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Conserved domains on  [gi|738093595|ref|WP_036052246|]
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bacteriohopanetetrol glucosamine biosynthesis glycosyltransferase HpnI [Burkholderia gladioli]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HpnI super family cl26110
hopanoid biosynthesis associated glycosyl transferase protein HpnI; This family of genes ...
10-383 1.88e-148

hopanoid biosynthesis associated glycosyl transferase protein HpnI; This family of genes include a glycosyl transferase, group 2 domain (pfam00535) which are responsible, generally for the transfer of nucleotide-diphosphate sugars to substrates such as polysaccharides and lipids. The member of this clade from Acidithiobacillus ferrooxidans ATCC 23270 (AFE_0974) is found in the same locus as squalene-hopene cyclase (SHC, TIGR01507) and other genes associated with the biosynthesis of hopanoid natural products. Similarly, in Ralstonia eutropha JMP134 (Reut_B4902) this gene is adjacent to HpnAB, IspH and HpnH (TIGR03470), although SHC itself is elsewhere in the genome. Notably, this gene (here named HpnI) and three others form a conserved set (HpnIJKL) which occur in a subset of all genomes containing the SHC enzyme. This relationship was discerned using the method of partial phylogenetic profiling. This group includes Zymomonas mobilis, the organism where the initial hopanoid biosynthesis locus was described consisting of the genes HpnA-E and SHC (HpnF). Continuing past SHC are found a phosphorylase enzyme (ZMO0873, i.e. HpnG, TIGR03468) and another radical SAM enzyme (ZMO0874), HpnH. Although discontinuous in Z. mobilis, we continue the gene symbol sequence with HpnIJKL. Hopanoids are known to feature polar glycosyl head groups in many organisms.


The actual alignment was detected with superfamily member TIGR03472:

Pssm-ID: 132512 [Multi-domain]  Cd Length: 373  Bit Score: 424.87  E-value: 1.88e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595   10 WLLVALTCAACAYAWFAALAPAPRTPSSAAREGWRAPVSVLKPLYGAEPRLYENLATFCSQRHPRYQIVCGVASPTDPAI 89
Cdd:TIGR03472   6 GVAALLSLAGCGYTLLAAALVRRFFRRAARAPRAWPPVSVLKPLHGDEPELYENLASFCRQDYPGFQMLFGVQDPDDPAL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595   90 AVVRRVQANFPGCDLELVIDSRVHGKNLKVSNLINIAQRARYDRLVIADSDIAVGPDYLERVSAPLADPSIGVVTCLYHA 169
Cdd:TIGR03472  86 AVVRRLRADFPDADIDLVIDARRHGPNRKVSNLINMLPHARHDILVIADSDISVGPDYLRQVVAPLADPDVGLVTCLYRG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  170 RDVGGFWARIGAQFVDAWFAPSVRVAHLGGSSDFGFGATLALTRDTLDRIGGLAALKDELADDYWLAALPRRVGRRTVLS 249
Cdd:TIGR03472 166 RPVPGFWSRLGAMGINHNFLPSVMVARALGRARFCFGATMALRRATLEAIGGLAALAHHLADDYWLGELVRALGLRVVLA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  250 EVSVRTDVIEASFAALWARETRWLRTIRSLKGGGFASLLITFTAPWLLvgahLAVRLEATLPGLIAACAASAGVLARLVL 329
Cdd:TIGR03472 246 PVVVDTDVHETSFATLLAHELRWSRTIRAVNPVGYAGSFITQPVPLAV----LALLLGAAWAWPLVAAALAARALLRLVM 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 738093595  330 HARGspsrLVFWRDLPLVPVRDALLFCVWIAAAFGTHVIWRGARIAVAGGARAS 383
Cdd:TIGR03472 322 SRAT----GAPLRAAWLLPLRDLLSFAIWVASFFGSRVVWRGRRFRVDRDGRLS 371
 
