NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1539789114|emb|VEE50758|]
View 

lipopolysaccharide core biosynthesis glycosyl transferase [Stenotrophomonas maltophilia]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 7-361 1.38e-58

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: 194.29  E-value: 1.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114   7 ILHTEAAKGMGGQEIYIFRHMQVMRARGHEVALLCQPEARLAQLARDDGFTVHTLRMGGLLRLLRGIW-SVSRLVRRERY 85
Cdd:cd03801     4 LLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLrELRPLLRLRKF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  86 DVVNTTSRRDALIAAAGARLGGTPLVVRSRHLMSPVNSLLT------------YTGLPHRVLTVSSFVKQLLAER-GIPA 152
Cdd:cd03801    84 DVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLaaerrllaraeaLLRRADAVIAVSEALRDELRALgGIPP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 153 EYIGIVPPIAVPPRWSeirkddpwqglqevrAEVRAELGFGEQDIVVGCVAVLREPKGHADLLQAMVPLCKTHPNLHLVV 232
Cdd:cd03801   164 EKIVVIPNGVDLERFS---------------PPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVI 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 233 VGDGQPVMDRLQALrdEHGLQQQVHLLGYRDGA--CRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMV 310
Cdd:cd03801   229 VGGDGPLRAELEEL--ELGLGDRVRFLGFVPDEelPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1539789114 311 VDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAGWDWMRSahRFTPD 361
Cdd:cd03801   307 EDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAE--RFSWE 355
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 7-361 1.38e-58

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: 194.29  E-value: 1.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114   7 ILHTEAAKGMGGQEIYIFRHMQVMRARGHEVALLCQPEARLAQLARDDGFTVHTLRMGGLLRLLRGIW-SVSRLVRRERY 85
Cdd:cd03801     4 LLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLrELRPLLRLRKF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  86 DVVNTTSRRDALIAAAGARLGGTPLVVRSRHLMSPVNSLLT------------YTGLPHRVLTVSSFVKQLLAER-GIPA 152
Cdd:cd03801    84 DVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLaaerrllaraeaLLRRADAVIAVSEALRDELRALgGIPP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 153 EYIGIVPPIAVPPRWSeirkddpwqglqevrAEVRAELGFGEQDIVVGCVAVLREPKGHADLLQAMVPLCKTHPNLHLVV 232
Cdd:cd03801   164 EKIVVIPNGVDLERFS---------------PPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVI 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 233 VGDGQPVMDRLQALrdEHGLQQQVHLLGYRDGA--CRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMV 310
Cdd:cd03801   229 VGGDGPLRAELEEL--ELGLGDRVRFLGFVPDEelPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1539789114 311 VDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAGWDWMRSahRFTPD 361
Cdd:cd03801   307 EDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAE--RFSWE 355
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 196-348 1.16e-34

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: 125.08  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 196 DIVVGCVAVLREPKGHADLLQAMVPLCKTHPNLHLVVVGDGqPVMDRLQALRDEHGLQQQVHLLGYRDGAC--RLMAGFD 273
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDG-EEEKRLKKLAEKLGLGDNVIFLGFVSDEDlpELLKIAD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1539789114 274 IFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAG 348
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENA 155
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 268-376 1.35e-22

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 91.98  E-value: 1.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 268 LMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRA 347
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96

                          90       100
                  ....*....|....*....|....*....
gi 1539789114 348 GWDWMRSahRFTPDGHGETTEHYYHQWLK 376
Cdd:COG0438    97 ARERAEE--RFSWEAIAERLLALYEELLA 123
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 184-354 7.83e-15

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 75.52  E-value: 7.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 184 AEVRAELGFGEQD-IVVGCVAVLREPKGHADLLQAMVPLckthPNLHLVVVGDGqPVMDRLQalrdEHGLQQQVHLLGYR 262
Cdd:PLN02871  250 EEMRARLSGGEPEkPLIVYVGRLGAEKNLDFLKRVMERL----PGARLAFVGDG-PYREELE----KMFAGTPTVFTGML 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 263 DGAcRLMAGF---DIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVD---GSNAILTRLGDNAALTGALRLLVD 336
Cdd:PLN02871  321 QGD-ELSQAYasgDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGDVDDCVEKLETLLA 399

                         170       180
                  ....*....|....*....|....
gi 1539789114 337 DPERRRQMGRAG------WDWMRS 354
Cdd:PLN02871  400 DPELRERMGAAAreevekWDWRAA 423
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 245-348 1.57e-05

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 46.85  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 245 ALRDEHGLQQQVHLLGYRDGAcRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMV--VDGSNAILTRLG 322
Cdd:NF038011  358 SLVASLGLQDKVKFLGFQKID-DLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLIegLDEEDRALGAAG 436

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1539789114 323 ------DNAALTGALRLLVDDPERRRQMGRAG 348
Cdd:NF038011  437 evvaiaDPQALARAALDLLRDPQRWQAAQAAG 468
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 7-361 1.38e-58

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: 194.29  E-value: 1.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114   7 ILHTEAAKGMGGQEIYIFRHMQVMRARGHEVALLCQPEARLAQLARDDGFTVHTLRMGGLLRLLRGIW-SVSRLVRRERY 85
Cdd:cd03801     4 LLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLrELRPLLRLRKF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  86 DVVNTTSRRDALIAAAGARLGGTPLVVRSRHLMSPVNSLLT------------YTGLPHRVLTVSSFVKQLLAER-GIPA 152
Cdd:cd03801    84 DVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLaaerrllaraeaLLRRADAVIAVSEALRDELRALgGIPP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 153 EYIGIVPPIAVPPRWSeirkddpwqglqevrAEVRAELGFGEQDIVVGCVAVLREPKGHADLLQAMVPLCKTHPNLHLVV 232
Cdd:cd03801   164 EKIVVIPNGVDLERFS---------------PPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVI 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 233 VGDGQPVMDRLQALrdEHGLQQQVHLLGYRDGA--CRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMV 310
Cdd:cd03801   229 VGGDGPLRAELEEL--ELGLGDRVRFLGFVPDEelPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1539789114 311 VDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAGWDWMRSahRFTPD 361
Cdd:cd03801   307 EDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAE--RFSWE 355
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 25-348 2.09e-45

