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Conserved domains on  [gi|1147393137|ref|WP_077205466|]
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flippase-like domain-containing protein [Halorientalis sp. IM1011]

Protein Classification

lysylphosphatidylglycerol synthetase family protein( domain architecture ID 10135793)

lysylphosphatidylglycerol synthetase family membrane protein similar to Escherichia coli inner membrane protein YbhN

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
9-217 2.41e-76

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: 242.09  E-value: 2.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   9 VVLPAYNEAETLEDTVEITLETLESFlPAESFEVIVAEDGCADRTPEIAERLASD-DERVRHFHSDERLGRGKALEAAFR 87
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEER-PSFSYEIIVVDDGSKDGTAEVARKLARKnPALIRVLTLPKNRGKGGAVRAGML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  88 ASEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATGSRWVPGAD--ADRPAKRGIPSKGYNRLVRLFLRSDLLDHQCG 165
Cdd:cd04188    80 AARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHLASAavVKRSWLRNLLGRGFNFLVRLLLGLGIKDTQCG 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1147393137 166 FKAFDREALLSLLDDVEDEHWFWDTEVLVRAQRAGYRVAEFPVEWTPQGDSK 217
Cdd:cd04188   160 FKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
AglD2 COG0392
Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis] ...
277-596 4.90e-37

Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440161  Cd Length: 289  Bit Score: 139.70  E-value: 4.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 277 ITGADPALVALSGVVYLLSWPLRGLRYRDILSRLDYDGDTWFLTGAIFISQTGNLVFP-ARAGDAVRAYVVKaRRSIPYP 355
Cdd:COG0392     1 LRAANPWWLLLALLLTLLSYLLLALRWRLLLRALGVKLPFRRLFLVSFIGYFGNNIGPgALGGEAVRARLLS-RRGVPAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 356 TGFASLAVERVFDLLSITVLGGTVLLGLVATggtdevvaaiaadvgtitIGGETLNPAAAAETAMGVAAGVGLVAILAVV 435
Cdd:COG0392    80 KAAAIVALERLTDLLGLLLLAGLGLLFGPGA------------------LPGLGNLPGALLLLLLGLALLAAVLLYLLLL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 436 VIVvnarrdtnlvRRGVRAISNDSYAEYVAGVIERFVGDVERVISDRGAFLRVGVGSLAIWTLDVVTALIVFAAFGIPVT 515
Cdd:COG0392   142 AFR----------PRLLLRLRRWKLLRKIREKLERFLEGLRRLRLSPRLLLLQLLLSLLDWLLAALILYFLLPALGVDVS 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 516 PyltAVAFFAVSVGNLAKILPLSPGGIGLYEGAFTIIVVGLtavpELTALVALGIAIVDHAVKNLITVAGGLVSMAWLNV 595
Cdd:COG0392   212 F---LAVLAVFLLASLAGLLPPTPGGLGVFEAALLLLLSLF----GVPAAAALAALLLYRLIYYLLPLLLGLLLLLLLEL 284

                  .
gi 1147393137 596 S 596
Cdd:COG0392   285 R 285
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
9-217 2.41e-76

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: 242.09  E-value: 2.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   9 VVLPAYNEAETLEDTVEITLETLESFlPAESFEVIVAEDGCADRTPEIAERLASD-DERVRHFHSDERLGRGKALEAAFR 87
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEER-PSFSYEIIVVDDGSKDGTAEVARKLARKnPALIRVLTLPKNRGKGGAVRAGML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  88 ASEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATGSRWVPGAD--ADRPAKRGIPSKGYNRLVRLFLRSDLLDHQCG 165
Cdd:cd04188    80 AARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHLASAavVKRSWLRNLLGRGFNFLVRLLLGLGIKDTQCG 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1147393137 166 FKAFDREALLSLLDDVEDEHWFWDTEVLVRAQRAGYRVAEFPVEWTPQGDSK 217
Cdd:cd04188   160 FKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
7-220 1.08e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 149.85  E-value: 1.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   7 VSVVLPAYNEAETLEdtveitlETLESFLPA--ESFEVIVAEDGCADRTPEIAERLASDDERVRHFHSDERLGRGKALEA 84
Cdd:COG0463     4 VSVVIPTYNEEEYLE-------EALESLLAQtyPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  85 AFRASEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATGSRWVpgaDADRPAKRGIPSKGYNRLVRLFlrsDLLDHQC 164
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLI---REGESDLRRLGSRLFNLVRLLT---NLPDSTS 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1147393137 165 GFKAFDREALLSLLddvEDEHWFWDTEvLVRAQRAGYRVAEFPVEWTPqGDSKVDL 220
Cdd:COG0463   151 GFRLFRREVLEELG---FDEGFLEDTE-LLRALRHGFRIAEVPVRYRA-GESKLNL 201
AglD2 COG0392
Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis] ...
277-596 4.90e-37

Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440161  Cd Length: 289  Bit Score: 139.70  E-value: 4.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 277 ITGADPALVALSGVVYLLSWPLRGLRYRDILSRLDYDGDTWFLTGAIFISQTGNLVFP-ARAGDAVRAYVVKaRRSIPYP 355
Cdd:COG0392     1 LRAANPWWLLLALLLTLLSYLLLALRWRLLLRALGVKLPFRRLFLVSFIGYFGNNIGPgALGGEAVRARLLS-RRGVPAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 356 TGFASLAVERVFDLLSITVLGGTVLLGLVATggtdevvaaiaadvgtitIGGETLNPAAAAETAMGVAAGVGLVAILAVV 435
Cdd:COG0392    80 KAAAIVALERLTDLLGLLLLAGLGLLFGPGA------------------LPGLGNLPGALLLLLLGLALLAAVLLYLLLL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 436 VIVvnarrdtnlvRRGVRAISNDSYAEYVAGVIERFVGDVERVISDRGAFLRVGVGSLAIWTLDVVTALIVFAAFGIPVT 515
Cdd:COG0392   142 AFR----------PRLLLRLRRWKLLRKIREKLERFLEGLRRLRLSPRLLLLQLLLSLLDWLLAALILYFLLPALGVDVS 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 516 PyltAVAFFAVSVGNLAKILPLSPGGIGLYEGAFTIIVVGLtavpELTALVALGIAIVDHAVKNLITVAGGLVSMAWLNV 595
Cdd:COG0392   212 F---LAVLAVFLLASLAGLLPPTPGGLGVFEAALLLLLSLF----GVPAAAALAALLLYRLIYYLLPLLLGLLLLLLLEL 284

