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Conserved domains on  [gi|2527434828|ref|WP_288450625|]
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sugar transferase, partial [uncultured Acinetobacter sp.]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10124 super family cl46974
putative UDP-glucose lipid carrier transferase; Provisional
3-310 9.98e-88

putative UDP-glucose lipid carrier transferase; Provisional


The actual alignment was detected with superfamily member PRK10124:

Pssm-ID: 481314 [Multi-domain]  Cd Length: 463  Bit Score: 270.05  E-value: 9.98e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828   3 IYLGLYVVFKINGLPITNYTLLAFLSIVSIFQLLGGVTDFYRSWRGMSFSNELISCIKNISLSVILFFLISALF--VQVK 80
Cdd:PRK10124   28 MFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTELALLLQNWTLSLIFSAGLVAFNndFDTQ 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828  81 AVIFLEVMLLLIVFMGLLRASIRLLNSIYYKLVNQSKDILVIGDSVKASKLFIDLSQSKWIGYHAIGLFS-FNIDFDKTN 159
Cdd:PRK10124  108 LKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEPWLGFEVVGVYHdPKPGGVSND 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828 160 FHGGIQDAIEKIQTGDIRKVYIVIDQHNMKQVESLLEVLADSTCSAVIIPDLFSYDFLYSRVEDINGTPVIPLFDSRIDG 239
Cdd:PRK10124  188 WAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVFTFNILHSRLEEMNGVPVVPLYDTPLSG 267
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2527434828 240 INHFLKRIEDIVIGSLILMLISPILLIVSVAIKVNSSGPVFFKQIRYGLNGKPILVYKFRTMKVMENGAVV 310
Cdd:PRK10124  268 INRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVV 338
 
Name Accession Description Interval E-value
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
3-310 9.98e-88

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 270.05  E-value: 9.98e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828   3 IYLGLYVVFKINGLPITNYTLLAFLSIVSIFQLLGGVTDFYRSWRGMSFSNELISCIKNISLSVILFFLISALF--VQVK 80
Cdd:PRK10124   28 MFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTELALLLQNWTLSLIFSAGLVAFNndFDTQ 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828  81 AVIFLEVMLLLIVFMGLLRASIRLLNSIYYKLVNQSKDILVIGDSVKASKLFIDLSQSKWIGYHAIGLFS-FNIDFDKTN 159
Cdd:PRK10124  108 LKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEPWLGFEVVGVYHdPKPGGVSND 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828 160 FHGGIQDAIEKIQTGDIRKVYIVIDQHNMKQVESLLEVLADSTCSAVIIPDLFSYDFLYSRVEDINGTPVIPLFDSRIDG 239
Cdd:PRK10124  188 WAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVFTFNILHSRLEEMNGVPVVPLYDTPLSG 267
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2527434828 240 INHFLKRIEDIVIGSLILMLISPILLIVSVAIKVNSSGPVFFKQIRYGLNGKPILVYKFRTMKVMENGAVV 310
Cdd:PRK10124  268 INRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVV 338
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
2-310 7.50e-84

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: 259.44  E-value: 7.50e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828   2 SIYLGLYVVFKINGLPITNYTLLAFLSIVSIFQLLGGVTDFYRSWRGMSFSNELISCIKNISLSVILFFLISALFVQVKA 81
Cdd:TIGR03023  10 ALLLAYLLRFGSRGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALLAFLLKTGTE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828  82 V---IFLEVMLLLIVFMGLLRASIRLLNSIYYKLVNQSKDILVIGDSVKASKLFIDLSQSKWIGYHAIGLFSFNID---- 154
Cdd:TIGR03023  90 FsrlWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFFDDRPDarts 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828 155 FDKTNFHGGIQDAIEKIQTGDIRKVYIVIDQHNMKQVESLLEVLADSTCSAVIIPDLFSYDFLYSRVEDINGTPVIPLFD 234
Cdd:TIGR03023 170 VRGVPVLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEIGGLPVISLRD 249
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527434828 235 SRIDGINHFLKRIEDIVIGSLILMLISPILLIVSVAIKVNSSGPVFFKQIRYGLNGKPILVYKFRTMKVMENGAVV 310
Cdd:TIGR03023 250 SPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVHAEGDGV 325
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
103-303 5.70e-31

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 118.30  E-value: 5.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828 103 RLLNSIYYKLVNQSKDILVIGDSVKASKLFIDLSQSKWIGYHAIGLFSFNIDFDKTNFHGGIQDAIEKIQTGDIRKVYIV 182
Cdd:COG2148     1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLLLLIAAAVVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828 183 IDQHNMKQVESLLEVLADSTCSAVIIPdlfsYDFLYSRVEDINGTPVIPLFDSRIDGINHFLKRIEDIVIGSLILMLISP 262
Cdd:COG2148    81 IIVLLALLLRELLLLLLLLLLRLLGVV----AELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGLILLSP 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2527434828 263 ILLIVSVAIKVNSSGPVFFKQIRYGLNGKPILVYKFRTMKV 303
Cdd:COG2148   157 LLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRV 197
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
245-303 1.50e-23

