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Conserved domains on  [gi|1332876537|ref|WP_102838814|]
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glycosyltransferase family 4 protein [Stutzerimonas frequens]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133453)

glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CAZY:  GT4
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  12691742|10521532|16037492
SCOP:  3001586

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 3-368 2.19e-44

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: 156.93  E-value: 2.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537   3 LAFILYKYFPF-GGLQRDFMRIALECQRRGHSIRVYAMIWEGEVPDGFE--VLIAPVKALFNHTRNERFTAWVEADLAKR 79
Cdd:cd03801     2 ILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEdgVIVPLLPSLAALLRARRLLRELRPLLRLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537  80 PVDRVIGFNKMPGLDVYYAADPCFEDKAQTLRNPIYRRWGRYKHFAE--YERAVFAPEAKTEILMISEVQQPLFVQHYGT 157
Cdd:cd03801    82 KFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERrlLARAEALLRRADAVIAVSEALRDELRALGGI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 158 PAERFHLLPPGIAQDRRAPanaaqiraEFREEFEVRPDELLLVQIGSGFKTKGLDRSLKALAALPRELSqRTRLLVIGQD 237
Cdd:cd03801   162 PPEKIVVIPNGVDLERFSP--------PLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGP-DVRLVIVGGD 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 238 DPKPFKLQAKTLGVSGMVEFL--KGRSDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCG 315
Cdd:cd03801   233 GPLRAELEELELGLGDRVRFLgfVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGG 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1332876537 316 rVVPSPFEQQALDQMLAQMLADDAQRSAWSRNALafAETADLYSMPQKAADVI 368
Cdd:cd03801   313 -LVVPPDDVEALADALLRLLADPELRARLGRAAR--ERVAERFSWERVAERLL 362
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 3-368 2.19e-44

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: 156.93  E-value: 2.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537   3 LAFILYKYFPF-GGLQRDFMRIALECQRRGHSIRVYAMIWEGEVPDGFE--VLIAPVKALFNHTRNERFTAWVEADLAKR 79
Cdd:cd03801     2 ILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEdgVIVPLLPSLAALLRARRLLRELRPLLRLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537  80 PVDRVIGFNKMPGLDVYYAADPCFEDKAQTLRNPIYRRWGRYKHFAE--YERAVFAPEAKTEILMISEVQQPLFVQHYGT 157
Cdd:cd03801    82 KFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERrlLARAEALLRRADAVIAVSEALRDELRALGGI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 158 PAERFHLLPPGIAQDRRAPanaaqiraEFREEFEVRPDELLLVQIGSGFKTKGLDRSLKALAALPRELSqRTRLLVIGQD 237
Cdd:cd03801   162 PPEKIVVIPNGVDLERFSP--------PLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGP-DVRLVIVGGD 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 238 DPKPFKLQAKTLGVSGMVEFL--KGRSDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCG 315
Cdd:cd03801   233 GPLRAELEELELGLGDRVRFLgfVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGG 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1332876537 316 rVVPSPFEQQALDQMLAQMLADDAQRSAWSRNALafAETADLYSMPQKAADVI 368
Cdd:cd03801   313 -LVVPPDDVEALADALLRLLADPELRARLGRAAR--ERVAERFSWERVAERLL 362
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 195-348 7.37e-34

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: 122.77  E-value: 7.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 195 DELLLVQIGSGFKTKGLDRSLKALAALPRELSQrTRLLVIG-QDDPKPFKLQAKTLGVSGMVEFLKGRS--DIPRFLLGA 271
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPN-LKLVIAGdGEEEKRLKKLAEKLGLGDNVIFLGFVSdeDLPELLKIA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1332876537 272 DLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCGRVVPsPFEQQALDQMLAQMLADDAQRSAWSRNA 348
Cdd:pfam00534  80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVK-PNNAEALAEAIDKLLEDEELRERLGENA 155
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 267-354 6.78e-17

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 76.18  E-value: 6.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 267 FLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCGRVVPsPFEQQALDQMLAQMLADDAQRSAWSR 346
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVP-PGDPEALAEAILRLLEDPELRRRLGE 95


                  ....*...
gi 1332876537 347 NALAFAET 354
Cdd:COG0438    96 AARERAEE 103
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 193-356 4.08e-03