                  .
gi 1147393137 596 S 596
Cdd:COG0392   285 R 285
LPG_synthase_TM pfam03706
Lysylphosphatidylglycerol synthase TM region; LPG_synthase_TM is the N-terminal region of this ...
252-586 5.25e-30

Lysylphosphatidylglycerol synthase TM region; LPG_synthase_TM is the N-terminal region of this family of bacterial phosphatidylglycerol lysyltransferases. The function of the family is to add lysyl groups to membrane lipids, and this region is the transmembrane domain of 7xTMs. In order to counteract attack by membrane-damaging external cationic antimicrobial molecules - from host immune systems, bacteriocins, defensins, etc - bacteria modify their anionic membrane phosphatidylglycerol with positively-charged L-lysine; this results in repulsion of the foreign cationic peptides.


Pssm-ID: 461018  Cd Length: 302  Bit Score: 120.16  E-value: 5.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 252 AGSVLVFVALALMLVYLEPAAVLDAITGADPALVALSGVVYLLSWPLRGLRYRDILSRLDYDGDTWFLTGAIFISQTGNL 331
Cdd:pfam03706   3 LGLLLSALLLWFLLRGFDLSELAELLRSADPGWLLLALLLALLSLLLRALRWRLLLRALGARISFRRAFRAYLIGYFANN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 332 VFPARA-GDAVRAYVVKARRSIPYPTGFASLAVERVFDLLSITVLGGTVLLGLVATGGTDEVVAAIAAdvgtitiggetl 410
Cdd:pfam03706  83 VTPGRLgGEVVRAYLLKRREGLSLSKALASVVLERLLDLLTLLLLGLLALLLLLGLLLSGPAVLLTLA------------ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 411 npaaaaeTAMGVAAGVGLVAILAVVVIVvnaRRDTNLVRRGVRAISndsyaeyVAGVIERFVGDVERVISDRGAFLRVGV 490
Cdd:pfam03706 151 -------LALALLALLLLLLLLLLRRRP---RALARVLLRLAALLS-------RFRGRLRSLERLLLSLSSPRRLLLAFL 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 491 GSLAIWTLDVVTALIVFAAFGIPVTPYLTAVAFFAVsvgNLAKILPLSPGGIGLYEGAFTIIVVGLTAVPEltalVALGI 570
Cdd:pfam03706 214 LSLLIWLLEALALYLLLRALGLDLSLLLVLLLLLAA---TLAGALPPTPGGLGVREAAFVLLLGLLGVPAE----LALAA 286
                         330
                  ....*....|....*.
gi 1147393137 571 AIVDHAVKNLITVAGG 586
Cdd:pfam03706 287 ALLYRLITFWLILLLG 302
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
8-233 6.89e-30

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 120.64  E-value: 6.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   8 SVVLPAYNEAETLEDTVEITLETLESFL---PAESFEVIVAEDGCADRTPEIAERLASDDER----VRHFHSDERLGRGK 80
Cdd:PTZ00260   73 SIVIPAYNEEDRLPKMLKETIKYLESRSrkdPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINpnidIRLLSLLRNKGKGG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  81 ALEAAFRASEGETLVYFDTDLATDMR---HLEELVERVRSDEFDVATGSR---WVPGADADRPAKRGIPSKGYNRLVRLF 154
Cdd:PTZ00260  153 AVRIGMLASRGKYILMVDADGATDIDdfdKLEDIMLKIEQNGLGIVFGSRnhlVDSDVVAKRKWYRNILMYGFHFIVNTI 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1147393137 155 LRSDLLDHQCGFKAFDREALLSLLDDVEDEHWFWDTEVLVRAQRAGYRVAEFPVEWTPQGDSKVDLVRDVFGMGSQILR 233
Cdd:PTZ00260  233 CGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTEVEGSKLNVISASIQMARDILL 311
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
8-174 5.30e-28

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: 110.18  E-value: 5.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   8 SVVLPAYNEAETLedtveitLETLESFL--PAESFEVIVAEDGCADRTPEIAERLASDDERVRHFHSDERLGRGKALEAA 85
Cdd:pfam00535   1 SVIIPTYNEEKYL-------LETLESLLnqTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  86 FRASEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATGSRWVPGAD--ADRPAKRGIPSKGYNRLVRLFLRSDLLDHQ 163
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGEtgEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153
                         170
                  ....*....|.
gi 1147393137 164 CGFKAFDREAL 174
Cdd:pfam00535 154 GGFALYRREAL 164
TIGR00374 TIGR00374
conserved hypothetical protein; This model is built on a superfamily of proteins in the ...
254-590 3.34e-21

conserved hypothetical protein; This model is built on a superfamily of proteins in the Archaea and in Aquifex aeolicus. The authenticity of homology can be seen in the presence of motifs in the alignment that include residues relatively rare among these sequences, even though the alignment includes long regions of low-complexity hydrophobic sequences. One apparent fusion protein contains a Glycos_transf_2 region in the N-terminal half of the protein and a region homologous to this superfamily in the C-terminal region. [Unknown function, General]


