|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12446 |
PRK12446 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
1-352 |
1.29e-158 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
Pssm-ID: 171505 [Multi-domain] Cd Length: 352 Bit Score: 448.54 E-value: 1.29e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 1 MKHIVLTGGGTAGHVTPNIAMIPRLKELGYTISYIGSYEGIEKKLIEEMGIPYYGISSGKLRRYFDVKNFTDPFKVMKGF 80
Cdd:PRK12446 1 MKKIVFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 81 AEAKKLMKQLKPDVVFSKGGFVTVPVVIAASRKKIPTFIHESDMTPGLANKISIPFATKVCCNFPETVSELPANKAVLTG 160
Cdd:PRK12446 81 MDAYVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAAKHLPKEKVIYTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 161 TPIRQELLEGSPERAREFTGFTSDKPVIMIIGGSLGAAAVNDAVRAVLPELLKNFQIIHLCGKGKLDESLKNTKGYVQYE 240
Cdd:PRK12446 161 SPVREEVLKGNREKGLAFLGFSRKKPVITIMGGSLGAKKINETVREALPELLLKYQIVHLCGKGNLDDSLQNKEGYRQFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 241 YIKKELADLFALADIVISRAGANAICELSALKKPNLLIPLSARASRGDQILNARSFERMGYSVVLEEEEITNEKLVDIIN 320
Cdd:PRK12446 241 YVHGELPDILAITDFVISRAGSNAIFEFLTLQKPMLLIPLSKFASRGDQILNAESFERQGYASVLYEEDVTVNSLIKHVE 320
|
330 340 350
....*....|....*....|....*....|..
gi 1575849020 321 SLYKGRAAYTEAMSKSKLTDSIEEIVQLFEQA 352
Cdd:PRK12446 321 ELSHNNEKYKTALKKYNGKEAIQTIIDHISEA 352
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-355 |
2.15e-156 |
|
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: 443.03 E-value: 2.15e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 1 MKHIVLTGGGTAGHVTPNIAMIPRLKELGYTISYIGSYEGIEKKLIEEMGIPYYGISSGKLRRYFDVKNFTDPFKVMKGF 80
Cdd:COG0707 2 SKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 81 AEAKKLMKQLKPDVVFSKGGFVTVPVVIAASRKKIPTFIHESDMTPGLANKISIPFATKVCCNFPETVSELPANKAVLTG 160
Cdd:COG0707 82 LQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPKKKAVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 161 TPIRQELLEGSPERAREFTGFTSDKPVIMIIGGSLGAAAVNDAVRAVLPELLK-NFQIIHLCGKGKLDESLKN-----TK 234
Cdd:COG0707 162 NPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEaRLQVVHQTGKGDYEEVRAAyaaaiRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 235 GYVQYEYIkKELADLFALADIVISRAGANAICELSALKKPNLLIPLSaRASRGDQILNARSFERMGYSVVLEEEEITNEK 314
Cdd:COG0707 242 NAEVFPFI-DDMADAYAAADLVISRAGASTVAELAALGKPAILVPLP-HAADDHQTKNARALVEAGAAVLIPQSELTPEK 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1575849020 315 LVDIINSLYKGR---AAYTEAMSKSKLTDSIEEIVQLFEQAVNR 355
Cdd:COG0707 320 LAEALEELLEDPerlAKMAEAARALARPDAAERIADLILELAKG 363
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
3-348 |
2.55e-129 |
|
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: 373.86 E-value: 2.55e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 3 HIVLTGGGTAGHVTPNIAMIPRLKELGYTISYIGSYEGIEKKLIEEMGIPYYGISSGKLRRYFDVKNFTDPFKVMKGFAE 82
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 83 AKKLMKQLKPDVVFSKGGFVTVPVVIAASRKKIPTFIHESDMTPGLANKISIPFATKVCCNFPETVSELPANKAVLTGTP 162
Cdd:cd03785 81 ARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVVVTGNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 163 IRQELLEGSPERAREftGFTSDKPVIMIIGGSLGAAAVNDAVRAVLPELL-KNFQIIHLCGKGKLDESLKN----TKGYV 237
Cdd:cd03785 161 VREEILNLRKELKRF--GLPPDKPTLLVFGGSQGARAINRAVPKALPKLLeRGIQVIHQTGKGDYDEVKKLyedlGINVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 238 QYEYIkKELADLFALADIVISRAGANAICELSALKKPNLLIPLSArASRGDQILNARSFERMGYSVVLEEEEITNEKLVD 317
Cdd:cd03785 239 VFPFI-DDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPY-AADDHQEANARALEKAGAAIVIDQEELTPEVLAE 316
|
330 340 350
....*....|....*....|....*....|....
