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Conserved domains on  [gi|1838886163|emb|CAB3777647|]
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UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase [Pararobbsia alpina]

Protein Classification

UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase( domain architecture ID 11479176)

UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase catalyzes the last step in the intracellular phase of peptidoglycan biosynthesis

EC:  2.4.1.227
Gene Ontology:  GO:0051991|GO:0008360|GO:0050511|GO:0051301|GO:0071555|GO:0030259|GO:0009252|GO:0005975|GO:0007049|GO:0005886
PubMed:  12455415|11699883

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
murG PRK00726
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
 5-348 1.39e-169

undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional


:

Pssm-ID: 234825 [Multi-domain]  Cd Length: 357  Bit Score: 476.55  E-value: 1.39e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163   5 RTLMVMAGGTGGHVFPGLAVAHWMQAHGWRVVWLGNPGGMEATLVPKHGIPIEFVRFGGLRGKGLMTKLRLPFNLLRACS 84
Cdd:PRK00726    2 KKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163  85 QSLGVLGRIKPDVVLGMGGYITFPAGIMAALTGRPLVLHEQNSIAGLANRVLAKLAKRVLVAFPDAL-----PGGEWTGN 159
Cdd:PRK00726   82 QARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFpeffkPKAVVTGN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 160 PIREELRDMPEPAGRYAARTGPLKLLVVGGSLGAAALNEAVPLALARLPAGsrPHVVHQAGAKHIGALKTYYENAgldhd 239
Cdd:PRK00726  162 PVREEILALAAPPARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEA--LQVIHQTGKGDLEEVRAAYAAG----- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 240 PDIRLVPFIDDMASAYAQADLVICRSGAMTVAEIAAVGVAALFVPFPYAVDDHQTTNGRFLADRGGALLIQQRELTVEGL 319
Cdd:PRK00726  235 INAEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEKL 314

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1838886163 320 ADWIGA--QTRESLAAMAARARECAKPDATE 348
Cdd:PRK00726  315 AEKLLEllSDPERLEAMAEAARALGKPDAAE 345
 
Name Accession Description Interval E-value
murG PRK00726
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
 5-348 1.39e-169

undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional


Pssm-ID: 234825 [Multi-domain]  Cd Length: 357  Bit Score: 476.55  E-value: 1.39e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163   5 RTLMVMAGGTGGHVFPGLAVAHWMQAHGWRVVWLGNPGGMEATLVPKHGIPIEFVRFGGLRGKGLMTKLRLPFNLLRACS 84
Cdd:PRK00726    2 KKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163  85 QSLGVLGRIKPDVVLGMGGYITFPAGIMAALTGRPLVLHEQNSIAGLANRVLAKLAKRVLVAFPDAL-----PGGEWTGN 159
Cdd:PRK00726   82 QARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFpeffkPKAVVTGN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 160 PIREELRDMPEPAGRYAARTGPLKLLVVGGSLGAAALNEAVPLALARLPAGsrPHVVHQAGAKHIGALKTYYENAgldhd 239
Cdd:PRK00726  162 PVREEILALAAPPARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEA--LQVIHQTGKGDLEEVRAAYAAG----- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 240 PDIRLVPFIDDMASAYAQADLVICRSGAMTVAEIAAVGVAALFVPFPYAVDDHQTTNGRFLADRGGALLIQQRELTVEGL 319
Cdd:PRK00726  235 INAEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEKL 314

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1838886163 320 ADWIGA--QTRESLAAMAARARECAKPDATE 348
Cdd:PRK00726  315 AEKLLEllSDPERLEAMAEAARALGKPDAAE 345
MurG COG0707
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ...
 4-348 4.64e-168

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: 473.08  E-value: 4.64e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163   4 ARTLMVMAGGTGGHVFPGLAVAHWMQAHGWRVVWLGNPGGMEATLVPKHGIPIEFVRFGGLRGKGLMTKLRLPFNLLRAC 83
Cdd:COG0707     2 SKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163  84 SQSLGVLGRIKPDVVLGMGGYITFPAGIMAALTGRPLVLHEQNSIAGLANRVLAKLAKRVLVAFPDAL-----PGGEWTG 158
Cdd:COG0707    82 LQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKkyfpkKKAVVTG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 159 NPIREELRDMPEPAGR--YAARTGPLKLLVVGGSLGAAALNEAVPLALARLPAgSRPHVVHQAGAKHIGALKTYYENAGL 236
Cdd:COG0707   162 NPVRKEILELDRPEARakLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLE-ARLQVVHQTGKGDYEEVRAAYAAAIR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 237 dhdPDIRLVPFIDDMASAYAQADLVICRSGAMTVAEIAAVGVAALFVPFPYAVDDHQTTNGRFLADRGGALLIQQRELTV 316
Cdd:COG0707   241 ---PNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTP 317