Pssm-ID: 129470  Cd Length: 319  Bit Score: 94.76  E-value: 3.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 254 SVLVFVALALMLVYLEPAAVLDAITGADPALVALSGVVYLLSWPLRGLRYRDILSRLDYDGDTWFLTGAIFISQTGNLVF 333
Cdd:TIGR00374   1 IVLSILFLLAIILYIGPGEILRALGNANPFYLLLAFLLQFLVLALWTLRWKLISNALGIKYSFRHLFMLLFVGMFINNIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 334 PARAGD-AVRAYVVKARRSIPYPTGFASLAVERVFDLLsitVLGGTVLLGLVATGGTDEVVAAIAADVGTITIGGETLNp 412
Cdd:TIGR00374  81 PSAAGGePMRAYMLKKKEGISASLGFSTVLAERVFDLV---IFILLLPLSAIMVFVLSIPKLFIYLILILITLLLFLII- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 413 aaaaetamgvaagvglvaILAVVVIVVNARRDTNLVRRGVRAIS-NDSYAEYVAGVIERFVGDVERVISDRGAFLRVGVG 491
Cdd:TIGR00374 157 ------------------LYIFGNKKILQKIASKILKAVVKFFSrKNELESKLRSFLVRFLGATKFFLKDTAELVVLILL 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 492 SLAIWTLDVVTALIVFAAFGIPVTPYLTAVAFFavsVGNLAKILPLSPGGIGLYEGaftiIVVGLTAVPELTALVALGIA 571
Cdd:TIGR00374 219 SLGMWLLEILRLYLIFLAFGVEVSFLEIIIIQL---IALLVGLLPLTPGGLGVAEV----SMIYLFSVFGVPPSVAGAVV 291
                         330
                  ....*....|....*....
gi 1147393137 572 IVDHAVKNLITVAGGLVSM 590
Cdd:TIGR00374 292 LLDRLISYWMITFLGAIAF 310
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
9-217 2.41e-76

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: 242.09  E-value: 2.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   9 VVLPAYNEAETLEDTVEITLETLESFlPAESFEVIVAEDGCADRTPEIAERLASD-DERVRHFHSDERLGRGKALEAAFR 87
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEER-PSFSYEIIVVDDGSKDGTAEVARKLARKnPALIRVLTLPKNRGKGGAVRAGML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  88 ASEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATGSRWVPGAD--ADRPAKRGIPSKGYNRLVRLFLRSDLLDHQCG 165
Cdd:cd04188    80 AARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHLASAavVKRSWLRNLLGRGFNFLVRLLLGLGIKDTQCG 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1147393137 166 FKAFDREALLSLLDDVEDEHWFWDTEVLVRAQRAGYRVAEFPVEWTPQGDSK 217
Cdd:cd04188   160 FKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
9-196 1.67e-51

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: 175.45  E-value: 1.67e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   9 VVLPAYNEAETLEDTVEitlETLESFLPAESFEVIVAEDGCADRTPEIAERLASDDERVRHFHSDERLGRGKALEAAFRA 88
Cdd:cd04179     1 VVIPAYNEEENIPELVE---RLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  89 SEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATGSRWVPGADADRPAKRGIPSKGYNRLVRLFLRSDLLDHQCGFKA 168
Cdd:cd04179    78 ARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGAGMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRL 157
                         170       180
                  ....*....|....*....|....*...
gi 1147393137 169 FDREALLSLLDDVEDEHWFWDTEVLVRA 196
Cdd:cd04179   158 FRREVLEALLSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
7-220 1.08e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 149.85  E-value: 1.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   7 VSVVLPAYNEAETLEdtveitlETLESFLPA--ESFEVIVAEDGCADRTPEIAERLASDDERVRHFHSDERLGRGKALEA 84
Cdd:COG0463     4 VSVVIPTYNEEEYLE-------EALESLLAQtyPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  85 AFRASEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATGSRWVpgaDADRPAKRGIPSKGYNRLVRLFlrsDLLDHQC 164
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLI---REGESDLRRLGSRLFNLVRLLT---NLPDSTS 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1147393137 165 GFKAFDREALLSLLddvEDEHWFWDTEvLVRAQRAGYRVAEFPVEWTPqGDSKVDL 220
Cdd:COG0463   151 GFRLFRREVLEELG---FDEGFLEDTE-LLRALRHGFRIAEVPVRYRA-GESKLNL 201
AglD2 COG0392
Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis] ...
277-596 4.90e-37

Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440161  Cd Length: 289  Bit Score: 139.70  E-value: 4.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 277 ITGADPALVALSGVVYLLSWPLRGLRYRDILSRLDYDGDTWFLTGAIFISQTGNLVFP-ARAGDAVRAYVVKaRRSIPYP 355
Cdd:COG0392     1 LRAANPWWLLLALLLTLLSYLLLALRWRLLLRALGVKLPFRRLFLVSFIGYFGNNIGPgALGGEAVRARLLS-RRGVPAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 356 TGFASLAVERVFDLLSITVLGGTVLLGLVATggtdevvaaiaadvgtitIGGETLNPAAAAETAMGVAAGVGLVAILAVV 435
Cdd:COG0392    80 KAAAIVALERLTDLLGLLLLAGLGLLFGPGA------------------LPGLGNLPGALLLLLLGLALLAAVLLYLLLL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 436 VIVvnarrdtnlvRRGVRAISNDSYAEYVAGVIERFVGDVERVISDRGAFLRVGVGSLAIWTLDVVTALIVFAAFGIPVT 515
Cdd:COG0392   142 AFR----------PRLLLRLRRWKLLRKIREKLERFLEGLRRLRLSPRLLLLQLLLSLLDWLLAALILYFLLPALGVDVS 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 516 PyltAVAFFAVSVGNLAKILPLSPGGIGLYEGAFTIIVVGLtavpELTALVALGIAIVDHAVKNLITVAGGLVSMAWLNV 595
Cdd:COG0392   212 F---LAVLAVFLLASLAGLLPPTPGGLGVFEAALLLLLSLF----GVPAAAALAALLLYRLIYYLLPLLLGLLLLLLLEL 284

