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Conserved domains on  [gi|2524478152|ref|WP_286608126|]
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glycosyltransferase family 4 protein [Citrobacter sp. Cpo126]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133453)

glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CAZY:  GT4
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  12691742|10521532|16037492
SCOP:  3001586

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-397 5.26e-61

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


:

Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 201.23  E-value: 5.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152   2 KVLLV-NKFFFIKGGAETVYFQERDMLKQAGVQVIDFSMQHENNFPSDYADYFVSNVDYHKAsnllgGIKTAVNFIhnsq 80
Cdd:cd03801     1 KILLLsPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLA-----ALLRARRLL---- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  81 acKKMLALLEIERPDIVHFHNIYHQLTPALikVARNFGCKTVLTAHDYKIVCPAYSMLRdgkvcdscitgtvfnafryrc 160
Cdd:cd03801    72 --RELRPLLRLRKFDVVHAHGLLAALLAAL--LALLLGAPLVVTLHGAEPGRLLLLLAA--------------------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 161 qegsaskslllslEATW-QYIAQNYQALDVIVSPSVFLRGVLLRTL--PNSRIDVIVNGVDDSRPLAEVS-------DEG 230
Cdd:cd03801   127 -------------ERRLlARAEALLRRADAVIAVSEALRDELRALGgiPPEKIVVIPNGVDLERFSPPLRrklgippDRP 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 231 YMLYFGRLSREKGVATLLAAHKKMQNKAP---LKVVG-HGPLHDELAAK----YPDVEFLGYVQQgEALDNLIKHARAVI 302
Cdd:cd03801   194 VLLFVGRLSPRKGVDLLLEALAKLLRRGPdvrLVIVGgDGPLRAELEELelglGDRVRFLGFVPD-EELPALYAAADVFV 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 303 LPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEK 382
Cdd:cd03801   273 LPSR-YEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAER 351

                         410
                  ....*....|....*
gi 2524478152 383 YALSKHMDTLQALYK 397
Cdd:cd03801   352 FSWERVAERLLDLYR 366
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-397 5.26e-61

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 201.23  E-value: 5.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152   2 KVLLV-NKFFFIKGGAETVYFQERDMLKQAGVQVIDFSMQHENNFPSDYADYFVSNVDYHKAsnllgGIKTAVNFIhnsq 80
Cdd:cd03801     1 KILLLsPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLA-----ALLRARRLL---- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  81 acKKMLALLEIERPDIVHFHNIYHQLTPALikVARNFGCKTVLTAHDYKIVCPAYSMLRdgkvcdscitgtvfnafryrc 160
Cdd:cd03801    72 --RELRPLLRLRKFDVVHAHGLLAALLAAL--LALLLGAPLVVTLHGAEPGRLLLLLAA--------------------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 161 qegsaskslllslEATW-QYIAQNYQALDVIVSPSVFLRGVLLRTL--PNSRIDVIVNGVDDSRPLAEVS-------DEG 230
Cdd:cd03801   127 -------------ERRLlARAEALLRRADAVIAVSEALRDELRALGgiPPEKIVVIPNGVDLERFSPPLRrklgippDRP 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 231 YMLYFGRLSREKGVATLLAAHKKMQNKAP---LKVVG-HGPLHDELAAK----YPDVEFLGYVQQgEALDNLIKHARAVI 302
Cdd:cd03801   194 VLLFVGRLSPRKGVDLLLEALAKLLRRGPdvrLVIVGgDGPLRAELEELelglGDRVRFLGFVPD-EELPALYAAADVFV 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 303 LPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEK 382
Cdd:cd03801   273 LPSR-YEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAER 351

                         410
                  ....*....|....*
gi 2524478152 383 YALSKHMDTLQALYK 397
Cdd:cd03801   352 FSWERVAERLLDLYR 366
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 289-401 7.85e-32

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 117.01  E-value: 7.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 289 EALDNLIKHARAVILPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKA 368
Cdd:COG0438    12 LLLEALLAAADVFVLPSR-SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELR 90

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2524478152 369 RNMGLHGRARLSEKYALSKHMDTLQALYKELLS 401
Cdd:COG0438    91 RRLGEAARERAEERFSWEAIAERLLALYEELLA 123
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 228-378 1.83e-31

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 117.38  E-value: 1.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 228 DEGYMLYFGRLSREKGVATLLAA---HKKMQNKAPLKVVGHGPLHDEL---AAKY---PDVEFLGYVQQgEALDNLIKHA 298
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAfalLKEKNPNLKLVIAGDGEEEKRLkklAEKLglgDNVIFLGFVSD-EDLPELLKIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 299 RAVILPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRAR 378
Cdd:pfam00534  80 DVFVLPSR-YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 196-400 2.00e-20

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. 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. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. 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, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 91.71  E-value: 2.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 196 FLRGVLlrTLPNSRIDVIVNGVDDSR------PLAEVS-------DEGYMLYFGRLSREKGVATLLAAHKKMQNKAP--- 259
Cdd:TIGR03088 150 WLRGPV--KVPPAKIHQIYNGVDTERfhpsrgDRSPILppdffadESVVVGTVGRLQAVKDQPTLVRAFALLVRQLPega 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 260 ----LKVVGHGPLHDELAAKYpDVEFLGYVQQ--GEALD--NLIKHARAVILPSECyENCSMAILEAMSLGKPVIGSRIG 331
Cdd:TIGR03088 228 erlrLVIVGDGPARGACEQMV-RAAGLAHLVWlpGERDDvpALMQALDLFVLPSLA-EGISNTILEAMASGLPVIATAVG 305

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524478152 332 GIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEKYALSKHMDTLQALYKELL 400
Cdd:TIGR03088 306 GNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSINAMVAAYAGLYDQLL 374
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 232-383 8.13e-18

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 84.76  E-value: 8.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 232 MLYFGRLSREKGVATLlaahKKMQNKAP---LKVVGHGPLHDELAAKYPD--VEFLGYVQqGEALDNLIKHARAVILPSE 306
Cdd:PLN02871  266 IVYVGRLGAEKNLDFL----KRVMERLPgarLAFVGDGPYREELEKMFAGtpTVFTGMLQ-GDELSQAYASGDVFVMPSE 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 307 CyENCSMAILEAMSLGKPVIGSRIGGIPEQIRD---GVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLsEKY 383
Cdd:PLN02871  341 S-ETLGFVVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEV-EKW 418
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-397 5.26e-61

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 201.23  E-value: 5.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152   2 KVLLV-NKFFFIKGGAETVYFQERDMLKQAGVQVIDFSMQHENNFPSDYADYFVSNVDYHKAsnllgGIKTAVNFIhnsq 80
Cdd:cd03801     1 KILLLsPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLA-----ALLRARRLL---- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  81 acKKMLALLEIERPDIVHFHNIYHQLTPALikVARNFGCKTVLTAHDYKIVCPAYSMLRdgkvcdscitgtvfnafryrc 160
Cdd:cd03801    72 --RELRPLLRLRKFDVVHAHGLLAALLAAL--LALLLGAPLVVTLHGAEPGRLLLLLAA--------------------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 161 qegsaskslllslEATW-QYIAQNYQALDVIVSPSVFLRGVLLRTL--PNSRIDVIVNGVDDSRPLAEVS-------DEG 230
Cdd:cd03801   127 -------------ERRLlARAEALLRRADAVIAVSEALRDELRALGgiPPEKIVVIPNGVDLERFSPPLRrklgippDRP 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 231 YMLYFGRLSREKGVATLLAAHKKMQNKAP---LKVVG-HGPLHDELAAK----YPDVEFLGYVQQgEALDNLIKHARAVI 302
Cdd:cd03801   194 VLLFVGRLSPRKGVDLLLEALAKLLRRGPdvrLVIVGgDGPLRAELEELelglGDRVRFLGFVPD-EELPALYAAADVFV 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 303 LPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEK 382
Cdd:cd03801   273 LPSR-YEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAER 351

