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Conserved domains on  [gi|2289277398|ref|WP_258366262|]
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MULTISPECIES: glycosyltransferase family 1 protein [unclassified Curtobacterium]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133585)

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:  16037492|12691742|10521532
SCOP:  3001586

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 16-386 4.50e-100

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: 302.29  E-value: 4.50e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  16 VAVVTESFLPTLNGVTTSVLAVLEHLRRRGHRAVVIAPDtpglaawrSRSEQERHLGfDVHRIPAVA---YRQFPVALPH 92
Cdd:cd03814     2 IALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVAPG--------PFDEAESAEG-RVVSVPSFPlpfYPEYRLALPL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  93 PVLDTILAASGA-DVLHAASPFLLGGRAITAAGRLGIPSVAVFQTDVAGFAQRNGLSAAAPLVRRVLGRIHAGASLTLAP 171
Cdd:cd03814    73 PRRVRRLIKEFQpDIIHIATPGPLGLAALRAARRLGLPVVTSYHTDFPEYLSYYTLGPLSWLAWAYLRWFHNPFDTTLVP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 172 SSATAAMLAEAGVPRVARWGRGVDTALFHPDRRSsahvRALRRRIAPNGETVVGYVGRLAPEKEVERLAE----LGGMPG 247
Cdd:cd03814   153 SPSIARELEGHGFERVRLWPRGVDTELFHPSRRD----AALRRRLGPPGRPLLLYVGRLAPEKNLEALLDadlpLAASPP 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 248 IRVVVAGGGPSRALLERRLrhLDVTFTGPLRGDALADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLV 327
Cdd:cd03814   229 VRLVVVGDGPARAELEARG--PDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIV 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2289277398 328 SPGLDGELYDPAAALSLRAAVARLHADRALAERMGSAGRLRVEGTTWESVGDELLAHHE 386
Cdd:cd03814   307 RPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERYSWEAFLDNLLDYYA 365
 
Name Accession Description Interval E-value
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 16-386 4.50e-100

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: 302.29  E-value: 4.50e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  16 VAVVTESFLPTLNGVTTSVLAVLEHLRRRGHRAVVIAPDtpglaawrSRSEQERHLGfDVHRIPAVA---YRQFPVALPH 92
Cdd:cd03814     2 IALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVAPG--------PFDEAESAEG-RVVSVPSFPlpfYPEYRLALPL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  93 PVLDTILAASGA-DVLHAASPFLLGGRAITAAGRLGIPSVAVFQTDVAGFAQRNGLSAAAPLVRRVLGRIHAGASLTLAP 171
Cdd:cd03814    73 PRRVRRLIKEFQpDIIHIATPGPLGLAALRAARRLGLPVVTSYHTDFPEYLSYYTLGPLSWLAWAYLRWFHNPFDTTLVP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 172 SSATAAMLAEAGVPRVARWGRGVDTALFHPDRRSsahvRALRRRIAPNGETVVGYVGRLAPEKEVERLAE----LGGMPG 247
Cdd:cd03814   153 SPSIARELEGHGFERVRLWPRGVDTELFHPSRRD----AALRRRLGPPGRPLLLYVGRLAPEKNLEALLDadlpLAASPP 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 248 IRVVVAGGGPSRALLERRLrhLDVTFTGPLRGDALADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLV 327
Cdd:cd03814   229 VRLVVVGDGPARAELEARG--PDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIV 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2289277398 328 SPGLDGELYDPAAALSLRAAVARLHADRALAERMGSAGRLRVEGTTWESVGDELLAHHE 386
Cdd:cd03814   307 RPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERYSWEAFLDNLLDYYA 365
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 7-376 2.17e-49

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 173.74  E-value: 2.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398   7 ERGDESPRTVAVVTE-SFLPTLNGVTTSVLAVLEHLRRRGHRAVVIAPD--TPglaawrsrseQERHlGFDV---HRIPA 80
Cdd:PLN02871   52 TDSRSRPRRIALFVEpSPFSYVSGYKNRFQNFIRYLREMGDEVLVVTTDegVP----------QEFH-GAKVigsWSFPC 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  81 VAYRQFP--VALPhPVLDTILAASGADVLHAASPFLLGGRAITAAGRLGIPSVAVFQTDVAGFAQRNGLSaaaPLVRRVL 158
Cdd:PLN02871  121 PFYQKVPlsLALS-PRIISEVARFKPDLIHASSPGIMVFGALFYAKLLCVPLVMSYHTHVPVYIPRYTFS---WLVKPMW 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 159 GRI---HAGASLTLAPSSATAAMLAEAGV---PRVARWGRGVDTALFHPDRRSSAhvraLRRRIApNGET---VVGYVGR 229
Cdd:PLN02871  197 DIIrflHRAADLTLVTSPALGKELEAAGVtaaNRIRVWNKGVDSESFHPRFRSEE----MRARLS-GGEPekpLIVYVGR 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 230 LAPEKEVERLAE-LGGMPGIRVVVAGGGPSRALLERRLRHLDVTFTGPLRGDALADAYAMLDVFVHTGAAETFGQTLQEA 308
Cdd:PLN02871  272 LGAEKNLDFLKRvMERLPGARLAFVGDGPYREELEKMFAGTPTVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEA 351

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2289277398 309 HAAGLPVVAPAAGGPLDLVSPGLDGE---LYDPAAALSLRAAVARLHADRALAERMGSAGRLRVEGTTWES 376
Cdd:PLN02871  352 MASGVPVVAARAGGIPDIIPPDQEGKtgfLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEKWDWRA 422
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 220-368 7.72e-27

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 105.05  E-value: 7.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 220 GETVVGYVGRLAPEKEVERLAE-----LGGMPGIRVVVAGGGPSRALLERRLRHL----DVTFTGPLRGDALADAYAMLD 290
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKafallKEKNPNLKLVIAGDGEEEKRLKKLAEKLglgdNVIFLGFVSDEDLPELLKIAD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2289277398 291 VFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAAALSLRAAVARLHADRALAERMGSAGRLR 368
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 169-370 1.68e-20

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 92.09  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 169 LAPSSATAAMLAEA-GVP--RVARWGRGVDTALFHPDRRSSAHVraLRRRIAPNGETVVGYVGRLAPEKE---------- 235
Cdd:TIGR03088 141 VAVSRDLEDWLRGPvKVPpaKIHQIYNGVDTERFHPSRGDRSPI--LPPDFFADESVVVGTVGRLQAVKDqptlvrafal 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 236 -VERLAElgGMPGIRVVVAGGGPSRALLERRLRHLDVTFTGPLRG--DALADAYAMLDVFVHTGAAETFGQTLQEAHAAG 312
Cdd:TIGR03088 219 lVRQLPE--GAERLRLVIVGDGPARGACEQMVRAAGLAHLVWLPGerDDVPALMQALDLFVLPSLAEGISNTILEAMASG 296

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2289277398 313 LPVVAPAAGGPLDLVSPGLDGELYDPAAALSLRAAVARLHADRALAERMGSAGRLRVE 370
Cdd:TIGR03088 297 LPVIATAVGGNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAE 354
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 280-384 5.80e-19

