|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
4-356 |
5.85e-170 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 477.32 E-value: 5.85e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 4 NVLIMAGGTGGHVFPALACAREFQARGYKVHWLGTPRGIENELVPQAGLTLHLINVTGLRGKGRLSLLKAPFMLLKALMQ 83
Cdd:PRK00726 3 KILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 84 ARKVVREVKPVCVVGFGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLASFASRVCEAFPNTFADSSKRRT--TGNP 161
Cdd:PRK00726 83 ARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAvvTGNP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 162 VRVELF-LETPRQALAGR--KARLLVLGGSLGAEPLNKLLPEALSQLPQDIQpeVFHQSGKNHDAVTAERYRNvGVEAQV 238
Cdd:PRK00726 163 VREEILaLAAPPARLAGRegKPTLLVVGGSQGARVLNEAVPEALALLPEALQ--VIHQTGKGDLEEVRAAYAA-GINAEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 239 APFIQNMAQAYGWADLVVCRAGALTISELAAAGLPSLLIPLPHAIDDHQSRNADYLAREGAAFVMPQATTGAAEMAARLK 318
Cdd:PRK00726 240 VPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEKLAEKLL 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 489526708 319 EVLMQPEQLNSMARTARSLAMPDATSTVVNVCVEVAHG 356
Cdd:PRK00726 320 ELLSDPERLEAMAEAARALGKPDAAERLADLIEELARK 357
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-356 |
2.40e-164 |
|
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: 463.45 E-value: 2.40e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 1 MDANVLIMAGGTGGHVFPALACAREFQARGYKVHWLGTPRGIENELVPQAGLTLHLINVTGLRGKGRLSLLKAPFMLLKA 80
Cdd:COG0707 1 MSKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 81 LMQARKVVREVKPVCVVGFGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLASFASRVCEAFPNT--FADSSKRRTT 158
Cdd:COG0707 81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETkkYFPKKKAVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 159 GNPVRVELFLETPRQALA-----GRKARLLVLGGSLGAEPLNKLLPEALSQLPQDiQPEVFHQSGKNHDAVTAERYRN-V 232
Cdd:COG0707 161 GNPVRKEILELDRPEARAklgldPDKPTLLVFGGSQGARALNEAVPAALAALLEA-RLQVVHQTGKGDYEEVRAAYAAaI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 233 GVEAQVAPFIQNMAQAYGWADLVVCRAGALTISELAAAGLPSLLIPLPHAIDDHQSRNADYLAREGAAFVMPQATTGAAE 312
Cdd:COG0707 240 RPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPEK 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489526708 313 MAARLKEVLMQPEQLNSMARTARSLAMPDATSTVVNVCVEVAHG 356
Cdd:COG0707 320 LAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
5-349 |
2.71e-151 |
|
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: 429.71 E-value: 2.71e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 5 VLIMAGGTGGHVFPALACAREFQARGYKVHWLGTPRGIENELVPQAGLTLHLINVTGLRGKGRLSLLKAPFMLLKALMQA 84
Cdd:cd03785 2 ILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 85 RKVVREVKPVCVVGFGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLASFASRVCEAFPNTFADSSKRRT--TGNPV 162
Cdd:cd03785 82 RKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVvvTGNPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 163 RVELFLETPRQA---LAGRKARLLVLGGSLGAEPLNKLLPEALSQLP-QDIQpeVFHQSGKNHDAVTAERYRNVGVEAQV 238
Cdd:cd03785 162 REEILNLRKELKrfgLPPDKPTLLVFGGSQGARAINRAVPKALPKLLeRGIQ--VIHQTGKGDYDEVKKLYEDLGINVKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 239 APFIQNMAQAYGWADLVVCRAGALTISELAAAGLPSLLIPLPHAIDDHQSRNADYLAREGAAFVMPQATTGAAEMAARLK 318
Cdd:cd03785 240 FPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVLAEAIL 319
|
330 340 350
....*....|....*....|....*....|.