                         410
                  ....*....|....*
gi 2524478152 383 YALSKHMDTLQALYK 397
Cdd:cd03801   352 FSWERVAERLLDLYR 366
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 2-390 6.88e-54

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 182.53  E-value: 6.88e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152   2 KVLLVNKFFF--IKGGAETV---YFQErdmLKQAGVQVIDFSMQHENNFPSDYA---DYFVSNVDYHKASNLLGGIKTAV 73
Cdd:cd03823     1 KILLVNSLYPpqRVGGAEISvhdLAEA---LVAEGHEVAVLTAGVGPPGQATVArsvVRYRRAPDETLPLALKRRGYELF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  74 NFiHNSQACKKMLALLEIERPDIVHFHNIyHQLTPALIKVARNFGCKTVLTAHDYKIVCPAYSMLRDGKvcdscitgtvf 153
Cdd:cd03823    78 ET-YNPGLRRLLARLLEDFRPDVVHTHNL-SGLGASLLDAARDLGIPVVHTLHDYWLLCPRQFLFKKGG----------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 154 nafryrcqegsaskslllsleatwqyiaqnyqalDVIVSPSVFLRGVLLRT-LPNSRIDVIVNGVDDSRPLAEVSDEGY- 231
Cdd:cd03823   145 ----------------------------------DAVLAPSRFTANLHEANgLFSARISVIPNAVEPDLAPPPRRRPGTe 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 232 ---MLYFGRLSREKGVATLLAAHKKM-QNKAPLKVVGHGPLHDELAAKYPD-VEFLGYVQQgEALDNLIKHARAVILPSE 306
Cdd:cd03823   191 rlrFGYIGRLTEEKGIDLLVEAFKRLpREDIELVIAGHGPLSDERQIEGGRrIAFLGRVPT-DDIKDFYEKIDVLVVPSI 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 307 CYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEKYALS 386
Cdd:cd03823   270 WPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAE 349


                  ....
gi 2524478152 387 KHMD 390
Cdd:cd03823   350 EYLK 353
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 73-387 4.05e-35

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 132.72  E-value: 4.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  73 VNFIHNSQACKKMLALLEIERPDIVHFH----NIYHQLtpalikVARNFG-CKTVLTAHDYKIVCPAYSMLRDgkvcdsc 147
Cdd:cd03808    61 INPLKDLKALFKLYKLLKKEKPDIVHCHtpkpGILGRL------AARLAGvPKVIYTVHGLGFVFTEGKLLRL------- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 148 ITGTVFN-AFRYrcqegsaskslllsleaTWQYIAQNYQALDVIVSpsvflrgvlLRTLPNSRIDVIV-NGVDDSR--PL 223
Cdd:cd03808   128 LYLLLEKlALLF-----------------TDKVIFVNEDDRDLAIK---------KGIIKKKKTVLIPgSGVDLDRfqYS 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 224 AEVSDEGY--MLYFGRLSREKGVATLLAAHKKMQNKAP---LKVVGHGPLHDELAAKY------PDVEFLGYVqqgEALD 292
Cdd:cd03808   182 PESLPSEKvvFLFVARLLKDKGIDELIEAAKILKKKGPnvrFLLVGDGELENPSEILIeklgleGRIEFLGFR---SDVP 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 293 NLIKHARAVILPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMG 372
Cdd:cd03808   259 ELLAESDVFVLPSY-REGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMG 337

                         330
                  ....*....|....*
gi 2524478152 373 LHGRARLSEKYALSK 387
Cdd:cd03808   338 EAARKRVEEKFDEEK 352
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 82-399 1.40e-32

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 125.96  E-value: 1.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  82 CKKMLALLEIER---PDIVHFHNIYHQLtPALIKVARNFGCKTVLTAHDYKI-VCPAYSMLRDgkvcdscitgtvFNAFR 157
Cdd:cd03798    81 APSLAKLLKRRRrgpPDLIHAHFAYPAG-FAAALLARLYGVPYVVTEHGSDInVFPPRSLLRK------------LLRWA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 158 YRcqegsaskslllslEATWqyiaqnyqalDVIVSPSvFLRGVLLRTLPNSRIDVIVNGVDDSR--PLAEVSDEG----Y 231
Cdd:cd03798   148 LR--------------RAAR----------VIAVSKA-LAEELVALGVPRDRVDVIPNGVDPARfqPEDRGLGLPldafV 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 232 MLYFGRLSREKGVATLLAAHKKMQNKAP---LKVVGHGPLHDELAAKY------PDVEFLGYVQQGEALDnLIKHARAVI 302
Cdd:cd03798   203 ILFVGRLIPRKGIDLLLEAFARLAKARPdvvLLIVGDGPLREALRALAedlglgDRVTFTGRLPHEQVPA-YYRACDVFV 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 303 LPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANA-MDALADSPEkaRNMGLHGRARLSE 381
Cdd:cd03798   282 LPSR-HEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAAlRRALAEPYL--RELGEAARARVAE 358

                         330
                  ....*....|....*...
gi 2524478152 382 KYALSKHMDTLQALYKEL 399
Cdd:cd03798   359 RFSWVKAADRIAAAYRDV 376
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 289-401 7.85e-32

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 117.01  E-value: 7.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 289 EALDNLIKHARAVILPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKA 368
Cdd:COG0438    12 LLLEALLAAADVFVLPSR-SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELR 90

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2524478152 369 RNMGLHGRARLSEKYALSKHMDTLQALYKELLS 401
Cdd:COG0438    91 RRLGEAARERAEERFSWEAIAERLLALYEELLA 123
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 228-378 1.83e-31

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 117.38  E-value: 1.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 228 DEGYMLYFGRLSREKGVATLLAA---HKKMQNKAPLKVVGHGPLHDEL---AAKY---PDVEFLGYVQQgEALDNLIKHA 298
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAfalLKEKNPNLKLVIAGDGEEEKRLkklAEKLglgDNVIFLGFVSD-EDLPELLKIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 299 RAVILPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRAR 378
Cdd:pfam00534  80 DVFVLPSR-YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 181-395 5.78e-31

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 121.41  E-value: 5.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 181 AQNYQALDVIVSPsvFLRGVLLRT-LPNSRIDVIVNGVDDSR--PLAEVSDEGYMLYFGRLSREKGVATLLAAHKKMQNK 257
Cdd:cd05844   140 LQRPAALFVAVSG--FIRDRLLARgLPAERIHVHYIGIDPAKfaPRDPAERAPTILFVGRLVEKKGCDVLIEAFRRLAAR 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 258 ---APLKVVGHGPLHDEL---AAKYPDVEFLGYVQQGEALDnLIKHARAVILPSEC-----YENCSMAILEAMSLGKPVI 326
Cdd:cd05844   218 hptARLVIAGDGPLRPALqalAAALGRVRFLGALPHAEVQD-WMRRAEIFCLPSVTaasgdSEGLGIVLLEAAACGVPVV 296

