|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
1-351 |
4.08e-135 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 389.10 E-value: 4.08e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 1 MTKIAYTGGGTVGHVSVNLSLIPTSIEKGHEAFYIGSKHGIEREMIESQlpNIQYYPISSGKLRRYLSFENAKDVFKVLK 80
Cdd:PRK00726 1 MKKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKA--GIEFHFIPSGGLRRKGSLANLKAPFKLLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 81 GILDARKILKKQKPDLLFSKGGFVSVPVVIAARSLKIPTIIHESDLTPGLANKISLKFAKKIYTTFEDTLAYLPKDKADF 160
Cdd:PRK00726 79 GVLQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 161 VGATVREDLKQGNKERgyQLTDFDKNKKVLLVMGGSLGSKKLNNIIRQNIEALLHDYQIIHLTGKGLVDD--SINKKG-- 236
Cdd:PRK00726 159 TGNPVREEILALAAPP--ARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEALQVIHQTGKGDLEEvrAAYAAGin 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 237 YVQFEFVkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLIPLGLdQSRGDQIDNAKNFESKGYGRHIPEDQLTEVNL 316
Cdd:PRK00726 237 AEVVPFI-DDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPH-AADDHQTANARALVDAGAALLIPQSDLTPEKL 314
|
330 340 350
....*....|....*....|....*....|....*
gi 488388277 317 LQELNDIELHRESiIKQMETYQESYTKEDLFDKII 351
Cdd:PRK00726 315 AEKLLELLSDPER-LEAMAEAARALGKPDAAERLA 348
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-334 |
4.83e-129 |
|
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: 373.70 E-value: 4.83e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 1 MTKIAYTGGGTVGHVSVNLSLIPTSIEKGHEAFYIGSKHGIEREMIESQlpNIQYYPISSGKLRRYLSFENAKDVFKVLK 80
Cdd:COG0707 2 SKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAA--GYPLHTIPVGGLRRKGSLKNLKAPFRLLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 81 GILDARKILKKQKPDLLFSKGGFVSVPVVIAARSLKIPTIIHESDLTPGLANKISLKFAKKIYTTFEDTLAYLPKDKADF 160
Cdd:COG0707 80 ALLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPKKKAVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 161 VGATVREDLKQGNKERGYQLTDFDKNKKVLLVMGGSLGSKKLNNIIRQNIEALL-HDYQIIHLTGKGLVDDSINK----- 234
Cdd:COG0707 160 TGNPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLeARLQVVHQTGKGDYEEVRAAyaaai 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 235 -KGYVQFEFVkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLIPLGLdQSRGDQIDNAKNFESKGYGRHIPEDQLTE 313
Cdd:COG0707 240 rPNAEVFPFI-DDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPH-AADDHQTKNARALVEAGAAVLIPQSELTP 317
|
330 340
....*....|....*....|.
