|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
144-523 |
0e+00 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 765.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 144 VLILMSDTGGGHRASAEAIRAAFNQEFGDEYQVFITDLWTDHTPWPFNQLPRSYNFLVKHGTLWKMTYYGTSPRIVHQSN 223
Cdd:PLN02605 1 VLILMSDTGGGHRASAEAIKDAFQLEFGDEYQVFIVDLWKEHTPWPFNQLPRSYKFLVKHPQLWKMTYHGTNPRLIHQSY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 224 FAATSTFIAREIAQGLMKYQPDIIISVHPLMQHVPLRVLRSKG--LLKKIVFTTVITDLSTCHPTWFHKLVTRCYCPSTE 301
Cdd:PLN02605 81 FAATSAFVAREVAKGLMKYKPDIIVSVHPLMQHVPLRVLRWQGkeLGKKIPFTTVVTDLGTCHPTWFHKGVTRCFCPSEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 302 VAKRAQKAGLETSQIKVYGLPVRPSFVKPVRPKVELRRELGMDENLPAVLLMGGGEGMGPIEATARALADALYDKNLGEA 381
Cdd:PLN02605 161 VAKRALKRGLEPSQIRVYGLPIRPSFARAVRPKDELRRELGMDEDLPAVLLMGGGEGMGPLEETARALGDSLYDKNLGKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 382 VGQVLIICGRNKKLQSKLSSLDWKIPVQVKGFITKMEECMGACDCIITKAGPGTIAEAMIRGLPIILNGYIAGQEAGNVP 461
Cdd:PLN02605 241 IGQVVVICGRNKKLQSKLESRDWKIPVKVRGFVTNMEEWMGACDCIITKAGPGTIAEALIRGLPIILNGYIPGQEEGNVP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236072 462 YVVENGCGKFSKSPKEISKIVADWFGPASKELEIMSQNALRLAKPEAVFKIVHDMHELVRKK 523
Cdd:PLN02605 321 YVVDNGFGAFSESPKEIARIVAEWFGDKSDELEAMSENALKLARPEAVFDIVHDLHELVRQR 382
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
144-522 |
5.70e-154 |
|
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: 444.07 E-value: 5.70e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 144 VLILMSDTGGGHRASAEAIRAAFNQEFGDeYQVFITDLWTDHTPWPFNQLPRSYNFLVKHGTLWKMTYYGTSPRIVHQSN 223
Cdd:cd17507 1 VLILTASTGGGHIQAAQALKEAFREKFDN-YEVIIEDLLKYSNPVVNKILKRGEKLYKKAPTLYKLFYNLTSDRLNSISN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 224 FAATstFIAREIAQGLMKYQPDIIISVHPLMQHVPLRVLRSKGLlkKIVFTTVITDLStCHPTWFHKLVTRCYCPSTEVA 303
Cdd:cd17507 80 KAAR--LGLKKLKELLREEQPDVIISTFPLMSALVELFKRKGLL--PIPVYTVITDYV-LHSTWIHPEVDRYFVASEEVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 304 KRAQKAGLETSQIKVYGLPVRPSFVKpVRPKVELRRELGMDENLPAVLLMGGGEGMGPIEATARALADALYDknlgeavG 383
Cdd:cd17507 155 RELVERGVTPSQIKVTGIPVRPSFAE-VRDKDEARNELNLSPDKPTVLLMGGGGGMGPVKETVEALLDSLRA-------G 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 384 QVLIICGRNKKLQSKLSSLDWK-IPVQVKGFITKMEECMGACDCIITKAGPGTIAEAMIRGLPIILNGYIAGQEAGNVPY 462
Cdd:cd17507 227 QVLVVCGKNKKLYEKLSGLEEDyINVRVLGYVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYDPIPGQEEENADF 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 463 VVENGCGKFSKSPKEISKIVADWFGPASkELEIMSQNALRLAKPeAVFKIVHDMHELVRK 522
Cdd:cd17507 307 LENNGAGIIARDPEELLEIVARLIDPPS-LLRMMSEAAKELKPP-AAAKVIADILSLLID 364
|
|
| MGDG_synth |
pfam06925 |
Monogalactosyldiacylglycerol (MGDG) synthase; This family represents a conserved region of ... |
155-323 |
1.96e-81 |
|
Monogalactosyldiacylglycerol (MGDG) synthase; This family represents a conserved region of approximately 180 residues within plant and bacterial monogalactosyldiacylglycerol (MGDG) synthase (EC:2.4.1.46). In Arabidopsis, there are two types of MGDG synthase which differ in their N-terminal portion: type A and type B.