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: 159.79  E-value: 2.09e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  25 RHMQVMRARgHEVALLCQPEARLAQLaRDDGFTVHTLRMGGLLRLLRgIWSVSRLVRRERYDVVNTTSRRDALIAAAGAR 104
Cdd:cd03807    23 EHMDKSRFE-HVVISLTGDGVLGEEL-LAAGVPVVCLGLSSGKDPGV-LLRLAKLIRKRNPDVVHTWMYHADLIGGLAAK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 105 L-GGTPLVVRSRHLMSPVNSL-------LTYTGLPHRVLTVSSFVKQLLAERGIPAEYIGIVPPIAVPPRwseIRKDDPw 176
Cdd:cd03807   100 LaGGVKVIWSVRSSNIPQRLTrlvrklcLLLSKFSPATVANSSAVAEFHQEQGYAKNKIVVIYNGIDLFK---LSPDDA- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 177 qglqeVRAEVRAELGFGEQDIVVGCVAVLREPKGHADLLQAMVPLCKTHPNLHLVVVGDGqPVMDRLQALRDEHGLQQQV 256
Cdd:cd03807   176 -----SRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRG-PERPNLERLLLELGLEDRV 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 257 HLLGYRDGACRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSnAILTRLGDNAALTGALRLLVD 336
Cdd:cd03807   250 HLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDGT-GFLVPAGDPQALADAIRALLE 328

                         330
                  ....*....|..
gi 1539789114 337 DPERRRQMGRAG 348
Cdd:cd03807   329 DPEKRARLGRAA 340
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 6-348 1.58e-43

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: 154.68  E-value: 1.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114   6 RILHTEAAKGMggqeIYIFRH--MQVMRARGHEVALLCQPEARLAQLARDDGFTVHTLRMGGLLRLL----RGIWSVSRL 79
Cdd:cd03808     1 KILFIVNVDGG----FQSFRLplIKALVKKGYEVHVIAPDGDKLSDELKELGVKVIDIPILRRGINPlkdlKALFKLYKL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  80 VRRERYDVVNTTSRRDALIAAAGARLGGTPLVVRSRH------LMSPVNSLLTYT------GLPHRVLTVSSFVKQLLAE 147
Cdd:cd03808    77 LKKEKPDIVHCHTPKPGILGRLAARLAGVPKVIYTVHglgfvfTEGKLLRLLYLLleklalLFTDKVIFVNEDDRDLAIK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 148 RG-IPAEYIGIVPPIAVPPrwseirkdDPWQglqevraevRAELGFGEQDIVVGCVAVLREPKGHADLLQAMVPLCKTHP 226
Cdd:cd03808   157 KGiIKKKKTVLIPGSGVDL--------DRFQ---------YSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGP 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 227 NLHLVVVGDGqPVMDRLQALRDEHGLQQQVHLLGYRDGACRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGV 306
Cdd:cd03808   220 NVRFLLVGDG-ELENPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGC 298

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1539789114 307 PEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAG 348
Cdd:cd03808   299 RELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAA 340
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 6-344 1.87e-42

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: 151.74  E-value: 1.87e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114   6 RILHTEAAKGMGGQEIYIFRHMQVMRARGHEVALLCQPEARLAQLARDDGFTV----HTLRMGGLLRLLRGIWSVSRLVR 81
Cdd:cd03811     1 KILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLirllIRVLKLIKLGLLKAILKLKRILK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  82 RERYDVVNTTSRRDALIAAAGArLGGTPLVVR-----SRHLMSPVNSLLTYTGLP--HRVLTVSSFVKQLLAERG-IPAE 153
Cdd:cd03811    81 RAKPDVVISFLGFATYIVAKLA-AARSKVIAWihsslSKLYYLKKKLLLKLKLYKkaDKIVCVSKGIKEDLIRLGpSPPE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 154 YIGIVP-PIavppRWSEIRKDDPwqglqevraevRAELGFGEQDIVVGCVAVLREPKGHADLLQAMVPLCKTHPNLHLVV 232
Cdd:cd03811   160 KIEVIYnPI----DIDRIRALAK-----------EPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVI 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 233 VGDGQPvMDRLQALRDEHGLQQQVHLLGYRDGACRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVD 312
Cdd:cd03811   225 LGDGPL-REELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDD 303

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1539789114 313 GSNAILTRLGDNAALTGALRLLVDDPERRRQM 344
Cdd:cd03811   304 GENGLLVPDGDAAALAGILAALLQKKLDAALR 335
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 5-373 2.18e-36

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: 135.97  E-value: 2.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114   5 LRILHTEAAKGMGGQEIYIFRHMQVMRARGHEVALLCQ-----------PEARLAQLARDDGFTVHTLRMGGLLRLLRGI 73
Cdd:cd03798     2 LILTNIYPNANSPGRGIFVRRQVRALSRRGVDVEVLAPapwgpaaarllRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  74 WSVSRL---VRRERYDVVNTT-SRRDALIAAAGARLGGTPLVVRSRHlmSPVNSLLTYTGL----------PHRVLTVSS 139
Cdd:cd03798    82 PSLAKLlkrRRRGPPDLIHAHfAYPAGFAAALLARLYGVPYVVTEHG--SDINVFPPRSLLrkllrwalrrAARVIAVSK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 140 FVKQLLAERGIPAEYIGIVPpIAVPPRWSEIRKddpwqglqevraevrAELGFGEQDIVVGCVAVLREPKGHADLLQAMV 219
Cdd:cd03798   160 ALAEELVALGVPRDRVDVIP-NGVDPARFQPED---------------RGLGLPLDAFVILFVGRLIPRKGIDLLLEAFA 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 220 PLCKTHPNLHLVVVGDGqPVMDRLQALRDEHGLQQQVHLLGY--RDGACRLMAGFDIFALASHKEAAGTVFLEAAYVGVP 297
Cdd:cd03798   224 RLAKARPDVVLLIVGDG-PLREALRALAEDLGLGDRVTFTGRlpHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLP 302