                  .
gi 1147393137 596 S 596
Cdd:COG0392   285 R 285
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
9-238 3.72e-36

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: 134.97  E-value: 3.72e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   9 VVLPAYNEAETLEDTVEItletLESFLPAESFEVIVAEDGCADRTPEIAERLASDDERVRHFHSDERLGRGKALEAAFRA 88
Cdd:cd06442     1 IIIPTYNERENIPELIER----LDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  89 SEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATGSRWVP-GADADRPAKRGIPSKGYNRLVRLFLRSDLLDHQCGFK 167
Cdd:cd06442    77 ARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEgGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFR 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1147393137 168 AFDREALLSLLDDVEDEHWFWDTEVLVRAQRAGYRVAEFPVEWTPQ--GDSKVDlvrdvfgmGSQILRTWWQV 238
Cdd:cd06442   157 AYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDRehGESKLG--------GKEIVEYLKGL 221
LPG_synthase_TM pfam03706
Lysylphosphatidylglycerol synthase TM region; LPG_synthase_TM is the N-terminal region of this ...
252-586 5.25e-30

Lysylphosphatidylglycerol synthase TM region; LPG_synthase_TM is the N-terminal region of this family of bacterial phosphatidylglycerol lysyltransferases. The function of the family is to add lysyl groups to membrane lipids, and this region is the transmembrane domain of 7xTMs. In order to counteract attack by membrane-damaging external cationic antimicrobial molecules - from host immune systems, bacteriocins, defensins, etc - bacteria modify their anionic membrane phosphatidylglycerol with positively-charged L-lysine; this results in repulsion of the foreign cationic peptides.


Pssm-ID: 461018  Cd Length: 302  Bit Score: 120.16  E-value: 5.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 252 AGSVLVFVALALMLVYLEPAAVLDAITGADPALVALSGVVYLLSWPLRGLRYRDILSRLDYDGDTWFLTGAIFISQTGNL 331
Cdd:pfam03706   3 LGLLLSALLLWFLLRGFDLSELAELLRSADPGWLLLALLLALLSLLLRALRWRLLLRALGARISFRRAFRAYLIGYFANN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 332 VFPARA-GDAVRAYVVKARRSIPYPTGFASLAVERVFDLLSITVLGGTVLLGLVATGGTDEVVAAIAAdvgtitiggetl 410
Cdd:pfam03706  83 VTPGRLgGEVVRAYLLKRREGLSLSKALASVVLERLLDLLTLLLLGLLALLLLLGLLLSGPAVLLTLA------------ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 411 npaaaaeTAMGVAAGVGLVAILAVVVIVvnaRRDTNLVRRGVRAISndsyaeyVAGVIERFVGDVERVISDRGAFLRVGV 490
Cdd:pfam03706 151 -------LALALLALLLLLLLLLLRRRP---RALARVLLRLAALLS-------RFRGRLRSLERLLLSLSSPRRLLLAFL 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 491 GSLAIWTLDVVTALIVFAAFGIPVTPYLTAVAFFAVsvgNLAKILPLSPGGIGLYEGAFTIIVVGLTAVPEltalVALGI 570
Cdd:pfam03706 214 LSLLIWLLEALALYLLLRALGLDLSLLLVLLLLLAA---TLAGALPPTPGGLGVREAAFVLLLGLLGVPAE----LALAA 286
                         330
                  ....*....|....*.
gi 1147393137 571 AIVDHAVKNLITVAGG 586
Cdd:pfam03706 287 ALLYRLITFWLILLLG 302
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
8-233 6.89e-30

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 120.64  E-value: 6.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   8 SVVLPAYNEAETLEDTVEITLETLESFL---PAESFEVIVAEDGCADRTPEIAERLASDDER----VRHFHSDERLGRGK 80
Cdd:PTZ00260   73 SIVIPAYNEEDRLPKMLKETIKYLESRSrkdPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINpnidIRLLSLLRNKGKGG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  81 ALEAAFRASEGETLVYFDTDLATDMR---HLEELVERVRSDEFDVATGSR---WVPGADADRPAKRGIPSKGYNRLVRLF 154
Cdd:PTZ00260  153 AVRIGMLASRGKYILMVDADGATDIDdfdKLEDIMLKIEQNGLGIVFGSRnhlVDSDVVAKRKWYRNILMYGFHFIVNTI 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1147393137 155 LRSDLLDHQCGFKAFDREALLSLLDDVEDEHWFWDTEVLVRAQRAGYRVAEFPVEWTPQGDSKVDLVRDVFGMGSQILR 233
Cdd:PTZ00260  233 CGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTEVEGSKLNVISASIQMARDILL 311
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
8-174 5.30e-28

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: 110.18  E-value: 5.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   8 SVVLPAYNEAETLedtveitLETLESFL--PAESFEVIVAEDGCADRTPEIAERLASDDERVRHFHSDERLGRGKALEAA 85
Cdd:pfam00535   1 SVIIPTYNEEKYL-------LETLESLLnqTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  86 FRASEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATGSRWVPGAD--ADRPAKRGIPSKGYNRLVRLFLRSDLLDHQ 163
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGEtgEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153
                         170
                  ....*....|.
gi 1147393137 164 CGFKAFDREAL 174
Cdd:pfam00535 154 GGFALYRREAL 164
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
5-208 1.05e-24

