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Conserved domains on  [gi|85542869|gb|ABC71344|]
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undecaprenyl-phosphate glucosyl-1-phosphate transferase precursor [Burkholderia cenocepacia]

Protein Classification

sugar transferase( domain architecture ID 11496316)

sugar transferase similar to Xanthomonas campestris UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase that 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)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
8-457 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: 541.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869     8 VIDIAMVVTGALIAAALHDGSIGLSDLQ--RTTVLFDCLLVVVFFPAVGIYQSWRGKRLVGLMGRVAFAWLAVELAGILM 85
Cdd:TIGR03023   1 LLDLLLIALALLLAYLLRFGSRGPPDIEsyLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869    86 SFSFHQSGDLSRLWLGYWALVTMALLAGSKACVHVVLRQLRRSGYNLKAVAIVGGTPAARRLIAQMRARPEAGFNPVCVY 165
Cdd:TIGR03023  81 AFLLKTGTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   166 DEsEAPSEVALDDVRIERQFESLVWLVRSRAISELWLTLPITEERRIHQIVTVFRHDFVNIRFIPDVRTLSFFNQEVVEV 245
Cdd:TIGR03023 161 DD-RPDARTSVRGVPVLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   246 LGVPAINLAASPITDVRILPKFVFDRLFALAALTALAPVMVLIAALIKLTSRGPVFFRQKRKGIDGHEFEIYKFRSMKVH 325
Cdd:TIGR03023 240 GGLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   326 QEvAGQVTQATKNDSRVTPVGRFLRRTSLDELPQFINVLKGEMSVVGPRPHALAHDDIYKDLVKGYMFRYRIKPGITGWA 405
Cdd:TIGR03023 320 AE-GDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWA 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 85542869   406 QINGFRGETDQIEKMMGRVKLDLYYMQNWSFWLDIKIVVLTLWKGFTGSNAY 457
Cdd:TIGR03023 399 QVNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
 
Name Accession Description Interval E-value
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
8-457 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: 541.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869     8 VIDIAMVVTGALIAAALHDGSIGLSDLQ--RTTVLFDCLLVVVFFPAVGIYQSWRGKRLVGLMGRVAFAWLAVELAGILM 85
Cdd:TIGR03023   1 LLDLLLIALALLLAYLLRFGSRGPPDIEsyLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869    86 SFSFHQSGDLSRLWLGYWALVTMALLAGSKACVHVVLRQLRRSGYNLKAVAIVGGTPAARRLIAQMRARPEAGFNPVCVY 165
Cdd:TIGR03023  81 AFLLKTGTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   166 DEsEAPSEVALDDVRIERQFESLVWLVRSRAISELWLTLPITEERRIHQIVTVFRHDFVNIRFIPDVRTLSFFNQEVVEV 245
Cdd:TIGR03023 161 DD-RPDARTSVRGVPVLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   246 LGVPAINLAASPITDVRILPKFVFDRLFALAALTALAPVMVLIAALIKLTSRGPVFFRQKRKGIDGHEFEIYKFRSMKVH 325
Cdd:TIGR03023 240 GGLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   326 QEvAGQVTQATKNDSRVTPVGRFLRRTSLDELPQFINVLKGEMSVVGPRPHALAHDDIYKDLVKGYMFRYRIKPGITGWA 405
Cdd:TIGR03023 320 AE-GDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWA 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 85542869   406 QINGFRGETDQIEKMMGRVKLDLYYMQNWSFWLDIKIVVLTLWKGFTGSNAY 457
Cdd:TIGR03023 399 QVNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
1-457 3.18e-117

