|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
4-356 |
2.35e-171 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 480.78 E-value: 2.35e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 4 NVLIMAGGTGGHVFPALACAREFQNRGYTVHWLGTPRGIENELVPNAGLPLHLINVTGLRGKSKLSLLKAPFVLLKAVWQ 83
Cdd:PRK00726 3 KILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 84 ARKVIRELKPVCVLGFGGYVTGPGGVAAKLAGVPVIVHEQNAVAGTANRLLVPLAARVCEAFPKTFGAS--DKLRTTGNP 161
Cdd:PRK00726 83 ARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFfkPKAVVTGNP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 162 VRTELF-MDIAREALQGR--KPHLLVMGGSLGSEPLNKLLPEALAQLPVELRpeVFHQAGKDHGEVTATRYrEAGVEANV 238
Cdd:PRK00726 163 VREEILaLAAPPARLAGRegKPTLLVVGGSQGARVLNEAVPEALALLPEALQ--VIHQTGKGDLEEVRAAY-AAGINAEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 239 QPFIKDMAHAYGWADLVVCRSGALTVSELAAAGLPSLLVPLPHAIDDHQTRNAEYLAGEGAAFLLPQRTTGAADLAARLT 318
Cdd:PRK00726 240 VPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEKLAEKLL 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 1510015361 319 EVLMQPERLNSMASTASRLAKPDATRTVVDICLEVAHG 356
Cdd:PRK00726 320 ELLSDPERLEAMAEAARALGKPDAAERLADLIEELARK 357
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-356 |
1.04e-168 |
|
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: 474.23 E-value: 1.04e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 1 MGANVLIMAGGTGGHVFPALACAREFQNRGYTVHWLGTPRGIENELVPNAGLPLHLINVTGLRGKSKLSLLKAPFVLLKA 80
Cdd:COG0707 1 MSKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 81 VWQARKVIRELKPVCVLGFGGYVTGPGGVAAKLAGVPVIVHEQNAVAGTANRLLVPLAARVCEAFPKT--FGASDKLRTT 158
Cdd:COG0707 81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETkkYFPKKKAVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 159 GNPVRTELFM---DIAREALQGR--KPHLLVMGGSLGSEPLNKLLPEALAQLPvELRPEVFHQAGKDHGEVTATRYREAG 233
Cdd:COG0707 161 GNPVRKEILEldrPEARAKLGLDpdKPTLLVFGGSQGARALNEAVPAALAALL-EARLQVVHQTGKGDYEEVRAAYAAAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 234 V-EANVQPFIKDMAHAYGWADLVVCRSGALTVSELAAAGLPSLLVPLPHAIDDHQTRNAEYLAGEGAAFLLPQRTTGAAD 312
Cdd:COG0707 240 RpNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPEK 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1510015361 313 LAARLTEVLMQPERLNSMASTASRLAKPDATRTVVDICLEVAHG 356
Cdd:COG0707 320 LAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
5-349 |
9.30e-152 |
|
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: 430.87 E-value: 9.30e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 5 VLIMAGGTGGHVFPALACAREFQNRGYTVHWLGTPRGIENELVPNAGLPLHLINVTGLRGKSKLSLLKAPFVLLKAVWQA 84
Cdd:cd03785 2 ILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 85 RKVIRELKPVCVLGFGGYVTGPGGVAAKLAGVPVIVHEQNAVAGTANRLLVPLAARVCEAFPKTFG--ASDKLRTTGNPV 162
Cdd:cd03785 82 RKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKyfPAAKVVVTGNPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 163 RTELFMD---IAREALQGRKPHLLVMGGSLGSEPLNKLLPEALAQLPvELRPEVFHQAGKDHGEVTATRYREAGVEANVQ 239
Cdd:cd03785 162 REEILNLrkeLKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLL-ERGIQVIHQTGKGDYDEVKKLYEDLGINVKVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 240 PFIKDMAHAYGWADLVVCRSGALTVSELAAAGLPSLLVPLPHAIDDHQTRNAEYLAGEGAAFLLPQRTTGAADLAARLTE 319