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 103.24  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   5 REVSVVLPAYNEAETLEDTVEITLETLESFlpaESFEVIVAEDGCADRTPEIAERL--ASDDERVRHFHSDERLGRGKAL 82
Cdd:PLN02726    9 MKYSIIVPTYNERLNIALIVYLIFKALQDV---KDFEIIVVDDGSPDGTQDVVKQLqkVYGEDRILLRPRPGKLGLGTAY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  83 EAAFRASEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATGSRWVPGAD-ADRPAKRGIPSKGYNRLVRLFLRSDLLD 161
Cdd:PLN02726   86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGvHGWDLRRKLTSRGANVLAQTLLWPGVSD 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1147393137 162 HQCGFKAFDREALLSLLDDVEDEHWFWDTEVLVRAQRAGYRVAEFPV 208
Cdd:PLN02726  166 LTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPI 212
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
9-178 3.42e-24

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: 99.86  E-value: 3.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   9 VVLPAYNEAETLEDTVEITLETLESflPAESFEVIVAEDGCADRTPEIAERLASDDERVRHFHSDERLGRGKALEAAFRA 88
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLES--LGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  89 SEGETLVYFDTDLATDMRHLEELVERVRSDeFDVATGSRwvpgADADRPAKRGIPSKGYNRLVRLFLRSDLLDHQCGFKA 168
Cdd:cd04187    79 ARGDAVITMDADLQDPPELIPEMLAKWEEG-YDVVYGVR----KNRKESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRL 153
                         170
                  ....*....|
gi 1147393137 169 FDREALLSLL 178
Cdd:cd04187   154 MDRKVVDALL 163
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
7-312 2.56e-21

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: 94.81  E-value: 2.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   7 VSVVLPAYNEAETLEdtveitlETLESFL----PAESFEVIVAEDGCADRTPEIAERLASDDERVRHFHSDERLGRGKAL 82
Cdd:COG1215    31 VSVIIPAYNEEAVIE-------ETLRSLLaqdyPKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAAL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  83 EAAFRASEGETLVYFDtdlatdmrhleelvervrsdefdvatgsrwvpgADAdrpakrgIPSKGY-NRLVRLFLRSDlLD 161
Cdd:COG1215   104 NAGLKAARGDIVVFLD---------------------------------ADT-------VLDPDWlRRLVAAFADPG-VG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 162 HQCGFKAFDREALLSlLDDVEDEHWFWDTEVLVRAQRAGYRVAEFP--VEWTPQGDSKVDLVRdvfgmgsQILRtwWQVS 239
Cdd:COG1215   143 ASGANLAFRREALEE-VGGFDEDTLGEDLDLSLRLLRAGYRIVYVPdaVVYEEAPETLRALFR-------QRRR--WARG 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1147393137 240 VSPRLTRRVSMTAGSVLVFVALALMLVYLEPAAVLDAITGadpALVALSGVVYLLSWPLRGLRYRDILSRLDY 312
Cdd:COG1215   213 GLQLLLKHRPLLRPRRLLLFLLLLLLPLLLLLLLLALLAL---LLLLLPALLLALLLALRRRRLLLPLLHLLY 282
TIGR00374 TIGR00374
conserved hypothetical protein; This model is built on a superfamily of proteins in the ...
254-590 3.34e-21

conserved hypothetical protein; This model is built on a superfamily of proteins in the Archaea and in Aquifex aeolicus. The authenticity of homology can be seen in the presence of motifs in the alignment that include residues relatively rare among these sequences, even though the alignment includes long regions of low-complexity hydrophobic sequences. One apparent fusion protein contains a Glycos_transf_2 region in the N-terminal half of the protein and a region homologous to this superfamily in the C-terminal region. [Unknown function, General]


Pssm-ID: 129470  Cd Length: 319  Bit Score: 94.76  E-value: 3.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 254 SVLVFVALALMLVYLEPAAVLDAITGADPALVALSGVVYLLSWPLRGLRYRDILSRLDYDGDTWFLTGAIFISQTGNLVF 333
Cdd:TIGR00374   1 IVLSILFLLAIILYIGPGEILRALGNANPFYLLLAFLLQFLVLALWTLRWKLISNALGIKYSFRHLFMLLFVGMFINNIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 334 PARAGD-AVRAYVVKARRSIPYPTGFASLAVERVFDLLsitVLGGTVLLGLVATGGTDEVVAAIAADVGTITIGGETLNp 412
Cdd:TIGR00374  81 PSAAGGePMRAYMLKKKEGISASLGFSTVLAERVFDLV---IFILLLPLSAIMVFVLSIPKLFIYLILILITLLLFLII- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 413 aaaaetamgvaagvglvaILAVVVIVVNARRDTNLVRRGVRAIS-NDSYAEYVAGVIERFVGDVERVISDRGAFLRVGVG 491
Cdd:TIGR00374 157 ------------------LYIFGNKKILQKIASKILKAVVKFFSrKNELESKLRSFLVRFLGATKFFLKDTAELVVLILL 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137 492 SLAIWTLDVVTALIVFAAFGIPVTPYLTAVAFFavsVGNLAKILPLSPGGIGLYEGaftiIVVGLTAVPELTALVALGIA 571
Cdd:TIGR00374 219 SLGMWLLEILRLYLIFLAFGVEVSFLEIIIIQL---IALLVGLLPLTPGGLGVAEV----SMIYLFSVFGVPPSVAGAVV 291
                         330
                  ....*....|....*....
gi 1147393137 572 IVDHAVKNLITVAGGLVSM 590
Cdd:TIGR00374 292 LLDRLISYWMITFLGAIAF 310
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
9-129 9.47e-18

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: 80.63  E-value: 9.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   9 VVLPAYNEAETLEdtveitlETLESFLPA--ESFEVIVAEDGCADRTPEIAERLASDDERVRHFHSDERLGRGKALEAAF 86
Cdd:cd00761     1 VIIPAYNEEPYLE-------RCLESLLAQtyPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGL 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1147393137  87 RASEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATGSRWV 129
Cdd:cd00761    74 KAARGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGN 116
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
9-177 1.55e-15

