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Conserved domains on  [gi|1541847123|gb|RTP85385|]
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glycosyltransferase family 2 protein [Enterobacter asburiae]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135282)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  10521532|12691742|9445404|12200473|10508766
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4261 COG4261
Predicted acyltransferase, LPLAT superfamily [General function prediction only];
248-558 7.16e-103

Predicted acyltransferase, LPLAT superfamily [General function prediction only];


:

Pssm-ID: 443403  Cd Length: 300  Bit Score: 312.12  E-value: 7.16e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 248 QHWAQQDEVKGLWGMRLMLRVWKLMGHRAFTVLLWPVIGVYWLIARPARLASRQWIGRvkqelRQRNMPVPPRLNSFFHF 327
Cdd:COG4261     2 AHWAGQKERGSRLGLRLFVWIARRLGRRVARLLLYPVVLYFFLFAPKARRASRAYLRR-----LLGRSGPPGWRDVYRHF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 328 MRFGNAMLDKVASWRGelQFDR-DVVFaPGAsETLN--IAAPQGKLLLASHLGDVEACRALAQLDGSKTITALVFSENAR 404
Cdd:COG4261    77 LAFAQTILDRVALLSG--RIDLfDIDV-DGE-ELLRalLAQGRGGILLGAHLGNFEVLRALARRRPGLKINVLMHTEHAQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 405 RFKQIMSEMAPQAGVNLMSVTDiGPDTAIAIKEKLERGEWVAIVGDRIAvnpqrGGEwRVIWSPFMGQPAPFPQGPFILA 484
Cdd:COG4261   153 KINRLLEALNPKSAINIIQVGE-DPSTMLELKEALDRGELVAILGDRTP-----GGE-KTVEVDFLGAPAPFPQGPFLLA 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541847123 485 SILRCPVVLIFALRQ-QGKLVLHSEPFADPLRLPRGERQQALQETVDRYAQRLEHYALMSPLDWFNFFDFWHLPE 558
Cdd:COG4261   226 ALLKVPVYLVFGLKEgGNRYHLYFEPFADFLDLPRKEREAALQELLQRYAARLEHYCRKAPYQWFNFYDFWQDDE 300
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 9-190 1.40e-39

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


:

Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 142.71  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHGAMIARVLSRL-----APFGLPCLVVDDGSEASTRQELERLAAEQPQVTLVRLAQNAGKGAAVIRGLEECAR 83
Cdd:cd04179     1 VVIPAYNEEENIPELVERLlavleEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123  84 AgytHAVQVDADGQHAIEDIPKLLALAERHPDALISGQPIYDDS---IPRSRLYGRWVTHVWVWIeTLSLQLKDSMCGFR 160
Cdd:cd04179    81 D---IVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGgagMPLLRRLGSRLFNFLIRL-LLGVRISDTQSGFR 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1541847123 161 VYPVSpTLRLAARETLGKRMDFDTEVMVRL 190
Cdd:cd04179   157 LFRRE-VLEALLSLLESNGFEFGLELLVGA 185
 
Name Accession Description Interval E-value
COG4261 COG4261
Predicted acyltransferase, LPLAT superfamily [General function prediction only];
248-558 7.16e-103

Predicted acyltransferase, LPLAT superfamily [General function prediction only];