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1539789114 298 IVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAGwdwMRSAHRFTPDGHGETTEHYYHQ 373
Cdd:cd03798   303 VVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALAEPYLRELGEAAR---ARVAERFSWVKAADRIAAAYRD 375
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 7-348 2.05e-35

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: 132.48  E-value: 2.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114   7 ILHTEAAKGMGGQEIYIFRHMQVMRARGHEVALLCqPEARLAQLARDDGFTVHTLRMGGLLRLLRGIwSVSRLVRRERYD 86
Cdd:cd03819     1 ILMLTPALEIGGAETYILDLARALAERGHRVLVVT-AGGPLLPRLRQIGIGLPGLKVPLLRALLGNV-RLARLIRRERID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  87 VVNTTSRRDALIAAAGARLGGTPLVV-------RSRHLMSPVNSLLTYTglpHRVLTVSSFVKQLLAER-GIPAEyigiv 158
Cdd:cd03819    79 LIHAHSRAPAWLGWLASRLTGVPLVTtvhgsylATYHPKDFALAVRARG---DRVIAVSELVRDHLIEAlGVDPE----- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 159 pPIAVPPRWSEIRKDDPwqglqEVRAEVRAELGFGEQDIVVGCVAVLREPKGHADLLQAMVPLcKTHPNLHLVVVGDGqP 238
Cdd:cd03819   151 -RIRVIPNGVDTDRFPP-----EAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAGDG-P 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 239 VMDRLQALRDEHGLQQQVHLLGYRDGACRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAIL 318
Cdd:cd03819   223 ERDEIRRLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLL 302

                         330       340       350
                  ....*....|....*....|....*....|
gi 1539789114 319 TRLGDNAALTGALRLLVDDPERRRQMGRAG 348
Cdd:cd03819   303 VPPGDAEALADAIRAAKLLPEAREKLQAAA 332
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 196-348 1.16e-34

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: 125.08  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 196 DIVVGCVAVLREPKGHADLLQAMVPLCKTHPNLHLVVVGDGqPVMDRLQALRDEHGLQQQVHLLGYRDGAC--RLMAGFD 273
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDG-EEEKRLKKLAEKLGLGDNVIFLGFVSDEDlpELLKIAD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1539789114 274 IFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAG 348
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENA 155
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
198-337 3.10e-28

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 107.60  E-value: 3.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 198 VVGCVAVLREP-KGHADLLQAMVPLCKTHPNLHLVVVGDGqpVMDRLQALrdEHGLQQQVHLLGYRDGACRLMAGFDIFA 276
Cdd:pfam13692   3 VILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVGDG--PEEELEEL--AAGLEDRVIFTGFVEDLAELLAAADVFV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1539789114 277 LASHKEAAGTVFLEAAYVGVPIVATRVGGVPEmVVDGSNAILTRLGDNAALTGALRLLVDD 337
Cdd:pfam13692  79 LPSLYEGFGLKLLEAMAAGLPVVATDVGGIPE-LVDGENGLLVPPGDPEALAEAILRLLED 138
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 73-374 2.95e-27

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: 110.40  E-value: 2.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  73 IWSVSRLVRRERYDVVNTTSRRD-ALIAAAGARLggtpLVVRSRHlMSPVNSLLTYTGLPHRVLTVSSFVK-QLLAERGI 150
Cdd:cd03820    76 VRRLRKYLKNNKPDVVISFRTSLlTFLALIGLKS----KLIVWEH-NNYEAYNKGLRRLLLRRLLYKRADKiVVLTEADK 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 151 PAEYIGIVPPIAVPPRWseirKDDPWQGLQEVRAEVRAelgfgeqdivvgcVAVLR-EP-KGHADLLQAMVPLCKTHPNL 228
Cdd:cd03820   151 LKKYKQPNSNVVVIPNP----LSFPSEEPSTNLKSKRI-------------LAVGRlTYqKGFDLLIEAWALIAKKHPDW 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 229 HLVVVGDGqPVMDRLQALRDEHGLQQQVHLLGYRDGACRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVAT-RVGGVP 307
Cdd:cd03820   214 KLRIYGDG-PEREELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFdCPTGPS 292

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539789114 308 EMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAGWDwmrSAHRFTPdghgettEHYYHQW 374
Cdd:cd03820   293 EIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARK---NAERFSI-------EKIIKQW 349
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 134-348 4.18e-23

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: 99.28  E-value: 4.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 134 VLTVSSFVKQLLAERGIPAeyigivpPIAVPPRWSEIrkdDPWQGlqEVRAEVRAELGFGEQDIVVGCVAVLREPKGHAD 213
Cdd:cd03817   151 VIAPSEKIKDTLREYGVKG-------PIEVIPNGIDL---DKFEK--PLNTEERRKLGLPPDEPILLYVGRLAKEKNIDF 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 214 LLQAMVPLcKTHPNLHLVVVGDGqPVMDRLQALRDEHGLQQQVHLLGY--RDGACRLMAGFDIFALASHKEAAGTVFLEA 291
Cdd:cd03817   219 LLRAFAEL-KKEPNIKLVIVGDG-PEREELKELARELGLADKVIFTGFvpREELPEYYKAADLFVFASTTETQGLVYLEA 296

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1539789114 292 AYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLvDDPERRRQMGRAG 348
Cdd:cd03817   297 MAAGLPVVAAKDPAASELVEDGENGFLFEPNDETLAEKLLHLR-ENLELLRKLSKNA 352
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 268-376 1.35e-22

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 91.98  E-value: 1.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 268 LMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRA 347
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96