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: 74.96  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   9 VVLPAYNEAETLEDTVEITLEtlesfLPAESFEVIVAEDGCADRTPEIAERLASDDERVRHFH-SDERLGRGKALEAAFR 87
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLA-----LDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVrDKENGGKAGALNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  88 ASEGETLVYFDTD--LATDMrhLEELVERVRSDEFDVATGSRWVPGADADRPAKRGIpSKGYNRLVRLFLRSDLLDH--- 162
Cdd:cd06423    76 HAKGDIVVVLDADtiLEPDA--LKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQ-AIEYLSIFRLGRRAQSALGgvl 152
                         170
                  ....*....|....*..
gi 1147393137 163 -QCG-FKAFDREALLSL 177
Cdd:cd06423   153 vLSGaFGAFRREALREV 169
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
7-126 5.04e-14

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: 72.23  E-value: 5.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   7 VSVVLPAYNEAETLEdtveitlETLESFL----PAESFEVIVAEDGCADRTPEIAERLASDDERVRHFHsdERLGRGKAL 82
Cdd:cd06439    31 VTIIIPAYNEEAVIE-------AKLENLLaldyPRDRLEIIVVSDGSTDGTAEIAREYADKGVKLLRFP--ERRGKAAAL 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1147393137  83 EAAFRASEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATGS 126
Cdd:cd06439   102 NRALALATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSGE 145
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
7-125 2.06e-12

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: 67.26  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   7 VSVVLPAYNEAETLEdtveitlETLESFL----PAESFEVIVAEDGCADRTPEIAERLASDDERVRHFHSDERLgRGKAL 82
Cdd:cd02525     2 VSIIIPVRNEEKYIE-------ELLESLLnqsyPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRI-QSAGL 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1147393137  83 EAAFRASEGETLVYFD--TDLATDMrhLEELVERVRSDEFDVATG 125
Cdd:cd02525    74 NIGIRNSRGDIIIRVDahAVYPKDY--ILELVEALKRTGADNVGG 116
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
7-113 1.02e-11

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 64.24  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   7 VSVVLPAYNEAETLEdtveitlETLESFL--PAESFEVIVAEDGCADRTPEIAERLASDdeRVRHFHSDERLGRGKALEA 84
Cdd:COG1216     5 VSVVIPTYNRPELLR-------RCLESLLaqTYPPFEVIVVDNGSTDGTAELLAALAFP--RVRVIRNPENLGFAAARNL 75
                          90       100
                  ....*....|....*....|....*....
gi 1147393137  85 AFRASEGETLVYFDTDLATDMRHLEELVE 113
Cdd:COG1216    76 GLRAAGGDYLLFLDDDTVVEPDWLERLLA 104
PRK10073 PRK10073
putative glycosyl transferase; Provisional
1-201 2.36e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 59.29  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   1 MSPSREVSVVLPAYNEAETLEDTVE-ITLETLESFlpaesfEVIVAEDGCADRTPEIAERLASDDERVRHFHSdERLGRG 79
Cdd:PRK10073    2 MNSTPKLSIIIPLYNAGKDFRAFMEsLIAQTWTAL------EIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQ-ANAGVS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  80 KALEAAFRASEGETLVYFDTD--LATDMrhLEELVERVRSDEFDVATGS-RWVpgADADRPAKRGIPSKgynRL------ 150
Cdd:PRK10073   75 VARNTGLAVATGKYVAFPDADdvVYPTM--YETLMTMALEDDLDVAQCNaDWC--FRDTGETWQSIPSD---RLrstgvl 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1147393137 151 -----VRLFLRSDLLDHQCGFKAFDREALlsllddveDEHWF------------WDTEVLVRAQRAGY 201
Cdd:PRK10073  148 sgpdwLRMALSSRRWTHVVWLGVYRRDFI--------VKNNIkfepglhhqdipWTTEVMFNALRVRY 207
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
9-100 1.55e-08

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: 55.37  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   9 VVLPAYNEAETLEDTVEiTLETLEsfLPAESFEVIVAEDGCADRTPEIAE-RLASDDERVRHFHSDERLGRGK--ALEAA 85
Cdd:cd04192     1 VVIAARNEAENLPRLLQ-SLSALD--YPKEKFEVILVDDHSTDGTVQILEfAAAKPNFQLKILNNSRVSISGKknALTTA 77
                          90
                  ....*....|....*
gi 1147393137  86 FRASEGETLVYFDTD 100
Cdd:cd04192    78 IKAAKGDWIVTTDAD 92
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
7-105 5.06e-08

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily 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: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 53.73  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   7 VSVVLPAYNEAETLEDtveiTLETLESfLPAESFEVIVAEDGCADRTPEIAERLAsdderVRHFHSdeRLGRGKALEAAF 86
Cdd:cd02522     1 LSIIIPTLNEAENLPR----LLASLRR-LNPLPLEIIVVDGGSTDGTVAIARSAG-----VVVISS--PKGRARQMNAGA 68
                          90       100
                  ....*....|....*....|..
gi 1147393137  87 RASEGETLvYF---DTDLATDM 105
Cdd:cd02522    69 AAARGDWL-LFlhaDTRLPPDW 89
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
4-101 1.44e-07

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 53.38  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   4 SREVSVVLPAYNEAETLEDTVEITLETLESFLPAesfEVIVAEDGCADRTPEIAER-----LASDDERVRHfhsDERLGR 78
Cdd:PRK13915   30 GRTVSVVLPALNEEETVGKVVDSIRPLLMEPLVD---ELIVIDSGSTDATAERAAAagarvVSREEILPEL---PPRPGK 103
                          90       100
                  ....*....|....*....|...
gi 1147393137  79 GKALEAAFRASEGETLVYFDTDL 101
Cdd:PRK13915  104 GEALWRSLAATTGDIVVFVDADL 126
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
3-222 2.22e-06