Pssm-ID: 443403  Cd Length: 300  Bit Score: 312.12  E-value: 7.16e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 248 QHWAQQDEVKGLWGMRLMLRVWKLMGHRAFTVLLWPVIGVYWLIARPARLASRQWIGRvkqelRQRNMPVPPRLNSFFHF 327
Cdd:COG4261     2 AHWAGQKERGSRLGLRLFVWIARRLGRRVARLLLYPVVLYFFLFAPKARRASRAYLRR-----LLGRSGPPGWRDVYRHF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 328 MRFGNAMLDKVASWRGelQFDR-DVVFaPGAsETLN--IAAPQGKLLLASHLGDVEACRALAQLDGSKTITALVFSENAR 404
Cdd:COG4261    77 LAFAQTILDRVALLSG--RIDLfDIDV-DGE-ELLRalLAQGRGGILLGAHLGNFEVLRALARRRPGLKINVLMHTEHAQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 405 RFKQIMSEMAPQAGVNLMSVTDiGPDTAIAIKEKLERGEWVAIVGDRIAvnpqrGGEwRVIWSPFMGQPAPFPQGPFILA 484
Cdd:COG4261   153 KINRLLEALNPKSAINIIQVGE-DPSTMLELKEALDRGELVAILGDRTP-----GGE-KTVEVDFLGAPAPFPQGPFLLA 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541847123 485 SILRCPVVLIFALRQ-QGKLVLHSEPFADPLRLPRGERQQALQETVDRYAQRLEHYALMSPLDWFNFFDFWHLPE 558
Cdd:COG4261   226 ALLKVPVYLVFGLKEgGNRYHLYFEPFADFLDLPRKEREAALQELLQRYAARLEHYCRKAPYQWFNFYDFWQDDE 300
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 9-190 1.40e-39

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 142.71  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHGAMIARVLSRL-----APFGLPCLVVDDGSEASTRQELERLAAEQPQVTLVRLAQNAGKGAAVIRGLEECAR 83
Cdd:cd04179     1 VVIPAYNEEENIPELVERLlavleEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123  84 AgytHAVQVDADGQHAIEDIPKLLALAERHPDALISGQPIYDDS---IPRSRLYGRWVTHVWVWIeTLSLQLKDSMCGFR 160
Cdd:cd04179    81 D---IVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGgagMPLLRRLGSRLFNFLIRL-LLGVRISDTQSGFR 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1541847123 161 VYPVSpTLRLAARETLGKRMDFDTEVMVRL 190
Cdd:cd04179   157 LFRRE-VLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 8-203 5.12e-34

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 128.28  E-value: 5.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   8 CVLIPCYNHGAMIARVLSRLA---PFGLPCLVVDDGSEASTRQELERLAAEQPQVTLVRLAQNAGKGAAVIRGLEecaRA 84
Cdd:COG0463     5 SVVIPTYNEEEYLEEALESLLaqtYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLA---AA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123  85 GYTHAVQVDADGQHAIEDIPKLLALAERHPDALISGQPIYDDSIPRSRLYGRWVTHVWVWIetlsLQLKDSMCGFRVYPV 164
Cdd:COG0463    82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLL----TNLPDSTSGFRLFRR 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1541847123 165 SPTLRLAaretLGKRMDFDTEvMVRLYWQGNTSVFLPTR 203
Cdd:COG0463   158 EVLEELG----FDEGFLEDTE-LLRALRHGFRIAEVPVR 191
LPLAT_LABLAT-like cd07984
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ...
 363-555 1.47e-21

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lipid A biosynthesis lauroyl/myristoyl (LABLAT, HtrB) acyltransferases and similar proteins.


Pssm-ID: 153246 [Multi-domain]  Cd Length: 192  Bit Score: 92.66  E-value: 1.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 363 IAAPQGKLLLASHLGDVEACRALAQLDGsKTITALVFSENARRFKQIMSEMAPQAGVNLMSVTDigpdTAIAIKEKLERG 442
Cdd:cd07984    16 LAKGKGVILLTAHFGNWELAGLALALLG-YPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGG----GLRELIRALKKG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 443 EWVAIVGDRiavNPQRGGewrVIWSPFMGQPAPFPQGPFILASILRCPVVLIFALRQQ-GKLVLHSEPFADPlrlprgER 521
Cdd:cd07984    91 EIVGILPDQ---DPGRKG---GVFVPFFGRPAATPTGPARLALKTGAPVVPAFAYRLPgGGYRIEFEPPLEN------PP 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1541847123 522 QQALQETVDRYAQRLEHYALMSPLDWFNFFDFWH 555
Cdd:cd07984   159 SEDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 8-166 2.99e-19