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 82.35  E-value: 5.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 280 DALADA-YAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAAALSLRAAVARLHADRALA 358
Cdd:COG0438    11 DLLLEAlLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELR 90

                          90       100
                  ....*....|....*....|....*..
gi 2289277398 359 ERMGSAGRLRVEGT-TWESVGDELLAH 384
Cdd:COG0438    91 RRLGEAARERAEERfSWEAIAERLLAL 117
 
Name Accession Description Interval E-value
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 16-386 4.50e-100

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: 302.29  E-value: 4.50e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  16 VAVVTESFLPTLNGVTTSVLAVLEHLRRRGHRAVVIAPDtpglaawrSRSEQERHLGfDVHRIPAVA---YRQFPVALPH 92
Cdd:cd03814     2 IALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVAPG--------PFDEAESAEG-RVVSVPSFPlpfYPEYRLALPL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  93 PVLDTILAASGA-DVLHAASPFLLGGRAITAAGRLGIPSVAVFQTDVAGFAQRNGLSAAAPLVRRVLGRIHAGASLTLAP 171
Cdd:cd03814    73 PRRVRRLIKEFQpDIIHIATPGPLGLAALRAARRLGLPVVTSYHTDFPEYLSYYTLGPLSWLAWAYLRWFHNPFDTTLVP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 172 SSATAAMLAEAGVPRVARWGRGVDTALFHPDRRSsahvRALRRRIAPNGETVVGYVGRLAPEKEVERLAE----LGGMPG 247
Cdd:cd03814   153 SPSIARELEGHGFERVRLWPRGVDTELFHPSRRD----AALRRRLGPPGRPLLLYVGRLAPEKNLEALLDadlpLAASPP 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 248 IRVVVAGGGPSRALLERRLrhLDVTFTGPLRGDALADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLV 327
Cdd:cd03814   229 VRLVVVGDGPARAELEARG--PDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIV 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2289277398 328 SPGLDGELYDPAAALSLRAAVARLHADRALAERMGSAGRLRVEGTTWESVGDELLAHHE 386
Cdd:cd03814   307 RPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERYSWEAFLDNLLDYYA 365
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 16-370 1.27e-56

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: 190.18  E-value: 1.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  16 VAVVTESFLPTLNGVTTSVLAVLEHLRRRGHRAVVIAPDTPGlaawrSRSEQERHlgfdVHRIPAVAYRQFP-VALPHPV 94
Cdd:cd03817     2 IAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITPSDPG-----AEDEEEVV----RYRSFSIPIRKYHrQHIPFPF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  95 LDTILAAS---GADVLHAASPFLLGGRAITAAGRLGIPSVAVFQT---DVAGFAQRNGLSA---AAPLVRRVLGRIHAga 165
Cdd:cd03817    73 KKAVIDRIkelGPDIIHTHTPFSLGKLGLRIARKLKIPIVHTYHTmyeDYLHYIPKGKLLVkavVRKLVRRFYNHTDA-- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 166 slTLAPSSATAAMLAEAG-------VPRvarwgrGVDTALFhpdrRSSAHVRALRRRIAPNGETVVGYVGRLAPEKEVER 238
Cdd:cd03817   151 --VIAPSEKIKDTLREYGvkgpievIPN------GIDLDKF----EKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDF 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 239 L----AELGGMPGIRVVVAGGGPSRALLERRLRHL----DVTFTGPLRGDALADAYAMLDVFVHTGAAETFGQTLQEAHA 310
Cdd:cd03817   219 LlrafAELKKEPNIKLVIVGDGPEREELKELARELgladKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMA 298

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 311 AGLPVVAPAAGGPLDLVSPGLDGELYDPAAALsLRAAVARLHADRALAERMGSAGRLRVE 370
Cdd:cd03817   299 AGLPVVAAKDPAASELVEDGENGFLFEPNDET-LAEKLLHLRENLELLRKLSKNAEISAR 357
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 7-376 2.17e-49

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 173.74  E-value: 2.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398   7 ERGDESPRTVAVVTE-SFLPTLNGVTTSVLAVLEHLRRRGHRAVVIAPD--TPglaawrsrseQERHlGFDV---HRIPA 80
Cdd:PLN02871   52 TDSRSRPRRIALFVEpSPFSYVSGYKNRFQNFIRYLREMGDEVLVVTTDegVP----------QEFH-GAKVigsWSFPC 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  81 VAYRQFP--VALPhPVLDTILAASGADVLHAASPFLLGGRAITAAGRLGIPSVAVFQTDVAGFAQRNGLSaaaPLVRRVL 158
Cdd:PLN02871  121 PFYQKVPlsLALS-PRIISEVARFKPDLIHASSPGIMVFGALFYAKLLCVPLVMSYHTHVPVYIPRYTFS---WLVKPMW 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 159 GRI---HAGASLTLAPSSATAAMLAEAGV---PRVARWGRGVDTALFHPDRRSSAhvraLRRRIApNGET---VVGYVGR 229
Cdd:PLN02871  197 DIIrflHRAADLTLVTSPALGKELEAAGVtaaNRIRVWNKGVDSESFHPRFRSEE----MRARLS-GGEPekpLIVYVGR 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 230 LAPEKEVERLAE-LGGMPGIRVVVAGGGPSRALLERRLRHLDVTFTGPLRGDALADAYAMLDVFVHTGAAETFGQTLQEA 308
Cdd:PLN02871  272 LGAEKNLDFLKRvMERLPGARLAFVGDGPYREELEKMFAGTPTVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEA 351

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2289277398 309 HAAGLPVVAPAAGGPLDLVSPGLDGE---LYDPAAALSLRAAVARLHADRALAERMGSAGRLRVEGTTWES 376
Cdd:PLN02871  352 MASGVPVVAARAGGIPDIIPPDQEGKtgfLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEKWDWRA 422
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 16-386 1.20e-42

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: 153.46  E-value: 1.20e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  16 VAVVTESFLPTLNGVTTSVLAVLEHLRRRGHRAVVIAPDTPGLAawrsrsEQERHLGFDVHRIPAVAYRQFPVALPHPvL 95
Cdd:cd03801     2 ILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEP------PEELEDGVIVPLLPSLAALLRARRLLRE-L 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  96 DTILAASGADVLHAASPFLLGGRAItAAGRLGIPSVAVFQTDVAGFaQRNGLSAAAPLVRRVLGRIHaGASLTLAPSSAT 175
Cdd:cd03801    75 RPLLRLRKFDVVHAHGLLAALLAAL-LALLLGAPLVVTLHGAEPGR-LLLLLAAERRLLARAEALLR-RADAVIAVSEAL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 176 AAMLAEAGVPRVARWGR---GVDTALFHPDRRssahvralRRRIAPNGETVVGYVGRLAPEKEVERLAE-----LGGMPG 247
Cdd:cd03801   152 RDELRALGGIPPEKIVVipnGVDLERFSPPLR--------RKLGIPPDRPVLLFVGRLSPRKGVDLLLEalaklLRRGPD 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 248 IRVVVAG-GGPSRALLERRLRHLD--VTFTGPLRGDALADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPL 324
Cdd:cd03801   224 VRLVIVGgDGPLRAELEELELGLGdrVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLP 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2289277398 325 DLVSPGLDGELYDPAAALSLRAAVARLHADRALAERMGSAGRLRVEGT-TWESVGDELLAHHE 386
Cdd:cd03801   304 EVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERfSWERVAERLLDLYR 366
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 40-388 9.67e-34