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 50.12  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   3 PSREVSVVLPAYNEAETLEDTVEITLETLESFlpAESFEVIVAEDGCADRTPEIAERLASD-DERVRHFHSDERLGRGKA 81
Cdd:PRK10714    4 PIKKVSVVIPVYNEQESLPELIRRTTAACESL--GKEYEILLIDDGSSDNSAEMLVEAAQApDSHIVAILLNRNYGQHSA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  82 LEAAFRASEGETLVYFDTDLATDMRHLEELVErVRSDEFDVATGSRwvpgADADRPAKRGIPSKGYNRLVRLFLRSDLLD 161
Cdd:PRK10714   82 IMAGFSHVTGDLIITLDADLQNPPEEIPRLVA-KADEGYDVVGTVR----QNRQDSWFRKTASKMINRLIQRTTGKAMGD 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1147393137 162 HQCGFKAFDREALLSLLDDVEDEhwfwdTEVLVRAQRAGYRVAEFPVEWTPQ--GDSKVDLVR 222
Cdd:PRK10714  157 YGCMLRAYRRHIVDAMLHCHERS-----TFIPILANTFARRAIEIPVHHAERefGDSKYSFMR 214
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
9-207 3.37e-06

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: 47.55  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   9 VVLPAYNeaetledTVEITLETLESFLPA--ESFEVIVAEDGCADRTPEIaerLASDDERVRHFHSDERLGRGKALEAAF 86
Cdd:cd04186     1 IIIVNYN-------SLEYLKACLDSLLAQtyPDFEVIVVDNASTDGSVEL---LRELFPEVRLIRNGENLGFGAGNNQGI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  87 RASEGETLVYFDTDLATDMRHLEELVERVRSDEfDVAT-GSRwVPGADadrpakrgipskgynrlvrLFLRSDLLDhQCG 165
Cdd:cd04186    71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDP-DVGIvGPK-VSGAF-------------------LLVRREVFE-EVG 128
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1147393137 166 FkaFDreallsllddvEDEHWFW-DTEVLVRAQRAGYRVAEFP 207
Cdd:cd04186   129 G--FD-----------EDFFLYYeDVDLCLRARLAGYRVLYVP 158
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
5-204 3.82e-06

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 48.52  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   5 REVSVVLPAYNEAETLEDTVEITLETLESflpaeSFEVIVAEDGCADRTPEIAERLASD--DERVRHFHSDERLG-RGK- 80
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYP-----PVEVVVVVNPSDAETLDVAEEIAARfpDVRLRVIRNARLLGpTGKs 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  81 -ALEAAFRASEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATG-------SRWVPGADADRPAKRGIpskgynRLVR 152
Cdd:pfam13641  77 rGLNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTpvfslnrSTMLSALGALEFALRHL------RMMS 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1147393137 153 LFLRSDLLDHQCGFKAFDREALLSLLDDVEDEHWFWDTEVLVRAQRAGYRVA 204
Cdd:pfam13641 151 LRLALGVLPLSGAGSAIRREVLKELGLFDPFFLLGDDKSLGRRLRRHGWRVA 202
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
9-100 1.15e-05

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 46.42  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   9 VVLPAYNEAETLEdtveITLETL--ESFLPaesFEVIVAEDGCADRTPEIAERLASDDE-RVRHF-HSDERLGRGKALEA 84
Cdd:cd06420     1 LIITTYNRPEALE----LVLKSVlnQSILP---FEVIIADDGSTEETKELIEEFKSQFPiPIKHVwQEDEGFRKAKIRNK 73
                          90
                  ....*....|....*.
gi 1147393137  85 AFRASEGETLVYFDTD 100
Cdd:cd06420    74 AIAAAKGDYLIFIDGD 89
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
9-526 4.57e-05

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 46.79  E-value: 4.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137    9 VVLPAY---NEAETLEDTVEITLETLESFLPAESFEVIVAEDGCADRTPEIAERLASDDERVRHFHSDERLGRGKALEAA 85
Cdd:COG3321    861 VPLPTYpfqREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAA 940
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   86 FRASEGETLVYFDTDLATDMRHLEELVERVRSDEFDVATGSRWVPGADADRPAKRGIPSKGYNRLVRLFLRSDLLDHQCG 165
Cdd:COG3321    941 ALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAA 1020
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  166 FKAFDREALLSLLDDVEDEHWFWDTEVLVRAQRAGYRVAEFPVEWTPQGDSKVDLVRDVFGMGSQILRTWWQVSVSPRLT 245
Cdd:COG3321   1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALA 1100
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  246 RRVSmtAGSVLVFVALALMLVYLEPAAVLDAITGADPALVALSGVVYLLSWPLRGLRYRDILSRLDYDGDTWFLTGAIFI 325
Cdd:COG3321   1101 ALAA--ALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALA 1178
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  326 SQTGNLVFPARAGDAVRAYVVKARRSIPYPTGFASLAVERVFDLLSITVLGGTVLLGLVATGGTDEVVAAIAADVGTITI 405
Cdd:COG3321   1179 LALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAA 1258
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  406 GGETLNPAAAAETAMGVAAGVGLVAILAVVVIVVNARRDTNLVRRGVRAISNDSYAEYVAGVIERFVGDVERVISDRGAF 485
Cdd:COG3321   1259 LAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVA 1338
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1147393137  486 LRVGVGSLAIWTLDVVTALIVFAAFGIPVTPYLTAVAFFAV 526
Cdd:COG3321   1339 AALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALA 1379
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
7-100 2.91e-04