Cdd:cd03785 241 PFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVLAEAILD 320
|
330 340 350
....*....|....*....|....*....|
gi 1510015361 320 VLMQPERLNSMASTASRLAKPDATRTVVDI 349
Cdd:cd03785 321 LLNDPERLKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
5-350 |
4.61e-137 |
|
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: 393.58 E-value: 4.61e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 5 VLIMAGGTGGHVFPALACAREFQNRGYTVHWLGTPRGIENELVPNAGLPLHLINVTGLRGKSKLSLLKAPFVLLKAVWQA 84
Cdd:TIGR01133 3 IALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVFKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 85 RKVIRELKPVCVLGFGGYVTGPGGVAAKLAGVPVIVHEQNAVAGTANRLLVPLAARVCEAFPKTFGASdKLRTTGNPVRT 164
Cdd:TIGR01133 83 RRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDHF-EAVLVGNPVRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 165 ELF-MDIAREALQGR--KPHLLVMGGSLGSEPLNKLLPEALAQLPVELRPeVFHQAGKDHGEVTATRYREAGVEANVQPF 241
Cdd:TIGR01133 162 EIRsLPVPRERFGRRegKPTILVLGGSQGAKILNELVPKALAKLQEKGIQ-IVHQGGKGDLEKVKNVYQELGQEKIVTFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 242 IKDMAHAYGWADLVVCRSGALTVSELAAAGLPSLLVPLPHAiDDHQTRNAEYLAGEGAAFLLPQRTTGAADLAARLTEVL 321
Cdd:TIGR01133 241 DENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPEKLLEALLKLL 319
|
330 340
....*....|....*....|....*....
gi 1510015361 322 MQPERLNSMASTASRLAKPDATRTVVDIC 350
Cdd:TIGR01133 320 LDPANLENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
5-141 |
1.30e-46 |
|
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: 155.14 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 5 VLIMAGGTGGHVFPALACAREFQNRGYTVHWLGTPRGIENELVPNAGLPLHLINVTGLRGKSKLSLLKAPFVLLKAVWQA 84
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1510015361 85 RKVIRELKPVCVLGFGGYVTGPGGVAAKLAGVPVIVHEQNAVAGTANRLLVPLAARV 141
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
4-356 |
2.35e-171 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 480.78 E-value: 2.35e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 4 NVLIMAGGTGGHVFPALACAREFQNRGYTVHWLGTPRGIENELVPNAGLPLHLINVTGLRGKSKLSLLKAPFVLLKAVWQ 83
Cdd:PRK00726 3 KILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 84 ARKVIRELKPVCVLGFGGYVTGPGGVAAKLAGVPVIVHEQNAVAGTANRLLVPLAARVCEAFPKTFGAS--DKLRTTGNP 161
Cdd:PRK00726 83 ARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFfkPKAVVTGNP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 162 VRTELF-MDIAREALQGR--KPHLLVMGGSLGSEPLNKLLPEALAQLPVELRpeVFHQAGKDHGEVTATRYrEAGVEANV 238
Cdd:PRK00726 163 VREEILaLAAPPARLAGRegKPTLLVVGGSQGARVLNEAVPEALALLPEALQ--VIHQTGKGDLEEVRAAY-AAGINAEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 239 QPFIKDMAHAYGWADLVVCRSGALTVSELAAAGLPSLLVPLPHAIDDHQTRNAEYLAGEGAAFLLPQRTTGAADLAARLT 318
Cdd:PRK00726 240 VPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEKLAEKLL 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 1510015361 319 EVLMQPERLNSMASTASRLAKPDATRTVVDICLEVAHG 356
Cdd:PRK00726 320 ELLSDPERLEAMAEAARALGKPDAAERLADLIEELARK 357
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-356 |
1.04e-168 |
|
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: 474.23 E-value: 1.04e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 1 MGANVLIMAGGTGGHVFPALACAREFQNRGYTVHWLGTPRGIENELVPNAGLPLHLINVTGLRGKSKLSLLKAPFVLLKA 80