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: 129.42  E-value: 9.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  40 HLRRRGHRAVVIAPDTPGLAAWRSRSEQERHLGFdvHRIPAVAYRQFPVALP-----HPVLDTILAASG---ADVLHAAS 111
Cdd:cd03798    26 ALSRRGVDVEVLAPAPWGPAAARLLRKLLGEAVP--PRDGRRLLPLKPRLRLlaplrAPSLAKLLKRRRrgpPDLIHAHF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 112 PFLLGGRAITAAGRLGIPSV-AVFQTDVAGFAQRnglsaaaPLVRRVLGRIHAGASLTLAPSSATAAMLAEAGVPR--VA 188
Cdd:cd03798   104 AYPAGFAAALLARLYGVPYVvTEHGSDINVFPPR-------SLLRKLLRWALRRAARVIAVSKALAEELVALGVPRdrVD 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 189 RWGRGVDTALFHPdrrssahvrALRRRIAPNGETVVGYVGRLAPEKEVERLAE-----LGGMPGIRVVVAGGGPSRALLE 263
Cdd:cd03798   177 VIPNGVDPARFQP---------EDRGLGLPLDAFVILFVGRLIPRKGIDLLLEafarlAKARPDVVLLIVGDGPLREALR 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 264 RRLRHL----DVTFTGPLRGDALADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPA 339
Cdd:cd03798   248 ALAEDLglgdRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPG 327

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2289277398 340 AALSLRAAVARLHADRALAERMGSAGRLRVEGTTWESVGDELLAHHETA 388
Cdd:cd03798   328 DADALAAALRRALAEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 16-382 5.52e-28

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: 113.19  E-value: 5.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  16 VAVVTESFLPTLNGVTTSVLAVL-EHLRRRGHRAVVIAPD-TPGLAAWRSRSEQERHLGFDVHRIPAVAYRQFPVALPH- 92
Cdd:cd03823     2 ILLVNSLYPPQRVGGAEISVHDLaEALVAEGHEVAVLTAGvGPPGQATVARSVVRYRRAPDETLPLALKRRGYELFETYn 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  93 ----PVLDTILAASGADVLHAASPFLLGGRAITAAGRLGIPSVAVFqTDVAGFAQRNGLsaaaplvrrvlgrIHAGASLT 168
Cdd:cd03823    82 pglrRLLARLLEDFRPDVVHTHNLSGLGASLLDAARDLGIPVVHTL-HDYWLLCPRQFL-------------FKKGGDAV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 169 LAPSSATAAMLAEAGVPRVARwgrgvdtALFHPdrRSSAHVRALRRRIAPNGETVVGYVGRLAPEKEVERL---AELGGM 245
Cdd:cd03823   148 LAPSRFTANLHEANGLFSARI-------SVIPN--AVEPDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLveaFKRLPR 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 246 PGIRVVVAGGGPsraLLERRLRHLD--VTFTGPLRGDALADAYAMLDVF-VHTGAAETFGQTLQEAHAAGLPVVAPAAGG 322
Cdd:cd03823   219 EDIELVIAGHGP---LSDERQIEGGrrIAFLGRVPTDDIKDFYEKIDVLvVPSIWPEPFGLVVREAIAAGLPVIASDLGG 295

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 323 PLDLVSPGLDGELYDPAAALSLRAAVARLHADRALAERMGSAGRlrvEGTTWESVGDELL 382
Cdd:cd03823   296 IAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAE---PPRSTESQAEEYL 352
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 220-368 7.72e-27

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 105.05  E-value: 7.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 220 GETVVGYVGRLAPEKEVERLAE-----LGGMPGIRVVVAGGGPSRALLERRLRHL----DVTFTGPLRGDALADAYAMLD 290
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKafallKEKNPNLKLVIAGDGEEEKRLKKLAEKLglgdNVIFLGFVSDEDLPELLKIAD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2289277398 291 VFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAAALSLRAAVARLHADRALAERMGSAGRLR 368
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 29-368 1.07e-26

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: 109.37  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  29 GVTTSVLAVLEHLRRRGHRAVVIAPDTPGLAAWRsrseqERHLGFDVHRIPAVayrqfpVALPHPVLDTILAAS-GADVL 107
Cdd:cd03819    12 GAETYILDLARALAERGHRVLVVTAGGPLLPRLR-----QIGIGLPGLKVPLL------RALLGNVRLARLIRReRIDLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 108 HAAS--PFLLGGRAitaAGRLGIPSVAVFQTDVAgfaqRNGLSAAAPLVRRVLGRIHAgASLTLAPSSATAAMLAEAGVP 185
Cdd:cd03819    81 HAHSraPAWLGWLA---SRLTGVPLVTTVHGSYL----ATYHPKDFALAVRARGDRVI-AVSELVRDHLIEALGVDPERI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 186 RVARwgRGVDTALFHPDRRssahVRALRRRIAPNGETVVGYVGRLAPEKE----VERLAELGGMPGIRVVVAGGGPSRAL 261
Cdd:cd03819   153 RVIP--NGVDTDRFPPEAE----AEERAQLGLPEGKPVVGYVGRLSPEKGwlllVDAAAELKDEPDFRLLVAGDGPERDE 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 262 LERRLRHLD----VTFTGPLrgDALADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYD 337
Cdd:cd03819   227 IRRLVERLGlrdrVTFTGFR--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVP 304

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2289277398 338 PAAALSLRAAVARLHADRALAERMGSAGRLR 368
Cdd:cd03819   305 PGDAEALADAIRAAKLLPEAREKLQAAAALT 335
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 193-383 4.02e-26

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: 108.87  E-value: 4.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 193 GVDTALFHP-DRRSSAHVRALRRRIAPngetVVGYVGRLAPEKEVERLAE-LGGMP----GIRVVVAGG--GPSRALLER 264
Cdd:cd03800   195 GVDLERFFPvDRAEARRARLLLPPDKP----VVLALGRLDPRKGIDTLVRaFAQLPelreLANLVLVGGpsDDPLSMDRE 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 265 RLRHL--------DVTFTGPLRGDALADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELY 336
Cdd:cd03800   271 ELAELaeelglidRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLV 350

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2289277398 337 DPAAALSLRAAVARLHADRALAERMGSAGRLRVEGT-TWESVGDELLA 383
Cdd:cd03800   351 DPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHyTWESVADQLLT 398
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 29-370 9.33e-25