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 85.14  E-value: 2.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   8 CVLIPCYNHGAMIARVLSRLAPFGLP---CLVVDDGSEASTRQELERLAAEQPQVTLVRLAQNAGKGAAVIRGLEEcARA 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPnfeIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA-ATG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123  85 GYthAVQVDADGQHAIEDIPKLLALAERHPDALISGQPIYDDSIPRSRLYGRWVTHVWVWIETLSLQLKDSM----CGFR 160
Cdd:pfam00535  80 DY--IAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLpfliGGFA 157


                  ....*.
gi 1541847123 161 VYPVSP 166
Cdd:pfam00535 158 LYRREA 163
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 9-187 2.59e-09

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 59.01  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHGAMIARVL----------SRLAP-FGLPCLVVDDGSEASTRQELERLAAEQPQ----VTLVRLAQNAGKGAA 73
Cdd:PTZ00260   74 IVIPAYNEEDRLPKMLketikylesrSRKDPkFKYEIIIVNDGSKDKTLKVAKDFWRQNINpnidIRLLSLLRNKGKGGA 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123  74 VIRGLeECARAGYThaVQVDADGQHAIEDIPKLLALAERHPD---ALISGQP--IYDDSIPRSRLYGRWVT----HVWVW 144
Cdd:PTZ00260  154 VRIGM-LASRGKYI--LMVDADGATDIDDFDKLEDIMLKIEQnglGIVFGSRnhLVDSDVVAKRKWYRNILmygfHFIVN 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1541847123 145 IeTLSLQLKDSMCGFRVYPvsptlRLAARETLG----KRMDFDTEVM 187
Cdd:PTZ00260  231 T-ICGTNLKDTQCGFKLFT-----RETARIIFPslhlERWAFDIEIV 271
 
Name Accession Description Interval E-value
COG4261 COG4261
Predicted acyltransferase, LPLAT superfamily [General function prediction only];
248-558 7.16e-103

Predicted acyltransferase, LPLAT superfamily [General function prediction only];


Pssm-ID: 443403  Cd Length: 300  Bit Score: 312.12  E-value: 7.16e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 248 QHWAQQDEVKGLWGMRLMLRVWKLMGHRAFTVLLWPVIGVYWLIARPARLASRQWIGRvkqelRQRNMPVPPRLNSFFHF 327
Cdd:COG4261     2 AHWAGQKERGSRLGLRLFVWIARRLGRRVARLLLYPVVLYFFLFAPKARRASRAYLRR-----LLGRSGPPGWRDVYRHF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 328 MRFGNAMLDKVASWRGelQFDR-DVVFaPGAsETLN--IAAPQGKLLLASHLGDVEACRALAQLDGSKTITALVFSENAR 404
Cdd:COG4261    77 LAFAQTILDRVALLSG--RIDLfDIDV-DGE-ELLRalLAQGRGGILLGAHLGNFEVLRALARRRPGLKINVLMHTEHAQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 405 RFKQIMSEMAPQAGVNLMSVTDiGPDTAIAIKEKLERGEWVAIVGDRIAvnpqrGGEwRVIWSPFMGQPAPFPQGPFILA 484
Cdd:COG4261   153 KINRLLEALNPKSAINIIQVGE-DPSTMLELKEALDRGELVAILGDRTP-----GGE-KTVEVDFLGAPAPFPQGPFLLA 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541847123 485 SILRCPVVLIFALRQ-QGKLVLHSEPFADPLRLPRGERQQALQETVDRYAQRLEHYALMSPLDWFNFFDFWHLPE 558
Cdd:COG4261   226 ALLKVPVYLVFGLKEgGNRYHLYFEPFADFLDLPRKEREAALQELLQRYAARLEHYCRKAPYQWFNFYDFWQDDE 300
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 9-190 1.40e-39