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 42.68  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   7 VSVVLPAYNEAETLEDTVEITLEtLEsfLPAESFEVIVAEDGCAD---RTPEIAERLASDDERVRHFHSDERLG-RGKAL 82
Cdd:cd06437     3 VTVQLPVFNEKYVVERLIEAACA-LD--YPKDRLEIQVLDDSTDEtvrLAREIVEEYAAQGVNIKHVRRADRTGyKAGAL 79
                          90
                  ....*....|....*...
gi 1147393137  83 EAAFRASEGETLVYFDTD 100
Cdd:cd06437    80 AEGMKVAKGEYVAIFDAD 97
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
168-620 3.16e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 44.09  E-value: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  168 AFDREALLSLLDDVEDEHWFWDTEVLVRAQRAGYRVAEFPVEWTPQGDSKVDLVRDVFGMGSQILRTWWQVSVSPRLTRR 247
Cdd:COG3321    867 PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALA 946
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  248 VSMTAGSVLVFVALALMLVYLEPAAVLDAITGADPALVALSGVVYLLSWPLRGLRYRDILSRldyDGDTWFLTGAIFISQ 327
Cdd:COG3321    947 AAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAA---ALLLAAAAAAAALLA 1023
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  328 TGNLVFPARAGDAVRAYVVKARRSIPYPTGFASLAVERVFDLLSITVLGGTVLLGLVATGGTDEVVAAIAADVGTITIGG 407
Cdd:COG3321   1024 LAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALA 1103
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  408 ETLNPAAAAETAMGVAAGVGLVAILAVVVIVVNARRDTNLVRRGVRAISNDSYAEYVAGVIERFVGDVERVISDRGAFLR 487
Cdd:COG3321   1104 AALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAA 1183
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137  488 VGVGSLAIWTLDVVTALIVFAAFGIPVTPYLTAVAFFAVSVGNLAKILPLSPGGIGLYEGAFTIIVVGLTAVPELTALVA 567
Cdd:COG3321   1184 ALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALA 1263
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1147393137  568 LGIAIVDHAVKNLITVAGGLVSMAWLNVSLTTAVAETEGETGASAAETGDEAA 620
Cdd:COG3321   1264 LLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAA 1316
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
7-100 3.73e-04

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 42.19  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   7 VSVVLPAYNeaeTLEDTVEitlETLESFLpAESFE----VIVAEDGCADRTPEIAERLASDDERVRHFHSDERLGRGKAL 82
Cdd:cd04184     3 ISIVMPVYN---TPEKYLR---EAIESVR-AQTYPnwelCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAAT 75
                          90
                  ....*....|....*...
gi 1147393137  83 EAAFRASEGETLVYFDTD 100
Cdd:cd04184    76 NSALELATGEFVALLDHD 93
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
7-154 5.36e-04

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 41.89  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   7 VSVVLPAYNEAETLEdtveitlETLESFLPAESfEVIVAEDGCADRTPEIAERLASddeRVRHF----HSDErlgRGKAL 82
Cdd:cd02511     2 LSVVIITKNEERNIE-------RCLESVKWAVD-EIIVVDSGSTDRTVEIAKEYGA---KVYQRwwdgFGAQ---RNFAL 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1147393137  83 EAAfrasEGETLVYFDTD--LATDMRhlEELVERVRSDEFDVATGSR--WVPGadadRPAKRGipSKGYNRLVRLF 154
Cdd:cd02511    68 ELA----TNDWVLSLDADerLTPELA--DEILALLATDDYDGYYVPRrnFFLG----RWIRHG--GWYPDRQLRLF 131
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
9-87 1.42e-03

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 39.89  E-value: 1.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1147393137   9 VVLPAYNEAETLEDTVEiTLETLESflPAESFEVIVAEDGCADRTPEIAErlASDDERVRHFHSDERlGRGKALEAAFR 87
Cdd:cd06438     1 ILIPAHNEEAVIGNTVR-SLKAQDY--PRELYRIFVVADNCTDDTAQVAR--AAGATVLERHDPERR-GKGYALDFGFR 73
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
8-118 4.26e-03

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 39.49  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   8 SVVLPAYNEA-ETLEDTVEITLE-TLESFLPaesfEVIVAEDGcADRtPEIAERLASDDER----VRHFHSDERLG--RG 79
Cdd:cd02510     1 SVIIIFHNEAlSTLLRTVHSVINrTPPELLK----EIILVDDF-SDK-PELKLLLEEYYKKylpkVKVLRLKKREGliRA 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1147393137  80 KALEAafRASEGETLVYFDTdlatdmrH-------LEELVERVRSD 118
Cdd:cd02510    75 RIAGA--RAATGDVLVFLDS-------HcevnvgwLEPLLARIAEN 111
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
6-112 8.10e-03

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 38.39  E-value: 8.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   6 EVSVVLPAYNEAEtledtvEITLETLESFLPAESFEVIVAEDGCADRTPEIAERLASDDeRVRHFhSDERLGRGKALEAA 85
Cdd:cd06434     1 DVTVIIPVYDEDP------DVFRECLRSILRQKPLEIIVVTDGDDEPYLSILSQTVKYG-GIFVI-TVPHPGKRRALAEG 72
                          90       100
                  ....*....|....*....|....*..
gi 1147393137  86 FRASEGETLVYFDTDLATDMRHLEELV 112
Cdd:cd06434    73 IRHVTTDIVVLLDSDTVWPPNALPEML 99
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
9-86 9.00e-03

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: 37.75  E-value: 9.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147393137   9 VVLPAYNEAETLEDTVEITLETLESFLpaesfeVIVAEDGCADRTPEIAeRLASDDERV---RHFHSDERLGRGKALEAA 85
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRNKPNFL------VLVIDDASDDDTAGIV-RLAITDSRVhllRRHLPNARTGKGDALNAA 73

                  .
gi 1147393137  86 F 86
Cdd:cd06436    74 Y 74
 
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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