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: 104.32  E-value: 9.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  29 GVTTSVLAVLEHLRRRGHRAVVIAPDTPGlaawrSRSEQERHLGFDVHRIPAVAYRQFPVALPhpvLDTILAASGADVLH 108
Cdd:cd03807    13 GAETMLLRLLEHMDKSRFEHVVISLTGDG-----VLGEELLAAGVPVVCLGLSSGKDPGVLLR---LAKLIRKRNPDVVH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 109 A--ASPFLLGGraiTAAGRLGIPSVavfqtdVAGFAQRNGLSAAAPLVRRVLGRIHAGASLTLAPSSATAAMLAEAGVP- 185
Cdd:cd03807    85 TwmYHADLIGG---LAAKLAGGVKV------IWSVRSSNIPQRLTRLVRKLCLLLSKFSPATVANSSAVAEFHQEQGYAk 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 186 ---RVARwgRGVDTALFHPDRRSSAhvRALRRRIAPNGETVVGYVGRLAPEKEVERLAELGGM-----PGIRVVVAGGGP 257
Cdd:cd03807   156 nkiVVIY--NGIDLFKLSPDDASRA--RARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALlvethPDLRLLLVGRGP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 258 SRALLERRLRHL----DVTFTGPlRGDaLADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGlDG 333
Cdd:cd03807   232 ERPNLERLLLELgledRVHLLGE-RSD-VPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TG 308

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2289277398 334 ELYDPAAALSLRAAVARLHADRALAERMGSAGRLRVE 370
Cdd:cd03807   309 FLVPAGDPQALADAIRALLEDPEKRARLGRAARERIA 345
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 15-382 1.34e-24

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: 104.35  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  15 TVAVVTESFLPTLNGVTTSVLAVLEHLRRRGHRAVVIAPDTPGLAAWRSRSEQERHLGFDVHRIP------------AVA 82
Cdd:cd03794     1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGATETKDGIRVIRVKlgpikknglirrLLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  83 YRQFPVALPHPVLdtiLAASGADVLHA-ASPFLLGGRAITAAGRLGIPSVAVFQ-------TDVAGFAQRNGLSAAAPLV 154
Cdd:cd03794    81 YLSFALAALLKLL---VREERPDVIIAySPPITLGLAALLLKKLRGAPFILDVRdlwpeslIALGVLKKGSLLKLLKKLE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 155 RRVLgrihAGASLTLAPSSATAAMLAEAGVP--RVARWGRGVDTALFHPDRRSSahvraLRRRIAPNGETVVGYVGRLAP 232
Cdd:cd03794   158 RKLY----RLADAIIVLSPGLKEYLLRKGVPkeKIIVIPNWADLEEFKPPPKDE-----LRKKLGLDDKFVVVYAGNIGK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 233 EKEVERL----AELGGMPGIRVVVAGGGPSRALLERRLRHL---DVTFTGPLRGDALADAYAMLDVFVHTGAAETFGQT- 304
Cdd:cd03794   229 AQGLETLleaaERLKRRPDIRFLFVGDGDEKERLKELAKARgldNVTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGs 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 305 ----LQEAHAAGLPVVApAAGGPLDLVS----PGLDGELYDPAAalsLRAAVARLHADRALAERMGSAGRLRVEGT-TWE 375
Cdd:cd03794   309 spskLFEYMAAGKPILA-SDDGGSDLAVeingCGLVVEPGDPEA---LADAILELLDDPELRRAMGENGRELAEEKfSRE 384


                  ....*..
gi 2289277398 376 SVGDELL 382
Cdd:cd03794   385 KLADRLL 391
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 34-370 3.03e-23

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: 99.98  E-value: 3.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  34 VLAVLEHLRRRGHRAVVIAPDtpglaaWRSRSEQERHLGFDVHRIPavayrqFPVALPHPVLD--------TILAASGAD 105
Cdd:cd03808    16 RLPLIKALVKKGYEVHVIAPD------GDKLSDELKELGVKVIDIP------ILRRGINPLKDlkalfklyKLLKKEKPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 106 VLHAAS--PFLLGGraiTAAGRLGIPSVAVFqtdVAGFAqrnGLSAAAPLVRRVLGRIH----AGASLTLAPSSATAAML 179
Cdd:cd03808    84 IVHCHTpkPGILGR---LAARLAGVPKVIYT---VHGLG---FVFTEGKLLRLLYLLLEklalLFTDKVIFVNEDDRDLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 180 AEAGVPRVARW----GRGVDTALFHPdrrssahvralRRRIAPNGETVVGYVGRLAPEKEVERLAELGGM-----PGIRV 250
Cdd:cd03808   155 IKKGIIKKKKTvlipGSGVDLDRFQY-----------SPESLPSEKVVFLFVARLLKDKGIDELIEAAKIlkkkgPNVRF 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 251 VVAGGGPSRALLERRLRHL----DVTFTGPLrgDALADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDL 326
Cdd:cd03808   224 LLVGDGELENPSEILIEKLglegRIEFLGFR--SDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCREL 301

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2289277398 327 VSPGLDGELYDPAAALSLRAAVARLHADRALAERMGSAGRLRVE 370
Cdd:cd03808   302 VIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVE 345
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 169-370 1.68e-20

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 92.09  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 169 LAPSSATAAMLAEA-GVP--RVARWGRGVDTALFHPDRRSSAHVraLRRRIAPNGETVVGYVGRLAPEKE---------- 235
Cdd:TIGR03088 141 VAVSRDLEDWLRGPvKVPpaKIHQIYNGVDTERFHPSRGDRSPI--LPPDFFADESVVVGTVGRLQAVKDqptlvrafal 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 236 -VERLAElgGMPGIRVVVAGGGPSRALLERRLRHLDVTFTGPLRG--DALADAYAMLDVFVHTGAAETFGQTLQEAHAAG 312
Cdd:TIGR03088 219 lVRQLPE--GAERLRLVIVGDGPARGACEQMVRAAGLAHLVWLPGerDDVPALMQALDLFVLPSLAEGISNTILEAMASG 296

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2289277398 313 LPVVAPAAGGPLDLVSPGLDGELYDPAAALSLRAAVARLHADRALAERMGSAGRLRVE 370
Cdd:TIGR03088 297 LPVIATAVGGNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAE 354
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 280-384 5.80e-19

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 82.35  E-value: 5.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 280 DALADA-YAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAAALSLRAAVARLHADRALA 358
Cdd:COG0438    11 DLLLEAlLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELR 90

                          90       100
                  ....*....|....*....|....*..
gi 2289277398 359 ERMGSAGRLRVEGT-TWESVGDELLAH 384
Cdd:COG0438    91 RRLGEAARERAEERfSWEAIAERLLAL 117
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 193-371 4.26e-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: 85.08  E-value: 4.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 193 GVDTALFHPDRRSSAhvralRRRIAPNGETVVGYVGRLAPEKE-------VERLAELGGMPGIRVVVAGG-GPSRALLER 264
Cdd:cd03825   169 GIDTEIFAPVDKAKA-----RKRLGIPQDKKVILFGAESVTKPrkgfdelIEALKLLATKDDLLLVVFGKnDPQIVILPF 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 265 RLRHLdvtftGPLRGDA-LADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAAALS 343
Cdd:cd03825   244 DIISL-----GYIDDDEqLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQA 318

                         170       180
                  ....*....|....*....|....*...
gi 2289277398 344 LRAAVARLHADRALAERMGSAGRLRVEG 371
Cdd:cd03825   319 LAEAIEWLLANPKERESLGERARALAEN 346
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
223-354 5.59e-18