gi 488388277 314 VNLLQELNDIELHRESiIKQM 334
Cdd:COG0707 318 EKLAEALEELLEDPER-LAKM 337
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
3-351 |
1.94e-104 |
|
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: 310.69 E-value: 1.94e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 3 KIAYTGGGTVGHVSVNLSLIPTSIEKGHEAFYIGSKHGIEREMIESQlpNIQYYPISSGKLRRYLSFENAKDVFKVLKGI 82
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEA--GIPFHTIPISGLRRKGSLKNLKAPFKLLKGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 83 LDARKILKKQKPDLLFSKGGFVSVPVVIAARSLKIPTIIHESDLTPGLANKISLKFAKKIYTTFEDTLAYLPKDKADFVG 162
Cdd:cd03785 79 RQARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVVVTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 163 ATVREDLKQGNKERGYQltDFDKNKKVLLVMGGSLGSKKLNNIIRQNIEALLH-DYQIIHLTGKGLVDDSINK-----KG 236
Cdd:cd03785 159 NPVREEILNLRKELKRF--GLPPDKPTLLVFGGSQGARAINRAVPKALPKLLErGIQVIHQTGKGDYDEVKKLyedlgIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 237 YVQFEFVkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLIPLGLdQSRGDQIDNAKNFESKGYGRHIPEDQLTEVNL 316
Cdd:cd03785 237 VKVFPFI-DDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPY-AADDHQEANARALEKAGAAIVIDQEELTPEVL 314
|
330 340 350
....*....|....*....|....*....|....*
gi 488388277 317 LQELNDIELHREsIIKQMETYQESYTKEDLFDKII 351
Cdd:cd03785 315 AEAILDLLNDPE-RLKKMAEAAKKLAKPDAAERIA 348
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
3-350 |
5.72e-84 |
|
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: 258.37 E-value: 5.72e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 3 KIAYTGGGTVGHVSVNLSLIPTSIEKGHEAFYIGSKHGIEREMIESQlpNIQYYPISSGKLRRYLSFENAKDVFKVLKGI 82
Cdd:TIGR01133 2 KIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKA--GIEFYFIPVGGLRRKGSKKLLKTPLKLLKAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 83 LDARKILKKQKPDLLFSKGGFVSVPVVIAARSLKIPTIIHESDLTPGLANKISLKFAKKIYTTFEDTLAYLpkdKADFVG 162
Cdd:TIGR01133 80 FKARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDHF---EAVLVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 163 ATVREDLKQGNKERGyQLTdFDKNKKVLLVMGGSLGSKKLNNIIRQNIEAL-LHDYQIIHLTGKGLVD---DSINKKGYV 238
Cdd:TIGR01133 157 NPVRKEIRSLPVPRE-RFG-RREGKPTILVLGGSQGAKILNELVPKALAKLqEKGIQIVHQGGKGDLEkvkNVYQELGQE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 239 QF-EFVKDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLIPlgLDQSRGDQIDNAKNFESKGYGRHIPEDQLTEVNLL 317
Cdd:TIGR01133 235 KIvTFIDENMAAAYAAADLVISRAGASTVAELAAAGVPAILIP--YPYAADDQYYNAKFLEDLGAGLVIRQKELLPEKLL 312
|
330 340 350
....*....|....*....|....*....|....*.
gi 488388277 318 QELNDIELHR---ESIIKQMETYQESYTKEDLFDKI 350
Cdd:TIGR01133 313 EALLKLLLDPanlENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
4-144 |
1.83e-46 |
|
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.
Pssm-ID: 427107 [Multi-domain] Cd Length: 139 Bit Score: 154.75 E-value: 1.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 4 IAYTGGGTVGHVSVNLSLIPTSIEKGHEAFYIGSKHGIEREMIESQlpNIQYYPISSGKLRRYLSFENAKDVFKVLKGIL 83
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKA--GIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488388277 84 DARKILKKQKPDLLFSKGGFVSVPVVIAARSLKIPTIIHESDLTPGLANKISLKFAKKIYT 144
Cdd:pfam03033 79 KAFRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
1-351 |
4.08e-135 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 389.10 E-value: 4.08e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 1 MTKIAYTGGGTVGHVSVNLSLIPTSIEKGHEAFYIGSKHGIEREMIESQlpNIQYYPISSGKLRRYLSFENAKDVFKVLK 80