Cdd:COG0707 1 MSKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 81 VWQARKVIRELKPVCVLGFGGYVTGPGGVAAKLAGVPVIVHEQNAVAGTANRLLVPLAARVCEAFPKT--FGASDKLRTT 158
Cdd:COG0707 81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETkkYFPKKKAVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 159 GNPVRTELFM---DIAREALQGR--KPHLLVMGGSLGSEPLNKLLPEALAQLPvELRPEVFHQAGKDHGEVTATRYREAG 233
Cdd:COG0707 161 GNPVRKEILEldrPEARAKLGLDpdKPTLLVFGGSQGARALNEAVPAALAALL-EARLQVVHQTGKGDYEEVRAAYAAAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 234 V-EANVQPFIKDMAHAYGWADLVVCRSGALTVSELAAAGLPSLLVPLPHAIDDHQTRNAEYLAGEGAAFLLPQRTTGAAD 312
Cdd:COG0707 240 RpNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPEK 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1510015361 313 LAARLTEVLMQPERLNSMASTASRLAKPDATRTVVDICLEVAHG 356
Cdd:COG0707 320 LAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
5-349 |
9.30e-152 |
|
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: 430.87 E-value: 9.30e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 5 VLIMAGGTGGHVFPALACAREFQNRGYTVHWLGTPRGIENELVPNAGLPLHLINVTGLRGKSKLSLLKAPFVLLKAVWQA 84
Cdd:cd03785 2 ILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 85 RKVIRELKPVCVLGFGGYVTGPGGVAAKLAGVPVIVHEQNAVAGTANRLLVPLAARVCEAFPKTFG--ASDKLRTTGNPV 162
Cdd:cd03785 82 RKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKyfPAAKVVVTGNPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 163 RTELFMD---IAREALQGRKPHLLVMGGSLGSEPLNKLLPEALAQLPvELRPEVFHQAGKDHGEVTATRYREAGVEANVQ 239
Cdd:cd03785 162 REEILNLrkeLKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLL-ERGIQVIHQTGKGDYDEVKKLYEDLGINVKVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 240 PFIKDMAHAYGWADLVVCRSGALTVSELAAAGLPSLLVPLPHAIDDHQTRNAEYLAGEGAAFLLPQRTTGAADLAARLTE 319
Cdd:cd03785 241 PFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVLAEAILD 320
|
330 340 350
....*....|....*....|....*....|
gi 1510015361 320 VLMQPERLNSMASTASRLAKPDATRTVVDI 349
Cdd:cd03785 321 LLNDPERLKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
5-350 |
4.61e-137 |
|
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: 393.58 E-value: 4.61e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 5 VLIMAGGTGGHVFPALACAREFQNRGYTVHWLGTPRGIENELVPNAGLPLHLINVTGLRGKSKLSLLKAPFVLLKAVWQA 84
Cdd:TIGR01133 3 IALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVFKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 85 RKVIRELKPVCVLGFGGYVTGPGGVAAKLAGVPVIVHEQNAVAGTANRLLVPLAARVCEAFPKTFGASdKLRTTGNPVRT 164
Cdd:TIGR01133 83 RRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDHF-EAVLVGNPVRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 165 ELF-MDIAREALQGR--KPHLLVMGGSLGSEPLNKLLPEALAQLPVELRPeVFHQAGKDHGEVTATRYREAGVEANVQPF 241
Cdd:TIGR01133 162 EIRsLPVPRERFGRRegKPTILVLGGSQGAKILNELVPKALAKLQEKGIQ-IVHQGGKGDLEKVKNVYQELGQEKIVTFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 242 IKDMAHAYGWADLVVCRSGALTVSELAAAGLPSLLVPLPHAiDDHQTRNAEYLAGEGAAFLLPQRTTGAADLAARLTEVL 321
Cdd:TIGR01133 241 DENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPEKLLEALLKLL 319
|
330 340
....*....|....*....|....*....