Pssm-ID: 284368 Cd Length: 169 Bit Score: 251.13 E-value: 1.96e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 155 HRASAEAIRAAFNQEFGDEYQVFITDLWTDHTPWPFNQLPRSYNFLVKHGTLWKMTYYGTSPRIVHQSNFAATSTFIARE 234
Cdd:pfam06925 1 HNQAAEALREAFNNEFGDEYQVVVHDSLKELNPFLIKFVLRSYLFLVKHSPLYRLLYYGTEPKIPHKSILAKLATFFARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 235 IAQGLMKYQPDIIISVHPLMQHVPLRVLRSKGLLKKIVFTTVITDLSTCHPTWFHKLVTRCYCPSTEVAKRAQKAGLETS 314
Cdd:pfam06925 81 LAALLEEFQPDIIISTHPLPAAVPLSVLKSKGLLKRVLVVTVVTDFRTCHPFWLHPEIDRYYVPSKEVKKEALEKGIDPS 160
|
....*....
gi 15236072 315 QIKVYGLPV 323
Cdd:pfam06925 161 NIKVTGIPV 169
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
307-522 |
5.87e-17 |
|
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: 82.48 E-value: 5.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 307 QKAGLETSQIKVYGLPVRPSFVKPVRPkvELRRELGMDENLP----------AVLlmgggegmgpIEATARALADALYDK 376
Cdd:COG0707 148 TKKYFPKKKAVVTGNPVRKEILELDRP--EARAKLGLDPDKPtllvfggsqgARA----------LNEAVPAALAALLEA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 377 NLgeavgQVLIICGRNK--KLQSKLSSLDWKiPVQVKGFITKMEECMGACDCIITKAGPGTIAEAMIRGLPIIL--NGYI 452
Cdd:COG0707 216 RL-----QVVHQTGKGDyeEVRAAYAAAIRP-NAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILvpLPHA 289
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236072 453 AG--QEAgNVPYVVENGCGKFSK----SPKEISKIVADWFGPASKeLEIMSQNALRLAKPEAVFKIVHDMHELVRK 522
Cdd:COG0707 290 ADdhQTK-NARALVEAGAAVLIPqselTPEKLAEALEELLEDPER-LAKMAEAARALARPDAAERIADLILELAKG 363
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
144-523 |
0e+00 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 765.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 144 VLILMSDTGGGHRASAEAIRAAFNQEFGDEYQVFITDLWTDHTPWPFNQLPRSYNFLVKHGTLWKMTYYGTSPRIVHQSN 223
Cdd:PLN02605 1 VLILMSDTGGGHRASAEAIKDAFQLEFGDEYQVFIVDLWKEHTPWPFNQLPRSYKFLVKHPQLWKMTYHGTNPRLIHQSY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 224 FAATSTFIAREIAQGLMKYQPDIIISVHPLMQHVPLRVLRSKG--LLKKIVFTTVITDLSTCHPTWFHKLVTRCYCPSTE 301
Cdd:PLN02605 81 FAATSAFVAREVAKGLMKYKPDIIVSVHPLMQHVPLRVLRWQGkeLGKKIPFTTVVTDLGTCHPTWFHKGVTRCFCPSEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 302 VAKRAQKAGLETSQIKVYGLPVRPSFVKPVRPKVELRRELGMDENLPAVLLMGGGEGMGPIEATARALADALYDKNLGEA 381
Cdd:PLN02605 161 VAKRALKRGLEPSQIRVYGLPIRPSFARAVRPKDELRRELGMDEDLPAVLLMGGGEGMGPLEETARALGDSLYDKNLGKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 382 VGQVLIICGRNKKLQSKLSSLDWKIPVQVKGFITKMEECMGACDCIITKAGPGTIAEAMIRGLPIILNGYIAGQEAGNVP 461