                          90       100
                  ....*....|....*....|....*....
gi 1539789114 348 GWDWMRSahRFTPDGHGETTEHYYHQWLK 376
Cdd:COG0438    97 ARERAEE--RFSWEAIAERLLALYEELLA 123
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 74-348 7.95e-21

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: 92.52  E-value: 7.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  74 WSVSRLVRRE--RYDVVNTTSRRDALIAAAGARLGGTPLVV--------RSRHLMSPVNSLLTYTGLPHRVLT------- 136
Cdd:cd05844    69 WSAPRLGGAAglAPALVHAHFGRDGVYALPLARALGVPLVVtfhgfditTSRAWLAASPGWPSQFQRHRRALQrpaalfv 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 137 -VSSFVKQLLAERGIPAEYIgIVPPIAVPPrwseirkddpwqglqevrAEVRAELGFGEQDIVVgCVAVLREPKGHADLL 215
Cdd:cd05844   149 aVSGFIRDRLLARGLPAERI-HVHYIGIDP------------------AKFAPRDPAERAPTIL-FVGRLVEKKGCDVLI 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 216 QAMVPLCKTHPNLHLVVVGDGqPVMDRLQALRDEHGlqqQVHLLGY--RDGACRLMAGFDIFALAS------HKEAAGTV 287
Cdd:cd05844   209 EAFRRLAARHPTARLVIAGDG-PLRPALQALAAALG---RVRFLGAlpHAEVQDWMRRAEIFCLPSvtaasgDSEGLGIV 284

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1539789114 288 FLEAAYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAG 348
Cdd:cd05844   285 LLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAA 345
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 100-359 1.16e-20

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: 92.04  E-value: 1.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 100 AAGARLGGTPLVV--------RSRHLMSPVNSLLTYTGLP---HR---VLTVSSFVKQLLAER-GIPAEYIGIVPPiAVP 164
Cdd:cd03809    94 TAPLLLKGCPQVVtihdliplRYPEFFPKRFRLYYRLLLPislRRadaIITVSEATRDDIIKFyGVPPEKIVVIPL-GVD 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 165 PRWSEIRKDDPWQGLQEVRAEVraelgfgeqdIVvgCVAVLREPKGHADLLQAMVPLCKTHPNLHLVVVGDGQPVMDRLQ 244
Cdd:cd03809   173 PSFFPPESAAVLIAKYLLPEPY----------FL--YVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEELL 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 245 ALRDEHGLQQQVHLLGY--RDGACRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEmvVDGSNAILTRLG 322
Cdd:cd03809   241 DLVKKLGLGGRVRFLGYvsDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPE--VAGDAALYFDPL 318

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1539789114 323 DNAALTGALRLLVDDPERRRQMGRAGWDWmrsAHRFT 359
Cdd:cd03809   319 DPESIADAILRLLEDPSLREELIRKGLER---AKKFS 352
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 197-308 3.78e-20

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: 91.15  E-value: 3.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 197 IVVGCVAVLRepKGhADLLQAMVP-LCKTHPNLHLVVVGDGqPVMDRLQALRDEHGLQQQVHLLGY--RDGACRLMAGFD 273
Cdd:cd03796   196 IVVISRLVYR--KG-IDLLVGIIPrICKKHPNVRFIIGGDG-PKRIELEEMREKYQLQDRVELLGAvpHEEVRDVLVQGH 271

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1539789114 274 IFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPE 308
Cdd:cd03796   272 IFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPE 306
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 183-368 1.26e-19

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: 89.61  E-value: 1.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 183 RAEVRAELGFGEQDIVVGCVAVLREPKGHADLLQAMVPLCKTHPNLHLVVVGDGQPVMD-----RLQALRDEHGLQQQVH 257
Cdd:cd03800   207 AEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGGPSDDPLsmdreELAELAEELGLIDRVR 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 258 LLGYRDGAcRLMAGF---DIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLL 334
Cdd:cd03800   287 FPGRVSRD-DLPELYraaDVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRL 365

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1539789114 335 VDDPERRRQMGRAGWDwmRSAHRFTPDGHGETTE 368
Cdd:cd03800   366 LDDPALWQRLSRAGLE--RARAHYTWESVADQLL 397
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 202-348 1.82e-19

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: 88.49  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 202 VAVLREPKGHADLLQAMVPLckthpNLHLVVVGDGqPVMDRLQALRDEHGLQQqVHLLGYRD--------GACrlmagfD 273
Cdd:cd03795   197 IGRLVYYKGLDYLIEAAQYL-----NYPIVIGGEG-PLKPDLEAQIELNLLDN-VKFLGRVDdeekviylHLC------D 263

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539789114 274 IFALASH--KEAAGTVFLEAAYVGVPIVATRVG-GVPEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAG 348
Cdd:cd03795   264 VFVFPSVlrSEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENA 341
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 133-371 2.55e-18

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: 85.48  E-value: 2.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 133 RVLTVSSFVKQLLAErgipaeYIGIVPPIAVPPRWSEIRKDDPwqglQEVRAEVRAELGFGEQDIVVGcVAVLREPKGHA 212
Cdd:cd04962   144 RVTAVSSSLRQETYE------LFDVDKDIEVIHNFIDEDVFKR----KPAGALKRRLLAPPDEKVVIH-VSNFRPVKRID 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 213 DLLQAMVPLCKTHPNlHLVVVGDGqPVMDRLQALRDEHGLQQQVHLLGYRDGACRLMAGFDIFALASHKEAAGTVFLEAA 292
Cdd:cd04962   213 DVVRVFARVRRKIPA-KLLLVGDG-PERVPAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAM 290

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1539789114 293 YVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAGWDWMRSahRFTPDGHGETTEHYY 371
Cdd:cd04962   291 ACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAE--RFDPERIVPQYEAYY 367
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 84-358 5.42e-18