gi 489526708 319 EVLMQPEQLNSMARTARSLAMPDATSTVVNV 349
Cdd:cd03785 320 DLLNDPERLKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
5-350 |
1.96e-138 |
|
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: 397.04 E-value: 1.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 5 VLIMAGGTGGHVFPALACAREFQARGYKVHWLGTPRGIENELVPQAGLTLHLINVTGLRGKGRLSLLKAPFMLLKALMQA 84
Cdd:TIGR01133 3 IALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVFKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 85 RKVVREVKPVCVVGFGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLASFASRVCEAFPNTFaDSSKRRTTGNPVRV 164
Cdd:TIGR01133 83 RRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAK-DHFEAVLVGNPVRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 165 ELF-LETPRQALAGR--KARLLVLGGSLGAEPLNKLLPEALSQLP-QDIQpeVFHQSGKNHDAVTAERYRNVGVEAQVAP 240
Cdd:TIGR01133 162 EIRsLPVPRERFGRRegKPTILVLGGSQGAKILNELVPKALAKLQeKGIQ--IVHQGGKGDLEKVKNVYQELGQEKIVTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 241 FIQNMAQAYGWADLVVCRAGALTISELAAAGLPSLLIPLPHAiDDHQSRNADYLAREGAAFVMPQATTGAAEMAARLKEV 320
Cdd:TIGR01133 240 IDENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPEKLLEALLKL 318
|
330 340 350
....*....|....*....|....*....|
gi 489526708 321 LMQPEQLNSMARTARSLAMPDATSTVVNVC 350
Cdd:TIGR01133 319 LLDPANLENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
5-141 |
4.92e-48 |
|
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: 158.99 E-value: 4.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 5 VLIMAGGTGGHVFPALACAREFQARGYKVHWLGTPRGIENELVPQAGLTLHLINVTGLRGKGRLSLLKAPFMLLKALMQA 84
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489526708 85 RKVVREVKPVCVVGFGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLASFASRV 141
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
4-356 |
5.85e-170 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 477.32 E-value: 5.85e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 4 NVLIMAGGTGGHVFPALACAREFQARGYKVHWLGTPRGIENELVPQAGLTLHLINVTGLRGKGRLSLLKAPFMLLKALMQ 83
Cdd:PRK00726 3 KILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 84 ARKVVREVKPVCVVGFGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLASFASRVCEAFPNTFADSSKRRT--TGNP 161
Cdd:PRK00726 83 ARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAvvTGNP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 162 VRVELF-LETPRQALAGR--KARLLVLGGSLGAEPLNKLLPEALSQLPQDIQpeVFHQSGKNHDAVTAERYRNvGVEAQV 238
Cdd:PRK00726 163 VREEILaLAAPPARLAGRegKPTLLVVGGSQGARVLNEAVPEALALLPEALQ--VIHQTGKGDLEEVRAAYAA-GINAEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 239 APFIQNMAQAYGWADLVVCRAGALTISELAAAGLPSLLIPLPHAIDDHQSRNADYLAREGAAFVMPQATTGAAEMAARLK 318
Cdd:PRK00726 240 VPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEKLAEKLL 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 489526708 319 EVLMQPEQLNSMARTARSLAMPDATSTVVNVCVEVAHG 356
Cdd:PRK00726 320 ELLSDPERLEAMAEAARALGKPDAAERLADLIEELARK 357
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-356 |
2.40e-164 |
|
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: 463.45 E-value: 2.40e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 1 MDANVLIMAGGTGGHVFPALACAREFQARGYKVHWLGTPRGIENELVPQAGLTLHLINVTGLRGKGRLSLLKAPFMLLKA 80
