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Conserved domains on  [gi|518172457|ref|WP_019342665|]
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undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase [Stutzerimonas stutzeri]

Protein Classification

UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase( domain architecture ID 11479176)

UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase catalyzes the last step in the intracellular phase of peptidoglycan biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
murG PRK00726
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
4-356 3.64e-167

undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional


:

Pssm-ID: 234825 [Multi-domain]  Cd Length: 357  Bit Score: 470.38  E-value: 3.64e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457   4 NVLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQ 83
Cdd:PRK00726   3 KILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVLQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  84 ARRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNSAKRRT--TGNP 161
Cdd:PRK00726  83 ARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAvvTGNP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 162 VRHELF-LETPRQTLLGR--RPRLLVLGGSLGAEPLNKLLPEALGQLSEELRpeIFHQAGKQHAEITRERYvAAGVEAEV 238
Cdd:PRK00726 163 VREEILaLAAPPARLAGRegKPTLLVVGGSQGARVLNEAVPEALALLPEALQ--VIHQTGKGDLEEVRAAY-AAGINAEV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 239 APFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLT 318
Cdd:PRK00726 240 VPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEKLAEKLL 319
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 518172457 319 EVMMQPEKLKAMGATARRLARPDATRTVVDICLEVAHG 356
Cdd:PRK00726 320 ELLSDPERLEAMAEAARALGKPDAAERLADLIEELARK 357
 
Name Accession Description Interval E-value
murG PRK00726
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
4-356 3.64e-167

undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional


Pssm-ID: 234825 [Multi-domain]  Cd Length: 357  Bit Score: 470.38  E-value: 3.64e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457   4 NVLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQ 83
Cdd:PRK00726   3 KILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVLQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  84 ARRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNSAKRRT--TGNP 161
Cdd:PRK00726  83 ARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAvvTGNP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 162 VRHELF-LETPRQTLLGR--RPRLLVLGGSLGAEPLNKLLPEALGQLSEELRpeIFHQAGKQHAEITRERYvAAGVEAEV 238
Cdd:PRK00726 163 VREEILaLAAPPARLAGRegKPTLLVVGGSQGARVLNEAVPEALALLPEALQ--VIHQTGKGDLEEVRAAY-AAGINAEV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 239 APFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLT 318
Cdd:PRK00726 240 VPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEKLAEKLL 319
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 518172457 319 EVMMQPEKLKAMGATARRLARPDATRTVVDICLEVAHG 356
Cdd:PRK00726 320 ELLSDPERLEAMAEAARALGKPDAAERLADLIEELARK 357
MurG COG0707
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ...
1-356 8.23e-163

UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440471 [Multi-domain]  Cd Length: 363  Bit Score: 459.59  E-value: 8.23e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457   1 MGGNVLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRS 80
Cdd:COG0707    1 MSKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  81 LGQARRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNT--FSNSAKRRTT 158
Cdd:COG0707   81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETkkYFPKKKAVVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 159 GNPVRHElFLETPRQTLLGR------RPRLLVLGGSLGAEPLNKLLPEALGQLSEElRPEIFHQAGKQHAEITRERYVAA 232
Cdd:COG0707  161 GNPVRKE-ILELDRPEARAKlgldpdKPTLLVFGGSQGARALNEAVPAALAALLEA-RLQVVHQTGKGDYEEVRAAYAAA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 233 GV-EAEVAPFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAA 311
Cdd:COG0707  239 IRpNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPE 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 518172457 312 ALAAQLTEVMMQPEKLKAMGATARRLARPDATRTVVDICLEVAHG 356
Cdd:COG0707  319 KLAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
5-349 6.20e-146

