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Conserved domains on  [gi|647321524|ref|WP_025758738|]
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MULTISPECIES: undecaprenyl-phosphate glucose phosphotransferase [Enterobacter]

Protein Classification

undecaprenyl-phosphate glucose phosphotransferase( domain architecture ID 11484584)

undecaprenyl-phosphate glucose phosphotransferase catalyzes the transfer of the glucose-1-phosphate moiety from UDP-Glc onto the carrier lipid undecaprenyl phosphate (C55-P), forming a phosphoanhydride bond yielding to glucosyl-pyrophosphoryl-undecaprenol (Glc-PP-C55); also possesses a weak galactose-1-P transferase activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
2-464 0e+00

putative UDP-glucose lipid carrier transferase; Provisional


:

Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 938.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524   2 TNLKKRERARTNASLISMVQRFSDITIMVGGLWAVCRISGQSFLYMHLLMALIALVVFQMIGGMTDFYRSWRGVKMTTEL 81
Cdd:PRK10124   1 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  82 MLLLQNWTLSLIFSAGLVAFSHDFDNRLVTYLCWYLVTSVGMVVCRSLIRFGAGWLRNRGYNRRFVAVAGDLPVGQVLLD 161
Cdd:PRK10124  81 ALLLQNWTLSLIFSAGLVAFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 162 SFRKEPWLGFEVVGIYHDAKPGGVPADWAGNYEQLIDDAKAGKIHNVYIAMQMKDESRIKQLMRELADTTCSVILIPDVF 241
Cdd:PRK10124 161 SFRNEPWLGFEVVGVYHDPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 242 TFNILHSRIEEVNGVPVVPLYDTPLSGINRVLKRLEDIVLSSLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 321
Cdd:PRK10124 241 TFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 322 IMVWKFRSMKVMENDKVVTQATQNDPRVTRVGNFLRRTSLDELPQFINVFTGGMSIVGPRPHAVAHNEQYRSLIEGYMLR 401
Cdd:PRK10124 321 IKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLR 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647321524 402 HKVKPGITGWAQINGWRGETDTLEKMEKRIEFDLEYIREWSLWFDIKIVFLTIFKGFVNKAAY 464
Cdd:PRK10124 401 HKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
 
Name Accession Description Interval E-value
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
2-464 0e+00

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 938.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524   2 TNLKKRERARTNASLISMVQRFSDITIMVGGLWAVCRISGQSFLYMHLLMALIALVVFQMIGGMTDFYRSWRGVKMTTEL 81
Cdd:PRK10124   1 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  82 MLLLQNWTLSLIFSAGLVAFSHDFDNRLVTYLCWYLVTSVGMVVCRSLIRFGAGWLRNRGYNRRFVAVAGDLPVGQVLLD 161
Cdd:PRK10124  81 ALLLQNWTLSLIFSAGLVAFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 162 SFRKEPWLGFEVVGIYHDAKPGGVPADWAGNYEQLIDDAKAGKIHNVYIAMQMKDESRIKQLMRELADTTCSVILIPDVF 241
Cdd:PRK10124 161 SFRNEPWLGFEVVGVYHDPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 242 TFNILHSRIEEVNGVPVVPLYDTPLSGINRVLKRLEDIVLSSLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 321
Cdd:PRK10124 241 TFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 322 IMVWKFRSMKVMENDKVVTQATQNDPRVTRVGNFLRRTSLDELPQFINVFTGGMSIVGPRPHAVAHNEQYRSLIEGYMLR 401
Cdd:PRK10124 321 IKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLR 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647321524 402 HKVKPGITGWAQINGWRGETDTLEKMEKRIEFDLEYIREWSLWFDIKIVFLTIFKGFVNKAAY 464
Cdd:PRK10124 401 HKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
23-464 0e+00

Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. coli WcaJ protein involved in colanic acid biosynthesis, the Methylobacillus EpsB protein involved in methanolan biosynthesis, as well as the GumD protein involved in the biosynthesis of xanthan. All of these are closely related to the well-characterized WbaP (formerly RfbP) protein, which is the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose (NOTE: not glucose) to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. Colanic acid biosynthesis utilizes a glucose-undecaprenyl carrier, knockout of EpsB abolishes incorporation of UDP-glucose into the lipid phase, and the C-terminal portion of GumD has been shown to be responsible for the glucosyl-1-transferase activity.