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 79.86  E-value: 5.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 223 VVGYVGRLAPE--------KEVERLAELGGmpGIRVVVAGGGPSRALlERRLRHLD--VTFTGPLrgDALADAYAMLDVF 292
Cdd:pfam13692   3 VILFVGRLHPNvkgvdyllEAVPLLRKRDN--DVRLVIVGDGPEEEL-EELAAGLEdrVIFTGFV--EDLAELLAAADVF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2289277398 293 VHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSpGLDGELYDPAAALSLRAAVARLHAD 354
Cdd:pfam13692  78 VLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVD-GENGLLVPPGDPEALAEAILRLLED 138
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 16-382 7.62e-18

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: 84.34  E-value: 7.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  16 VAVVTESFLPTLNGVTTSVLAVLEHLRRRGHRAVVIAPDTPGLAAWRSRSEQERHLGFDVHRIPA--VAYRQFPVAlPHP 93
Cdd:cd03821     2 ILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEENGRYIPPQDGFASIPLlrQGAGRTDFS-PGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  94 VLDTILAASGADVLH---AASPFLLggRAITAAGRLGIPSVAVFQTDVAGFAQRNGLSAAAPLVRRVLGRIHAGASLTLA 170
Cdd:cd03821    81 PNWLRRNLREYDVVHihgVWTYTSL--AACKLARRRGIPYVVSPHGMLDPWALQQKHWKKRIALHLIERRNLNNAALVHF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 171 PSSATAAMLAEAGVP-RVARWGRGVDTALFHPDRRSSAHVRAL-RRRIapngetvVGYVGRLAPEKEVERLAE-----LG 243
Cdd:cd03821   159 TSEQEADELRRFGLEpPIAVIPNGVDIPEFDPGLRDRRKHNGLeDRRI-------ILFLGRIHPKKGLDLLIRaarklAE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 244 GMPGIRVVVAGGGPSRALLERR------LRHlDVTFTGPLRGDALADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVV- 316
Cdd:cd03821   232 QGRDWHLVIAGPDDGAYPAFLQlqsslgLGD-RVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVi 310

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2289277398 317 APAAGGPlDLVSPGlDGELYDPAAAlSLRAAVA---RLHADRALAERMGSAGRLRVEGTTWESVGDELL 382
Cdd:cd03821   311 TDKCGLS-ELVEAG-CGVVVDPNVS-SLAEALAealRDPADRKRLGEMARRARQVEENFSWEAVAGQLG 376
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 223-360 1.62e-17

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: 83.18  E-value: 1.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 223 VVGYVGRLAPEKEVERL----AEL-GGMPGIRVVVAGGGPSRALLERRLRHLD----VTFTGPLrgdalADAYAML---D 290
Cdd:cd03811   190 VILAVGRLDPQKGHDLLieafAKLrKKYPDVKLVILGDGPLREELEKLAKELGlaerVIFLGFQ-----SNPYPYLkkaD 264

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2289277398 291 VFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAAALSLRAAVARLHA---DRALAER 360
Cdd:cd03811   265 LFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQkklDAALRER 337
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
28-197 1.11e-15

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 74.49  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  28 NGVTTSVLAVLEHLRRRGHRAVVIAPDTPGlaawrsRSEQERHLGFDVHRIPAVAYRQFPVALP-HPVLDTILAASGADV 106
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPG------PLAEEVVRVVRVPRVPLPLPPRLLRSLAfLRRLRRLLRRERPDV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 107 LHAASPFLLGGRAITAAGRLGIPSVAVF-QTDVAGFAQRNGLSAAAPLVRRVLGRIHAGASLTLAPSSATAAMLAEA-GV 184
Cdd:pfam13439  75 VHAHSPFPLGLAALAARLRLGIPLVVTYhGLFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLyGV 154

                         170
                  ....*....|....*
gi 2289277398 185 P--RVARWGRGVDTA 197
Cdd:pfam13439 155 PpeKIRVIPNGVDLE 169
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 40-366 1.41e-15

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: 77.49  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  40 HLRRrgHRAVVIAPDTPGLAAWRSRSEQERHLGFDVHRIPAVAYRQFPVALPHPVLdtilAASGADVLHAASPFLLGGRA 119
Cdd:cd05844    23 GLRR--YRPTFVGCRRLAPAPFDGVALRALGGSGPLRWLRQMAQRLLGWSAPRLGG----AAGLAPALVHAHFGRDGVYA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 120 ITAAGRLGIPSVAVFQ-----TDVAGFAQRNGLSAAAPLVRRVLGRihaGASLTLAPSSATAAMLAEAGVP--RVARWGR 192
Cdd:cd05844    97 LPLARALGVPLVVTFHgfditTSRAWLAASPGWPSQFQRHRRALQR---PAALFVAVSGFIRDRLLARGLPaeRIHVHYI 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 193 GVDTALFHPdrrssAHVRALRRRIApngetvvgYVGRLAPEKEVERLAEL-----GGMPGIRVVVAGGGPSRALLERRLR 267
Cdd:cd05844   174 GIDPAKFAP-----RDPAERAPTIL--------FVGRLVEKKGCDVLIEAfrrlaARHPTARLVIAGDGPLRPALQALAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 268 HLD-VTFTGPLRGDALADAYAMLDVFV------HTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAA 340
Cdd:cd05844   241 ALGrVRFLGALPHAEVQDWMRRAEIFClpsvtaASGDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGD 320

                         330       340
                  ....*....|....*....|....*.
gi 2289277398 341 ALSLRAAVARLHADRALAERMGSAGR 366
Cdd:cd05844   321 VDALADALQALLADRALADRMGGAAR 346
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 194-372 3.99e-14

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: 73.15  E-value: 3.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 194 VDTALFHPDRRSSAHvralRRRIAPNGETVVGYVGRLAPEKE----VERLAELGGMPGIRVVVAGGGPSRALLERRLRHL 269
Cdd:cd04962   173 IDEDVFKRKPAGALK----RRLLAPPDEKVVIHVSNFRPVKRiddvVRVFARVRRKIPAKLLLVGDGPERVPAEELAREL 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 270 ----DVTFTGPLrgDALADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAAALSLR 345
Cdd:cd04962   249 gvedRVLFLGKQ--DDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMA 326

                         170       180
                  ....*....|....*....|....*..
gi 2289277398 346 AAVARLHADRALAERMGSAGRLRVEGT 372
Cdd:cd04962   327 KSALSILEDDELYNRMGRAARKRAAER 353
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 16-322 1.22e-12

