|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
4-356 |
3.64e-167 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 470.38 E-value: 3.64e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 4 NVLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQ 83
Cdd:PRK00726 3 KILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 84 ARRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNSAKRRT--TGNP 161
Cdd:PRK00726 83 ARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAvvTGNP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 162 VRHELF-LETPRQTLLGR--RPRLLVLGGSLGAEPLNKLLPEALGQLSEELRpeIFHQAGKQHAEITRERYvAAGVEAEV 238
Cdd:PRK00726 163 VREEILaLAAPPARLAGRegKPTLLVVGGSQGARVLNEAVPEALALLPEALQ--VIHQTGKGDLEEVRAAY-AAGINAEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 239 APFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLT 318
Cdd:PRK00726 240 VPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEKLAEKLL 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 518172457 319 EVMMQPEKLKAMGATARRLARPDATRTVVDICLEVAHG 356
Cdd:PRK00726 320 ELLSDPERLEAMAEAARALGKPDAAERLADLIEELARK 357
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-356 |
8.23e-163 |
|
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440471 [Multi-domain] Cd Length: 363 Bit Score: 459.59 E-value: 8.23e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 1 MGGNVLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRS 80
Cdd:COG0707 1 MSKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 81 LGQARRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNT--FSNSAKRRTT 158
Cdd:COG0707 81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETkkYFPKKKAVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 159 GNPVRHElFLETPRQTLLGR------RPRLLVLGGSLGAEPLNKLLPEALGQLSEElRPEIFHQAGKQHAEITRERYVAA 232
Cdd:COG0707 161 GNPVRKE-ILELDRPEARAKlgldpdKPTLLVFGGSQGARALNEAVPAALAALLEA-RLQVVHQTGKGDYEEVRAAYAAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 233 GV-EAEVAPFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAA 311
Cdd:COG0707 239 IRpNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 518172457 312 ALAAQLTEVMMQPEKLKAMGATARRLARPDATRTVVDICLEVAHG 356
Cdd:COG0707 319 KLAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
5-349 |
6.20e-146 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340818 [Multi-domain] Cd Length: 350 Bit Score: 416.23 E-value: 6.20e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:cd03785 2 ILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNSAKRRT--TGNPV 162
Cdd:cd03785 82 RKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVvvTGNPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 163 RHELFLETPRQTLLGR---RPRLLVLGGSLGAEPLNKLLPEALGQLSEElRPEIFHQAGKQHAEITRERYVAAGVEAEVA 239
Cdd:cd03785 162 REEILNLRKELKRFGLppdKPTLLVFGGSQGARAINRAVPKALPKLLER-GIQVIHQTGKGDYDEVKKLYEDLGINVKVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 240 PFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLTE 319
Cdd:cd03785 241 PFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVLAEAILD 320
|
330 340 350
....*....|....*....|....*....|
gi 518172457 320 VMMQPEKLKAMGATARRLARPDATRTVVDI 349
Cdd:cd03785 321 LLNDPERLKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
5-350 |
7.14e-136 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. RA Bupp K, van Heijenoort J. RL J Bacteriol 1993 Mar;175(6):1841-3 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273460 [Multi-domain] Cd Length: 348 Bit Score: 390.50 E-value: 7.14e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:TIGR01133 3 IALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVFKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNsAKRRTTGNPVRH 164
Cdd:TIGR01133 83 RRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDH-FEAVLVGNPVRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 165 ELFLETPRQTLLGRR---PRLLVLGGSLGAEPLNKLLPEALGQLSEELRPeIFHQAGKQHAEITRERYVAAGVEAEVAPF 241
Cdd:TIGR01133 162 EIRSLPVPRERFGRRegkPTILVLGGSQGAKILNELVPKALAKLQEKGIQ-IVHQGGKGDLEKVKNVYQELGQEKIVTFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 242 IKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAiDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLTEVM 321
Cdd:TIGR01133 241 DENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPEKLLEALLKLL 319
|
330 340
....*....|....*....|....*....
gi 518172457 322 MQPEKLKAMGATARRLARPDATRTVVDIC 350
Cdd:TIGR01133 320 LDPANLENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
5-141 |
1.26e-45 |
|
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.
