|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
4-348 |
0e+00 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 511.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 4 PKRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAW 83
Cdd:PRK00726 1 MKKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 84 RQARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGAF-----PKADVVG 158
Cdd:PRK00726 81 LQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFpeffkPKAVVTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 159 NPVRVDVLALPLPEVRLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDAVTLWHQSGKGAQQTVEQAYAEAgqPQHK 238
Cdd:PRK00726 161 NPVREEILALAAPPARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEALQVIHQTGKGDLEEVRAAYAAG--INAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 239 VTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHK-DRQQYWNALPLEKAGAAKIFEQPQFTADAVATTL 317
Cdd:PRK00726 239 VVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAaDDHQTANARALVDAGAALLIPQSDLTPEKLAEKL 318
|
330 340 350
....*....|....*....|....*....|...
gi 779794054 318 AGW--NRDVLLEMAERARATAIPDATERVAKEV 348
Cdd:PRK00726 319 LELlsDPERLEAMAEAARALGKPDAAERLADLI 351
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
4-348 |
7.72e-174 |
|
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: 487.33 E-value: 7.72e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 4 PKRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAW 83
Cdd:COG0707 2 SKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 84 RQARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGA---FP--KADVVG 158
Cdd:COG0707 82 LQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETkkyFPkkKAVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 159 NPVRVDVLALPLPEVR--LAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDA-VTLWHQSGKGAQQTVEQAYAEAGQP 235
Cdd:COG0707 162 NPVRKEILELDRPEARakLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEArLQVVHQTGKGDYEEVRAAYAAAIRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 236 QHKVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHK-DRQQYWNALPLEKAGAAKIFEQPQFTADAVA 314
Cdd:COG0707 242 NAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAaDDHQTKNARALVEAGAAVLIPQSELTPEKLA 321
|
330 340 350
....*....|....*....|....*....|....*.
gi 779794054 315 TTLAGW--NRDVLLEMAERARATAIPDATERVAKEV 348
Cdd:COG0707 322 EALEELleDPERLAKMAEAARALARPDAAERIADLI 357
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
6-347 |
1.35e-151 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340818 [Multi-domain] Cd Length: 350 Bit Score: 430.48 E-value: 1.35e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 6 RLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWRQ 85
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 86 ARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGAFP-----KADVVGNP 160
Cdd:cd03785 81 ARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKyfpaaKVVVTGNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 161 VRVDVLALPLPEVRLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDA-VTLWHQSGKGAQQTVEQAYAEAGqPQHKV 239
Cdd:cd03785 161 VREEILNLRKELKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLERgIQVIHQTGKGDYDEVKKLYEDLG-INVKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 240 TEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQH-KDRQQYWNALPLEKAGAAKIFEQPQFTADAVATTLA 318
Cdd:cd03785 240 FPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYaADDHQEANARALEKAGAAIVIDQEELTPEVLAEAIL 319
|
330 340 350
....*....|....*....|....*....|.
gi 779794054 319 GW--NRDVLLEMAERARATAIPDATERVAKE 347
Cdd:cd03785 320 DLlnDPERLKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
5-348 |
2.74e-145 |
|
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: 414.38 E-value: 2.74e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 5 KRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWR 84
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 85 QARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGA--FPKADVVGNPVR 162
Cdd:TIGR01133 81 KARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAkdHFEAVLVGNPVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 163 VDVLALPLPEVRLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDAVTLW-HQSGKGAQQTVEQAYAEAGqpQHKVTE 241
Cdd:TIGR01133 161 KEIRSLPVPRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKGIQIvHQGGKGDLEKVKNVYQELG--QEKIVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 242 FID-DMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHKDRQQYWNALPLEKAGAAKIFEQPQFTADAVATTLAGW 320
Cdd:TIGR01133 239 FIDeNMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYAADDQYYNAKFLEDLGAGLVIRQKELLPEKLLEALLKL 318
|
330 340 350
....*....|....*....|....*....|
gi 779794054 321 NRD--VLLEMAERARATAIPDATERVAKEV 348
Cdd:TIGR01133 319 LLDpaNLENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
7-145 |
5.16e-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: 5.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 7 LMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWRQA 86
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 779794054 87 RTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQ 145
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
4-348 |
0e+00 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 511.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 4 PKRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAW 83
Cdd:PRK00726 1 MKKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 84 RQARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGAF-----PKADVVG 158
Cdd:PRK00726 81 LQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFpeffkPKAVVTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 159 NPVRVDVLALPLPEVRLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDAVTLWHQSGKGAQQTVEQAYAEAgqPQHK 238
Cdd:PRK00726 161 NPVREEILALAAPPARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEALQVIHQTGKGDLEEVRAAYAAG--INAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 239 VTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHK-DRQQYWNALPLEKAGAAKIFEQPQFTADAVATTL 317
Cdd:PRK00726 239 VVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAaDDHQTANARALVDAGAALLIPQSDLTPEKLAEKL 318
|
330 340 350
....*....|....*....|....*....|...