Cdd:PRK00726 1 MKKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKA--GIEFHFIPSGGLRRKGSLANLKAPFKLLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 81 GILDARKILKKQKPDLLFSKGGFVSVPVVIAARSLKIPTIIHESDLTPGLANKISLKFAKKIYTTFEDTLAYLPKDKADF 160
Cdd:PRK00726 79 GVLQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 161 VGATVREDLKQGNKERgyQLTDFDKNKKVLLVMGGSLGSKKLNNIIRQNIEALLHDYQIIHLTGKGLVDD--SINKKG-- 236
Cdd:PRK00726 159 TGNPVREEILALAAPP--ARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEALQVIHQTGKGDLEEvrAAYAAGin 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 237 YVQFEFVkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLIPLGLdQSRGDQIDNAKNFESKGYGRHIPEDQLTEVNL 316
Cdd:PRK00726 237 AEVVPFI-DDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPH-AADDHQTANARALVDAGAALLIPQSDLTPEKL 314
|
330 340 350
....*....|....*....|....*....|....*
gi 488388277 317 LQELNDIELHRESiIKQMETYQESYTKEDLFDKII 351
Cdd:PRK00726 315 AEKLLELLSDPER-LEAMAEAARALGKPDAAERLA 348
|
|
| PRK12446 |
PRK12446 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
1-350 |
1.22e-129 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
Pssm-ID: 171505 [Multi-domain] Cd Length: 352 Bit Score: 374.96 E-value: 1.22e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 1 MTKIAYTGGGTVGHVSVNLSLIPTSIEKGHEAFYIGSKHGIEREMIESQlpNIQYYPISSGKLRRYLSFENAKDVFKVLK 80
Cdd:PRK12446 1 MKKIVFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKE--NIPYYSISSGKLRRYFDLKNIKDPFLVMK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 81 GILDARKILKKQKPDLLFSKGGFVSVPVVIAARSLKIPTIIHESDLTPGLANKISLKFAKKIYTTFEDTLAYLPKDKADF 160
Cdd:PRK12446 79 GVMDAYVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAAKHLPKEKVIY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 161 VGATVREDLKQGNKERGYQLTDFDKNKKVLLVMGGSLGSKKLNNIIRQNIEALLHDYQIIHLTGKGLVDDSI-NKKGYVQ 239
Cdd:PRK12446 159 TGSPVREEVLKGNREKGLAFLGFSRKKPVITIMGGSLGAKKINETVREALPELLLKYQIVHLCGKGNLDDSLqNKEGYRQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 240 FEFVKDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLIPLGLDQSRGDQIDNAKNFESKGYGRHIPEDQLTEVNLLQE 319
Cdd:PRK12446 239 FEYVHGELPDILAITDFVISRAGSNAIFEFLTLQKPMLLIPLSKFASRGDQILNAESFERQGYASVLYEEDVTVNSLIKH 318
|
330 340 350
....*....|....*....|....*....|.
gi 488388277 320 LNDIELHRESIIKQMETYQESYTKEDLFDKI 350
Cdd:PRK12446 319 VEELSHNNEKYKTALKKYNGKEAIQTIIDHI 349
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-334 |
4.83e-129 |
|
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: 373.70 E-value: 4.83e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 1 MTKIAYTGGGTVGHVSVNLSLIPTSIEKGHEAFYIGSKHGIEREMIESQlpNIQYYPISSGKLRRYLSFENAKDVFKVLK 80
Cdd:COG0707 2 SKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAA--GYPLHTIPVGGLRRKGSLKNLKAPFRLLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 81 GILDARKILKKQKPDLLFSKGGFVSVPVVIAARSLKIPTIIHESDLTPGLANKISLKFAKKIYTTFEDTLAYLPKDKADF 160
Cdd:COG0707 80 ALLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPKKKAVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 161 VGATVREDLKQGNKERGYQLTDFDKNKKVLLVMGGSLGSKKLNNIIRQNIEALL-HDYQIIHLTGKGLVDDSINK----- 234
Cdd:COG0707 160 TGNPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLeARLQVVHQTGKGDYEEVRAAyaaai 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 235 -KGYVQFEFVkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLIPLGLdQSRGDQIDNAKNFESKGYGRHIPEDQLTE 313
Cdd:COG0707 240 rPNAEVFPFI-DDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPH-AADDHQTKNARALVEAGAAVLIPQSELTP 317
|
330 340
....*....|....*....|.