Name Accession Description Interval E-value
HpnI TIGR03472
hopanoid biosynthesis associated glycosyl transferase protein HpnI; This family of genes ...
10-383 1.88e-148

hopanoid biosynthesis associated glycosyl transferase protein HpnI; This family of genes include a glycosyl transferase, group 2 domain (pfam00535) which are responsible, generally for the transfer of nucleotide-diphosphate sugars to substrates such as polysaccharides and lipids. The member of this clade from Acidithiobacillus ferrooxidans ATCC 23270 (AFE_0974) is found in the same locus as squalene-hopene cyclase (SHC, TIGR01507) and other genes associated with the biosynthesis of hopanoid natural products. Similarly, in Ralstonia eutropha JMP134 (Reut_B4902) this gene is adjacent to HpnAB, IspH and HpnH (TIGR03470), although SHC itself is elsewhere in the genome. Notably, this gene (here named HpnI) and three others form a conserved set (HpnIJKL) which occur in a subset of all genomes containing the SHC enzyme. This relationship was discerned using the method of partial phylogenetic profiling. This group includes Zymomonas mobilis, the organism where the initial hopanoid biosynthesis locus was described consisting of the genes HpnA-E and SHC (HpnF). Continuing past SHC are found a phosphorylase enzyme (ZMO0873, i.e. HpnG, TIGR03468) and another radical SAM enzyme (ZMO0874), HpnH. Although discontinuous in Z. mobilis, we continue the gene symbol sequence with HpnIJKL. Hopanoids are known to feature polar glycosyl head groups in many organisms.


Pssm-ID: 132512 [Multi-domain]  Cd Length: 373  Bit Score: 424.87  E-value: 1.88e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595   10 WLLVALTCAACAYAWFAALAPAPRTPSSAAREGWRAPVSVLKPLYGAEPRLYENLATFCSQRHPRYQIVCGVASPTDPAI 89
Cdd:TIGR03472   6 GVAALLSLAGCGYTLLAAALVRRFFRRAARAPRAWPPVSVLKPLHGDEPELYENLASFCRQDYPGFQMLFGVQDPDDPAL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595   90 AVVRRVQANFPGCDLELVIDSRVHGKNLKVSNLINIAQRARYDRLVIADSDIAVGPDYLERVSAPLADPSIGVVTCLYHA 169
Cdd:TIGR03472  86 AVVRRLRADFPDADIDLVIDARRHGPNRKVSNLINMLPHARHDILVIADSDISVGPDYLRQVVAPLADPDVGLVTCLYRG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  170 RDVGGFWARIGAQFVDAWFAPSVRVAHLGGSSDFGFGATLALTRDTLDRIGGLAALKDELADDYWLAALPRRVGRRTVLS 249
Cdd:TIGR03472 166 RPVPGFWSRLGAMGINHNFLPSVMVARALGRARFCFGATMALRRATLEAIGGLAALAHHLADDYWLGELVRALGLRVVLA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  250 EVSVRTDVIEASFAALWARETRWLRTIRSLKGGGFASLLITFTAPWLLvgahLAVRLEATLPGLIAACAASAGVLARLVL 329
Cdd:TIGR03472 246 PVVVDTDVHETSFATLLAHELRWSRTIRAVNPVGYAGSFITQPVPLAV----LALLLGAAWAWPLVAAALAARALLRLVM 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 738093595  330 HARGspsrLVFWRDLPLVPVRDALLFCVWIAAAFGTHVIWRGARIAVAGGARAS 383
Cdd:TIGR03472 322 SRAT----GAPLRAAWLLPLRDLLSFAIWVASFFGSRVVWRGRRFRVDRDGRLS 371
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
46-276 3.32e-85