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 68.80  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  16 VAVVTESFLPTLNGVTTSVLAVLEHLRRRGHRAVVI---APDTPGLaawrsrseqeRHL--GFDVHRIP-AVAYRQ--FP 87
Cdd:cd03796     2 ICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVIthaYGNRVGV----------RYLtnGLKVYYLPfKVFYNQstLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  88 -VALPHPVLDTILAASGADVLHAASPF-LLGGRAITAAGRLGIPsvAVFqTD--VAGFAQrnglsaaaplvrrvLGRIHA 163
Cdd:cd03796    72 tLFSTFPLLRNILIRERIQIVHGHQAFsSLAHEALFHARTLGLK--TVF-TDhsLFGFAD--------------ASSILT 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 164 GASLTLAPS--------SATAA--MLAEAGVP--RVARWGRGVDTALFHPDRRssahvralrrRIAPNGETVVgYVGRLA 231
Cdd:cd03796   135 NKLLRFSLAdidhvicvSHTSKenTVLRASLDprIVSVIPNAVDSSDFTPDPS----------KPDPNKITIV-VISRLV 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 232 PEKEVERLAEL-----GGMPGIRVVVAGGGPSRALLER-RLRHL---DVTFTGPLRGDALADAYAMLDVFVHTGAAETFG 302
Cdd:cd03796   204 YRKGIDLLVGIipricKKHPNVRFIIGGDGPKRIELEEmREKYQlqdRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFC 283

                         330       340
                  ....*....|....*....|
gi 2289277398 303 QTLQEAHAAGLPVVAPAAGG 322
Cdd:cd03796   284 IAIVEAASCGLLVVSTRVGG 303
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 212-370 1.94e-12

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: 68.03  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 212 LRRRIAPNGETVVGYVGRLAPEKEVERLAE-----LGGMPGIRVVVAGGGPSRALLER---RLRHLDVTFTGPLRGDaLA 283
Cdd:cd03820   172 SEEPSTNLKSKRILAVGRLTYQKGFDLLIEawaliAKKHPDWKLRIYGDGPEREELEKlidKLGLEDRVKLLGPTKN-IA 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 284 DAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAA-GGPLDLVSPGLDGELYDPAAALSLRAAVARLHADRALAERMG 362
Cdd:cd03820   251 EEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCpTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMG 330


                  ....*...
gi 2289277398 363 SAGRLRVE 370
Cdd:cd03820   331 KNARKNAE 338
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 34-367 1.68e-11

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: 65.00  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  34 VLAVLEHLRRRGHRAVVIAP-DTPGLAawrsrseqerHLGFDVHRIPAVAYRQFPVALPHPV--LDTILAASGADVLHAA 110
Cdd:cd03802    24 VSALTEGLVRRGHEVTLFAPgDSHTSA----------PLVAVIPRALRLDPIPQESKLAELLeaLEVQLRASDFDVIHNH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 111 SPFLLGgraiTAAGRLGIPSVAvfqTDVAGFAQRNGLSAAAPlvRRVLgrihagaslTLAPSSATAAmlAEAGVPRVARW 190
Cdd:cd03802    94 SYDWLP----PFAPLIGTPFVT---TLHGPSIPPSLAIYAAE--PPVN---------YVSISDAQRA--ATPPIDYLTVV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 191 GRGVDTALFHPdrrssahvralrrriAPNGETVVGYVGRLAPEKEVERLAELGGMPGIRVVVAGGGPSRA---LLERRLR 267
Cdd:cd03802   154 HNGLDPADYRF---------------QPDPEDYLAFLGRIAPEKGLEDAIRVARRAGLPLKIAGKVRDEDyfyYLQEPLP 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 268 HLDVTFTGPL----RGDALADAYAMLDVFVHTgaaETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAAAls 343
Cdd:cd03802   219 GPRIEFIGEVghdeKQELLGGARALLFPINWD---EPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDSVEE-- 293

                         330       340
                  ....*....|....*....|....*....
gi 2289277398 344 LRAAVARL-----HADRALAERMGSAGRL 367
Cdd:cd03802   294 MAEAIANIdridrAACRRYAEDRFSAARM 322
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 226-336 1.84e-11

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: 63.58  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 226 YVGRLAPEKE----VERLAELG-GMPGIRVVVAGGGPSRALLERRLRHLD-----VTFTGPLRGDALADAYAMLDVFVHT 295
Cdd:cd01635   115 SVGRLVPEKGidllLEALALLKaRLPDLVLVLVGGGGEREEEEALAAALGllervVIIGGLVDDEVLELLLAAADVFVLP 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2289277398 296 GAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELY 336
Cdd:cd01635   195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 18-370 4.82e-11

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: 63.62  E-value: 4.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  18 VVTESFLptLNGVTtsvlavleHLRRRGHRaVVIAPDTPGlaawrsrSEQERHLGFDVHRIPAVayRQFPVALphpvldT 97
Cdd:cd03799    11 VLSETFI--LNQIT--------GLIDRGHE-VDIYAVNPG-------DLVKRHPDVEKYNVPSL--NLLYAIV------G 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  98 ILAASGADVLH-----AASPFLLGGRAITAAGRLgipsVAVFQ-TDVAGFAQRNGlsaaaplvRRVLGRIHAGASLTLAP 171
Cdd:cd03799    65 LNKKGAYDIIHcqfgpLGALGALLRRLKVLKGKL----VTSFRgYDISMYVILEG--------NKVYPQLFAQGDLFLPN 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 172 SSATAAMLAEAGVP--RVARWGRGVDTALFhpdrrssahvRALRRRIAPNGETVVGYVGRLAPEKEVE-------RLAEL 242
Cdd:cd03799   133 CELFKHRLIALGCDekKIIVHRSGIDCNKF----------RFKPRYLPLDGKIRILTVGRLTEKKGLEyaieavaKLAQK 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 243 GgmPGIRVVVAGGGPSRALLERRLRHLDVTFTGPLRG--------DAL--ADAYAMLDVFVHTGAAETFGQTLQEAHAAG 312
Cdd:cd03799   203 Y--PNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGwkpqeeiiEILdeADIFIAPSVTAADGDQDGPPNTLKEAMAMG 280

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2289277398 313 LPVVAPAAGGPLDLVSPGLDGELYDPAAALSLRAAVARLHADRALAERMGSAGRLRVE 370
Cdd:cd03799   281 LPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVE 338
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 226-370 5.78e-11

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 63.46  E-value: 5.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 226 YVGRLAPEKEVERLAELGGMPGIRVVVAGGGPSRALLERRLRHlDVTFTGPLRGDALADAYAMLDVFVHTGAaETFGQTL 305
Cdd:cd03804   204 TASRLVPYKRIDLAVEAFNELPKRLVVIGDGPDLDRLRAMASP-NVEFLGYQPDEVLKELLSKARAFVFAAE-EDFGIVP 281