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1838886163 317 EGLADWIG--AQTRESLAAMAARARECAKPDATE 348
Cdd:COG0707   318 EKLAEALEelLEDPERLAKMAEAARALARPDAAE 351
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
 7-348 1.88e-139

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: 400.05  E-value: 1.88e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163   7 LMVMAGGTGGHVFPGLAVAHWMQAHGWRVVWLGNPGGMEATLVPKHGIPIEFVRFGGLRGKGLMTKLRLPFNLLRACSQS 86
Cdd:cd03785     2 ILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163  87 LGVLGRIKPDVVLGMGGYITFPAGIMAALTGRPLVLHEQNSIAGLANRVLAKLAKRVLVAFPDA-----LPGGEWTGNPI 161
Cdd:cd03785    82 RKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETkkyfpAAKVVVTGNPV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 162 REELRDMPEPAGRYAARTGPLKLLVVGGSLGAAALNEAVPLALARLPAGsRPHVVHQAGAKHIGALKTYYENAGldhdPD 241
Cdd:cd03785   162 REEILNLRKELKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLER-GIQVIHQTGKGDYDEVKKLYEDLG----IN 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 242 IRLVPFIDDMASAYAQADLVICRSGAMTVAEIAAVGVAALFVPFPYAVDDHQTTNGRFLADRGGALLIQQRELTVEGLAD 321
Cdd:cd03785   237 VKVFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVLAE 316

                         330       340
                  ....*....|....*....|....*....
gi 1838886163 322 WIGA--QTRESLAAMAARARECAKPDATE 348
Cdd:cd03785   317 AILDllNDPERLKKMAEAAKKLAKPDAAE 345
murG TIGR01133
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ...
 5-348 1.10e-127

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: 370.08  E-value: 1.10e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163   5 RTLMVMAGGTGGHVFPGLAVAHWMQAHGWRVVWLGNPGGMEATLVPKHGIPIEFVRFGGLRGKGLMTKLRLPFNLLRACS 84
Cdd:TIGR01133   1 KKIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163  85 QSLGVLGRIKPDVVLGMGGYITFPAGIMAALTGRPLVLHEQNSIAGLANRVLAKLAKRVLVAFPDA--LPGGEWTGNPIR 162
Cdd:TIGR01133  81 KARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAkdHFEAVLVGNPVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 163 EELRDMPEPAGRYAARTGPLKLLVVGGSLGAAALNEAVPLALARLPAGSRPhVVHQAGAKHIGALKTYYENAGLDHdpdi 242
Cdd:TIGR01133 161 KEIRSLPVPRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKGIQ-IVHQGGKGDLEKVKNVYQELGQEK---- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 243 rLVPFID-DMASAYAQADLVICRSGAMTVAEIAAVGVAALFVPFPYAvDDHQTTNGRFLADRGGALLIQQRELTVEGLAD 321
Cdd:TIGR01133 236 -IVTFIDeNMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPEKLLE 313

                         330       340
                  ....*....|....*....|....*....
gi 1838886163 322 WIG--AQTRESLAAMAARARECAKPDATE 348
Cdd:TIGR01133 314 ALLklLLDPANLENMAEAARKLAKPDAAK 342
Glyco_tran_28_C pfam04101
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ...
 184-348 5.57e-44

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: 149.40  E-value: 5.57e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 184 LLVVGGSLGAAALNEAVPLALARLPAGSRPHVVHQAGAKHIGALKTYYENAGLDHDPdirlVPFIDDMASAYAQADLVIC 263
Cdd:pfam04101   2 ILVTGGSQGARALNELVLSVLPLLELKGELQVLHQTGKGDLEEVKIDYAELGINYEV----FPFIDNMAEYIKAADLVIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 264 RSGAMTVAEIAAVGVAALFVPFPYAVDDHQTTNGRFLADRGGALLIQQRELTVEGLADWI--GAQTRESLAAMAARAREC 341
Cdd:pfam04101  78 RAGAGTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALlkLLLNPLRLAEMAKASKAS 157