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 38.92  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 193 RPDELLLVQIGSGFKTKGLDRSLKALAALPRelsqrTRLLVIGqDDPKPFKLQAKTLGV----SGMvefLKGrSDIPRFL 268
Cdd:PLN02871  260 EPEKPLIVYVGRLGAEKNLDFLKRVMERLPG-----ARLAFVG-DGPYREELEKMFAGTptvfTGM---LQG-DELSQAY 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 269 LGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCGrVVPSPFEQQALD---QMLAQMLADDAQRSAWS 345
Cdd:PLN02871  330 ASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPDQEG-KTGFLYTPGDVDdcvEKLETLLADPELRERMG 408

                         170
                  ....*....|.
gi 1332876537 346 RNALAFAETAD 356
Cdd:PLN02871  409 AAAREEVEKWD 419
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 3-368 2.19e-44

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: 156.93  E-value: 2.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537   3 LAFILYKYFPF-GGLQRDFMRIALECQRRGHSIRVYAMIWEGEVPDGFE--VLIAPVKALFNHTRNERFTAWVEADLAKR 79
Cdd:cd03801     2 ILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEdgVIVPLLPSLAALLRARRLLRELRPLLRLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537  80 PVDRVIGFNKMPGLDVYYAADPCFEDKAQTLRNPIYRRWGRYKHFAE--YERAVFAPEAKTEILMISEVQQPLFVQHYGT 157
Cdd:cd03801    82 KFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERrlLARAEALLRRADAVIAVSEALRDELRALGGI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 158 PAERFHLLPPGIAQDRRAPanaaqiraEFREEFEVRPDELLLVQIGSGFKTKGLDRSLKALAALPRELSqRTRLLVIGQD 237
Cdd:cd03801   162 PPEKIVVIPNGVDLERFSP--------PLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGP-DVRLVIVGGD 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 238 DPKPFKLQAKTLGVSGMVEFL--KGRSDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCG 315
Cdd:cd03801   233 GPLRAELEELELGLGDRVRFLgfVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGG 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1332876537 316 rVVPSPFEQQALDQMLAQMLADDAQRSAWSRNALafAETADLYSMPQKAADVI 368
Cdd:cd03801   313 -LVVPPDDVEALADALLRLLADPELRARLGRAAR--ERVAERFSWERVAERLL 362
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 195-348 7.37e-34

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: 122.77  E-value: 7.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 195 DELLLVQIGSGFKTKGLDRSLKALAALPRELSQrTRLLVIG-QDDPKPFKLQAKTLGVSGMVEFLKGRS--DIPRFLLGA 271
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPN-LKLVIAGdGEEEKRLKKLAEKLGLGDNVIFLGFVSdeDLPELLKIA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1332876537 272 DLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCGRVVPsPFEQQALDQMLAQMLADDAQRSAWSRNA 348
Cdd:pfam00534  80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVK-PNNAEALAEAIDKLLEDEELRERLGENA 155
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 154-349 1.33e-24

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: 103.47  E-value: 1.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 154 HYGTPAERFHLLPPGIAQDRRAPANAAQiraEFREEFEVRPDELLLVQIGSGFKTKGLDRSLKALAALPReLSQRTRLLV 233
Cdd:cd03800   181 LYGADPSRINVVPPGVDLERFFPVDRAE---ARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPE-LRELANLVL 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 234 IG------QDDPKPFKLQ-AKTLGVSGMVEFLKG--RSDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCG 304
Cdd:cd03800   257 VGgpsddpLSMDREELAElAEELGLIDRVRFPGRvsRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGG 336

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1332876537 305 YAHYITDANCGRVVPsPFEQQALDQMLAQMLADDAQRSAWSRNAL 349
Cdd:cd03800   337 LQDIVRDGRTGLLVD-PHDPEALAAALRRLLDDPALWQRLSRAGL 380
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 3-343 3.19e-23

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: 98.97  E-value: 3.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537   3 LAFILYKyFPFGGLQRDFMRIALECQRRGHSIRVYAM----IWEGEVPDGFEVLIAPVKALFNHTRNERFTAWVEADLAK 78
Cdd:cd03811     2 ILFVIPS-LSGGGAERVLLNLANALDKRGYDVTLVLLrdegDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRILK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537  79 R-PVDRVIGFNKMPGLDVyyAADPCFEDK-AQTLRN-PIYRRWGRYKHFAEYERAVFApeakTEILMISEVQQPLFVQHY 155
Cdd:cd03811    81 RaKPDVVISFLGFATYIV--AKLAAARSKvIAWIHSsLSKLYYLKKKLLLKLKLYKKA----DKIVCVSKGIKEDLIRLG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 156 GTPAERFHLLPPGIAQDrrapanaaQIRAEFREEFEV-RPDELLLVQIGSGFKTKGLDRSLKALAALPRELSQrTRLLVI 234
Cdd:cd03811   155 PSPPEKIEVIYNPIDID--------RIRALAKEPILNePEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPD-VKLVIL 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 235 GQ-DDPKPFKLQAKTLGVSGMVEFLKGRSDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDAN 313
Cdd:cd03811   226 GDgPLREELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGE 305