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2289277398 306 QEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAAALSLRAAVARL---------HADRALAERMgSAGRLRVE 370
Cdd:cd03804   282 VEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEFeqnfdrfkpQAIRANAERF-SRARFRQE 354
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 220-370 1.96e-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: 61.91  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 220 GETVVGYVGRLAPEKEVERLAElgGMPGIR--VVVAGGGPSRALLERR---LRHLDVTFTGPLRGDALADAYAMLDVFV- 293
Cdd:cd03795   190 GKKIFLFIGRLVYYKGLDYLIE--AAQYLNypIVIGGEGPLKPDLEAQielNLLDNVKFLGRVDDEEKVIYLHLCDVFVf 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 294 --HTgAAETFGQTLQEAHAAGLPVVAPA-AGGPLDLVSPGLDGELYDPAAALSLRAAVARLHADRALAERMGSAGRLRVE 370
Cdd:cd03795   268 psVL-RSEAFGIVLLEAMMCGKPVISTNiGTGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFE 346
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 193-370 2.46e-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: 61.97  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 193 GVDTALFHPdrrssahvrALRRRiaPNGET-VVGYVGRLAPEKEVERLAE-----LGGMPGIRVVVAGG---GPSRALLE 263
Cdd:cd03813   275 GIDIQRFAP---------AREER--PEKEPpVVGLVGRVVPIKDVKTFIRafklvRRAMPDAEGWLIGPedeDPEYAQEC 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 264 RRL-RHLD----VTFTGPLRgdaLADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLD-----G 333
Cdd:cd03813   344 KRLvASLGlenkVKFLGFQN---IKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIYGADDalgqaG 420

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2289277398 334 ELYDPAAALSLRAAVARLHADRALAERMGSAGRLRVE 370
Cdd:cd03813   421 LVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVE 457
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 29-383 3.67e-10

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: 61.23  E-value: 3.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  29 GVTTSVLAVLEHLRRR-GHRAVVIAPDTPGLAAWRSRSEQERHLGFdvHRIPAVAYRqfpvALPHPVLDTILAASGADVL 107
Cdd:cd03809    15 GIGRYTRELLKALAKNdPDESVLAVPPLPGELLRLLREYPELSLGV--IKIKLWREL----ALLRWLQILLPKKDKPDLL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 108 HAASPFLLGGRAitaagrlGIPSVAVFQtDVAGFAQRNGLSAAAPLVRRVLGRIHA-GASLTLAPSSATAAMLAE--AGV 184
Cdd:cd03809    89 HSPHNTAPLLLK-------GCPQVVTIH-DLIPLRYPEFFPKRFRLYYRLLLPISLrRADAIITVSEATRDDIIKfyGVP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 185 PRVARWGRGVDTALFHPDRRSSAhvraLRRRIAPNGETVVgYVGRLAPEKEVERLAE-----LGGMPGIRVVVAGGGPSR 259
Cdd:cd03809   161 PEKIVVIPLGVDPSFFPPESAAV----LIAKYLLPEPYFL-YVGTLEPRKNHERLLKafallKKQGGDLKLVIVGGKGWE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 260 -----ALLERRLRHLDVTFTGPLRGDALADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVA------PAAGGPldlvs 328
Cdd:cd03809   236 deellDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIAsnisvlPEVAGD----- 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2289277398 329 pglDGELYDPAAALSLRAAVARLHADRALAERMGSAGRLRVEGTTWESVGDELLA 383
Cdd:cd03809   311 ---AALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 193-329 1.06e-09

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: 59.77  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 193 GVDTALFhpdRRSSAHVRALRRRIA-PNGETVVGYVGRLAPEKEVERLAE-----LGGMPGIRVVVAGGGPSRALLERRL 266
Cdd:cd04951   162 GIDLNKF---KKDINVRLKIRNKLNlKNDEFVILNVGRLTEAKDYPNLLLaiselILSKNDFKLLIAGDGPLRNELERLI 238

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2289277398 267 RHLD----VTFTGPLrgDALADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSP 329
Cdd:cd04951   239 CNLNlvdrVILLGQI--SNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGD 303
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
28-389 5.41e-09

Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 56.86  E-value: 5.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  28 NGVTTSVLAVLEHLRRRGHRAVVIAPDTPGLAAWRSrseqerhlgfdvhripavayrqfpvalphpvlDTILAASGADVL 107
Cdd:COG4641     6 NGHATYYRGLLRALAALGHEVTFLEPDDPWHDPLYA--------------------------------AELLDAFRPDLV 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 108 HAASpfllGGRAITAAGRLGIPSVAVFQTDVAGFAQrngLSAAAPLVRRVLgrihagasltlAPSSATAAMLAEAGVPRV 187
Cdd:COG4641    54 LVIS----GVELVAALRARGIPTVFWDTDDPVTLDR---FRELLPLYDLVF-----------TFDGDCVEEYRALGARRV 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 188 ARWGRGVDTALFHPDRRSSAHVRAlrrriapngetvVGYVGRLAPEKEvERLAEL-GGMPGIRVVVAGGG-PSRALLERR 265
Cdd:COG4641   116 FYLPFAADPELHRPVPPEARFRYD------------VAFVGNYYPDRR-ARLEELlLAPAGLRLKIYGPGwPKLALPANV 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 266 LRHldvtftGPLRGDALADAYA----MLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAAA 341
Cdd:COG4641   183 RRG------GHLPGEEHPAAYAsskiTLNVNRMAASPDSPTRRTFEAAACGAFLLSDPWEGLEELFEPGEEVLVFRDGEE 256

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2289277398 342 lsLRAAVARLHADRALAERMGSAGRLRV-EGTTWESVGDELLAHHETAR 389
Cdd:COG4641   257 --LAEKLRYLLADPEERRAIAEAGRRRVlAEHTYAHRARELLAILEELG 303
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
28-187 1.43e-08

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 53.56  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  28 NGVTTSVLAVLEHLRRRGHRAVVIAPDTPGlaawrsRSEQERHLGFDVHRIPAVAYRQFPVALPH-PVLDTILAASGADV 106
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPP------GRPELVGDGVRVHRLPVPPRPSPLADLAAlRRLRRLLRAERPDV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 107 LHAASPfLLGGRAITAAGRLGIPSVAVFQTDVAgfaqRNGLSAAAPLVRRVLGRIHAGASLTLAPSSATAAMLAEAGVPR 186
Cdd:pfam13579  75 VHAHSP-TAGLAARLARRRRGVPLVVTVHGLAL----DYGSGWKRRLARALERRLLRRADAVVVVSEAEAELLRALGVPA 149


                  .
gi 2289277398 187 V 187
Cdd:pfam13579 150 A 150
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 291-357 1.31e-06

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


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 50.55  E-value: 1.31e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2289277398  291 VFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAAALSLRAAVARLHADRAL 357
Cdd:TIGR02468  574 VFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKLVADKQL 640
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 16-384 2.54e-06

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: 49.31  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  16 VAVVTeSFLPTLNGVTTSVLAVLEHLRRRGHR--AVVIAPDTPGLAAwrsrseQERHLGFDVHRIPAVAYRQFPvalphp 93
Cdd:cd03822     2 IAVLG-TLPPRKCGIATYTDDLVEGLRKGGPVviVVIVSPQDEILKD------DDFEVPNEIKSWNSNEYFRLL------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398  94 vldTILAASGADVLHAASPF-LLGGRAITAAGRL----GIPSVAVFQTDVAgfaqrngLSAAAPLVRRVLGRIhagasLT 168
Cdd:cd03822    69 ---DHLNFKKPDVVHIQHEFgIFGGKYGLYALGLllhlRIPVITTLHTVLD-------LSDPGKQALKVLFRI-----AT 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 169 LAPSSATAAMLAEAGVPRVARWGRGVDTALFHP-DRRSSAHVRALRRRIAPNGETVVGYVGRLAPEKEVERLAE-----L 242
Cdd:cd03822   134 LSERVVVMAPISRFLLVRIKLIPAVNIEVIPHGvPEVPQDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEalpelK 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 243 GGMPGIRVVVAGG-GPS----------RALLERRLRHLDVTF-TGPLRGDALADAYAMLDVFV--HTGAAETFGQTLQEA 308
Cdd:cd03822   214 AEFPDVRLVIAGElHPSlaryegeryrKAAIEELGLQDHVDFhNNFLPEEEVPRYISAADVVVlpYLNTEQSSSGTLSYA 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 309 HAAGLPVVAPAAGGPLDLVSpGLDGELYDPAAALSLRAAVARLHAD----RALAERMGSAGRLRvegtTWESVGDELLAH 384
Cdd:cd03822   294 IACGKPVISTPLRHAEELLA-DGRGVLVPFDDPSAIAEAILRLLEDderrQAIAERAYAYARAM----TWESIADRYLRL 368
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 241-370 5.88e-06