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: 84.34  E-value: 5.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  84 RYDVVNTTSRRD--ALIAAAGARLGGTPLVVRSR-------HLMSPVNSLLTYTGLPHRVLTVSSFVKQLLAERGIPAEY 154
Cdd:cd03821    90 EYDVVHIHGVWTytSLAACKLARRRGIPYVVSPHgmldpwaLQQKHWKKRIALHLIERRNLNNAALVHFTSEQEADELRR 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 155 IGIVPPIAVPPRWSEIRKDDPwqglqevRAEVRAELGFGEQDIVVGCVAVLREPKGHADLLQAMVPLCKTHPNLHLVVVG 234
Cdd:cd03821   170 FGLEPPIAVIPNGVDIPEFDP-------GLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAG 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 235 DGQPVMDRLQALRDEHGLQQQVHLLG--YRDGACRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVD 312
Cdd:cd03821   243 PDDGAYPAFLQLQSSLGLGDRVTFTGplYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEA 322

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1539789114 313 GsNAILTRLGDN---AALTGALRlLVDDPERRRQMGRAG------WDWMRSAHRF 358
Cdd:cd03821   323 G-CGVVVDPNVSslaEALAEALR-DPADRKRLGEMARRArqveenFSWEAVAGQL 375
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 181-345 5.75e-18

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: 84.42  E-value: 5.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 181 EVRAEVRAELGFGEQDIVVGCVAVLREPKGHADLLQAMVPLCKTHPNLHLVVVGDGqPVMDRLQALRDEHGLQQQVHLLG 260
Cdd:cd04951   173 NVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDG-PLRNELERLICNLNLVDRVILLG 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 261 YRDGACRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEmVVDGSNAILTrLGDNAALTGALR-LLVDDPE 339
Cdd:cd04951   252 QISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAE-VVGDHNYVVP-VSDPQLLAEKIKeIFDMSDE 329


                  ....*.
gi 1539789114 340 RRRQMG 345
Cdd:cd04951   330 ERDILG 335
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 132-349 3.47e-17

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: 81.96  E-value: 3.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 132 HRVLTVSSFVKQLLAERGIPaeyigivpPIAVPPR------WSEIRKDDPWqglqevraevRAELGFGEqDIVVGCVAVL 205
Cdd:cd03814   147 DTTLVPSPSIARELEGHGFE--------RVRLWPRgvdtelFHPSRRDAAL----------RRRLGPPG-RPLLLYVGRL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 206 REPKGHADLLQAMVPLCKtHPNLHLVVVGDGqPVMDRLQALRDehglqqQVHLLGYRDGA--CRLMAGFDIFALASHKEA 283
Cdd:cd03814   208 APEKNLEALLDADLPLAA-SPPVRLVVVGDG-PARAELEARGP------DVIFTGFLTGEelARAYASADVFVFPSRTET 279

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1539789114 284 AGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAGW 349
Cdd:cd03814   280 FGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARAR 345
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 7-348 4.54e-17

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: 82.00  E-value: 4.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114   7 ILHTEAAKGMGGQEIYIFRHMQVMRARGHEVALLC----QPEARLAQLARD--DGFTVH-------TLRMGGLLRLLRGI 73
Cdd:cd03794     4 LISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTpspnYPLGRIFAGATEtkDGIRVIrvklgpiKKNGLIRRLLNYLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  74 WSVS----RLVRRERYDVV--NTTSRRDALIAAAGARLGGTPLVVRSRHLM--SPVNSLLTYTGLPHR------------ 133
Cdd:cd03794    84 FALAallkLLVREERPDVIiaYSPPITLGLAALLLKKLRGAPFILDVRDLWpeSLIALGVLKKGSLLKllkklerklyrl 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 134 ---VLTVSSFVKQLLAERGIPAEYIGIVPPIAVPPRWSEIRKDdpwqglqevraEVRAELGfGEQDIVVGCVAVLREPKG 210
Cdd:cd03794   164 adaIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPKD-----------ELRKKLG-LDDKFVVVYAGNIGKAQG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 211 HADLLQAMVPLcKTHPNLHLVVVGDGQPVmDRLQALRDEHGLQQqVHLLGYRDGAC--RLMAGFDI--FALASHKEAAGT 286
Cdd:cd03794   232 LETLLEAAERL-KRRPDIRFLFVGDGDEK-ERLKELAKARGLDN-VTFLGRVPKEEvpELLSAADVglVPLKDNPANRGS 308

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1539789114 287 V---FLEAAYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAG 348
Cdd:cd03794   309 SpskLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENG 373
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 16-344 5.71e-16

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: 78.14  E-value: 5.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  16 MGGQEIYIFRHMQVMRARGHEVALLCqPEARLAQLARDDGFTVHTLRMGGLLRLLRGIW---------------SVSRLV 80
Cdd:cd03823    14 VGGAEISVHDLAEALVAEGHEVAVLT-AGVGPPGQATVARSVVRYRRAPDETLPLALKRrgyelfetynpglrrLLARLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  81 RRERYDVVNTTSRRD-ALIAAAGARLGGTPLVVRSR--HLMSPVNSLLTYTGLphRVLTVSSFVKQLLAERGIPAEYIGI 157
Cdd:cd03823    93 EDFRPDVVHTHNLSGlGASLLDAARDLGIPVVHTLHdyWLLCPRQFLFKKGGD--AVLAPSRFTANLHEANGLFSARISV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 158 VPPiAVPPrwseirkddpwqglqEVRAEVRAelGFGEQDIVVGCVAVLREPKGhADLLQAMVPLCKtHPNLHLVVVGDGq 237
Cdd:cd03823   171 IPN-AVEP---------------DLAPPPRR--RPGTERLRFGYIGRLTEEKG-IDLLVEAFKRLP-REDIELVIAGHG- 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 238 pvmdRLQALRdEHGLQQQVHLLGY--RDGACRLMAGFDIFALASH-KEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGS 314
Cdd:cd03823   230 ----PLSDER-QIEGGRRIAFLGRvpTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGV 304

                         330       340       350
                  ....*....|....*....|....*....|
gi 1539789114 315 NAILTRLGDNAALTGALRLLVDDPERRRQM 344
Cdd:cd03823   305 NGLLFAPGDAEDLAAAMRRLLTDPALLERL 334
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 195-348 3.19e-15