gi 1575849020 318 IINSLYKGR---AAYTEAMSKSKLTDSIEEIVQL 348
Cdd:cd03785 317 AILDLLNDPerlKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
2-348 |
2.34e-102 |
|
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: 305.37 E-value: 2.34e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 2 KHIVLTGGGTAGHVTPNIAMIPRLKELGYTISYIGSYEGIEKKLIEEMGIPYYGISSGKLRRYFDVKNFTDPFKVMKGFA 81
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 82 EAKKLMKQLKPDVVFSKGGFVTVPVVIAASRKKIPTFIHESDMTPGLANKISIPFATKVCCNFPETvseLPANKAVLTGT 161
Cdd:TIGR01133 81 KARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGA---KDHFEAVLVGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 162 PIRQELLEGSPERAREftGFTSDKPVIMIIGGSLGAAAVNDAVRAVLPEL-LKNFQIIHLCGKGKLDESLK--NTKGYVQ 238
Cdd:TIGR01133 158 PVRKEIRSLPVPRERF--GRREGKPTILVLGGSQGAKILNELVPKALAKLqEKGIQIVHQGGKGDLEKVKNvyQELGQEK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 239 Y-EYIKKELADLFALADIVISRAGANAICELSALKKPNLLIPLSARAsrGDQILNARSFERMGYSVVLEEEEITNEKLVD 317
Cdd:TIGR01133 236 IvTFIDENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYAA--DDQYYNAKFLEDLGAGLVIRQKELLPEKLLE 313
|
330 340 350
....*....|....*....|....*....|....
gi 1575849020 318 IINSLYKGRA---AYTEAMSKSKLTDSIEEIVQL 348
Cdd:TIGR01133 314 ALLKLLLDPAnleNMAEAARKLAKPDAAKRIAEL 347
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
4-140 |
3.12e-48 |
|
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.
Pssm-ID: 427107 [Multi-domain] Cd Length: 139 Bit Score: 159.38 E-value: 3.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 4 IVLTGGGTAGHVTPNIAMIPRLKELGYTISYIGSYEGIEKKLIEEMGIPYYGISSGKLRRYFDVKNFTDPFKVMKGFAEA 83
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1575849020 84 KKLMKQLKPDVVFSKGGFVTVPVVIAASRKKIPTFIHESDMTPGLANKISIPFATKV 140
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12446 |
PRK12446 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
1-352 |
1.29e-158 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
Pssm-ID: 171505 [Multi-domain] Cd Length: 352 Bit Score: 448.54 E-value: 1.29e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 1 MKHIVLTGGGTAGHVTPNIAMIPRLKELGYTISYIGSYEGIEKKLIEEMGIPYYGISSGKLRRYFDVKNFTDPFKVMKGF 80
Cdd:PRK12446 1 MKKIVFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 81 AEAKKLMKQLKPDVVFSKGGFVTVPVVIAASRKKIPTFIHESDMTPGLANKISIPFATKVCCNFPETVSELPANKAVLTG 160
Cdd:PRK12446 81 MDAYVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAAKHLPKEKVIYTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 161 TPIRQELLEGSPERAREFTGFTSDKPVIMIIGGSLGAAAVNDAVRAVLPELLKNFQIIHLCGKGKLDESLKNTKGYVQYE 240
Cdd:PRK12446 161 SPVREEVLKGNREKGLAFLGFSRKKPVITIMGGSLGAKKINETVREALPELLLKYQIVHLCGKGNLDDSLQNKEGYRQFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 241 YIKKELADLFALADIVISRAGANAICELSALKKPNLLIPLSARASRGDQILNARSFERMGYSVVLEEEEITNEKLVDIIN 320
Cdd:PRK12446 241 YVHGELPDILAITDFVISRAGSNAIFEFLTLQKPMLLIPLSKFASRGDQILNAESFERQGYASVLYEEDVTVNSLIKHVE 320
|
330 340 350
....*....|....*....|....*....|..