Cdd:COG0707 1 MSKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 81 LMQARKVVREVKPVCVVGFGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLASFASRVCEAFPNT--FADSSKRRTT 158
Cdd:COG0707 81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETkkYFPKKKAVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 159 GNPVRVELFLETPRQALA-----GRKARLLVLGGSLGAEPLNKLLPEALSQLPQDiQPEVFHQSGKNHDAVTAERYRN-V 232
Cdd:COG0707 161 GNPVRKEILELDRPEARAklgldPDKPTLLVFGGSQGARALNEAVPAALAALLEA-RLQVVHQTGKGDYEEVRAAYAAaI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 233 GVEAQVAPFIQNMAQAYGWADLVVCRAGALTISELAAAGLPSLLIPLPHAIDDHQSRNADYLAREGAAFVMPQATTGAAE 312
Cdd:COG0707 240 RPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPEK 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489526708 313 MAARLKEVLMQPEQLNSMARTARSLAMPDATSTVVNVCVEVAHG 356
Cdd:COG0707 320 LAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
5-349 |
2.71e-151 |
|
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: 429.71 E-value: 2.71e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 5 VLIMAGGTGGHVFPALACAREFQARGYKVHWLGTPRGIENELVPQAGLTLHLINVTGLRGKGRLSLLKAPFMLLKALMQA 84
Cdd:cd03785 2 ILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 85 RKVVREVKPVCVVGFGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLASFASRVCEAFPNTFADSSKRRT--TGNPV 162
Cdd:cd03785 82 RKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVvvTGNPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 163 RVELFLETPRQA---LAGRKARLLVLGGSLGAEPLNKLLPEALSQLP-QDIQpeVFHQSGKNHDAVTAERYRNVGVEAQV 238
Cdd:cd03785 162 REEILNLRKELKrfgLPPDKPTLLVFGGSQGARAINRAVPKALPKLLeRGIQ--VIHQTGKGDYDEVKKLYEDLGINVKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 239 APFIQNMAQAYGWADLVVCRAGALTISELAAAGLPSLLIPLPHAIDDHQSRNADYLAREGAAFVMPQATTGAAEMAARLK 318
Cdd:cd03785 240 FPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVLAEAIL 319
|
330 340 350
....*....|....*....|....*....|.
gi 489526708 319 EVLMQPEQLNSMARTARSLAMPDATSTVVNV 349
Cdd:cd03785 320 DLLNDPERLKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
5-350 |
1.96e-138 |
|
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: 397.04 E-value: 1.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 5 VLIMAGGTGGHVFPALACAREFQARGYKVHWLGTPRGIENELVPQAGLTLHLINVTGLRGKGRLSLLKAPFMLLKALMQA 84
Cdd:TIGR01133 3 IALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVFKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 85 RKVVREVKPVCVVGFGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLASFASRVCEAFPNTFaDSSKRRTTGNPVRV 164
Cdd:TIGR01133 83 RRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAK-DHFEAVLVGNPVRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 165 ELF-LETPRQALAGR--KARLLVLGGSLGAEPLNKLLPEALSQLP-QDIQpeVFHQSGKNHDAVTAERYRNVGVEAQVAP 240
Cdd:TIGR01133 162 EIRsLPVPRERFGRRegKPTILVLGGSQGAKILNELVPKALAKLQeKGIQ--IVHQGGKGDLEKVKNVYQELGQEKIVTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 241 FIQNMAQAYGWADLVVCRAGALTISELAAAGLPSLLIPLPHAiDDHQSRNADYLAREGAAFVMPQATTGAAEMAARLKEV 320
Cdd:TIGR01133 240 IDENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPEKLLEALLKL 318
|
330 340 350
....*....|....*....|....*....|
gi 489526708 321 LMQPEQLNSMARTARSLAMPDATSTVVNVC 350
Cdd:TIGR01133 319 LLDPANLENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
5-141 |
4.92e-48 |
|