gi 1510015361 322 MQPERLNSMASTASRLAKPDATRTVVDIC 350
Cdd:TIGR01133 320 LDPANLENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
5-141 |
1.30e-46 |
|
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: 155.14 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 5 VLIMAGGTGGHVFPALACAREFQNRGYTVHWLGTPRGIENELVPNAGLPLHLINVTGLRGKSKLSLLKAPFVLLKAVWQA 84
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1510015361 85 RKVIRELKPVCVLGFGGYVTGPGGVAAKLAGVPVIVHEQNAVAGTANRLLVPLAARV 141
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
|
|
| PRK12446 |
PRK12446 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
5-308 |
8.70e-44 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
Pssm-ID: 171505 [Multi-domain] Cd Length: 352 Bit Score: 154.63 E-value: 8.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 5 VLIMAGGTGGHVFPALACAREFQNRGYTVHWLGTPRGIENELVPNAGLPLHLINVTGLRGKSKLSLLKAPFVLLKAVWQA 84
Cdd:PRK12446 4 IVFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGVMDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 85 RKVIRELKPVCVLGFGGYVTGPGGVAAKLAGVPVIVHEQNAVAGTANRLLVPLAARVCEAFPKTFG--ASDKLRTTGNPV 162
Cdd:PRK12446 84 YVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAAKhlPKEKVIYTGSPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 163 RTELFMDIAREAL-----QGRKPHLLVMGGSLGSEPLNKLLPEALAQLpvELRPEVFHQAGKdhGEVTATRyreAGVEAN 237
Cdd:PRK12446 164 REEVLKGNREKGLaflgfSRKKPVITIMGGSLGAKKINETVREALPEL--LLKYQIVHLCGK--GNLDDSL---QNKEGY 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1510015361 238 VQ-PFIKD-MAHAYGWADLVVCRSGALTVSELAAAGLPSLLVPLPH-AIDDHQTRNAEYLAGEG-AAFLLPQRTT 308
Cdd:PRK12446 237 RQfEYVHGeLPDILAITDFVISRAGSNAIFEFLTLQKPMLLIPLSKfASRGDQILNAESFERQGyASVLYEEDVT 311
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
181-342 |
3.80e-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: 3.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 181 HLLVMGGSLGSEPLNKLLPEALAQLPVELRPEVFHQAGKDHGEVTATRYREAGVEANVQPFIKDMAHAYGWADLVVCRSG 260
Cdd:pfam04101 1 TILVTGGSQGARALNELVLSVLPLLELKGELQVLHQTGKGDLEEVKIDYAELGINYEVFPFIDNMAEYIKAADLVISRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 261 ALTVSELAAAGLPSLLVPLPHAIDDHQTRNAEYLAGEGAAFLLPQRTTGAADLAARLTEVLMQPERLNSMASTASRLAKP 340
Cdd:pfam04101 81 AGTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALLKLLLNPLRLAEMAKASKASGFK 160
|
..
gi 1510015361 341 DA 342
Cdd:pfam04101 161 DA 162
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
4-339 |
2.54e-17 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 80.67 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 4 NVLIMAGGTGGHVFPALACAREFQNRGYTVHWLGTPRGIEneLVPNAGLPLHlinvtglrgksklsllkapfvllkavwq 83
Cdd:COG1819 1 RILFVTLGGRGHVNPLLALARALRARGHEVTFATGPDFAD--LVEAAGLEFV---------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 84 arkvirELKPVCVLGfgGYVTGPGGVAAKLAGVPVIVHeqnavagtanrllvplaarvceaFPKTFGA-----SDKLRTT 158
Cdd:COG1819 51 ------DWRPDLVVS--DPLALAAALAAEALGIPVVSL-----------------------TPPELEYprppdPANVRFV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 159 GNPVRTELFMDIAREALQGRKPHLLVMGGSL--GSEPLNKLLPEALAQLPVELrpeVFHQAGKDHGEVTAtryreagVEA 236
Cdd:COG1819 100 GPLLPDGPAELPPWLEEDAGRPLVYVTLGTSanDRADLLRAVLEALADLGVRV---VVTTGGLDPAELGP-------LPD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 237 NVQ-----PFIKDMAHAygwaDLVVCRSGALTVSELAAAGLPSLLVplPHAIDdhQTRNAEYLAGEGAAFLLPQRTTGAA 311
Cdd:COG1819 170 NVRvvdyvPQDALLPRA----DAVVHHGGAGTTAEALRAGVPQVVV--PFGGD--QPLNAARVERLGAGLALPPRRLTAE 241
|
330 340
....*....|....*....|....*...
