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Conserved domains on  [gi|15832106|ref|NP_310879|]
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colanic biosynthesis UDP-glucose lipid carrier transferase [Escherichia coli O157:H7 str. Sakai]

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: 962.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106    2 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVRAATEF 81
Cdd:PRK10124   1 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   82 ALLLQNWTLSVIFSAGLVAFNNDFDTQLKIWLAWYGLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLAAGQMLME 161
Cdd:PRK10124  81 ALLLQNWTLSLIFSAGLVAFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106  162 SFRNQPWLGFEVVGVYHDPKLGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMQMCDGARVKKLVHQLADTTCSVLLIPDVF 241
Cdd:PRK10124 161 SFRNEPWLGFEVVGVYHDPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106  242 TFNILHSRLEEMNGVPVVPLYDTPLSGVNRLLKRAEDIVLATLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 321
Cdd:PRK10124 241 TFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106  322 IKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLR 401
Cdd:PRK10124 321 IKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLR 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832106  402 HKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 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: 962.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106    2 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVRAATEF 81
Cdd:PRK10124   1 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   82 ALLLQNWTLSVIFSAGLVAFNNDFDTQLKIWLAWYGLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLAAGQMLME 161
Cdd:PRK10124  81 ALLLQNWTLSLIFSAGLVAFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106  162 SFRNQPWLGFEVVGVYHDPKLGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMQMCDGARVKKLVHQLADTTCSVLLIPDVF 241
Cdd:PRK10124 161 SFRNEPWLGFEVVGVYHDPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106  242 TFNILHSRLEEMNGVPVVPLYDTPLSGVNRLLKRAEDIVLATLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 321
Cdd:PRK10124 241 TFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106  322 IKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLR 401
Cdd:PRK10124 321 IKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLR 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832106  402 HKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 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: 606.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106    23 FSDITIMFAGLWLVCEVSGLSFLYM----HLLVALITLVVFQMLGGITDFYRSWRGVRAATEFALLLQNWTLSVIFSAGL 98
Cdd:TIGR03023   1 LLDLLLIALALLLAYLLRFGSRGPPdiesYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106    99 VAFNNDFDTQLKIWLA-WYGLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLAAGQMLMESFRNQPWLGFEVVGVY 177
Cdd:TIGR03023  81 AFLLKTGTEFSRLWLLlWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   178 HDPKLGGVSNDW---AGNLQQLVEDAKAGKIHNVYIAMQMCDGARVKKLVHQLADTTCSVLLIPDVFTFNILHSRLEEMN 254
Cdd:TIGR03023 161 DDRPDARTSVRGvpvLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEIG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   255 GVPVVPLYDTPLSGVNRLLKRAEDIVLATLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVME 334
Cdd:TIGR03023 241 GLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVHA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   335 NDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVKPGITGWAQI 414
Cdd:TIGR03023 321 EGDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWAQV 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 15832106   415 NGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 464
Cdd:TIGR03023 401 NGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
131-463 7.81e-114

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 337.86  E-value: 7.81e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106 131 RIGAGWLRNHGYNKRMVAVAGDLAAGQMLMESFRNQPWLGFEVVGVYHDPKLGGVSNDWAGNLQQLVEDAKAGKIHNVYI 210
Cdd:COG2148   1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLLLLIAAAVVVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106 211 AMQMCDGARVKKLVHQLADttcsvLLIPDVFTFNILHSRLEEMNGVPVVPLYDTPLSGVNRLLKRAEDIVLATLILLLIS 290
Cdd:COG2148  81 IIVLLALLLRELLLLLLLL-----LLRLLGVVAELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGLILLS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106 291 PVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVM-ENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFIN 369
Cdd:COG2148 156 PLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELPQLWN 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106 370 VLTGGMSIVGPRPHAVAHNEQYRQliEGYMLRHKVKPGITGWAQINGWRGETdtlekMEKRVEFDLEYIREWSVWFDIKI 449
Cdd:COG2148 236 VLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWLDLKI 308
                       330
                ....*....|....
gi 15832106 450 VFLTVFKGFVNKAA 463
Cdd:COG2148 309 LLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
274-458 5.17e-100