Pssm-ID: 427107 [Multi-domain] Cd Length: 139 Bit Score: 152.44 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 518172457 85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRV 141
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
4-356 |
3.64e-167 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 470.38 E-value: 3.64e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 4 NVLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQ 83
Cdd:PRK00726 3 KILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 84 ARRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNSAKRRT--TGNP 161
Cdd:PRK00726 83 ARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAvvTGNP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 162 VRHELF-LETPRQTLLGR--RPRLLVLGGSLGAEPLNKLLPEALGQLSEELRpeIFHQAGKQHAEITRERYvAAGVEAEV 238
Cdd:PRK00726 163 VREEILaLAAPPARLAGRegKPTLLVVGGSQGARVLNEAVPEALALLPEALQ--VIHQTGKGDLEEVRAAY-AAGINAEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 239 APFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLT 318
Cdd:PRK00726 240 VPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEKLAEKLL 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 518172457 319 EVMMQPEKLKAMGATARRLARPDATRTVVDICLEVAHG 356
Cdd:PRK00726 320 ELLSDPERLEAMAEAARALGKPDAAERLADLIEELARK 357
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-356 |
8.23e-163 |
|
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440471 [Multi-domain] Cd Length: 363 Bit Score: 459.59 E-value: 8.23e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 1 MGGNVLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRS 80
Cdd:COG0707 1 MSKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 81 LGQARRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNT--FSNSAKRRTT 158
Cdd:COG0707 81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETkkYFPKKKAVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 159 GNPVRHElFLETPRQTLLGR------RPRLLVLGGSLGAEPLNKLLPEALGQLSEElRPEIFHQAGKQHAEITRERYVAA 232
Cdd:COG0707 161 GNPVRKE-ILELDRPEARAKlgldpdKPTLLVFGGSQGARALNEAVPAALAALLEA-RLQVVHQTGKGDYEEVRAAYAAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 233 GV-EAEVAPFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAA 311
Cdd:COG0707 239 IRpNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 518172457 312 ALAAQLTEVMMQPEKLKAMGATARRLARPDATRTVVDICLEVAHG 356
Cdd:COG0707 319 KLAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
5-349 |
6.20e-146 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340818 [Multi-domain] Cd Length: 350 Bit Score: 416.23 E-value: 6.20e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:cd03785 2 ILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNSAKRRT--TGNPV 162
Cdd:cd03785 82 RKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVvvTGNPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 163 RHELFLETPRQTLLGR---RPRLLVLGGSLGAEPLNKLLPEALGQLSEElRPEIFHQAGKQHAEITRERYVAAGVEAEVA 239
Cdd:cd03785 162 REEILNLRKELKRFGLppdKPTLLVFGGSQGARAINRAVPKALPKLLER-GIQVIHQTGKGDYDEVKKLYEDLGINVKVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 240 PFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLTE 319
Cdd:cd03785 241 PFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVLAEAILD 320
|
330 340 350
....*....|....*....|....*....|
gi 518172457 320 VMMQPEKLKAMGATARRLARPDATRTVVDI 349
Cdd:cd03785 321 LLNDPERLKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
5-350 |
7.14e-136 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. RA Bupp K, van Heijenoort J. RL J Bacteriol 1993 Mar;175(6):1841-3 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273460 [Multi-domain] Cd Length: 348 Bit Score: 390.50 E-value: 7.14e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:TIGR01133 3 IALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVFKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNsAKRRTTGNPVRH 164
Cdd:TIGR01133 83 RRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDH-FEAVLVGNPVRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 165 ELFLETPRQTLLGRR---PRLLVLGGSLGAEPLNKLLPEALGQLSEELRPeIFHQAGKQHAEITRERYVAAGVEAEVAPF 241
Cdd:TIGR01133 162 EIRSLPVPRERFGRRegkPTILVLGGSQGAKILNELVPKALAKLQEKGIQ-IVHQGGKGDLEKVKNVYQELGQEKIVTFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 242 IKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHAiDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLTEVM 321
Cdd:TIGR01133 241 DENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPEKLLEALLKLL 319
|
330 340
....*....|....*....|....*....
gi 518172457 322 MQPEKLKAMGATARRLARPDATRTVVDIC 350
Cdd:TIGR01133 320 LDPANLENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
5-141 |
1.26e-45 |
|
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.