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: 158.99 E-value: 4.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 5 VLIMAGGTGGHVFPALACAREFQARGYKVHWLGTPRGIENELVPQAGLTLHLINVTGLRGKGRLSLLKAPFMLLKALMQA 84
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489526708 85 RKVVREVKPVCVVGFGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLASFASRV 141
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
|
|
| PRK12446 |
PRK12446 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
5-305 |
3.34e-45 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
Pssm-ID: 171505 [Multi-domain] Cd Length: 352 Bit Score: 158.10 E-value: 3.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 5 VLIMAGGTGGHVFPALACAREFQARGYKVHWLGTPRGIENELVPQAGLTLHLINVTGLRGKGRLSLLKAPFMLLKALMQA 84
Cdd:PRK12446 4 IVFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGVMDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 85 RKVVREVKPVCVVGFGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLASFASRVCEAFPNTFADSSKRRT--TGNPV 162
Cdd:PRK12446 84 YVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAAKHLPKEKViyTGSPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 163 RVELFLETPRQALA-----GRKARLLVLGGSLGAEPLNKLLPEALSQLPQDIQpeVFHQSGK---NHDAVTAERYRNVGV 234
Cdd:PRK12446 164 REEVLKGNREKGLAflgfsRKKPVITIMGGSLGAKKINETVREALPELLLKYQ--IVHLCGKgnlDDSLQNKEGYRQFEY 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489526708 235 EAQVAPFIQNMaqaygwADLVVCRAGALTISELAAAGLPSLLIPLPH-AIDDHQSRNADYLAREGAAFVMPQ 305
Cdd:PRK12446 242 VHGELPDILAI------TDFVISRAGSNAIFEFLTLQKPMLLIPLSKfASRGDQILNAESFERQGYASVLYE 307
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
182-346 |
1.67e-41 |
|
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: 142.85 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 182 LLVLGGSLGAEPLNKLLPEALSQLPQDIQPEVFHQSGKNHDAVTAERYRNVGVEAQVAPFIQNMAQAYGWADLVVCRAGA 261
Cdd:pfam04101 2 ILVTGGSQGARALNELVLSVLPLLELKGELQVLHQTGKGDLEEVKIDYAELGINYEVFPFIDNMAEYIKAADLVISRAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 262 LTISELAAAGLPSLLIPLPHAIDDHQSRNADYLAREGAAFVMPQATTGAAEMAARLKEVLMQPEQLNSMARTARSLAMPD 341
Cdd:pfam04101 82 GTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALLKLLLNPLRLAEMAKASKASGFKD 161
|
....*
gi 489526708 342 ATSTV 346
Cdd:pfam04101 162 AAKRL 166
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
4-338 |
6.79e-17 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 79.51 E-value: 6.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 4 NVLIMAGGTGGHVFPALACAREFQARGYKVHWLGTPRGIEneLVPQAGLTLHlinvtglrgkgrlsllkapfmllkalmq 83
Cdd:COG1819 1 RILFVTLGGRGHVNPLLALARALRARGHEVTFATGPDFAD--LVEAAGLEFV---------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 84 arkvvrEVKPVCVVGfgGYVTGPGGLAAKLAGVPLIIHeqnavagtanrSLASFasrvceaFPNTFADSSKRRTTGNPVR 163
Cdd:COG1819 51 ------DWRPDLVVS--DPLALAAALAAEALGIPVVSL-----------TPPEL-------EYPRPPDPANVRFVGPLLP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 164 VELFLETPRQALAGRKARLLVLGGSL--GAEPLNKLLPEALSQLPQDIqpeVFhQSGKNHDAVTAERYRNVGVEAQVaPF 241
Cdd:COG1819 105 DGPAELPPWLEEDAGRPLVYVTLGTSanDRADLLRAVLEALADLGVRV---VV-TTGGLDPAELGPLPDNVRVVDYV-PQ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 242 IQNMAQAygwaDLVVCRAGALTISELAAAGLPSLLIplPHAIDdhQSRNADYLAREGAAFVMPQATTGAAEMAARLKEVL 321
Cdd:COG1819 180 DALLPRA----DAVVHHGGAGTTAEALRAGVPQVVV--PFGGD--QPLNAARVERLGAGLALPPRRLTAEALRAALRRLL 251
|
330
....*....|....*..