                  ....*..
gi 1838886163 342 AKPDATE 348
Cdd:pfam04101 158 GFKDAAK 164
 
Name Accession Description Interval E-value
murG PRK00726
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
 5-348 1.39e-169

undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional


Pssm-ID: 234825 [Multi-domain]  Cd Length: 357  Bit Score: 476.55  E-value: 1.39e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163   5 RTLMVMAGGTGGHVFPGLAVAHWMQAHGWRVVWLGNPGGMEATLVPKHGIPIEFVRFGGLRGKGLMTKLRLPFNLLRACS 84
Cdd:PRK00726    2 KKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163  85 QSLGVLGRIKPDVVLGMGGYITFPAGIMAALTGRPLVLHEQNSIAGLANRVLAKLAKRVLVAFPDAL-----PGGEWTGN 159
Cdd:PRK00726   82 QARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFpeffkPKAVVTGN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 160 PIREELRDMPEPAGRYAARTGPLKLLVVGGSLGAAALNEAVPLALARLPAGsrPHVVHQAGAKHIGALKTYYENAgldhd 239
Cdd:PRK00726  162 PVREEILALAAPPARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEA--LQVIHQTGKGDLEEVRAAYAAG----- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 240 PDIRLVPFIDDMASAYAQADLVICRSGAMTVAEIAAVGVAALFVPFPYAVDDHQTTNGRFLADRGGALLIQQRELTVEGL 319
Cdd:PRK00726  235 INAEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEKL 314

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1838886163 320 ADWIGA--QTRESLAAMAARARECAKPDATE 348
Cdd:PRK00726  315 AEKLLEllSDPERLEAMAEAARALGKPDAAE 345
MurG COG0707
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ...
 4-348 4.64e-168

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: 473.08  E-value: 4.64e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163   4 ARTLMVMAGGTGGHVFPGLAVAHWMQAHGWRVVWLGNPGGMEATLVPKHGIPIEFVRFGGLRGKGLMTKLRLPFNLLRAC 83
Cdd:COG0707     2 SKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163  84 SQSLGVLGRIKPDVVLGMGGYITFPAGIMAALTGRPLVLHEQNSIAGLANRVLAKLAKRVLVAFPDAL-----PGGEWTG 158
Cdd:COG0707    82 LQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKkyfpkKKAVVTG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 159 NPIREELRDMPEPAGR--YAARTGPLKLLVVGGSLGAAALNEAVPLALARLPAgSRPHVVHQAGAKHIGALKTYYENAGL 236
Cdd:COG0707   162 NPVRKEILELDRPEARakLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLE-ARLQVVHQTGKGDYEEVRAAYAAAIR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 237 dhdPDIRLVPFIDDMASAYAQADLVICRSGAMTVAEIAAVGVAALFVPFPYAVDDHQTTNGRFLADRGGALLIQQRELTV 316
Cdd:COG0707   241 ---PNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTP 317

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1838886163 317 EGLADWIG--AQTRESLAAMAARARECAKPDATE 348
Cdd:COG0707   318 EKLAEALEelLEDPERLAKMAEAARALARPDAAE 351
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
 7-348 1.88e-139

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: 400.05  E-value: 1.88e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163   7 LMVMAGGTGGHVFPGLAVAHWMQAHGWRVVWLGNPGGMEATLVPKHGIPIEFVRFGGLRGKGLMTKLRLPFNLLRACSQS 86
Cdd:cd03785     2 ILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163  87 LGVLGRIKPDVVLGMGGYITFPAGIMAALTGRPLVLHEQNSIAGLANRVLAKLAKRVLVAFPDA-----LPGGEWTGNPI 161
Cdd:cd03785    82 RKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETkkyfpAAKVVVTGNPV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 162 REELRDMPEPAGRYAARTGPLKLLVVGGSLGAAALNEAVPLALARLPAGsRPHVVHQAGAKHIGALKTYYENAGldhdPD 241
Cdd:cd03785   162 REEILNLRKELKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLER-GIQVIHQTGKGDYDEVKKLYEDLG----IN 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 242 IRLVPFIDDMASAYAQADLVICRSGAMTVAEIAAVGVAALFVPFPYAVDDHQTTNGRFLADRGGALLIQQRELTVEGLAD 321
Cdd:cd03785   237 VKVFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVLAE 316