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: 296.96  E-value: 5.17e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   274 KRAEDIVLATLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVVTQATQNDPRVTKVG 353
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   354 NFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHneQYRQLIEGYMLRHKVKPGITGWAQINGWRGETDtlekMEKRVEF 433
Cdd:pfam02397  81 RFLRKTSLDELPQLINVLKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLEL 154
                         170       180
                  ....*....|....*....|....*
gi 15832106   434 DLEYIREWSVWFDIKIVFLTVFKGF 458
Cdd:pfam02397 155 DLYYIENWSLWLDLKILLKTVKVVL 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: 962.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106    2 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVRAATEF 81
Cdd:PRK10124   1 TNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   82 ALLLQNWTLSVIFSAGLVAFNNDFDTQLKIWLAWYGLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLAAGQMLME 161
Cdd:PRK10124  81 ALLLQNWTLSLIFSAGLVAFNNDFDTQLKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106  162 SFRNQPWLGFEVVGVYHDPKLGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMQMCDGARVKKLVHQLADTTCSVLLIPDVF 241
Cdd:PRK10124 161 SFRNEPWLGFEVVGVYHDPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106  242 TFNILHSRLEEMNGVPVVPLYDTPLSGVNRLLKRAEDIVLATLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 321
Cdd:PRK10124 241 TFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106  322 IKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLR 401
Cdd:PRK10124 321 IKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLR 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832106  402 HKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 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: 606.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106    23 FSDITIMFAGLWLVCEVSGLSFLYM----HLLVALITLVVFQMLGGITDFYRSWRGVRAATEFALLLQNWTLSVIFSAGL 98
Cdd:TIGR03023   1 LLDLLLIALALLLAYLLRFGSRGPPdiesYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106    99 VAFNNDFDTQLKIWLA-WYGLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLAAGQMLMESFRNQPWLGFEVVGVY 177
Cdd:TIGR03023  81 AFLLKTGTEFSRLWLLlWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   178 HDPKLGGVSNDW---AGNLQQLVEDAKAGKIHNVYIAMQMCDGARVKKLVHQLADTTCSVLLIPDVFTFNILHSRLEEMN 254
Cdd:TIGR03023 161 DDRPDARTSVRGvpvLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEIG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   255 GVPVVPLYDTPLSGVNRLLKRAEDIVLATLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVME 334
Cdd:TIGR03023 241 GLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVHA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   335 NDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVKPGITGWAQI 414
Cdd:TIGR03023 321 EGDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWAQV 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 15832106   415 NGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 464
Cdd:TIGR03023 401 NGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
26-464 0e+00

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: 531.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106    26 ITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFqmLGGITDFYRSWRGVRAATEFALLLQNWTLSVIFSAGLVAFNNDF 105
Cdd:TIGR03025   9 LAFLLAFLLLGLGLLPPPDFYSLLLLLLLLLFLI--LFALSGLYRSWRGRSLLEELARVLLAWLVAFLLLLALAFLFKSF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   106 DTQLKIWLAWYGLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLAAGQMLMESFRNQPWLGFEVVGVYHDPKLGGV 185
Cdd:TIGR03025  87 DFSRLVLLLWFVLALVLLLLWRLLLRRLLRRLRKRGKNLRRVLIVGTGEAAERLARALRRNPALGYRVVGFVDDRPSDRV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   186 ---SNDWAGNLQQLVEDAKAGKIHNVYIAMQMCDGARVKKLVHQLADTTCSVLLIPDVFTFNILHSRLEEMNGVPVVPLY 262
Cdd:TIGR03025 167 evaGLPVLGKLDDLVELVRAHRVDEVIIALPLSEEARILRLLLQLEDLGVDVYLVPDLFELLLLRLRVEELGGVPLLSLS 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   263 DTPLSGVNRLLKRAEDIVLATLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVM-ENDKVVTQ 341
Cdd:TIGR03025 247 NFPLSGLNRALKRLFDIVLSLLALLLLSPLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRVDaEEGGGPVQ 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   342 ATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVKPGITGWAQINGwRGET 421
Cdd:TIGR03025 327 ATKNDPRITRVGRFLRRTSLDELPQLFNVLKGDMSLVGPRPERPAEVEKYEQEIPGYMLRHKVKPGITGWAQVSG-RGET 405
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 15832106   422 DTlekMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 464
Cdd:TIGR03025 406 ST---MEERVEYDLYYIENWSLWLDLKILLKTVKVVLTGKGAY 445
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
131-463 7.81e-114