gi 489526708 322 MQPeqlnSMARTARSLA 338
Cdd:COG1819 252 ADP----SYRERAARLA 264
|
|
| SpsG |
COG3980 |
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall ... |
161-337 |
2.64e-15 |
|
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443179 [Multi-domain] Cd Length: 342 Bit Score: 75.73 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 161 PVRVElFLETPRQALAGRKA--RLLV-LGGSlgaEPLN---KLLpEALSQLPQDIQPEVFHQSGKNHDAVTAERYRNVGV 234
Cdd:COG3980 151 LLRPE-FLALRPASRRISEEvrRILVtFGGS---DPDNltlKVL-RALLQLDPDLKITVVVGPGYPHLDELRALAAERPL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 235 EAQVAPFIQNMAQAYGWADLVVCRAGAlTISELAAAGLPSLLIplphAIDDHQSRNADYLAREGAAFVM-PQATTGAAEM 313
Cdd:COG3980 226 NIELHRNVKDMAELMAQADLAISAAGT-TTYELAALGLPTIVV----AVADNQRAIAEALEENGAAINLgLGEELTDEEL 300
|
170 180
....*....|....*....|....
gi 489526708 314 AARLKEVLMQPEQLNSMARTARSL 337
Cdd:COG3980 301 ANALDELLLDPERRARMSRKARSL 324
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
151-348 |
1.38e-13 |
|
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: 70.81 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 151 DSSKRRTTGNPVRVElFLETPRQALAGRKARL-------LVLGGSLGAEPLNKLLpEALSQLPQDIQPEVFhqSGKNHDA 223
Cdd:cd17507 163 TPSQIKVTGIPVRPS-FAEVRDKDEARNELNLspdkptvLLMGGGGGMGPVKETV-EALLDSLRAGQVLVV--CGKNKKL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 224 V-----TAERYRNVgveaQVAPFIQNMAQAYGWADLVVCRAGALTISELAAAGLPSLLIPlphAIDDHQSRNADYLAREG 298
Cdd:cd17507 239 YeklsgLEEDYINV----RVLGYVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYD---PIPGQEEENADFLENNG 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489526708 299 AAFVmpqatTGAAEMAARLKEVLM-QPEQLNSMARTARSLAMPDATSTVVN 348
Cdd:cd17507 312 AGII-----ARDPEELLEIVARLIdPPSLLRMMSEAAKELKPPAAAKVIAD 357
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
158-355 |
2.31e-13 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 70.52 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 158 TGNPVRVELFLETP------RQALAGRKARLLVLGGSLGAEPLNKLLPEALSQLPQdiqPEVFHQSGKNhdavTAERYRN 231
Cdd:PRK13609 175 TGIPIRSSFELKINpdiiynKYQLCPNKKILLIMAGAHGVLGNVKELCQSLMSVPD---LQVVVVCGKN----EALKQSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 232 VGVEAQ------VAPFIQNMAQAYGWADLVVCRAGALTISELAAAGLPSLLI-PLPhaidDHQSRNADYLAREGAAFVMP 304
Cdd:PRK13609 248 EDLQETnpdalkVFGYVENIDELFRVTSCMITKPGGITLSEAAALGVPVILYkPVP----GQEKENAMYFERKGAAVVIR 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489526708 305 QAttgaAEMAARLKEVLMQPEQLNSMARTARSLAMPDATSTVVNVCVEVAH 355
Cdd:PRK13609 324 DD----EEVFAKTEALLQDDMKLLQMKEAMKSLYLPEPADHIVDDILAENH 370
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
3-344 |
1.48e-06 |
|
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: 49.47 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 3 ANVLIMAGGTGGHVFPALACAREFQARGYKVHWLGTPRGIEnELVPQAGLTLHLI-------NVTGLRGKGRLSLLKAPF 75