                         330       340
                  ....*....|....*....|....*....
gi 1838886163 322 WIGA--QTRESLAAMAARARECAKPDATE 348
Cdd:cd03785   317 AILDllNDPERLKKMAEAAKKLAKPDAAE 345
murG TIGR01133
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ...
 5-348 1.10e-127

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: 370.08  E-value: 1.10e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163   5 RTLMVMAGGTGGHVFPGLAVAHWMQAHGWRVVWLGNPGGMEATLVPKHGIPIEFVRFGGLRGKGLMTKLRLPFNLLRACS 84
Cdd:TIGR01133   1 KKIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163  85 QSLGVLGRIKPDVVLGMGGYITFPAGIMAALTGRPLVLHEQNSIAGLANRVLAKLAKRVLVAFPDA--LPGGEWTGNPIR 162
Cdd:TIGR01133  81 KARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAkdHFEAVLVGNPVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 163 EELRDMPEPAGRYAARTGPLKLLVVGGSLGAAALNEAVPLALARLPAGSRPhVVHQAGAKHIGALKTYYENAGLDHdpdi 242
Cdd:TIGR01133 161 KEIRSLPVPRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKGIQ-IVHQGGKGDLEKVKNVYQELGQEK---- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 243 rLVPFID-DMASAYAQADLVICRSGAMTVAEIAAVGVAALFVPFPYAvDDHQTTNGRFLADRGGALLIQQRELTVEGLAD 321
Cdd:TIGR01133 236 -IVTFIDeNMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPEKLLE 313

                         330       340
                  ....*....|....*....|....*....
gi 1838886163 322 WIG--AQTRESLAAMAARARECAKPDATE 348
Cdd:TIGR01133 314 ALLklLLDPANLENMAEAARKLAKPDAAK 342
Glyco_tran_28_C pfam04101
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ...
 184-348 5.57e-44

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: 149.40  E-value: 5.57e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 184 LLVVGGSLGAAALNEAVPLALARLPAGSRPHVVHQAGAKHIGALKTYYENAGLDHDPdirlVPFIDDMASAYAQADLVIC 263
Cdd:pfam04101   2 ILVTGGSQGARALNELVLSVLPLLELKGELQVLHQTGKGDLEEVKIDYAELGINYEV----FPFIDNMAEYIKAADLVIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 264 RSGAMTVAEIAAVGVAALFVPFPYAVDDHQTTNGRFLADRGGALLIQQRELTVEGLADWI--GAQTRESLAAMAARAREC 341
Cdd:pfam04101  78 RAGAGTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALlkLLLNPLRLAEMAKASKAS 157


                  ....*..
gi 1838886163 342 AKPDATE 348
Cdd:pfam04101 158 GFKDAAK 164
Glyco_transf_28 pfam03033
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ...
 7-145 1.61e-39

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: 137.03  E-value: 1.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163   7 LMVMAGGTGGHVFPGLAVAHWMQAHGWRVVWLGNPGGMEATLVPKHGIPIEFVRFGGLRGKGLMTKLRLPFNLLRACSQS 86
Cdd:pfam03033   1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1838886163  87 LGVLGRIKPDVVLGMGGYITFPAGIMAALTGRPLVLHEQNSIAGLANRVLAKLAKRVLV 145
Cdd:pfam03033  81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
PRK12446 PRK12446
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
 5-323 1.25e-36

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed


Pssm-ID: 171505 [Multi-domain]  Cd Length: 352  Bit Score: 135.76  E-value: 1.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163   5 RTLMVMAGGTGGHVFPGLAVAHWMQAHGWRVVWLGNPGGMEATLVPKHGIPIEFVRFGGLRGKGLMTKLRLPFNLLRACS 84
Cdd:PRK12446    2 KKIVFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGVM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163  85 QSLGVLGRIKPDVVLGMGGYITFPAGIMAALTGRPLVLHEQNSIAGLANRVLAKLAKRVLVAFPDA---LPGGE--WTGN 159
Cdd:PRK12446   82 DAYVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAakhLPKEKviYTGS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 160 PIREE-LRDMPEPAGRYA--ARTGPLkLLVVGGSLGAAALNEAVPLALARLPAGSrpHVVHQAGA----KHIGALKTY-- 230
Cdd:PRK12446  162 PVREEvLKGNREKGLAFLgfSRKKPV-ITIMGGSLGAKKINETVREALPELLLKY--QIVHLCGKgnldDSLQNKEGYrq 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 231 YENAGlDHDPDIrlvpfiddmasaYAQADLVICRSGAMTVAEIAAVGVAALFVPFP-YAVDDHQTTNGRFLADRGGALLI 309
Cdd:PRK12446  239 FEYVH-GELPDI------------LAITDFVISRAGSNAIFEFLTLQKPMLLIPLSkFASRGDQILNAESFERQGYASVL 305

