPDLIHAHFA-----YPAGFAAALLARLygvpYVVTEHG--SDiNVFPPRSLL-RKLLRWALRRAARV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 163 LYLTED--ERAALLRVQPEAAVRhLRNGVPGYEGTPAAARADPTAGRVEVLYLARLQVRKRPALFVKAAARLLAAGCDAR 240
Cdd:cd03798  155 IAVSKAlaEELVALGVPRDRVDV-IPNGVDPARFQPEDRGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVV 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 241 FTLVGpdEGEGPEVLDTIMRSDIRFDEIRWEGALPPDRTVLRMAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGL 320
Cdd:cd03798  234 LLIVG--DGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGI 311

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 808669993 321 ADTVRASGSGLVV-DESEDALMEAMRTLIIDQRLREKM 357
Cdd:cd03798  312 PEVVGDPETGLLVpPGDADALAAALRRALAEPYLRELG 349

GT4_GT28_WabH-like

cd03811

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...

17-356

7.40e-29

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: 115.15 E-value: 7.40e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  17 VTLITPDGAYGGPVRVAFNQSRQLRAAGHR-TLVAGAVRGYPQIPTVLDgVPVRLAKARSIIPRLGFSGLLAPALLVWMv 95
Cdd:cd03811    2 ILFVIPSLSGGGAERVLLNLANALDKRGYDvTLVLLRDEGDLDKQLNGD-VKLIRLLIRVLKLIKLGLLKAILKLKRIL- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  96 rNRRSFDVVHVHLARDLITlpAAAIALILRKRVIVQtHGMITDSSHPIAPILdrvLTRPILRRAAAVLYLTEDERAALLR 175
Cdd:cd03811   80 -KRAKPDVVISFLGFATYI--VAKLAAARSKVIAWI-HSSLSKLYYLKKKLL---LKLKLYKKADKIVCVSKGIKEDLIR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 176 V--QPEAAVRHLRNGVPgYEGTPAAARAD----PTAGRVeVLYLARLQVRKRPALFVKAAARLLAAGCDARFTLVGpdeg 249
Cdd:cd03811  153 LgpSPPEKIEVIYNPID-IDRIRALAKEPilnePEDGPV-ILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILG---- 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 250 EGP---EVLDTIMRSDIRfDEIRWEGALPPdrtVLR-MAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVR 325
Cdd:cd03811  227 DGPlreELEKLAKELGLA-ERVIFLGFQSN---PYPyLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILD 302

                        330       340       350
                 ....*....|....*....|....*....|.
gi 808669993 326 ASGSGLVVDESEDALMEAMRTLIIDQRLREK 356
Cdd:cd03811  303 DGENGLLVPDGDAAALAGILAALLQKKLDAA 333

Glycos_transf_1

pfam00534

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...

210-358

1.26e-27

Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 106.59 E-value: 1.26e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  210 VLYLARLQVRKRPALFVKAAARLLAAGCDARFTLVGpdEGEGPEVLDTIMRSDIRFDEIRWEGALPPDRTVLRMAAASIY 289
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAG--DGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVF 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  290 VLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVDE-SEDALMEAMRTLIIDQRLREKMS 358
Cdd:pfam00534  83 VLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPnNAEALAEAIDKLLEDEELRERLG 152

GT4_CapM-like

cd03808

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...

101-378

1.80e-26

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: 108.45 E-value: 1.80e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 101 FDVVHVHLARDLItLPAAAIALILRKRVIVQTHGM-ITDSSHPIAPILDRVLTRPILRRAAAVLYLTEDERAALLR---V 176
Cdd:cd03808   82 PDIVHCHTPKPGI-LGRLAARLAGVPKVIYTVHGLgFVFTEGKLLRLLYLLLEKLALLFTDKVIFVNEDDRDLAIKkgiI 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 177 QPEAAVRHLRNGVPgyEGTPAAARADPTAGRVEVLYLARLQVRKRPALFVKAAARLLAAGCDARFTLVGPDEGEGPevlD 256
Cdd:cd03808  161 KKKKTVLIPGSGVD--LDRFQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENP---S 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 257 TIMRSDIRFDE-IRWEGALppdRTVLR-MAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVD 334
Cdd:cd03808  236 EILIEKLGLEGrIEFLGFR---SDVPElLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVP 312

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 808669993 335 -ESEDALMEAMRTLIIDQRLREKMSAAARQTAAAVFSMEAIARDL 378
Cdd:cd03808  313 pGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKL 357

GT4_WavL-like

cd03819

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...

27-357

1.93e-21

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: 94.34 E-value: 1.93e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  27 GGPVRVAFNQSRQLRAAGHRTLVAGA----VRGYPQIPTVLDGVPVRLAKArsiiprlgfsglLAPALLVWMVRNRRSFD 102
Cdd:cd03819   11 GGAETYILDLARALAERGHRVLVVTAggplLPRLRQIGIGLPGLKVPLLRA------------LLGNVRLARLIRRERID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 103 VVHVHLARdlitlPAAAIAL---ILRKRVIVQTHGmitdsSHPIAPILDRVLTRPILR--RAAAVLYLTEDERAALLRVq 177
Cdd:cd03819   79 LIHAHSRA-----PAWLGWLasrLTGVPLVTTVHG-----SYLATYHPKDFALAVRARgdRVIAVSELVRDHLIEALGV- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 178 PEAAVRHLRNGVPGYEGTPAAARADPTAGRVE-----VLYLARLQVRKRPALFVKAAARLlAAGCDARFTLVGpDEGEGP 252
Cdd:cd03819  148 DPERIRVIPNGVDTDRFPPEAEAEERAQLGLPegkpvVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAG-DGPERD 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 253 EVLDTIMRSDIRfDEIRWEGALPPDRTVlrMAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLV 332
Cdd:cd03819  226 EIRRLVERLGLR-DRVTFTGFREDVPAA--LAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLL 302

                        330       340
                 ....*....|....*....|....*.
gi 808669993 333 VDESED-ALMEAMRTLIIDQRLREKM 357
Cdd:cd03819  303 VPPGDAeALADAIRAAKLLPEAREKL 328

RfaB

COG0438

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...