gi 488388277 314 VNLLQELNDIELHRESiIKQM 334
Cdd:COG0707 318 EKLAEALEELLEDPER-LAKM 337
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
3-351 |
1.94e-104 |
|
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: 310.69 E-value: 1.94e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 3 KIAYTGGGTVGHVSVNLSLIPTSIEKGHEAFYIGSKHGIEREMIESQlpNIQYYPISSGKLRRYLSFENAKDVFKVLKGI 82
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEA--GIPFHTIPISGLRRKGSLKNLKAPFKLLKGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 83 LDARKILKKQKPDLLFSKGGFVSVPVVIAARSLKIPTIIHESDLTPGLANKISLKFAKKIYTTFEDTLAYLPKDKADFVG 162
Cdd:cd03785 79 RQARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVVVTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 163 ATVREDLKQGNKERGYQltDFDKNKKVLLVMGGSLGSKKLNNIIRQNIEALLH-DYQIIHLTGKGLVDDSINK-----KG 236
Cdd:cd03785 159 NPVREEILNLRKELKRF--GLPPDKPTLLVFGGSQGARAINRAVPKALPKLLErGIQVIHQTGKGDYDEVKKLyedlgIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 237 YVQFEFVkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLIPLGLdQSRGDQIDNAKNFESKGYGRHIPEDQLTEVNL 316
Cdd:cd03785 237 VKVFPFI-DDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPY-AADDHQEANARALEKAGAAIVIDQEELTPEVL 314
|
330 340 350
....*....|....*....|....*....|....*
gi 488388277 317 LQELNDIELHREsIIKQMETYQESYTKEDLFDKII 351
Cdd:cd03785 315 AEAILDLLNDPE-RLKKMAEAAKKLAKPDAAERIA 348
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
3-350 |
5.72e-84 |
|
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: 258.37 E-value: 5.72e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 3 KIAYTGGGTVGHVSVNLSLIPTSIEKGHEAFYIGSKHGIEREMIESQlpNIQYYPISSGKLRRYLSFENAKDVFKVLKGI 82
Cdd:TIGR01133 2 KIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKA--GIEFYFIPVGGLRRKGSKKLLKTPLKLLKAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 83 LDARKILKKQKPDLLFSKGGFVSVPVVIAARSLKIPTIIHESDLTPGLANKISLKFAKKIYTTFEDTLAYLpkdKADFVG 162
Cdd:TIGR01133 80 FKARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDHF---EAVLVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 163 ATVREDLKQGNKERGyQLTdFDKNKKVLLVMGGSLGSKKLNNIIRQNIEAL-LHDYQIIHLTGKGLVD---DSINKKGYV 238
Cdd:TIGR01133 157 NPVRKEIRSLPVPRE-RFG-RREGKPTILVLGGSQGAKILNELVPKALAKLqEKGIQIVHQGGKGDLEkvkNVYQELGQE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 239 QF-EFVKDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLIPlgLDQSRGDQIDNAKNFESKGYGRHIPEDQLTEVNLL 317
Cdd:TIGR01133 235 KIvTFIDENMAAAYAAADLVISRAGASTVAELAAAGVPAILIP--YPYAADDQYYNAKFLEDLGAGLVIRQKELLPEKLL 312
|
330 340 350
....*....|....*....|....*....|....*.
gi 488388277 318 QELNDIELHR---ESIIKQMETYQESYTKEDLFDKI 350
Cdd:TIGR01133 313 EALLKLLLDPanlENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
4-144 |
1.83e-46 |
|
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.
