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Conserved domains on  [gi|2029784844|gb|QUF80510|]
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GT4 family glycosyltransferase PelF [Anaerobutyricum hallii]

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 ...
 2-469 1.89e-169

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 cd03813:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 474  Bit Score: 486.07  E-value: 1.89e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844   2 KVCIVAEGCYPYVVGGVSGWINSLIRSFPNVEFILLAIVANRSFRGKFVYELPENLTQVYEVYLDDcEWESGNRK----- 76
Cdd:cd03813     1 DIGLLLEGTYPYVRGGVSSWVHQLITGLPEHEFAVYFIGGREETYGEIKYEIPPNVVHVEEHPLWE-RLDDGSFSggssq 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844  77 RKSLRQVHLSHKEYDEMLNMVLNRRTDWGVIFDLFHRKHLSVDAFLMGEDFFRIARECYDRNYSNINFSDFLWTLRSIYL 156
Cdd:cd03813    80 KANLENLEREGTQLEEGQPILEADRFAIDLLRESELKRDGSLTDFLYSKASWDILLEAYLEYCTEPSFLDYFWTLRNMLL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 157 PMF--WALRMDVPKADLYHCVATGYSGILGSMAKHFHGSSLLISEHGIYTREREEELIKASWVRGVYKNIWIEQFKKMSL 234
Cdd:cd03813   160 PLFklAIAADDLPEADLYHSVSTGYAGLLGALARHRRGIPFLLTEHGIYTRERKIEILQSTWIMGYIKKLWIRFFERLGK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 235 LAYEKADMVTCLYDHAKDLQMELGCPPEKIRVTPNGINTQTLADlPGKTEEEKQFINAGAVLRVTPIKDVKTMIQAFAFA 314
Cdd:cd03813   240 LAYQQADKIISLYEGNRRRQIRLGADPDKTRVIPNGIDIQRFAP-AREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 315 KKKVKNMKLWIMGPADEDKKYAKECYDLVESLGVQD-VEFTGRVNVKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVI 393
Cdd:cd03813   319 RRAMPDAEGWLIGPEDEDPEYAQECKRLVASLGLENkVKFLGFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVV 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2029784844 394 ATDVGNCRELIYGNNDGFGEAGILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRVNALYRIDQMKEVYREIYK 469
Cdd:cd03813   399 ATDVGSCRELIYGADDALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
 
Name Accession Description Interval E-value
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 2-469 1.89e-169

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: 486.07  E-value: 1.89e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844   2 KVCIVAEGCYPYVVGGVSGWINSLIRSFPNVEFILLAIVANRSFRGKFVYELPENLTQVYEVYLDDcEWESGNRK----- 76
Cdd:cd03813     1 DIGLLLEGTYPYVRGGVSSWVHQLITGLPEHEFAVYFIGGREETYGEIKYEIPPNVVHVEEHPLWE-RLDDGSFSggssq 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844  77 RKSLRQVHLSHKEYDEMLNMVLNRRTDWGVIFDLFHRKHLSVDAFLMGEDFFRIARECYDRNYSNINFSDFLWTLRSIYL 156
Cdd:cd03813    80 KANLENLEREGTQLEEGQPILEADRFAIDLLRESELKRDGSLTDFLYSKASWDILLEAYLEYCTEPSFLDYFWTLRNMLL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 157 PMF--WALRMDVPKADLYHCVATGYSGILGSMAKHFHGSSLLISEHGIYTREREEELIKASWVRGVYKNIWIEQFKKMSL 234
Cdd:cd03813   160 PLFklAIAADDLPEADLYHSVSTGYAGLLGALARHRRGIPFLLTEHGIYTRERKIEILQSTWIMGYIKKLWIRFFERLGK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 235 LAYEKADMVTCLYDHAKDLQMELGCPPEKIRVTPNGINTQTLADlPGKTEEEKQFINAGAVLRVTPIKDVKTMIQAFAFA 314
Cdd:cd03813   240 LAYQQADKIISLYEGNRRRQIRLGADPDKTRVIPNGIDIQRFAP-AREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 315 KKKVKNMKLWIMGPADEDKKYAKECYDLVESLGVQD-VEFTGRVNVKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVI 393
Cdd:cd03813   319 RRAMPDAEGWLIGPEDEDPEYAQECKRLVASLGLENkVKFLGFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVV 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2029784844 394 ATDVGNCRELIYGNNDGFGEAGILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRVNALYRIDQMKEVYREIYK 469
Cdd:cd03813   399 ATDVGSCRELIYGADDALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 3-468 1.53e-119

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: 359.24  E-value: 1.53e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844   3 VCIVAEGCYPYVVGGVSGWINSLIRSFPNVEFILLAIVANRSFRGKFVYELPENLTQVYEVYLDDCEWESGNRKRK---- 78
Cdd:NF038011    2 ICLLLEGTFPYVRGGVSSWVNQMIRGFPELTFAVVFIGSRREDYGKRAYALPDNVVHLEEHYLYDAWAPPQPRASRgdaa 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844  79 ---SLRQVHLSHKEYDEMLNMV-LNRRtdwgVIFDLFHRKHLSVDAFLMGEDFFRIARECYDRNYSNINFSDFLWTLRSI 154
Cdd:NF038011   82 afaRVADLHDALRHPDAPAEAGaLGRE----LLPMLADGGRLSEEDFLHSRASWDYITEQYRRYCTDPSFVDYFWTVRIM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 155 YLPMFWALR--MDVPKADLYHCVATGYSGILGSMAKHFHGSSLLISEHGIYTREREEELIKASWVR-------------G 219
Cdd:NF038011  158 HKPLWQLARiaRNLPPARVYHTISTGYAGFLGALLHRRTGRPLLLSEHGIYTKERKIDLAQSQWIRdnrglferddsevS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 220 VYKNIWIEQFKKMSLLAYEKADMVTCLYDHAKDLQMELGCPPEKIRVTPNGINTQTLADLPGKTEEEKQFInAGAVLRVT 299
Cdd:NF038011  238 YFRELWIRFFEALGRLCYDAADPIVALYEGNRLRQIADGAPPERTRVIPNGIDLPRLAPLRAQRPAGIPPV-VGLIGRVV 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 300 PIKDVKTMIQAFAFAKKKVKNMKLWIMGPADEDKKYAKECYDLVESLGVQD-VEFTGRVNVKDYLGKMDFTLLTSISEGQ 378
Cdd:NF038011  317 PIKDIKTFIRAMRTVVRAMPEAEGWIVGPEEEDPAYAAECRSLVASLGLQDkVKFLGFQKIDDLLPQVGLMVLSSISEAL 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 379 PLTILESYAAHKPVIATDVGNCRELIYGNND---GFGEAGILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRVNALY 455
Cdd:NF038011  397 PLVVLEAFAAGVPVVTTDVGSCRQLIEGLDEedrALGAAGEVVAIADPQALARAALDLLRDPQRWQAAQAAGLARVERYY 476

                         490
                  ....*....|...
gi 2029784844 456 RIDQMKEVYREIY 468
Cdd:NF038011  477 TEELMFDRYRELY 489
DUF3492 pfam11997
Domain of unknown function (DUF3492); This presumed domain is functionally uncharacterized. ...
 1-262 3.03e-85

Domain of unknown function (DUF3492); This presumed domain is functionally uncharacterized. This domain is found in bacteria, archaea and eukaryotes. This domain is typically between 259 to 282 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: GGVS and EHGIY.