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 257.14  E-value: 3.32e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  46 PVSVLKPLYGAEPRLYENLATFCSQRHPRYQIVCGVASPTDPAIAVVRRVQANFPGCDLELVIDSRVHGKNLKVSNLINI 125
Cdd:cd02520    2 GVSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVGINPKVNNLIKG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 126 AQRARYDRLVIADSDIAVGPDYLERVSAPLADPSIGVVTCLyhardvggfwarigaqfvdawfapsvrvahlggssdFGF 205
Cdd:cd02520   82 YEEARYDILVISDSDISVPPDYLRRMVAPLMDPGVGLVTCL------------------------------------CAF 125
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738093595 206 GATLALTRDTLDRIGGLAALKDELADDYWLAALPRRVGRRTVLSEVSVRTDVIEASFAALWARETRWLRTI 276
Cdd:cd02520  126 GKSMALRREVLDAIGGFEAFADYLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSRTR 196
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
100-274 5.22e-41

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 142.81  E-value: 5.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  100 PGCDLELVIDSRVhGKNLKVSNLINIAQRARYDRLVIADSDIAVGPDYLERVSAPLADPSIGVVTCLYHARDVGGFWARI 179
Cdd:pfam13506   1 PSVRALVVGGPPV-GVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLADPKVGLVTSPPVGSDPKGLAAAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  180 GAQFVDawFAPSVRVAHLGGSSdFGFGATLALTRDTLDRIGGLAALKDELADDYWLAALPRRVGRRTVLS-EVSVRTDVI 258
Cdd:pfam13506  80 EAAFFN--TLAGVLQAALSGIG-FAVGMSMAFRRADLERIGGFEALADYLAEDYALGKLLRAAGLKVVLSpRPILQTSGP 156
                         170
                  ....*....|....*..
gi 738093595  259 EA-SFAALWARETRWLR 274
Cdd:pfam13506 157 RRtSFRAFMARQLRWAR 173
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
46-371 1.41e-22

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 96.73  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  46 PVSVLKPLYGAEPRLYENLATFCSQRHP--RYQIVCGVASPTDPAIAVVRRVQANFPgcDLELVIDSRVHGKnlkVSNLI 123
Cdd:COG1215   30 RVSVIIPAYNEEAVIEETLRSLLAQDYPkeKLEVIVVDDGSTDETAEIARELAAEYP--RVRVIERPENGGK---AAALN 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 124 NIAQRARYDRLVIADSDIAVGPDYLERVSAPLADPSIGVVtclyhardvggfwarigaqfvdawfapsvrvahlggssdf 203
Cdd:COG1215  105 AGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS---------------------------------------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 204 gfGATLALTRDTLDRIGGLAAlkDELADDYWLAALPRRVGRRTVLSEVSVRTDVIEASFAALWARETRWLRTI------- 276
Cdd:COG1215  145 --GANLAFRREALEEVGGFDE--DTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGlqlllkh 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 277 -RSLKGGGFASLLITFTAPWLLVGahlavrleATLPGLIAACAASAGVLARLVLHARgspsrlvfWRDLPLVPVRDALLF 355
Cdd:COG1215  221 rPLLRPRRLLLFLLLLLLPLLLLL--------LLLALLALLLLLLPALLLALLLALR--------RRRLLLPLLHLLYGL 284
                        330
                 ....*....|....*.
gi 738093595 356 CVWIAAAFGTHVIWRG 371
Cdd:COG1215  285 LLLLAALRGKKVVWKK 300
 
Name Accession Description Interval E-value
HpnI TIGR03472
hopanoid biosynthesis associated glycosyl transferase protein HpnI; This family of genes ...
10-383 1.88e-148

hopanoid biosynthesis associated glycosyl transferase protein HpnI; This family of genes include a glycosyl transferase, group 2 domain (pfam00535) which are responsible, generally for the transfer of nucleotide-diphosphate sugars to substrates such as polysaccharides and lipids. The member of this clade from Acidithiobacillus ferrooxidans ATCC 23270 (AFE_0974) is found in the same locus as squalene-hopene cyclase (SHC, TIGR01507) and other genes associated with the biosynthesis of hopanoid natural products. Similarly, in Ralstonia eutropha JMP134 (Reut_B4902) this gene is adjacent to HpnAB, IspH and HpnH (TIGR03470), although SHC itself is elsewhere in the genome. Notably, this gene (here named HpnI) and three others form a conserved set (HpnIJKL) which occur in a subset of all genomes containing the SHC enzyme. This relationship was discerned using the method of partial phylogenetic profiling. This group includes Zymomonas mobilis, the organism where the initial hopanoid biosynthesis locus was described consisting of the genes HpnA-E and SHC (HpnF). Continuing past SHC are found a phosphorylase enzyme (ZMO0873, i.e. HpnG, TIGR03468) and another radical SAM enzyme (ZMO0874), HpnH. Although discontinuous in Z. mobilis, we continue the gene symbol sequence with HpnIJKL. Hopanoids are known to feature polar glycosyl head groups in many organisms.