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 351.33  E-value: 3.18e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869    1 MLSVLARVIDIAMVVTGALIAAALHDGSIGlsdlqrTTVLFDCLLVVVFFPAVG----IYQSWRGKRLVGLMGRVAFAW- 75
Cdd:PRK10124  15 LISMVQRFSDITIMFAGLWLVCEVSGLSFL------YMHLLVALITLVVFQMLGgitdFYRSWRGVKASTELALLLQNWt 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   76 LAVELAGILMSFSFHQSGDLsRLWLGyWALVTMALLAGSKACVHVVLRQLRRSGYNLKAVAIVGGTPAARRLIAQMRARP 155
Cdd:PRK10124  89 LSLIFSAGLVAFNNDFDTQL-KIWLA-WYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEP 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869  156 EAGFNPVCVYDESEapsevaLDDVRIER--QFESLVWLVRSRAISELWLTLPITEERRIHQIVTVFRHDFVNIRFIPDVR 233
Cdd:PRK10124 167 WLGFEVVGVYHDPK------PGGVSNDWagNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869  234 TLSFFNQEVVEVLGVPAINLAASPITDVRILPKFVFDRLFALAALTALAPVMVLIAALIKLTSRGPVFFRQKRKGIDGHE 313
Cdd:PRK10124 241 TFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869  314 FEIYKFRSMKVhQEVAGQVTQATKNDSRVTPVGRFLRRTSLDELPQFINVLKGEMSVVGPRPHALAHDDIYKDLVKGYMF 393
Cdd:PRK10124 321 IKVWKFRSMKV-MENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYML 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 85542869  394 RYRIKPGITGWAQINGFRGETDQIEKMMGRVKLDLYYMQNWSFWLDIKIVVLTLWKGFTGSNAY 457
Cdd:PRK10124 400 RHKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
118-456 1.12e-96

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 293.57  E-value: 1.12e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869 118 VHVVLRQLRRSGYNLKAVAIVGGTPAARRLIAQMRARPEAGFNPVCVYDESEAPSEVALDDVRIERQfESLVWLVRSRAI 197
Cdd:COG2148   1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAE-LLLLLIAAAVVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869 198 SELWLTLPITEERRIHQIVTVFRHDFVNIRFIpdvrtlsffNQEVVEVLGVPAINLAASPITDVRILPKFVFDRLFALAA 277
Cdd:COG2148  80 VIIVLLALLLRELLLLLLLLLLRLLGVVAELG---------RVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869 278 LTALAPVMVLIAALIKLTSRGPVFFRQKRKGIDGHEFEIYKFRSMKVHQEVAGQVTQATKNDSRVTPVGRFLRRTSLDEL 357
Cdd:COG2148 151 LILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDAEKLLGAVFKLKNDPRITRVGRFLRKTSLDEL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869 358 PQFINVLKGEMSVVGPRPHALAHDDIYKDlvKGYMFRYRIKPGITGWAQINGFRGETdqiekMMGRVKLDLYYMQNWSFW 437
Cdd:COG2148 231 PQLWNVLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLW 303
                       330
                ....*....|....*....
gi 85542869 438 LDIKIVVLTLWKGFTGSNA 456
Cdd:COG2148 304 LDLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
283-452 4.06e-87

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: 263.84  E-value: 4.06e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   283 PVMVLIAALIKLTSRGPVFFRQKRKGIDGHEFEIYKFRSMKVHQEVAGqVTQATKNDSRVTPVGRFLRRTSLDELPQFIN 362
Cdd:pfam02397  18 PLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRG-PLFKLKNDPRITRVGRFLRKTSLDELPQLIN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   363 VLKGEMSVVGPRPHALAHDdiYKDLVKGYMFRYRIKPGITGWAQINGFRGETDqiekMMGRVKLDLYYMQNWSFWLDIKI 442
Cdd:pfam02397  97 VLKGDMSLVGPRPELPEFE--YELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLELDLYYIENWSLWLDLKI 170
                         170
                  ....*....|
gi 85542869   443 VVLTLWKGFT 452
Cdd:pfam02397 171 LLKTVKVVLK 180
 