gi 779794054 318 AGW--NRDVLLEMAERARATAIPDATERVAKEV 348
Cdd:PRK00726 319 LELlsDPERLEAMAEAARALGKPDAAERLADLI 351
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
4-348 |
7.72e-174 |
|
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: 487.33 E-value: 7.72e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 4 PKRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAW 83
Cdd:COG0707 2 SKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 84 RQARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGA---FP--KADVVG 158
Cdd:COG0707 82 LQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETkkyFPkkKAVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 159 NPVRVDVLALPLPEVR--LAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDA-VTLWHQSGKGAQQTVEQAYAEAGQP 235
Cdd:COG0707 162 NPVRKEILELDRPEARakLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEArLQVVHQTGKGDYEEVRAAYAAAIRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 236 QHKVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHK-DRQQYWNALPLEKAGAAKIFEQPQFTADAVA 314
Cdd:COG0707 242 NAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAaDDHQTKNARALVEAGAAVLIPQSELTPEKLA 321
|
330 340 350
....*....|....*....|....*....|....*.
gi 779794054 315 TTLAGW--NRDVLLEMAERARATAIPDATERVAKEV 348
Cdd:COG0707 322 EALEELleDPERLAKMAEAARALARPDAAERIADLI 357
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
6-347 |
1.35e-151 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340818 [Multi-domain] Cd Length: 350 Bit Score: 430.48 E-value: 1.35e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 6 RLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWRQ 85
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 86 ARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGAFP-----KADVVGNP 160
Cdd:cd03785 81 ARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKyfpaaKVVVTGNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 161 VRVDVLALPLPEVRLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDA-VTLWHQSGKGAQQTVEQAYAEAGqPQHKV 239
Cdd:cd03785 161 VREEILNLRKELKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLERgIQVIHQTGKGDYDEVKKLYEDLG-INVKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 240 TEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQH-KDRQQYWNALPLEKAGAAKIFEQPQFTADAVATTLA 318
Cdd:cd03785 240 FPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYaADDHQEANARALEKAGAAIVIDQEELTPEVLAEAIL 319
|
330 340 350
....*....|....*....|....*....|.
gi 779794054 319 GW--NRDVLLEMAERARATAIPDATERVAKE 347
Cdd:cd03785 320 DLlnDPERLKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
5-348 |
2.74e-145 |
|
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: 414.38 E-value: 2.74e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 5 KRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWR 84
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 85 QARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGA--FPKADVVGNPVR 162
Cdd:TIGR01133 81 KARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAkdHFEAVLVGNPVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 163 VDVLALPLPEVRLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDAVTLW-HQSGKGAQQTVEQAYAEAGqpQHKVTE 241
Cdd:TIGR01133 161 KEIRSLPVPRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKGIQIvHQGGKGDLEKVKNVYQELG--QEKIVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 242 FID-DMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHKDRQQYWNALPLEKAGAAKIFEQPQFTADAVATTLAGW 320
Cdd:TIGR01133 239 FIDeNMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYAADDQYYNAKFLEDLGAGLVIRQKELLPEKLLEALLKL 318
|
330 340 350
....*....|....*....|....*....|
gi 779794054 321 NRD--VLLEMAERARATAIPDATERVAKEV 348
Cdd:TIGR01133 319 LLDpaNLENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
7-145 |
5.16e-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: 5.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 7 LMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWRQA 86
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 779794054 87 RTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQ 145
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
184-344 |
2.84e-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: 134.38 E-value: 2.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 184 VLVVGGSQGARILNQTMPQVAAKLGDA--VTLWHQSGKGAQQTVEQAYAEAGqPQHKVTEFIDDMAAAYAWADVVVCRSG 261
Cdd:pfam04101 2 ILVTGGSQGARALNELVLSVLPLLELKgeLQVLHQTGKGDLEEVKIDYAELG-INYEVFPFIDNMAEYIKAADLVISRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 262 ALTVSEIAAAGLPALFVPFQHKDR-QQYWNALPLEKAGAAKIFEQPQFTADAVATTLAG--WNRDVLLEMAERARATAIP 338
Cdd:pfam04101 81 AGTIAELLALGKPAILVPNPSAARgHQDNNAKELVKAGAALVILQKELTPEKLIEALLKllLNPLRLAEMAKASKASGFK 160
|
....*.