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 142.71  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHGAMIARVLSRL-----APFGLPCLVVDDGSEASTRQELERLAAEQPQVTLVRLAQNAGKGAAVIRGLEECAR 83
Cdd:cd04179     1 VVIPAYNEEENIPELVERLlavleEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123  84 AgytHAVQVDADGQHAIEDIPKLLALAERHPDALISGQPIYDDS---IPRSRLYGRWVTHVWVWIeTLSLQLKDSMCGFR 160
Cdd:cd04179    81 D---IVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGgagMPLLRRLGSRLFNFLIRL-LLGVRISDTQSGFR 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1541847123 161 VYPVSpTLRLAARETLGKRMDFDTEVMVRL 190
Cdd:cd04179   157 LFRRE-VLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 8-203 5.12e-34

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 128.28  E-value: 5.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   8 CVLIPCYNHGAMIARVLSRLA---PFGLPCLVVDDGSEASTRQELERLAAEQPQVTLVRLAQNAGKGAAVIRGLEecaRA 84
Cdd:COG0463     5 SVVIPTYNEEEYLEEALESLLaqtYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLA---AA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123  85 GYTHAVQVDADGQHAIEDIPKLLALAERHPDALISGQPIYDDSIPRSRLYGRWVTHVWVWIetlsLQLKDSMCGFRVYPV 164
Cdd:COG0463    82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLL----TNLPDSTSGFRLFRR 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1541847123 165 SPTLRLAaretLGKRMDFDTEvMVRLYWQGNTSVFLPTR 203
Cdd:COG0463   158 EVLEELG----FDEGFLEDTE-LLRALRHGFRIAEVPVR 191
LPLAT_LABLAT-like cd07984
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ...
 363-555 1.47e-21

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lipid A biosynthesis lauroyl/myristoyl (LABLAT, HtrB) acyltransferases and similar proteins.


Pssm-ID: 153246 [Multi-domain]  Cd Length: 192  Bit Score: 92.66  E-value: 1.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 363 IAAPQGKLLLASHLGDVEACRALAQLDGsKTITALVFSENARRFKQIMSEMAPQAGVNLMSVTDigpdTAIAIKEKLERG 442
Cdd:cd07984    16 LAKGKGVILLTAHFGNWELAGLALALLG-YPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGG----GLRELIRALKKG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 443 EWVAIVGDRiavNPQRGGewrVIWSPFMGQPAPFPQGPFILASILRCPVVLIFALRQQ-GKLVLHSEPFADPlrlprgER 521
Cdd:cd07984    91 EIVGILPDQ---DPGRKG---GVFVPFFGRPAATPTGPARLALKTGAPVVPAFAYRLPgGGYRIEFEPPLEN------PP 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1541847123 522 QQALQETVDRYAQRLEHYALMSPLDWFNFFDFWH 555
Cdd:cd07984   159 SEDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 8-166 2.99e-19

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 85.14  E-value: 2.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   8 CVLIPCYNHGAMIARVLSRLAPFGLP---CLVVDDGSEASTRQELERLAAEQPQVTLVRLAQNAGKGAAVIRGLEEcARA 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPnfeIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA-ATG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123  85 GYthAVQVDADGQHAIEDIPKLLALAERHPDALISGQPIYDDSIPRSRLYGRWVTHVWVWIETLSLQLKDSM----CGFR 160
Cdd:pfam00535  80 DY--IAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLpfliGGFA 157


                  ....*.
gi 1541847123 161 VYPVSP 166
Cdd:pfam00535 158 LYRREA 163
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 9-162 2.30e-18

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 82.91  E-value: 2.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHGAMI----ARVLSRLAPFGLPC--LVVDDGSEASTRQELERLAAEQPQVTLVRLAQNAGKGAAVIRGLEEcA 82
Cdd:cd04187     1 IVVPVYNEEENLpelyERLKAVLESLGYDYeiIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDH-A 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123  83 RAGYthAVQVDADGQHAIEDIPKLLALAERHPDaLISGQPIY-DDSIPR---SRLYGRWVTHVwvwietLSLQLKDSMCG 158
Cdd:cd04187    80 RGDA--VITMDADLQDPPELIPEMLAKWEEGYD-VVYGVRKNrKESWLKrltSKLFYRLINKL------SGVDIPDNGGD 150