                         330       340       350
                  ....*....|....*....|....*....|
gi 1332876537 314 CGRVVpsPFEQQALDQMLAQMLADDAQRSA 343
Cdd:cd03811   306 NGLLV--PDGDAAALAGILAALLQKKLDAA 333
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 151-360 5.69e-20

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: 90.07  E-value: 5.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 151 FVQHYGTPAERFHLLPPGIAQDRRAPANAaqIRAEFREEFEVRPDELLLVQIGSGFKTKGLDRSLKALAALPRELSQrTR 230
Cdd:cd03807   147 FHQEQGYAKNKIVVIYNGIDLFKLSPDDA--SRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPD-LR 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 231 LLVIGQDDPKPFKL-QAKTLGVSGMVEFLKGRSDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVcGYAHYI 309
Cdd:cd03807   224 LLLVGRGPERPNLErLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDV-GGAAEL 302

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1332876537 310 TDANCGRVVPsPFEQQALDQMLAQMLADDAQRSAWSRNALAF-AETADLYSM 360
Cdd:cd03807   303 VDDGTGFLVP-AGDPQALADAIRALLEDPEKRARLGRAARERiANEFSIDAM 353
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 147-361 9.12e-20

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: 89.74  E-value: 9.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 147 QQPLFVQHYGTPAERFHLLPPGIAQDRRAPANAaqiraeFREEFEVRPDELLLVQIGSGFKTKGLDRSLKALAALpRELS 226
Cdd:cd03821   161 EQEADELRRFGLEPPIAVIPNGVDIPEFDPGLR------DRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKL-AEQG 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 227 QRTRLLVIGQDD---PKPFKLQAKTLGVS--GMVEFLKGRsDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTD 301
Cdd:cd03821   234 RDWHLVIAGPDDgayPAFLQLQSSLGLGDrvTFTGPLYGE-AKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITD 312

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 302 VCGYAHYITdANCGRVVPSpfEQQALDQMLAQMLADDAQRSAWSRNALAFAETADLYSMP 361
Cdd:cd03821   313 KCGLSELVE-AGCGVVVDP--NVSSLAEALAEALRDPADRKRLGEMARRARQVEENFSWE 369
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 151-369 3.38e-19

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: 87.82  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 151 FVQHYGTPAERFHLLPPGIAQDRRAPANaaqiraefrEEFEVRPDELLLVQIGSGFKTKGLDRSLKALAALPRElSQRTR 230
Cdd:cd03798   164 ELVALGVPRDRVDVIPNGVDPARFQPED---------RGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKA-RPDVV 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 231 LLVIGQD-DPKPFKLQAKTLGVSGMVEFLkGR---SDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYA 306
Cdd:cd03798   234 LLIVGDGpLREALRALAEDLGLGDRVTFT-GRlphEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIP 312

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1332876537 307 HYITDANCGRVVPSPFEqQALDQMLAQMLADDAQRSAWsrnALAFAETADLYSmPQKAADVIL 369
Cdd:cd03798   313 EVVGDPETGLLVPPGDA-DALAAALRRALAEPYLRELG---EAARARVAERFS-WVKAADRIA 370
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 109-353 1.36e-18

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: 85.85  E-value: 1.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 109 TLRNPIYRRWGRYKHFAEYERAVFAPeAKTEILMIS-----EVQQPLFVQHYgtpaeRFHLLPPGIAQDRRAPANaaqiR 183
Cdd:cd03825   111 NLNSYPPAKKDLSRQLFRRKREALAK-KRLTIVAPSrwladMVRRSPLLKGL-----PVVVIPNGIDTEIFAPVD----K 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 184 AEFREEFEVRPDE--LLLVQIGSGFKTKGLDRSLKALAALPRElsQRTRLLVIGQDDPKPFKLQAKTLGVSgmveFLKGR 261
Cdd:cd03825   181 AKARKRLGIPQDKkvILFGAESVTKPRKGFDELIEALKLLATK--DDLLLVVFGKNDPQIVILPFDIISLG----YIDDD 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 262 SDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCGRVVPsPFEQQALDQMLAQMLADDAQR 341
Cdd:cd03825   255 EQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVP-PGDVQALAEAIEWLLANPKER 333