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: 47.97  E-value: 5.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 241 ELGGMPGIRVVVAGGGPSRaLLE-----RRLRHL---------DVTF----TGPLRGDALADAYAMLdvfvHTGAAETFG 302
Cdd:cd03805   239 KLPEFENVRLVIAGGYDPR-VAEnveylEELQRLaeellnvedQVLFlrsiSDSQKEQLLSSALALL----YTPSNEHFG 313

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2289277398 303 QTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAAAlSLRAAVARLHADRALAERMGSAGRLRVE 370
Cdd:cd03805   314 IVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPE-AFAEAMLKLANDPDLADRMGAAGRKRVK 380
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 254-337 1.15e-05

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: 47.07  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 254 GGGPS----RALLERRLRHLDVTFTGPLRGDALADAYAM--LDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLV 327
Cdd:cd04946   264 GGGPLkerlEKLAENKLENVKVNFTGEVSNKEVKQLYKEndVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIV 343

                          90
                  ....*....|
gi 2289277398 328 SPGLDGELYD 337
Cdd:cd04946   344 ENETNGLLLD 353
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 206-316 2.00e-05

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: 46.13  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 206 SAHVRALRR-RIAPNGETVVGYVGRLAPEKEVERL----AELGGM-PGIRVVVAGGGPSRALLERRLRHL----DVTFTG 275
Cdd:cd03812   175 NKEKRRKRRkLLILEDKLVLGHVGRFNEQKNHSFLidifEELKKKnPNVKLVLVGEGELKEKIKEKVKELgledKVIFLG 254

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2289277398 276 pLRGDaLADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVV 316
Cdd:cd03812   255 -FRND-VSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCL 293
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 224-377 5.38e-05

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 44.98  E-value: 5.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 224 VGYVGRLAPEKEVERLAELGG-----MPGIRVVVAG-GGPSRALLERRLR-HLD--VTFTGPLRGdaLADAYAMLDVFVH 294
Cdd:cd04949   163 IITISRLAPEKQLDHLIEAVAkavkkVPEITLDIYGyGEEREKLKKLIEElHLEdnVFLKGYHSN--LDQEYQDAYLSLL 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 295 TGAAETFGQTLQEAHAAGLPVVA-PAAGGPLDLVSPGLDGELYDPAAALSLRAAVARLHADRALAERMGSAGRLRVEGTT 373
Cdd:cd04949   241 TSQMEGFGLTLMEAIGHGLPVVSyDVKYGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAEKYS 320


                  ....
gi 2289277398 374 WESV 377
Cdd:cd04949   321 TENV 324
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 211-360 5.87e-05

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 45.41  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 211 ALRRRIAPNGETVvGYVGRLAPEKEVERLAELGGM-----PGIRVVVAGGGP---SRALLERRLRHLD-VTFTGPLRgdA 281
Cdd:PRK15179  508 QFDARTSDARFTV-GTVMRVDDNKRPFLWVEAAQRfaashPKVRFIMVGGGPlleSVREFAQRLGMGErILFTGLSR--R 584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 282 LADAYAMLDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGEL--YDPAAALSLRAAVARLH----ADR 355
Cdd:PRK15179  585 VGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTlpADTVTAPDVAEALARIHdmcaADP 664


                  ....*
gi 2289277398 356 ALAER 360
Cdd:PRK15179  665 GIARK 669
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
297-383 7.65e-05

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 41.44  E-value: 7.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 297 AAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDGELYDPAAalSLRAAVARLHADRALAERMGSAGRLRV-EGTTWE 375
Cdd:pfam13524   8 RPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYRDPE--ELAEKIRYLLEHPEERRAIAAAGRERVlAEHTYA 85


                  ....*...
gi 2289277398 376 SVGDELLA 383
Cdd:pfam13524  86 HRAEQLLD 93
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
216-377 1.34e-04

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 43.63  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 216 IAPNgETVVGYVGRLAPEKEV-------ERLAELggMPGIRVVVAG-----GGPSRALLERRLRHL------DVTFTGPL 277
Cdd:PRK15484  189 ISPD-ETVLLYAGRISPDKGIlllmqafEKLATA--HSNLKLVVVGdptasSKGEKAAYQKKVLEAakrigdRCIMLGGQ 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 278 RGDALADAYAMLD-VFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGPLDLVSPGLDG-ELYDPAAALSLRAAVARLHADR 355
Cdd:PRK15484  266 PPEKMHNYYPLADlVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGyHLAEPMTSDSIISDINRTLADP 345

                         170       180
                  ....*....|....*....|..
gi 2289277398 356 ALAERMGSAGRLRVEGTTWESV 377
Cdd:PRK15484  346 ELTQIAEQAKDFVFSKYSWEGV 367
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 290-369 8.93e-04

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: 41.15  E-value: 8.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 290 DVFVHTGAAETFGQTLQEAHAAGLPVVA-PAAGGPLDlVSPGLDGELYDPAAALSLRaaVARLHADRALAERMGSAGRLR 368
Cdd:cd03792   281 TVVLQLSTREGFGLTVSEALWKGKPVIAtPAGGIPLQ-VIDGETGFLVNSVEGAAVR--ILRLLTDPELRRKMGLAAREH 357


                  .
gi 2289277398 369 V 369
Cdd:cd03792   358 V 358
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
290-340 2.61e-03

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 39.69  E-value: 2.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2289277398 290 DVFVHTGAAETFGQTLQEAHAAGLPVV-APAAGGPLDLVSPGLDGELYDPAA 340
Cdd:PRK09922  259 SALLLTSKFEGFPMTLLEAMSYGIPCIsSDCMSGPRDIIKPGLNGELYTPGN 310
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
246-347 3.46e-03

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 39.68  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289277398 246 PGIRVVVAGGGPSRALLERRLRHLDVTFTGPLRGDALADAYAM--LDVFVHTGAAETFGQTLQEAHAAGLPVVAPAAGGP 323
Cdd:PRK15490  428 PATRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLqkMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGS 507

                          90       100
                  ....*....|....*....|....
gi 2289277398 324 LDLVSPGLDGELYDPAAALSLRAA 347
Cdd:PRK15490  508 AECFIEGVSGFILDDAQTVNLDQA 531
 
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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