                  ....
gi 1541847123 159 FRVY 162
Cdd:cd04187   151 FRLM 154
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 9-196 3.25e-17

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 80.66  E-value: 3.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNH----GAMIARVLSRLAPFGLPCLVVDDGSEASTRQELERLAAEQPQVTLVRLAQNAGKGAAVIRGLEEcARA 84
Cdd:cd06442     1 IIIPTYNEreniPELIERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKA-ARG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123  85 GYthAVQVDADGQHAIEDIPKLLAlAERHPDA-------LISGQPIYDDSIPR------SRLYGRWVthvwvwietLSLQ 151
Cdd:cd06442    80 DV--IVVMDADLSHPPEYIPELLE-AQLEGGAdlvigsrYVEGGGVEGWGLKRklisrgANLLARLL---------LGRK 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1541847123 152 LKDSMCGFRVYPVSpTLRLAARETLGKRMDFDTEVMVRLYWQGNT 196
Cdd:cd06442   148 VSDPTSGFRAYRRE-VLEKLIDSLVSKGYKFQLELLVRARRLGYR 191
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 9-190 1.34e-16

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 78.76  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNH----GAMIARV---LSRLAPFGLPCLVVDDGSEASTRQELERLAAEQPQ-VTLVRLAQNAGKGAAVIRGLeE 80
Cdd:cd04188     1 VVIPAYNEekrlPPTLEEAveyLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPAlIRVLTLPKNRGKGGAVRAGM-L 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123  81 CARAGYthAVQVDADGQHAIEDIPKLLALAE-RHPDALI------SGQPIYDDSIPRsRLYGRwVTHVWVWIeTLSLQLK 153
Cdd:cd04188    80 AARGDY--ILFADADLATPFEELEKLEEALKtSGYDIAIgsrahlASAAVVKRSWLR-NLLGR-GFNFLVRL-LLGLGIK 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1541847123 154 DSMCGFRVYPVSPTLRLAARETLgKRMDFDTEVMVRL 190
Cdd:cd04188   155 DTQCGFKLFTRDAARRLFPRLHL-ERWAFDVELLVLA 190
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 9-124 9.57e-15

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 71.77  E-value: 9.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHGAMIARVLSRLAPFGLP---CLVVDDGSEASTRQELERLAAEQPQVTLVRLAQNAGKGAAVIRGLEEcARAG 85
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPnfeVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKA-ARGE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1541847123  86 YThaVQVDADGQHAIEDIPKLLALAERHPDA-LISGQPIY 124
Cdd:cd00761    80 YI--LFLDADDLLLPDWLERLVAELLADPEAdAVGGPGNL 117
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 9-116 1.01e-11

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 63.79  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHGAMIARVLSRLA-----PFGLpcLVVDDGSEASTRQELERLAAEQPQ-VTLVRLAQNAGKGAAVIRGLEeca 82
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLaldypKLEV--IVVDDGSTDDTLEILEELAALYIRrVLVVRDKENGGKAGALNAGLR--- 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1541847123  83 RAGYTHAVQVDADGQhaIED--IPKLLALAERHPDA 116
Cdd:cd06423    76 HAKGDIVVVLDADTI--LEPdaLKRLVVPFFADPKV 109
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 9-120 1.54e-11

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 65.53  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHGAMIARVLSRLA-----PFGLPCLVVDDGSEASTRQELERLAAEQPQVTLVRLAQNAGKGAAVIRGLEecaR 83
Cdd:COG1215    33 VIIPAYNEEAVIEETLRSLLaqdypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAGLK---A 109

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1541847123  84 AGYTHAVQVDADGQHAIEDIPKLLALAErHPDALISG 120
Cdd:COG1215   110 ARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGVGASG 145
LpxP COG1560
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ...
 326-554 9.59e-10

Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and metabolism]; Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 441168 [Multi-domain]  Cd Length: 271  Bit Score: 59.43  E-value: 9.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 326 HFMRFGNAMLDKVASWRGELQFDRDVVFAPGAsETLNIAAPQGK--LLLASHLGDVEACRALAQLDGSKTITalVFSEN- 402
Cdd:COG1560    58 SFRNLGRTLLETLRLWRLSPERLRKRVEVEGL-EHLEAALAEGRgvILLTPHFGNWELAGAALALRGYPVTA--VYRPLk 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 403 ----ARRFKQI----MSEMAPQAgvnlmsvtdigpDTAIAIKEKLERGEWVAIVGDriavnpQRGGEWRVIWSPFMGQPA 474
Cdd:COG1560   135 npllDRLIRRGrerfGGELIPRK------------DGVRALLRALRKGGIVGLLPD------QDPGRKSGVFVPFFGVPA 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123 475 PFPQGPFILASILRCPVVLIFALRQQG----KLVLHsEPFADPlrlprgerQQALQETVDRYAQRLEHYALMSPLDWFNF 550
Cdd:COG1560   197 ATPTGPARLARRTGAPVVPVFARRLPDgrgyRLEIE-PPLEDF--------SEDVEADTQRLNRALEAWIREHPEQWLWL 267


                  ....
gi 1541847123 551 FDFW 554
Cdd:COG1560   268 HRRW 271
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 9-187 2.59e-09

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 59.01  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHGAMIARVL----------SRLAP-FGLPCLVVDDGSEASTRQELERLAAEQPQ----VTLVRLAQNAGKGAA 73
Cdd:PTZ00260   74 IVIPAYNEEDRLPKMLketikylesrSRKDPkFKYEIIIVNDGSKDKTLKVAKDFWRQNINpnidIRLLSLLRNKGKGGA 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123  74 VIRGLeECARAGYThaVQVDADGQHAIEDIPKLLALAERHPD---ALISGQP--IYDDSIPRSRLYGRWVT----HVWVW 144
Cdd:PTZ00260  154 VRIGM-LASRGKYI--LMVDADGATDIDDFDKLEDIMLKIEQnglGIVFGSRnhLVDSDVVAKRKWYRNILmygfHFIVN 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1541847123 145 IeTLSLQLKDSMCGFRVYPvsptlRLAARETLG----KRMDFDTEVM 187
Cdd:PTZ00260  231 T-ICGTNLKDTQCGFKLFT-----RETARIIFPslhlERWAFDIEIV 271
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
9-81 1.10e-06

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 49.61  E-value: 1.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1541847123   9 VLIPCYNHGAMIARVLSRLA---PFGLPCLVVDDGSEASTRQELERLAAeqPQVTLVRLAQNAGKGAAVIRGLEEC 81
Cdd:COG1216     7 VVIPTYNRPELLRRCLESLLaqtYPPFEVIVVDNGSTDGTAELLAALAF--PRVRVIRNPENLGFAAARNLGLRAA 80
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 9-111 1.13e-05

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 47.42  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHG----AMIARVLSRLAPFGLP--CLVVDDGSEASTRQELERlAAEQP--QVTLVRLAQNAGKGAAVIrglee 80
Cdd:PRK10714   10 VVIPVYNEQeslpELIRRTTAACESLGKEyeILLIDDGSSDNSAEMLVE-AAQAPdsHIVAILLNRNYGQHSAIM----- 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1541847123  81 carAGYTHA-----VQVDADGQHAIEDIPKLLALAE 111
Cdd:PRK10714   84 ---AGFSHVtgdliITLDADLQNPPEEIPRLVAKAD 116
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 9-97 2.06e-05

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 45.45  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHGAMIARVLSRLAPF--GLPCLVVDDGSEASTrQELERLAAEQPQVTLV-RLAQNA--GKGAAV------IRG 77
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRNkpNFLVLVIDDASDDDT-AGIVRLAITDSRVHLLrRHLPNArtGKGDALnaaydqIRQ 79

                          90       100
                  ....*....|....*....|..
gi 1541847123  78 LEECARAGYTHAV--QVDADGQ 97
Cdd:cd06436    80 ILIEEGADPERVIiaVIDADGR 101
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 9-131 3.20e-05

