|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
4-348 |
7.43e-177 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 494.65 E-value: 7.43e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 4 PKRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAW 83
Cdd:PRK00726 1 MKKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 84 RQARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGAF-----PKADVVG 158
Cdd:PRK00726 81 LQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFpeffkPKAVVTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 159 NPVRVDVLALPLPDARLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDAVTIWHQSGKGAQQTVEQAYAEAgqPQHN 238
Cdd:PRK00726 161 NPVREEILALAAPPARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEALQVIHQTGKGDLEEVRAAYAAG--INAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 239 VTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHK-DRQQYWNALPLEKAGAAKIFEQPQFTADAVATTL 317
Cdd:PRK00726 239 VVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAaDDHQTANARALVDAGAALLIPQSDLTPEKLAEKL 318
|
330 340 350
....*....|....*....|....*....|...
gi 544824523 318 AGW--NRDVLLEMAERARAAAIPDATERVAKEV 348
Cdd:PRK00726 319 LELlsDPERLEAMAEAARALGKPDAAERLADLI 351
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
4-348 |
2.29e-167 |
|
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: 470.77 E-value: 2.29e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 4 PKRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAW 83
Cdd:COG0707 2 SKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 84 RQARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGA---FP--KADVVG 158
Cdd:COG0707 82 LQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETkkyFPkkKAVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 159 NPVRVDVLALPLPDAR--LAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDA-VTIWHQSGKGAQQTVEQAYAEAGQP 235
Cdd:COG0707 162 NPVRKEILELDRPEARakLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEArLQVVHQTGKGDYEEVRAAYAAAIRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 236 QHNVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHK-DRQQYWNALPLEKAGAAKIFEQPQFTADAVA 314
Cdd:COG0707 242 NAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAaDDHQTKNARALVEAGAAVLIPQSELTPEKLA 321
|
330 340 350
....*....|....*....|....*....|....*.
gi 544824523 315 TTLAGW--NRDVLLEMAERARAAAIPDATERVAKEV 348
Cdd:COG0707 322 EALEELleDPERLAKMAEAARALARPDAAERIADLI 357
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
6-347 |
6.09e-145 |
|
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: 413.53 E-value: 6.09e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 6 RLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWRQ 85
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 86 ARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGAFP-----KADVVGNP 160
Cdd:cd03785 81 ARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKyfpaaKVVVTGNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 161 VRVDVLALPLPDARLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDA-VTIWHQSGKGAQQTVEQAYAEAGqPQHNV 239
Cdd:cd03785 161 VREEILNLRKELKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLERgIQVIHQTGKGDYDEVKKLYEDLG-INVKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 240 TEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQH-KDRQQYWNALPLEKAGAAKIFEQPQFTADAVATTLA 318
Cdd:cd03785 240 FPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYaADDHQEANARALEKAGAAIVIDQEELTPEVLAEAIL 319
|
330 340 350
....*....|....*....|....*....|.