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524478152 327 GSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEKYALSKHMDTLQAL 395
Cdd:cd05844   297 SSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFDIRVQTAKLEAI 365
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 174-382 1.95e-30

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 120.09  E-value: 1.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 174 EATWQYIAQNYQALDVIVSPSVFLRGVLLRTlPNSRIDVIVNGVD---------DSRPLAEVSDEG--YMLYFGRLSREK 242
Cdd:cd03814   133 WLAWAYLRWFHNPFDTTLVPSPSIARELEGH-GFERVRLWPRGVDtelfhpsrrDAALRRRLGPPGrpLLLYVGRLAPEK 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 243 GVATLLAAHKKMQNKAPLK--VVGHGPLHDELAAKYPDVEFLGYvQQGEALDNLIKHARAVILPSEcYENCSMAILEAMS 320
Cdd:cd03814   212 NLEALLDADLPLAASPPVRlvVVGDGPARAELEARGPDVIFTGF-LTGEELARAYASADVFVFPSR-TETFGLVVLEAMA 289

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524478152 321 LGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEK 382
Cdd:cd03814   290 SGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERY 351
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 14-371 7.43e-30

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 118.23  E-value: 7.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  14 GGAETVYfqeRDMLKQ---AGVQVIDFSMQHENNFPsDYADYFVSNVDYHKASNLLggiktavNFIHNSQACKKMLALLE 90
Cdd:cd03811    12 GGAERVL---LNLANAldkRGYDVTLVLLRDEGDLD-KQLNGDVKLIRLLIRVLKL-------IKLGLLKAILKLKRILK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  91 IERPDIVHfhnIYHQLTPALIKVARNFGCKTVLTAHdykivcpaysmlrdgkvcdscitgtvfNAFRYRcqegsasksll 170
Cdd:cd03811    81 RAKPDVVI---SFLGFATYIVAKLAAARSKVIAWIH---------------------------SSLSKL----------- 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 171 LSLEATWQYIAQNYQALDVIVSPSVFLRGVLLRTLPN--SRIDVIVNGVD--DSRPLAEVSDEG------YMLYFGRLSR 240
Cdd:cd03811   120 YYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSppEKIEVIYNPIDidRIRALAKEPILNepedgpVILAVGRLDP 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 241 EKGVATLLAAHKKMQNKAP---LKVVGHGPLHDEL---AAKY---PDVEFLGYVqqgealDN---LIKHARAVILPSEcY 308
Cdd:cd03811   200 QKGHDLLIEAFAKLRKKYPdvkLVILGDGPLREELeklAKELglaERVIFLGFQ------SNpypYLKKADLFVLSSR-Y 272

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524478152 309 ENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNM 371
Cdd:cd03811   273 EGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQKKLDAALR 335
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
233-363 1.37e-29

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 111.45  E-value: 1.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 233 LYFGRLS-REKGVATLLAAHKKMQNK---APLKVVGHGP---LHDELAAKYPDVEFLGYVqqgEALDNLIKHARAVILPS 305
Cdd:pfam13692   5 LFVGRLHpNVKGVDYLLEAVPLLRKRdndVRLVIVGDGPeeeLEELAAGLEDRVIFTGFV---EDLAELLAAADVFVLPS 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2524478152 306 EcYENCSMAILEAMSLGKPVIGSRIGGIPEQIrDGVEGILFEPGNAQELANAMDALAD 363
Cdd:pfam13692  82 L-YEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLE 137
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 2-392 1.42e-28

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 115.13  E-value: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152   2 KVLLVNKFFFIKGGAETVYFQERDM-LKQAGVQVIDFSMQHENNFPSDYADYF--VSNVDYHK----ASNLLGGIKTAVN 74
Cdd:cd03794     1 KILLISQYYPPPKGAAAARVYELAKeLVRRGHEVTVLTPSPNYPLGRIFAGATetKDGIRVIRvklgPIKKNGLIRRLLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  75 FIhnSQACKKMLALL-EIERPDIVHFHNIYHQLTPALIKVARNFGCKTVLTAHD-YKIVCPAYSMLRDGKVCDSCitgtv 152
Cdd:cd03794    81 YL--SFALAALLKLLvREERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDlWPESLIALGVLKKGSLLKLL----- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 153 FNAFRYrcqegsaskslllsleatwqyiaqNYQALDVIVSPS-VFLRGVLLRTLPNSRIDVIVNGVDDSRPLAEVSDEGY 231
Cdd:cd03794   154 KKLERK------------------------LYRLADAIIVLSpGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPKDELR 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 232 M----------LYFGRLSREKGVATLLAAHKKMQNKAPLKV--VGHGPLHDEL-----AAKYPDVEFLGYVQQgEALDNL 294
Cdd:cd03794   210 KklglddkfvvVYAGNIGKAQGLETLLEAAERLKRRPDIRFlfVGDGDEKERLkelakARGLDNVTFLGRVPK-EEVPEL 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 295 IKHARAVILP---SECYENCSMA-ILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARN 370
Cdd:cd03794   289 LSAADVGLVPlkdNPANRGSSPSkLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRA 368

                         410       420
                  ....*....|....*....|..
gi 2524478152 371 MGLHGRARLSEKYALSKHMDTL 392
Cdd:cd03794   369 MGENGRELAEEKFSREKLADRL 390
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 188-384 2.08e-27

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 111.69  E-value: 2.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 188 DVIVSPSVFLRGVLLRTL--PNSRIDVIVNGVDDSRPLAEVS---------DEGYMLYFGRLSREKGVATLLAAHK--KM 254
Cdd:cd03809   140 DAIITVSEATRDDIIKFYgvPPEKIVVIPLGVDPSFFPPESAavliakyllPEPYFLYVGTLEPRKNHERLLKAFAllKK 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 255 QNKA-PLKVVG-HGPLHDELAAKY------PDVEFLGYVQQGEaLDNLIKHARAVILPSEcYENCSMAILEAMSLGKPVI 326
Cdd:cd03809   220 QGGDlKLVIVGgKGWEDEELLDLVkklglgGRVRFLGYVSDED-LPALYRGARAFVFPSL-YEGFGLPVLEAMACGTPVI 297

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524478152 327 GSRIGGIPEQIRDgvEGILFEPGNAQELANAMDALADSP---EKARNMGLHGRARLS-EKYA 384
Cdd:cd03809   298 ASNISVLPEVAGD--AALYFDPLDPESIADAILRLLEDPslrEELIRKGLERAKKFSwEKTA 357
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 83-399 1.21e-25