283-383

8.39e-21

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 86.97 E-value: 8.39e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 283 MAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVD-ESEDALMEAMRTLIIDQRLREKMSAAA 361
Cdd:COG0438   18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPpGDPEALAEAILRLLEDPELRRRLGEAA 97

                         90       100
                 ....*....|....*....|..
gi 808669993 362 RQTAAAVFSMEAIARDLTAVYA 383
Cdd:COG0438   98 RERAEERFSWEAIAERLLALYE 119

Glyco_trans_1_4

pfam13692

Glycosyl transferases group 1;

210-350

5.06e-20

Glycosyl transferases group 1;

Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 85.26 E-value: 5.06e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  210 VLYLARLQVR-KRPALFVKAAARLLAAGCDARFTLVGpdEGEGPEVLDTIMRSDirfDEIRWEGALPPDRTVLrmAAASI 288
Cdd:pfam13692   4 ILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVG--DGPEEELEELAAGLE---DRVIFTGFVEDLAELL--AAADV 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808669993  289 YVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVDESEDALMEAMRTLIID 350
Cdd:pfam13692  77 FVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENGLLVPPGDPEALAEAILRLLED 138

GT4_sucrose_synthase

cd03800

sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...

210-378

7.78e-20

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.

Pssm-ID: 340830 [Multi-domain] Cd Length: 398 Bit Score: 89.99 E-value: 7.78e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 210 VLYLARLQVRKRPALFVKAAARLLAAGCDARFTLVGPDEGEG----PEVLDTIMRSDIRFDEIRWEGALPPDRTVLRMAA 285
Cdd:cd03800  223 VLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGGPSDDPlsmdREELAELAEELGLIDRVRFPGRVSRDDLPELYRA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 286 ASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVD-ESEDALMEAMRTLIIDQRLREKMSAAARQT 364
Cdd:cd03800  303 ADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDpHDPEALAAALRRLLDDPALWQRLSRAGLER 382

                        170
                 ....*....|....
gi 808669993 365 AAAVFSMEAIARDL 378
Cdd:cd03800  383 ARAHYTWESVADQL 396

GT4_WbnK-like

cd03807

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...

80-376

2.59e-18

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: 85.45 E-value: 2.59e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  80 LGFSGLLAPALLVWMVRNRRSF--DVVHVHLAR-DLITLPAAaiaLILRKRVIVQTHGMITDSshPIAPILDRVLTRPIL 156
Cdd:cd03807   57 LGLSSGKDPGVLLRLAKLIRKRnpDVVHTWMYHaDLIGGLAA---KLAGGVKVIWSVRSSNIP--QRLTRLVRKLCLLLS 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 157 RRAAAVLYLTEDERAALLRVQ-PEAAVRHLRNGVPGYEGTPAAARADPTAGRVE-------VLYLARLQVRKRPALFVKA 228
Cdd:cd03807  132 KFSPATVANSSAVAEFHQEQGyAKNKIVVIYNGIDLFKLSPDDASRARARRRLGlaedrrvIGIVGRLHPVKDHSDLLRA 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 229 AARLLAAGCDARFTLVGpdegEGPEvldtimRSDIRfdEIRWEGALPpDRTVLR---------MAAASIYVLPSVDEPFP 299
Cdd:cd03807  212 AALLVETHPDLRLLLVG----RGPE------RPNLE--RLLLELGLE-DRVHLLgersdvpalLPAMDIFVLSSRTEGFP 278

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808669993 300 MSVLEAMSVGLPVVITESCGLADTVRASGSGLVVDESEDALMEAMRTLIIDQRLREKMSAAARQTAAAVFSMEAIAR 376
Cdd:cd03807  279 NALLEAMACGLPVVATDVGGAAELVDDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVR 355

GT4_WbuB-like

cd03794

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...

38-378

3.50e-17

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.

Pssm-ID: 340825 [Multi-domain] Cd Length: 391 Bit Score: 82.39 E-value: 3.50e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  38 RQLRAAGHRTLVAGAVRGYPQIP------TVLDGVPVRLAKARSI----IPRLGFSGLLAP-ALLVWMVRNRRSFDVVHV 106
Cdd:cd03794   25 KELVRRGHEVTVLTPSPNYPLGRifagatETKDGIRVIRVKLGPIkkngLIRRLLNYLSFAlAALLKLLVREERPDVIIA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 107 HLARDLITLPAAAIALILRKRVIVQTH----------GMITdSSHPIAPIldRVLTRPILRRAAAVLYLTEDERAALL-R 175
Cdd:cd03794  105 YSPPITLGLAALLLKKLRGAPFILDVRdlwpeslialGVLK-KGSLLKLL--KKLERKLYRLADAIIVLSPGLKEYLLrK 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 176 VQPEAAVRHLRNGV----PGYEGTPAAARADPTAGRVEVLYLARLQVRKRPALFVKAAARLlAAGCDARFTLVGpDEGEG 251
Cdd:cd03794  182 GVPKEKIIVIPNWAdleeFKPPPKDELRKKLGLDDKFVVVYAGNIGKAQGLETLLEAAERL-KRRPDIRFLFVG-DGDEK 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 252 PEVLDTIMRSDIrfDEIRWEGALPPDRTVLRMAAASIYVLPSVDEP-----FPMSVLEAMSVGLPVVITESCGLADTVRA 326
Cdd:cd03794  260 ERLKELAKARGL--DNVTFLGRVPKEEVPELLSAADVGLVPLKDNPanrgsSPSKLFEYMAAGKPILASDDGGSDLAVEI 337

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 808669993 327 SGSGLVVD-ESEDALMEAMRTLIIDQRLREKMSAAARQTAAAVFSMEAIARDL 378
Cdd:cd03794  338 NGCGLVVEpGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRL 390

Glycosyltransferase_GTB-type

cd01635

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...

