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Conserved domains on  [gi|1702130535|gb|QDK99216|]
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sugar transferase [Acinetobacter tandoii]

Protein Classification

sugar transferase( domain architecture ID 10005412)

sugar transferase catalyzes the transfer of a sugar from a donor such as UDP-glucose or UDP-galactose, to a lipid carrier such as undecaprenyl phosphate

EC:  2.-.-.-
Gene Ontology:  GO:0016780|GO:0000271|GO:0005886
PubMed:  29769739
SCOP:  4007826

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
 19-181 9.23e-86

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


:

Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 256.20  E-value: 9.23e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  19 PIFLIVCYKVRKNLGSPIFFCQERPGKNGKLFKMIKFRSMKDAFDQDGNP---LPDEKRITPFGQKLRSTSLDEMPQLIN 95
Cdd:COG2148   156 PLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDAEKLLGAvfkLKNDPRITRVGRFLRKTSLDELPQLWN 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  96 VLKGDMSVVGPRPMLKDFVELYSP-EQARRLEVRPGMTGLAQVSGRNELDYEERFKCDVWYVDNHNTLVDFKIMFRTVAV 174
Cdd:COG2148   236 VLKGDMSLVGPRPELPEEVELYEEeEYRRRLLVKPGITGLAQVNGRNGETFEERVELDLYYIENWSLWLDLKILLKTVLV 315


                  ....*..
gi 1702130535 175 MAKREGI 181
Cdd:COG2148   316 VLKGKGA 322
 
Name Accession Description Interval E-value
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
 19-181 9.23e-86

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 256.20  E-value: 9.23e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  19 PIFLIVCYKVRKNLGSPIFFCQERPGKNGKLFKMIKFRSMKDAFDQDGNP---LPDEKRITPFGQKLRSTSLDEMPQLIN 95
Cdd:COG2148   156 PLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDAEKLLGAvfkLKNDPRITRVGRFLRKTSLDELPQLWN 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  96 VLKGDMSVVGPRPMLKDFVELYSP-EQARRLEVRPGMTGLAQVSGRNELDYEERFKCDVWYVDNHNTLVDFKIMFRTVAV 174
Cdd:COG2148   236 VLKGDMSLVGPRPELPEEVELYEEeEYRRRLLVKPGITGLAQVNGRNGETFEERVELDLYYIENWSLWLDLKILLKTVLV 315


                  ....*..
gi 1702130535 175 MAKREGI 181
Cdd:COG2148   316 VLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
 19-177 3.16e-80

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: 236.87  E-value: 3.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  19 PIFLIVCYKVRKNLGSPIFFCQERPGKNGKLFKMIKFRSMKDAFDQDGNP--LPDEKRITPFGQKLRSTSLDEMPQLINV 96
Cdd:pfam02397  18 PLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLfkLKNDPRITRVGRFLRKTSLDELPQLINV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  97 LKGDMSVVGPRPMLKDF-VELYSPEQARRLEVRPGMTGLAQV-SGRNELDYEERFKCDVWYVDNHNTLVDFKIMFRTVAV 174
Cdd:pfam02397  98 LKGDMSLVGPRPELPEFeYELYERDQRRRLSVKPGITGLAQVnGGRSELSFEEKLELDLYYIENWSLWLDLKILLKTVKV 177


                  ...
gi 1702130535 175 MAK 177
Cdd:pfam02397 178 VLK 180
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
 19-180 2.59e-71

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: 222.85  E-value: 2.59e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  19 PIFLIVCYKVRKNLGSPIFFCQERPGKNGKLFKMIKFRSMK-DAfDQDGNPL---PDEKRITPFGQKLRSTSLDEMPQLI 94
Cdd:TIGR03025 275 PLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRvDA-EEGGGPVqatKNDPRITRVGRFLRRTSLDELPQLF 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  95 NVLKGDMSVVGPRPMLKDFVELYS---PEQARRLEVRPGMTGLAQVSGRNELD-YEERFKCDVWYVDNHNTLVDFKIMFR 170
Cdd:TIGR03025 354 NVLKGDMSLVGPRPERPAEVEKYEqeiPGYMLRHKVKPGITGWAQVSGRGETStMEERVEYDLYYIENWSLWLDLKILLK 433

                         170
                  ....*....|
gi 1702130535 171 TVAVMAKREG 180
Cdd:TIGR03025 434 TVKVVLTGKG 443
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
 1-180 6.30e-45