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340818 [Multi-domain]  Cd Length: 350  Bit Score: 416.23  E-value: 6.20e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457   5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:cd03785    2 ILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNSAKRRT--TGNPV 162
Cdd:cd03785   82 RKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVvvTGNPV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 163 RHELFLETPRQTLLGR---RPRLLVLGGSLGAEPLNKLLPEALGQLSEElRPEIFHQAGKQHAEITRERYVAAGVEAEVA 239
Cdd:cd03785  162 REEILNLRKELKRFGLppdKPTLLVFGGSQGARAINRAVPKALPKLLER-GIQVIHQTGKGDYDEVKKLYEDLGINVKVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 240 PFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLTE 319
Cdd:cd03785  241 PFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVLAEAILD 320
                        330       340       350
                 ....*....|....*....|....*....|
gi 518172457 320 VMMQPEKLKAMGATARRLARPDATRTVVDI 349
Cdd:cd03785  321 LLNDPERLKKMAEAAKKLAKPDAAERIADL 350
murG TIGR01133
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ...
5-350 7.14e-136

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. RA Bupp K, van Heijenoort J. RL J Bacteriol 1993 Mar;175(6):1841-3 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273460 [Multi-domain]  Cd Length: 348  Bit Score: 390.50  E-value: 7.14e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457    5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:TIGR01133   3 IALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVFKA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457   85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNsAKRRTTGNPVRH 164
Cdd:TIGR01133  83 RRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDH-FEAVLVGNPVRK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  165 ELFLETPRQTLLGRR---PRLLVLGGSLGAEPLNKLLPEALGQLSEELRPeIFHQAGKQHAEITRERYVAAGVEAEVAPF 241
Cdd:TIGR01133 162 EIRSLPVPRERFGRRegkPTILVLGGSQGAKILNELVPKALAKLQEKGIQ-IVHQGGKGDLEKVKNVYQELGQEKIVTFI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  242 IKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAiDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLTEVM 321
Cdd:TIGR01133 241 DENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPEKLLEALLKLL 319
                         330       340
                  ....*....|....*....|....*....
gi 518172457  322 MQPEKLKAMGATARRLARPDATRTVVDIC 350
Cdd:TIGR01133 320 LDPANLENMAEAARKLAKPDAAKRIAELI 348
Glyco_transf_28 pfam03033
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ...
5-141 1.26e-45

Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.


Pssm-ID: 427107 [Multi-domain]  Cd Length: 139  Bit Score: 152.44  E-value: 1.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457    5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:pfam03033   1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 518172457   85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRV 141
Cdd:pfam03033  81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
 
Name Accession Description Interval E-value
murG PRK00726
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
4-356 3.64e-167

undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional


Pssm-ID: 234825 [Multi-domain]  Cd Length: 357  Bit Score: 470.38  E-value: 3.64e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457   4 NVLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQ 83
Cdd:PRK00726   3 KILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVLQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  84 ARRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNSAKRRT--TGNP 161
Cdd:PRK00726  83 ARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAvvTGNP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 162 VRHELF-LETPRQTLLGR--RPRLLVLGGSLGAEPLNKLLPEALGQLSEELRpeIFHQAGKQHAEITRERYvAAGVEAEV 238
Cdd:PRK00726 163 VREEILaLAAPPARLAGRegKPTLLVVGGSQGARVLNEAVPEALALLPEALQ--VIHQTGKGDLEEVRAAY-AAGINAEV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 239 APFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLT 318
Cdd:PRK00726 240 VPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEKLAEKLL 319
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 518172457 319 EVMMQPEKLKAMGATARRLARPDATRTVVDICLEVAHG 356
Cdd:PRK00726 320 ELLSDPERLEAMAEAARALGKPDAAERLADLIEELARK 357
MurG COG0707
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ...
1-356 8.23e-163

UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440471 [Multi-domain]  Cd Length: 363  Bit Score: 459.59  E-value: 8.23e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457   1 MGGNVLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRS 80
Cdd:COG0707    1 MSKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  81 LGQARRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNT--FSNSAKRRTT 158
Cdd:COG0707   81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETkkYFPKKKAVVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 159 GNPVRHElFLETPRQTLLGR------RPRLLVLGGSLGAEPLNKLLPEALGQLSEElRPEIFHQAGKQHAEITRERYVAA 232
Cdd:COG0707  161 GNPVRKE-ILELDRPEARAKlgldpdKPTLLVFGGSQGARALNEAVPAALAALLEA-RLQVVHQTGKGDYEEVRAAYAAA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 233 GV-EAEVAPFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAA 311
Cdd:COG0707  239 IRpNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPE 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 518172457 312 ALAAQLTEVMMQPEKLKAMGATARRLARPDATRTVVDICLEVAHG 356
Cdd:COG0707  319 KLAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
5-349 6.20e-146