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 106.65  E-value: 1.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  83 KKMLALLEIERPDIVHFHNI--YHQLTPALIKVARNfgCKTVLTAHD---------YKIVCPAYsmlRDGkvCDSCITGT 151
Cdd:cd03825    41 KNLISKPEFIEADIIHLHWIhgGYLSLKALFKLLRR--KPVVWTLHDmwpftggchYPMECEGW---KTG--CGNCPNLN 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 152 VFNAFRYRCQEgsaskslllsleATWQYIAQNYQALD-VIVSPSVFLRGVLLRT--LPNSRIDVIVNGVD---------- 218
Cdd:cd03825   114 SYPPAKKDLSR------------QLFRRKREALAKKRlTIVAPSRWLADMVRRSplLKGLPVVVIPNGIDteifapvdka 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 219 DSRPLAEVSDEGYMLYFGRLS---REKGVATLLAAHKKMQNKAPLKVVGHGPLHDELAAKYPDVEFLGYVQQGEALDNLI 295
Cdd:cd03825   182 KARKRLGIPQDKKVILFGAESvtkPRKGFDELIEALKLLATKDDLLLVVFGKNDPQIVILPFDIISLGYIDDDEQLVDIY 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 296 KHARAVILPSECyENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHG 375
Cdd:cd03825   262 SAADLFVHPSLA-DNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERA 340

                         330       340
                  ....*....|....*....|....
gi 2524478152 376 RARLSEKYALSKHMDTLQALYKEL 399
Cdd:cd03825   341 RALAENHFDQRVQAQRYLELYKDL 364
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 2-383 2.03e-25

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 105.82  E-value: 2.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152   2 KVLLVNKFFFI-KGGAETVYFQERDMLKQAGVQVIDFSMQHENNFPsdyaDYFVSNVDYHKASnllggiktaVNFIHNSQ 80
Cdd:cd03795     1 KVLHVFKFYYPdIGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETP----EKEENGIRIHRVK---------SFLNVAST 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  81 ackkMLALLEIER-------PDIVHFH--NIYHQLTPALIKVARnfgcKTVLTAHD--------YKIVCPAYS-MLRDGK 142
Cdd:cd03795    68 ----PFSPSYIKRfkklakeYDIIHYHfpNPLADLLLFFSGAKK----PVVVHWHSdivkqkklLKLYKPLMTrFLRRAD 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 143 VcdscITGTvfnafryrcqegsaskslllsleatwqyiAQNYqaldviVSPSVFLRG--VLLRTLPnSRIDVI---VNGV 217
Cdd:cd03795   140 R----IIAT-----------------------------SPNY------VETSPTLREfkNKVRVIP-LGIDKNvynIPRV 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 218 DDSRPLAEVSDEGYMLYFGRLSREKGVATLLAAHKKmqNKAPLKVVGHGPLHDELAA-----KYPDVEFLGYVQQGEALD 292
Cdd:cd03795   180 DFENIKREKKGKKIFLFIGRLVYYKGLDYLIEAAQY--LNYPIVIGGEGPLKPDLEAqielnLLDNVKFLGRVDDEEKVI 257

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 293 nLIKHARAVILPS-ECYENCSMAILEAMSLGKPVIGSRIG-GIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARN 370
Cdd:cd03795   258 -YLHLCDVFVFPSvLRSEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRES 336

                         410
                  ....*....|...
gi 2524478152 371 MGLHGRARLSEKY 383
Cdd:cd03795   337 YGENAKKRFEELF 349
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 14-397 3.89e-24

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 102.39  E-value: 3.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  14 GGAETvyfQERDMLKQA---GVQVIDFSMQHENNFPSDYADYfvsNVDYHkasnLLGgiktaVNFIHNSQACKKMLALLE 90
Cdd:cd03807    12 GGAET---MLLRLLEHMdksRFEHVVISLTGDGVLGEELLAA---GVPVV----CLG-----LSSGKDPGVLLRLAKLIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  91 IERPDIVHFHNiYHQLTPALIKVARNFGCKTVLTAHDykIVCPAYSMLRDGKVCdscitgtvfnafryrcqegsasksll 170
Cdd:cd03807    77 KRNPDVVHTWM-YHADLIGGLAAKLAGGVKVIWSVRS--SNIPQRLTRLVRKLC-------------------------- 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 171 lsleatwqYIAQNYQALDVIVSPSVFLRgVLLRTLPNSRIDVIVNGVD------------DSRPLAEVSDEGYML-YFGR 237
Cdd:cd03807   128 --------LLLSKFSPATVANSSAVAEF-HQEQGYAKNKIVVIYNGIDlfklspddasraRARRRLGLAEDRRVIgIVGR 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 238 LSREKGVATLLAAHKKMQNKAP---LKVVGHGPLHDEL-----AAKYPD-VEFLGYVQQGEALdnlIKHARAVILPSeCY 308
Cdd:cd03807   199 LHPVKDHSDLLRAAALLVETHPdlrLLLVGRGPERPNLerlllELGLEDrVHLLGERSDVPAL---LPAMDIFVLSS-RT 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 309 ENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVeGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEKYALSKH 388
Cdd:cd03807   275 EGFPNALLEAMACGLPVVATDVGGAAELVDDGT-GFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAM 353


                  ....*....
gi 2524478152 389 MDTLQALYK 397
Cdd:cd03807   354 VRRYETLYY 362
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 189-376 2.27e-23

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 99.74  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 189 VIVSPSVflRGVLLRTLPNS--RIDVIVNGVDDSRPLAEVSDEGYM-----------LYFGRLSREKGVATLLAAHKKMQ 255
Cdd:cd03819   131 IAVSELV--RDHLIEALGVDpeRIRVIPNGVDTDRFPPEAEAEERAqlglpegkpvvGYVGRLSPEKGWLLLVDAAAELK 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 256 NKAP--LKVVGHGPLHDELAAKY------PDVEFLGYVqqgEALDNLIKHARAVILPSEcYENCSMAILEAMSLGKPVIG 327
Cdd:cd03819   209 DEPDfrLLVAGDGPERDEIRRLVerlglrDRVTFTGFR---EDVPAALAASDVVVLPSL-HEEFGRVALEAMACGTPVVA 284

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2524478152 328 SRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGR 376
Cdd:cd03819   285 TDVGGAREIVVHGRTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAA 333
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 184-399 7.99e-22

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 95.81  E-value: 7.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 184 YQALDVIVSPSVFLRGVLLRTLPNSRIDVIVNGVDDSRPLAEVS----------DEGYML-YFGRLSREKGVATLLAAHK 252
Cdd:cd03817   145 YNHTDAVIAPSEKIKDTLREYGVKGPIEVIPNGIDLDKFEKPLNteerrklglpPDEPILlYVGRLAKEKNIDFLLRAFA 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 253 --KMQNKAPLKVVGHGPLHDELAA------KYPDVEFLGYVQQGEaLDNLIKHARAVILPSEcYENCSMAILEAMSLGKP 324
Cdd:cd03817   225 elKKEPNIKLVIVGDGPEREELKElarelgLADKVIFTGFVPREE-LPEYYKAADLFVFAST-TETQGLVYLEAMAAGLP 302

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524478152 325 VIGSRIGGIPEQIRDGVEGILFEPGNAqELANAMDALADSPEKARNMGLHGRARlSEKYALSKhmdTLQALYKEL 399
Cdd:cd03817   303 VVAAKDPAASELVEDGENGFLFEPNDE-TLAEKLLHLRENLELLRKLSKNAEIS-AREFAFAK---SVEKLYEEV 372
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 183-387 2.03e-21