gi 1510015361 312 DLAARLTEVLMQPerlnSMASTASRLAK 339
Cdd:COG1819 242 ALRAALRRLLADP----SYRERAARLAA 265
|
|
| SpsG |
COG3980 |
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall ... |
14-354 |
1.86e-16 |
|
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443179 [Multi-domain] Cd Length: 342 Bit Score: 79.20 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 14 GHVFPALACAREFQNRGYTVHWLGTPRGIE-NELVPNAGLPLHLINVTGLRG-----KSKLSLLKAPFVL-----LKAVW 82
Cdd:COG3980 16 GHVMRCLALAEALRERGAEVTFLCRDDSGSlIELLKERGFPVILLPAPSWEDdaeelLELLKDLQPDWLVvdhyaLDAEY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 83 QarKVIREL-KPVCV---LGFGGYvtgpggvaakLAGVpVIVheQNAVAGTANRLLVPLAARVC---EAFPktfgasdkL 155
Cdd:COG3980 96 E--KALKALgKKLVViddLGDRAH----------PADL-VIN--QNLGASAEDYRGVPPGTKLLlgpEYAL--------L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 156 RttgnpvrtELFMDIAREA--LQGRKPHLLV-MGGSlgsEPLN---KLLpEALAQLPVELRPEVFHQAGKDHGEVTATRY 229
Cdd:COG3980 153 R--------PEFLALRPASrrISEEVRRILVtFGGS---DPDNltlKVL-RALLQLDPDLKITVVVGPGYPHLDELRALA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 230 REAGVEANVQPFIKDMAHAYGWADLVVCRSGAlTVSELAAAGLPSLLVplphAIDDHQTRNAEYLAGEGAAFLL-PQRTT 308
Cdd:COG3980 221 AERPLNIELHRNVKDMAELMAQADLAISAAGT-TTYELAALGLPTIVV----AVADNQRAIAEALEENGAAINLgLGEEL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1510015361 309 GAADLAARLTEVLMQPERLNSMASTASRLAKPDATRTVVDICLEVA 354
Cdd:COG3980 296 TDEELANALDELLLDPERRARMSRKARSLVDGRGAERIVEAILELL 341
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
153-355 |
6.61e-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: 68.88 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 153 DKLRTTGNPVRTELFMDIAREALQGR------KPHLLVMGGSLGSEPLNKLLpEALAQLPVELRPEVFhqAGKDHGEVTA 226
Cdd:cd17507 165 SQIKVTGIPVRPSFAEVRDKDEARNElnlspdKPTVLLMGGGGGMGPVKETV-EALLDSLRAGQVLVV--CGKNKKLYEK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 227 TRYREA-GVEANVQPFIKDMAHAYGWADLVVCRSGALTVSELAAAGLPSLLVPlphAIDDHQTRNAEYLAGEGAAFLLPQ 305
Cdd:cd17507 242 LSGLEEdYINVRVLGYVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYD---PIPGQEEENADFLENNGAGIIARD 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1510015361 306 RTTgAADLAARLTEvlmQPERLNSMASTASRLAKPDATRTVVDICLEVAH 355
Cdd:cd17507 319 PEE-LLEIVARLID---PPSLLRMMSEAAKELKPPAAAKVIADILSLLID 364
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
153-355 |
7.15e-13 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 68.98 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 153 DKLRTTGNPVRTELFMDIAREALQGR------KPHLLVMGGSLGSEPLNKLLPEALAQLPvELrpEVFHQAGKDHG--EV 224
Cdd:PRK13609 170 EQVVETGIPIRSSFELKINPDIIYNKyqlcpnKKILLIMAGAHGVLGNVKELCQSLMSVP-DL--QVVVVCGKNEAlkQS 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 225 TATRYREAGVEANVQPFIKDMAHAYGWADLVVCRSGALTVSELAAAGLPSLLV-PLPhaidDHQTRNAEYLAGEGAAFLL 303
Cdd:PRK13609 247 LEDLQETNPDALKVFGYVENIDELFRVTSCMITKPGGITLSEAAALGVPVILYkPVP----GQEKENAMYFERKGAAVVI 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1510015361 304 PQRttgaADLAARLTEVLMQPERLNSMASTASRLAKPDATRTVVDICLEVAH 355
Cdd:PRK13609 323 RDD----EEVFAKTEALLQDDMKLLQMKEAMKSLYLPEPADHIVDDILAENH 370
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
3-331 |
3.17e-08 |
|
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: 54.86 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 3 ANVLIMAGGTGGHVFPALACAREFQNRGYTVHWLGTPRGIEnELVPNAGLPLHLINVTGLRGKSKLSLLKAPFVLLKAVW 82
Cdd:cd03784 1 MRILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFNFA-DLVEAAGLTFVPVGDDPDELELDSETNLGPDSLLELLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 83 QARKVIREL------------KPVCVLgfGGYVTGPGGVAAKLAGVPVIVH------------------EQNAVAGTANR 132