211-333

3.89e-17

Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 79.76 E-value: 3.89e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 211 LYLARLQVRKRPALFVKAAARLLAAGCDARFTLVGPDeGEGPEVLDTIMRSDIRFDEIRWEGALPPDRTVLRMAAASIYV 290
Cdd:cd01635  114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGG-GEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFV 192

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 808669993 291 LPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVV 333
Cdd:cd01635  193 LPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235

GT4_UGDG-like

cd03817

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...

27-358

9.02e-17

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: 80.79 E-value: 9.02e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  27 GGPVRVAFNQSRQLRAAGHR-TLVAGAvrgYPQIPTVLDGVPVR-LAKARSIIPRLGFSGLLAPALLVWMVRnrRSFDVV 104
Cdd:cd03817   14 NGVATSVRNLARALEKRGHEvYVITPS---DPGAEDEEEVVRYRsFSIPIRKYHRQHIPFPFKKAVIDRIKE--LGPDII 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 105 HVHLARDLITLpAAAIALILRKRVIVQTHGMITDSSH--PIAPILDRVLTRPI----LRRAAAVLYLTEDERAALLRVQP 178
Cdd:cd03817   89 HTHTPFSLGKL-GLRIARKLKIPIVHTYHTMYEDYLHyiPKGKLLVKAVVRKLvrrfYNHTDAVIAPSEKIKDTLREYGV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 179 EAAVRHLRNGVPgyegTPAAARADPTAGRVE---------VLYLARLQVRKRPALFVKAAARLLAAGcDARFTLVGpdeg 249
Cdd:cd03817  168 KGPIEVIPNGID----LDKFEKPLNTEERRKlglppdepiLLYVGRLAKEKNIDFLLRAFAELKKEP-NIKLVIVG---- 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 250 EGPE--VLDTIMRSDIRFDEIRWEGALPPDRTVLRMAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRAS 327
Cdd:cd03817  239 DGPEreELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDG 318

                        330       340       350
                 ....*....|....*....|....*....|.
gi 808669993 328 GSGLVVDESEDALMEAMRTLIIDQRLREKMS 358
Cdd:cd03817  319 ENGFLFEPNDETLAEKLLHLRENLELLRKLS 349

GT4-like

cd03814

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...

25-383

1.69e-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: 80.03 E-value: 1.69e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  25 AYGGPVRVAFNQSRQLRAAGHRTLVAGAVRGYPQIPTVLDGVPVRLakarsiIPRLGFSGL-LAPALLVWMVRNRRSFDV 103
Cdd:cd03814   12 QVNGVVRTLERLVDHLRRRGHEVRVVAPGPFDEAESAEGRVVSVPS------FPLPFYPEYrLALPLPRRVRRLIKEFQP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 104 VHVHLA-RDLITLPAAAIALILRKRVIVQTHgmiTDSSHPIAPILDRVLTRPIL-------RRAAAVLYLTEDERAALLR 175
Cdd:cd03814   86 DIIHIAtPGPLGLAALRAARRLGLPVVTSYH---TDFPEYLSYYTLGPLSWLAWaylrwfhNPFDTTLVPSPSIARELEG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 176 VQPEAaVRHLRNGV------PGyEGTPAAARADPTAGRVEVLYLARLQVRKRPALFVKAAARLlAAGCDARFTLVGpdEG 249
Cdd:cd03814  163 HGFER-VRLWPRGVdtelfhPS-RRDAALRRRLGPPGRPLLLYVGRLAPEKNLEALLDADLPL-AASPPVRLVVVG--DG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 250 EGPEVLDTimrsdiRFDEIRWEGALppDRTVLRMAAAS--IYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRAS 327
Cdd:cd03814  238 PARAELEA------RGPDVIFTGFL--TGEELARAYASadVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPG 309

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 808669993 328 GSGLVVDESEDALM-EAMRTLIIDQRLREKMSAAARQTAAAvFSMEAIARDLTAVYA 383
Cdd:cd03814  310 GTGALVEPGDAAAFaAALRALLEDPELRRRMAARARAEAER-YSWEAFLDNLLDYYA 365

GT4-like

cd05844

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...

79-358

7.25e-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: 72.10 E-value: 7.25e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  79 RLGFSGLLAPALLVWMVRNRRS-----------FDVVHVHLARDLITlpAAAIALILRKRVIVQTHGM-ITDSSH----- 141
Cdd:cd05844   49 ALGGSGPLRWLRQMAQRLLGWSaprlggaaglaPALVHAHFGRDGVY--ALPLARALGVPLVVTFHGFdITTSRAwlaas 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 142 PIAPILDRVLTRPILRRAAAVLYLTEDERAALLRVQPEAAVRHLRNgvPGYEGTPAAARADPTAGRVeVLYLARLQVRKR 221
Cdd:cd05844  127 PGWPSQFQRHRRALQRPAALFVAVSGFIRDRLLARGLPAERIHVHY--IGIDPAKFAPRDPAERAPT-ILFVGRLVEKKG 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 222 PALFVKAAARLLAAGCDARFTLVGpdegEGPEVLDTIMRSDiRFDEIRWEGALPPDRTVLRMAAASIYVLPSV------D 295
Cdd:cd05844  204 CDVLIEAFRRLAARHPTARLVIAG----DGPLRPALQALAA-ALGRVRFLGALPHAEVQDWMRRAEIFCLPSVtaasgdS 278

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808669993 296 EPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVDESE-DALMEAMRTLIIDQRLREKMS 358
Cdd:cd05844  279 EGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDvDALADALQALLADRALADRMG 342

GT4_AmsD-like

cd03820

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...