Pssm-ID: 274396 [Multi-domain]  Cd Length: 450  Bit Score: 581.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524   23 FSDITIMVGGLWAVCRISGQSFLYM----HLLMALIALVVFQMIGGMTDFYRSWRGVKMTTELMLLLQNWTLSLIFSAGL 98
Cdd:TIGR03023   1 LLDLLLIALALLLAYLLRFGSRGPPdiesYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524   99 VAFSHDFDN--RLVTYLcWYLVTSVGMVVCRSLIRFGAGWLRNRGYNRRFVAVAGDLPVGQVLLDSFRKEPWLGFEVVGI 176
Cdd:TIGR03023  81 AFLLKTGTEfsRLWLLL-WFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  177 YHDAKPGGVPADW---AGNYEQLIDDAKAGKIHNVYIAMQMKDESRIKQLMRELADTTCSVILIPDVFTFNILHSRIEEV 253
Cdd:TIGR03023 160 FDDRPDARTSVRGvpvLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  254 NGVPVVPLYDTPLSGINRVLKRLEDIVLSSLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIMVWKFRSMKVM 333
Cdd:TIGR03023 240 GGLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  334 ENDKVVTQATQNDPRVTRVGNFLRRTSLDELPQFINVFTGGMSIVGPRPHAVAHNEQYRSLIEGYMLRHKVKPGITGWAQ 413
Cdd:TIGR03023 320 AEGDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWAQ 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 647321524  414 INGWRGETDTLEKMEKRIEFDLEYIREWSLWFDIKIVFLTIFKGFVNKAAY 464
Cdd:TIGR03023 400 VNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
131-463 5.33e-104

Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 312.44  E-value: 5.33e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 131 RFGAGWLRNRGYNRRFVAVAGDLPVGQVLLDSFRKEPWLGFEVVGIYHDAKPGGVPADWAGNYEQLIDDAKAGKIHNVYI 210
Cdd:COG2148    1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLLLLIAAAVVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 211 AMQMKDESRIKQLMRELADttcsvILIPDVFTFNILHSRIEEVNGVPVVPLYDTPLSGINRVLKRLEDIVLSSLILLLIS 290
Cdd:COG2148   81 IIVLLALLLRELLLLLLLL-----LLRLLGVVAELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGLILLS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 291 PVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIMVWKFRSMKVM-ENDKVVTQATQNDPRVTRVGNFLRRTSLDELPQFIN 369
Cdd:COG2148  156 PLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELPQLWN 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 370 VFTGGMSIVGPRPHAVAHNEQYRSliEGYMLRHKVKPGITGWAQINGWRGETdtlekMEKRIEFDLEYIREWSLWFDIKI 449
Cdd:COG2148  236 VLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWLDLKI 308
                        330
                 ....*....|....
gi 647321524 450 VFLTIFKGFVNKAA 463
Cdd:COG2148  309 LLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
291-458 2.66e-88

Bacterial sugar transferase; This Pfam family represents a conserved region from a number of different bacterial sugar transferases, involved in diverse biosynthesis pathways.


Pssm-ID: 460547 [Multi-domain]  Cd Length: 180  Bit Score: 266.92  E-value: 2.66e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  291 PVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIMVWKFRSMKVMENDKVVTQATQNDPRVTRVGNFLRRTSLDELPQFINV 370
Cdd:pfam02397  18 PLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVGRFLRKTSLDELPQLINV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  371 FTGGMSIVGPRPHAVAHneQYRSLIEGYMLRHKVKPGITGWAQINGWRGETDtlekMEKRIEFDLEYIREWSLWFDIKIV 450
Cdd:pfam02397  98 LKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLELDLYYIENWSLWLDLKIL 171

                  ....*...
gi 647321524  451 FLTIFKGF 458
Cdd:pfam02397 172 LKTVKVVL 179
 
Name Accession Description Interval E-value
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
2-464 0e+00

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 938.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524   2 TNLKKRERARTNASLISMVQRFSDITIMVGGLWAVCRISGQSFLYMHLLMALIALVVFQMIGGMTDFYRSWRGVKMTTEL 81
Cdd:PRK10124   1 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  82 MLLLQNWTLSLIFSAGLVAFSHDFDNRLVTYLCWYLVTSVGMVVCRSLIRFGAGWLRNRGYNRRFVAVAGDLPVGQVLLD 161
Cdd:PRK10124  81 ALLLQNWTLSLIFSAGLVAFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 162 SFRKEPWLGFEVVGIYHDAKPGGVPADWAGNYEQLIDDAKAGKIHNVYIAMQMKDESRIKQLMRELADTTCSVILIPDVF 241
Cdd:PRK10124 161 SFRNEPWLGFEVVGVYHDPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 242 TFNILHSRIEEVNGVPVVPLYDTPLSGINRVLKRLEDIVLSSLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 321
Cdd:PRK10124 241 TFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 322 IMVWKFRSMKVMENDKVVTQATQNDPRVTRVGNFLRRTSLDELPQFINVFTGGMSIVGPRPHAVAHNEQYRSLIEGYMLR 401
Cdd:PRK10124 321 IKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLR 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647321524 402 HKVKPGITGWAQINGWRGETDTLEKMEKRIEFDLEYIREWSLWFDIKIVFLTIFKGFVNKAAY 464
Cdd:PRK10124 401 HKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
23-464 0e+00

Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. coli WcaJ protein involved in colanic acid biosynthesis, the Methylobacillus EpsB protein involved in methanolan biosynthesis, as well as the GumD protein involved in the biosynthesis of xanthan. All of these are closely related to the well-characterized WbaP (formerly RfbP) protein, which is the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose (NOTE: not glucose) to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. Colanic acid biosynthesis utilizes a glucose-undecaprenyl carrier, knockout of EpsB abolishes incorporation of UDP-glucose into the lipid phase, and the C-terminal portion of GumD has been shown to be responsible for the glucosyl-1-transferase activity.


Pssm-ID: 274396 [Multi-domain]  Cd Length: 450  Bit Score: 581.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524   23 FSDITIMVGGLWAVCRISGQSFLYM----HLLMALIALVVFQMIGGMTDFYRSWRGVKMTTELMLLLQNWTLSLIFSAGL 98
Cdd:TIGR03023   1 LLDLLLIALALLLAYLLRFGSRGPPdiesYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524   99 VAFSHDFDN--RLVTYLcWYLVTSVGMVVCRSLIRFGAGWLRNRGYNRRFVAVAGDLPVGQVLLDSFRKEPWLGFEVVGI 176
Cdd:TIGR03023  81 AFLLKTGTEfsRLWLLL-WFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  177 YHDAKPGGVPADW---AGNYEQLIDDAKAGKIHNVYIAMQMKDESRIKQLMRELADTTCSVILIPDVFTFNILHSRIEEV 253
Cdd:TIGR03023 160 FDDRPDARTSVRGvpvLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  254 NGVPVVPLYDTPLSGINRVLKRLEDIVLSSLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIMVWKFRSMKVM 333
Cdd:TIGR03023 240 GGLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  334 ENDKVVTQATQNDPRVTRVGNFLRRTSLDELPQFINVFTGGMSIVGPRPHAVAHNEQYRSLIEGYMLRHKVKPGITGWAQ 413
Cdd:TIGR03023 320 AEGDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWAQ 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 647321524  414 INGWRGETDTLEKMEKRIEFDLEYIREWSLWFDIKIVFLTIFKGFVNKAAY 464
Cdd:TIGR03023 400 VNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
26-464 3.04e-170

exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family are generally found near other genes involved in the biosynthesis of a variety of exopolysaccharides. These proteins consist of two fused domains, an N-terminal hydrophobic domain of generally low conservation and a highly conserved C-terminal sugar transferase domain (pfam02397). Characterized and partially characterized members of this subfamily include Salmonella WbaP (originally RfbP), E. coli WcaJ, Methylobacillus EpsB, Xanthomonas GumD, Vibrio CpsA, Erwinia AmsG, Group B Streptococcus CpsE (originally CpsD), and Streptococcus suis Cps2E. Each of these is believed to act in transferring the sugar from, for instance, UDP-glucose or UDP-galactose, to a lipid carrier such as undecaprenyl phosphate as the first (priming) step in the synthesis of an oligosaccharide "block". This function is encoded in the C-terminal domain. The liposaccharide is believed to be subsequently transferred through a "flippase" function from the cytoplasmic to the periplasmic face of the inner membrane by the N-terminal domain. Certain closely related transferase enzymes, such as Sinorhizobium ExoY and Lactococcus EpsD, lack the N-terminal domain and are not found by this model.


Pssm-ID: 274398 [Multi-domain]  Cd Length: 445  Bit Score: 485.94  E-value: 3.04e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524   26 ITIMVGGLWAVCRISGQSFLYMHLLMALIALVVFqmIGGMTDFYRSWRGVKMTTELMLLLQNWTLSLIFSAGLVAFSHDF 105
Cdd:TIGR03025   9 LAFLLAFLLLGLGLLPPPDFYSLLLLLLLLLFLI--LFALSGLYRSWRGRSLLEELARVLLAWLVAFLLLLALAFLFKSF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  106 DNRLVTYLCWYLVTSVGMVVCRSLIRFGAGWLRNRGYNRRFVAVAGDLPVGQVLLDSFRKEPWLGFEVVGIYHDAKPGGV 185
Cdd:TIGR03025  87 DFSRLVLLLWFVLALVLLLLWRLLLRRLLRRLRKRGKNLRRVLIVGTGEAAERLARALRRNPALGYRVVGFVDDRPSDRV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  186 PAD---WAGNYEQLIDDAKAGKIHNVYIAMQMKDESRIKQLMRELADTTCSVILIPDVFTFNILHSRIEEVNGVPVVPLY 262
Cdd:TIGR03025 167 EVAglpVLGKLDDLVELVRAHRVDEVIIALPLSEEARILRLLLQLEDLGVDVYLVPDLFELLLLRLRVEELGGVPLLSLS 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  263 DTPLSGINRVLKRLEDIVLSSLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIMVWKFRSMKVM-ENDKVVTQ 341
Cdd:TIGR03025 247 NFPLSGLNRALKRLFDIVLSLLALLLLSPLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRVDaEEGGGPVQ 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  342 ATQNDPRVTRVGNFLRRTSLDELPQFINVFTGGMSIVGPRPHAVAHNEQYRSLIEGYMLRHKVKPGITGWAQINGwRGET 421
Cdd:TIGR03025 327 ATKNDPRITRVGRFLRRTSLDELPQLFNVLKGDMSLVGPRPERPAEVEKYEQEIPGYMLRHKVKPGITGWAQVSG-RGET 405
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 647321524  422 DTlekMEKRIEFDLEYIREWSLWFDIKIVFLTIFKGFVNKAAY 464
Cdd:TIGR03025 406 ST---MEERVEYDLYYIENWSLWLDLKILLKTVKVVLTGKGAY 445
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
131-463 5.33e-104

Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 312.44  E-value: 5.33e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 131 RFGAGWLRNRGYNRRFVAVAGDLPVGQVLLDSFRKEPWLGFEVVGIYHDAKPGGVPADWAGNYEQLIDDAKAGKIHNVYI 210
Cdd:COG2148    1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLLLLIAAAVVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 211 AMQMKDESRIKQLMRELADttcsvILIPDVFTFNILHSRIEEVNGVPVVPLYDTPLSGINRVLKRLEDIVLSSLILLLIS 290
Cdd:COG2148   81 IIVLLALLLRELLLLLLLL-----LLRLLGVVAELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGLILLS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 291 PVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIMVWKFRSMKVM-ENDKVVTQATQNDPRVTRVGNFLRRTSLDELPQFIN 369
Cdd:COG2148  156 PLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELPQLWN 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 370 VFTGGMSIVGPRPHAVAHNEQYRSliEGYMLRHKVKPGITGWAQINGWRGETdtlekMEKRIEFDLEYIREWSLWFDIKI 449
Cdd:COG2148  236 VLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWLDLKI 308
                        330
                 ....*....|....
gi 647321524 450 VFLTIFKGFVNKAA 463
Cdd:COG2148  309 LLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
291-458 2.66e-88