gi 544824523 319 GW--NRDVLLEMAERARAAAIPDATERVAKE 347
Cdd:cd03785 320 DLlnDPERLKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
5-348 |
1.64e-140 |
|
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: 402.44 E-value: 1.64e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 5 KRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWR 84
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 85 QARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGA--FPKADVVGNPVR 162
Cdd:TIGR01133 81 KARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAkdHFEAVLVGNPVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 163 VDVLALPLPDARLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDA-VTIWHQSGKGAQQTVEQAYAEAGqpQHNVTE 241
Cdd:TIGR01133 161 KEIRSLPVPRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKgIQIVHQGGKGDLEKVKNVYQELG--QEKIVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 242 FID-DMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHKDRQQYWNALPLEKAGAAKIFEQPQFTADAVATTLAGW 320
Cdd:TIGR01133 239 FIDeNMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYAADDQYYNAKFLEDLGAGLVIRQKELLPEKLLEALLKL 318
|
330 340 350
....*....|....*....|....*....|
gi 544824523 321 NRD--VLLEMAERARAAAIPDATERVAKEV 348
Cdd:TIGR01133 319 LLDpaNLENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
7-145 |
4.73e-56 |
|
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: 179.41 E-value: 4.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 7 LMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWRQA 86
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 544824523 87 RTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQ 145
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
4-348 |
7.43e-177 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 494.65 E-value: 7.43e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 4 PKRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAW 83
Cdd:PRK00726 1 MKKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 84 RQARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGAF-----PKADVVG 158
Cdd:PRK00726 81 LQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFpeffkPKAVVTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 159 NPVRVDVLALPLPDARLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDAVTIWHQSGKGAQQTVEQAYAEAgqPQHN 238
Cdd:PRK00726 161 NPVREEILALAAPPARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEALQVIHQTGKGDLEEVRAAYAAG--INAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 239 VTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHK-DRQQYWNALPLEKAGAAKIFEQPQFTADAVATTL 317
Cdd:PRK00726 239 VVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAaDDHQTANARALVDAGAALLIPQSDLTPEKLAEKL 318
|
330 340 350
....*....|....*....|....*....|...
gi 544824523 318 AGW--NRDVLLEMAERARAAAIPDATERVAKEV 348
Cdd:PRK00726 319 LELlsDPERLEAMAEAARALGKPDAAERLADLI 351
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
4-348 |
2.29e-167 |
|
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: 470.77 E-value: 2.29e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 4 PKRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAW 83
Cdd:COG0707 2 SKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 84 RQARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGA---FP--KADVVG 158
Cdd:COG0707 82 LQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETkkyFPkkKAVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 159 NPVRVDVLALPLPDAR--LAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDA-VTIWHQSGKGAQQTVEQAYAEAGQP 235
Cdd:COG0707 162 NPVRKEILELDRPEARakLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEArLQVVHQTGKGDYEEVRAAYAAAIRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 236 QHNVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHK-DRQQYWNALPLEKAGAAKIFEQPQFTADAVA 314
Cdd:COG0707 242 NAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAaDDHQTKNARALVEAGAAVLIPQSELTPEKLA 321
|
330 340 350
....*....|....*....|....*....|....*.
gi 544824523 315 TTLAGW--NRDVLLEMAERARAAAIPDATERVAKEV 348
Cdd:COG0707 322 EALEELleDPERLAKMAEAARALARPDAAERIADLI 357
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
6-347 |
6.09e-145 |
|
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: 413.53 E-value: 6.09e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 6 RLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWRQ 85
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 86 ARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGAFP-----KADVVGNP 160
Cdd:cd03785 81 ARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKyfpaaKVVVTGNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 161 VRVDVLALPLPDARLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDA-VTIWHQSGKGAQQTVEQAYAEAGqPQHNV 239
Cdd:cd03785 161 VREEILNLRKELKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLERgIQVIHQTGKGDYDEVKKLYEDLG-INVKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 240 TEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQH-KDRQQYWNALPLEKAGAAKIFEQPQFTADAVATTLA 318
Cdd:cd03785 240 FPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYaADDHQEANARALEKAGAAIVIDQEELTPEVLAEAIL 319
|
330 340 350
....*....|....*....|....*....|.