Pssm-ID: 427107 [Multi-domain] Cd Length: 139 Bit Score: 154.75 E-value: 1.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 4 IAYTGGGTVGHVSVNLSLIPTSIEKGHEAFYIGSKHGIEREMIESQlpNIQYYPISSGKLRRYLSFENAKDVFKVLKGIL 83
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKA--GIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488388277 84 DARKILKKQKPDLLFSKGGFVSVPVVIAARSLKIPTIIHESDLTPGLANKISLKFAKKIYT 144
Cdd:pfam03033 79 KAFRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
189-330 |
1.13e-23 |
|
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: 95.86 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 189 VLLVMGGSLGSKKLNNIIRQN--IEALLHDYQIIHLTGKGLVDD-----SINKKGYVQFEFvKDDLTDLLAITDTVISRA 261
Cdd:pfam04101 1 TILVTGGSQGARALNELVLSVlpLLELKGELQVLHQTGKGDLEEvkidyAELGINYEVFPF-IDNMAEYIKAADLVISRA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488388277 262 GSNAIYEFLTLRIPMLLIPLGlDQSRGDQIDNAKNFESKGYGRHIPEDQLTEVNLLQELNDIELHRESI 330
Cdd:pfam04101 80 GAGTIAELLALGKPAILVPNP-SAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALLKLLLNPLRL 147
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
182-356 |
1.88e-12 |
|
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: 67.73 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 182 DFDKNKKVLLVMGGSLGSKKLNNIIrQNIEALLHDYQIIHLTGK---------GLVDDSINKK--GYVqfefvkDDLTDL 250
Cdd:cd17507 192 NLSPDKPTVLLMGGGGGMGPVKETV-EALLDSLRAGQVLVVCGKnkklyeklsGLEEDYINVRvlGYV------DDMNEL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 251 LAITDTVISRAGSNAIYEFLTLRIPMLLI-PLGldqsrGDQIDNAKNFESKGYGRHI--PEDQLTEVNLLqeLNDIELHR 327
Cdd:cd17507 265 MAASDLVITKPGGLTISEALARGLPVIIYdPIP-----GQEEENADFLENNGAGIIArdPEELLEIVARL--IDPPSLLR 337
|
170 180
....*....|....*....|....*....
gi 488388277 328 ESIIKQMETYQESYtkedlfDKIIHDALN 356
Cdd:cd17507 338 MMSEAAKELKPPAA------AKVIADILS 360
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
93-323 |
3.72e-10 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 59.87 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 93 KPDLLFSkgGFVSVPVVIAARSLKIPTIIhesdLTPGlankislkfakkiytTFEDTLAYLPkDKADFVGATVREdlkqG 172
Cdd:COG1819 53 RPDLVVS--DPLALAAALAAEALGIPVVS----LTPP---------------ELEYPRPPDP-ANVRFVGPLLPD----G 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 173 NKERGYQLTDFDKNKKVLLVMGGSLGSKKlnNIIRQNIEAL-LHDYQIIHLTGKGLVDDSINKKGYVQF-EFVkdDLTDL 250
Cdd:COG1819 107 PAELPPWLEEDAGRPLVYVTLGTSANDRA--DLLRAVLEALaDLGVRVVVTTGGLDPAELGPLPDNVRVvDYV--PQDAL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488388277 251 LAITDTVISRAGSNAIYEFLTLRIPMLLIPLGldqsrGDQIDNAKNFESKGYGRHIPEDQLTEVNLLQELNDI 323
Cdd:COG1819 183 LPRADAVVHHGGAGTTAEALRAGVPQVVVPFG-----GDQPLNAARVERLGAGLALPPRRLTAEALRAALRRL 250
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
13-316 |
1.38e-07 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 52.94 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 13 GHVSVNLSLIPTSIEKGHEAFYIGSKHGIeREMIESqlPNIQYYPISSG----------KLRRYLSFENAKDVFKVLKGI 82
Cdd:cd03784 12 GHVNPMLPLAKALAARGHEVTVATPPFNF-ADLVEA--AGLTFVPVGDDpdeleldsetNLGPDSLLELLRRLLKAADEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 83 LDA--RKILKKQKPDLLFSkgGFVSVPVVIAARSLKIPTIIH------------------ESDLTPGLANKISLKFAKKI 142