Pssm-ID: 432249  Cd Length: 268  Bit Score: 263.36  E-value: 3.03e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844   1 MKVCIVAEGCYPYVVGGVSGWINSLIRSFPNVEFILLAIVANRSFRGKFVYELPENLTQVYEVYLDDCEWES-GNRKRKS 79
Cdd:pfam11997   1 ADVCLLLEGTYPYVSGGVSSWVHQLITGLPEVRFAILFIGSRREDYGEFKYELPPNVVHVEEHYLWDPLETSpAPVRRRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844  80 LRQ-VHLSHKEYDEMLNMVLNRRTDWGVIFDLFHRKH--LSVDAFLMGEDFFRIARECYDRNYSNINFSDFLWTLRSIYL 156
Cdd:pfam11997  81 DRAaFETLRRLHEALREGGPLAEELLRELLYELGSKGrgLSPEDFLYSKRAWDIICEQYREYCEDPSFVDYFWTVRNMHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 157 PMFWALRMDVPKADLYHCVATGYSGILGSMAKHFHGSSLLISEHGIYTREREEELIKASWVRGV--YKNIWIEQFKKMSL 234
Cdd:pfam11997 161 PLLPLIARELPPADVYHAVSTGYAGLLGALLKHRTGRPLILTEHGIYTRERKIEIFQAEWISEVsyFRELWIRFFESLGR 240

                         250       260
                  ....*....|....*....|....*...
gi 2029784844 235 LAYEKADMVTCLYDHAKDLQMELGCPPE 262
Cdd:pfam11997 241 LCYRAADPIITLYEYNRERQIEDGADPE 268
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 362-469 3.79e-20

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 85.81  E-value: 3.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 362 YLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVGNCRELIYGnndgfGEAGILTHIMNIEEIAHAMVTMSVNEKDRR 441
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIED-----GETGLLVPPGDPEALAEAILRLLEDPELRR 91

                          90       100
                  ....*....|....*....|....*...
gi 2029784844 442 CMGEAGYRRVNALYRIDQMKEVYREIYK 469
Cdd:COG0438    92 RLGEAARERAEERFSWEAIAERLLALYE 119
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
260-411 8.11e-06

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 47.86  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 260 PPEKIRVTPNGINTQTLADLPGKTEEEKQFINAGAVL-----RVTPIKDVKTMIQAFAFAKKKVKNMKLWIMGPADEDKK 334
Cdd:PRK15484  159 PNADISIVPNGFCLETYQSNPQPNLRQQLNISPDETVllyagRISPDKGILLLMQAFEKLATAHSNLKLVVVGDPTASSK 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 335 -----YAKECYDLVESLGVQDVEFTGRV--NVKDYLGKMDFTLLTS-ISEGQPLTILESYAAHKPVIATDVGNCRELIYG 406
Cdd:PRK15484  239 gekaaYQKKVLEAAKRIGDRCIMLGGQPpeKMHNYYPLADLVVVPSqVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLE 318


                  ....*
gi 2029784844 407 NNDGF 411
Cdd:PRK15484  319 GITGY 323
 
Name Accession Description Interval E-value
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 2-469 1.89e-169

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: 486.07  E-value: 1.89e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844   2 KVCIVAEGCYPYVVGGVSGWINSLIRSFPNVEFILLAIVANRSFRGKFVYELPENLTQVYEVYLDDcEWESGNRK----- 76
Cdd:cd03813     1 DIGLLLEGTYPYVRGGVSSWVHQLITGLPEHEFAVYFIGGREETYGEIKYEIPPNVVHVEEHPLWE-RLDDGSFSggssq 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844  77 RKSLRQVHLSHKEYDEMLNMVLNRRTDWGVIFDLFHRKHLSVDAFLMGEDFFRIARECYDRNYSNINFSDFLWTLRSIYL 156
Cdd:cd03813    80 KANLENLEREGTQLEEGQPILEADRFAIDLLRESELKRDGSLTDFLYSKASWDILLEAYLEYCTEPSFLDYFWTLRNMLL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 157 PMF--WALRMDVPKADLYHCVATGYSGILGSMAKHFHGSSLLISEHGIYTREREEELIKASWVRGVYKNIWIEQFKKMSL 234
Cdd:cd03813   160 PLFklAIAADDLPEADLYHSVSTGYAGLLGALARHRRGIPFLLTEHGIYTRERKIEILQSTWIMGYIKKLWIRFFERLGK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 235 LAYEKADMVTCLYDHAKDLQMELGCPPEKIRVTPNGINTQTLADlPGKTEEEKQFINAGAVLRVTPIKDVKTMIQAFAFA 314
Cdd:cd03813   240 LAYQQADKIISLYEGNRRRQIRLGADPDKTRVIPNGIDIQRFAP-AREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 315 KKKVKNMKLWIMGPADEDKKYAKECYDLVESLGVQD-VEFTGRVNVKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVI 393
Cdd:cd03813   319 RRAMPDAEGWLIGPEDEDPEYAQECKRLVASLGLENkVKFLGFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVV 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2029784844 394 ATDVGNCRELIYGNNDGFGEAGILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRVNALYRIDQMKEVYREIYK 469
Cdd:cd03813   399 ATDVGSCRELIYGADDALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 3-468 1.53e-119