gi 544824523 319 GW--NRDVLLEMAERARAAAIPDATERVAKE 347
Cdd:cd03785 320 DLlnDPERLKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
5-348 |
1.64e-140 |
|
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: 402.44 E-value: 1.64e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 5 KRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWR 84
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 85 QARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGA--FPKADVVGNPVR 162
Cdd:TIGR01133 81 KARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAkdHFEAVLVGNPVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 163 VDVLALPLPDARLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDA-VTIWHQSGKGAQQTVEQAYAEAGqpQHNVTE 241
Cdd:TIGR01133 161 KEIRSLPVPRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKgIQIVHQGGKGDLEKVKNVYQELG--QEKIVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 242 FID-DMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHKDRQQYWNALPLEKAGAAKIFEQPQFTADAVATTLAGW 320
Cdd:TIGR01133 239 FIDeNMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYAADDQYYNAKFLEDLGAGLVIRQKELLPEKLLEALLKL 318
|
330 340 350
....*....|....*....|....*....|
gi 544824523 321 NRD--VLLEMAERARAAAIPDATERVAKEV 348
Cdd:TIGR01133 319 LLDpaNLENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
7-145 |
4.73e-56 |
|
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: 179.41 E-value: 4.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 7 LMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWRQA 86
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 544824523 87 RTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQ 145
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
|
|
| PRK12446 |
PRK12446 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
5-312 |
2.73e-36 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
Pssm-ID: 171505 [Multi-domain] Cd Length: 352 Bit Score: 134.60 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 5 KRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWR 84
Cdd:PRK12446 2 KKIVFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 85 QARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGA---FPKADVV--GN 159
Cdd:PRK12446 82 DAYVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAakhLPKEKVIytGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 160 PVRVDVLALPLPDARLA---GREGPVrVLVVGGSQGARILNQTMPQVAAKLGDAVTIWHQSGKGAQQTVEQayaeaGQPQ 236
Cdd:PRK12446 162 PVREEVLKGNREKGLAFlgfSRKKPV-ITIMGGSLGAKKINETVREALPELLLKYQIVHLCGKGNLDDSLQ-----NKEG 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544824523 237 HNVTEFI-DDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHKDRQ--QYWNALPLEKAGAAKIFEQPQFTADA 312
Cdd:PRK12446 236 YRQFEYVhGELPDILAITDFVISRAGSNAIFEFLTLQKPMLLIPLSKFASRgdQILNAESFERQGYASVLYEEDVTVNS 314
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
184-305 |
6.32e-36 |
|
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: 128.21 E-value: 6.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 184 VLVVGGSQGARILNQTMPQVAAKLGDA--VTIWHQSGKGAQQTVEQAYAEAGqPQHNVTEFIDDMAAAYAWADVVVCRSG 261
Cdd:pfam04101 2 ILVTGGSQGARALNELVLSVLPLLELKgeLQVLHQTGKGDLEEVKIDYAELG-INYEVFPFIDNMAEYIKAADLVISRAG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 544824523 262 ALTVSEIAAAGLPALFVPFQHKDR-QQYWNALPLEKAGAAKIFEQ 305
Cdd:pfam04101 81 AGTIAELLALGKPAILVPNPSAARgHQDNNAKELVKAGAALVILQ 125
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
6-318 |
5.25e-13 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 68.34 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 6 RLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADrmEADLVPKHGIEidFIRisglrgkglkamllapvrifnawrq 85