Bacterial sugar transferase; This Pfam family represents a conserved region from a number of different bacterial sugar transferases, involved in diverse biosynthesis pathways.


Pssm-ID: 460547 [Multi-domain]  Cd Length: 180  Bit Score: 266.92  E-value: 2.66e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  291 PVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIMVWKFRSMKVMENDKVVTQATQNDPRVTRVGNFLRRTSLDELPQFINV 370
Cdd:pfam02397  18 PLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVGRFLRKTSLDELPQLINV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  371 FTGGMSIVGPRPHAVAHneQYRSLIEGYMLRHKVKPGITGWAQINGWRGETDtlekMEKRIEFDLEYIREWSLWFDIKIV 450
Cdd:pfam02397  98 LKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLELDLYYIENWSLWLDLKIL 171

                  ....*...
gi 647321524  451 FLTIFKGF 458
Cdd:pfam02397 172 LKTVKVVL 179
WbaP_sugtrans TIGR03022
Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein ...
23-454 2.82e-68

Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein has been characterized as the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. This model includes the enterobacterial enzymes, where the function is presumed to be identical to the S. typhimurium enzyme as well as a somewhat broader group which are likely to catalyze the same or highly similar reactions based on a phylogenetic tree-building analysis of the broader sugar transferase family. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. The most likely heterogeneity would be in the precise nature of the sugar molecule transferred.


Pssm-ID: 274395 [Multi-domain]  Cd Length: 456  Bit Score: 224.93  E-value: 2.82e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524   23 FSDITIMVGGLWA--VCRIS-GQSFLYMHLLMALIALVVFQMI--GGMTdfYRSWRGVKMTTELMLLLQNWTLSLIFSAG 97
Cdd:TIGR03022   3 LGDIAALVFAIYLalLLRYLfGDSSLIWFLLLRSLPVGLFFVAyrAHYG--LYPGTGMSPWEELRRLTLATFALFLFILA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524   98 LVAFSH--DFDNRLVTYLCWyLVTSVGMVVCRSLIR----FGAGWLRNrgynrrfVAVAGDLPVGQVLLDSFRKEPWLGF 171
Cdd:TIGR03022  81 LAFFTKvsEPYSRLVFLLAW-GLALVLVPLARILVRkllsRRGWWGRP-------AVIIGAGQNAAILYRALQSNPQLGL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  172 EVVGIY------HDAKPGGVPAdwAGNYEQLIDDAKAGKIHnVYIAMQMKDESRIKQLMRELADTTCSVILI-PDVFTFN 244
Cdd:TIGR03022 153 RPLAVVdtdpaaSGRLLTGLPV--VGADDALRLYARTRYAY-VIVAMPGTQAEDMARLVRKLGALHFRNVLIvPSLFGLP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  245 ILHSRIEEVNGVPVVPLYDTPLSGINRVLKRLEDIVLSSLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIMV 324
Cdd:TIGR03022 230 NLWISPRFIGGVLGLRVRNNLLLPSARLIKRTLDLVLSLLALPLLLPLLLVIALLIRLDSKGPAFYKQERVGRNGKLFKC 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  325 WKFRSMkVMENDKVVTQ----------------ATQNDPRVTRVGNFLRRTSLDELPQFINVFTGGMSIVGPRPHAVAHN 388
Cdd:TIGR03022 310 YKFRTM-VMNSDQVLEEllaadpelraeweeyhKLRNDPRITRIGKFLRKTSLDELPQLWNVLKGDMSLVGPRPYLTSEL 388
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647321524  389 EQYRSLIEGYmlrHKVKPGITGWAQINGwRGETDtlekMEKRIEFDLEYIREWSLWFDIKIVFLTI 454
Cdd:TIGR03022 389 SRYGEALELY---LRVRPGITGLWQVSG-RNETT----YDERVYLDVWYIKNWSLWLDIVILAKTI 446
EpsB_2 TIGR03013
sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the ...
25-454 3.27e-53

sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the family of bacterial sugar transferases (pfam02397). Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria (notable exceptions appear to include Magnetococcus sp. MC-1 and Myxococcus xanthus DK 1622 ). These genes are generally found near one or more of the PrsK, PrsR or PrsT genes that have been related to the PEP-CTERM system by phylogenetic profiling methods. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species. These proteins are homologs of the EpsB protein found in Methylobacillus sp. strain 12S, which is also associated with a PEP-CTERM system, but of a distinct type. A name which appears attached to a number of genes (by transitive annotation) in this family is "undecaprenyl-phosphate galactose phosphotransferase", which comes from relatively distant characterized enterobacterial homologs, and is considerably more specific than warranted from the currently available evidence.


Pssm-ID: 274390 [Multi-domain]  Cd Length: 442  Bit Score: 184.90  E-value: 3.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524   25 DITIMVGGLWAVCRISG------QSFLYM--HLLMALIALVVfQMIGGMTDFYR-----SWRGVKMTTELMLLLQNWTLS 91
Cdd:TIGR03013   2 ELVVLVLALYLAVLLRFfyqigmFSLLSLvpLAQLVTFALVV-IISAIALGLYNvdlreDFRGIIARLAISLLVSFLALS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524   92 LIF--------SAGLVAFShdfdnrlvtYLCWYLVTSVGMVVCRSLIRFGAGwlrnrgynRRFVAVAGDLPVGQVLLDSF 163
Cdd:TIGR03013  81 FIFyfypefylGRGLLALA---------IVLAGSLVLLSRLFFLKILGLQGL--------KRRILVLGTGPRAREIARLR 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  164 RKEPWLGFEVVGIYHDA-KPGGVPAD-WAGNYEQLIDDAKAGKIHNVYIAMqmkDESRIKQLMRELADTTCSVILIPDVF 241
Cdd:TIGR03013 144 RSSDRRGHEIVGFVPLPdEPAYVPSEhVIENGDGLVEYVLRHRIDEIVIAL---DERRGSLPVDELLECKLSGIEVVDAP 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  242 TFnilhsrIEEVNG-VPVVPLYDTPL--------SGINRVLKRLEDIVLSSLILLLISPVLCCIALAVKLSSPGPVIFRQ 312
Cdd:TIGR03013 221 SF------FERETGkIAIDLIYPSWLifsngfrnSSLRRITKRSFDVVASLILLILTLPVMLFTALAIKLESGGPVLYRQ 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  313 TRYGMDGKPIMVWKFRSMKVMENDKVVTQATQNDPRVTRVGNFLRRTSLDELPQFINVFTGGMSIVGPRPHAVAHNEQYR 392
Cdd:TIGR03013 295 ERVGLNGRPFNLIKFRSMRADAEKNGAVWAQKDDPRVTRVGRFLRKTRIDELPQIFNVLRGDMSFVGPRPERPEFVEKLS 374
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647321524  393 SLIEGYMLRHKVKPGITGWAQINGWRG--ETDTLEKMekriEFDLEYIREWSLWFDIKIVFLTI 454
Cdd:TIGR03013 375 EEIPYYNERHRVKPGITGWAQIKYPYGasVADAKEKL----RYDLYYIKNMSLLLDLIILIQTF 434
CoA_binding_3 pfam13727
CoA-binding domain;
66-238 1.56e-44

CoA-binding domain;