283-374

9.36e-14

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: 71.88 E-value: 9.36e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 283 MAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITES-CGLADTVRASGSGLVVD-ESEDALMEAMRTLIIDQRLREKMSaA 360
Cdd:cd03820  253 YANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCpTGPSEIIEDGENGLLVPnGDVDALAEALLRLMEDEELRKKMG-K 331

                         90
                 ....*....|....
gi 808669993 361 ARQTAAAVFSMEAI 374
Cdd:cd03820  332 NARKNAERFSIEKI 345

GT4_ExpE7-like

cd03823

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...

13-358

1.50e-13

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: 71.21 E-value: 1.50e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  13 VLHVVTLITPDgAYGGPVRVAFNQSRQLRAAGHRTLVAGAVRGYPQIPTVL-DGVPVRLAKARSIIPRLGFSGLLA---- 87
Cdd:cd03823    2 ILLVNSLYPPQ-RVGGAEISVHDLAEALVAEGHEVAVLTAGVGPPGQATVArSVVRYRRAPDETLPLALKRRGYELfety 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  88 -PALLVWMVR--NRRSFDVVHVHlarDLITLPAAAIALIL-RKRVIVQThgmitdsSHPIAPILDRVltRPILRRAAAVL 163
Cdd:cd03823   81 nPGLRRLLARllEDFRPDVVHTH---NLSGLGASLLDAARdLGIPVVHT-------LHDYWLLCPRQ--FLFKKGGDAVL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 164 YLTEDERAALLRV-QPEAAVRHLRNGVPGyeGTPAAARADPTAGRVEVLYLARLQVRKRPALFVKAAARLLAAgcDARFT 242
Cdd:cd03823  149 APSRFTANLHEANgLFSARISVIPNAVEP--DLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLPRE--DIELV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 243 LVGpdegEGPEvldtimrSDIRFDE----IRWEGALPPDRTVLRMAAASIYVLPSV-DEPFPMSVLEAMSVGLPVVITES 317
Cdd:cd03823  225 IAG----HGPL-------SDERQIEggrrIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDL 293

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 808669993 318 CGLADTVRASGSGLVVDESE-DALMEAMRTLIIDQRLREKMS 358
Cdd:cd03823  294 GGIAELIQPGVNGLLFAPGDaEDLAAAMRRLLTDPALLERLR 335

GT4_MtfB-like

cd03809

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...

26-376

3.32e-13

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: 70.08 E-value: 3.32e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  26 YGGPVRVAFNQSRQLRAAGH--RTLVAGAVRGYPQIPTVLDgvPVRLAKARSIIPRLGFSGLLAPALLVWMVRNRRSFDV 103
Cdd:cd03809   13 LTGIGRYTRELLKALAKNDPdeSVLAVPPLPGELLRLLREY--PELSLGVIKIKLWRELALLRWLQILLPKKDKPDLLHS 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 104 VHvhlardlITLPAaaiaLILRKRVIVQTHGMIT----DSSHPIAPILDRVLTRPILRRAAAVLYLTE---DERAALLRV 176
Cdd:cd03809   91 PH-------NTAPL----LLKGCPQVVTIHDLIPlrypEFFPKRFRLYYRLLLPISLRRADAIITVSEatrDDIIKFYGV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 177 QPE--AAVRHLRNGVPGYEGTPAAARA-----DPTagrveVLYLARLQVRKRPALFVKAAARLLAAGCDARFTLVGPDEG 249
Cdd:cd03809  160 PPEkiVVIPLGVDPSFFPPESAAVLIAkyllpEPY-----FLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGW 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 250 EGPEVLDTIMRSDIRfDEIRWEGALPPDRTVLRMAAASIYVLPSVDEPFPMSVLEAMSVGLPVVitescgLADT-----V 324
Cdd:cd03809  235 EDEELLDLVKKLGLG-GRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVI------ASNIsvlpeV 307

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 808669993 325 rASGSGLVVD-ESEDALMEAMRTLIIDQRLREKMSAAARQTAAAvFSMEAIAR 376
Cdd:cd03809  308 -AGDAALYFDpLDPESIADAILRLLEDPSLREELIRKGLERAKK-FSWEKTAE 358

stp2

TIGR03088

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...