gi 1575849020 321 SLYKGRAAYTEAMSKSKLTDSIEEIVQLFEQA 352
Cdd:PRK12446 321 ELSHNNEKYKTALKKYNGKEAIQTIIDHISEA 352
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-355 |
2.15e-156 |
|
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: 443.03 E-value: 2.15e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 1 MKHIVLTGGGTAGHVTPNIAMIPRLKELGYTISYIGSYEGIEKKLIEEMGIPYYGISSGKLRRYFDVKNFTDPFKVMKGF 80
Cdd:COG0707 2 SKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 81 AEAKKLMKQLKPDVVFSKGGFVTVPVVIAASRKKIPTFIHESDMTPGLANKISIPFATKVCCNFPETVSELPANKAVLTG 160
Cdd:COG0707 82 LQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPKKKAVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 161 TPIRQELLEGSPERAREFTGFTSDKPVIMIIGGSLGAAAVNDAVRAVLPELLK-NFQIIHLCGKGKLDESLKN-----TK 234
Cdd:COG0707 162 NPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEaRLQVVHQTGKGDYEEVRAAyaaaiRP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 235 GYVQYEYIkKELADLFALADIVISRAGANAICELSALKKPNLLIPLSaRASRGDQILNARSFERMGYSVVLEEEEITNEK 314
Cdd:COG0707 242 NAEVFPFI-DDMADAYAAADLVISRAGASTVAELAALGKPAILVPLP-HAADDHQTKNARALVEAGAAVLIPQSELTPEK 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1575849020 315 LVDIINSLYKGR---AAYTEAMSKSKLTDSIEEIVQLFEQAVNR 355
Cdd:COG0707 320 LAEALEELLEDPerlAKMAEAARALARPDAAERIADLILELAKG 363
|
|
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
1-355 |
6.22e-152 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 431.48 E-value: 6.22e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 1 MKHIVLTGGGTAGHVTPNIAMIPRLKELGYTISYIGSYEGIEKKLIEEMGIPYYGISSGKLRRYFDVKNFTDPFKVMKGF 80
Cdd:PRK00726 1 MKKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 81 AEAKKLMKQLKPDVVFSKGGFVTVPVVIAASRKKIPTFIHESDMTPGLANKISIPFATKVCCNFPETVSELPANKAVLTG 160
Cdd:PRK00726 81 LQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAVVTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 161 TPIRQELLEGSPERAREftGFTSDKPVIMIIGGSLGAAAVNDAVRAVLPELLKNFQIIHLCGKGKLDESLKNTKGYVQYE 240
Cdd:PRK00726 161 NPVREEILALAAPPARL--AGREGKPTLLVVGGSQGARVLNEAVPEALALLPEALQVIHQTGKGDLEEVRAAYAAGINAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 241 ---YIkKELADLFALADIVISRAGANAICELSALKKPNLLIPLSaRASRGDQILNARSFERMGYSVVLEEEEITNEKLVD 317
Cdd:PRK00726 239 vvpFI-DDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLP-HAADDHQTANARALVDAGAALLIPQSDLTPEKLAE 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1575849020 318 IINSLYKGRAAYTEAMSKSK---LTDSIEEIVQLFEQAVNR 355
Cdd:PRK00726 317 KLLELLSDPERLEAMAEAARalgKPDAAERLADLIEELARK 357
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
3-348 |
2.55e-129 |
|
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: 373.86 E-value: 2.55e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 3 HIVLTGGGTAGHVTPNIAMIPRLKELGYTISYIGSYEGIEKKLIEEMGIPYYGISSGKLRRYFDVKNFTDPFKVMKGFAE 82
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 83 AKKLMKQLKPDVVFSKGGFVTVPVVIAASRKKIPTFIHESDMTPGLANKISIPFATKVCCNFPETVSELPANKAVLTGTP 162
Cdd:cd03785 81 ARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVVVTGNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 163 IRQELLEGSPERAREftGFTSDKPVIMIIGGSLGAAAVNDAVRAVLPELL-KNFQIIHLCGKGKLDESLKN----TKGYV 237
Cdd:cd03785 161 VREEILNLRKELKRF--GLPPDKPTLLVFGGSQGARAINRAVPKALPKLLeRGIQVIHQTGKGDYDEVKKLyedlGINVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 238 QYEYIkKELADLFALADIVISRAGANAICELSALKKPNLLIPLSArASRGDQILNARSFERMGYSVVLEEEEITNEKLVD 317
Cdd:cd03785 239 VFPFI-DDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPY-AADDHQEANARALEKAGAAIVIDQEELTPEVLAE 316
|
330 340 350
....*....|....*....|....*....|....