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340818 [Multi-domain]  Cd Length: 350  Bit Score: 416.23  E-value: 6.20e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457   5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:cd03785    2 ILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNSAKRRT--TGNPV 162
Cdd:cd03785   82 RKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVvvTGNPV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 163 RHELFLETPRQTLLGR---RPRLLVLGGSLGAEPLNKLLPEALGQLSEElRPEIFHQAGKQHAEITRERYVAAGVEAEVA 239
Cdd:cd03785  162 REEILNLRKELKRFGLppdKPTLLVFGGSQGARAINRAVPKALPKLLER-GIQVIHQTGKGDYDEVKKLYEDLGINVKVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 240 PFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLTE 319
Cdd:cd03785  241 PFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVLAEAILD 320
                        330       340       350
                 ....*....|....*....|....*....|
gi 518172457 320 VMMQPEKLKAMGATARRLARPDATRTVVDI 349
Cdd:cd03785  321 LLNDPERLKKMAEAAKKLAKPDAAERIADL 350
murG TIGR01133
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ...
5-350 7.14e-136

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. RA Bupp K, van Heijenoort J. RL J Bacteriol 1993 Mar;175(6):1841-3 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273460 [Multi-domain]  Cd Length: 348  Bit Score: 390.50  E-value: 7.14e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457    5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:TIGR01133   3 IALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVFKA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457   85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNsAKRRTTGNPVRH 164
Cdd:TIGR01133  83 RRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDH-FEAVLVGNPVRK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  165 ELFLETPRQTLLGRR---PRLLVLGGSLGAEPLNKLLPEALGQLSEELRPeIFHQAGKQHAEITRERYVAAGVEAEVAPF 241
Cdd:TIGR01133 162 EIRSLPVPRERFGRRegkPTILVLGGSQGAKILNELVPKALAKLQEKGIQ-IVHQGGKGDLEKVKNVYQELGQEKIVTFI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  242 IKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAiDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLTEVM 321
Cdd:TIGR01133 241 DENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPEKLLEALLKLL 319
                         330       340
                  ....*....|....*....|....*....
gi 518172457  322 MQPEKLKAMGATARRLARPDATRTVVDIC 350
Cdd:TIGR01133 320 LDPANLENMAEAARKLAKPDAAKRIAELI 348
Glyco_transf_28 pfam03033
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ...
5-141 1.26e-45

Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.


Pssm-ID: 427107 [Multi-domain]  Cd Length: 139  Bit Score: 152.44  E-value: 1.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457    5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:pfam03033   1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 518172457   85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRV 141
Cdd:pfam03033  81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
PRK12446 PRK12446
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
5-303 4.42e-40

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed


Pssm-ID: 171505 [Multi-domain]  Cd Length: 352  Bit Score: 144.62  E-value: 4.42e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457   5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:PRK12446   4 IVFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGVMDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNSAKRRT--TGNPV 162
Cdd:PRK12446  84 YVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAAKHLPKEKViyTGSPV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 163 RHEL----------FLETPRqtllgRRPRLLVLGGSLGAEPLNKLLPEALGQLSeeLRPEIFHQAGKQHAEIT---RERY 229
Cdd:PRK12446 164 REEVlkgnrekglaFLGFSR-----KKPVITIMGGSLGAKKINETVREALPELL--LKYQIVHLCGKGNLDDSlqnKEGY 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518172457 230 VAAGVEAEVAPFIKDMarayawADLVICRAGALTVCELAAAGLPSFLVPLPH-AIDDHQTRNAEYLAKEGAAILL 303
Cdd:PRK12446 237 RQFEYVHGELPDILAI------TDFVISRAGSNAIFEFLTLQKPMLLIPLSKfASRGDQILNAESFERQGYASVL 305
Glyco_tran_28_C pfam04101
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ...
182-342 4.69e-38

Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.