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: 75.95  E-value: 3.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 195 QDIVVGCVAVLREPKGHADLLQAMVPLCKTHPNLHLVVVGDGqPVMDRLQALRDEHGLQQQVHLLGYRDGA--CRLMAGF 272
Cdd:cd03799   173 GKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDG-DLKEQLQQLIQELNIGDCVKLLGWKPQEeiIEILDEA 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 273 DIFALAS------HKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGR 346
Cdd:cd03799   252 DIFIAPSvtaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGK 331


                  ..
gi 1539789114 347 AG 348
Cdd:cd03799   332 AG 333
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 183-347 4.48e-15

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: 75.83  E-value: 4.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 183 RAEVRAELGFGEQDIVVGCVA--VLREPKGHADLLQAMVPLcKTHPNLHLVVVGDGQPvmdrlQALRDEHglqqQVHLLG 260
Cdd:cd03825   180 KAKARKRLGIPQDKKVILFGAesVTKPRKGFDELIEALKLL-ATKDDLLLVVFGKNDP-----QIVILPF----DIISLG 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 261 YRDGACRLM---AGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLVDD 337
Cdd:cd03825   250 YIDDDEQLVdiySAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLAN 329

                         170
                  ....*....|
gi 1539789114 338 PERRRQMGRA 347
Cdd:cd03825   330 PKERESLGER 339
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 184-354 7.83e-15

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 75.52  E-value: 7.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 184 AEVRAELGFGEQD-IVVGCVAVLREPKGHADLLQAMVPLckthPNLHLVVVGDGqPVMDRLQalrdEHGLQQQVHLLGYR 262
Cdd:PLN02871  250 EEMRARLSGGEPEkPLIVYVGRLGAEKNLDFLKRVMERL----PGARLAFVGDG-PYREELE----KMFAGTPTVFTGML 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 263 DGAcRLMAGF---DIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVD---GSNAILTRLGDNAALTGALRLLVD 336
Cdd:PLN02871  321 QGD-ELSQAYasgDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGDVDDCVEKLETLLA 399

                         170       180
                  ....*....|....*....|....
gi 1539789114 337 DPERRRQMGRAG------WDWMRS 354
Cdd:PLN02871  400 DPELRERMGAAAreevekWDWRAA 423
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 201-318 1.21e-14

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: 72.82  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 201 CVAVLREPKGHADLLQAMVPLCKTHPNLHLVVVGDGQPVMDRLQALRDEHGLQQQVHLLGYRDGACR--LMAGFDIFALA 278
Cdd:cd01635   115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLelLLAAADVFVLP 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1539789114 279 SHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAIL 318
Cdd:cd01635   195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLL 234
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
17-160 1.63e-11

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 62.16  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  17 GGQEIYIFRHMQVMRARGHEVALLCQPEARLAQLARDDGFTVHTLRMGGLLRLLRGIWSVSRL---VRRERYDVVNTTSR 93
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLrrlLRRERPDVVHAHSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  94 RDALIAAAGARLGGTPLVVRSRHLMSPVNSLLTYTGLP----------------HRVLTVSSFVKQLLAER-GIPAEYIG 156
Cdd:pfam13439  81 FPLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPlrrllrrlerrllrraDRVIAVSEAVADELRRLyGVPPEKIR 160


                  ....
gi 1539789114 157 IVPP 160
Cdd:pfam13439 161 VIPN 164
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 180-299 2.81e-11

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 64.23  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 180 QEVRaEVRAELGFGEQDIVVGCVAVLREPKGHADLLQAMVPLCKTHPNLHLVVVGDGQpVMDRLQALRDEHGLQQQVHLL 259
Cdd:cd03812   176 KEKR-RKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGE-LKEKIKEKVKELGLEDKVIFL 253

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1539789114 260 GYRDGACRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIV 299
Cdd:cd03812   254 GFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCL 293
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 149-348 3.91e-11

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: 64.28  E-value: 3.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 149 GIPAEYIGIVPPIAVPPRWSEIRKDDPwqglqevRAEVraelgfgeqdIVVGcvAVLR-EP-KGHADLLQAMVPLCKTHP 226
Cdd:cd03813   263 GADPDKTRVIPNGIDIQRFAPAREERP-------EKEP----------PVVG--LVGRvVPiKDVKTFIRAFKLVRRAMP 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 227 NLHLVVVG---DGQPVMDRLQALRDEHGLQQQVHLLGYRDGAcRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRV 303
Cdd:cd03813   324 DAEGWLIGpedEDPEYAQECKRLVASLGLENKVKFLGFQNIK-EYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDV 402

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1539789114 304 GGVPEMVVDGSNA-----ILTRLGDNAALTGALRLLVDDPERRRQMGRAG 348
Cdd:cd03813   403 GSCRELIYGADDAlgqagLVVPPADPEALAEALIKLLRDPELRQAFGEAG 452
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 212-374 3.92e-10

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: 60.39  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 212 ADLLQAMVPLCKTHPNLHLVVVGDGQPVMDrLQALRDEHGLQQQVHLLGYRDGACRLMAGFDIFALASHKEAAGTVFLEA 291
Cdd:cd04949   176 DHLIEAVAKAVKKVPEITLDIYGYGEEREK-LKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEA 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 292 AYVGVPIVATRVG-GVPEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQMGRAGWDwmrSAHRFtpdghgeTTEHY 370
Cdd:cd04949   255 IGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYK---IAEKY-------STENV 324


                  ....
gi 1539789114 371 YHQW 374
Cdd:cd04949   325 MEKW 328
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 202-363 1.29e-09