Pssm-ID: 132512 [Multi-domain]  Cd Length: 373  Bit Score: 424.87  E-value: 1.88e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595   10 WLLVALTCAACAYAWFAALAPAPRTPSSAAREGWRAPVSVLKPLYGAEPRLYENLATFCSQRHPRYQIVCGVASPTDPAI 89
Cdd:TIGR03472   6 GVAALLSLAGCGYTLLAAALVRRFFRRAARAPRAWPPVSVLKPLHGDEPELYENLASFCRQDYPGFQMLFGVQDPDDPAL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595   90 AVVRRVQANFPGCDLELVIDSRVHGKNLKVSNLINIAQRARYDRLVIADSDIAVGPDYLERVSAPLADPSIGVVTCLYHA 169
Cdd:TIGR03472  86 AVVRRLRADFPDADIDLVIDARRHGPNRKVSNLINMLPHARHDILVIADSDISVGPDYLRQVVAPLADPDVGLVTCLYRG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  170 RDVGGFWARIGAQFVDAWFAPSVRVAHLGGSSDFGFGATLALTRDTLDRIGGLAALKDELADDYWLAALPRRVGRRTVLS 249
Cdd:TIGR03472 166 RPVPGFWSRLGAMGINHNFLPSVMVARALGRARFCFGATMALRRATLEAIGGLAALAHHLADDYWLGELVRALGLRVVLA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  250 EVSVRTDVIEASFAALWARETRWLRTIRSLKGGGFASLLITFTAPWLLvgahLAVRLEATLPGLIAACAASAGVLARLVL 329
Cdd:TIGR03472 246 PVVVDTDVHETSFATLLAHELRWSRTIRAVNPVGYAGSFITQPVPLAV----LALLLGAAWAWPLVAAALAARALLRLVM 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 738093595  330 HARGspsrLVFWRDLPLVPVRDALLFCVWIAAAFGTHVIWRGARIAVAGGARAS 383
Cdd:TIGR03472 322 SRAT----GAPLRAAWLLPLRDLLSFAIWVASFFGSRVVWRGRRFRVDRDGRLS 371
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
46-276 3.32e-85

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 257.14  E-value: 3.32e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  46 PVSVLKPLYGAEPRLYENLATFCSQRHPRYQIVCGVASPTDPAIAVVRRVQANFPGCDLELVIDSRVHGKNLKVSNLINI 125
Cdd:cd02520    2 GVSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVGINPKVNNLIKG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 126 AQRARYDRLVIADSDIAVGPDYLERVSAPLADPSIGVVTCLyhardvggfwarigaqfvdawfapsvrvahlggssdFGF 205
Cdd:cd02520   82 YEEARYDILVISDSDISVPPDYLRRMVAPLMDPGVGLVTCL------------------------------------CAF 125
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738093595 206 GATLALTRDTLDRIGGLAALKDELADDYWLAALPRRVGRRTVLSEVSVRTDVIEASFAALWARETRWLRTI 276
Cdd:cd02520  126 GKSMALRREVLDAIGGFEAFADYLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSRTR 196
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
100-274 5.22e-41