Pssm-ID: 427107 [Multi-domain] Cd Length: 139 Bit Score: 152.44 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 518172457 85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRV 141
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
|
|
| PRK12446 |
PRK12446 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
5-303 |
4.42e-40 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
Pssm-ID: 171505 [Multi-domain] Cd Length: 352 Bit Score: 144.62 E-value: 4.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 5 VLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRGKGVGSLLKAPFQLLRSLGQA 84
Cdd:PRK12446 4 IVFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGVMDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 85 RRIMRELQPVCVLGLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANRSLVPFAQRVCEAFPNTFSNSAKRRT--TGNPV 162
Cdd:PRK12446 84 YVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAAKHLPKEKViyTGSPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 163 RHEL----------FLETPRqtllgRRPRLLVLGGSLGAEPLNKLLPEALGQLSeeLRPEIFHQAGKQHAEIT---RERY 229
Cdd:PRK12446 164 REEVlkgnrekglaFLGFSR-----KKPVITIMGGSLGAKKINETVREALPELL--LKYQIVHLCGKGNLDDSlqnKEGY 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518172457 230 VAAGVEAEVAPFIKDMarayawADLVICRAGALTVCELAAAGLPSFLVPLPH-AIDDHQTRNAEYLAKEGAAILL 303
Cdd:PRK12446 237 RQFEYVHGELPDILAI------TDFVISRAGSNAIFEFLTLQKPMLLIPLSKfASRGDQILNAESFERQGYASVL 305
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
182-342 |
4.69e-38 |
|
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.
Pssm-ID: 427711 [Multi-domain] Cd Length: 166 Bit Score: 133.99 E-value: 4.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 182 LLVLGGSLGAEPLNKLLPEALGQLSEELRPEIFHQAGKQHAEITRERYVAAGVEAEVAPFIKDMARAYAWADLVICRAGA 261
Cdd:pfam04101 2 ILVTGGSQGARALNELVLSVLPLLELKGELQVLHQTGKGDLEEVKIDYAELGINYEVFPFIDNMAEYIKAADLVISRAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 262 LTVCELAAAGLPSFLVPLPHAIDDHQTRNAEYLAKEGAAILLPQATTDAAALAAQLTEVMMQPEKLKAMGATARRLARPD 341
Cdd:pfam04101 82 GTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALLKLLLNPLRLAEMAKASKASGFKD 161
|
.
gi 518172457 342 A 342
Cdd:pfam04101 162 A 162
|
|
| SpsG |
COG3980 |
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall ... |
161-354 |
1.31e-16 |
|
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443179 [Multi-domain] Cd Length: 342 Bit Score: 79.58 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 161 PVRHElFLETPRQ--TLLGRRPRLLV-LGGSlgaEPLN---KLLpEALGQLSEELRPEIFHQAGKQHAEITRERYVAAGV 234
Cdd:COG3980 151 LLRPE-FLALRPAsrRISEEVRRILVtFGGS---DPDNltlKVL-RALLQLDPDLKITVVVGPGYPHLDELRALAAERPL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 235 EAEVAPFIKDMARAYAWADLVICRAGAlTVCELAAAGLPSFLVplphAIDDHQTRNAEYLAKEGAAILL-PQATTDAAAL 313
Cdd:COG3980 226 NIELHRNVKDMAELMAQADLAISAAGT-TTYELAALGLPTIVV----AVADNQRAIAEALEENGAAINLgLGEELTDEEL 300
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518172457 314 AAQLTEVMMQPEKLKAMGATARRLARPDATRTVVDICLEVA 354
Cdd:COG3980 301 ANALDELLLDPERRARMSRKARSLVDGRGAERIVEAILELL 341
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
4-304 |
7.94e-13 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 67.57 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 4 NVLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIEneVVPAAGLPLHliqvsglrgkgvgsllkapfqllrslgq 83