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 337.86  E-value: 7.81e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106 131 RIGAGWLRNHGYNKRMVAVAGDLAAGQMLMESFRNQPWLGFEVVGVYHDPKLGGVSNDWAGNLQQLVEDAKAGKIHNVYI 210
Cdd:COG2148   1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLLLLIAAAVVVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106 211 AMQMCDGARVKKLVHQLADttcsvLLIPDVFTFNILHSRLEEMNGVPVVPLYDTPLSGVNRLLKRAEDIVLATLILLLIS 290
Cdd:COG2148  81 IIVLLALLLRELLLLLLLL-----LLRLLGVVAELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGLILLS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106 291 PVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVM-ENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFIN 369
Cdd:COG2148 156 PLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDaEKLLGAVFKLKNDPRITRVGRFLRKTSLDELPQLWN 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106 370 VLTGGMSIVGPRPHAVAHNEQYRQliEGYMLRHKVKPGITGWAQINGWRGETdtlekMEKRVEFDLEYIREWSVWFDIKI 449
Cdd:COG2148 236 VLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLWLDLKI 308
                       330
                ....*....|....
gi 15832106 450 VFLTVFKGFVNKAA 463
Cdd:COG2148 309 LLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
274-458 5.17e-100

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: 296.96  E-value: 5.17e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   274 KRAEDIVLATLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVVTQATQNDPRVTKVG 353
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLFKLKNDPRITRVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   354 NFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHneQYRQLIEGYMLRHKVKPGITGWAQINGWRGETDtlekMEKRVEF 433
Cdd:pfam02397  81 RFLRKTSLDELPQLINVLKGDMSLVGPRPELPEF--EYELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLEL 154
                         170       180
                  ....*....|....*....|....*
gi 15832106   434 DLEYIREWSVWFDIKIVFLTVFKGF 458
Cdd:pfam02397 155 DLYYIENWSLWLDLKILLKTVKVVL 179
WbaP_sugtrans TIGR03022
Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein ...
23-454 6.91e-72