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 142.81  E-value: 5.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  100 PGCDLELVIDSRVhGKNLKVSNLINIAQRARYDRLVIADSDIAVGPDYLERVSAPLADPSIGVVTCLYHARDVGGFWARI 179
Cdd:pfam13506   1 PSVRALVVGGPPV-GVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLADPKVGLVTSPPVGSDPKGLAAAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  180 GAQFVDawFAPSVRVAHLGGSSdFGFGATLALTRDTLDRIGGLAALKDELADDYWLAALPRRVGRRTVLS-EVSVRTDVI 258
Cdd:pfam13506  80 EAAFFN--TLAGVLQAALSGIG-FAVGMSMAFRRADLERIGGFEALADYLAEDYALGKLLRAAGLKVVLSpRPILQTSGP 156
                         170
                  ....*....|....*..
gi 738093595  259 EA-SFAALWARETRWLR 274
Cdd:pfam13506 157 RRtSFRAFMARQLRWAR 173
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
46-371 1.41e-22

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 96.73  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  46 PVSVLKPLYGAEPRLYENLATFCSQRHP--RYQIVCGVASPTDPAIAVVRRVQANFPgcDLELVIDSRVHGKnlkVSNLI 123
Cdd:COG1215   30 RVSVIIPAYNEEAVIEETLRSLLAQDYPkeKLEVIVVDDGSTDETAEIARELAAEYP--RVRVIERPENGGK---AAALN 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 124 NIAQRARYDRLVIADSDIAVGPDYLERVSAPLADPSIGVVtclyhardvggfwarigaqfvdawfapsvrvahlggssdf 203
Cdd:COG1215  105 AGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS---------------------------------------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 204 gfGATLALTRDTLDRIGGLAAlkDELADDYWLAALPRRVGRRTVLSEVSVRTDVIEASFAALWARETRWLRTI------- 276
Cdd:COG1215  145 --GANLAFRREALEEVGGFDE--DTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGlqlllkh 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 277 -RSLKGGGFASLLITFTAPWLLVGahlavrleATLPGLIAACAASAGVLARLVLHARgspsrlvfWRDLPLVPVRDALLF 355
Cdd:COG1215  221 rPLLRPRRLLLFLLLLLLPLLLLL--------LLLALLALLLLLLPALLLALLLALR--------RRRLLLPLLHLLYGL 284
                        330
                 ....*....|....*.
gi 738093595 356 CVWIAAAFGTHVIWRG 371
Cdd:COG1215  285 LLLLAALRGKKVVWKK 300
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
47-275 5.10e-21

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 90.89  E-value: 5.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595   47 VSVLKPLYGAEPRLYENLATFCSQRHPRYQIVCGVASPTDPAIAVVRRVQANFPGCDLELVIDSRVHGKNLKVSNLINIA 126
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTGKSRGLNHGF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  127 QRARYDRLVIADSDIAVGPDYLERVSAPLADPSIGVVTCLYHARDVGGFWARIGAQFVDAWFAPSVRVAHLGGSSDFGfG 206
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRSTMLSALGALEFALRHLRMMSLRLALGVLPLS-G 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738093595  207 ATLALTRDTLDRIGGLAALkDELADDYWLAALPRRVGRRTVLSEVSVRTDVIEASFAALWARETRWLRT 275
Cdd:pfam13641 163 AGSAIRREVLKELGLFDPF-FLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
49-188 4.38e-10

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 57.90  E-value: 4.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  49 VLKPLYGAEPRLYENLATFCSQRHPRYQIVCGVASPTDPAIAVVRRVQANFPgcdlelVIDSRVHGKNLKVSNLINIA-Q 127
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDP------RVIRVINEENQGLAAARNAGlK 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738093595 128 RARYDRLVIADSDIAVGPDYLER-VSAPLADPSIGVVTC----LYHA---RDVGGFWARIGAQFVDAWF 188
Cdd:cd00761   75 AARGEYILFLDADDLLLPDWLERlVAELLADPEADAVGGpgnlLFRRellEEIGGFDEALLSGEEDDDF 143
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
134-304 1.17e-09