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 94.23  E-value: 2.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 183 NYQALDVIVspsVFLRGVLLRT--LPNSRIDVIVNGVDD--SRPLAEVSDEgYMLYFGRLSREKGVATLLAAHKKMQNKA 258
Cdd:cd03820   135 LYKRADKIV---VLTEADKLKKykQPNSNVVVIPNPLSFpsEEPSTNLKSK-RILAVGRLTYQKGFDLLIEAWALIAKKH 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 259 P---LKVVGHGPLHDELAAKYPD------VEFLGYVQQgeaLDNLIKHARAVILPSEcYENCSMAILEAMSLGKPVIGSR 329
Cdd:cd03820   211 PdwkLRIYGDGPEREELEKLIDKlgledrVKLLGPTKN---IAEEYANSSIFVLSSR-YEGFPMVLLEAMAYGLPIISFD 286

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2524478152 330 I-GGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARlSEKYALSK 387
Cdd:cd03820   287 CpTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKN-AERFSIEK 344
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 208-392 1.03e-20

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 93.07  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 208 SRIDVIVNGVDDSR------------PLAEVSDEGYMLYFGRLSREKGVATLLAAHKKM---QNKAPLKVVGhGP----- 267
Cdd:cd03800   187 SRINVVPPGVDLERffpvdraearraRLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLpelRELANLVLVG-GPsddpl 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 268 -----LHDELAAKY---PDVEFLGYVQQGEaLDNLIKHARAVILPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRD 339
Cdd:cd03800   266 smdreELAELAEELgliDRVRFPGRVSRDD-LPELYRAADVFVVPSL-YEPFGLTAIEAMACGTPVVATAVGGLQDIVRD 343

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2524478152 340 GVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEKYALSKHMDTL 392
Cdd:cd03800   344 GRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQL 396
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 196-400 2.00e-20

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. 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. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. 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, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 91.71  E-value: 2.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 196 FLRGVLlrTLPNSRIDVIVNGVDDSR------PLAEVS-------DEGYMLYFGRLSREKGVATLLAAHKKMQNKAP--- 259
Cdd:TIGR03088 150 WLRGPV--KVPPAKIHQIYNGVDTERfhpsrgDRSPILppdffadESVVVGTVGRLQAVKDQPTLVRAFALLVRQLPega 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 260 ----LKVVGHGPLHDELAAKYpDVEFLGYVQQ--GEALD--NLIKHARAVILPSECyENCSMAILEAMSLGKPVIGSRIG 331
Cdd:TIGR03088 228 erlrLVIVGDGPARGACEQMV-RAAGLAHLVWlpGERDDvpALMQALDLFVLPSLA-EGISNTILEAMASGLPVIATAVG 305

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524478152 332 GIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEKYALSKHMDTLQALYKELL 400
Cdd:TIGR03088 306 GNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSINAMVAAYAGLYDQLL 374
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 204-380 1.30e-19

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 88.88  E-value: 1.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 204 TLPNSRIDVIVNGVDDSRPLAEVSDEGYMLYFGRLSREKGVATLLAAHKkmQNKAPLKVVGhgPLHDELAAKY------- 276
Cdd:cd03802   144 TPPIDYLTVVHNGLDPADYRFQPDPEDYLAFLGRIAPEKGLEDAIRVAR--RAGLPLKIAG--KVRDEDYFYYlqeplpg 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 277 PDVEFLGYVQQGEALDnLIKHARAVILPSECYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGnaQELAN 356
Cdd:cd03802   220 PRIEFIGEVGHDEKQE-LLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDSV--EEMAE 296

                         170       180
                  ....*....|....*....|....*
gi 2524478152 357 AMDALAD-SPEKARnmgLHGRARLS 380
Cdd:cd03802   297 AIANIDRiDRAACR---RYAEDRFS 318
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 236-392 2.89e-19

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 88.28  E-value: 2.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 236 GRLSREKGVATLLAAHKKMQNKAP---LKVVGHGPLHDELAAKYPD------VEFLGYVQQGEALDnLIKHARAVILPSE 306
Cdd:cd03799   181 GRLTEKKGLEYAIEAVAKLAQKYPnieYQIIGDGDLKEQLQQLIQElnigdcVKLLGWKPQEEIIE-ILDEADIFIAPSV 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 307 CYENCSM-----AILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSE 381
Cdd:cd03799   260 TAADGDQdgppnTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEE 339

                         170
                  ....*....|.
gi 2524478152 382 KYALSKHMDTL 392
Cdd:cd03799   340 EYDINKLNDEL 350
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 188-399 2.93e-19

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 88.56  E-value: 2.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 188 DVIVSPSVFLRGVLLRTLPNSR-IDVIVNGVD-----------DSRPLAEVSDEGYMLYFGRLSREKGVATLLAAHKKMQ 255
Cdd:cd04962   143 DRVTAVSSSLRQETYELFDVDKdIEVIHNFIDedvfkrkpagaLKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVR 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 256 NKAPLKV--VGHGPLHD---ELAAKY---PDVEFLGYVqqgEALDNLIKHARAVILPSEcYENCSMAILEAMSLGKPVIG 327
Cdd:cd04962   223 RKIPAKLllVGDGPERVpaeELARELgveDRVLFLGKQ---DDVEELLSIADLFLLPSE-KESFGLAALEAMACGVPVVS 298

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524478152 328 SRIGGIPEQIRDGVEGILFEPGNAQELA-NAMDALADsPEKARNMGLHGRARLSEKYALSKHMDTLQALYKEL 399
Cdd:cd04962   299 SNAGGIPEVVKHGETGFLSDVGDVDAMAkSALSILED-DELYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 232-383 8.13e-18

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 84.76  E-value: 8.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 232 MLYFGRLSREKGVATLlaahKKMQNKAP---LKVVGHGPLHDELAAKYPD--VEFLGYVQqGEALDNLIKHARAVILPSE 306
Cdd:PLN02871  266 IVYVGRLGAEKNLDFL----KRVMERLPgarLAFVGDGPYREELEKMFAGtpTVFTGMLQ-GDELSQAYASGDVFVMPSE 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 307 CyENCSMAILEAMSLGKPVIGSRIGGIPEQIRD---GVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLsEKY 383
Cdd:PLN02871  341 S-ETLGFVVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEV-EKW 418
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 233-346 1.14e-17

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 81.68  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 233 LYFGRLSREKGVATLLAA---HKKMQNKAPLKVVGHGPLHDELAAKY------PDVEFLGYVQQGEALDNLIKHARAVIL 303
Cdd:cd01635   114 VSVGRLVPEKGIDLLLEAlalLKARLPDLVLVLVGGGGEREEEEALAaalgllERVVIIGGLVDDEVLELLLAAADVFVL 193

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2524478152 304 PSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILF 346
Cdd:cd01635   194 PSR-SEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 89-377 4.40e-16

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 78.95  E-value: 4.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  89 LEIERPDIVHFHNIYHQLTPALIKVARNFGCKTVLTAHDykIVCPaysMLRDGKvcdscitgTVFNAfryrcqegsasks 168
Cdd:cd03821    86 RNLREYDVVHIHGVWTYTSLAACKLARRRGIPYVVSPHG--MLDP---WALQQK--------HWKKR------------- 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 169 lllsleatWQYIAQNYQALD----VIVSPSVFLRgVLLRTLPNSRIDVIVNGVD---------DSRPLAEVSDEGYMLYF 235
Cdd:cd03821   140 --------IALHLIERRNLNnaalVHFTSEQEAD-ELRRFGLEPPIAVIPNGVDipefdpglrDRRKHNGLEDRRIILFL 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 236 GRLSREKGVATLLAAHKKMQNKAP---LKVVGHGP-LHDELAAKY------PDVEFLGYVQqGEALDNLIKHARAVILPS 305
Cdd:cd03821   211 GRIHPKKGLDLLIRAARKLAEQGRdwhLVIAGPDDgAYPAFLQLQsslglgDRVTFTGPLY-GEAKWALYASADLFVLPS 289