Cdd:cd03784 80 RLLKAADELlddllaalrsswKPDLVI--ADPFAYAGPLVAEELGIPSVRLftgpatllsaylhpfgvlNLLLSSLLEPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 133 LLVPLAARVCEAFPKTFGAS--DKLRTTGNPVRTELFMDIAREALQGRKPHLLVMGGSLGSEPLNKLLPEALAQLPVELR 210
Cdd:cd03784 158 LFLDPLLEVLDRLRERLGLPpfSLVLLLLRLVPPLYVIGPTFPSLPPDRPRLPSVLGGLRIVPKNGPLPDELWEWLDKQP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 211 PE---------VFHQAGKDHGEVTAtryreAGVEANVQPFI--------------KDMAHAYGWA-----------DLVV 256
Cdd:cd03784 238 PRsvvyvsfgsMVRDLPEELLELIA-----EALASLGQRFLwvvgpdplgglerlPDNVLVVKWVpqdellahpavGAFV 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1510015361 257 CRSGALTVSELAAAGLPSLLVPLpHAiDdhQTRNAEYLAGEGAAFLLPQRTTGAADLAARLTEVLMQPERLNSMA 331
Cdd:cd03784 313 THGGWNSTLEALYAGVPMVVVPL-FA-D--QPNNAARVEELGAGVELDKDELTAEELAKAVREVLEDESYRRAAE 383
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
8-339 |
5.60e-08 |
|
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: 54.08 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 8 MAGGTGGHVFpALAcaREFQNRGYTVHWLGTPRGienelvpnaglPLHLINVTGLRGKSKLSLLKAPFVLLKAVWQARKV 87
Cdd:cd03801 12 PVGGAERHVR-ELA--RALAARGHDVTVLTPADP-----------GEPPEELEDGVIVPLLPSLAALLRARRLLRELRPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 88 IRELKPVCVLGFGGYVTGPGGVAAKLAGVPVIVHEQNAVAGTANRLLVPLAARVCEAFPKTFGAS----------DKLRT 157
Cdd:cd03801 78 LRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLARAEALLRRADaviavsealrDELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 158 TG-----------NPVRTELFMDIAREALQGRKPH-LLVMGGSLGSEPLNKLLPEALAQLPVELRPEVFHQAGKDHGEVT 225
Cdd:cd03801 158 LGgippekivvipNGVDLERFSPPLRRKLGIPPDRpVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLRA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 226 ATRYREAGVEANVQ----PFIKDMAHAYGWADLVVCRS----GALTVSELAAAGLPSLLVPLPHAiddhqtrnAEYLAGE 297
Cdd:cd03801 238 ELEELELGLGDRVRflgfVPDEELPALYAAADVFVLPSryegFGLVVLEAMAAGLPVVATDVGGL--------PEVVEDG 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1510015361 298 GAAFLLPqrTTGAADLAARLTEVLMQPERLNSMASTASRLAK 339
Cdd:cd03801 310 EGGLVVP--PDDVEALADALLRLLADPELRARLGRAARERVA 349
|
|
| COG4671 |
COG4671 |
Predicted glycosyl transferase [General function prediction only]; |
140-338 |
3.81e-07 |
|
Predicted glycosyl transferase [General function prediction only];
Pssm-ID: 443708 [Multi-domain] Cd Length: 391 Bit Score: 51.39 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 140 RVCEAFPKTFGASDKLRTTG---NPVRTELFMDIAREALQGRKPHLLVM--GGSLGSEPLNKLLpEALAQLPVELRP--- 211
Cdd:COG4671 174 DLEESFPLPAEIADKVRYTGyvaRPAPEPPPEERDALGLLPEEPLILVSagGGGDGAELLEAAL-AAAELLPPPDHRwll 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 212 -----------EVFHQAGKDHGEVTatryreagveanVQPFIKDMAHAYGWADLVVCRSGALTVSELAAAGLPSLLVPLP 280
Cdd:COG4671 253 vtgpfmpaadrAALRARAAALPNVT------------VERFTPDFEALLAAADLSVSMGGYNTVCEILSTGKPALIVPRT 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1510015361 281 HaIDDHQTRNAEYLAGEGAAFLLPQRTTGAADLAARLTEVLMQPER-----LNSMASTASRLA 338
Cdd:COG4671 321 A-PRTEQLIRAERLAELGLVDVLHPEDLTPEALARAIAAALARPPRrspldLDGLARTARILA 382
|
|
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
162-348 |
7.06e-05 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 44.19 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 162 VRTELFMDIARealqgrkPHLLVMGGSLGSEPLNKLLpEALAQ-LPVELRPEVFHQ----AGKDHGEVTATRYREAGVEA 236
Cdd:PLN02605 196 LRRELGMDEDL-------PAVLLMGGGEGMGPLEETA-RALGDsLYDKNLGKPIGQvvviCGRNKKLQSKLESRDWKIPV 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 237 NVQPFIKDMAHAYGWADLVVCRSGALTVSELAAAGLPSLL---VPlphaidDHQTRNAEYL--AGEGAAFLLPQRTtgAA 311
Cdd:PLN02605 268 KVRGFVTNMEEWMGACDCIITKAGPGTIAEALIRGLPIILngyIP------GQEEGNVPYVvdNGFGAFSESPKEI--AR 339
|
170 180 190
....*....|....*....|....*....|....*..