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: 234.18  E-value: 6.91e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106    23 FSDITIMFAGLWLVCEVS---GLSFLYMHLLVALITLVVFQMlggitdFYRSWRGVRAATEFA----LLLQNWTLSVIFS 95
Cdd:TIGR03022   3 LGDIAALVFAIYLALLLRylfGDSSLIWFLLLRSLPVGLFFV------AYRAHYGLYPGTGMSpweeLRRLTLATFALFL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106    96 AGLVA---FNNDFDTQLKIWLAWYGLTSIGLVVCRSCIRigaGWLRNHGYNKRMVAVAGDLAAGQMLMESFRNQPWLGFE 172
Cdd:TIGR03022  77 FILALaffTKVSEPYSRLVFLLAWGLALVLVPLARILVR---KLLSRRGWWGRPAVIIGAGQNAAILYRALQSNPQLGLR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   173 VVGVY------HDPKLGGVsnDWAGNLQQLVEDAKAGKIHnVYIAMQMCDGARVKKLVHQLADTTCS-VLLIPDVFTFNI 245
Cdd:TIGR03022 154 PLAVVdtdpaaSGRLLTGL--PVVGADDALRLYARTRYAY-VIVAMPGTQAEDMARLVRKLGALHFRnVLIVPSLFGLPN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   246 LHSRLEEMNGVPVVPLYDTPLSGVNRLLKRAEDIVLATLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVW 325
Cdd:TIGR03022 231 LWISPRFIGGVLGLRVRNNLLLPSARLIKRTLDLVLSLLALPLLLPLLLVIALLIRLDSKGPAFYKQERVGRNGKLFKCY 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   326 KFRSMkVMENDKVVTQ----------------ATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNE 389
Cdd:TIGR03022 311 KFRTM-VMNSDQVLEEllaadpelraeweeyhKLRNDPRITRIGKFLRKTSLDELPQLWNVLKGDMSLVGPRPYLTSELS 389
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832106   390 QYRQLIEGYmlrHKVKPGITGWAQINGwRGETDtlekMEKRVEFDLEYIREWSVWFDIKIVFLTV 454
Cdd:TIGR03022 390 RYGEALELY---LRVRPGITGLWQVSG-RNETT----YDERVYLDVWYIKNWSLWLDIVILAKTI 446
EpsB_2 TIGR03013
sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the ...
25-454 2.41e-56

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: 192.99  E-value: 2.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106    25 DITIMFAGLWLVCEVSGL------SFLYMHLLVALITLVVFQMLGGIT-DFYR-----SWRGVRAATEFALLLQNWTLSV 92
Cdd:TIGR03013   2 ELVVLVLALYLAVLLRFFyqigmfSLLSLVPLAQLVTFALVVIISAIAlGLYNvdlreDFRGIIARLAISLLVSFLALSF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106    93 IF--------SAGLVAFNNdfdtqlkiwLAWYGLTSIGLVVCRscirigagWLRNHGYNKRMVAVagdLAAGQM---LME 161
Cdd:TIGR03013  82 IFyfypefylGRGLLALAI---------VLAGSLVLLSRLFFL--------KILGLQGLKRRILV---LGTGPRareIAR 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   162 SFRNQPWLGFEVVGVY--HDPKLGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMQmcdgARVKKL-VHQLADTTCSVLLIP 238
Cdd:TIGR03013 142 LRRSSDRRGHEIVGFVplPDEPAYVPSEHVIENGDGLVEYVLRHRIDEIVIALD----ERRGSLpVDELLECKLSGIEVV 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   239 DVFTFnilhsrLEEMNG-VPVVPLYDTPL--------SGVNRLLKRAEDIVLATLILLLISPVLCCIALAVKLSSPGPVI 309
Cdd:TIGR03013 218 DAPSF------FERETGkIAIDLIYPSWLifsngfrnSSLRRITKRSFDVVASLILLILTLPVMLFTALAIKLESGGPVL 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   310 FRQTRYGMDGKPIKVWKFRSMKV-MENDKVVtQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHN 388
Cdd:TIGR03013 292 YRQERVGLNGRPFNLIKFRSMRAdAEKNGAV-WAQKDDPRVTRVGRFLRKTRIDELPQIFNVLRGDMSFVGPRPERPEFV 370
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832106   389 EQYRQLIEGYMLRHKVKPGITGWAQINGWRG--ETDTLEKMekrvEFDLEYIREWSVWFDIKIVFLTV 454
Cdd:TIGR03013 371 EKLSEEIPYYNERHRVKPGITGWAQIKYPYGasVADAKEKL----RYDLYYIKNMSLLLDLIILIQTF 434
CoA_binding_3 pfam13727
CoA-binding domain;
65-238 1.64e-48

CoA-binding domain;