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: 359.24  E-value: 1.53e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844   3 VCIVAEGCYPYVVGGVSGWINSLIRSFPNVEFILLAIVANRSFRGKFVYELPENLTQVYEVYLDDCEWESGNRKRK---- 78
Cdd:NF038011    2 ICLLLEGTFPYVRGGVSSWVNQMIRGFPELTFAVVFIGSRREDYGKRAYALPDNVVHLEEHYLYDAWAPPQPRASRgdaa 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844  79 ---SLRQVHLSHKEYDEMLNMV-LNRRtdwgVIFDLFHRKHLSVDAFLMGEDFFRIARECYDRNYSNINFSDFLWTLRSI 154
Cdd:NF038011   82 afaRVADLHDALRHPDAPAEAGaLGRE----LLPMLADGGRLSEEDFLHSRASWDYITEQYRRYCTDPSFVDYFWTVRIM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 155 YLPMFWALR--MDVPKADLYHCVATGYSGILGSMAKHFHGSSLLISEHGIYTREREEELIKASWVR-------------G 219
Cdd:NF038011  158 HKPLWQLARiaRNLPPARVYHTISTGYAGFLGALLHRRTGRPLLLSEHGIYTKERKIDLAQSQWIRdnrglferddsevS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 220 VYKNIWIEQFKKMSLLAYEKADMVTCLYDHAKDLQMELGCPPEKIRVTPNGINTQTLADLPGKTEEEKQFInAGAVLRVT 299
Cdd:NF038011  238 YFRELWIRFFEALGRLCYDAADPIVALYEGNRLRQIADGAPPERTRVIPNGIDLPRLAPLRAQRPAGIPPV-VGLIGRVV 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 300 PIKDVKTMIQAFAFAKKKVKNMKLWIMGPADEDKKYAKECYDLVESLGVQD-VEFTGRVNVKDYLGKMDFTLLTSISEGQ 378
Cdd:NF038011  317 PIKDIKTFIRAMRTVVRAMPEAEGWIVGPEEEDPAYAAECRSLVASLGLQDkVKFLGFQKIDDLLPQVGLMVLSSISEAL 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 379 PLTILESYAAHKPVIATDVGNCRELIYGNND---GFGEAGILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRVNALY 455
Cdd:NF038011  397 PLVVLEAFAAGVPVVTTDVGSCRQLIEGLDEedrALGAAGEVVAIADPQALARAALDLLRDPQRWQAAQAAGLARVERYY 476

                         490
                  ....*....|...
gi 2029784844 456 RIDQMKEVYREIY 468
Cdd:NF038011  477 TEELMFDRYRELY 489
DUF3492 pfam11997
Domain of unknown function (DUF3492); This presumed domain is functionally uncharacterized. ...
 1-262 3.03e-85

Domain of unknown function (DUF3492); This presumed domain is functionally uncharacterized. This domain is found in bacteria, archaea and eukaryotes. This domain is typically between 259 to 282 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: GGVS and EHGIY.


Pssm-ID: 432249  Cd Length: 268  Bit Score: 263.36  E-value: 3.03e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844   1 MKVCIVAEGCYPYVVGGVSGWINSLIRSFPNVEFILLAIVANRSFRGKFVYELPENLTQVYEVYLDDCEWES-GNRKRKS 79
Cdd:pfam11997   1 ADVCLLLEGTYPYVSGGVSSWVHQLITGLPEVRFAILFIGSRREDYGEFKYELPPNVVHVEEHYLWDPLETSpAPVRRRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844  80 LRQ-VHLSHKEYDEMLNMVLNRRTDWGVIFDLFHRKH--LSVDAFLMGEDFFRIARECYDRNYSNINFSDFLWTLRSIYL 156
Cdd:pfam11997  81 DRAaFETLRRLHEALREGGPLAEELLRELLYELGSKGrgLSPEDFLYSKRAWDIICEQYREYCEDPSFVDYFWTVRNMHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 157 PMFWALRMDVPKADLYHCVATGYSGILGSMAKHFHGSSLLISEHGIYTREREEELIKASWVRGV--YKNIWIEQFKKMSL 234
Cdd:pfam11997 161 PLLPLIARELPPADVYHAVSTGYAGLLGALLKHRTGRPLILTEHGIYTRERKIEIFQAEWISEVsyFRELWIRFFESLGR 240

                         250       260
                  ....*....|....*....|....*...
gi 2029784844 235 LAYEKADMVTCLYDHAKDLQMELGCPPE 262
Cdd:pfam11997 241 LCYRAADPIITLYEYNRERQIEDGADPE 268
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 168-469 1.90e-35

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: 135.36  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 168 KADLYHCVATgYSGILGSMAKHFHGSSLLISEHGIYTREReeelikasWVRGVYKNIWIEQFKKMsllaYEKADMVTCLY 247
Cdd:cd03801    82 KFDVVHAHGL-LAALLAALLALLLGAPLVVTLHGAEPGRL--------LLLLAAERRLLARAEAL----LRRADAVIAVS 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 248 DHAKDLQMEL-GCPPEKIRVTPNGINTQTLADL----PGKTEEEKQFINAGavlRVTPIKDVKTMIQAFAFAKKKVKNMK 322
Cdd:cd03801   149 EALRDELRALgGIPPEKIVVIPNGVDLERFSPPlrrkLGIPPDRPVLLFVG---RLSPRKGVDLLLEALAKLLRRGPDVR 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 323 LWIMGPADEDKKYAKEcydlvESLGVQD-VEFTGRVN---VKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVG 398
Cdd:cd03801   226 LVIVGGDGPLRAELEE-----LELGLGDrVRFLGFVPdeeLPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVG 300

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2029784844 399 NCRELIygnndGFGEAGILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRVNALYRIDQMKEVYREIYK 469
Cdd:cd03801   301 GLPEVV-----EDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 111-443 3.09e-32

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: 126.32  E-value: 3.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 111 FHRKHLSVDAFLMGEDF-FRIARECYDRNYSNINFSDFLWTLRSIYLPMFWALRMDVPKADLYHCVATGYSGILGSMAKH 189
Cdd:cd03811    25 LDKRGYDVTLVLLRDEGdLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRILKRAKPDVVISFLGFATYIVAKLAAA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 190 fhGSSLLISEHGIYTREReeelikaswvrgvykniWIEQFKKMSLLAYEKADMVTCLYDHAK-DLQMELGCPPEKIRVTP 268
Cdd:cd03811   105 --RSKVIAWIHSSLSKLY-----------------YLKKKLLLKLKLYKKADKIVCVSKGIKeDLIRLGPSPPEKIEVIY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 269 NGI---NTQTLADLPGKTEEEKQ--FINAGavlRVTPIKDVKTMIQAFAFAKKKVKNMKLWIMGPADEDKKYAKecydLV 343
Cdd:cd03811   166 NPIdidRIRALAKEPILNEPEDGpvILAVG---RLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEK----LA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 344 ESLGVQD-VEFTGRV-NVKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVGNCRELIygnndGFGEAGILTHIM 421
Cdd:cd03811   239 KELGLAErVIFLGFQsNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREIL-----DDGENGLLVPDG 313

                         330       340
                  ....*....|....*....|..
gi 2029784844 422 NIEEIAHAMVTMSVNEKDRRCM 443
Cdd:cd03811   314 DAAALAGILAALLQKKLDAALR 335
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 168-469 2.61e-31