gi 1510015361 312 DLAARLTEVlmqPERLNSMASTASRLAKPDATRTVVD 348
Cdd:PLN02605 340 IVAEWFGDK---SDELEAMSENALKLARPEAVFDIVH 373
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
9-121 |
7.65e-05 |
|
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: 44.12 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 9 AGGTGGHVFPalaCAREFQNRGYTVHWLGTPRGIENELVPNAGLPLHLINVTGlRGKSklsllkaPFVLLKAVWQARKVI 88
Cdd:cd03808 9 DGGFQSFRLP---LIKALVKKGYEVHVIAPDGDKLSDELKELGVKVIDIPILR-RGIN-------PLKDLKALFKLYKLL 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 1510015361 89 RELKPVCVLGF---GGYVtgpGGVAAKLAGVPVIVH 121
Cdd:cd03808 78 KKEKPDIVHCHtpkPGIL---GRLAARLAGVPKVIY 110
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
5-120 |
6.70e-04 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 39.61 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 5 VLIMAGGTGGHVFPalaCAREFQNRGYTVHWLGTPRGIENELVPNaGLPLHLINVtglRGKSKLSLLKApfvllkavWQA 84
Cdd:pfam13477 2 ILLLANADSIHTLR---WADALADRGYDVHVISSKGPAKDELIAE-GIHVHRLKV---PRKGPLGYLKA--------FRL 66
|
90 100 110
....*....|....*....|....*....|....*....
gi 1510015361 85 RKVIRELKPVCVLGFggYVTGP---GGVAAKLAGVPVIV 120
Cdd:pfam13477 67 KKLIKKIKPDVVHVH--YAKPYgllAGLAARLSGFPPVV 103
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
23-141 |
2.75e-03 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 38.15 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 23 AREFQNRGYTVHWLGTPRGIENELVPNAGLPLHLINVTGLRGksklsllkaPFVLLKAVWQARKVIRELKPVCVLGFGGY 102
Cdd:pfam13579 11 ARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPVPPRPS---------PLADLAALRRLRRLLRAERPDVVHAHSPT 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 1510015361 103 VTGPGGVAAKLAGVPVIVHEQNAVAGTANRLLVPLAARV 141
Cdd:pfam13579 82 AGLAARLARRRRGVPLVVTVHGLALDYGSGWKRRLARAL 120
|
|
| PRK13608 |
PRK13608 |
diacylglycerol glucosyltransferase; Provisional |
153-346 |
4.23e-03 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 184179 [Multi-domain] Cd Length: 391 Bit Score: 38.62 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 153 DKLRTTGNPVRTELFMDIAREA------LQGRKPHLLVMGGSLG-SEPLNKLLPEALAQLPvelRPEVFHQAGKDHG--E 223
Cdd:PRK13608 170 STVKVTGIPIDNKFETPIDQKQwlidnnLDPDKQTILMSAGAFGvSKGFDTMITDILAKSA---NAQVVMICGKSKElkR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510015361 224 VTATRYREagvEANVQ--PFIKDMAHAYGWADLVVCRSGALTVSELAAAGLPSL-LVPLPhaidDHQTRNAEYLAGEGAA 300
Cdd:PRK13608 247 SLTAKFKS---NENVLilGYTKHMNEWMASSQLMITKPGGITISEGLARCIPMIfLNPAP----GQELENALYFEEKGFG 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1510015361 301 fLLPQRTTGAADLAARLTEvlmQPERLNSMASTASRLAKPDATRTV 346
Cdd:PRK13608 320 -KIADTPEEAIKIVASLTN---GNEQLTNMISTMEQDKIKYATQTI 361
|
|
| |