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: 59.26  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 202 VAVLREPKGHADLLQAMVPLCKTHPNLHLVVVG-------DGQPVMDRLQALRDEHGLQQQVHLLGYRDGACRLMAGFDI 274
Cdd:cd03792   203 VARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGhgavddpEGSVVYEEVMEYAGDDHDIHVLRLPPSDQEINALQRAATV 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 275 FALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTgaLRLLVDDPERRRQMGRAGWDWMRs 354
Cdd:cd03792   283 VLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAVR--ILRLLTDPELRRKMGLAAREHVR- 359


                  ....*....
gi 1539789114 355 aHRFTPDGH 363
Cdd:cd03792   360 -DNFLITGN 367
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 73-361 2.54e-09

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 58.89  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  73 IWSVSRL---VRRERYDVVNTTSRRDALIAAAGARLGGTPLVVRSRHLMSPV--------------NSLLTYTGLphRVL 135
Cdd:PRK15179  386 IEGTTKLtdvMRSSVPSVVHIWQDGSIFACALAALLAGVPRIVLSVRTMPPVdrpdryrveydiiySELLKMRGV--ALS 463

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 136 TVSSFVKQLLAE------RGIPAEYIGiVPPIAVPPRWSEIRKddpWQGLQEVRAEVRaelgfgeqdIVVGCVAVLREPK 209
Cdd:PRK15179  464 SNSQFAAHRYADwlgvdeRRIPVVYNG-LAPLKSVQDDACTAM---MAQFDARTSDAR---------FTVGTVMRVDDNK 530

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 210 GHADLLQAMVPLCKTHPNLHLVVVGDGqPVMDRLQALRDEHGLQQQVHLLGYRDGACRLMAGFDIFALASHKEAAGTVFL 289
Cdd:PRK15179  531 RPFLWVEAAQRFAASHPKVRFIMVGGG-PLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLI 609

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1539789114 290 EAAYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAA--LTGALRLLVDDPERRRQMGRAGWDWmrSAHRFTPD 361
Cdd:PRK15179  610 EAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTApdVAEALARIHDMCAADPGIARKAADW--ASARFSLN 681
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 128-357 4.27e-09

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: 57.39  E-value: 4.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 128 TGLPHRVLTVSSFVKQLL-AERGIPAEYIGIVPpIAVPprwseIRKDDPwqglqevrAEVRAELGFGEQDIVVGCVAVLR 206
Cdd:cd03822   132 ATLSERVVVMAPISRFLLvRIKLIPAVNIEVIP-HGVP-----EVPQDP--------TTALKRLLLPEGKKVILTFGFIG 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 207 EPKGHADLLQAMVPLCKTHPNLHLVVVGDGQPVMDRLQALR------DEHGLQQQVHL---------LGYRDGACRLMag 271
Cdd:cd03822   198 PGKGLEILLEALPELKAEFPDVRLVIAGELHPSLARYEGERyrkaaiEELGLQDHVDFhnnflpeeeVPRYISAADVV-- 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 272 fdIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAILTrLGDNAALTGALRLLVDDPERRRQMGRAGWD- 350
Cdd:cd03822   276 --VLPYLNTEQSSSGTLSYAIACGKPVISTPLRHAEELLADGRGVLVP-FDDPSAIAEAILRLLEDDERRQAIAERAYAy 352

                         250
                  ....*....|.
gi 1539789114 351 ----WMRSAHR 357
Cdd:cd03822   353 aramTWESIAD 363
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 196-348 5.46e-09

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: 57.37  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 196 DIVVGCVAVLREP-KGHADLLQAMVPLCKTHPNLHLVVVGD-----GQPVMD----RLQALRDEHGLQQQVHLLGYRDGA 265
Cdd:cd03818   213 DPVITYVARNLEPyRGFHVFMRALPRIQARRPDARVVVVGGdgvsyGSPPPDggswKQKMLAELGVDLERVHFVGKVPYD 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 266 --CRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLVDDPERRRQ 343
Cdd:cd03818   293 qyVRLLQLSDAHVYLTYPFVLSWSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAA 372


                  ....*
gi 1539789114 344 MGRAG 348
Cdd:cd03818   373 LRRAA 377
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
17-160 8.44e-09

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 54.33  E-value: 8.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  17 GGQEIYIFRHMQVMRARGHEVALLCQPEARLAQLARDDGFTVH---TLRMGGLLRLLRGIWSVSRLVRRERYDVVNTTSR 93
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHrlpVPPRPSPLADLAALRRLRRLLRAERPDVVHAHSP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539789114  94 RDALIAAAGARLGGTPLVV--------RSRHLMSPVNSLLTYTGLPH--RVLTVSSFVKQLLAERGIPAEYIGIVPP 160
Cdd:pfam13579  81 TAGLAARLARRRRGVPLVVtvhglaldYGSGWKRRLARALERRLLRRadAVVVVSEAEAELLRALGVPAARVVVVPN 157
LpxB COG0763
Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide ...
 133-344 4.81e-07

Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440526  Cd Length: 378  Bit Score: 51.22  E-value: 4.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 133 RVLTVSSFVKQLLAERGIPAEYIGivPPIA--VPPRWSeirkddpwqglqevRAEVRAELGFGEQDIVVgcvAVL----- 205
Cdd:COG0763   136 HVLAIFPFEPEFYRKHGVPVTFVG--HPLAdeIPLEPD--------------RAAARARLGLDPDKPVI---ALLpgsrr 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 206 REPKGHA-DLLQAMVPLCKTHPNLHLVVVGDGQPVMDRLQALRDEHGLQqqVHLLgyRDGACRLMAGFDiFALAshkeAA 284
Cdd:COG0763   197 SEIKRLLpVFLEAAKLLAARRPDLQFVVPLAPSLRRELIEAALADWPLP--VTLV--DGQTYDAMAAAD-AALV----AS 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 285 GTVFLEAAYVGVP-IVATRVGG--------------------------VPEMvvdgsnailtrLGDNA---ALTGALRLL 334
Cdd:COG0763   268 GTATLEAALLGVPmVVAYKVSPltywiakrlvkvpyislpnllagrevVPEL-----------LQDDAtpeNLAAALLRL 336