                         250
                  ....*....|..
gi 1332876537 342 SAWSRNALAFAE 353
Cdd:cd03825   334 ESLGERARALAE 345
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
209-337 1.49e-17

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 78.32  E-value: 1.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 209 KGLDRSLKALAALpRELSQRTRLLVIGQDDPKpfKLQAKTLGVSGMVEFLKGRSDIPRFLLGADLLIHPAYNENTGTVLL 288
Cdd:pfam13692  15 KGVDYLLEAVPLL-RKRDNDVRLVIVGDGPEE--ELEELAAGLEDRVIFTGFVEDLAELLAAADVFVLPSLYEGFGLKLL 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1332876537 289 EALVAGLPVLVTDVCGYAHYITDANcGRVVPsPFEQQALDQMLAQMLAD 337
Cdd:pfam13692  92 EAMAAGLPVVATDVGGIPELVDGEN-GLLVP-PGDPEALAEAILRLLED 138
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 10-348 3.10e-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: 81.63  E-value: 3.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537  10 YFPFGGLQRDFMRIALECQRRGHSIRVYAMiwegeVPDGFEVLIAPVKALFNHTRNeRFTAWVEADLAKRPVDRvigfnk 89
Cdd:cd03819     7 ALEIGGAETYILDLARALAERGHRVLVVTA-----GGPLLPRLRQIGIGLPGLKVP-LLRALLGNVRLARLIRR------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537  90 mPGLDVYYAadpcfEDKAQTLRNPIYRRWGRYK--------HFAEYE--RAVFAPEAKTE-ILMISEVQQPLFVQHYGTP 158
Cdd:cd03819    75 -ERIDLIHA-----HSRAPAWLGWLASRLTGVPlvttvhgsYLATYHpkDFALAVRARGDrVIAVSELVRDHLIEALGVD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 159 AERFHLLPPGIAQDRRAPANAAqiraEFREEFEVRPDELLLVQIGSGFKTKGLDRSLKALAALPRELSQRtrLLVIGQDD 238
Cdd:cd03819   149 PERIRVIPNGVDTDRFPPEAEA----EERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFR--LLVAGDGP 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 239 PKP-FKLQAKTLGVSGMVEFLKGRSDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCGRV 317
Cdd:cd03819   223 ERDeIRRLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLL 302

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1332876537 318 VPsPFEQQALDQMLAQMLADDAQRSAWSRNA 348
Cdd:cd03819   303 VP-PGDAEALADAIRAAKLLPEAREKLQAAA 332
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 267-354 6.78e-17

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 76.18  E-value: 6.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 267 FLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCGRVVPsPFEQQALDQMLAQMLADDAQRSAWSR 346
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVP-PGDPEALAEAILRLLEDPELRRRLGE 95


                  ....*...
gi 1332876537 347 NALAFAET 354
Cdd:COG0438    96 AARERAEE 103
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 156-354 1.23e-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: 80.42  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 156 GTPAERFHLLPPGIAQDRRAPANAAQ-IRAEFREefevrPDELLLVQIGSGFKTKGLDRSLKALAALPRELsqRTRLLVI 234
Cdd:cd03814   162 GHGFERVRLWPRGVDTELFHPSRRDAaLRRRLGP-----PGRPLLLYVGRLAPEKNLEALLDADLPLAASP--PVRLVVV 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 235 GqDDPKPFKLQAKTLgvsgMVEFL--KGRSDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDA 312
Cdd:cd03814   235 G-DGPARAELEARGP----DVIFTgfLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPG 309

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1332876537 313 NCGRVVPsPFEQQALDQMLAQMLADDAQRSAWSRNALAFAET 354
Cdd:cd03814   310 GTGALVE-PGDAAAFAAALRALLEDPELRRRMAARARAEAER 350
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 200-318 3.85e-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: 73.98  E-value: 3.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 200 VQIGSGFKTKGLDRSLKALAALPRELSqRTRLLVIGQDDPKPFKLQ-AKTLGVSGMVEFLKGRSD---IPRFLLGADLLI 275
Cdd:cd01635   114 VSVGRLVPEKGIDLLLEALALLKARLP-DLVLVLVGGGGEREEEEAlAAALGLLERVVIIGGLVDdevLELLLAAADVFV 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1332876537 276 HPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCGRVV 318
Cdd:cd01635   193 LPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 113-367 1.08e-13