Name Accession Description Interval E-value
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
8-457 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: 541.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869     8 VIDIAMVVTGALIAAALHDGSIGLSDLQ--RTTVLFDCLLVVVFFPAVGIYQSWRGKRLVGLMGRVAFAWLAVELAGILM 85
Cdd:TIGR03023   1 LLDLLLIALALLLAYLLRFGSRGPPDIEsyLALLLLAVLLFLLIFALFGLYRSWRRSRLREELLRILLAWTLTFLILALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869    86 SFSFHQSGDLSRLWLGYWALVTMALLAGSKACVHVVLRQLRRSGYNLKAVAIVGGTPAARRLIAQMRARPEAGFNPVCVY 165
Cdd:TIGR03023  81 AFLLKTGTEFSRLWLLLWFLLALALLLLGRLILRLLLRRLRRKGFNLRRVLIVGAGELGRRLAERLARNPELGYRVVGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   166 DEsEAPSEVALDDVRIERQFESLVWLVRSRAISELWLTLPITEERRIHQIVTVFRHDFVNIRFIPDVRTLSFFNQEVVEV 245
Cdd:TIGR03023 161 DD-RPDARTSVRGVPVLGKLDDLEDLIREGEVDEVYIALPLAAEKRILELLDALRDLTVDVRLVPDLFDFALLRSRIEEI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   246 LGVPAINLAASPITDVRILPKFVFDRLFALAALTALAPVMVLIAALIKLTSRGPVFFRQKRKGIDGHEFEIYKFRSMKVH 325
Cdd:TIGR03023 240 GGLPVISLRDSPLDGWNRFIKRAFDIVLALLVLLLLSPLLLLIAIAIKLTSPGPVLFRQERYGLDGRPFMVYKFRSMRVH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   326 QEvAGQVTQATKNDSRVTPVGRFLRRTSLDELPQFINVLKGEMSVVGPRPHALAHDDIYKDLVKGYMFRYRIKPGITGWA 405
Cdd:TIGR03023 320 AE-GDGVTQATRNDPRVTRVGAFLRRTSLDELPQFFNVLKGDMSIVGPRPHAVAHNEQYRKLIPGYMLRHKVKPGITGWA 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 85542869   406 QINGFRGETDQIEKMMGRVKLDLYYMQNWSFWLDIKIVVLTLWKGFTGSNAY 457
Cdd:TIGR03023 399 QVNGLRGETDTLEKMEKRVEYDLYYIENWSLWLDLKIILLTVFKGFVGKNAY 450
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
8-457 3.22e-166

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: 475.54  E-value: 3.22e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869     8 VIDIAMVVTGALIAAAL-HDGSIGLSDLQRTTVLFDCLLVVVFFPAVGIYQSWRGKRLVGLMGRVAFAWLAVelAGILMS 86
Cdd:TIGR03025   1 LADLLALVLAFLLAFLLlGLGLLPPPDFYSLLLLLLLLLFLILFALSGLYRSWRGRSLLEELARVLLAWLVA--FLLLLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869    87 FSFH-QSGDLSRLWLGYWALVTMALLAGSKACVHVVLRQLRRSGYNLKAVAIVGGTPAARRLIAQMRARPEAGFNPVCVY 165
Cdd:TIGR03025  79 LAFLfKSFDFSRLVLLLWFVLALVLLLLWRLLLRRLLRRLRKRGKNLRRVLIVGTGEAAERLARALRRNPALGYRVVGFV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   166 DEsEAPSEVALDDVRIERQFESLVWLVRSRAISELWLTLPITEERRIHQIVTVFRHDFVNIRFIPDVRTLSFFNQEVVEV 245
Cdd:TIGR03025 159 DD-RPSDRVEVAGLPVLGKLDDLVELVRAHRVDEVIIALPLSEEARILRLLLQLEDLGVDVYLVPDLFELLLLRLRVEEL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   246 LGVPAINLAASPITDVRILPKFVFDRLFALAALTALAPVMVLIAALIKLTSRGPVFFRQKRKGIDGHEFEIYKFRSMKVH 325
Cdd:TIGR03025 238 GGVPLLSLSNFPLSGLNRALKRLFDIVLSLLALLLLSPLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRVD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   326 QEVAGQVTQATKNDSRVTPVGRFLRRTSLDELPQFINVLKGEMSVVGPRPHALAHDDIYKDLVKGYMFRYRIKPGITGWA 405
Cdd:TIGR03025 318 AEEGGGPVQATKNDPRITRVGRFLRRTSLDELPQLFNVLKGDMSLVGPRPERPAEVEKYEQEIPGYMLRHKVKPGITGWA 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 85542869   406 QINGfRGETDQIEKmmgRVKLDLYYMQNWSFWLDIKIVVLTLWKGFTGSNAY 457
Cdd:TIGR03025 398 QVSG-RGETSTMEE---RVEYDLYYIENWSLWLDLKILLKTVKVVLTGKGAY 445
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
1-457 3.18e-117