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: 123.97  E-value: 2.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 168 KADLYHCVATG---YSGILGSMAkhfHGSSLLISEHGIYTREReeeliKASWVRgvykniWIEqfkkmslLAYEKADMVT 244
Cdd:cd03807    79 NPDVVHTWMYHadlIGGLAAKLA---GGVKVIWSVRSSNIPQR-----LTRLVR------KLC-------LLLSKFSPAT 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 245 -CLYDHAKDLQMELGCPPEKIRVTPNGINTQTLA-DLPGKTEEEKQF------INAGAVLRVTPIKDVKTMIQAFAFAKK 316
Cdd:cd03807   138 vANSSAVAEFHQEQGYAKNKIVVIYNGIDLFKLSpDDASRARARRRLglaedrRVIGIVGRLHPVKDHSDLLRAAALLVE 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 317 KVKNMKLWIMGpaDEDKKYAKEcyDLVESLGVQD-VEFTG-RVNVKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIA 394
Cdd:cd03807   218 THPDLRLLLVG--RGPERPNLE--RLLLELGLEDrVHLLGeRSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVA 293

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2029784844 395 TDVGNCRELIygnNDGfgeAGILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRVNALYRIDQMKEVYREIYK 469
Cdd:cd03807   294 TDVGGAAELV---DDG---TGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 135-460 2.37e-28

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 115.39  E-value: 2.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 135 YDRNYSNINFSDFLWTLRSIYLpMFWALRMDV-----PKADLYHCVATGYSGILGSMAkHFHGsslliseHGIYTreree 209
Cdd:cd03808    54 IPILRRGINPLKDLKALFKLYK-LLKKEKPDIvhchtPKPGILGRLAARLAGVPKVIY-TVHG-------LGFVF----- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 210 elIKASWVRGVYKNIWieqfkKMSLLayeKADMVTCLYDHAKDLQMELGCPPEKIRVT--PNGINTQTLADLPGKTEEEK 287
Cdd:cd03808   120 --TEGKLLRLLYLLLE-----KLALL---FTDKVIFVNEDDRDLAIKKGIIKKKKTVLipGSGVDLDRFQYSPESLPSEK 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 288 -QFINAGavlRVTPIKDVKTMIQAFAFAKKKVKNMKLWIMGPADEDKkyakECYDLVESLGVQD-VEFTG-RVNVKDYLG 364
Cdd:cd03808   190 vVFLFVA---RLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELEN----PSEILIEKLGLEGrIEFLGfRSDVPELLA 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 365 KMDFTLLTSISEGQPLTILESYAAHKPVIATDVGNCRELIygnNDGFGeaGILTHIMNIEEIAHAMVTMSVNEKDRRCMG 444
Cdd:cd03808   263 ESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELV---IDGVN--GFLVPPGDVEALADAIEKLIEDPELRKEMG 337

                         330
                  ....*....|....*.
gi 2029784844 445 EAGYRRVNALYRIDQM 460
Cdd:cd03808   338 EAARKRVEEKFDEEKV 353
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 167-467 1.17e-27

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: 114.01  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 167 PKADLYHCVATGYSGILGSMAKHFHGSSLLISEHGiytrereeelikaswvRGVYKNIWIEQFKKMSLLAYEKADMVTCL 246
Cdd:cd03798    94 GPPDLIHAHFAYPAGFAAALLARLYGVPYVVTEHG----------------SDINVFPPRSLLRKLLRWALRRAARVIAV 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 247 ydhAKDLQ---MELGCPPEKIRVTPNGINT---QTLADLPGKTEEEKQFINAGavlRVTPIKDVKTMIQAFAFAKKKVKN 320
Cdd:cd03798   158 ---SKALAeelVALGVPRDRVDVIPNGVDParfQPEDRGLGLPLDAFVILFVG---RLIPRKGIDLLLEAFARLAKARPD 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 321 MKLWIMGpADEDKKYakeCYDLVESLGVQD-VEFTGRV---NVKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATD 396
Cdd:cd03798   232 VVLLIVG-DGPLREA---LRALAEDLGLGDrVTFTGRLpheQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATD 307

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2029784844 397 VGNCRELIygnndGFGEAGILTHIMNIEEIAHAMVTMsVNEKDRRCMGEAGYRRVNALY----RIDQMKEVYREI 467
Cdd:cd03798   308 VGGIPEVV-----GDPETGLLVPPGDADALAAALRRA-LAEPYLRELGEAARARVAERFswvkAADRIAAAYRDV 376
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
298-433 8.35e-22

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 91.03  E-value: 8.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 298 VTPIKDVKTMIQAFAFAKKKVKNMKLWIMGPADEdkkyaKECYDLVESLGvQDVEFTGRV-NVKDYLGKMDFTLLTSISE 376
Cdd:pfam13692  11 HPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPE-----EELEELAAGLE-DRVIFTGFVeDLAELLAAADVFVLPSLYE 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2029784844 377 GQPLTILESYAAHKPVIATDVGNCRELIYgnndgfGEAGILTHIMNIEEIAHAMVTM 433
Cdd:pfam13692  85 GFGLKLLEAMAAGLPVVATDVGGIPELVD------GENGLLVPPGDPEALAEAILRL 135
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 137-451 2.89e-21

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: 95.49  E-value: 2.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 137 RNYSNINFSDFLWTLRSIYLPMFWALRMDVPKADLYHCVAT-GYSGILGSMAKHFHGSSLLISEHGIYTrereEELIKAS 215
Cdd:cd03794    67 GPIKKNGLIRRLLNYLSFALAALLKLLVREERPDVIIAYSPpITLGLAALLLKKLRGAPFILDVRDLWP----ESLIALG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 216 WVRgvyKNIWIEQFKKMSLLAYEKADMVTCLYDHAKDLQMELGCPPEKIRVTPNGINTQTLADLPGktEEEKQFINAGAV 295
Cdd:cd03794   143 VLK---KGSLLKLLKKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPK--DELRKKLGLDDK 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 296 LRV------TPIKDVKTMIQAFAFAKKKvKNMKLWIMGPADEdkkyAKECYDLVESLGVQDVEFTGRVN---VKDYLGKM 366
Cdd:cd03794   218 FVVvyagniGKAQGLETLLEAAERLKRR-PDIRFLFVGDGDE----KERLKELAKARGLDNVTFLGRVPkeeVPELLSAA 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 367 DFTLLT-----SISEGQPLTILESYAAHKPVIATDVGNCRELIygnndGFGEAGILTHIMNIEEIAHAMVTMSVNEKDRR 441
Cdd:cd03794   293 DVGLVPlkdnpANRGSSPSKLFEYMAAGKPILASDDGGSDLAV-----EINGCGLVVEPGDPEALADAILELLDDPELRR 367

                         330
                  ....*....|
gi 2029784844 442 CMGEAGYRRV 451
Cdd:cd03794   368 AMGENGRELA 377
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 285-450 3.34e-20