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: 71.54  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 113 PIYRRWGRYKH------FAEYERAVFAPEAKTEILMISEvqqplfvqHYGTPaerFHLLPPGIAQDRRAPAnaaqIRAEF 186
Cdd:cd03817   127 PKGKLLVKAVVrklvrrFYNHTDAVIAPSEKIKDTLREY--------GVKGP---IEVIPNGIDLDKFEKP----LNTEE 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 187 REEFEVRPDELLLVQIGSGFKTKGLDRSLKALAALPRElsQRTRLLVIGQ-DDPKPFKLQAKTLGVSGMVEFLkG---RS 262
Cdd:cd03817   192 RRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKE--PNIKLVIVGDgPEREELKELARELGLADKVIFT-GfvpRE 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 263 DIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCGRVVPSpfEQQALDQMLAQMLADDAQRS 342
Cdd:cd03817   269 ELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEP--NDETLAEKLLHLRENLELLR 346

                         250       260
                  ....*....|....*....|....*
gi 1332876537 343 AWSRNALAFAETadlYSMPQKAADV 367
Cdd:cd03817   347 KLSKNAEISARE---FAFAKSVEKL 368
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 209-353 7.60e-13

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: 68.78  E-value: 7.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 209 KGLDRSLKAlAALPRELSQRTRLLVIGQDDPK-PFKLQAKTLGVSGMVEFLKGRSDIPRFLLGADLLIHPAYNENTGTVL 287
Cdd:cd03808   202 KGIDELIEA-AKILKKKGPNVRFLLVGDGELEnPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSL 280

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1332876537 288 LEALVAGLPVLVTDVCGYAHYITDANCGRVVPsPFEQQALDQMLAQMLADDAQRSAWSRNALAFAE 353
Cdd:cd03808   281 LEAMAAGRPVITTDVPGCRELVIDGVNGFLVP-PGDVEALADAIEKLIEDPELRKEMGEAARKRVE 345
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 184-354 4.08e-12

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: 66.61  E-value: 4.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 184 AEFREEFEVRPDELLLVQIGSGFKTKGLDRSLKALAALPRELsqRTRLLVIGqDDPK--PFKLQAKTLGVSGMVEFLKGR 261
Cdd:cd04962   184 GALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKI--PAKLLLVG-DGPErvPAEELARELGVEDRVLFLGKQ 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 262 SDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCGRVVPSPFEQQALDQMLaQMLADDAQR 341
Cdd:cd04962   261 DDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSAL-SILEDDELY 339

                         170
                  ....*....|...
gi 1332876537 342 SAWSRNALAFAET 354
Cdd:cd04962   340 NRMGRAARKRAAE 352
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 151-353 1.33e-11

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: 65.08  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 151 FVQHYGTPAERFHLLPPGIAQDRRAPANAAQIRAEFREefevrPDELLLVqIGSGFKTKGLDRSLKALAALPRELSQRtR 230
Cdd:cd03809   153 IIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLL-----PEPYFLY-VGTLEPRKNHERLLKAFALLKKQGGDL-K 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 231 LLVIGQDDPKPFKLQ--AKTLGVSGMVEFLKGRSD--IPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTD----- 301
Cdd:cd03809   226 LVIVGGKGWEDEELLdlVKKLGLGGRVRFLGYVSDedLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNisvlp 305

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1332876537 302 -VCGY-AHYItdancgrvvpSPFEQQALDQMLAQMLADDAQRSAWSRNALAFAE 353
Cdd:cd03809   306 eVAGDaALYF----------DPLDPESIADAILRLLEDPSLREELIRKGLERAK 349
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 140-354 7.09e-11

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: 63.13  E-value: 7.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 140 ILMISEVQQPLFVQHyGTPAERFHLLPPGIAQDRRAPANAAQIRAEFREefevrPDELLLVQIGSGFKTKGLDRSLKALA 219
Cdd:cd03794   167 IIVLSPGLKEYLLRK-GVPKEKIIVIPNWADLEEFKPPPKDELRKKLGL-----DDKFVVVYAGNIGKAQGLETLLEAAE 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 220 ALPRElsQRTRLLVIGQ-DDPKPFKLQAKTLGVSGmVEFLKG--RSDIPRFLLGADLLIHP-----AYNENTGTVLLEAL 291
Cdd:cd03794   241 RLKRR--PDIRFLFVGDgDEKERLKELAKARGLDN-VTFLGRvpKEEVPELLSAADVGLVPlkdnpANRGSSPSKLFEYM 317

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1332876537 292 VAGLPVLVTDVCGYAHYITDANCGRVVPsPFEQQALDQMLAQMLADDAQRSAWSRNALAFAET 354
Cdd:cd03794   318 AAGKPILASDDGGSDLAVEINGCGLVVE-PGDPEALADAILELLDDPELRRAMGENGRELAEE 379
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 154-354 2.42e-10