149-382

1.93e-11

Pssm-ID: 132132 [Multi-domain] Cd Length: 374 Bit Score: 64.74 E-value: 1.93e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  149 RVLTRPILRRAAAVLYLTEDERAALLRVQPeAAVRHLRNGV------PGYEGTPAAARADPTAGR-VEVLYLARLQVRKR 221
Cdd:TIGR03088 130 RRLYRPLIHHYVAVSRDLEDWLRGPVKVPP-AKIHQIYNGVdterfhPSRGDRSPILPPDFFADEsVVVGTVGRLQAVKD 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  222 PALFVKAAARLLAAGCD----ARFTLVGpdEGEGPEVLDTIMRSDiRFDEIRWegaLPPDRTVLR--MAAASIYVLPSVD 295
Cdd:TIGR03088 209 QPTLVRAFALLVRQLPEgaerLRLVIVG--DGPARGACEQMVRAA-GLAHLVW---LPGERDDVPalMQALDLFVLPSLA 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  296 EPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVDESE-DALMEAMRTLIIDQRLREKMSAAARQTAAAVFSMEAI 374
Cdd:TIGR03088 283 EGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPGDaVALARALQPYVSDPAARRAHGAAGRARAEQQFSINAM 362


                  ....*...
gi 808669993  375 ARDLTAVY 382
Cdd:TIGR03088 363 VAAYAGLY 370

GT4_WfcD-like

cd03795

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...

13-358

2.30e-11

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: 64.60 E-value: 2.30e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  13 VLHVVTLITPDgaYGGPVRVAFNQSRQLRAAGHRT--LVAGAVRGYPQIPTvlDGVPVRLAKARSIIPRLGFSgllaPAL 90
Cdd:cd03795    2 VLHVFKFYYPD--IGGIEQVIYDLAEGLKKKGIEVdvLCFSKEKETPEKEE--NGIRIHRVKSFLNVASTPFS----PSY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  91 LVWMVRNRRSFDVVHVHlardlITLPAAAIALIL---RKRVIVQTHGMITDSSHpIAPILDRVLTRpILRRAAAVL---- 163
Cdd:cd03795   74 IKRFKKLAKEYDIIHYH-----FPNPLADLLLFFsgaKKPVVVHWHSDIVKQKK-LLKLYKPLMTR-FLRRADRIIatsp 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 164 -YLTEDEraALLRVQPEAAVRHL---RNGVPGYEGTPAAARaDPTAGRVEVLYLARLQVRKRPALFVKAAARLlaagcDA 239
Cdd:cd03795  147 nYVETSP--TLREFKNKVRVIPLgidKNVYNIPRVDFENIK-REKKGKKIFLFIGRLVYYKGLDYLIEAAQYL-----NY 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 240 RFTLVGpdegEGPEVLDtiMRSDIRF---DEIRWEGALPPDRTVLRMAAASIYVLPSV--DEPFPMSVLEAMSVGLPVVI 314
Cdd:cd03795  219 PIVIGG----EGPLKPD--LEAQIELnllDNVKFLGRVDDEEKVIYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVIS 292

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 808669993 315 TE-SCGLADTVRASGSGLVVD-ESEDALMEAMRTLIIDQRLREKMS 358
Cdd:cd03795  293 TNiGTGVPYVNNNGETGLVVPpKDPDALAEAIDKLLSDEELRESYG 338

GT4_AmsK-like

cd03799

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...

196-357

1.74e-10

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: 61.70 E-value: 1.74e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 196 PAAARADPTAGRVEVLYLARLQVRKRPALFVKAAARLLAAGCDARFTLVGpdEGEGPEVLDTIMRSDIRFDEIRWEGALP 275
Cdd:cd03799  163 RFKPRYLPLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIG--DGDLKEQLQQLIQELNIGDCVKLLGWKP 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 276 PDRTVLRMAAASIYVLPSV-----DEPFPMSVL-EAMSVGLPVVITESCGLADTVRASGSGLVVDESE-DALMEAMRTLI 348
Cdd:cd03799  241 QEEIIEILDEADIFIAPSVtaadgDQDGPPNTLkEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDaEAIAEKLTYLI 320


                 ....*....
gi 808669993 349 IDQRLREKM 357
Cdd:cd03799  321 EHPAIWPEM 329

Glyco_trans_4_4

pfam13579

Glycosyl transferase 4-like domain;

27-188

3.69e-10

Glycosyl transferase 4-like domain;

Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 58.18 E-value: 3.69e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993   27 GGPVRVAFNQSRQLRAAGHRTLVAGAVRGYPQIPTVLDGVPVRLAKARsiiPRLGFSGLLAPALLVWMVRNRRSFDVVHV 106
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPVP---PRPSPLADLAALRRLRRLLRAERPDVVHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  107 HLArdLITLPAAAIALILRKRVIVQTHGMITDSSHPIAPILDRVLTRPILRRAAAVLYLTEDERAALLRVQPEAA-VRHL 185
Cdd:pfam13579  78 HSP--TAGLAARLARRRRGVPLVVTVHGLALDYGSGWKRRLARALERRLLRRADAVVVVSEAEAELLRALGVPAArVVVV 155


                  ...
gi 808669993  186 RNG 188
Cdd:pfam13579 156 PNG 158

Glyco_transf_4

pfam13439

Glycosyltransferase Family 4;

27-189

5.74e-10

Glycosyltransferase Family 4;

Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 57.93 E-value: 5.74e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993   27 GGPVRVAFNQSRQLRAAGHRTLVAgAVRGYPQIPTVLDGVPVRLAKARSIIPRLGFSGLLAPALLVWMVRNRrsFDVVHV 106
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVV-TPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRER--PDVVHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  107 HLARDLItLPAAAIALILRKRVIVQTHGMITDSSHP-----IAPILDRVLTRPILRRAAAVLYLTEDERAALLRVQ--PE 179
Cdd:pfam13439  78 HSPFPLG-LAALAARLRLGIPLVVTYHGLFPDYKRLgarlsPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYgvPP 156

                         170
                  ....*....|
gi 808669993  180 AAVRHLRNGV 189
Cdd:pfam13439 157 EKIRVIPNGV 166

GT4_WcaC-like

cd03825

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...

14-382

1.10e-09

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.