Pssm-ID: 433435 [Multi-domain]  Cd Length: 175  Bit Score: 153.58  E-value: 1.56e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524   66 TDFYRSWRGVKMTTELMLLLQNWTLSLIFSAGLVAFSHDFDNRLVtyLCWYLVTSVGMVVCRSLIRF--GAGWLRNRGYN 143
Cdd:pfam13727   3 FGVYQSWRGRSLLRELRRVLSAWLLVFLLLALLSFSLHDIFSRLW--LAYWAVSGIALLILSRLLLRavLRRYRRHGRNN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  144 RRFVAVAGDLPVGQVLldsfRKEPWLGFEVVGIYHDAKPGGVPA----DWAGNYEQLIDDAKAGKIHNVYIAMQMKDESR 219
Cdd:pfam13727  81 RRVVAVGGGLELARQI----RANPWLGFRVVGVFDDRDDDRVPEvagvPVLGNLADLVEYVRETRVDEVYLALPLSAEAR 156
                         170
                  ....*....|....*....
gi 647321524  220 IKQLMRELADTTCSVILIP 238
Cdd:pfam13727 157 ILRLVKELRDDPVNIRLIP 175
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
80-454 3.37e-39

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 147.46  E-value: 3.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524  80 ELMLLLQNWTLSLIFSAGLVAFSHDFDNRLVTYLCWYLVtsvgmVVCRSLIRFGAGWLRNR-GYNRRFVAVAGDLPVGQV 158
Cdd:PRK15204  86 ELKEIFRTIVIFAIFDLALIAFTKWQFSRYVWVFCWTFA-----LILVPFFRALTKHLLNKlGIWKKKTIILGSGQNARG 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 159 LLDSFRKEPWLGFEVVGIYH----DAKPGGVPADWAGNYeqLIDDAKAGKIHNVyIAMQMKDESRIKQLMRELADTTC-S 233
Cdd:PRK15204 161 AYSALQSEEMMGFDVIAFFDtdasDAEINMLPVIKDTEI--IWDLNRTGDVHYI-LAYEYTELEKTHFWLRELSKHHCrS 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 234 VILIPDVFTfnilhsrieevngvpvVPLYDTPLSGI------------------NRVLKRLEDIVLSSLILLLISPVLcc 295
Cdd:PRK15204 238 VTVVPSFRG----------------LPLYNTDMSFIfshevmllriqnnlakrsSRFLKRTFDIVCSIMILIIASPLM-- 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 296 IALAVKLSSPG-PVIFRQTRYGMDGKPIMVWKFRSM---------KVMENDKVVTQ------ATQNDPRVTRVGNFLRRT 359
Cdd:PRK15204 300 IYLWYKVTRDGgPAIYGHQRVGRHGKLFPCYKFRSMvmnsqevlkELLANDPIARAewekdfKLKNDPRITAVGRFIRKT 379
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 360 SLDELPQFINVFTGGMSIVGPRPHAVAHNEQYRSLIEGYMLrhkVKPGITGWAQINGwRGETDtlekMEKRIEFDLEYIR 439
Cdd:PRK15204 380 SLDELPQLFNVLKGDMSLVGPRPIVSDELERYCDDVDYYLM---AKPGMTGLWQVSG-RNDVD----YDTRVYFDSWYVK 451
                        410
                 ....*....|....*
gi 647321524 440 EWSLWFDIKIVFLTI 454
Cdd:PRK15204 452 NWTLWNDIAILFKTA 466
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
124-239 4.74e-19

NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440703 [Multi-domain]  Cd Length: 121  Bit Score: 82.67  E-value: 4.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647321524 124 VVCRSLIRFGAGWLRNRGYNRRFVAVAGDLPVGQVLLDSFRKEPWLGFEVVGIY------HDAKPGGVPadWAGNYEQLI 197
Cdd:COG1086    1 LLLRLLLRLLLRRLRRRGRNKRRVLIVGAGEAGRQLARALRRNPDLGYRVVGFVdddpdkRGRRIEGVP--VLGTLDDLP 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 647321524 198 DDAKAGKIHNVYIAMQMKDESRIKQLMRELADTTCSVILIPD 239
Cdd:COG1086   79 ELVRRLGVDEVIIALPSASRERLRELLEQLEDLGVKVKIVPD 120
 
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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