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524478152 306 EcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVeGILFEPgNAQELANAMDALADSPEKARNMGLHGRA 377
Cdd:cd03821   290 Y-SENFGNVVAEALACGLPVVITDKCGLSELVEAGC-GVVVDP-NVSSLAEALAEALRDPADRKRLGEMARR 358
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 176-388 1.27e-15

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 77.75  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 176 TWQYIAQNYQALDVIVS-PSVFLR-GVLLRT--LPNSrIDVI------VNGVDDSRPLAEVS----DEGYMLYFGRLSRE 241
Cdd:cd03792   131 VWDFLWNYIEGYDLFVFhPPEFVPpQVPPPKfyIPPS-IDPLsgknkdLSPADIRYYLEKPFvidpERPYILQVARFDPS 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 242 KGVATLLAAHKKMQNKAP---LKVVGHGPLHDELAA-------KYPDVEFLGYVQQ---GEALDNLIKHARAVILPSECY 308
Cdd:cd03792   210 KDPLGVIDAYKLFKRRAEepqLVICGHGAVDDPEGSvvyeevmEYAGDDHDIHVLRlppSDQEINALQRAATVVLQLSTR 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 309 ENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPG--NAQELanaMDALADsPEKARNMGLHGRARLSEKYALS 386
Cdd:cd03792   290 EGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVegAAVRI---LRLLTD-PELRRKMGLAAREHVRDNFLIT 365


                  ..
gi 2524478152 387 KH 388
Cdd:cd03792   366 GN 367
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
 75-378 2.73e-15

glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273969 [Multi-domain]  Cd Length: 473  Bit Score: 77.31  E-value: 2.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  75 FIHNSQACKKMLALLEiERPDIVHFHNIYHQLTPALIK-VARNFGCKTVLTAH--DYKIVCPAYSMLRDGKVCDSCitgt 151
Cdd:TIGR02095 111 FAFFSRAAAELLSGLG-WQPDVVHAHDWHTALVPALLKaVYRPNPIKTVFTIHnlAYQGVFPADDFSELGLPPEYF---- 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 152 VFNAFRYRCQegsaskslllsleATWQYIAQNYQALDVIVSPSVFL------RGVLLRTLPNSRIDV---IVNGVD---- 218
Cdd:TIGR02095 186 HMEGLEFYGR-------------VNFLKGGIVYADRVTTVSPTYAReiltpeFGYGLDGVLKARSGKlrgILNGIDtevw 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 219 ------------DSRPLA---------------EVSDEGYMLYF-GRLSREKGVATLLAA-HKKMQNKAPLKVVGHGPLH 269
Cdd:TIGR02095 253 npatdpylkanySADDLAgkaenkealqeelglPVDDDVPLFGViSRLTQQKGVDLLLAAlPELLELGGQLVVLGTGDPE 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 270 DE-----LAAKYPD--VEFLGYvqqGEALDNLIkHARA--VILPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDG 340
Cdd:TIGR02095 333 LEealreLAERYPGnvRVIIGY---DEALAHLI-YAGAdfILMPSR-FEPCGLTQLYAMRYGTVPIVRRTGGLADTVVDG 407

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2524478152 341 VE------GILFEPGNAQELANAM----DALADSPEKARNMGLHGRAR 378
Cdd:TIGR02095 408 DPeaesgtGFLFEEYDPGALLAALsralRLYRQDPSLWEALQKNAMSQ 455
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
190-383 3.55e-14

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 73.29  E-value: 3.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 190 IVSPSVFLRGVLLRTLPNSRIDVIVNGVDDS-----------RPLAEVSDEGYMLYFGRLSREKGVATLLAAHKKM---Q 255
Cdd:PRK15484  143 IIVPSQFLKKFYEERLPNADISIVPNGFCLEtyqsnpqpnlrQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLataH 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 256 NKAPLKVVG-------------HGPLHDELAAKYPDVEFLGYvQQGEALDNLIKHARAVILPSECYENCSMAILEAMSLG 322
Cdd:PRK15484  223 SNLKLVVVGdptasskgekaayQKKVLEAAKRIGDRCIMLGG-QPPEKMHNYYPLADLVVVPSQVEEAFCMVAVEAMAAG 301

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524478152 323 KPVIGSRIGGIPEQIRDGVEGI-LFEPGNAQELANAMDALADSPEKArNMGLHGRARLSEKY 383
Cdd:PRK15484  302 KPVLASTKGGITEFVLEGITGYhLAEPMTSDSIISDINRTLADPELT-QIAEQAKDFVFSKY 362
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 211-383 5.43e-14

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 72.70  E-value: 5.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 211 DVIVNGVDDSRPLAEVSDEGYMLYFGRLSREKGVATLLAAHKKMQNkaPLKVVGHGPLHDELAAKY-PDVEFLGYVQQGE 289
Cdd:cd03804   181 TVIYPPVDTDAFAPAADKEDYYLTASRLVPYKRIDLAVEAFNELPK--RLVVIGDGPDLDRLRAMAsPNVEFLGYQPDEV 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 290 ALDNLIKhARAVILPSEcyENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALAD-----S 364
Cdd:cd03804   259 LKELLSK-ARAFVFAAE--EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEFEQnfdrfK 335

                         170       180
                  ....*....|....*....|
gi 2524478152 365 PEKAR-NMGLHGRARLSEKY 383
Cdd:cd03804   336 PQAIRaNAERFSRARFRQEI 355
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 206-397 5.03e-13

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 70.44  E-value: 5.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 206 PNSRIDVIVNGVDDSR--PLAEVSDEGYML---YFGRLSREKGVATLLAAHKKMQNKAP---LKVVGhGPLHDELAAKY- 276
Cdd:cd03813   265 DPDKTRVIPNGIDIQRfaPAREERPEKEPPvvgLVGRVVPIKDVKTFIRAFKLVRRAMPdaeGWLIG-PEDEDPEYAQEc 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 277 ----------PDVEFLGYVQQGEALDNLikharAVILPSECYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVE---- 342
Cdd:cd03813   344 krlvaslgleNKVKFLGFQNIKEYYPKL-----GLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIYGADDalgq 418

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2524478152 343 -GILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEKYALSKHMDTLQALYK 397
Cdd:cd03813   419 aGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 232-390 2.34e-12

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 67.33  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 232 MLYFGRLSREKGVATLLAAHKKMQNKAP---LKVVGHGP-------LHDEL-AAKYpdVEFLGYVQQgeaLDNLIKHARA 300
Cdd:cd04949   163 IITISRLAPEKQLDHLIEAVAKAVKKVPeitLDIYGYGEereklkkLIEELhLEDN--VFLKGYHSN---LDQEYQDAYL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 301 VILPSEcYENCSMAILEAMSLGKPVIGSRIG-GIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRArL 379
Cdd:cd04949   238 SLLTSQ-MEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYK-I 315