                         330
                  ....*....|....
gi 1838886163 310 QQRELTVEGLADWI 323
Cdd:PRK12446  306 YEEDVTVNSLIKHV 319
COG4671 COG4671
Predicted glycosyl transferase [General function prediction only];
161-348 2.27e-15

Predicted glycosyl transferase [General function prediction only];


Pssm-ID: 443708 [Multi-domain]  Cd Length: 391  Bit Score: 76.43  E-value: 2.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 161 IREELRDMPEPAGRYAARTGPLKLLVV---GGSLGAAaLNEAVPLALARLPAGSRPHVV---HQAGAKHIGALKtyyenA 234
Cdd:COG4671   195 VARPAPEPPPEERDALGLLPEEPLILVsagGGGDGAE-LLEAALAAAELLPPPDHRWLLvtgPFMPAADRAALR-----A 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 235 GLDHDPDIRLVPFIDDMASAYAQADLVICRSGAMTVAEIAAVGVAALFVPFPyAVDDHQTTNGRFLADRGGALLIQQREL 314
Cdd:COG4671   269 RAAALPNVTVERFTPDFEALLAAADLSVSMGGYNTVCEILSTGKPALIVPRT-APRTEQLIRAERLAELGLVDVLHPEDL 347

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1838886163 315 TVEGLADWIGAQTRES----------LAAMAARARECAKPDATE 348
Cdd:COG4671   348 TPEALARAIAAALARPprrspldldgLARTARILAELLGARSAA 391
SpsG COG3980
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall ...
 16-340 1.14e-12

Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443179 [Multi-domain]  Cd Length: 342  Bit Score: 68.03  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163  16 GHVFPGLAVAHWMQAHGWRVVWLGNPGGMEAT-LVPKHGIPIefvrfgglrgkglmtkLRLP-FNLLRACSQSLGVLGRI 93
Cdd:COG3980    16 GHVMRCLALAEALRERGAEVTFLCRDDSGSLIeLLKERGFPV----------------ILLPaPSWEDDAEELLELLKDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163  94 KPDVVLgMGGYiTFPAGIMAAL--TGRPLV--------LHE------QNSIAGLANRVLAKLAKRVLVafpdalpGGEWT 157
Cdd:COG3980    80 QPDWLV-VDHY-ALDAEYEKALkaLGKKLVviddlgdrAHPadlvinQNLGASAEDYRGVPPGTKLLL-------GPEYA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 158 gnPIREELRDMPEPAGRYAARtgPLKLLVvggSLGAA-ALNEAVPL--ALARLPAGSRPHVVHQAGAKHIGALKTYYEna 234
Cdd:COG3980   151 --LLRPEFLALRPASRRISEE--VRRILV---TFGGSdPDNLTLKVlrALLQLDPDLKITVVVGPGYPHLDELRALAA-- 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 235 glDHDPDIRLVPFIDDMASAYAQADLVICRSGAmTVAEIAAVGVAALFVpfpyAVDDHQTTNGRFLADRGGALLIQ-QRE 313
Cdd:COG3980   222 --ERPLNIELHRNVKDMAELMAQADLAISAAGT-TTYELAALGLPTIVV----AVADNQRAIAEALEENGAAINLGlGEE 294

                         330       340
                  ....*....|....*....|....*....
gi 1838886163 314 LTVEGLADWIGA--QTRESLAAMAARARE 340
Cdd:COG3980   295 LTDEELANALDEllLDPERRARMSRKARS 323
YjiC COG1819
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
8-339 4.45e-12

UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];