gi 779794054 339 DATERV 344
Cdd:pfam04101 161 DAAKRL 166
|
|
| PRK12446 |
PRK12446 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
5-312 |
9.25e-36 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
Pssm-ID: 171505 [Multi-domain] Cd Length: 352 Bit Score: 133.06 E-value: 9.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 5 KRLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWR 84
Cdd:PRK12446 2 KKIVFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 85 QARTIMKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGA---FPKADVV--GN 159
Cdd:PRK12446 82 DAYVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAakhLPKEKVIytGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 160 PVRVDVLALPLPEVRLA---GREGPVrVLVVGGSQGARILNQTMPQVAAKLGDAVTLWHQSGKGAQQTVEQayaeaGQPQ 236
Cdd:PRK12446 162 PVREEVLKGNREKGLAFlgfSRKKPV-ITIMGGSLGAKKINETVREALPELLLKYQIVHLCGKGNLDDSLQ-----NKEG 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 779794054 237 HKVTEFI-DDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHKDRQ--QYWNALPLEKAGAAKIFEQPQFTADA 312
Cdd:PRK12446 236 YRQFEYVhGELPDILAITDFVISRAGSNAIFEFLTLQKPMLLIPLSKFASRgdQILNAESFERQGYASVLYEEDVTVNS 314
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
6-337 |
2.08e-14 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 72.20 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 6 RLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADrmEADLVPKHGIEidFIRisglrgkglkamllapvrifnawrq 85
Cdd:COG1819 1 RILFVTLGGRGHVNPLLALARALRARGHEVTFATGPD--FADLVEAAGLE--FVD------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 86 artimkrFKPDVVLGmgGYVSGPGGLAAWSLGIPVVLheqngiagltnkwlakIATKVMQAFPGAFP-KADVVGNPVRVD 164
Cdd:COG1819 52 -------WRPDLVVS--DPLALAAALAAEALGIPVVS----------------LTPPELEYPRPPDPaNVRFVGPLLPDG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 165 VLALPLPEVRLAGRegPvRVLVVGGS--QGARILNQTMPQVAAKLGDAVTLwhQSGKGAQQTVEQAYAEAgqpqhKVTEF 242
Cdd:COG1819 107 PAELPPWLEEDAGR--P-LVYVTLGTsaNDRADLLRAVLEALADLGVRVVV--TTGGLDPAELGPLPDNV-----RVVDY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 243 IDdMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHkDrqQYWNALPLEKAGAAKIFEQPQFTADAVATTLagwnR 322
Cdd:COG1819 177 VP-QDALLPRADAVVHHGGAGTTAEALRAGVPQVVVPFGG-D--QPLNAARVERLGAGLALPPRRLTAEALRAAL----R 248
|
330
....*....|....*
gi 779794054 323 DVLLEMAERARATAI 337
Cdd:COG1819 249 RLLADPSYRERAARL 263
|
|
| COG4671 |
COG4671 |
Predicted glycosyl transferase [General function prediction only]; |
16-318 |
6.47e-11 |
|
Predicted glycosyl transferase [General function prediction only];
Pssm-ID: 443708 [Multi-domain] Cd Length: 391 Bit Score: 62.95 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 16 GHVFPGLAVAHHLMDQGWQVrwLGTADRMEADLVPKHGiEIDFIRISGLRGKGLKAML-LAPVRIFNAWRQAR-----TI 89
Cdd:COG4671 16 GHLRRSLAIARALVADGFSV--LLISGGPPAPGFDLPP-GVDVVRLPGLRKDSFGEYLsRDLGPDLEAVLALRsqlllAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 90 MKRFKPDVVL------GMGGYVSGP-GGLAAWSLGIPVVLH---------------EQNGIAGLTNKWLAKI---ATKVM 144
Cdd:COG4671 93 FEAFQPDLLIvdkfpfGLRFELLPLlEALRARGPRTRVVLSlrdildepsvlrrewREEEVLDLIERYYDAVlvhGDPDV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 145 QAFPGAFPKADVVGNPVR-----VDVLALPLPEVRLAGREGPVRVLVV----GGSQGARILNQTMpQVAAKLGDAVTLWH 215