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: 87.33  E-value: 3.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 285 EEKQFINAGavlRVTPIKDVKTMIQAFAFAKKKVKNMKLWIMGpadeDKKYAKECYDLVESLGVQD-VEFTGRVN---VK 360
Cdd:pfam00534   1 KKKIILFVG---RLEPEKGLDLLIKAFALLKEKNPNLKLVIAG----DGEEEKRLKKLAEKLGLGDnVIFLGFVSdedLP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 361 DYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVGNCRELIygnndGFGEAGILTHIMNIEEIAHAMVTMSVNEKDR 440
Cdd:pfam00534  74 ELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV-----KDGETGFLVKPNNAEALAEAIDKLLEDEELR 148

                         170
                  ....*....|
gi 2029784844 441 RCMGEAGYRR 450
Cdd:pfam00534 149 ERLGENARKR 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 362-469 3.79e-20

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 85.81  E-value: 3.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 362 YLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVGNCRELIYGnndgfGEAGILTHIMNIEEIAHAMVTMSVNEKDRR 441
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIED-----GETGLLVPPGDPEALAEAILRLLEDPELRR 91

                          90       100
                  ....*....|....*....|....*...
gi 2029784844 442 CMGEAGYRRVNALYRIDQMKEVYREIYK 469
Cdd:COG0438    92 RLGEAARERAEERFSWEAIAERLLALYE 119
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 244-450 1.87e-17

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: 83.56  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 244 TCLYDHAKDLqmeLGCPPEKIRVTPNGINTQtLADLPGKTEEEKQFINAGAVL------RVTPIKDVKTMIQAFAFAKKK 317
Cdd:cd03819   135 ELVRDHLIEA---LGVDPERIRVIPNGVDTD-RFPPEAEAEERAQLGLPEGKPvvgyvgRLSPEKGWLLLVDAAAELKDE 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 318 vKNMKLWIMGPADEDKkyakECYDLVESLGVQD-VEFTGRV-NVKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIAT 395
Cdd:cd03819   211 -PDFRLLVAGDGPERD----EIRRLVERLGLRDrVTFTGFReDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVAT 285

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2029784844 396 DVGNCRELIygnndGFGEAGILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRR 450
Cdd:cd03819   286 DVGGAREIV-----VHGRTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAALT 335
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 221-466 2.01e-17

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: 83.57  E-value: 2.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 221 YKNIWIEQFKKMSLlayEKADMVTCLYDHAK-DLQMELGCPPEKIRVTPNGINTQTLADLPGKTEEEKQFINAGAVL--- 296
Cdd:cd03809   123 RFRLYYRLLLPISL---RRADAIITVSEATRdDIIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLPEPYFLyvg 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 297 RVTPIKDVKTMIQAFAFAKKKVKNMKLWIMGPADEdkKYAKECYDLVESLGVQDVEFTGRVN---VKDYLGKMDFTLLTS 373
Cdd:cd03809   200 TLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGW--EDEELLDLVKKLGLGGRVRFLGYVSdedLPALYRGARAFVFPS 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 374 ISEGQPLTILESYAAHKPVIATDVGNCRELIygnndgfGEAGILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRVnA 453
Cdd:cd03809   278 LYEGFGLPVLEAMACGTPVIASNISVLPEVA-------GDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERA-K 349

                         250
                  ....*....|...
gi 2029784844 454 LYRIDQMKEVYRE 466
Cdd:cd03809   350 KFSWEKTAEKTLE 362
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 186-451 1.80e-16

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: 80.74  E-value: 1.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 186 MAKHFHGSSLLISEHGIYTrereeelikasWVRGVYKNIWIEqfkkmsLLAYEKADMVTCLYDHAKDLQMELgcPPEKIR 265
Cdd:cd03820   102 LALIGLKSKLIVWEHNNYE-----------AYNKGLRRLLLR------RLLYKRADKIVVLTEADKLKKYKQ--PNSNVV 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 266 VTPNGIN---TQTLADLpgkteEEKQFINAGavlRVTPIKDVKTMIQAFAFAKKKVKNMKLWIMGPADEDKKYAkecyDL 342
Cdd:cd03820   163 VIPNPLSfpsEEPSTNL-----KSKRILAVG---RLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELE----KL 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 343 VESLGVQD-VEFTGRV-NVKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDvgnC----RELIYGNNDGFgeagi 416
Cdd:cd03820   231 IDKLGLEDrVKLLGPTkNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFD---CptgpSEIIEDGENGL----- 302

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2029784844 417 LTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRV 451
Cdd:cd03820   303 LVPNGDVDALAEALLRLMEDEELRKKMGKNARKNA 337
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 229-469 2.47e-15

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 77.39  E-value: 2.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 229 FKKMSLLAYEKADMVTCLYDHAKDLQMELGCPPEKIRVTPNGINTQTLADLPGKTEEEKQFINAGA--VLRVT---PIKD 303
Cdd:cd04962   131 LQPAVRFSINKSDRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKPAGALKRRLLAPPDEkvVIHVSnfrPVKR 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 304 VKTMIQAFAFAKKKVKNmKLWIMGPADEdKKYAKEcydLVESLGVQD-VEFTGRVN-VKDYLGKMDFTLLTSISEGQPLT 381
Cdd:cd04962   211 IDDVVRVFARVRRKIPA-KLLLVGDGPE-RVPAEE---LARELGVEDrVLFLGKQDdVEELLSIADLFLLPSEKESFGLA 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 382 ILESYAAHKPVIATDVGNCRELIYGNNDGFgeagiLTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRVNALYRIDQMK 461
Cdd:cd04962   286 ALEAMACGVPVVSSNAGGIPEVVKHGETGF-----LSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIV 360


                  ....*...
gi 2029784844 462 EVYREIYK 469
Cdd:cd04962   361 PQYEAYYR 368
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 191-411 4.68e-15

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 74.75  E-value: 4.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 191 HGSSLLISEHGIYTREREEELIKASWVRGVYKNIWIEQFKKMSLLAYEKADMVTCLYDHAKDLQMELGC--PPEKIRVTP 268
Cdd:cd01635     6 GEYPPLRGGLELHVRALARALAALGHEVTVLALLLLALRRILKKLLELKPDVVHAHSPHAAALAALLAArlLGIPIVVTV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 269 NGINTQTLAD--LPGKTEEEKQFINAGAVL--RVTPIKDVKTMIQAFAFAKKKVKNMKLWIMGPADEDKKYAKEcydLVE 344
Cdd:cd01635    86 HGPDSLESTRseLLALARLLVSLPLADKVSvgRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEAL---AAA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2029784844 345 SLGVQDVEFTG----RVNVKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVGNCRELIYGNNDGF 411
Cdd:cd01635   163 LGLLERVVIIGglvdDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 146-455 3.94e-14