Pssm-ID: 340851 [Multi-domain] Cd Length: 364 Bit Score: 59.27 E-value: 1.10e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  14 LHVVTLITPDgAYGGPVRVAFNQSRQLRAAGHRTLVAGAVRgypqiptvldgvpvrlakaRSIIPRLGFSgllaPAllvw 93
Cdd:cd03825    1 MKVLHINTVD-LSGGAARAAYRLHQALLAYGIDSTMLVGRK-------------------KNLISKPEFI----EA---- 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  94 mvrnrrsfDVVHVHLARDLItLPAAAIALILRKRVIVQT-HGM--ITDSSH---------------P---IAPILDRVLT 152
Cdd:cd03825   53 --------DIIHLHWIHGGY-LSLKALFKLLRRKPVVWTlHDMwpFTGGCHypmecegwktgcgncPnlnSYPPAKKDLS 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 153 RPILRR---AAAVLYLT----------EDERAALLRVQPeaaVRHLRNGVPGYEGTPAAARADPTAGRVE-----VLYLA 214
Cdd:cd03825  124 RQLFRRkreALAKKRLTivapsrwladMVRRSPLLKGLP---VVVIPNGIDTEIFAPVDKAKARKRLGIPqdkkvILFGA 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 215 R--LQVRKRPALFVkAAARLLAAGCDARFTLVGPDEgegpevlDTIMRSDIrfdEIRWEGALPPDRTVLRM-AAASIYVL 291
Cdd:cd03825  201 EsvTKPRKGFDELI-EALKLLATKDDLLLVVFGKND-------PQIVILPF---DIISLGYIDDDEQLVDIySAADLFVH 269

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 292 PSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVDESE-DALMEAMRTLIIDQRLREKMSAAARQTAAAVFS 370
Cdd:cd03825  270 PSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDvQALAEAIEWLLANPKERESLGERARALAENHFD 349

                        410
                 ....*....|..
gi 808669993 371 MEAIARDLTAVY 382
Cdd:cd03825  350 QRVQAQRYLELY 361

GT4_BshA-like

cd04962

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...

220-383

2.91e-09

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: 58.13 E-value: 2.91e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 220 KRPALFVKAAARLlAAGCDARFTLVGpdegEGPEvLDTIMRSDIRF---DEIRWEGALPPDRTVLrmAAASIYVLPSVDE 296
Cdd:cd04962  209 KRIDDVVRVFARV-RRKIPAKLLLVG----DGPE-RVPAEELARELgveDRVLFLGKQDDVEELL--SIADLFLLPSEKE 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 297 PFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVDESE-DALMEAMRTLIIDQRLREKMSAAARQTAAAVFSMEAIA 375
Cdd:cd04962  281 SFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDvDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIV 360


                 ....*...
gi 808669993 376 RDLTAVYA 383
Cdd:cd04962  361 PQYEAYYR 368

GT4_AviGT4-like

cd03802

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...

13-347

7.67e-09

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: 56.53 E-value: 7.67e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  13 VLHVVTLI--TPDGAYGGPVRVAFNQSRQLRAAGHR-TLVA--GAVRGYPQIPTVldgvPVRLAKARSIIPRLGFSGLLA 87
Cdd:cd03802    2 IAQVSPPRgpVPPGKYGGTELVVSALTEGLVRRGHEvTLFApgDSHTSAPLVAVI----PRALRLDPIPQESKLAELLEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  88 PALlvwmVRNRRSFDVVHVHlardlITLPAAAIALILRKRVIVQTHGmitdssHPIAPILDRVLtrpiLRRAAAVLYLTE 167
Cdd:cd03802   78 LEV----QLRASDFDVIHNH-----SYDWLPPFAPLIGTPFVTTLHG------PSIPPSLAIYA----AEPPVNYVSISD 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 168 DERAALLRVQPEAAVRHlrnGVPgyegtPAAARADPTAGRVeVLYLARLQVRKRPALFVKAAARllaagCDARFTLVGPD 247
Cdd:cd03802  139 AQRAATPPIDYLTVVHN---GLD-----PADYRFQPDPEDY-LAFLGRIAPEKGLEDAIRVARR-----AGLPLKIAGKV 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 248 EGEGP-----EVLDTimrsdirfDEIRWEGALPPDR--TVLRMAAASIyVLPSVDEPFPMSVLEAMSVGLPVVITESCGL 320
Cdd:cd03802  205 RDEDYfyylqEPLPG--------PRIEFIGEVGHDEkqELLGGARALL-FPINWDEPFGLVMIEAMACGTPVIAYRRGGL 275

                        330       340
                 ....*....|....*....|....*..
gi 808669993 321 ADTVRASGSGLVVDeSEDALMEAMRTL 347
Cdd:cd03802  276 PEVIQHGETGFLVD-SVEEMAEAIANI 301

GT4_trehalose_phosphorylase

cd03792

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...

199-358

6.39e-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: 6.39e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 199 ARADPTAGRVEVLYLARLQVRKRPALfvkaaaRLLAAGCDArftlvgPDEGEGPEVLDTIMRSDIRFDEIRWEGALPPDR 278
Cdd:cd03792  204 ARFDPSKDPLGVIDAYKLFKRRAEEP------QLVICGHGA------VDDPEGSVVYEEVMEYAGDDHDIHVLRLPPSDQ 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 279 TV-LRMAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVDESEDALMEAMRtLIIDQRLREKM 357
Cdd:cd03792  272 EInALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAVRILR-LLTDPELRRKM 350


                 .
gi 808669993 358 S 358
Cdd:cd03792  351 G 351

GT4-like

cd03813

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...