Cdd:COG4671 173 YDLEESFPLPAEIADKVRytgyvARPAPEPPPEERDALGLLPEEPLILvsagGGGDGAELLEAAL-AAAELLPPPDHRWL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 216 Q-SGKGAQQTVEQAYAEAGQPQHKVT--EFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHKDRQQYWNAL 292
Cdd:COG4671 252 LvTGPFMPAADRAALRARAAALPNVTveRFTPDFEALLAAADLSVSMGGYNTVCEILSTGKPALIVPRTAPRTEQLIRAE 331
|
330 340
....*....|....*....|....*.
gi 779794054 293 PLEKAGAAKIFEQPQFTADAVATTLA 318
Cdd:COG4671 332 RLAELGLVDVLHPEDLTPEALARAIA 357
|
|
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
156-348 |
6.02e-09 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 56.90 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 156 VVGNPVRVD--VLALPLPEVR--LAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDAVTlwhqsGKGAQQTV------ 225
Cdd:PLN02605 177 VYGLPIRPSfaRAVRPKDELRreLGMDEDLPAVLLMGGGEGMGPLEETARALGDSLYDKNL-----GKPIGQVVvicgrn 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 226 ----EQAYAEAGQPQHKVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPAL---FVPFQHKDRQQYwnalpLEKAG 298
Cdd:PLN02605 252 kklqSKLESRDWKIPVKVRGFVTNMEEWMGACDCIITKAGPGTIAEALIRGLPIIlngYIPGQEEGNVPY-----VVDNG 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 779794054 299 AAKIFEQPQFTADAVATTLAGwNRDVLLEMAERARATAIPDATERVAKEV 348
Cdd:PLN02605 327 FGAFSESPKEIARIVAEWFGD-KSDELEAMSENALKLARPEAVFDIVHDL 375
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
10-274 |
3.23e-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: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 10 MAGGTGGHVFpglAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIrisglrgkglkAMLLAPVRIFNAWRQARTI 89
Cdd:cd03801 12 PVGGAERHVR---ELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLL-----------PSLAALLRARRLLRELRPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 90 MKRFKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTN-------KWLAKI-----------------ATKVMQ 145
Cdd:cd03801 78 LRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLlllaaerRLLARAeallrradaviavsealRDELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 146 AFPGAFPKADVVGNPVRVDVLALPLPEvRLAGREGPVRVLVVGgsqgaRILNQ----TMPQVAAKLGDAVTLWHQ---SG 218
Cdd:cd03801 158 LGGIPPEKIVVIPNGVDLERFSPPLRR-KLGIPPDRPVLLFVG-----RLSPRkgvdLLLEALAKLLRRGPDVRLvivGG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779794054 219 KGAQQTVEQAYAEAGQPQHKVTEFI--DDMAAAYAWADVVVCRS----GALTVSEIAAAGLP 274
Cdd:cd03801 232 DGPLRAELEELELGLGDRVRFLGFVpdEELPALYAAADVFVLPSryegFGLVVLEAMAAGLP 293
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
238-347 |
1.05e-06 |
|
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: 50.01 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 238 KVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFqhKDRQQYWNALPLEKAGAAKIFEQPQFTADAVATTL 317
Cdd:cd17507 253 RVLGYVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYDP--IPGQEEENADFLENNGAGIIARDPEELLEIVARLI 330
|
90 100 110
....*....|....*....|....*....|
gi 779794054 318 AGwnrDVLLEMAERARATAIPDATERVAKE 347
Cdd:cd17507 331 DP---PSLLRMMSEAAKELKPPAAAKVIAD 357
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
238-348 |
1.12e-06 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 49.72 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 238 KVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALF---VPFQHKDrqqywNALPLEKAGAAKIFEQPQFTADAVA 314
Cdd:PRK13609 259 KVFGYVENIDELFRVTSCMITKPGGITLSEAAALGVPVILykpVPGQEKE-----NAMYFERKGAAVVIRDDEEVFAKTE 333
|
90 100 110
....*....|....*....|....*....|....