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: 61.58  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 154 HYGTPAERFHLLPPGIAQDRRAPAnaaqirAEFREEfevrPDELLLVQIGSGFKTKGLDRSLKALAALPRELSQrTRLLV 233
Cdd:cd03813   261 RLGADPDKTRVIPNGIDIQRFAPA------REERPE----KEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPD-AEGWL 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 234 IGQDDPKPFKLQ-----AKTLGVSGMVEFLkGRSDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDV--CGYA 306
Cdd:cd03813   330 IGPEDEDPEYAQeckrlVASLGLENKVKFL-GFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVgsCREL 408

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1332876537 307 HYITDAN---CGRVVPsPFEQQALDQMLAQMLADDAQRSAWSRNALAFAET 354
Cdd:cd03813   409 IYGADDAlgqAGLVVP-PADPEALAEALIKLLRDPELRQAFGEAGRKRVEK 458
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 156-352 4.17e-10

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: 60.54  E-value: 4.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 156 GTPAERFHLLPPGIAQDRRAPAnaaqiraefreefEVRPDELLLVQIGSGFKTKGLDRSLKALAAL-PRELSQRtrlLVI 234
Cdd:cd05844   162 GLPAERIHVHYIGIDPAKFAPR-------------DPAERAPTILFVGRLVEKKGCDVLIEAFRRLaARHPTAR---LVI 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 235 GQDDPKPFKLQAKTLGVsGMVEFL--KGRSDIPRFLLGADLLIHPAY------NENTGTVLLEALVAGLPVLVTDVCGYA 306
Cdd:cd05844   226 AGDGPLRPALQALAAAL-GRVRFLgaLPHAEVQDWMRRAEIFCLPSVtaasgdSEGLGIVLLEAAACGVPVVSSRHGGIP 304

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1332876537 307 HYITDANCGRVVPsPFEQQALDQMLAQMLADDAQRSAWSRNALAFA 352
Cdd:cd05844   305 EAILDGETGFLVP-EGDVDALADALQALLADRALADRMGGAARAFV 349
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 135-359 1.63e-09

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: 58.94  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 135 EAKTEILMISEVQQPLFVQHYGTPAERFHLLPPGIaqdrraPANAAQIRAEFREEFEVRpDELLLVQIGSGFKTKGLDRS 214
Cdd:cd03822   133 TLSERVVVMAPISRFLLVRIKLIPAVNIEVIPHGV------PEVPQDPTTALKRLLLPE-GKKVILTFGFIGPGKGLEIL 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 215 LKALAALPRElSQRTRLLVIGQDDPKP--------FKLQAKTLGVSGMVEFLKG---RSDIPRFLLGADLLIHPAYNENT 283
Cdd:cd03822   206 LEALPELKAE-FPDVRLVIAGELHPSLaryegeryRKAAIEELGLQDHVDFHNNflpEEEVPRYISAADVVVLPYLNTEQ 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 284 GT--VLLEALVAGLPVLVTDVcGYAHYITDANCGRVVPsPFEQQALDQMLAQMLADDAQRSAWSRNALAFA------ETA 355
Cdd:cd03822   285 SSsgTLSYAIACGKPVISTPL-RHAEELLADGRGVLVP-FDDPSAIAEAILRLLEDDERRQAIAERAYAYAramtweSIA 362


                  ....
gi 1332876537 356 DLYS 359
Cdd:cd03822   363 DRYL 366
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 160-302 2.24e-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: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 160 ERFHLLPPGIAQDRraPANAAQIRAEFREEfEVRPDELLLVQIGSGFKTKGLDRSLKALAALPrELSQRTRLLVIGQ-DD 238
Cdd:cd03812   158 GKFKVIPNGIDIEK--YKFNKEKRRKRRKL-LILEDKLVLGHVGRFNEQKNHSFLIDIFEELK-KKNPNVKLVLVGEgEL 233

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1332876537 239 PKPFKLQAKTLGVSGMVEFLKGRSDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDV 302
Cdd:cd03812   234 KEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDT 297
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 151-341 1.27e-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: 52.83  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 151 FVQHYGTPAERFHLLPPGIAQDR--RAPANaaqiRAEFREEFEVRPDELLLVQIGSGFKTKGLDRSLKALAALPrELSQR 228
Cdd:cd04951   145 FIAKKAFSKNKSVPVYNGIDLNKfkKDINV----RLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELI-LSKND 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 229 TRLLVIGqDDPKPFKLQ--AKTLGVSGMVEFLKGRSDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYA 306
Cdd:cd04951   220 FKLLIAG-DGPLRNELErlICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVA 298