85-358

6.53e-08

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: 54.26 E-value: 6.53e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  85 LLAPALLVWMVRNR-RSFDVVHVHlardlITLPAAAIALILRKR----VIVQTHGMITD-------SSHPIAPILDRV-- 150
Cdd:cd03813  157 MLLPLFKLAIAADDlPEADLYHSV-----STGYAGLLGALARHRrgipFLLTEHGIYTRerkieilQSTWIMGYIKKLwi 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 151 -----LTRPILRRAAAVLYLTEDERAALLRV-QPEAAVRHLRNGVPGYEGTPAAARADPTAGRVEVLyLARLQVRKRPAL 224
Cdd:cd03813  232 rfferLGKLAYQQADKIISLYEGNRRRQIRLgADPDKTRVIPNGIDIQRFAPAREERPEKEPPVVGL-VGRVVPIKDVKT 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 225 FVKAAARLLAAGCDARFTLVGPDEgEGP----EVLDTIMRSDIRfDEIRWEGalpPDRTVLRMAAASIYVLPSVDEPFPM 300
Cdd:cd03813  311 FIRAFKLVRRAMPDAEGWLIGPED-EDPeyaqECKRLVASLGLE-NKVKFLG---FQNIKEYYPKLGLLVLTSISEGQPL 385

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808669993 301 SVLEAMSVGLPVVITE--SCG--LADTVRASGS-GLVVD-ESEDALMEAMRTLIIDQRLREKMS 358
Cdd:cd03813  386 VILEAMASGVPVVATDvgSCRelIYGADDALGQaGLVVPpADPEALAEALIKLLRDPELRQAFG 449

GT4_WbdM_like

cd04951

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...

210-384

2.75e-07

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: 52.06 E-value: 2.75e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 210 VLYLARL-QVRKRPALfVKAAARLLAAGCDARFTLVGpdegEGP---EVLDTIMRSDIRfDEIRWEGALppDRTVLRMAA 285
Cdd:cd04951  191 ILNVGRLtEAKDYPNL-LLAISELILSKNDFKLLIAG----DGPlrnELERLICNLNLV-DRVILLGQI--SNISEYYNA 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 286 ASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVraSGSGLVVDESEDALM-EAMRTLIIDQRLREKMSAAARQT 364
Cdd:cd04951  263 ADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVV--GDHNYVVPVSDPQLLaEKIKEIFDMSDEERDILGNKNEY 340

                        170       180
                 ....*....|....*....|
gi 808669993 365 AAAVFSMEAIARDLTAVYAG 384
Cdd:cd04951  341 IAKNFSINTIVNEWERLYSG 360

GT4_ExpC-like

cd03818

Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...

225-379

6.33e-07

Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).

Pssm-ID: 340845 [Multi-domain] Cd Length: 396 Bit Score: 50.82 E-value: 6.33e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 225 FVKAAARLLAAGCDARFTLVGPD------EGEGPEVLDTIMRSDIRFD--EIRWEGALPPD--RTVLRMAAASIYVLpsv 294
Cdd:cd03818  232 FMRALPRIQARRPDARVVVVGGDgvsygsPPPDGGSWKQKMLAELGVDleRVHFVGKVPYDqyVRLLQLSDAHVYLT--- 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 295 dEPFPMS--VLEAMSVGLPVVITESCGLADTVRASGSGLVVD-ESEDALMEAMRTLIIDQRLREKMSAAARQTAAAVFSM 371
Cdd:cd03818  309 -YPFVLSwsLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDfFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSL 387


                 ....*....
gi 808669993 372 E-AIARDLT 379
Cdd:cd03818  388 DvCLARYLA 396

PLN02871

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase

77-357

1.02e-06

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase

Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 50.48 E-value: 1.02e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993  77 IPRLGFSGLLAPallVWMVrnrrsfdVVHVHLARDLITLPAAAIALILR-------KRVIVQTHGMITDSSHPiapildr 149
Cdd:PLN02871 183 IPRYTFSWLVKP---MWDI-------IRFLHRAADLTLVTSPALGKELEaagvtaaNRIRVWNKGVDSESFHP------- 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 150 vltrpilrraaavlyltederaallRVQPEAAVRHLRNGVPGyegtpaaaraDPTagrveVLYLARLQVRKRpalfVKAA 229
Cdd:PLN02871 246 -------------------------RFRSEEMRARLSGGEPE----------KPL-----IVYVGRLGAEKN----LDFL 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 230 ARLLAAGCDARFTLVGpdegEGPEvldtimRSDIR--FDEIR--WEGALPPDRTVLRMAAASIYVLPSVDEPFPMSVLEA 305
Cdd:PLN02871 282 KRVMERLPGARLAFVG----DGPY------REELEkmFAGTPtvFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEA 351

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 808669993 306 MSVGLPVVITESCGLADTV---RASGSGLVVDESE-DALMEAMRTLIIDQRLREKM 357
Cdd:PLN02871 352 MASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDvDDCVEKLETLLADPELRERM 407

sucrsPsyn_pln

TIGR02468

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...

276-353

2.64e-06

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.

Pssm-ID: 274147 [Multi-domain] Cd Length: 1050 Bit Score: 49.39 E-value: 2.64e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993   276 PDrtVLRMAAAS--IYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVD-ESEDALMEAMRTLIIDQR 352
Cdd:TIGR02468  562 PD--IYRLAAKTkgVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDpHDQQAIADALLKLVADKQ 639


                   .
gi 808669993   353 L 353
Cdd:TIGR02468  640 L 640

GT4_ALG2-like

cd03805

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...