                         170
                  ....*....|.
gi 2524478152 380 SEKYALSKHMD 390
Cdd:cd04949   316 AEKYSTENVME 326
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 188-392 1.21e-11

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 65.69  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 188 DVIVSPSVFLRGVLLRTLPN---------------SRIDVIVNGVDDSRPLAeVSDEGYMLYFGRLSREKGVA-TLLAAH 251
Cdd:cd03805   156 DQIVVNSNFTAGVFKKTFPSlaknppevlypcvdtDSFDSTSEDPDPGDLIA-KSNKKFFLSINRFERKKNIAlAIEAFA 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 252 K---KMQNKAPLKVV---GHGP-------LHDEL---AAKYPD----VEFLGYVQQGEALdNLIKHARAVIL-PSecYEN 310
Cdd:cd03805   235 KlkqKLPEFENVRLViagGYDPrvaenveYLEELqrlAEELLNvedqVLFLRSISDSQKE-QLLSSALALLYtPS--NEH 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 311 CSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPgNAQELANAMDALADSPEKARNMGLHGRARLSEKYALSKHMD 390
Cdd:cd03805   312 FGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAE 390


                  ..
gi 2524478152 391 TL 392
Cdd:cd03805   391 RL 392
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 79-371 4.15e-10

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 61.04  E-value: 4.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  79 SQACKKMLALLEIeRPDIVHFHNiYHQ-LTPALIKVARN----FGCKTVLTAH--DYKIVCPAYSMLRDGKVCDscitgt 151
Cdd:cd03791   115 SRAALELLRRLGF-QPDIIHAND-WHTaLVPAYLKTRYRgpgfKKIKTVFTIHnlAYQGLFPLDTLAELGLPPE------ 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 152 vfnafrYRCQEGSaskslllsleatWQYIAQNY-----QALDVI--VSPS--------VFLRGV--LLRTLpNSRIDVIV 214
Cdd:cd03791   187 ------LFHIDGL------------EFYGQINFlkagiVYADRVttVSPTyakeiltpEYGEGLdgVLRAR-AGKLSGIL 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 215 NGVD----------------DSRPLA---------------EVSDEGYMLYF-GRLSREKGVATLL-AAHKKMQNKAPLK 261
Cdd:cd03791   248 NGIDydewnpatdklipanySANDLEgkaenkaalqkelglPVDPDAPLFGFvGRLTEQKGVDLILdALPELLEEGGQLV 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 262 VVGHGPLHDE-----LAAKYPDVE--FLGYVqqgEALDNLI-KHARAVILPSEcYENCSMAILEAMSLGKPVIGSRIGGI 333
Cdd:cd03791   328 VLGSGDPEYEqafreLAERYPGKVavVIGFD---EALAHRIyAGADFFLMPSR-FEPCGLVQMYAMRYGTLPIVRRTGGL 403

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2524478152 334 PEQIRDGVE------GILFEPGNAQELANAMD---ALADSPEKARNM 371
Cdd:cd03791   404 ADTVFDYDPetgegtGFVFEDYDAEALLAALRralALYRNPELWRKL 450
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 312-385 5.46e-10

Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 60.45  E-value: 5.46e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524478152 312 SMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEKYAL 385
Cdd:cd03818   314 SWSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSL 387
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
301-394 3.08e-09

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 53.76  E-value: 3.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 301 VILPSECYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGILFEpgNAQELANAMDALADSPEKARNMGLHGRARLS 380
Cdd:pfam13524   2 VLNPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERVL 79

                          90
                  ....*....|....
gi 2524478152 381 EKYALSKHMDTLQA 394
Cdd:pfam13524  80 AEHTYAHRAEQLLD 93
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
203-355 3.44e-09

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 57.80  E-value: 3.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 203 RTLPNSRIDVIVNGVDDSR---PLAEVSDEGYMLYFGRLSRE--KGVATLLAAHKKMQNKAPLKVVGHGPLHDELAAKYP 277
Cdd:PRK09922  151 RGISAQRISVIYNPVEIKTiiiPPPERDKPAVFLYVGRLKFEgqKNVKELFDGLSQTTGEWQLHIIGDGSDFEKCKAYSR 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 278 DVE------FLGYVQQG-EALDNLIKHARAVILPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQ-IRDGVEGILFEPG 349
Cdd:PRK09922  231 ELGieqriiWHGWQSQPwEVVQQKIKNVSALLLTSK-FEGFPMTLLEAMSYGIPCISSDCMSGPRDiIKPGLNGELYTPG 309


                  ....*.
gi 2524478152 350 NAQELA 355
Cdd:PRK09922  310 NIDEFV 315
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 14-371 4.02e-08

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 54.76  E-value: 4.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  14 GGAETVYFQERDMLKQAGVQVIDFSMQHENNF-PSDYADYFVSnvdyhkasnlLGGIKTAVNFIHNSQACKKMLALLeie 92
Cdd:cd04951    12 GGAEKQTVLLADQMFIRGHDVNIVYLTGEVEVkPLNNNIIIYN----------LGMDKNPRSLLKALLKLKKIISAF--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  93 RPDIVH---FH-NIYHQLTPALIKVarnfgcktvltahdYKIVCPAYSMLRDGKVcdscitgtvfNAFRYRCQEGSASKS 168
Cdd:cd04951    79 KPDVVHshmFHaNIFARFLRMLYPI--------------PLLICTAHNKNEGGRI----------RMFIYRLTDFLCDIT 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 169 LLLSLEATWQYIAQnyqaldvivspsvflrgvllRTLPNSRIDVIVNGVDDSR-------------PLAEVSDEGYMLYF 235
Cdd:cd04951   135 TNVSREALDEFIAK--------------------KAFSKNKSVPVYNGIDLNKfkkdinvrlkirnKLNLKNDEFVILNV 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 236 GRLSREKGVATLLAAHKKM---QNKAPLKVVGHGPLHDELAAKYPD------VEFLGYVQQGEALDNLikhARAVILPSE 306
Cdd:cd04951   195 GRLTEAKDYPNLLLAISELilsKNDFKLLIAGDGPLRNELERLICNlnlvdrVILLGQISNISEYYNA---ADLFVLSSE 271

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524478152 307 cYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDgvEGILFEPGNAQELANAMDALADSPEKARNM 371
Cdd:cd04951   272 -WEGFGLVVAEAMACERPVVATDAGGVAEVVGD--HNYVVPVSDPQLLAEKIKEIFDMSDEERDI 333
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
14-220 4.52e-08

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 52.53  E-value: 4.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  14 GGAETVYFQERDMLKQAGVQVIDFSmqheNNFPSDYADYFVSNVDYHKASNLLGGiktavNFIHNSQACKKMLALLEIER 93
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVT----PGGPGPLAEEVVRVVRVPRVPLPLPP-----RLLRSLAFLRRLRRLLRRER 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152  94 PDIVHFHNiYHQLTPALIKVARNFGCKTVLTAHdykivcpaysmlrdgkvcdscitGTVFNAFRYRcqegsasKSLLLSL 173
Cdd:pfam13439  72 PDVVHAHS-PFPLGLAALAARLRLGIPLVVTYH-----------------------GLFPDYKRLG-------ARLSPLR 120