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: 94.73  E-value: 1.50e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2527434828 245 KRIEDIVIGSLILMLISPILLIVSVAIKVNSSGPVFFKQIRYGLNGKPILVYKFRTMKV 303
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVV 59
 
Name Accession Description Interval E-value
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
3-310 9.98e-88

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 270.05  E-value: 9.98e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828   3 IYLGLYVVFKINGLPITNYTLLAFLSIVSIFQLLGGVTDFYRSWRGMSFSNELISCIKNISLSVILFFLISALF--VQVK 80
Cdd:PRK10124   28 MFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVKASTELALLLQNWTLSLIFSAGLVAFNndFDTQ 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828  81 AVIFLEVMLLLIVFMGLLRASIRLLNSIYYKLVNQSKDILVIGDSVKASKLFIDLSQSKWIGYHAIGLFS-FNIDFDKTN 159
Cdd:PRK10124  108 LKIWLAWYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEPWLGFEVVGVYHdPKPGGVSND 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828 160 FHGGIQDAIEKIQTGDIRKVYIVIDQHNMKQVESLLEVLADSTCSAVIIPDLFSYDFLYSRVEDINGTPVIPLFDSRIDG 239
Cdd:PRK10124  188 WAGNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVFTFNILHSRLEEMNGVPVVPLYDTPLSG 267
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2527434828 240 INHFLKRIEDIVIGSLILMLISPILLIVSVAIKVNSSGPVFFKQIRYGLNGKPILVYKFRTMKVMENGAVV 310
Cdd:PRK10124  268 INRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVV 338
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
2-310 7.50e-84

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: 259.44  E-value: 7.50e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828   2 SIYLGLYVVFKINGLPITNYTLLAFLSIVSIFQLLGGVTDFYRSWRGMSFSNELISCIKNISLSVILFFLISALFVQVKA 81
Cdd:TIGR03023  10 ALLLAYLLRFGSRGPPDIESYLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALLAFLLKTGTE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828  82 V---IFLEVMLLLIVFMGLLRASIRLLNSIYYKLVNQSKDILVIGDSVKASKLFIDLSQSKWIGYHAIGLFSFNID---- 154
Cdd:TIGR03023  90 FsrlWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFFDDRPDarts 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828 155 FDKTNFHGGIQDAIEKIQTGDIRKVYIVIDQHNMKQVESLLEVLADSTCSAVIIPDLFSYDFLYSRVEDINGTPVIPLFD 234
Cdd:TIGR03023 170 VRGVPVLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEIGGLPVISLRD 249
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527434828 235 SRIDGINHFLKRIEDIVIGSLILMLISPILLIVSVAIKVNSSGPVFFKQIRYGLNGKPILVYKFRTMKVMENGAVV 310
Cdd:TIGR03023 250 SPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVHAEGDGV 325
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
4-310 1.34e-68

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: 220.15  E-value: 1.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828   4 YLGLYVVFKINGLPITNYTLLAFLSIVSIFQLLGGVTDFYRSWRGMSFSNELISCIKNISLSVILFFLISALF--VQVKA 81
Cdd:TIGR03025  11 FLLAFLLLGLGLLPPPDFYSLLLLLLLLLFLILFALSGLYRSWRGRSLLEELARVLLAWLVAFLLLLALAFLFksFDFSR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828  82 VIFLEVMLLLIVFMGLLRASIRLLNSIYYKLVNQSKDILVIGDSVKASKLFIDLSQSKWIGYHAIGLFSFNID----FDK 157
Cdd:TIGR03025  91 LVLLLWFVLALVLLLLWRLLLRRLLRRLRKRGKNLRRVLIVGTGEAAERLARALRRNPALGYRVVGFVDDRPSdrveVAG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828 158 TNFHGGIQDAIEKIQTGDIRKVYIVIDQHNMKQVESLLEVLADSTCSAVIIPDLFSYDFLYSRVEDINGTPVIPLFDSRI 237
Cdd:TIGR03025 171 LPVLGKLDDLVELVRAHRVDEVIIALPLSEEARILRLLLQLEDLGVDVYLVPDLFELLLLRLRVEELGGVPLLSLSNFPL 250
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527434828 238 DGINHFLKRIEDIVIGSLILMLISPILLIVSVAIKVNSSGPVFFKQIRYGLNGKPILVYKFRTMKVM-ENGAVV 310
Cdd:TIGR03025 251 SGLNRALKRLFDIVLSLLALLLLSPLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRVDaEEGGGP 324
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
103-303 5.70e-31