Pssm-ID: 427711 [Multi-domain]  Cd Length: 166  Bit Score: 133.99  E-value: 4.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  182 LLVLGGSLGAEPLNKLLPEALGQLSEELRPEIFHQAGKQHAEITRERYVAAGVEAEVAPFIKDMARAYAWADLVICRAGA 261
Cdd:pfam04101   2 ILVTGGSQGARALNELVLSVLPLLELKGELQVLHQTGKGDLEEVKIDYAELGINYEVFPFIDNMAEYIKAADLVISRAGA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  262 LTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLTEVMMQPEKLKAMGATARRLARPD 341
Cdd:pfam04101  82 GTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALLKLLLNPLRLAEMAKASKASGFKD 161

                  .
gi 518172457  342 A 342
Cdd:pfam04101 162 A 162
SpsG COG3980
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall ...
161-354 1.31e-16

Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443179 [Multi-domain]  Cd Length: 342  Bit Score: 79.58  E-value: 1.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 161 PVRHElFLETPRQ--TLLGRRPRLLV-LGGSlgaEPLN---KLLpEALGQLSEELRPEIFHQAGKQHAEITRERYVAAGV 234
Cdd:COG3980  151 LLRPE-FLALRPAsrRISEEVRRILVtFGGS---DPDNltlKVL-RALLQLDPDLKITVVVGPGYPHLDELRALAAERPL 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 235 EAEVAPFIKDMARAYAWADLVICRAGAlTVCELAAAGLPSFLVplphAIDDHQTRNAEYLAKEGAAILL-PQATTDAAAL 313
Cdd:COG3980  226 NIELHRNVKDMAELMAQADLAISAAGT-TTYELAALGLPTIVV----AVADNQRAIAEALEENGAAINLgLGEELTDEEL 300
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 518172457 314 AAQLTEVMMQPEKLKAMGATARRLARPDATRTVVDICLEVA 354
Cdd:COG3980  301 ANALDELLLDPERRARMSRKARSLVDGRGAERIVEAILELL 341
YjiC COG1819
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
4-304 7.94e-13

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


Pssm-ID: 441424 [Multi-domain]  Cd Length: 268  Bit Score: 67.57  E-value: 7.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457   4 NVLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIEneVVPAAGLPLHliqvsglrgkgvgsllkapfqllrslgq 83
Cdd:COG1819    1 RILFVTLGGRGHVNPLLALARALRARGHEVTFATGPDFAD--LVEAAGLEFV---------------------------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  84 arrimrELQPVCVLGlgGYVTGPGGLAAKLAGVPLIiheqnavagtanrSLVPfaqrvcEAF-PNTFSNSAKRRTTGNPV 162
Cdd:COG1819   51 ------DWRPDLVVS--DPLALAAALAAEALGIPVV-------------SLTP------PELeYPRPPDPANVRFVGPLL 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 163 RHELFLETPRQTLLGRRPRLLVLGGSL--GAEPLNKLLPEALGQLSEELrpeIFHQAGKQHAEITReryVAAGVEA-EVA 239
Cdd:COG1819  104 PDGPAELPPWLEEDAGRPLVYVTLGTSanDRADLLRAVLEALADLGVRV---VVTTGGLDPAELGP---LPDNVRVvDYV 177
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518172457 240 PFIKDMARAyawaDLVICRAGALTVCELAAAGLPsfLVPLPHAIDdhQTRNAEYLAKEGAAILLP 304
Cdd:COG1819  178 PQDALLPRA----DAVVHHGGAGTTAEALRAGVP--QVVVPFGGD--QPLNAARVERLGAGLALP 234
GT28_Beta-DGS-like cd17507
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ...
156-355 1.54e-09

beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340861 [Multi-domain]  Cd Length: 364  Bit Score: 58.87  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 156 RTTGNPVRHELFLETPRQTLLGR------RPRLLVLGGSLGAEPLNKLLpEALGQLSEELRPEIFhqAGKQHA--EITRE 227
Cdd:cd17507  168 KVTGIPVRPSFAEVRDKDEARNElnlspdKPTVLLMGGGGGMGPVKETV-EALLDSLRAGQVLVV--CGKNKKlyEKLSG 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 228 RYvAAGVEAEVAPFIKDMARAYAWADLVICRAGALTVCELAAAGLPsflVPLPHAIDDHQTRNAEYLAKEGAAILLPQAT 307
Cdd:cd17507  245 LE-EDYINVRVLGYVDDMNELMAASDLVITKPGGLTISEALARGLP---VIIYDPIPGQEEENADFLENNGAGIIARDPE 320
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 518172457 308 TDAAALAAQLTevmmQPEKLKAMGATARRLARPDATRTVVDICLEVAH 355
Cdd:cd17507  321 ELLEIVARLID----PPSLLRMMSEAAKELKPPAAAKVIADILSLLID 364
COG4671 COG4671
Predicted glycosyl transferase [General function prediction only];
139-304 2.24e-08

Predicted glycosyl transferase [General function prediction only];


Pssm-ID: 443708 [Multi-domain]  Cd Length: 391  Bit Score: 55.24  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 139 QRVCEAFPNTFSNSAKRRTTG---NPVRHELFLETPRQTLLGRRPRLLVL--GGSLGAEplnklLPEALGQLSEELRPEI 213
Cdd:COG4671  173 YDLEESFPLPAEIADKVRYTGyvaRPAPEPPPEERDALGLLPEEPLILVSagGGGDGAE-----LLEAALAAAELLPPPD 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 214 FH--------QAGKQHAEItrERYVAAGVEAEVAPFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHaIDD 285
Cdd:COG4671  248 HRwllvtgpfMPAADRAAL--RARAAALPNVTVERFTPDFEALLAAADLSVSMGGYNTVCEILSTGKPALIVPRTA-PRT 324
                        170
                 ....*....|....*....
gi 518172457 286 HQTRNAEYLAKEGAAILLP 304
Cdd:COG4671  325 EQLIRAERLAELGLVDVLH 343
PRK13609 PRK13609
diacylglycerol glucosyltransferase; Provisional
158-355 2.22e-07

diacylglycerol glucosyltransferase; Provisional


Pssm-ID: 237445 [Multi-domain]  Cd Length: 380  Bit Score: 52.03  E-value: 2.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 158 TGNPVRHELFLETPRQTLLGR------RPRLLVLGGSLGAEPLNKLLPEALGQLSEelrPEIFHQAGKQHAEitreRYVA 231
Cdd:PRK13609 175 TGIPIRSSFELKINPDIIYNKyqlcpnKKILLIMAGAHGVLGNVKELCQSLMSVPD---LQVVVVCGKNEAL----KQSL 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 232 AGVEAE------VAPFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLV-PLPhaidDHQTRNAEYLAKEGAAILLp 304
Cdd:PRK13609 248 EDLQETnpdalkVFGYVENIDELFRVTSCMITKPGGITLSEAAALGVPVILYkPVP----GQEKENAMYFERKGAAVVI- 322
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518172457 305 qatTDAAALAAQLTEVMMQPEKLKAMGATARRLARPDATRTVVDICLEVAH 355
Cdd:PRK13609 323 ---RDDEEVFAKTEALLQDDMKLLQMKEAMKSLYLPEPADHIVDDILAENH 370
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
4-304 2.26e-07

UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.