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 57.35  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  134 LVIADSDIAVGPDYLERVSAPLADPSIGVVTCLYHARDVGGFWARIGAQFVDAWFAPSVRVAHLGGSSDFGFGATLALTR 213
Cdd:pfam13632   2 ILLLDADTVLPPDCLLGIANEMASPEVAIIQGPILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAFLRR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  214 DTLDRIGGLAalKDELADDYWLAALPRRVGRRTVLSEVSVRTDVIEASFAALWARETRWLR---TIRSLKGGGFASLLIT 290
Cdd:pfam13632  82 SALQEVGGWD--DGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYgclLILLIRLLGYLGTLLW 159
                         170
                  ....*....|....
gi 738093595  291 FTAPWLLVGAHLAV 304
Cdd:pfam13632 160 SGLPLALLLLLLFS 173
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
28-175 3.99e-08

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 53.74  E-value: 3.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  28 LAPAPRTPSSAAREGWRAPVSVLKPLYGAEPRLYENLATFCSQRHPRYQIVCGVAS--PTDPAIAVVRRVQANfpgcDLE 105
Cdd:cd06439   12 LARLRPKPPSLPDPAYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRDRLEIIVVSdgSTDGTAEIAREYADK----GVK 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738093595 106 LVIDSRVHGKNlkvsNLINIA-QRARYDRLVIADSDIAVGPDYLERVSAPLADPSIGVVTCLYHARDVGGF 175
Cdd:cd06439   88 LLRFPERRGKA----AALNRAlALATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSGELVIVDGGGS 154
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
49-232 4.05e-08

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 52.61  E-value: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  49 VLKPLYGAEPRLYENLATFCSQRHPRYQIVCGVASPTDPAIAVVRRVQANFPGCDLeLVIDSRVHGKnlkvSNLINIA-Q 127
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVL-VVRDKENGGK----AGALNAGlR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 128 RARYDRLVIADSDIAVGPDYLERVSAP-LADPSIGVVT-CLYHARDVGGFWARigaqFVDAWFAPSVRVAHLGGSSDFGF 205
Cdd:cd06423   76 HAKGDIVVVLDADTILEPDALKRLVVPfFADPKVGAVQgRVRVRNGSENLLTR----LQAIEYLSIFRLGRRAQSALGGV 151
                        170       180       190
                 ....*....|....*....|....*....|.
gi 738093595 206 ----GATLALTRDTLDRIGGLAAlkDELADD 232
Cdd:cd06423  152 lvlsGAFGAFRREALREVGGWDE--DTLTED 180
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
44-201 1.06e-07

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 51.92  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  44 RAPVSVLKPLYGAEPRLYENLATFCSQRHPRYQIVCGVASPTDPAIAVVRRVQANfpgcDLELVidsrVHGKNLKVSNLI 123
Cdd:COG1216    2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFP----RVRVI----RNPENLGFAAAR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 124 NIA-QRARYDRLVIADSDIAVGPDYLERVSAPLAdpsigvvtCLYHA---RDVGGFWARIGAQFVDA------------- 186
Cdd:COG1216   74 NLGlRAAGGDYLLFLDDDTVVEPDWLERLLAAAC--------LLIRRevfEEVGGFDERFFLYGEDVdlclrlrkagyri 145
                        170
                 ....*....|....*
gi 738093595 187 WFAPSVRVAHLGGSS 201
Cdd:COG1216  146 VYVPDAVVYHLGGAS 160
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
47-248 2.41e-07

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 50.86  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  47 VSVLKPLYGAEPRLYENLATFCSQRHPRYQIVCGVASPTDPAIAVVRRVQANFPGCdleLVIDsrvHGKNLKVSNLINIA 126
Cdd:COG0463    4 VSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRI---RVIR---LERNRGKGAARNAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 127 -QRARYDRLVIADSDIAVGPDYLERVSAPLADPSIGVVTCLYHARDVGGFWARIGAQFvdawFAPSVRVAHLGGSSdfgf 205
Cdd:COG0463   78 lAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRL----FNLVRLLTNLPDST---- 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 738093595 206 GATLALTRDTLDRIGglaaLKDELADDYWLAALPRRVGRRTVL 248
Cdd:COG0463  150 SGFRLFRREVLEELG----FDEGFLEDTELLRALRHGFRIAEV 188
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
48-232 3.24e-07