Cdd:PLN02605 241 IGQVVVICGRNKKLQSKLESRDWKIPVKVRGFVTNMEEWMGACDCIITKAGPGTIAEALIRGLPIILNGYIPGQEEGNVP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236072 462 YVVENGCGKFSKSPKEISKIVADWFGPASKELEIMSQNALRLAKPEAVFKIVHDMHELVRKK 523
Cdd:PLN02605 321 YVVDNGFGAFSESPKEIARIVAEWFGDKSDELEAMSENALKLARPEAVFDIVHDLHELVRQR 382
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
144-522 |
5.70e-154 |
|
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: 444.07 E-value: 5.70e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 144 VLILMSDTGGGHRASAEAIRAAFNQEFGDeYQVFITDLWTDHTPWPFNQLPRSYNFLVKHGTLWKMTYYGTSPRIVHQSN 223
Cdd:cd17507 1 VLILTASTGGGHIQAAQALKEAFREKFDN-YEVIIEDLLKYSNPVVNKILKRGEKLYKKAPTLYKLFYNLTSDRLNSISN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 224 FAATstFIAREIAQGLMKYQPDIIISVHPLMQHVPLRVLRSKGLlkKIVFTTVITDLStCHPTWFHKLVTRCYCPSTEVA 303
Cdd:cd17507 80 KAAR--LGLKKLKELLREEQPDVIISTFPLMSALVELFKRKGLL--PIPVYTVITDYV-LHSTWIHPEVDRYFVASEEVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 304 KRAQKAGLETSQIKVYGLPVRPSFVKpVRPKVELRRELGMDENLPAVLLMGGGEGMGPIEATARALADALYDknlgeavG 383
Cdd:cd17507 155 RELVERGVTPSQIKVTGIPVRPSFAE-VRDKDEARNELNLSPDKPTVLLMGGGGGMGPVKETVEALLDSLRA-------G 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 384 QVLIICGRNKKLQSKLSSLDWK-IPVQVKGFITKMEECMGACDCIITKAGPGTIAEAMIRGLPIILNGYIAGQEAGNVPY 462
Cdd:cd17507 227 QVLVVCGKNKKLYEKLSGLEEDyINVRVLGYVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYDPIPGQEEENADF 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 463 VVENGCGKFSKSPKEISKIVADWFGPASkELEIMSQNALRLAKPeAVFKIVHDMHELVRK 522
Cdd:cd17507 307 LENNGAGIIARDPEELLEIVARLIDPPS-LLRMMSEAAKELKPP-AAAKVIADILSLLID 364
|
|
| MGDG_synth |
pfam06925 |
Monogalactosyldiacylglycerol (MGDG) synthase; This family represents a conserved region of ... |
155-323 |
1.96e-81 |
|
Monogalactosyldiacylglycerol (MGDG) synthase; This family represents a conserved region of approximately 180 residues within plant and bacterial monogalactosyldiacylglycerol (MGDG) synthase (EC:2.4.1.46). In Arabidopsis, there are two types of MGDG synthase which differ in their N-terminal portion: type A and type B.
Pssm-ID: 284368 Cd Length: 169 Bit Score: 251.13 E-value: 1.96e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 155 HRASAEAIRAAFNQEFGDEYQVFITDLWTDHTPWPFNQLPRSYNFLVKHGTLWKMTYYGTSPRIVHQSNFAATSTFIARE 234
Cdd:pfam06925 1 HNQAAEALREAFNNEFGDEYQVVVHDSLKELNPFLIKFVLRSYLFLVKHSPLYRLLYYGTEPKIPHKSILAKLATFFARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 235 IAQGLMKYQPDIIISVHPLMQHVPLRVLRSKGLLKKIVFTTVITDLSTCHPTWFHKLVTRCYCPSTEVAKRAQKAGLETS 314
Cdd:pfam06925 81 LAALLEEFQPDIIISTHPLPAAVPLSVLKSKGLLKRVLVVTVVTDFRTCHPFWLHPEIDRYYVPSKEVKKEALEKGIDPS 160
|
....*....