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 45.69  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHGAMIARVLSRLAPFGLPC-----LVVDDGSEASTRQELERLAAEQPQVTLVrlaQNAGK--GAAVIRGLEEc 81
Cdd:cd02525     4 IIIPVRNEEKYIEELLESLLNQSYPKdlieiIVVDGGSTDGTREIVQEYAAKDPRIRLI---DNPKRiqSAGLNIGIRN- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1541847123  82 ARAGYThaVQVDADGQHAIEDIPKLLALAERhPDALISGQPIydDSIPRS 131
Cdd:cd02525    80 SRGDII--IRVDAHAVYPKDYILELVEALKR-TGADNVGGPM--ETIGES 124
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 3-145 8.33e-05

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 44.20  E-value: 8.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   3 VTFRPcvlipcyNHGAMIARVLSrLAPFGLPCLVVDDGSEASTRQELERLAAeqpQVTLVRLAQNAGKGAAVIRGLEECA 82
Cdd:cd02526     4 VTYNP-------DLSKLKELLAA-LAEQVDKVVVVDNSSGNDIELRLRLNSE---KIELIHLGENLGIAKALNIGIKAAL 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1541847123  83 RAGYTHAVQVDAD---GQHAIEDIPKLLALAERHPDALISGqPIYDDSIPRSRLYGRWVTHVWVWI 145
Cdd:cd02526    73 ENGADYVLLFDQDsvpPPDMVEKLLAYKILSDKNSNIGAVG-PRIIDRRTGENSPGVRKSGYKLRI 137
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 9-120 3.41e-04

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 41.39  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHGAMIARV---LSRLAPFGLPCLVVDDGSEASTRQELERLaaeQPQVTLVRLAQNAGKGAAVIRGLeecARAG 85
Cdd:cd04186     1 IIIVNYNSLEYLKACldsLLAQTYPDFEVIVVDNASTDGSVELLREL---FPEVRLIRNGENLGFGAGNNQGI---REAK 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1541847123  86 YTHAVQVDADGQHAIEDIPKLLALAERHPDALISG 120
Cdd:cd04186    75 GDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIVG 109
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 1-133 5.89e-04

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 42.34  E-value: 5.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   1 MSVTFRPCVLIPCYNHGAM--------IARVLSRLApfglpCLVVDDGSEASTRQELERLAAEQPQVTLVRlAQNAGKGA 72
Cdd:PRK10073    2 MNSTPKLSIIIPLYNAGKDfrafmeslIAQTWTALE-----IIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1541847123  73 AVIRGLeecARAGYTHAVQVDADGQHAIEDIPKLLALAER-HPD-ALISGQPIYDD------SIPRSRL 133
Cdd:PRK10073   76 ARNTGL---AVATGKYVAFPDADDVVYPTMYETLMTMALEdDLDvAQCNADWCFRDtgetwqSIPSDRL 141
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 9-81 5.94e-04

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 41.80  E-value: 5.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541847123   9 VLIPCYNHGAMIARVLSRLAPFGLP-----CLVVDDGSEASTRQELERLAaeQPQVTLVRLAQNAGKGAAVIRGLEEC 81
Cdd:cd06439    33 IIIPAYNEEAVIEAKLENLLALDYPrdrleIIVVSDGSTDGTAEIAREYA--DKGVKLLRFPERRGKAAALNRALALA 108
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 9-124 3.03e-03

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 39.58  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541847123   9 VLIPCYNHGAMIARVLSRLAPFGLP-----CLVVDDGSEASTRQELERLAAEQ-PQVTLVRLAQ--NAGKGAAVIRGLEE 80
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPkekfeVILVDDHSTDGTVQILEFAAAKPnFQLKILNNSRvsISGKKNALTTAIKA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1541847123  81 carAGYTHAVQVDADGQHAIEDIPKLLALAERHPDALISGQPIY 124
Cdd:cd04192    81 ---AKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIY 121
 
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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