Cdd:cd03784 1 MRILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFNFA-DLVEAAGLTFVPVgddpdelELDSETNLGPDSLLELLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 76 MLLKALMQA-----RKVVREVKPVCVVgfGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANR---SLASFASRVCEAFPN 147
Cdd:cd03784 80 RLLKAADELlddllAALRSSWKPDLVI--ADPFAYAGPLVAEELGIPSVRLFTGPATLLSAYlhpFGVLNLLLSSLLEPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 148 TFADSSKRRTTGNPVRVELFLETPRQALAGRKARLLVLGGSL-GAEPLNKLLPEALSQLPQDIQPEVFHQSGKNHDAVTA 226
Cdd:cd03784 158 LFLDPLLEVLDRLRERLGLPPFSLVLLLLRLVPPLYVIGPTFpSLPPDRPRLPSVLGGLRIVPKNGPLPDELWEWLDKQP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 227 ERYR---------NVGVEAQVAPFIQNMAQ-------AYGWAD-----------------------------LVVCRAGA 261
Cdd:cd03784 238 PRSVvyvsfgsmvRDLPEELLELIAEALASlgqrflwVVGPDPlgglerlpdnvlvvkwvpqdellahpavgAFVTHGGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 262 LTISELAAAGLPSLLIPLpHAiDdhQSRNADYLAREGAAFVMPQATTGAAEMAARLKEVLMQPEQLNSMARTARSLAMPD 341
Cdd:cd03784 318 NSTLEALYAGVPMVVVPL-FA-D--QPNNAARVEELGAGVELDKDELTAEELAKAVREVLEDESYRRAAELLAELREEDG 393
|
...
gi 489526708 342 ATS 344
Cdd:cd03784 394 APS 396
|
|
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
237-347 |
1.73e-06 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 49.20 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 237 QVAPFIQNMAQAYGWADLVVCRAGALTISELAAAGLPSLL---IPlphaidDHQSRNADYLAREGA-AFV-MPQATtgAA 311
Cdd:PLN02605 268 KVRGFVTNMEEWMGACDCIITKAGPGTIAEALIRGLPIILngyIP------GQEEGNVPYVVDNGFgAFSeSPKEI--AR 339
|
90 100 110
....*....|....*....|....*....|....*.
gi 489526708 312 EMAARLKEVlmqPEQLNSMARTARSLAMPDATSTVV 347
Cdd:PLN02605 340 IVAEWFGDK---SDELEAMSENALKLARPEAVFDIV 372
|
|
| COG4671 |
COG4671 |
Predicted glycosyl transferase [General function prediction only]; |
140-338 |
2.94e-06 |
|
Predicted glycosyl transferase [General function prediction only];
Pssm-ID: 443708 [Multi-domain] Cd Length: 391 Bit Score: 48.70 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 140 RVCEAFPNTFADSSKRRTTG---NPVRVELFLETPRQALAGRKARLLVL--GGSLGAEPLNKLLpEALSQLPQDIQP--- 211
Cdd:COG4671 174 DLEESFPLPAEIADKVRYTGyvaRPAPEPPPEERDALGLLPEEPLILVSagGGGDGAELLEAAL-AAAELLPPPDHRwll 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 212 -----------EVFHQSGKNHDAVTAERYRNvgveaqvaPFIQNMAQAygwaDLVVCRAGALTISELAAAGLPSLLIPLP 280
Cdd:COG4671 253 vtgpfmpaadrAALRARAAALPNVTVERFTP--------DFEALLAAA----DLSVSMGGYNTVCEILSTGKPALIVPRT 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489526708 281 HaIDDHQSRNADYLAREGAAFVMPQATTGAAEMAARLKEVLMQPE-----QLNSMARTARSLA 338
Cdd:COG4671 321 A-PRTEQLIRAERLAELGLVDVLHPEDLTPEALARAIAAALARPPrrsplDLDGLARTARILA 382
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
8-338 |
1.10e-04 |
|
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