gi 779794054 315 TTLAgwNRDVLLEMAERARATAIPDATERVAKEV 348
Cdd:PRK13609 334 ALLQ--DDMKLLQMKEAMKSLYLPEPADHIVDDI 365
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
12-157 |
1.75e-06 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 47.53 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 12 GGTGGHVfpgLAVAHHLMDQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGkglkamllaPVRIFNAWRQARTIMK 91
Cdd:pfam13439 1 GGVERYV---LELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPR---------LLRSLAFLRRLRRLLR 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779794054 92 RFKPDVVLGMGGYVSGPGGLAAW-SLGIPVVLH-----EQNGIAGLTNKWLAKIATKVMQAFpgaFPKADVV 157
Cdd:pfam13439 69 RERPDVVHAHSPFPLGLAALAARlRLGIPLVVTyhglfPDYKRLGARLSPLRRLLRRLERRL---LRRADRV 137
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
6-334 |
2.94e-04 |
|
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: 42.54 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 6 RLMVMAGGTGGHVFPGLAVAHHLMDQGWQVRWLGTADRMeADLVPKHGIEIDFIRISGLRGKGLKAMLLAPVRIFNAWRQ 85
Cdd:cd03784 2 RILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFNF-ADLVEAAGLTFVPVGDDPDELELDSETNLGPDSLLELLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 86 ARTIMKRF------------KPDVVLgmGGYVSGPGGLAAWSLGIPVVLH-----------------------------E 124
Cdd:cd03784 81 LLKAADELlddllaalrsswKPDLVI--ADPFAYAGPLVAEELGIPSVRLftgpatllsaylhpfgvlnlllssllepeL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 125 QNGIAGLTNKWLAK----IATKVMQAFPGAFPKADVVGN-----------------PVRVDVLALPLP---EVRLAGREG 180
Cdd:cd03784 159 FLDPLLEVLDRLRErlglPPFSLVLLLLRLVPPLYVIGPtfpslppdrprlpsvlgGLRIVPKNGPLPdelWEWLDKQPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 181 PVRVLVVGGSQGARILNQT--MPQVAAKLGDAVTLW---HQSGKGAQQTVEQAYAEAGQPQHKVtefiddmaAAYAWADV 255
Cdd:cd03784 239 RSVVYVSFGSMVRDLPEELleLIAEALASLGQRFLWvvgPDPLGGLERLPDNVLVVKWVPQDEL--------LAHPAVGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 256 VVCRSGALTVSEIAAAGLPALFVPFqHKDrqQYWNALPLEKAGAAKIFEQPQFTADAVATTLagwnRDVLL-EMAERARA 334
Cdd:cd03784 311 FVTHGGWNSTLEALYAGVPMVVVPL-FAD--QPNNAARVEELGAGVELDKDELTAEELAKAV----REVLEdESYRRAAE 383
|
|
| PRK13608 |
PRK13608 |
diacylglycerol glucosyltransferase; Provisional |
219-348 |
3.04e-04 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 184179 [Multi-domain] Cd Length: 391 Bit Score: 42.47 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779794054 219 KGAQQTVEQAYAEagQPQHKVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFvpFQHKDRQQYWNALPLEKAG 298
Cdd:PRK13608 242 KELKRSLTAKFKS--NENVLILGYTKHMNEWMASSQLMITKPGGITISEGLARCIPMIF--LNPAPGQELENALYFEEKG 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 779794054 299 AAKIFEQPQFTADAVATTLAGWNRdvLLEMAERARATAIPDATERVAKEV 348
Cdd:PRK13608 318 FGKIADTPEEAIKIVASLTNGNEQ--LTNMISTMEQDKIKYATQTICRDL 365
|
|
| |