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 351.33  E-value: 3.18e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869    1 MLSVLARVIDIAMVVTGALIAAALHDGSIGlsdlqrTTVLFDCLLVVVFFPAVG----IYQSWRGKRLVGLMGRVAFAW- 75
Cdd:PRK10124  15 LISMVQRFSDITIMFAGLWLVCEVSGLSFL------YMHLLVALITLVVFQMLGgitdFYRSWRGVKASTELALLLQNWt 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   76 LAVELAGILMSFSFHQSGDLsRLWLGyWALVTMALLAGSKACVHVVLRQLRRSGYNLKAVAIVGGTPAARRLIAQMRARP 155
Cdd:PRK10124  89 LSLIFSAGLVAFNNDFDTQL-KIWLA-WYLLTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLPAGQMLLESFRNEP 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869  156 EAGFNPVCVYDESEapsevaLDDVRIER--QFESLVWLVRSRAISELWLTLPITEERRIHQIVTVFRHDFVNIRFIPDVR 233
Cdd:PRK10124 167 WLGFEVVGVYHDPK------PGGVSNDWagNLQQLVEDAKAGKIHNVYIAMSMCDGARVKKLVRQLADTTCSVLLIPDVF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869  234 TLSFFNQEVVEVLGVPAINLAASPITDVRILPKFVFDRLFALAALTALAPVMVLIAALIKLTSRGPVFFRQKRKGIDGHE 313
Cdd:PRK10124 241 TFNILHSRLEEMNGVPVVPLYDTPLSGINRLLKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869  314 FEIYKFRSMKVhQEVAGQVTQATKNDSRVTPVGRFLRRTSLDELPQFINVLKGEMSVVGPRPHALAHDDIYKDLVKGYMF 393
Cdd:PRK10124 321 IKVWKFRSMKV-MENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYML 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 85542869  394 RYRIKPGITGWAQINGFRGETDQIEKMMGRVKLDLYYMQNWSFWLDIKIVVLTLWKGFTGSNAY 457
Cdd:PRK10124 400 RHKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY 463
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
118-456 1.12e-96

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 293.57  E-value: 1.12e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869 118 VHVVLRQLRRSGYNLKAVAIVGGTPAARRLIAQMRARPEAGFNPVCVYDESEAPSEVALDDVRIERQfESLVWLVRSRAI 197
Cdd:COG2148   1 RLRLLLARLLGRLLAIIVLVGLGDLAAAALLRALGLGIGGGGLVGGALAALPALGRVAGGPLLGDAE-LLLLLIAAAVVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869 198 SELWLTLPITEERRIHQIVTVFRHDFVNIRFIpdvrtlsffNQEVVEVLGVPAINLAASPITDVRILPKFVFDRLFALAA 277
Cdd:COG2148  80 VIIVLLALLLRELLLLLLLLLLRLLGVVAELG---------RVSLSELGGLPLLSVRGPPLSGYQRVLKRLFDIVLALLG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869 278 LTALAPVMVLIAALIKLTSRGPVFFRQKRKGIDGHEFEIYKFRSMKVHQEVAGQVTQATKNDSRVTPVGRFLRRTSLDEL 357
Cdd:COG2148 151 LILLSPLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDAEKLLGAVFKLKNDPRITRVGRFLRKTSLDEL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869 358 PQFINVLKGEMSVVGPRPHALAHDDIYKDlvKGYMFRYRIKPGITGWAQINGFRGETdqiekMMGRVKLDLYYMQNWSFW 437
Cdd:COG2148 231 PQLWNVLKGDMSLVGPRPELPEEVELYEE--EEYRRRLLVKPGITGLAQVNGRNGET-----FEERVELDLYYIENWSLW 303
                       330
                ....*....|....*....
gi 85542869 438 LDIKIVVLTLWKGFTGSNA 456
Cdd:COG2148 304 LDLKILLKTVLVVLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
283-452 4.06e-87