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 155.16  E-value: 6.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535   1 MKRLVDIIISLIALILLSPIFLIVCYKVRKNlGSPIFFCQERPGKNGKLFKMIKFRSM--------KDAFDQDGNP---- 68
Cdd:PRK15204  279 LKRTFDIVCSIMILIIASPLMIYLWYKVTRD-GGPAIYGHQRVGRHGKLFPCYKFRSMvmnsqevlKELLANDPIAraew 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  69 -----LPDEKRITPFGQKLRSTSLDEMPQLINVLKGDMSVVGPRPMLKDFVELYSPEQARRLEVRPGMTGLAQVSGRNEL 143
Cdd:PRK15204  358 ekdfkLKNDPRITAVGRFIRKTSLDELPQLFNVLKGDMSLVGPRPIVSDELERYCDDVDYYLMAKPGMTGLWQVSGRNDV 437

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1702130535 144 DYEERFKCDVWYVDNHNTLVDFKIMFRTVAVMAKREG 180
Cdd:PRK15204  438 DYDTRVYFDSWYVKNWTLWNDIAILFKTAKVVLRRDG 474
 
Name Accession Description Interval E-value
WcaJ COG2148
Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane ...
 19-181 9.23e-86

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


Pssm-ID: 441751 [Multi-domain]  Cd Length: 322  Bit Score: 256.20  E-value: 9.23e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  19 PIFLIVCYKVRKNLGSPIFFCQERPGKNGKLFKMIKFRSMKDAFDQDGNP---LPDEKRITPFGQKLRSTSLDEMPQLIN 95
Cdd:COG2148   156 PLLLLIALAIKLDSGGPVFFRQERVGRNGRPFTIYKFRTMRVDAEKLLGAvfkLKNDPRITRVGRFLRKTSLDELPQLWN 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  96 VLKGDMSVVGPRPMLKDFVELYSP-EQARRLEVRPGMTGLAQVSGRNELDYEERFKCDVWYVDNHNTLVDFKIMFRTVAV 174
Cdd:COG2148   236 VLKGDMSLVGPRPELPEEVELYEEeEYRRRLLVKPGITGLAQVNGRNGETFEERVELDLYYIENWSLWLDLKILLKTVLV 315


                  ....*..
gi 1702130535 175 MAKREGI 181
Cdd:COG2148   316 VLKGKGA 322
Bac_transf pfam02397
Bacterial sugar transferase; This Pfam family represents a conserved region from a number of ...
 19-177 3.16e-80

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: 236.87  E-value: 3.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  19 PIFLIVCYKVRKNLGSPIFFCQERPGKNGKLFKMIKFRSMKDAFDQDGNP--LPDEKRITPFGQKLRSTSLDEMPQLINV 96
Cdd:pfam02397  18 PLLLLIAIAIKLLSGGPVFFRQERVGKNGKPFTIYKFRTMVVDAEKRGPLfkLKNDPRITRVGRFLRKTSLDELPQLINV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  97 LKGDMSVVGPRPMLKDF-VELYSPEQARRLEVRPGMTGLAQV-SGRNELDYEERFKCDVWYVDNHNTLVDFKIMFRTVAV 174
Cdd:pfam02397  98 LKGDMSLVGPRPELPEFeYELYERDQRRRLSVKPGITGLAQVnGGRSELSFEEKLELDLYYIENWSLWLDLKILLKTVKV 177


                  ...
gi 1702130535 175 MAK 177
Cdd:pfam02397 178 VLK 180
EPS_sugtrans TIGR03025
exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase; Members of this family ...
 19-180 2.59e-71

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: 222.85  E-value: 2.59e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  19 PIFLIVCYKVRKNLGSPIFFCQERPGKNGKLFKMIKFRSMK-DAfDQDGNPL---PDEKRITPFGQKLRSTSLDEMPQLI 94
Cdd:TIGR03025 275 PLMLAIALAIKLDSPGPVFFRQERVGLNGKPFTVYKFRSMRvDA-EEGGGPVqatKNDPRITRVGRFLRRTSLDELPQLF 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  95 NVLKGDMSVVGPRPMLKDFVELYS---PEQARRLEVRPGMTGLAQVSGRNELD-YEERFKCDVWYVDNHNTLVDFKIMFR 170
Cdd:TIGR03025 354 NVLKGDMSLVGPRPERPAEVEKYEqeiPGYMLRHKVKPGITGWAQVSGRGETStMEERVEYDLYYIENWSLWLDLKILLK 433

                         170
                  ....*....|
gi 1702130535 171 TVAVMAKREG 180
Cdd:TIGR03025 434 TVKVVLTGKG 443
WcaJ_sugtrans TIGR03023
Undecaprenyl-phosphate glucose phosphotransferase; This family of proteins encompasses the E. ...
 19-172 6.78e-55