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: 73.81  E-value: 3.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 146 DFLWTlrsiYLPMF-------WALRMDVPkaDLYHcvaTGY--SGILGSMAKHFHGSSLLISEH--GIYTREREEelikA 214
Cdd:cd03800    78 EELWP----YLEEFadgllrfIAREGGRY--DLIH---SHYwdSGLVGALLARRLGVPLVHTFHslGRVKYRHLG----A 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 215 SWVRGVYKNIWIEQfkkmslLAYEKADMV--TClYDHAKDLQMELGCPPEKIRVTPNGINTQTLADLPGKTEEEKQFINA 292
Cdd:cd03800   145 QDTYHPSLRITAEE------QILEAADRViaST-PQEADELISLYGADPSRINVVPPGVDLERFFPVDRAEARRARLLLP 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 293 G------AVLRVTPIKDVKTMIQAFAFAKKKVKNMKLWI-MGPADEDKKYAKECYD-LVESLGVQD-VEFTGRVN---VK 360
Cdd:cd03800   218 PdkpvvlALGRLDPRKGIDTLVRAFAQLPELRELANLVLvGGPSDDPLSMDREELAeLAEELGLIDrVRFPGRVSrddLP 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 361 DYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVGNCRELIygnNDgfGEAGILTHIMNIEEIAHAMVTMSVNEKDR 440
Cdd:cd03800   298 ELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIV---RD--GRTGLLVDPHDPEALAAALRRLLDDPALW 372

                         330
                  ....*....|....*
gi 2029784844 441 RCMGEAGYRRVNALY 455
Cdd:cd03800   373 QRLSRAGLERARAHY 387
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 262-448 8.65e-14

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: 72.33  E-value: 8.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 262 EKIRVTPNGINTQTLADLPGKTEEEKQFINAGavlRVTPIKDVKTMIQAFAFAKKKVKNMKLWIMGPADEDKKYAKecyd 341
Cdd:cd04949   136 PPIFTIPVGYVDQLDTAESNHERKSNKIITIS---RLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKK---- 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 342 LVESLGVQD-VEFTG-RVNVKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVGncreliYGNNDgF---GEAGI 416
Cdd:cd04949   209 LIEELHLEDnVFLKGyHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVK------YGPSE-LiedGENGY 281

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2029784844 417 LTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGY 448
Cdd:cd04949   282 LIEKNNIDALADKIIELLNDPEKLQQFSEESY 313
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 225-451 9.42e-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: 72.49  E-value: 9.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 225 WIEQFKKMSLLAYEKADMVTCLYDHAKDLQMELGCPPEKIRVTPNGINTQTLADLPgKTEEEKQFINAGavlRVTPIKDV 304
Cdd:cd05844   129 WPSQFQRHRRALQRPAALFVAVSGFIRDRLLARGLPAERIHVHYIGIDPAKFAPRD-PAERAPTILFVG---RLVEKKGC 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 305 KTMIQAFAFAKKKVKNMKLWIMGpadeDKKYAKECYDLVESLGvqDVEFTGRV---NVKDYLGKMDFTLLTSI------S 375
Cdd:cd05844   205 DVLIEAFRRLAARHPTARLVIAG----DGPLRPALQALAAALG--RVRFLGALphaEVQDWMRRAEIFCLPSVtaasgdS 278

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2029784844 376 EGQPLTILESYAAHKPVIATDVGNCRELIygnndGFGEAGILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRV 451
Cdd:cd05844   279 EGLGIVLLEAAACGVPVVSSRHGGIPEAI-----LDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFV 349
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 256-465 2.26e-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: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 256 ELGCPPEKIRVTPNGIntQTLADLPGKTEEEKQFINAGAVLRVTPIKDVKTMIQAFAFAKKKvkNMKLWIMGPADEDKKY 335
Cdd:cd03823   160 ANGLFSARISVIPNAV--EPDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLPRE--DIELVIAGHGPLSDER 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 336 AKECYDLVESLGvqdveFTGRVNVKDYLGKMDFTLLTSI-SEGQPLTILESYAAHKPVIATDVGNCRELIYGNNDGF-GE 413
Cdd:cd03823   236 QIEGGRRIAFLG-----RVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLlFA 310

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2029784844 414 AGilthimNIEEIAHAMVTMSVNEKDRRCMGEAGYRRVNALYRIDQMKEVYR 465
Cdd:cd03823   311 PG------DAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEEYLKLYR 356
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 167-460 4.59e-13

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: 70.17  E-value: 4.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 167 PKADLYHCvATGYSGILGSMAKHFHGSS--LLISEHGI-YTREREEELIKaswvrgVYKNIwieqfkkmsllaYEKADMV 243
Cdd:cd03799    69 GAYDIIHC-QFGPLGALGALLRRLKVLKgkLVTSFRGYdISMYVILEGNK------VYPQL------------FAQGDLF 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 244 TCLYDHAKDLQMELGCPPEKIRVTPNGINTQTLaDLPGKTEEEKQFINAGAVLRVTPIKDVKTMIQAFAFAKKKVKNMKL 323
Cdd:cd03799   130 LPNCELFKHRLIALGCDEKKIIVHRSGIDCNKF-RFKPRYLPLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEY 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 324 WIM--GPADEDKKyakecyDLVESLGVQD----VEFTGRVNVKDYLGKMDFTLLTSIS------EGQPLTILESYAAHKP 391
Cdd:cd03799   209 QIIgdGDLKEQLQ------QLIQELNIGDcvklLGWKPQEEIIEILDEADIFIAPSVTaadgdqDGPPNTLKEAMAMGLP 282

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2029784844 392 VIATDVGNCRELIYGNNDGFgeagiLTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRVNALYRIDQM 460
Cdd:cd03799   283 VISTEHGGIPELVEDGVSGF-----LVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDINKL 346
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 263-469 1.49e-12

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: 68.90  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 263 KIRVTPNGINTQT-----LADLPGK--TEEEKQFINAGAVLRVTPIKDVKTMIQAFAFAKKKvKNMKLWIMGPADEDKKY 335
Cdd:cd03825   162 PVVVIPNGIDTEIfapvdKAKARKRlgIPQDKKVILFGAESVTKPRKGFDELIEALKLLATK-DDLLLVVFGKNDPQIVI 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 336 AKecYDLVeSLGVQDVEftgrVNVKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVGNCRELIygnndGFGEAG 415
Cdd:cd03825   241 LP--FDII-SLGYIDDD----EQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIV-----QHGVTG 308

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2029784844 416 ILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRVNALYRIDQMKEVYREIYK 469
Cdd:cd03825   309 YLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYK 362
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 260-439 2.41e-11

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: 65.16  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 260 PPEKIRVTPNGINT----------QTLADLPGKTEEEKQFINAGavlRVTPIKDVKTMIQAFAFAKKKVKNMKLWIMGpa 329
Cdd:cd04951   152 SKNKSVPVYNGIDLnkfkkdinvrLKIRNKLNLKNDEFVILNVG---RLTEAKDYPNLLLAISELILSKNDFKLLIAG-- 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 330 deDKKYAKECYDLVESLGVQD-VEFTG-RVNVKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVGNCRELIygn 407
Cdd:cd04951   227 --DGPLRNELERLICNLNLVDrVILLGqISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVV--- 301