Cdd:COG1819 1 RILFVTLGGRGHVNPLLALARALRARGHEVTFATGPD--FADLVEAAGLE--FVD------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 86 artimkrFKPDVVLGmgGYVSGPGGLAAWSLGIPVVLheqngiagltnkwlakIATKVMQAFPGAFP-KADVVGNPVRVD 164
Cdd:COG1819 52 -------WRPDLVVS--DPLALAAALAAEALGIPVVS----------------LTPPELEYPRPPDPaNVRFVGPLLPDG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 165 VLALPLPDARLAGRegPvRVLVVGGS--QGARILNQTMPQVAAKLGDAVTIwhqsgkgaqQTVEQAYAEAGQPQHNVT-- 240
Cdd:COG1819 107 PAELPPWLEEDAGR--P-LVYVTLGTsaNDRADLLRAVLEALADLGVRVVV---------TTGGLDPAELGPLPDNVRvv 174
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544824523 241 EFIDdMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHkDrqQYWNALPLEKAGAAKIFEQPQFTADAVATTLA 318
Cdd:COG1819 175 DYVP-QDALLPRADAVVHHGGAGTTAEALRAGVPQVVVPFGG-D--QPLNAARVERLGAGLALPPRRLTAEALRAALR 248
|
|
| COG4671 |
COG4671 |
Predicted glycosyl transferase [General function prediction only]; |
16-318 |
2.00e-12 |
|
Predicted glycosyl transferase [General function prediction only];
Pssm-ID: 443708 [Multi-domain] Cd Length: 391 Bit Score: 67.57 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 16 GHVFPGLAVAHHLMDQGWQVrwLGTADRMEADLVPKHGiEIDFIRISGLRGKGLKAML-LAPVRIFNAWRQAR-----TI 89
Cdd:COG4671 16 GHLRRSLAIARALVADGFSV--LLISGGPPAPGFDLPP-GVDVVRLPGLRKDSFGEYLsRDLGPDLEAVLALRsqlllAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 90 MKRFKPDVVL------GMGGYVSGP-GGLAAWSLGIPVVLH---------------EQNGIAGLTNKWLAKI---ATKVM 144
Cdd:COG4671 93 FEAFQPDLLIvdkfpfGLRFELLPLlEALRARGPRTRVVLSlrdildepsvlrrewREEEVLDLIERYYDAVlvhGDPDV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 145 QAFPGAFPKADVVGNPVR-----VDVLALPLPDARLAGREGPVRVLVV----GGSQGARILNQTMpQVAAKLGDAVTIWH 215
Cdd:COG4671 173 YDLEESFPLPAEIADKVRytgyvARPAPEPPPEERDALGLLPEEPLILvsagGGGDGAELLEAAL-AAAELLPPPDHRWL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 216 Q-SGKGAQQTVEQAYAEAGQPQHNVT--EFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHKDRQQYWNAL 292
Cdd:COG4671 252 LvTGPFMPAADRAALRARAAALPNVTveRFTPDFEALLAAADLSVSMGGYNTVCEILSTGKPALIVPRTAPRTEQLIRAE 331
|
330 340
....*....|....*....|....*.
gi 544824523 293 PLEKAGAAKIFEQPQFTADAVATTLA 318
Cdd:COG4671 332 RLAELGLVDVLHPEDLTPEALARAIA 357
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
10-274 |
3.41e-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: 54.47 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 10 MAGGTGGHVFpglAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIrisglrgkglkAMLLAPVRIFNAWRQARTI 89
Cdd:cd03801 12 PVGGAERHVR---ELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLL-----------PSLAALLRARRLLRELRPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 90 MKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTN-------KWLAKI-----------------ATKVMQ 145
Cdd:cd03801 78 LRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLlllaaerRLLARAeallrradaviavsealRDELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 146 AFPGAFPKADVVGNPVRVDVLAlPLPDARLAGREGPVRVLVVGGSQ---GARILNQTMPQVAAKLGDAVtiWHQSGKGAQ 222
Cdd:cd03801 158 LGGIPPEKIVVIPNGVDLERFS-PPLRRKLGIPPDRPVLLFVGRLSprkGVDLLLEALAKLLRRGPDVR--LVIVGGDGP 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544824523 223 QtveqaYAEAGQPQHNVTEFI--------DDMAAAYAWADVVVCRS----GALTVSEIAAAGLP 274
Cdd:cd03801 235 L-----RAELEELELGLGDRVrflgfvpdEELPALYAAADVFVLPSryegFGLVVLEAMAAGLP 293
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
12-157 |
1.66e-06 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 47.53 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 12 GGTGGHVfpgLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGkglkamllaPVRIFNAWRQARTIMK 91