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: 263.84  E-value: 4.06e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   283 PVMVLIAALIKLTSRGPVFFRQKRKGIDGHEFEIYKFRSMKVHQEVAGqVTQATKNDSRVTPVGRFLRRTSLDELPQFIN 362
Cdd:pfam02397  18 PLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRG-PLFKLKNDPRITRVGRFLRKTSLDELPQLIN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   363 VLKGEMSVVGPRPHALAHDdiYKDLVKGYMFRYRIKPGITGWAQINGFRGETDqiekMMGRVKLDLYYMQNWSFWLDIKI 442
Cdd:pfam02397  97 VLKGDMSLVGPRPELPEFE--YELYERDQRRRLSVKPGITGLAQVNGGRSELS----FEEKLELDLYYIENWSLWLDLKI 170
                         170
                  ....*....|
gi 85542869   443 VVLTLWKGFT 452
Cdd:pfam02397 171 LLKTVKVVLK 180
WbaP_sugtrans TIGR03022
Undecaprenyl-phosphate galactose phosphotransferase, WbaP; The WbaP (formerly RfbP) protein ...
10-457 3.17e-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: 224.55  E-value: 3.17e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869    10 DIAmVVTGALIAAALHDGSIGLSdLQRTTVLFDCLLVVVFFPAVGIYQSWR---GKRLVGLMGRVAFAWLAVELAGILMS 86
Cdd:TIGR03022   5 DIA-ALVFAIYLALLLRYLFGDS-SLIWFLLLRSLPVGLFFVAYRAHYGLYpgtGMSPWEELRRLTLATFALFLFILALA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869    87 FSFHQSGDLSRL-WLGYWALVTMALLAgskaCVHVVLRQLRRSGYNLKAVAIVGGTPAARRLIAQMRARPEAGFNPVCVY 165
Cdd:TIGR03022  83 FFTKVSEPYSRLvFLLAWGLALVLVPL----ARILVRKLLSRRGWWGRPAVIIGAGQNAAILYRALQSNPQLGLRPLAVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   166 DESEAPSEVALDDVRIERQFESLVWLVRSRAISELwLTLPITEERRIHQIV-TVFRHDFVNIRFIPDVRTLSFFNQEVVE 244
Cdd:TIGR03022 159 DTDPAASGRLLTGLPVVGADDALRLYARTRYAYVI-VAMPGTQAEDMARLVrKLGALHFRNVLIVPSLFGLPNLWISPRF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   245 VLGVPAINLAASPITDVRILPKFVFDRLFALAALTALAPVMVLIAALIKLTSRGPVFFRQKRKGIDGHEFEIYKFRSMKV 324
Cdd:TIGR03022 238 IGGVLGLRVRNNLLLPSARLIKRTLDLVLSLLALPLLLPLLLVIALLIRLDSKGPAFYKQERVGRNGKLFKCYKFRTMVM 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   325 H-QEVAGQVTQAT-------------KNDSRVTPVGRFLRRTSLDELPQFINVLKGEMSVVGPRPHALAHDDIYKDLVKG 390
Cdd:TIGR03022 318 NsDQVLEELLAADpelraeweeyhklRNDPRITRIGKFLRKTSLDELPQLWNVLKGDMSLVGPRPYLTSELSRYGEALEL 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 85542869   391 YMfryRIKPGITGWAQINGfRGETDQIEkmmgRVKLDLYYMQNWSFWLDIKIVVLTLWKGFTGSNAY 457
Cdd:TIGR03022 398 YL---RVRPGITGLWQVSG-RNETTYDE----RVYLDVWYIKNWSLWLDIVILAKTIKVVLRRKGAY 456
CoA_binding_3 pfam13727
CoA-binding domain;
51-230 1.11e-55

CoA-binding domain;


Pssm-ID: 433435 [Multi-domain]  Cd Length: 175  Bit Score: 182.85  E-value: 1.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869    51 PAVGIYQSWRGKRLVGLMGRVAFAWLAVELAGILMSFSFHQsgDLSRLWLGYWALVTMALLAGSKACVHVVLRQLRRSGY 130
Cdd:pfam13727   1 PAFGVYQSWRGRSLLRELRRVLSAWLLVFLLLALLSFSLHD--IFSRLWLAYWAVSGIALLILSRLLLRAVLRRYRRHGR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   131 NLKAVAIVGGtpaARRLIAQMRARPEAGFNPVCVYDESEAPSEVALDDVRIERQFESLVWLVRSRAISELWLTLPITEER 210
Cdd:pfam13727  79 NNRRVVAVGG---GLELARQIRANPWLGFRVVGVFDDRDDDRVPEVAGVPVLGNLADLVEYVRETRVDEVYLALPLSAEA 155
                         170       180
                  ....*....|....*....|
gi 85542869   211 RIHQIVTVFRHDFVNIRFIP 230
Cdd:pfam13727 156 RILRLVKELRDDPVNIRLIP 175
EpsB_2 TIGR03013
sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the ...
44-446 8.94e-50