303-378

2.70e-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: 2.70e-05

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808669993 303 LEAMSVGLPVVITESCGLADTVRASGSGLVVDESEDALMEAMRTLIIDQRLREKMSAAARQTAAAVFSMEAIARDL 378
Cdd:cd03805  317 LEAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAERL 392

GT4_GtfA-like

cd04949

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...

210-358

8.19e-05

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: 44.21 E-value: 8.19e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 210 VLYLARLQVRKRPALFVKAAARLLAAGCDARFTLVGpdEGEGPEVLdTIMRSDIRF-DEIRWEGALppdRTVLRMAA-AS 287
Cdd:cd04949  163 IITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYG--YGEEREKL-KKLIEELHLeDNVFLKGYH---SNLDQEYQdAY 236

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808669993 288 IYVLPSVDEPFPMSVLEAMSVGLPVVITE-SCGLADTVRASGSGLVVD-ESEDALMEAMRTLIIDQRLREKMS 358
Cdd:cd04949  237 LSLLTSQMEGFGLTLMEAIGHGLPVVSYDvKYGPSELIEDGENGYLIEkNNIDALADKIIELLNDPEKLQQFS 309

GT4_CapH-like

cd03812

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...

100-356

3.23e-04

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: 42.28 E-value: 3.23e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 100 SFDVVHVH-LARDLITLPAAAIALIlRKRvIVQTHGMiTDSSHPIAPILDRVLTRPILRRAAAVLYLTEDERAALLRVQP 178
Cdd:cd03812   80 KYDIVHVHgSSSNGIILLLAAKAGV-PVR-IAHSHNT-KDSSIKLRKIRKNVLKKLIERLSTKYLACSEDAGEWLFGEVE 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 179 EAAVRHLRNGVP--GYEGTPAAARADPT----AGRVEVLYLARLQVRKRPALFVKAAARLLAAGCDARFTLVGpdEGEgp 252
Cdd:cd03812  157 NGKFKVIPNGIDieKYKFNKEKRRKRRKllilEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVG--EGE-- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 253 evldtiMRSDIRFdEIRWEGALppDRTVLR---------MAAASIYVLPSVDEPFPMSVLEAMSVGLPVV----ITESCG 319
Cdd:cd03812  233 ------LKEKIKE-KVKELGLE--DKVIFLgfrndvseiLSAMDVFLFPSLYEGLPLVAVEAQASGLPCLlsdtITKECD 303

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 808669993 320 LADTVrasgSGLVVDESEDALMEAMRTLIIDQRLREK 356
Cdd:cd03812  304 ITNNV----EFLPLNETPSTWAEKILKLIKRKRRINK 336

PRK15179

Vi polysaccharide biosynthesis protein TviE; Provisional

178-374

4.02e-04

Vi polysaccharide biosynthesis protein TviE; Provisional

Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 42.33 E-value: 4.02e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 178 PEAAVRHLRNGVP--------GYEGTPAAARADPTAGRVEVLYLARLQVRKRPALFVKAAARLLAAGCDARFTLVGpdeg 249
Cdd:PRK15179 480 DERRIPVVYNGLAplksvqddACTAMMAQFDARTSDARFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVG---- 555

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 250 eGPEVLDTIMRSDIRF---DEIRWEGAlpPDRTVLRMAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRA 326
Cdd:PRK15179 556 -GGPLLESVREFAQRLgmgERILFTGL--SRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQE 632

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 808669993 327 SGSGLVV---DESEDALMEAMRTLIIDQRLREKMSAAARQTAAAVFSMEAI 374
Cdd:PRK15179 633 GVTGLTLpadTVTAPDVAEALARIHDMCAADPGIARKAADWASARFSLNQM 683

GT4_AmsK-like

cd04946

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...

282-335

8.28e-04

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: 41.29 E-value: 8.28e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 808669993 282 RMAAASIYVLPSVDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVDE 335
Cdd:cd04946  301 KENDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLLLDK 354

GT4_WbaZ-like

cd03804

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...

211-344

1.31e-03

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: 40.35 E-value: 1.31e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 211 LYLARLQVRKRPALFVKAAARLlaagcDARFTLVGpdegEGPEvLDTImrSDIRFDEIRWEGALPPDRTVLRMAAASIYV 290
Cdd:cd03804  203 LTASRLVPYKRIDLAVEAFNEL-----PKRLVVIG----DGPD-LDRL--RAMASPNVEFLGYQPDEVLKELLSKARAFV 270

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808669993 291 LPSVdEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSGLVVDE-SEDALMEAM 344
Cdd:cd03804  271 FAAE-EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEqTVESLKAAV 324

PRK15484

lipopolysaccharide N-acetylglucosaminyltransferase;

272-330

4.48e-03

lipopolysaccharide N-acetylglucosaminyltransferase;

Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 39.00 E-value: 4.48e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808669993 272 GALPPDRTVLRMAAASIYVLPS-VDEPFPMSVLEAMSVGLPVVITESCGLADTVRASGSG 330
Cdd:PRK15484 263 GGQPPEKMHNYYPLADLVVVPSqVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITG 322

GT5_Glycogen_synthase_DULL1-like

cd03791

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...

283-348

4.55e-03

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.

Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 39.08 E-value: 4.55e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808669993 283 MAAASIYVLPSVDEPFPMSVLEAMSVG-LPVViTESCGLADTV------RASGSGLVVDE-SEDALMEAMRTLI 348
Cdd:cd03791  366 YAGADFFLMPSRFEPCGLVQMYAMRYGtLPIV-RRTGGLADTVfdydpeTGEGTGFVFEDyDAEALLAALRRAL 438

Blast search parameters

Data Source:	Precalculated data, version = cdd.v.3.21
Preset Options:	Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01