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2029784844 408 ndgfGEAGILTHIMNIEEIAHAM---VTMSVNEKD 439
Cdd:cd04951   302 ----GDHNYVVPVSDPQLLAEKIkeiFDMSDEERD 332
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 259-449 4.42e-11

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: 64.31  E-value: 4.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 259 CPPEKIRVTPNGINT------QTLADLPGKTEEEKQFINAGavlRVTPIKDVKTMIQAFAFAKKKVKNMKLWIMGPADED 332
Cdd:cd03821   171 GLEPPIAVIPNGVDIpefdpgLRDRRKHNGLEDRRIILFLG---RIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDGA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 333 kkYAKECYDLVESLGVQDVEFTGRVNVKDYLGKM---DFTLLTSISEGQPLTILESYAAHKPVIATD-VGNCRELIYGnn 408
Cdd:cd03821   248 --YPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYasaDLFVLPSYSENFGNVVAEALACGLPVVITDkCGLSELVEAG-- 323

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2029784844 409 dgfgeAGILThIMNIEEIAHAMVTMSVNEKDRRCMGEAGYR 449
Cdd:cd03821   324 -----CGVVV-DPNVSSLAEALAEALRDPADRKRLGEMARR 358
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 230-434 4.77e-11

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: 64.22  E-value: 4.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 230 KKMSLLAYEKADMVTCLYDHAKDLQMELG--CPpekIRVTPNGINTQTLADLPGKTEEEKQFINAGA-----VLRVTPIK 302
Cdd:cd03817   138 RKLVRRFYNHTDAVIAPSEKIKDTLREYGvkGP---IEVIPNGIDLDKFEKPLNTEERRKLGLPPDEpillyVGRLAKEK 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 303 DVKTMIQAFAFAKKKvKNMKLWIMG--PadeDKKYAKEcydLVESLGVQD-VEFTGRVN---VKDYLGKMDFTLLTSISE 376
Cdd:cd03817   215 NIDFLLRAFAELKKE-PNIKLVIVGdgP---EREELKE---LARELGLADkVIFTGFVPreeLPEYYKAADLFVFASTTE 287

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2029784844 377 GQPLTILESYAAHKPVIATDVGNCRELIYGNNDGF----GEAGILTHIMNIEEIAHAMVTMS 434
Cdd:cd03817   288 TQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFlfepNDETLAEKLLHLRENLELLRKLS 349
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 262-461 3.30e-10

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: 61.52  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 262 EKIRVTPNGINTQTLaDLPGKTEEEKQFINAG-----AVLRVTPIKDVKTMIQAfafakKKVKNMKLWIMGPADEdKKYA 336
Cdd:cd03795   160 NKVRVIPLGIDKNVY-NIPRVDFENIKREKKGkkiflFIGRLVYYKGLDYLIEA-----AQYLNYPIVIGGEGPL-KPDL 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 337 KEcydLVESLGVQDVEFTGRVNVKD---YLGKMDFTLLTSI--SEGQPLTILESYAAHKPVIATDVGNcrELIYGNNDgf 411
Cdd:cd03795   233 EA---QIELNLLDNVKFLGRVDDEEkviYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVISTNIGT--GVPYVNNN-- 305

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2029784844 412 GEAGILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRVNALYRIDQMK 461
Cdd:cd03795   306 GETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEKMK 355
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 261-411 3.14e-08

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: 55.37  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 261 PEKIRVTPNGINTQTLA---------DLPGKTEEEKQFINAGavlRVTPIKDVKTMIQAFAFAKKKVKNMKLWIMG--PA 329
Cdd:cd03812   157 NGKFKVIPNGIDIEKYKfnkekrrkrRKLLILEDKLVLGHVG---RFNEQKNHSFLIDIFEELKKKNPNVKLVLVGegEL 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 330 DEDKKYakecydLVESLGVQD-VEFTGRVN-VKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVGNcRELIYGN 407
Cdd:cd03812   234 KEKIKE------KVKELGLEDkVIFLGFRNdVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTIT-KECDITN 306


                  ....
gi 2029784844 408 NDGF 411
Cdd:cd03812   307 NVEF 310
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 279-451 1.52e-07

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: 53.48  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 279 LPGKTEEEKQFINAgaVLRVTPIKDVKTMIQAFAFAKKKVKNMKLWIMG-PADED----------KKYAKECYDL-VESL 346
Cdd:cd03792   189 KPFVIDPERPYILQ--VARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGhGAVDDpegsvvyeevMEYAGDDHDIhVLRL 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 347 GVQDVEftgrVNVkdYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVGNCRELIYGNNDGFgeagilthIMN-IEE 425
Cdd:cd03792   267 PPSDQE----INA--LQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGF--------LVNsVEG 332

                         170       180
                  ....*....|....*....|....*.
gi 2029784844 426 IAHAMVTMSVNEKDRRCMGEAGYRRV 451
Cdd:cd03792   333 AAVRILRLLTDPELRRKMGLAAREHV 358
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
152-274 7.66e-06

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 46.37  E-value: 7.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 152 RSIYLPMFWALR--MDVPKADLYHCVATGYSGILGSMAKHFHGSSLLISEHGIYTREReeeLIKASWVRGVYKNIWIEQF 229
Cdd:pfam13439  53 LLRSLAFLRRLRrlLRRERPDVVHAHSPFPLGLAALAARLRLGIPLVVTYHGLFPDYK---RLGARLSPLRRLLRRLERR 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2029784844 230 kkmsllAYEKADMVTCL-YDHAKDLQMELGCPPEKIRVTPNGINTQ 274
Cdd:pfam13439 130 ------LLRRADRVIAVsEAVADELRRLYGVPPEKIRVIPNGVDLE 169
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
260-411 8.11e-06

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 47.86  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 260 PPEKIRVTPNGINTQTLADLPGKTEEEKQFINAGAVL-----RVTPIKDVKTMIQAFAFAKKKVKNMKLWIMGPADEDKK 334
Cdd:PRK15484  159 PNADISIVPNGFCLETYQSNPQPNLRQQLNISPDETVllyagRISPDKGILLLMQAFEKLATAHSNLKLVVVGDPTASSK 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 335 -----YAKECYDLVESLGVQDVEFTGRV--NVKDYLGKMDFTLLTS-ISEGQPLTILESYAAHKPVIATDVGNCRELIYG 406
Cdd:PRK15484  239 gekaaYQKKVLEAAKRIGDRCIMLGGQPpeKMHNYYPLADLVVVPSqVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLE 318