Pssm-ID: 340817 [Multi-domain]  Cd Length: 404  Bit Score: 52.17  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457   4 NVLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIEnEVVPAAGLPLHLI-----------QVSGLRGKGVGSLLK 72
Cdd:cd03784    2 RILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFNFA-DLVEAAGLTFVPVgddpdeleldsETNLGPDSLLELLRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457  73 APFQLLRSLGQARRIMRELQPVCVLgLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANR---SLVPFAQRVCEAFPNTF 149
Cdd:cd03784   81 LLKAADELLDDLLAALRSSWKPDLV-IADPFAYAGPLVAEELGIPSVRLFTGPATLLSAYlhpFGVLNLLLSSLLEPELF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 150 SNSAKRRTTGNPVRHELFLETPRQTLLGRRPRLLVLGGSL------GAEPLNKLLPEALGQLSEELRPEIFH-------- 215
Cdd:cd03784  160 LDPLLEVLDRLRERLGLPPFSLVLLLLRLVPPLYVIGPTFpslppdRPRLPSVLGGLRIVPKNGPLPDELWEwldkqppr 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 216 ---------QAGKQHAEITREryVAAGVEAEVAPFI--------------KDMARAYAWA-----------DLVICRAGA 261
Cdd:cd03784  240 svvyvsfgsMVRDLPEELLEL--IAEALASLGQRFLwvvgpdplgglerlPDNVLVVKWVpqdellahpavGAFVTHGGW 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 518172457 262 LTVCELAAAGLPsfLVPLPHAIDdhQTRNAEYLAKEGAAILLP 304
Cdd:cd03784  318 NSTLEALYAGVP--MVVVPLFAD--QPNNAARVEELGAGVELD 356
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
9-121 2.28e-04

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


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 42.58  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457   9 AGGTGGHVFPalaCAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRgkgvgsllKAPFQLLRSLGQARRIM 88
Cdd:cd03808    9 DGGFQSFRLP---LIKALVKKGYEVHVIAPDGDKLSDELKELGVKVIDIPILRRG--------INPLKDLKALFKLYKLL 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 518172457  89 RELQPVCVL------GLggYvtgpGGLAAKLAGVPLIIH 121
Cdd:cd03808   78 KKEKPDIVHchtpkpGI--L----GRLAARLAGVPKVIY 110
Glyco_trans_4_2 pfam13477
Glycosyl transferase 4-like;
5-120 4.52e-04

Glycosyl transferase 4-like;


Pssm-ID: 433241 [Multi-domain]  Cd Length: 139  Bit Score: 40.00  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457    5 VLIMAGGTGGHVFPalaCAQEFQSRGYSVHwLGTPRGIENEVVPAAGLPLHLIQVsglRGKGVGSLLKApFQLlrslgqa 84
Cdd:pfam13477   2 ILLLANADSIHTLR---WADALADRGYDVH-VISSKGPAKDELIAEGIHVHRLKV---PRKGPLGYLKA-FRL------- 66
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 518172457   85 RRIMRELQPVCVLGLggYVTGP---GGLAAKLAGVPLII 120
Cdd:pfam13477  67 KKLIKKIKPDVVHVH--YAKPYgllAGLAARLSGFPPVV 103
PLN02605 PLN02605
monogalactosyldiacylglycerol synthase
162-348 9.13e-03

monogalactosyldiacylglycerol synthase


Pssm-ID: 215325 [Multi-domain]  Cd Length: 382  Bit Score: 37.64  E-value: 9.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 162 VRHELFLETprqtllgRRPRLLVLGGSLGAEPLNKLLpEALGQ-LSEELRPEIFHQ----AGKQHAEITRERYVAAGVEA 236
Cdd:PLN02605 196 LRRELGMDE-------DLPAVLLMGGGEGMGPLEETA-RALGDsLYDKNLGKPIGQvvviCGRNKKLQSKLESRDWKIPV 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 237 EVAPFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFL---VP------LPHAIDDHQ---TRNAEYLAKEGAAILLP 304
Cdd:PLN02605 268 KVRGFVTNMEEWMGACDCIITKAGPGTIAEALIRGLPIILngyIPgqeegnVPYVVDNGFgafSESPKEIARIVAEWFGD 347
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 518172457 305 QattdaaalaaqltevmmqPEKLKAMGATARRLARPDATRTVVD 348
Cdd:PLN02605 348 K------------------SDELEAMSENALKLARPEAVFDIVH 373
 
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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