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1332876537 307 HYITDANcgRVVPSPFEQQALDQMLAQMLADDAQR 341
Cdd:cd04951   299 EVVGDHN--YVVPVSDPQLLAEKIKEIFDMSDEER 331
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 207-353 2.25e-07

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: 52.24  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 207 KTKGLDRSLKALAALPRELSQRTrlLVI---GQDDPKpFKLQAKTLGVSGMVEFLKGRSDIPRFLLGADLLIHPAYNENT 283
Cdd:cd03820   192 YQKGFDLLIEAWALIAKKHPDWK--LRIygdGPEREE-LEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGF 268

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1332876537 284 GTVLLEALVAGLPVLVTD-VCGYAHYITDANCGRVVPsPFEQQALDQMLAQMLADDAQRSAWSRNALAFAE 353
Cdd:cd03820   269 PMVLLEAMAYGLPIISFDcPTGPSEIIEDGENGLLVP-NGDVDALAEALLRLMEDEELRKKMGKNARKNAE 338
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 209-348 6.42e-07

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: 50.74  E-value: 6.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 209 KGLDRSLKALAALPRELsqrtrllVIGQDDPKPFKLQAK-TLGVSGMVEFLKGRSDIPR--FLLGADLLIHPAY--NENT 283
Cdd:cd03795   204 KGLDYLIEAAQYLNYPI-------VIGGEGPLKPDLEAQiELNLLDNVKFLGRVDDEEKviYLHLCDVFVFPSVlrSEAF 276

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1332876537 284 GTVLLEALVAGLPVLVTDV-CGYAHYITDANCGRVVPsPFEQQALDQMLAQMLADDAQRSAWSRNA 348
Cdd:cd03795   277 GIVLLEAMMCGKPVISTNIgTGVPYVNNNGETGLVVP-PKDPDALAEAIDKLLSDEELRESYGENA 341
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 110-321 5.59e-06

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: 47.70  E-value: 5.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 110 LRNPIYRRWGRYKHFAE-YERAVFAPeakteilmisevqqPLFVQHygTPAERFHLLPPGIAQ--DRRAPANAAQIRAEF 186
Cdd:cd03792   124 LTEPQPRVWDFLWNYIEgYDLFVFHP--------------PEFVPP--QVPPPKFYIPPSIDPlsGKNKDLSPADIRYYL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 187 REEFEVRPDELLLVQIGSGFKTKGLDRSLKALAaLPRELSQRTRLLVIGQ---DDPKPFKLQAKTLGVSG------MVEF 257
Cdd:cd03792   188 EKPFVIDPERPYILQVARFDPSKDPLGVIDAYK-LFKRRAEEPQLVICGHgavDDPEGSVVYEEVMEYAGddhdihVLRL 266

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1332876537 258 LKGRSDIPRFLLGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCGRVVPSP 321
Cdd:cd03792   267 PPSDQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSV 330
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 156-319 3.53e-04

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: 42.32  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 156 GTPAERFHLLPPGIAQDRRAPANAAQIRAEFREEFevrpdelllvqIGSGFKTKGLDRSLKALAALPRElsqRTRLLVIG 235
Cdd:cd03823   162 GLFSARISVIPNAVEPDLAPPPRRRPGTERLRFGY-----------IGRLTEEKGIDLLVEAFKRLPRE---DIELVIAG 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 236 QDDpkpfKLQAKTLGVSGMVEFLkGR---SDIPRFLLGADLLIHPA-YNENTGTVLLEALVAGLPVLVTDVCGYAHYITD 311
Cdd:cd03823   228 HGP----LSDERQIEGGRRIAFL-GRvptDDIKDFYEKIDVLVVPSiWPEPFGLVVREAIAAGLPVIASDLGGIAELIQP 302


                  ....*...
gi 1332876537 312 ANCGRVVP 319
Cdd:cd03823   303 GVNGLLFA 310
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
14-169 9.01e-04

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 39.82  E-value: 9.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537  14 GGLQRDFMRIALECQRRGHSIRVYAMIWEGEVPDGFEVLIAPVKALFNHTRNERFTAW----VEADLAKRPVDRVIGFNK 89
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAflrrLRRLLRRERPDVVHAHSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537  90 MPGLDVYYAA-----------------DPCFEDKAQTLRNPIYRRWgrYKHFAEYERAVFAPeakteilmiSEVQQPLFV 152
Cdd:pfam13439  81 FPLGLAALAArlrlgiplvvtyhglfpDYKRLGARLSPLRRLLRRL--ERRLLRRADRVIAV---------SEAVADELR 149