Cdd:cd03784 89 LDDllAALRSSWKPDLVIA--DPFAYAGPLVAEELGIPSVRLftgpatllsaylhpfgvlNLLLSSLLEPELFLDPLLEV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 143 YTTFEDTLAYLPKDKADFVGATVREDLKQGN-------------------------KERGYQLTDFDKNKK---VLLVMG 194
Cdd:cd03784 167 LDRLRERLGLPPFSLVLLLLRLVPPLYVIGPtfpslppdrprlpsvlgglrivpknGPLPDELWEWLDKQPprsVVYVSF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 195 GSLGSKKLNNIIRQNIEALLH-DYQIIHLTGKGLVDDSINKKGYVqfeFVKDDL--TDLLA--ITDTVISRAGSNAIYEF 269
Cdd:cd03784 247 GSMVRDLPEELLELIAEALASlGQRFLWVVGPDPLGGLERLPDNV---LVVKWVpqDELLAhpAVGAFVTHGGWNSTLEA 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 488388277 270 LTLRIPMLLIPLGldqsrGDQIDNAKNFESKGYGRHIPEDQLTEVNL 316
Cdd:cd03784 324 LYAGVPMVVVPLF-----ADQPNNAARVEELGAGVELDKDELTAEEL 365
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
13-316 |
2.77e-07 |
|
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) subfamily of the UDP-glucuronosyltransferase family. Members include a number of glucosyl transferases for macrolide antibiotic inactivation, but also include transferases of glucose-related sugars for macrolide antibiotic production. [Cellular processes, Toxin production and resistance]
Pssm-ID: 273616 [Multi-domain] Cd Length: 392 Bit Score: 51.99 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 13 GHVSVNLSLIPTSIEKGHEAFYigskhGIEREM---IESQLPNIQYYP--ISSGKLRRYLSFEN--------AKDVFKVL 79
Cdd:TIGR01426 7 GHVNPTLGVVEELVARGHRVTY-----ATTEEFaerVEAAGAEFVLYGsaLPPPDNPPENTEEEpidiieklLDEAEDVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 80 KGILDArkiLKKQKPDLLFSKggFVSVPVVIAARSLKIPTII----------HESD---LTPGLANKIS----------- 135
Cdd:TIGR01426 82 PQLEEA---YKGDRPDLIVYD--IASWTGRLLARKWDVPVISsfptfaaneeFEEMvspAGEGSAEEGAiaerglaeyva 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 136 --LKFAKKIYTTFEDT-----------LAYLPK----------DKADFVGATVREDLKQGNKERGyqltdfDKNKKVLLV 192
Cdd:TIGR01426 157 rlSALLEEHGITTPPVeflaaprrdlnLVYTPKafqpagetfdDSFTFVGPCIGDRKEDGSWERP------GDGRPVVLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 193 mggSLGS--KKLNNIIRQNIEALLH-DYQIIHLTGKGLVDDSINK--KGYVQFEFVKddLTDLLAITDTVISRAGSNAIY 267
Cdd:TIGR01426 231 ---SLGTvfNNQPSFYRTCVEAFRDlDWHVVLSVGRGVDPADLGElpPNVEVRQWVP--QLEILKKADAFITHGGMNSTM 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488388277 268 EFLTLRIPMLLIPLGLDQSRgdqidNAKNFESKGYGRHIPEDQLTEVNL 316
Cdd:TIGR01426 306 EALFNGVPMVAVPQGADQPM-----TARRIAELGLGRHLPPEEVTAEKL 349
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
86-355 |
4.68e-07 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 51.26 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 86 RKILKKQKPDLLFSKGGFVSVPVVIAARSLKIPT--IIHESDLtpglaNKISLKFAKKIYTTFEDTLAY------LPKDK 157
Cdd:PRK13609 97 KLLLQAEKPDIVINTFPIIAVPELKKQTGISIPTynVLTDFCL-----HKIWVHREVDRYFVATDHVKKvlvdigVPPEQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 158 ADFVGATVREDLKQG-NKERGYQLTDFDKNKKVLLVMGGSLGSkkLNNiIRQNIEALLHD--YQIIHLTGKG------LV 228
Cdd:PRK13609 172 VVETGIPIRSSFELKiNPDIIYNKYQLCPNKKILLIMAGAHGV--LGN-VKELCQSLMSVpdLQVVVVCGKNealkqsLE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 229 D------DSINKKGYVqfefvkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLL---IPlgldqsrGDQIDNAKNFES 299