gi 1575849020 318 IINSLYKGR---AAYTEAMSKSKLTDSIEEIVQL 348
Cdd:cd03785 317 AILDLLNDPerlKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
2-348 |
2.34e-102 |
|
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: 305.37 E-value: 2.34e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 2 KHIVLTGGGTAGHVTPNIAMIPRLKELGYTISYIGSYEGIEKKLIEEMGIPYYGISSGKLRRYFDVKNFTDPFKVMKGFA 81
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 82 EAKKLMKQLKPDVVFSKGGFVTVPVVIAASRKKIPTFIHESDMTPGLANKISIPFATKVCCNFPETvseLPANKAVLTGT 161
Cdd:TIGR01133 81 KARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGA---KDHFEAVLVGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 162 PIRQELLEGSPERAREftGFTSDKPVIMIIGGSLGAAAVNDAVRAVLPEL-LKNFQIIHLCGKGKLDESLK--NTKGYVQ 238
Cdd:TIGR01133 158 PVRKEIRSLPVPRERF--GRREGKPTILVLGGSQGAKILNELVPKALAKLqEKGIQIVHQGGKGDLEKVKNvyQELGQEK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 239 Y-EYIKKELADLFALADIVISRAGANAICELSALKKPNLLIPLSARAsrGDQILNARSFERMGYSVVLEEEEITNEKLVD 317
Cdd:TIGR01133 236 IvTFIDENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYAA--DDQYYNAKFLEDLGAGLVIRQKELLPEKLLE 313
|
330 340 350
....*....|....*....|....*....|....
gi 1575849020 318 IINSLYKGRA---AYTEAMSKSKLTDSIEEIVQL 348
Cdd:TIGR01133 314 ALLKLLLDPAnleNMAEAARKLAKPDAAKRIAEL 347
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
4-140 |
3.12e-48 |
|
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.
Pssm-ID: 427107 [Multi-domain] Cd Length: 139 Bit Score: 159.38 E-value: 3.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 4 IVLTGGGTAGHVTPNIAMIPRLKELGYTISYIGSYEGIEKKLIEEMGIPYYGISSGKLRRYFDVKNFTDPFKVMKGFAEA 83
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1575849020 84 KKLMKQLKPDVVFSKGGFVTVPVVIAASRKKIPTFIHESDMTPGLANKISIPFATKV 140
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
187-345 |
2.16e-31 |
|
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: 116.27 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 187 VIMIIGGSLGAAAVNDAVRAVLPELLK--NFQIIHLCGKGKLDE----SLKNTKGYVQYEYIKKeLADLFALADIVISRA 260
Cdd:pfam04101 1 TILVTGGSQGARALNELVLSVLPLLELkgELQVLHQTGKGDLEEvkidYAELGINYEVFPFIDN-MAEYIKAADLVISRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 261 GANAICELSALKKPNLLIPLSaRASRGDQILNARSFERMGYSVVLEEEEITNEKLVDIINSLYKGRAAYTEAMSKSK--- 337
Cdd:pfam04101 80 GAGTIAELLALGKPAILVPNP-SAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALLKLLLNPLRLAEMAKASKasg 158
|
....*...