Pssm-ID: 433435 [Multi-domain]  Cd Length: 175  Bit Score: 163.98  E-value: 1.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106    65 ITDFYRSWRGVRAATEFALLLQNWTLSVIFSAGLVAFNNDFDTQLkiWLAWYGLTSIGLVVCRSCI--RIGAGWLRNHGY 142
Cdd:pfam13727   2 AFGVYQSWRGRSLLRELRRVLSAWLLVFLLLALLSFSLHDIFSRL--WLAYWAVSGIALLILSRLLlrAVLRRYRRHGRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   143 NKRMVAVAGDLAAGQMLmesfRNQPWLGFEVVGVYHDPKLGGVSN----DWAGNLQQLVEDAKAGKIHNVYIAMQMCDGA 218
Cdd:pfam13727  80 NRRVVAVGGGLELARQI----RANPWLGFRVVGVFDDRDDDRVPEvagvPVLGNLADLVEYVRETRVDEVYLALPLSAEA 155
                         170       180
                  ....*....|....*....|
gi 15832106   219 RVKKLVHQLADTTCSVLLIP 238
Cdd:pfam13727 156 RILRLVKELRDDPVNIRLIP 175
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
80-454 1.30e-40

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 151.70  E-value: 1.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106   80 EFALLLQNWTLSVIFSAGLVAFNNdFDTQLKIWLAWYGLTSIGLVVCRSCIRigaGWLRNHGYNKRMVAVAGDLAAGQML 159
Cdd:PRK15204  86 ELKEIFRTIVIFAIFDLALIAFTK-WQFSRYVWVFCWTFALILVPFFRALTK---HLLNKLGIWKKKTIILGSGQNARGA 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106  160 MESFRNQPWLGFEVVGVYHDPklggvSNDWAGNLQQLVEDA-------KAGKIHNVyIAMQMCDGARVKKLVHQLADTTC 232
Cdd:PRK15204 162 YSALQSEEMMGFDVIAFFDTD-----ASDAEINMLPVIKDTeiiwdlnRTGDVHYI-LAYEYTELEKTHFWLRELSKHHC 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106  233 -SVLLIPDVFTFNILHSRLEEM--NGVPVVPLYDTPLSGVNRLLKRAEDIVLATLILLLISPVLccIALAVKLSSPG-PV 308
Cdd:PRK15204 236 rSVTVVPSFRGLPLYNTDMSFIfsHEVMLLRIQNNLAKRSSRFLKRTFDIVCSIMILIIASPLM--IYLWYKVTRDGgPA 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106  309 IFRQTRYGMDGKPIKVWKFRSM---------KVMENDKVVTQ------ATQNDPRVTKVGNFLRRTSLDELPQFINVLTG 373
Cdd:PRK15204 314 IYGHQRVGRHGKLFPCYKFRSMvmnsqevlkELLANDPIARAewekdfKLKNDPRITAVGRFIRKTSLDELPQLFNVLKG 393
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106  374 GMSIVGPRPHAVAHNEQYRQLIEGYMLrhkVKPGITGWAQINGwRGETDtlekMEKRVEFDLEYIREWSVWFDIKIVFLT 453
Cdd:PRK15204 394 DMSLVGPRPIVSDELERYCDDVDYYLM---AKPGMTGLWQVSG-RNDVD----YDTRVYFDSWYVKNWTLWNDIAILFKT 465

                 .
gi 15832106  454 V 454
Cdd:PRK15204 466 A 466
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
124-239 2.42e-20

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: 86.13  E-value: 2.42e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832106 124 VVCRSCIRIGAGWLRNHGYNKRMVAVAGDLAAGQMLMESFRNQPWLGFEVVGVY------HDPKLGGVSndWAGNLQQLV 197
Cdd:COG1086   1 LLLRLLLRLLLRRLRRRGRNKRRVLIVGAGEAGRQLARALRRNPDLGYRVVGFVdddpdkRGRRIEGVP--VLGTLDDLP 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15832106 198 EDAKAGKIHNVYIAMQMCDGARVKKLVHQLADTTCSVLLIPD 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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