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2524478152 174 EATWQYIAQNYQALDVIVSPSVFLRGVLLRT--LPNSRIDVIVNGVDDS 220
Cdd:pfam13439 121 RLLRRLERRLLRRADRVIAVSEAVADELRRLygVPPEKIRVIPNGVDLE 169
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 180-400 2.83e-06

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 48.92  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 180 IAQNYQALDVIVSPSVFLRGVLLRTL-------PNSRIDVIVNGVDD--SRPLAEVSDEGY------MLYFGRLSREKGV 244
Cdd:cd03822   123 QALKVLFRIATLSERVVVMAPISRFLlvrikliPAVNIEVIPHGVPEvpQDPTTALKRLLLpegkkvILTFGFIGPGKGL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 245 ATLLAAHKKMQNKAP-LKVVGHGPLHDELA------AKYPDVEFLG----------YVQQGEALDnLIKHARAVILPsec 307
Cdd:cd03822   203 EILLEALPELKAEFPdVRLVIAGELHPSLAryegerYRKAAIEELGlqdhvdfhnnFLPEEEVPR-YISAADVVVLP--- 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 308 YEN----CSMAILEAMSLGKPVIGSRIGGIPEQIRDGvEGILFEPGNAQELANAMDALADSPEKARNMglhgrARLSEKY 383
Cdd:cd03822   279 YLNteqsSSGTLSYAIACGKPVISTPLRHAEELLADG-RGVLVPFDDPSAIAEAILRLLEDDERRQAI-----AERAYAY 352

                         250
                  ....*....|....*..
gi 2524478152 384 ALSKHMDTLQALYKELL 400
Cdd:cd03822   353 ARAMTWESIADRYLRLF 369
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 263-383 3.17e-06

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 49.00  E-value: 3.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 263 VGHGPLHDE---LAAKYPD---VEFLGYVQQGEALDNLIKHARAVILPSECYENCSMAILEAMSLGKPVIGSRIGGIPEQ 336
Cdd:cd04946   263 IGGGPLKERlekLAENKLEnvkVNFTGEVSNKEVKQLYKENDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREI 342

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2524478152 337 IRDGVEG-ILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEKY 383
Cdd:cd04946   343 VENETNGlLLDKDPTPNEIVSSIMKFYLDGGDYKTMKISARECWEERF 390
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 205-397 3.47e-06

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 49.26  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 205 LPNSRIDVIVNGVDDSRPLAEVSDEGYMLYFGRLSRE--KGVATLL---------------AAHKKMQNKAPLKVVGHGP 267
Cdd:PRK15179  479 VDERRIPVVYNGLAPLKSVQDDACTAMMAQFDARTSDarFTVGTVMrvddnkrpflwveaaQRFAASHPKVRFIMVGGGP 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 268 LHD---ELAAKYPDVEFLGYVQQGEALDNLIKHARAVILPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVEGI 344
Cdd:PRK15179  559 LLEsvrEFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSR-FEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGL 637

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2524478152 345 LF------EPGNAQELANAMDALADSPEKARnmglHGRARLSEKYALSKHMDTLQALYK 397
Cdd:PRK15179  638 TLpadtvtAPDVAEALARIHDMCAADPGIAR----KAADWASARFSLNQMIASTVRCYQ 692
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 202-335 8.14e-06

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 47.62  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 202 LRT-LPNSRIDVIVNGVDDSR----PLAEVSDEGYMLYFGRLSREKGVATLLAAHKKMQNKAP---LKVVGHGPLHDELA 273
Cdd:cd03796   161 LRAsLDPRIVSVIPNAVDSSDftpdPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPnvrFIIGGDGPKRIELE 240

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524478152 274 A---KY---PDVEFLGYVQQGEAldnlikhaRAVILPSECYENCS------MAILEAMSLGKPVIGSRIGGIPE 335
Cdd:cd03796   241 EmreKYqlqDRVELLGAVPHEEV--------RDVLVQGHIFLNTSlteafcIAIVEAASCGLLVVSTRVGGIPE 306
PRK14099 PRK14099
glycogen synthase GlgA;
233-402 8.42e-06

glycogen synthase GlgA;


Pssm-ID: 237610 [Multi-domain]  Cd Length: 485  Bit Score: 47.79  E-value: 8.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 233 LYFG---RLSREKGVATLLAA-HKKMQNKAPLKVVGHG--PLHDEL---AAKYPDV--EFLGYvqqGEALDNLIKH-ARA 300
Cdd:PRK14099  296 LLLGvisRLSWQKGLDLLLEAlPTLLGEGAQLALLGSGdaELEARFraaAQAYPGQigVVIGY---DEALAHLIQAgADA 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 301 VILPSEcYENCSMAILEAMSLGKPVIGSRIGGIPEQIRDGVE---------GILFEPGNAQELANAMD---ALADSPEKA 368
Cdd:PRK14099  373 LLVPSR-FEPCGLTQLCALRYGAVPVVARVGGLADTVVDANEmaiatgvatGVQFSPVTADALAAALRktaALFADPVAW 451

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2524478152 369 RNMGLHGRA------RLSEKYAlskhmdtlqALYKELLSR 402
Cdd:PRK14099  452 RRLQRNGMTtdvswrNPAQHYA---------ALYRSLVAE 482
KdtA COG1519
3-deoxy-D-manno-octulosonic-acid transferase [Cell wall/membrane/envelope biogenesis]; ...
 315-399 5.51e-05

3-deoxy-D-manno-octulosonic-acid transferase [Cell wall/membrane/envelope biogenesis]; 3-deoxy-D-manno-octulosonic-acid transferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 441128 [Multi-domain]  Cd Length: 424  Bit Score: 45.13  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 315 ILEAMSLGKPVI-GSRIGGIPEQIRDGVE-GILFEPGNAQELANAMDALADSPEKARNMGLHGRARLSEKY-ALSKHMDT 391
Cdd:COG1519   337 PLEPAALGKPVLfGPHTFNFAEAAELLIAaGAAIQVADAEELAAAVLALLADPELRAAMGAAARAVVEANRgATDRTLAA 416


                  ....*...
gi 2524478152 392 LQALYKEL 399
Cdd:COG1519   417 LEPLLPQA 424
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
233-395 1.56e-04

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 43.43  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 233 LYFGRLSREKGVATLLAAHKKMQNKAPLKVV--GHGPLHDEL-----AAKYPDVEFLGyVQQGEALDNLIKHA------- 298
Cdd:PRK10307  233 LYSGNIGEKQGLELVIDAARRLRDRPDLIFVicGQGGGKARLekmaqCRGLPNVHFLP-LQPYDRLPALLKMAdchllpq 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524478152 299 RA----VILPSEcyencsmaiLEAM-SLGKPVI-----GSRIGgipeQIRDGVeGILFEPGNAQELANAMDALADSPEKA 368
Cdd:PRK10307  312 KAgaadLVLPSK---------LTNMlASGRNVVataepGTELG----QLVEGI-GVCVEPESVEALVAAIAALARQALLR 377

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2524478152 369 RNMGLHGR----ARLSEKYALSKHMDTLQAL 395
Cdd:PRK10307  378 PKLGTVAReyaeRTLDKENVLRQFIADIRGL 408
 
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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