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: 175.27  E-value: 8.94e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869    44 LLVVVFFPAVGIYQSWRGKRLVGLMGRVAFAWLaveLAGILMSFSFHQSGDLsrlWLGYWALVTMALLAGskaCVHVVLR 123
Cdd:TIGR03013  41 LVVIISAIALGLYNVDLREDFRGIIARLAISLL---VSFLALSFIFYFYPEF---YLGRGLLALAIVLAG---SLVLLSR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   124 QLRRSGYNLKA----VAIVGGTPAARRLIAQMRARPE-----AGFNPvCVYDESEAPSEValddvRIERQfESLVWLVRS 194
Cdd:TIGR03013 112 LFFLKILGLQGlkrrILVLGTGPRAREIARLRRSSDRrgheiVGFVP-LPDEPAYVPSEH-----VIENG-DGLVEYVLR 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   195 RAISELwlTLPITEERRIHQIVTVFRHDFVNIRfIPDVrtLSFFNQEVvevlGVPAINLAASPI---------TDVRILP 265
Cdd:TIGR03013 185 HRIDEI--VIALDERRGSLPVDELLECKLSGIE-VVDA--PSFFERET----GKIAIDLIYPSWlifsngfrnSSLRRIT 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   266 KFVFDRLFALAALTALAPVMVLIAALIKLTSRGPVFFRQKRKGIDGHEFEIYKFRSMKVHQEVAGQVtQATKNDSRVTPV 345
Cdd:TIGR03013 256 KRSFDVVASLILLILTLPVMLFTALAIKLESGGPVLYRQERVGLNGRPFNLIKFRSMRADAEKNGAV-WAQKDDPRVTRV 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869   346 GRFLRRTSLDELPQFINVLKGEMSVVGPRPHALAHDDIYKDLVKGYMFRYRIKPGITGWAQINGFRG--ETDQIEKMmgr 423
Cdd:TIGR03013 335 GRFLRKTRIDELPQIFNVLRGDMSFVGPRPERPEFVEKLSEEIPYYNERHRVKPGITGWAQIKYPYGasVADAKEKL--- 411
                         410       420
                  ....*....|....*....|...
gi 85542869   424 vKLDLYYMQNWSFWLDIKIVVLT 446
Cdd:TIGR03013 412 -RYDLYYIKNMSLLLDLIILIQT 433
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
125-446 8.73e-35

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 135.13  E-value: 8.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869  125 LRRSGYNLKAVAIVGGTPAARRLIAQMRARPEAGFNPVCVYDESEAPSEVALDDVRierQFESLVWLVRSRAISELWLTL 204
Cdd:PRK15204 139 LNKLGIWKKKTIILGSGQNARGAYSALQSEEMMGFDVIAFFDTDASDAEINMLPVI---KDTEIIWDLNRTGDVHYILAY 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869  205 PITE-ERRIHQIVTVFRHDFVNIRFIPDVRTLSFFNQEVV-----EVLGVPAINLAASPITdvRILpKFVFDRLFALAAL 278
Cdd:PRK15204 216 EYTElEKTHFWLRELSKHHCRSVTVVPSFRGLPLYNTDMSfifshEVMLLRIQNNLAKRSS--RFL-KRTFDIVCSIMIL 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869  279 TALAPVMVLIaaLIKLTSRG-PVFFRQKRKGIDGHEFEIYKFRSMKVH-QEVAGQVTQAT-------------KNDSRVT 343
Cdd:PRK15204 293 IIASPLMIYL--WYKVTRDGgPAIYGHQRVGRHGKLFPCYKFRSMVMNsQEVLKELLANDpiaraewekdfklKNDPRIT 370
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869  344 PVGRFLRRTSLDELPQFINVLKGEMSVVGPRPHALAHDDIYKDLVKGYMFryrIKPGITGWAQINGfRGETDQIEkmmgR 423
Cdd:PRK15204 371 AVGRFIRKTSLDELPQLFNVLKGDMSLVGPRPIVSDELERYCDDVDYYLM---AKPGMTGLWQVSG-RNDVDYDT----R 442
                        330       340
                 ....*....|....*....|...
gi 85542869  424 VKLDLYYMQNWSFWLDIKIVVLT 446
Cdd:PRK15204 443 VYFDSWYVKNWTLWNDIAILFKT 465
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
118-231 3.98e-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: 85.75  E-value: 3.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85542869 118 VHVVLRQLRRSGYNLKAVAIVGGTPAARRLIAQMRARPEAGFNPVCVYDESEAPSEVALDDVRIERQFESLVWLVRSRAI 197
Cdd:COG1086   7 LRLLLRRLRRRGRNKRRVLIVGAGEAGRQLARALRRNPDLGYRVVGFVDDDPDKRGRRIEGVPVLGTLDDLPELVRRLGV 86
                        90       100       110
                ....*....|....*....|....*....|....
gi 85542869 198 SELWLTLPITEERRIHQIVTVFRHDFVNIRFIPD 231
Cdd:COG1086  87 DEVIIALPSASRERLRELLEQLEDLGVKVKIVPD 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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