Cdd:COG1819 1 RILFVTLGGRGHVNPLLALARALRARGHEVTFATGPDFAD--LVEAAGLEFV---------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 84 arrimrELQPVCVLGlgGYVTGPGGLAAKLAGVPLIiheqnavagtanrSLVPfaqrvcEAF-PNTFSNSAKRRTTGNPV 162
Cdd:COG1819 51 ------DWRPDLVVS--DPLALAAALAAEALGIPVV-------------SLTP------PELeYPRPPDPANVRFVGPLL 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 163 RHELFLETPRQTLLGRRPRLLVLGGSL--GAEPLNKLLPEALGQLSEELrpeIFHQAGKQHAEITReryVAAGVEA-EVA 239
Cdd:COG1819 104 PDGPAELPPWLEEDAGRPLVYVTLGTSanDRADLLRAVLEALADLGVRV---VVTTGGLDPAELGP---LPDNVRVvDYV 177
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518172457 240 PFIKDMARAyawaDLVICRAGALTVCELAAAGLPsfLVPLPHAIDdhQTRNAEYLAKEGAAILLP 304
Cdd:COG1819 178 PQDALLPRA----DAVVHHGGAGTTAEALRAGVP--QVVVPFGGD--QPLNAARVERLGAGLALP 234
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
156-355 |
1.54e-09 |
|
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340861 [Multi-domain] Cd Length: 364 Bit Score: 58.87 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 156 RTTGNPVRHELFLETPRQTLLGR------RPRLLVLGGSLGAEPLNKLLpEALGQLSEELRPEIFhqAGKQHA--EITRE 227
Cdd:cd17507 168 KVTGIPVRPSFAEVRDKDEARNElnlspdKPTVLLMGGGGGMGPVKETV-EALLDSLRAGQVLVV--CGKNKKlyEKLSG 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 228 RYvAAGVEAEVAPFIKDMARAYAWADLVICRAGALTVCELAAAGLPsflVPLPHAIDDHQTRNAEYLAKEGAAILLPQAT 307
Cdd:cd17507 245 LE-EDYINVRVLGYVDDMNELMAASDLVITKPGGLTISEALARGLP---VIIYDPIPGQEEENADFLENNGAGIIARDPE 320
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518172457 308 TDAAALAAQLTevmmQPEKLKAMGATARRLARPDATRTVVDICLEVAH 355
Cdd:cd17507 321 ELLEIVARLID----PPSLLRMMSEAAKELKPPAAAKVIADILSLLID 364
|
|
| COG4671 |
COG4671 |
Predicted glycosyl transferase [General function prediction only]; |
139-304 |
2.24e-08 |
|
Predicted glycosyl transferase [General function prediction only];
Pssm-ID: 443708 [Multi-domain] Cd Length: 391 Bit Score: 55.24 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 139 QRVCEAFPNTFSNSAKRRTTG---NPVRHELFLETPRQTLLGRRPRLLVL--GGSLGAEplnklLPEALGQLSEELRPEI 213
Cdd:COG4671 173 YDLEESFPLPAEIADKVRYTGyvaRPAPEPPPEERDALGLLPEEPLILVSagGGGDGAE-----LLEAALAAAELLPPPD 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 214 FH--------QAGKQHAEItrERYVAAGVEAEVAPFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLVPLPHaIDD 285
Cdd:COG4671 248 HRwllvtgpfMPAADRAAL--RARAAALPNVTVERFTPDFEALLAAADLSVSMGGYNTVCEILSTGKPALIVPRTA-PRT 324
|
170
....*....|....*....
gi 518172457 286 HQTRNAEYLAKEGAAILLP 304
Cdd:COG4671 325 EQLIRAERLAELGLVDVLH 343
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
158-355 |
2.22e-07 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 52.03 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 158 TGNPVRHELFLETPRQTLLGR------RPRLLVLGGSLGAEPLNKLLPEALGQLSEelrPEIFHQAGKQHAEitreRYVA 231
Cdd:PRK13609 175 TGIPIRSSFELKINPDIIYNKyqlcpnKKILLIMAGAHGVLGNVKELCQSLMSVPD---LQVVVVCGKNEAL----KQSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 232 AGVEAE------VAPFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFLV-PLPhaidDHQTRNAEYLAKEGAAILLp 304
Cdd:PRK13609 248 EDLQETnpdalkVFGYVENIDELFRVTSCMITKPGGITLSEAAALGVPVILYkPVP----GQEKENAMYFERKGAAVVI- 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518172457 305 qatTDAAALAAQLTEVMMQPEKLKAMGATARRLARPDATRTVVDICLEVAH 355