gi 15236072 315 QIKVYGLPV 323
Cdd:pfam06925 161 NIKVTGIPV 169
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
140-519 |
5.06e-38 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 143.71 E-value: 5.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 140 RPKKVLILMSDTGGGHRASAEAIRAAFNQEfGDEyQVFITDLWTDHTPWpFNQLPRsYNFLVKHG---TLWKMTYYGTSP 216
Cdd:PRK13609 3 KNPKVLILTAHYGNGHVQVAKTLEQTFRQK-GIK-DVIVCDLFGESHPV-ITEITK-YLYLKSYTigkELYRLFYYGVEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 217 rIVHQSNFAATSTFIAREIAQGLMKYQPDIIISVHPlMQHVPlrVLRSKgLLKKIVFTTVITDLSTcHPTWFHKLVTRCY 296
Cdd:PRK13609 79 -IYDKKIFSWYANFGRKRLKLLLQAEKPDIVINTFP-IIAVP--ELKKQ-TGISIPTYNVLTDFCL-HKIWVHREVDRYF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 297 CPSTEVAKRAQKAGLETSQIKVYGLPVRPSFVKPVrPKVELRRELGMDENLPAVLLMGGGEGMGPieaTARALADAL-YD 375
Cdd:PRK13609 153 VATDHVKKVLVDIGVPPEQVVETGIPIRSSFELKI-NPDIIYNKYQLCPNKKILLIMAGAHGVLG---NVKELCQSLmSV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 376 KNLgeavgQVLIICGRNKKLQSKLSSLDWKIPVQVK--GFITKMEECMGACDCIITKAGPGTIAEAMIRGLPIILNGYIA 453
Cdd:PRK13609 229 PDL-----QVVVVCGKNEALKQSLEDLQETNPDALKvfGYVENIDELFRVTSCMITKPGGITLSEAAALGVPVILYKPVP 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 454 GQEAGNVPYVVENGCGKFSKSPKEI----SKIVADwfgpaSKELEIMSQNALRLAKPEAVFKIVHDMHEL 519
Cdd:PRK13609 304 GQEKENAMYFERKGAAVVIRDDEEVfaktEALLQD-----DMKLLQMKEAMKSLYLPEPADHIVDDILAE 368
|
|
| PRK13608 |
PRK13608 |
diacylglycerol glucosyltransferase; Provisional |
142-520 |
1.64e-23 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 184179 [Multi-domain] Cd Length: 391 Bit Score: 102.57 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 142 KKVLILMSDTGGGHRASAEAIRAAFNQEFGDEYQVFITDLWTDHTP--------WPFNqlprSYNFLvkhGTLWKMTYYG 213
Cdd:PRK13608 6 KKILIITGSFGNGHMQVTQSIVNQLNDMNLDHLSVIEHDLFMEAHPiltsickkWYIN----SFKYF---RNMYKGFYYS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 214 TSPRIvhQSNFaaTSTFIAREIAQGLMKYQPDIIISVHPlmqhVPLRVLRSKGLLKKIVFTTVITDLsTCHPTWFHKLVT 293
Cdd:PRK13608 79 RPDKL--DKCF--YKYYGLNKLINLLIKEKPDLILLTFP----TPVMSVLTEQFNINIPVATVMTDY-RLHKNWITPYST 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 294 RCYCPSTEVAKRAQKAGLETSQIKVYGLPVRPSFVKPVRPKVELRRElGMDENLPAVLlmgggegmgpIEATARALA--- 370
Cdd:PRK13608 150 RYYVATKETKQDFIDVGIDPSTVKVTGIPIDNKFETPIDQKQWLIDN-NLDPDKQTIL----------MSAGAFGVSkgf 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 371 DALYDKNLGE-AVGQVLIICGRNKKLQSKLSSlDWK--IPVQVKGFITKMEECMGACDCIITKAGPGTIAEAMIRGLPII 447
Cdd:PRK13608 219 DTMITDILAKsANAQVVMICGKSKELKRSLTA-KFKsnENVLILGYTKHMNEWMASSQLMITKPGGITISEGLARCIPMI 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15236072 448 LNGYIAGQEAGNVPYVVENGCGKFSKSPKEISKIVADWFGPASKeLEIMSQNALRLAKPEAVFKIVHDMHELV 520
Cdd:PRK13608 298 FLNPAPGQELENALYFEEKGFGKIADTPEEAIKIVASLTNGNEQ-LTNMISTMEQDKIKYATQTICRDLLDLI 369
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
307-522 |
5.87e-17 |
|
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: 82.48 E-value: 5.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 307 QKAGLETSQIKVYGLPVRPSFVKPVRPkvELRRELGMDENLP----------AVLlmgggegmgpIEATARALADALYDK 376
Cdd:COG0707 148 TKKYFPKKKAVVTGNPVRKEILELDRP--EARAKLGLDPDKPtllvfggsqgARA----------LNEAVPAALAALLEA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 377 NLgeavgQVLIICGRNK--KLQSKLSSLDWKiPVQVKGFITKMEECMGACDCIITKAGPGTIAEAMIRGLPIIL--NGYI 452
Cdd:COG0707 216 RL-----QVVHQTGKGDyeEVRAAYAAAIRP-NAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILvpLPHA 289
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236072 453 AG--QEAgNVPYVVENGCGKFSK----SPKEISKIVADWFGPASKeLEIMSQNALRLAKPEAVFKIVHDMHELVRK 522
Cdd:COG0707 290 ADdhQTK-NARALVEAGAAVLIPqselTPEKLAEALEELLEDPER-LAKMAEAARALARPDAAERIADLILELAKG 363
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
316-513 |
7.87e-17 |
|