Pssm-ID: 340831 [Multi-domain] Cd Length: 366 Bit Score: 43.68 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 8 MAGGTGGHVFpALAcaREFQARGYKVHWLGTPRGIENELVPQAGLTLHLINVtglrgkgrlslLKAPFMLLKALMQARKV 87
Cdd:cd03801 12 PVGGAERHVR-ELA--RALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPS-----------LAALLRARRLLRELRPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 88 VREVKPVCVVGFGGYVTGPGGLAAKLAGVPLII-------HEQNAVAGTANRSLASFASR---------VCEAFPNTF-- 149
Cdd:cd03801 78 LRLRKFDVVHAHGLLAALLAALLALLLGAPLVVtlhgaepGRLLLLLAAERRLLARAEALlrradaviaVSEALRDELra 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 150 ---ADSSKRRTTGNPVRVELFLETPRQALAGRKARLLVL-GGSLGAEPLNKLLPEALSQLPQDIQPEVFHQSGKNHDAVT 225
Cdd:cd03801 158 lggIPPEKIVVIPNGVDLERFSPPLRRKLGIPPDRPVLLfVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLRA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 226 AERYRNVGVEAQV----APFIQNMAQAYGWADLVVC----RAGALTISELAAAGLPSLLIPLPHAiddhqsrnADYLARE 297
Cdd:cd03801 238 ELEELELGLGDRVrflgFVPDEELPALYAAADVFVLpsryEGFGLVVLEAMAAGLPVVATDVGGL--------PEVVEDG 309
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489526708 298 GAAFVMPqaTTGAAEMAARLKEVLMQPEQLNSMARTARSLA 338
Cdd:cd03801 310 EGGLVVP--PDDVEALADALLRLLADPELRARLGRAARERV 348
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
5-120 |
1.82e-04 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 41.15 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 5 VLIMAGGTGGHVFPalaCAREFQARGYKVHWLGTPRGIENELVPQaGLTLHLINVtglRGKGRLSLLKApfmllkalMQA 84
Cdd:pfam13477 2 ILLLANADSIHTLR---WADALADRGYDVHVISSKGPAKDELIAE-GIHVHRLKV---PRKGPLGYLKA--------FRL 66
|
90 100 110
....*....|....*....|....*....|....*....
gi 489526708 85 RKVVREVKPVCVVGFggYVTGP---GGLAAKLAGVPLII 120
Cdd:pfam13477 67 KKLIKKIKPDVVHVH--YAKPYgllAGLAARLSGFPPVV 103
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
9-121 |
2.22e-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: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 9 AGGTGGHVFPalaCAREFQARGYKVHwLGTPRGIENELVPQA-GLTLHLINVTglrgkgRLSLlkAPFMLLKALMQARKV 87
Cdd:cd03808 9 DGGFQSFRLP---LIKALVKKGYEVH-VIAPDGDKLSDELKElGVKVIDIPIL------RRGI--NPLKDLKALFKLYKL 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 489526708 88 VREVKP---VCVVGFGGYVtgpGGLAAKLAGVPLIIH 121
Cdd:cd03808 77 LKKEKPdivHCHTPKPGIL---GRLAARLAGVPKVIY 110
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
23-141 |
6.99e-03 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 36.61 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526708 23 AREFQARGYKVHWLGTPRGIENELVPQAGLTLHLINVTGLRGkgrlsllkaPFMLLKALMQARKVVREVKPVCVVGFGGY 102
Cdd:pfam13579 11 ARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPVPPRPS---------PLADLAALRRLRRLLRAERPDVVHAHSPT 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 489526708 103 VTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLASFASRV 141
Cdd:pfam13579 82 AGLAARLARRRRGVPLVVTVHGLALDYGSGWKRRLARAL 120
|
|
| |