Cdd:PRK13609 323 ---RDDEEVFAKTEALLQDDMKLLQMKEAMKSLYLPEPADHIVDDILAENH 370
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
4-304 |
2.26e-07 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 52.17 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 4 NVLIMAGGTGGHVFPALACAQEFQSRGYSVHWLGTPRGIEnEVVPAAGLPLHLI-----------QVSGLRGKGVGSLLK 72
Cdd:cd03784 2 RILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFNFA-DLVEAAGLTFVPVgddpdeleldsETNLGPDSLLELLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 73 APFQLLRSLGQARRIMRELQPVCVLgLGGYVTGPGGLAAKLAGVPLIIHEQNAVAGTANR---SLVPFAQRVCEAFPNTF 149
Cdd:cd03784 81 LLKAADELLDDLLAALRSSWKPDLV-IADPFAYAGPLVAEELGIPSVRLFTGPATLLSAYlhpFGVLNLLLSSLLEPELF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 150 SNSAKRRTTGNPVRHELFLETPRQTLLGRRPRLLVLGGSL------GAEPLNKLLPEALGQLSEELRPEIFH-------- 215
Cdd:cd03784 160 LDPLLEVLDRLRERLGLPPFSLVLLLLRLVPPLYVIGPTFpslppdRPRLPSVLGGLRIVPKNGPLPDELWEwldkqppr 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 216 ---------QAGKQHAEITREryVAAGVEAEVAPFI--------------KDMARAYAWA-----------DLVICRAGA 261
Cdd:cd03784 240 svvyvsfgsMVRDLPEELLEL--IAEALASLGQRFLwvvgpdplgglerlPDNVLVVKWVpqdellahpavGAFVTHGGW 317
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 518172457 262 LTVCELAAAGLPsfLVPLPHAIDdhQTRNAEYLAKEGAAILLP 304
Cdd:cd03784 318 NSTLEALYAGVP--MVVVPLFAD--QPNNAARVEELGAGVELD 356
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
9-121 |
2.28e-04 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
Pssm-ID: 340837 [Multi-domain] Cd Length: 358 Bit Score: 42.58 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 9 AGGTGGHVFPalaCAQEFQSRGYSVHWLGTPRGIENEVVPAAGLPLHLIQVSGLRgkgvgsllKAPFQLLRSLGQARRIM 88
Cdd:cd03808 9 DGGFQSFRLP---LIKALVKKGYEVHVIAPDGDKLSDELKELGVKVIDIPILRRG--------INPLKDLKALFKLYKLL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 518172457 89 RELQPVCVL------GLggYvtgpGGLAAKLAGVPLIIH 121
Cdd:cd03808 78 KKEKPDIVHchtpkpGI--L----GRLAARLAGVPKVIY 110
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
5-120 |
4.52e-04 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 40.00 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 5 VLIMAGGTGGHVFPalaCAQEFQSRGYSVHwLGTPRGIENEVVPAAGLPLHLIQVsglRGKGVGSLLKApFQLlrslgqa 84
Cdd:pfam13477 2 ILLLANADSIHTLR---WADALADRGYDVH-VISSKGPAKDELIAEGIHVHRLKV---PRKGPLGYLKA-FRL------- 66
|
90 100 110
....*....|....*....|....*....|....*....
gi 518172457 85 RRIMRELQPVCVLGLggYVTGP---GGLAAKLAGVPLII 120
Cdd:pfam13477 67 KKLIKKIKPDVVHVH--YAKPYgllAGLAARLSGFPPVV 103
|
|
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
162-348 |
9.13e-03 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 37.64 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 162 VRHELFLETprqtllgRRPRLLVLGGSLGAEPLNKLLpEALGQ-LSEELRPEIFHQ----AGKQHAEITRERYVAAGVEA 236
Cdd:PLN02605 196 LRRELGMDE-------DLPAVLLMGGGEGMGPLEETA-RALGDsLYDKNLGKPIGQvvviCGRNKKLQSKLESRDWKIPV 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172457 237 EVAPFIKDMARAYAWADLVICRAGALTVCELAAAGLPSFL---VP------LPHAIDDHQ---TRNAEYLAKEGAAILLP 304
Cdd:PLN02605 268 KVRGFVTNMEEWMGACDCIITKAGPGTIAEALIRGLPIILngyIPgqeegnVPYVVDNGFgafSESPKEIARIVAEWFGD 347
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518172457 305 QattdaaalaaqltevmmqPEKLKAMGATARRLARPDATRTVVD 348
Cdd:PLN02605 348 K------------------SDELEAMSENALKLARPEAVFDIVH 373
|
|
|