                         170
                  ....*....|....*..
gi 1332876537 153 QHYGTPAERFHLLPPGI 169
Cdd:pfam13439 150 RLYGVPPEKIRVIPNGV 166
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 209-321 1.24e-03

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: 40.35  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 209 KGLDRSLKALAALPRelsqrtRLLVIGQDDPKP--FKLQAKTLGvsGMVEFLKGRSDI--PRFLLGADLLIHP-AYNENT 283
Cdd:cd03802   182 KGLEDAIRVARRAGL------PLKIAGKVRDEDyfYYLQEPLPG--PRIEFIGEVGHDekQELLGGARALLFPiNWDEPF 253

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1332876537 284 GTVLLEALVAGLPVLVTDVCGYAHYITDANCGRVVPSP 321
Cdd:cd03802   254 GLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDSV 291
YjiC COG1819
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
211-353 1.81e-03

UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];


Pssm-ID: 441424 [Multi-domain]  Cd Length: 268  Bit Score: 39.45  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 211 LDRSLKALAALPRELsqrtrLLVIGQDDPKPFKLQAKTLGVsgmVEFLKGRSDIPRfllgADLLIHPAyneNTGTVLlEA 290
Cdd:COG1819   138 LRAVLEALADLGVRV-----VVTTGGLDPAELGPLPDNVRV---VDYVPQDALLPR----ADAVVHHG---GAGTTA-EA 201

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1332876537 291 LVAGLPVLV----TDVCGYAHYITDANCGRVVPSP-FEQQALDQMLAQMLADDAQRsawsRNALAFAE 353
Cdd:COG1819   202 LRAGVPQVVvpfgGDQPLNAARVERLGAGLALPPRrLTAEALRAALRRLLADPSYR----ERAARLAA 265
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 209-301 3.27e-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: 39.11  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 209 KGLDRSLKALAALPREL--SQRTRLLVIGQDDPKP----------FKLQAKTLGVSGMVEFLKGRSDIPRFLL--GADLL 274
Cdd:cd03805   224 KNIALAIEAFAKLKQKLpeFENVRLVIAGGYDPRVaenveyleelQRLAEELLNVEDQVLFLRSISDSQKEQLlsSALAL 303

                          90       100
                  ....*....|....*....|....*..
gi 1332876537 275 IHPAYNENTGTVLLEALVAGLPVLVTD 301
Cdd:cd03805   304 LYTPSNEHFGIVPLEAMYAGKPVIACN 330
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 193-356 4.08e-03

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 38.92  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 193 RPDELLLVQIGSGFKTKGLDRSLKALAALPRelsqrTRLLVIGqDDPKPFKLQAKTLGV----SGMvefLKGrSDIPRFL 268
Cdd:PLN02871  260 EPEKPLIVYVGRLGAEKNLDFLKRVMERLPG-----ARLAFVG-DGPYREELEKMFAGTptvfTGM---LQG-DELSQAY 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 269 LGADLLIHPAYNENTGTVLLEALVAGLPVLVTDVCGYAHYITDANCGrVVPSPFEQQALD---QMLAQMLADDAQRSAWS 345
Cdd:PLN02871  330 ASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPDQEG-KTGFLYTPGDVDdcvEKLETLLADPELRERMG 408

                         170
                  ....*....|.
gi 1332876537 346 RNALAFAETAD 356
Cdd:PLN02871  409 AAAREEVEKWD 419
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 199-354 5.63e-03

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: 38.59  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 199 LVQIGSGFKTKGLDRSLKALAALpRELSQRTRLLVIGQDDPKPFKLQA-KTLGVSGMVEFL--KGRSDIPRFLLGADLLI 275
Cdd:cd03799   177 ILTVGRLTEKKGLEYAIEAVAKL-AQKYPNIEYQIIGDGDLKEQLQQLiQELNIGDCVKLLgwKPQEEIIEILDEADIFI 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876537 276 HPAYNENTG------TVLLEALVAGLPVLVTDVCGYAHYITDANCGRVVPSPfEQQALDQMLAQMLADDAQRSAWSRNAL 349
Cdd:cd03799   256 APSVTAADGdqdgppNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPER-DAEAIAEKLTYLIEHPAIWPEMGKAGR 334


                  ....*
gi 1332876537 350 AFAET 354
Cdd:cd03799   335 ARVEE 339
 
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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