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: 81.88 E-value: 7.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 316 IKVYGLPVRPSFVKPVRPkvelRRELGMDENLPAVLLMGGGEGMGPIEATARALADALYDKNLgeavgQVLIICGRNKKL 395
Cdd:cd03785 154 VVVTGNPVREEILNLRKE----LKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLERGI-----QVIHQTGKGDYD 224
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 396 QSKLSSLDWKIPVQVKGFITKMEECMGACDCIITKAGPGTIAEAMIRGLPIILNGY-IAG---QEAgNVPYVVENGCGKF 471
Cdd:cd03785 225 EVKKLYEDLGINVKVFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYpYAAddhQEA-NARALEKAGAAIV 303
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170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15236072 472 ----SKSPKEISKIVADWFGpASKELEIMSQNALRLAKPEAVFKIV 513
Cdd:cd03785 304 idqeELTPEVLAEAILDLLN-DPERLKKMAEAAKKLAKPDAAERIA 348
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| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
366-522 |
9.86e-13 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 69.39 E-value: 9.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 366 ARALADALYD--KNLGEAVgQVLIICGRNKKLQSKlSSLDWKIPVQVKGFITKMEECMGACDCIITKAGPGTIAEAMIRG 443
Cdd:PRK00726 195 ARVLNEAVPEalALLPEAL-QVIHQTGKGDLEEVR-AAYAAGINAEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAG 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 444 LPIIL--NGYIAG--QEAgNVPYVVENGCGKFSK----SPKEISKIVADWFGPASKeLEIMSQNALRLAKPEAVFKIVHD 515
Cdd:PRK00726 273 LPAILvpLPHAADdhQTA-NARALVDAGAALLIPqsdlTPEKLAEKLLELLSDPER-LEAMAEAARALGKPDAAERLADL 350
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....*..
gi 15236072 516 MHELVRK 522
Cdd:PRK00726 351 IEELARK 357
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| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
384-509 |
2.74e-10 |
|
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: 59.26 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 384 QVLIICGRNKKLQSKLSSLDWKIPVQVKGFITKMEECMGACDCIITKAGPGTIAEAMIRGLPIIL--NGYIAGQEAG-NV 460
Cdd:pfam04101 32 QVLHQTGKGDLEEVKIDYAELGINYEVFPFIDNMAEYIKAADLVISRAGAGTIAELLALGKPAILvpNPSAARGHQDnNA 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15236072 461 PYVVENGCGKF----SKSPKEISKIVADWFGPASKELEiMSQNALRLAKPEAV 509
Cdd:pfam04101 112 KELVKAGAALVilqkELTPEKLIEALLKLLLNPLRLAE-MAKASKASGFKDAA 163
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| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
240-468 |
2.80e-04 |
|
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.
Pssm-ID: 340846 [Multi-domain] Cd Length: 345 Bit Score: 43.11 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 240 MKYQPDIIiSVHPLMQhVPLRVLRSKGLLKKIVFTTVITDLSTCHPTWFHKLV----TRCYCPSTEVAKRaQKAGLETSQ 315
Cdd:cd03819 73 RRERIDLI-HAHSRAP-AWLGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVrargDRVIAVSELVRDH-LIEALGVDP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 316 IKVYGLP--VRPSFVKPvRPKVELRRELGMDENLPAVLLMGGGEGmgpiEATARALADALYDknLGEAVGQVLIICG--- 390
Cdd:cd03819 150 ERIRVIPngVDTDRFPP-EAEAEERAQLGLPEGKPVVGYVGRLSP----EKGWLLLVDAAAE--LKDEPDFRLLVAGdgp 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236072 391 --RNKKLQSKLSSLDWKipVQVKGFITKMEECMGACDCII----TKAGPGTIAEAMIRGLPII---LNGYIAGQEAGNVP 461
Cdd:cd03819 223 erDEIRRLVERLGLRDR--VTFTGFREDVPAALAASDVVVlpslHEEFGRVALEAMACGTPVVatdVGGAREIVVHGRTG 300
|
....*..
gi 15236072 462 YVVENGC 468
Cdd:cd03819 301 LLVPPGD 307
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| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
386-447 |
2.22e-03 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 38.65 E-value: 2.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15236072 386 LIICGRN--KKLQSKLSSLDWKipVQVKGFITKMEECMGACDCII----TKAGPGTIAEAMIRGLPII 447
Cdd:pfam13692 36 LVIVGDGpeEELEELAAGLEDR--VIFTGFVEDLAELLAAADVFVlpslYEGFGLKLLEAMAAGLPVV 101
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