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 118.30  E-value: 5.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828 103 RLLNSIYYKLVNQSKDILVIGDSVKASKLFIDLSQSKWIGYHAIGLFSFNIDFDKTNFHGGIQDAIEKIQTGDIRKVYIV 182
Cdd:COG2148     1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAELLLLLIAAAVVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828 183 IDQHNMKQVESLLEVLADSTCSAVIIPdlfsYDFLYSRVEDINGTPVIPLFDSRIDGINHFLKRIEDIVIGSLILMLISP 262
Cdd:COG2148    81 IIVLLALLLRELLLLLLLLLLRLLGVV----AELGRVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLGLILLSP 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2527434828 263 ILLIVSVAIKVNSSGPVFFKQIRYGLNGKPILVYKFRTMKV 303
Cdd:COG2148   157 LLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRV 197
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
245-303 1.50e-23

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: 94.73  E-value: 1.50e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2527434828 245 KRIEDIVIGSLILMLISPILLIVSVAIKVNSSGPVFFKQIRYGLNGKPILVYKFRTMKV 303
Cdd:pfam02397   1 KRLFDIVLSLLGLILLSPLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVV 59
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
97-211 2.80e-08

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: 51.46  E-value: 2.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828  97 LLRASIRLLNSIYYKLVNQSKDILVIGDSVKASKLFIDLSQSKWIGYHAIGLFSFNIDFDKTNFH-----GGIQDAIEKI 171
Cdd:COG1086     2 LLRLLLRLLLRRLRRRGRNKRRVLIVGAGEAGRQLARALRRNPDLGYRVVGFVDDDPDKRGRRIEgvpvlGTLDDLPELV 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2527434828 172 QTGDIRKVYIVIDQHNMKQVESLLEVLADSTCSAVIIPDL 211
Cdd:COG1086    82 RRLGVDEVIIALPSASRERLRELLEQLEDLGVKVKIVPDL 121
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
42-310 4.30e-08

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 54.24  E-value: 4.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828  42 FYRSWRGMSFSNELISCIKNISLSVILFFLISALFV-----QVKAVIFLEVMLLLIVFMGLLRASIR-LLNsiyyKLVNQ 115
Cdd:PRK15204   70 FWIRLRHYTYRKPFWYELKEIFRTIVIFAIFDLALIaftkwQFSRYVWVFCWTFALILVPFFRALTKhLLN----KLGIW 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828 116 SKDILVIGDSVKASKLFIDLSQSKWIGYHAIGLFSFNIDFDKTNFHGGIQDA---IEKIQTGDIRKVyIVIDQHNMKQVE 192
Cdd:PRK15204  146 KKKTIILGSGQNARGAYSALQSEEMMGFDVIAFFDTDASDAEINMLPVIKDTeiiWDLNRTGDVHYI-LAYEYTELEKTH 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828 193 SLLEVLADSTCSAV-IIPDLFSYDFLYSRVEDINGTPVIPLfdsRIDG-----INHFLKRIEDIVIGSLILMLISPILLI 266
Cdd:PRK15204  225 FWLRELSKHHCRSVtVVPSFRGLPLYNTDMSFIFSHEVMLL---RIQNnlakrSSRFLKRTFDIVCSIMILIIASPLMIY 301
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2527434828 267 VSVAIkVNSSGPVFFKQIRYGLNGKPILVYKFRTMkVMENGAVV 310
Cdd:PRK15204  302 LWYKV-TRDGGPAIYGHQRVGRHGKLFPCYKFRSM-VMNSQEVL 343
CoA_binding_3 pfam13727
CoA-binding domain;
39-209 2.86e-07

CoA-binding domain;


Pssm-ID: 433435 [Multi-domain]  Cd Length: 175  Bit Score: 49.57  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828  39 VTDFYRSWRGMSFSNELISCIKNISLSVILFFLISALFVQ-VKAVIFLEVMLLLIVFMGLLRASIRLLNSIYYKLVNQSK 117
Cdd:pfam13727   2 AFGVYQSWRGRSLLRELRRVLSAWLLVFLLLALLSFSLHDiFSRLWLAYWAVSGIALLILSRLLLRAVLRRYRRHGRNNR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527434828 118 DILVIGDSVKASKLfidLSQSKWIGYHAIGLFSfniDFDKTNFH--------GGIQDAIEKIQTGDIRKVYIVIDQHNMK 189
Cdd:pfam13727  82 RVVAVGGGLELARQ---IRANPWLGFRVVGVFD---DRDDDRVPevagvpvlGNLADLVEYVRETRVDEVYLALPLSAEA 155
                         170       180
                  ....*....|....*....|
gi 2527434828 190 QVESLLEVLADSTCSAVIIP 209
Cdd:pfam13727 156 RILRLVKELRDDPVNIRLIP 175
 
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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