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: 180.47  E-value: 6.78e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  19 PIFLIVCYKVRknLGS--PIFFCQERPGKNGKLFKMIKFRSMK--DAFDQDGNPLPDEKRITPFGQKLRSTSLDEMPQLI 94
Cdd:TIGR03023 277 PLLLLIAIAIK--LTSpgPVLFRQERYGLDGRPFMVYKFRSMRvhAEGDGVTQATRNDPRVTRVGAFLRRTSLDELPQFF 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  95 NVLKGDMSVVGPRPMLKDFVELYS---PEQARRLEVRPGMTGLAQVSG-RNELDY----EERFKCDVWYVDNHNTLVDFK 166
Cdd:TIGR03023 355 NVLKGDMSIVGPRPHAVAHNEQYRkliPGYMLRHKVKPGITGWAQVNGlRGETDTlekmEKRVEYDLYYIENWSLWLDLK 434


                  ....*.
gi 1702130535 167 IMFRTV 172
Cdd:TIGR03023 435 IILLTV 440
PRK15204 PRK15204
undecaprenyl-phosphate galactose phosphotransferase; Provisional
 1-180 6.30e-45

undecaprenyl-phosphate galactose phosphotransferase; Provisional


Pssm-ID: 185126 [Multi-domain]  Cd Length: 476  Bit Score: 155.16  E-value: 6.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535   1 MKRLVDIIISLIALILLSPIFLIVCYKVRKNlGSPIFFCQERPGKNGKLFKMIKFRSM--------KDAFDQDGNP---- 68
Cdd:PRK15204  279 LKRTFDIVCSIMILIIASPLMIYLWYKVTRD-GGPAIYGHQRVGRHGKLFPCYKFRSMvmnsqevlKELLANDPIAraew 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  69 -----LPDEKRITPFGQKLRSTSLDEMPQLINVLKGDMSVVGPRPMLKDFVELYSPEQARRLEVRPGMTGLAQVSGRNEL 143
Cdd:PRK15204  358 ekdfkLKNDPRITAVGRFIRKTSLDELPQLFNVLKGDMSLVGPRPIVSDELERYCDDVDYYLMAKPGMTGLWQVSGRNDV 437

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1702130535 144 DYEERFKCDVWYVDNHNTLVDFKIMFRTVAVMAKREG 180
Cdd:PRK15204  438 DYDTRVYFDSWYVKNWTLWNDIAILFKTAKVVLRRDG 474
EpsB_2 TIGR03013
sugar transferase, PEP-CTERM system associated; Members of this protein family belong to the ...
 1-180 1.55e-43

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: 150.62  E-value: 1.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535   1 MKRLVDIIISLIALILLSPIFLIVCYKVRKNLGSPIFFCQERPGKNGKLFKMIKFRSMKDAFDQDGN--PLPDEKRITPF 78
Cdd:TIGR03013 255 TKRSFDVVASLILLILTLPVMLFTALAIKLESGGPVLYRQERVGLNGRPFNLIKFRSMRADAEKNGAvwAQKDDPRVTRV 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  79 GQKLRSTSLDEMPQLINVLKGDMSVVGPRPMLKDFVELYS---PEQARRLEVRPGMTGLAQVS---GRNELDYEERFKCD 152
Cdd:TIGR03013 335 GRFLRKTRIDELPQIFNVLRGDMSFVGPRPERPEFVEKLSeeiPYYNERHRVKPGITGWAQIKypyGASVADAKEKLRYD 414

                         170       180
                  ....*....|....*....|....*...
gi 1702130535 153 VWYVDNHNTLVDFKIMFRTVAVMAKREG 180
Cdd:TIGR03013 415 LYYIKNMSLLLDLIILIQTFEVVLFGKG 442
PRK10124 PRK10124
putative UDP-glucose lipid carrier transferase; Provisional
 1-172 1.58e-31

putative UDP-glucose lipid carrier transferase; Provisional


Pssm-ID: 182254 [Multi-domain]  Cd Length: 463  Bit Score: 119.05  E-value: 1.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535   1 MKRLVDIIISLIALILLSPIFLIVCYKVRKNLGSPIFFCQERPGKNGKLFKMIKFRSMKDAFDQDG--NPLPDEKRITPF 78
Cdd:PRK10124  272 LKRAEDIVLASLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVvtQATQNDPRVTKV 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702130535  79 GQKLRSTSLDEMPQLINVLKGDMSVVGPRPMlkdfvELYSPEQARRL--------EVRPGMTGLAQVSG-RNELD----Y 145
Cdd:PRK10124  352 GNFLRRTSLDELPQFINVLTGGMSIVGPRPH-----AVAHNEQYRQLiegymlrhKVKPGITGWAQINGwRGETDtlekM 426

                         170       180
                  ....*....|....*....|....*..
gi 1702130535 146 EERFKCDVWYVDNHNTLVDFKIMFRTV 172
Cdd:PRK10124  427 EKRVEFDLEYIREWSVWFDIKIVFLTV 453
 
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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