Cdd:PRK13609 249 DlqetnpDALKVFGYV------ENIDELFRVTSCMITKPGGITLSEAAALGVPVILykpVP-------GQEKENAMYFER 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 488388277 300 KGYGRHI--PEDQLTEV-NLLQelNDIELHresiikQMETYQESYTKEDLFDKIIHDAL 355
Cdd:PRK13609 316 KGAAVVIrdDEEVFAKTeALLQ--DDMKLL------QMKEAMKSLYLPEPADHIVDDIL 366
|
|
| PRK13608 |
PRK13608 |
diacylglycerol glucosyltransferase; Provisional |
88-356 |
1.66e-06 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 184179 [Multi-domain] Cd Length: 391 Bit Score: 49.41 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 88 ILKKQKPDLLFSKGGFVSVPVVIAARSLKIP--TII-----HESDLTPglankislkFAKKIYTTFEDTLAYL-----PK 155
Cdd:PRK13608 99 LLIKEKPDLILLTFPTPVMSVLTEQFNINIPvaTVMtdyrlHKNWITP---------YSTRYYVATKETKQDFidvgiDP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 156 DKADFVGATVREDLKQG-NKERGYQLTDFDKNKKVLLVMGGSLG-SKKLNNIIRQNIEALLHdYQIIHLTGKglvddSIN 233
Cdd:PRK13608 170 STVKVTGIPIDNKFETPiDQKQWLIDNNLDPDKQTILMSAGAFGvSKGFDTMITDILAKSAN-AQVVMICGK-----SKE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 234 KKGYVQFEFVKDD----------LTDLLAITDTVISRAGSNAIYEFLTLRIPMLLiplgLDQSRGDQIDNAKNFESKGYG 303
Cdd:PRK13608 244 LKRSLTAKFKSNEnvlilgytkhMNEWMASSQLMITKPGGITISEGLARCIPMIF----LNPAPGQELENALYFEEKGFG 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 488388277 304 R--HIPEDQLTEVNLLqelndieLHRESIIKQM-ETYQESYTKEDLFdKIIHDALN 356
Cdd:PRK13608 320 KiaDTPEEAIKIVASL-------TNGNEQLTNMiSTMEQDKIKYATQ-TICRDLLD 367
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
3-122 |
3.56e-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: 48.36 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 3 KIAYTGGGTVGHVSVNLSLIPTSIEKGHEAFYIGSKHGIEREMIESQlpNIQYYPISSgkLRRYLSFenakdvFKVLKGI 82
Cdd:cd03808 1 KILFIVNVDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKEL--GVKVIDIPI--LRRGINP------LKDLKAL 70
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 488388277 83 LDARKILKKQKPDLL---FSKGGFVSvpvVIAARSLKIPTIIH 122
Cdd:cd03808 71 FKLYKLLKKEKPDIVhchTPKPGILG---RLAARLAGVPKVIY 110
|
|
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
249-332 |
3.81e-05 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 45.48 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388277 249 DLLA--ITDTVISRAGSNAIYEFLTLRIPMLLIPLgldqsRGDQIDNAKNFESKGYGRHIPEDQLTE---VNLLQELNDI 323
Cdd:pfam00201 334 DLLGhpKTRAFITHAGSNGVYEAICHGVPMVGMPL-----FGDQMDNAKHMEAKGAAVTLNVLTMTSedlLNALKEVIND 408
|
....*....
gi 488388277 324 ELHRESIIK 332
Cdd:pfam00201 409 PSYKENIMR 417
|
|
| COG4671 |
COG4671 |
Predicted glycosyl transferase [General function prediction only]; |
245-312 |
7.79e-03 |
|
Predicted glycosyl transferase [General function prediction only];
Pssm-ID: 443708 [Multi-domain] Cd Length: 391 Bit Score: 37.91 E-value: 7.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488388277 245 DDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLIPlgLDQSRGDQIDNAKNFESKGYGRHIPEDQLT 312
Cdd:COG4671 283 PDFEALLAAADLSVSMGGYNTVCEILSTGKPALIVP--RTAPRTEQLIRAERLAELGLVDVLHPEDLT 348
|
|
| |