gi 1575849020 338 LTDSIEEI 345
Cdd:pfam04101 159 FKDAAKRL 166
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
3-328 |
3.98e-13 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 68.73 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 3 HIVLTGGGTAGHVTPNIAMIPRLKELGYTISYIGSYEGIEkkLIEEMGIPYYGIssgklrryfdvknftdpfkvmkgfae 82
Cdd:COG1819 1 RILFVTLGGRGHVNPLLALARALRARGHEVTFATGPDFAD--LVEAAGLEFVDW-------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 83 akklmkqlKPDVVFSkgGFVTVPVVIAASRKKIPTFIHesdMTPGLankisipfatkvccNFPEtvSELPANkAVLTGTP 162
Cdd:COG1819 53 --------RPDLVVS--DPLALAAALAAEALGIPVVSL---TPPEL--------------EYPR--PPDPAN-VRFVGPL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 163 IRQELLEGSPERAREftgftSDKPVIMIiggSLGAAAVNDAvrAVLPELLKNFQ------IIHLCG--KGKLDESLKNTK 234
Cdd:COG1819 103 LPDGPAELPPWLEED-----AGRPLVYV---TLGTSANDRA--DLLRAVLEALAdlgvrvVVTTGGldPAELGPLPDNVR 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 235 --GYVqyeyikkELADLFALADIVISRAGANAICELSALKKPNLLIPLsarasRGDQILNARSFERMGYSVVLEEEEITN 312
Cdd:COG1819 173 vvDYV-------PQDALLPRADAVVHHGGAGTTAEALRAGVPQVVVPF-----GGDQPLNAARVERLGAGLALPPRRLTA 240
|
330 340
....*....|....*....|.
gi 1575849020 313 EKLVDIINSL-----YKGRAA 328
Cdd:COG1819 241 EALRAALRRLladpsYRERAA 261
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
65-320 |
7.32e-13 |
|
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340861 [Multi-domain] Cd Length: 364 Bit Score: 68.88 E-value: 7.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 65 FDVKNFTDPFKVMKGFAEAKKLMKQLKPDVVFS--KGGFVTVPVVIAASRKKIPTFiheSDMTPGLANKISI-PFATKVC 141
Cdd:cd17507 71 SDRLNSISNKAARLGLKKLKELLREEQPDVIIStfPLMSALVELFKRKGLLPIPVY---TVITDYVLHSTWIhPEVDRYF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 142 CNFPETVSEL-----PANKAVLTGTPIRQELLEGSPER-AREFTGFTSDKPVIMIIGGSLGAAAVNDAVRAvLPELLKNF 215
Cdd:cd17507 148 VASEEVKRELvergvTPSQIKVTGIPVRPSFAEVRDKDeARNELNLSPDKPTVLLMGGGGGMGPVKETVEA-LLDSLRAG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 216 QIIHLCGK-GKLDESL-------KNTK--GYVqyeyikKELADLFALADIVISRAGANAICELSALKKPNLL---IPlsa 282
Cdd:cd17507 227 QVLVVCGKnKKLYEKLsgleedyINVRvlGYV------DDMNELMAASDLVITKPGGLTISEALARGLPVIIydpIP--- 297
|
250 260 270
....*....|....*....|....*....|....*...