Pssm-ID: 441424 [Multi-domain]  Cd Length: 268  Bit Score: 65.65  E-value: 4.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163   8 MVMAGGTGGHVFPGLAVAHWMQAHGWRVVWLGNPGGmeATLVPKHGIpiEFVRFgglrgkglmtklrlpfnllracsqsl 87
Cdd:COG1819     3 LFVTLGGRGHVNPLLALARALRARGHEVTFATGPDF--ADLVEAAGL--EFVDW-------------------------- 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163  88 gvlgriKPDVVLGmgGYITFPAGIMAALTGRPLVLHeqnsiaglanrvlakLAKRVLVAFPDALPGGEWTGNPIREELRD 167
Cdd:COG1819    53 ------RPDLVVS--DPLALAAALAAEALGIPVVSL---------------TPPELEYPRPPDPANVRFVGPLLPDGPAE 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 168 MPEPAgryAARTGPLKLLVVGGSL--GAAALNEAVPLALARLPAgsrpHVVHQAGAKHIGALKTYYENagldhdpdIRLV 245
Cdd:COG1819   110 LPPWL---EEDAGRPLVYVTLGTSanDRADLLRAVLEALADLGV----RVVVTTGGLDPAELGPLPDN--------VRVV 174

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 246 PFIDdMASAYAQADLVICRSGAMTVAEIAAVGVAALFVPFpyAVDdhQTTNGRFLADRGGALLIQQRELTVEGLADWIGA 325
Cdd:COG1819   175 DYVP-QDALLPRADAVVHHGGAGTTAEALRAGVPQVVVPF--GGD--QPLNAARVERLGAGLALPPRRLTAEALRAALRR 249

                         330
                  ....*....|....*....
gi 1838886163 326 -----QTRESLAAMAARAR 339
Cdd:COG1819   250 lladpSYRERAARLAAEIR 268
GT28_Beta-DGS-like cd17507
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ...
 157-348 2.25e-08

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: 55.02  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 157 TGNPIR---EELRDMPEPAGRYAARTGPLKLLVVGGSLGAAALNEAVpLALARLPAGSRPHVVhqAGAKHigalKTYYEN 233
Cdd:cd17507   170 TGIPVRpsfAEVRDKDEARNELNLSPDKPTVLLMGGGGGMGPVKETV-EALLDSLRAGQVLVV--CGKNK----KLYEKL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 234 AGLDHDPD-IRLVPFIDDMASAYAQADLVICRSGAMTVAEIAAVGVAALFV-PFPyavdDHQTTNGRFLADRGGALLIQQ 311
Cdd:cd17507   243 SGLEEDYInVRVLGYVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYdPIP----GQEEENADFLENNGAGIIARD 318

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1838886163 312 RELTVEGLADWIGAqtrESLAAMAARARECAKPDATE 348
Cdd:cd17507   319 PEELLEIVARLIDP---PSLLRMMSEAAKELKPPAAA 352
PLN02605 PLN02605
monogalactosyldiacylglycerol synthase
 247-348 8.90e-04

monogalactosyldiacylglycerol synthase


Pssm-ID: 215325 [Multi-domain]  Cd Length: 382  Bit Score: 41.11  E-value: 8.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 247 FIDDMASAYAQADLVICRSGAMTVAEIAAVGVAAL---FVP------FPYAVDdhqttNGrfladrGGALLIQQRElTVE 317
Cdd:PLN02605  272 FVTNMEEWMGACDCIITKAGPGTIAEALIRGLPIIlngYIPgqeegnVPYVVD-----NG------FGAFSESPKE-IAR 339

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1838886163 318 GLADWIGAQTREsLAAMAARARECAKPDATE 348
Cdd:PLN02605  340 IVAEWFGDKSDE-LEAMSENALKLARPEAVF 369
PRK13609 PRK13609
diacylglycerol glucosyltransferase; Provisional
 226-313 1.12e-03

diacylglycerol glucosyltransferase; Provisional


Pssm-ID: 237445 [Multi-domain]  Cd Length: 380  Bit Score: 40.48  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838886163 226 ALKTYYENAGLDHDPDIRLVPFIDDMASAYAQADLVICRSGAMTVAEIAAVGVAA-LFVPFPyavdDHQTTNGRFLADRG 304
Cdd:PRK13609  242 ALKQSLEDLQETNPDALKVFGYVENIDELFRVTSCMITKPGGITLSEAAALGVPViLYKPVP----GQEKENAMYFERKG 317


                  ....*....
gi 1838886163 305 GALLIQQRE 313
Cdd:PRK13609  318 AAVVIRDDE 326
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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