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 49.70  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595   48 SVLKPLYGAEPRLYENLATFCSQRHPRYQIVCGVASPTDPAIAVVRRVQANFPGCdleLVIdsrVHGKNL-KVSNLINIA 126
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRV---RVI---RLPENRgKAGARNAGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  127 QRARYDRLVIADSDIAVGPDYLERVSAPLADPSIGVVTCLYHARDVGGFWARigaqfvdawfapsvRVAHLGGSSDFGFG 206
Cdd:pfam00535  75 RAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR--------------RASRITLSRLPFFL 140
                         170       180
                  ....*....|....*....|....*.
gi 738093595  207 ATLALTRDTLDRIGGLAALKDELADD 232
Cdd:pfam00535 141 GLRLLGLNLPFLIGGFALYRREALEE 166
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
47-185 1.38e-05

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 46.09  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  47 VSVLKPLYGAEPRLYENLATFCSQRHPRYQIVCGVASPTDPAIAVVRrvQANFPGCdleLVIDSRVHGKNLKVSNLINIA 126
Cdd:cd06434    2 VTVIIPVYDEDPDVFRECLRSILRQKPLEIIVVTDGDDEPYLSILSQ--TVKYGGI---FVITVPHPGKRRALAEGIRHV 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 127 QRaryDRLVIADSDIAVGPDYLERVSAPLADPSIG-VVTCLYHARDVGGFWARIGAQFVD 185
Cdd:cd06434   77 TT---DIVVLLDSDTVWPPNALPEMLKPFEDPKVGgVGTNQRILRPRDSKWSFLAAEYLE 133
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
118-274 1.50e-04

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 42.94  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 118 KVSNLINIAQRARYDRLVIADSDIAVGPDYLERVSAPLAD-PSIGVVT---CLYHARDVGgfWARIGAQFVDAWFAPSVR 193
Cdd:cd06421   72 KAGNLNNALAHTTGDFVAILDADHVPTPDFLRRTLGYFLDdPKVALVQtpqFFYNPDPFD--WLADGAPNEQELFYGVIQ 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595 194 VAHLGGSSDFGFGATLALTRDTLDRIGGLAalKDELADDYWLAALPRRVGRRTV-LSEVSVRTDVIEaSFAALWARETRW 272
Cdd:cd06421  150 PGRDRWGAAFCCGSGAVVRREALDEIGGFP--TDSVTEDLATSLRLHAKGWRSVyVPEPLAAGLAPE-TLAAYIKQRLRW 226

                 ..
gi 738093595 273 LR 274
Cdd:cd06421  227 AR 228
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
53-391 4.89e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 42.55  E-value: 4.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595   53 LYGAEPRLYENLATFCSQRHPRYQIVCGVASPTDPAIAVVRRVQANFPGCDLELVIDSRVHGKNLKVSNLINIAQRARYD 132
Cdd:COG3321   852 LYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLA 931
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  133 RLVIADSDIAVGPDYLERVSAPLADPSIGVVTCLYHARDVggfWARIGAQFVDAWFAPSVRVAHLGGSSDFGFGATLALT 212
Cdd:COG3321   932 LVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAA---AAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAA 1008
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  213 RDTLDRIGGLAALKDELADDYWLAALPRRVGRRTVLSEVSVRTDVIEASFAALWARETRWLRTIRSLKGGGFASLLITFT 292
Cdd:COG3321  1009 ALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAA 1088
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093595  293 APWLLVGAHLAVRLEATLPGLIAACAASAGVLARLVLHARGSPSRLVFWRDLPLVPVRDALLFCVWIAAAFGTHVIWRGA 372
Cdd:COG3321  1089 ALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALL 1168
                         330
                  ....*....|....*....
gi 738093595  373 RIAVAGGARASFGEGGDGR 391
Cdd:COG3321  1169 AAAALLLALALALAAALAA 1187
 
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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