gi 1575849020 283 rasrGDQILNARSFERMGYSVVLEEEEITNEKLVDIIN 320
Cdd:cd17507 298 ----GQEEENADFLENNGAGIIARDPEELLEIVARLID 331
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
34-347 |
9.60e-12 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 65.52 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 34 YIGSYeGIEKKLieeMGIPYYGIssgklRRYFDVKNFTDPFKVmkGFAEAKKLMKQLKPDVVFSKGGFVTVPVVIAASRK 113
Cdd:PRK13609 58 YLKSY-TIGKEL---YRLFYYGV-----EKIYDKKIFSWYANF--GRKRLKLLLQAEKPDIVINTFPIIAVPELKKQTGI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 114 KIPTFiheSDMTPGLANKISIP-------FATKvccNFPETVSEL--PANKAVLTGTPIRQEL-LEGSPERAREFTGFTS 183
Cdd:PRK13609 127 SIPTY---NVLTDFCLHKIWVHrevdryfVATD---HVKKVLVDIgvPPEQVVETGIPIRSSFeLKINPDIIYNKYQLCP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 184 DKPVIMIIGGSLGaaaVNDAVRAVLPELLK--NFQIIHLCGKGK-LDESLKNTK----------GYVQyeyikkELADLF 250
Cdd:PRK13609 201 NKKILLIMAGAHG---VLGNVKELCQSLMSvpDLQVVVVCGKNEaLKQSLEDLQetnpdalkvfGYVE------NIDELF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 251 ALADIVISRAGANAICELSALKKPNLLIplsaRASRGDQILNARSFERMGYSVVL-EEEEITN--EKLVDIINSLYKGRa 327
Cdd:PRK13609 272 RVTSCMITKPGGITLSEAAALGVPVILY----KPVPGQEKENAMYFERKGAAVVIrDDEEVFAktEALLQDDMKLLQMK- 346
|
330 340
....*....|....*....|
gi 1575849020 328 aytEAMSKSKLTDSIEEIVQ 347
Cdd:PRK13609 347 ---EAMKSLYLPEPADHIVD 363
|
|
| COG4671 |
COG4671 |
Predicted glycosyl transferase [General function prediction only]; |
163-322 |
3.45e-08 |
|
Predicted glycosyl transferase [General function prediction only];
Pssm-ID: 443708 [Multi-domain] Cd Length: 391 Bit Score: 54.47 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 163 IRQELLEGSPErAREFTGFTSDKP--VIMIIGGSLGAAAVNDAVRAVLPELLKNFQIIHLCGkGKLDESLKN-------T 233
Cdd:COG4671 195 VARPAPEPPPE-ERDALGLLPEEPliLVSAGGGGDGAELLEAALAAAELLPPPDHRWLLVTG-PFMPAADRAalraraaA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 234 KGYVQYEYIKKELADLFALADIVISRAGANAICELSALKKPNLLIPLSARasRGDQILNARSFERMGYSVVLEEEEITNE 313
Cdd:COG4671 273 LPNVTVERFTPDFEALLAAADLSVSMGGYNTVCEILSTGKPALIVPRTAP--RTEQLIRAERLAELGLVDVLHPEDLTPE 350
|
....*....
gi 1575849020 314 KLVDIINSL 322
Cdd:COG4671 351 ALARAIAAA 359
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
3-120 |
2.35e-06 |
|
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: 48.75 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 3 HIVLTGGGTAGHVTPniaMIPRLKELGYTISYIGSYEGIEKKLIEEMGIPYYGISSgkLRRyfdvknFTDPFKVMKGFAE 82
Cdd:cd03808 4 FIVNVDGGFQSFRLP---LIKALVKKGYEVHVIAPDGDKLSDELKELGVKVIDIPI--LRR------GINPLKDLKALFK 72
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1575849020 83 AKKLMKQLKPDVVF---SKGGFVtvpVVIAASRKKIPTFIH 120
Cdd:cd03808 73 LYKLLKKEKPDIVHchtPKPGIL---GRLAARLAGVPKVIY 110
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
3-351 |
6.22e-06 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 47.55 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 3 HIVLTGGGTAGHVTPNIAMIPRLKELGYTISYIgSYEGIEKKLIEEMGIPYYGISSGKLRRYFDVKNFTDPFKVMKGFAE 82
Cdd:cd03784 2 RILFVPFPGQGHVNPMLPLAKALAARGHEVTVA-TPPFNFADLVEAAGLTFVPVGDDPDELELDSETNLGPDSLLELLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 83 AKKLMKQL------------KPDVVFSkgGFVTVPVVIAASRKKIPTFIH----------------------ESDMTPGL 128
Cdd:cd03784 81 LLKAADELlddllaalrsswKPDLVIA--DPFAYAGPLVAEELGIPSVRLftgpatllsaylhpfgvlnlllSSLLEPEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 129 ANKISIPFATKV-----CCNFPETVSELPANKAVLTGTPIRQELLEGSPERAREFTGFTS-------------------D 184
Cdd:cd03784 159 FLDPLLEVLDRLrerlgLPPFSLVLLLLRLVPPLYVIGPTFPSLPPDRPRLPSVLGGLRIvpkngplpdelwewldkqpP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 185 KPVIMIiggSLG--AAAVNDAVRAVLPELLKNFQ--IIHLCGKGKLDEsLKNTKGYVqyeYIKKEL--ADLFA--LADIV 256
Cdd:cd03784 239 RSVVYV---SFGsmVRDLPEELLELIAEALASLGqrFLWVVGPDPLGG-LERLPDNV---LVVKWVpqDELLAhpAVGAF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 257 ISRAGANAICELSALKKPNLLIPLSArasrgDQILNARSFERMGYSVVLEEEEITNEKLVDIINSL----YKGRAAytEA 332
Cdd:cd03784 312 VTHGGWNSTLEALYAGVPMVVVPLFA-----DQPNNAARVEELGAGVELDKDELTAEELAKAVREVledeSYRRAA--EL 384
|
410
....*....|....*....