Cdd:pfam13439 1 GGVERYV---LELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPR---------LLRSLAFLRRLRRLLR 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544824523 92 RFKPDVVLGMGGYVSGPGGLAAW-SLGIPVVLH-----EQNGIAGLTNKWLAKIATKVMQAFpgaFPKADVV 157
Cdd:pfam13439 69 RERPDVVHAHSPFPLGLAALAARlRLGIPLVVTyhglfPDYKRLGARLSPLRRLLRRLERRL---LRRADRV 137
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
242-314 |
7.77e-05 |
|
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: 44.23 E-value: 7.77e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544824523 242 FIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFqhKDRQQYWNALPLEKAGAAKIFEQPQFTADAVA 314
Cdd:cd17507 257 YVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYDP--IPGQEEENADFLENNGAGIIARDPEELLEIVA 327
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
242-348 |
5.54e-04 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 41.63 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 242 FIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALF---VPFQHKDrqqywNALPLEKAGAAKIFEQPQFTADAVATTLA 318
Cdd:PRK13609 263 YVENIDELFRVTSCMITKPGGITLSEAAALGVPVILykpVPGQEKE-----NAMYFERKGAAVVIRDDEEVFAKTEALLQ 337
|
90 100 110
....*....|....*....|....*....|
gi 544824523 319 gwNRDVLLEMAERARAAAIPDATERVAKEV 348
Cdd:PRK13609 338 --DDMKLLQMKEAMKSLYLPEPADHIVDDI 365
|
|
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
156-348 |
2.90e-03 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 39.18 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 156 VVGNPVRVD--VLALPLPDAR--LAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDAVT--IWHQ------SGKGAQQ 223
Cdd:PLN02605 177 VYGLPIRPSfaRAVRPKDELRreLGMDEDLPAVLLMGGGEGMGPLEETARALGDSLYDKNLgkPIGQvvvicgRNKKLQS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 224 TVEqayAEAGQPQHNVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPAL---FVPFQHKDRQQYwnalpLEKAGAA 300
Cdd:PLN02605 257 KLE---SRDWKIPVKVRGFVTNMEEWMGACDCIITKAGPGTIAEALIRGLPIIlngYIPGQEEGNVPY-----VVDNGFG 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 544824523 301 KIFEQPQFTADAVATTLAGwNRDVLLEMAERARAAAIPDATERVAKEV 348
Cdd:PLN02605 329 AFSESPKEIARIVAEWFGD-KSDELEAMSENALKLARPEAVFDIVHDL 375
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
6-317 |
4.69e-03 |
|
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: 38.69 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 6 RLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMeADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWRQ 85
Cdd:cd03784 2 RILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFNF-ADLVEAAGLTFVPVGDDPDELELDSETNLGPDSLLELLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 86 ARTIMKRF------------KPDVVLgmGGYVSGPGGLAAWSLGIPVVLH-----------------------------E 124
Cdd:cd03784 81 LLKAADELlddllaalrsswKPDLVI--ADPFAYAGPLVAEELGIPSVRLftgpatllsaylhpfgvlnlllssllepeL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 125 QNGIAGLTNKWLAK----IATKVMQAFPGAFPKADVVGN-----------------PVRVDVLALPLPD---ARLAGREG 180
Cdd:cd03784 159 FLDPLLEVLDRLRErlglPPFSLVLLLLRLVPPLYVIGPtfpslppdrprlpsvlgGLRIVPKNGPLPDelwEWLDKQPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824523 181 PVRVLVVGGSQGARILNQT--MPQVAAKLGDAVTIW---HQSGKGAQQTVEQAYAEAGQPQHNVtefiddmaAAYAWADV 255
Cdd:cd03784 239 RSVVYVSFGSMVRDLPEELleLIAEALASLGQRFLWvvgPDPLGGLERLPDNVLVVKWVPQDEL--------LAHPAVGA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544824523 256 VVCRSGALTVSEIAAAGLPALFVPFqHKDrqQYWNALPLEKAGAAKIFEQPQFTADAVATTL 317
Cdd:cd03784 311 FVTHGGWNSTLEALYAGVPMVVVPL-FAD--QPNNAARVEELGAGVELDKDELTAEELAKAV 369
|
|
| |