                  ....*
gi 2029784844 407 NNDGF 411
Cdd:PRK15484  319 GITGY 323
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 257-460 1.89e-05

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 47.34  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 257 LGCPPEKIRVTPNGINTQTLADLPGKTEEEKQF--------INAGAVLRVTPIKDVKTMIQAFAFAKKKVKNMKLWIMGp 328
Cdd:PRK15179  477 LGVDERRIPVVYNGLAPLKSVQDDACTAMMAQFdartsdarFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVG- 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 329 adeDKKYAKECYDLVESLGVQD-VEFTGRVN-VKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVGncreliyg 406
Cdd:PRK15179  556 ---GGPLLESVREFAQRLGMGErILFTGLSRrVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAG-------- 624

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2029784844 407 nndGFGEA---GILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRR-----VNALYRIDQM 460
Cdd:PRK15179  625 ---GAGEAvqeGVTGLTLPADTVTAPDVAEALARIHDMCAADPGIARkaadwASARFSLNQM 683
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 260-451 1.24e-04

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: 44.21  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 260 PPEKIRVTPNGINTQT---------LADLPGKtEEEKQFINAGavlRVTPIKDVKTMIQAFAFAKKKVKNMKLWI-MGPA 329
Cdd:cd03814   164 GFERVRLWPRGVDTELfhpsrrdaaLRRRLGP-PGRPLLLYVG---RLAPEKNLEALLDADLPLAASPPVRLVVVgDGPA 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 330 dedKKYAKECYDlveslgvqDVEFTG---RVNVKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATDVGNCRELIyg 406
Cdd:cd03814   240 ---RAELEARGP--------DVIFTGfltGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIV-- 306

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2029784844 407 nndGFGEAGILTHIMNIEEIAHAMVTMSVNEKDRRCMGEAGYRRV 451
Cdd:cd03814   307 ---RPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEA 348
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
147-270 2.10e-04

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 41.62  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 147 FLWTLRSiylpMFWALRmdvpkADLYHcVATGYSGILGSMAKHFHGSSLLISEHGIYTREreeeliKASWVRGVYKniWI 226
Cdd:pfam13579  59 ALRRLRR----LLRAER-----PDVVH-AHSPTAGLAARLARRRRGVPLVVTVHGLALDY------GSGWKRRLAR--AL 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2029784844 227 EQFkkmsllAYEKADMVTCLYDHAKDLQMELGCPPEKIRVTPNG 270
Cdd:pfam13579 121 ERR------LLRRADAVVVVSEAEAELLRALGVPAARVVVVPNG 158
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 351-412 2.49e-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: 43.22  E-value: 2.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2029784844 351 VEFTGRV---NVKDYLGKMDFTLLT--SISEGQPLTILESYAAHKPVIATDVGNCRELIygnNDGFG 412
Cdd:cd04946   285 VNFTGEVsnkEVKQLYKENDVDVFVnvSESEGIPVSIMEAISFGIPVIATNVGGTREIV---ENETN 348
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
368-462 5.55e-04

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 39.12  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 368 FTLLTSISEGQP-LTILESYAAHKPVIATDVGNCRELiygnndgF--GEAGILTHimNIEEIAHAMVTMSVNEKDRRCMG 444
Cdd:pfam13524   1 IVLNPSRRPDSPnMRVFEAAACGAPLLTDRTPGLEEL-------FepGEEILLYR--DPEELAEKIRYLLEHPEERRAIA 71

                          90       100
                  ....*....|....*....|..
gi 2029784844 445 EAGYRRV----NALYRIDQMKE 462
Cdd:pfam13524  72 AAGRERVlaehTYAHRAEQLLD 93
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
251-440 1.01e-03

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 41.24  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 251 KDLQMELGCPPEKIRVTPNGINTQTLADLPGKTEEEKQFINAGAVLrVTPIKDVKTMIQAFAFAKKkvkNMKLWIMGPAD 330
Cdd:PRK09922  145 KEQMMARGISAQRISVIYNPVEIKTIIIPPPERDKPAVFLYVGRLK-FEGQKNVKELFDGLSQTTG---EWQLHIIGDGS 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 331 EDKKyakeCYDLVESLGVQD-VEFTGRVN-----VKDYLGKMDFTLLTSISEGQPLTILESYAAHKPVIATD-VGNCREL 403
Cdd:PRK09922  221 DFEK----CKAYSRELGIEQrIIWHGWQSqpwevVQQKIKNVSALLLTSKFEGFPMTLLEAMSYGIPCISSDcMSGPRDI 296

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2029784844 404 IygnNDGFGeaGILTHIMNIEEIAHAMVTMSVNEKDR 440
Cdd:PRK09922  297 I---KPGLN--GELYTPGNIDEFVGKLNKVISGEVKY 328
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 302-462 1.15e-03

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: 41.04  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 302 KDVKTMIQAFAFAKKK---VKNMKLWIMGPAD----EDKKYAKECYDLVESLgvqdveftgrVNVKDYLgkmdfTLLTSI 374
Cdd:cd03805   224 KNIALAIEAFAKLKQKlpeFENVRLVIAGGYDprvaENVEYLEELQRLAEEL----------LNVEDQV-----LFLRSI 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 375 SEGQPLTIL--------------------ESYAAHKPVIATDVGNCRELIYGNNDGFGEAGilthimNIEEIAHAMVTMS 434
Cdd:cd03805   289 SDSQKEQLLssalallytpsnehfgivplEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP------TPEAFAEAMLKLA 362

                         170       180
                  ....*....|....*....|....*...
gi 2029784844 435 VNEKDRRCMGEAGYRRVNALYRIDQMKE 462
Cdd:cd03805   363 NDPDLADRMGAAGRKRVKEKFSREAFAE 390
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 227-409 2.69e-03

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: 40.06  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 227 EQFKKMSLLAYEKADMVTCLYDHAKDLQMELGCPPEKIRVTPNGINtqtLADLPGKTEEEKQFINAGAVL-----RVTPI 301
Cdd:cd03822   123 QALKVLFRIATLSERVVVMAPISRFLLVRIKLIPAVNIEVIPHGVP---EVPQDPTTALKRLLLPEGKKViltfgFIGPG 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029784844 302 KDVKTMIQAFAFAKKKVKNMKLWIMG-PADEDKKYAKECYDL--VESLGVQDV-----EFTGRVNVKDYLGKMDFTLL-- 371
Cdd:cd03822   200 KGLEILLEALPELKAEFPDVRLVIAGeLHPSLARYEGERYRKaaIEELGLQDHvdfhnNFLPEEEVPRYISAADVVVLpy 279

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2029784844 372 TSISEGQPLTILESYAAHKPVIATDVGNCRELIYGNND 409
Cdd:cd03822   280 LNTEQSSSGTLSYAIACGKPVISTPLRHAEELLADGRG 317
 
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

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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