gi 1575849020 333 MSKSKLTDSIEEIVQLFEQ 351
Cdd:cd03784 385 LAELREEDGAPSAADVVER 403
|
|
| Glyco_trans_1_3 |
pfam13528 |
Glycosyl transferase family 1; |
206-322 |
1.44e-04 |
|
Glycosyl transferase family 1;
Pssm-ID: 404422 Cd Length: 321 Bit Score: 43.25 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 206 AVLPELLKNFQI-IHLCGKGKlDESLKNTKGYVQYEYIKKE--LADLfALADIVISRAGANAICELSALKKPNLLIPLsa 282
Cdd:pfam13528 206 EALPETLAQFGVeCRIYGLRR-DLTEEGREGNLTYRPFSEAgfLDDL-ATARAVIAGGGFTLMTEAVYLRKPYLAVPV-- 281
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1575849020 283 rASRGDQILNARSFERMGYSVVLEEEEITNEKLVDIINSL 322
Cdd:pfam13528 282 -AGQFEQVLNARYLERLGYGANWDLQDLDPAVVGDFLYRL 320
|
|
| PRK13608 |
PRK13608 |
diacylglycerol glucosyltransferase; Provisional |
135-345 |
1.91e-04 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 184179 [Multi-domain] Cd Length: 391 Bit Score: 42.86 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 135 PFATKVCCNFPETVSEL-----PANKAVLTGTPIRQELLEGSPERA-REFTGFTSDKPVIMIIGGSLGAAAVNDAVRAVL 208
Cdd:PRK13608 146 PYSTRYYVATKETKQDFidvgiDPSTVKVTGIPIDNKFETPIDQKQwLIDNNLDPDKQTILMSAGAFGVSKGFDTMITDI 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 209 PELLKNFQIIHLCGKGK-LDESLKNTkgYVQYEYI-----KKELADLFALADIVISRAGANAICElsALKKPNLLIPLSA 282
Cdd:PRK13608 226 LAKSANAQVVMICGKSKeLKRSLTAK--FKSNENVlilgyTKHMNEWMASSQLMITKPGGITISE--GLARCIPMIFLNP 301
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1575849020 283 raSRGDQILNARSFERMGYSVVLEEEEITNEKLVDIINSLYKgRAAYTEAMSKSKLTDSIEEI 345
Cdd:PRK13608 302 --APGQELENALYFEEKGFGKIADTPEEAIKIVASLTNGNEQ-LTNMISTMEQDKIKYATQTI 361
|
|
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
150-277 |
1.46e-03 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 40.34 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1575849020 150 ELPANKAVLTGTPIRQELLEGSPERA--REFTGFTSDKPVIMIIGGSLGAAAVNDAVRAvLPELLKNF-------QIIHL 220
Cdd:PLN02605 169 GLEPSQIRVYGLPIRPSFARAVRPKDelRRELGMDEDLPAVLLMGGGEGMGPLEETARA-LGDSLYDKnlgkpigQVVVI 247
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1575849020 221 CGKGK-LDESLK--------NTKGYVqyeyikKELADLFALADIVISRAGANAICELSALKKPNLL 277
Cdd:PLN02605 248 CGRNKkLQSKLEsrdwkipvKVRGFV------TNMEEWMGACDCIITKAGPGTIAEALIRGLPIIL 307
|
|
| |