                         250
                  ....*....|
gi 1539789114 335 VDDPERRRQM 344
Cdd:COG0763   337 LDDPAARAAQ 346
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 201-318 4.86e-07

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: 51.31  E-value: 4.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 201 CVAVLREPKghadLLQAMVPLCKTHPNL-----HLvvvgDGQPVMDRLQALRDEHGLQQQVHLLGYRDG----ACRLMAG 271
Cdd:cd04946   233 IVPVKRIDL----IIETLNSLCVAHPSIciswtHI----GGGPLKERLEKLAENKLENVKVNFTGEVSNkevkQLYKEND 304

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1539789114 272 FDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAIL 318
Cdd:cd04946   305 VDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLL 351
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
275-356 7.39e-07

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 46.83  E-value: 7.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 275 FALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAILTRlgDNAALTGALRLLVDDPERRRQMGRAGWDWMRS 354
Cdd:pfam13524   3 LNPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERVLA 80


                  ..
gi 1539789114 355 AH 356
Cdd:pfam13524  81 EH 82
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 183-357 1.45e-06

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: 49.87  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 183 RAEVRAELGFgEQDI---VVGCVAVLREPKGhADLLQAMVP-LCKThpNLHLVVVGDGQPVM-DRLQALRDEHGLQQQVH 257
Cdd:cd03791   279 KAALQKELGL-PVDPdapLFGFVGRLTEQKG-VDLILDALPeLLEE--GGQLVVLGSGDPEYeQAFRELAERYPGKVAVV 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 258 LlGYRDG-ACRLMAGFDIFALASHKEAAGTVFLEA-AYVGVPIVaTRVGGVPEMVVDGSNAILTRLG------DNAALTG 329
Cdd:cd03791   355 I-GFDEAlAHRIYAGADFFLMPSRFEPCGLVQMYAmRYGTLPIV-RRTGGLADTVFDYDPETGEGTGfvfedyDAEALLA 432

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1539789114 330 ALR---LLVDDPERRRQMGRAG----WDWMRSAHR 357
Cdd:cd03791   433 ALRralALYRNPELWRKLQKNAmkqdFSWDKSAKE 467
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
138-314 1.61e-06

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 49.79  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 138 SSFVKQLLAERgIPAEYIGIVPPIAVPPRWSEIRKDDpwqglqevraeVRAELGFGEQDIVVGCVAVLREPKGHADLLQA 217
Cdd:PRK15484  147 SQFLKKFYEER-LPNADISIVPNGFCLETYQSNPQPN-----------LRQQLNISPDETVLLYAGRISPDKGILLLMQA 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 218 MVPLCKTHPNLHLVVVGDgqPVMDRlqalRDEHG-LQQQVHLLGYRDGACRLMAG-------------FDIFALASH-KE 282
Cdd:PRK15484  215 FEKLATAHSNLKLVVVGD--PTASS----KGEKAaYQKKVLEAAKRIGDRCIMLGgqppekmhnyyplADLVVVPSQvEE 288

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1539789114 283 AAGTVFLEAAYVGVPIVATRVGGVPEMVVDGS 314
Cdd:PRK15484  289 AFCMVAVEAMAAGKPVLASTKGGITEFVLEGI 320
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
225-332 1.17e-05

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 47.39  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 225 HPNLHLVVVGDGQpVMDRLQALRDEHGLQQQVHLLGYRDGACRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVG 304
Cdd:PRK15490  427 HPATRFVLVGDGD-LRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAG 505

                          90       100
                  ....*....|....*....|....*...
gi 1539789114 305 GVPEMVVDGSNAILTRLGDNAALTGALR 332
Cdd:PRK15490  506 GSAECFIEGVSGFILDDAQTVNLDQACR 533
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 245-348 1.57e-05

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 46.85  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 245 ALRDEHGLQQQVHLLGYRDGAcRLMAGFDIFALASHKEAAGTVFLEAAYVGVPIVATRVGGVPEMV--VDGSNAILTRLG 322
Cdd:NF038011  358 SLVASLGLQDKVKFLGFQKID-DLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLIegLDEEDRALGAAG 436

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1539789114 323 ------DNAALTGALRLLVDDPERRRQMGRAG 348
Cdd:NF038011  437 evvaiaDPQALARAALDLLRDPQRWQAAQAAG 468
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 285-365 8.13e-05

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: 44.12  E-value: 8.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 285 GTVFLEAAYVGVPIVATRVGGVPEMVVDGSNAILtRLGDNAALTGALRLLVDDPERRRQMGRAGWDwmRSAHRFTPDGHG 364
Cdd:cd03805   313 GIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFL-CEPTPEAFAEAMLKLANDPDLADRMGAAGRK--RVKEKFSREAFA 389


                  .
gi 1539789114 365 E 365
Cdd:cd03805   390 E 390
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
132-351 8.91e-05

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 44.20  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 132 HRVLTVSSFVKQLLAERGIPAEyigivpPIAVPPRWSEIRKDDPWQGLQEVraEVRAELGFGEQDIVVGCVAVLREPKGH 211
Cdd:PRK10307  173 DNVSTISRSMMNKAREKGVAAE------KVIFFPNWSEVARFQPVADADVD--ALRAQLGLPDGKKIVLYSGNIGEKQGL 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 212 ADLLQAMVPLCkTHPNLHLVVVGDGqPVMDRLQALRDEHGLQQqVHL--LGYRDGACRLMAGFDIFALASHKEAAGTVF- 288
Cdd:PRK10307  245 ELVIDAARRLR-DRPDLIFVICGQG-GGKARLEKMAQCRGLPN-VHFlpLQPYDRLPALLKMADCHLLPQKAGAADLVLp 321

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1539789114 289 -----LEAayVGVPIVAT-RVGGVPEMVVDGsNAILTRLGDNAALTGALRLLVDDPERRRQMGRAGWDW 351
Cdd:PRK10307  322 skltnMLA--SGRNVVATaEPGTELGQLVEG-IGVCVEPESVEALVAAIAALARQALLRPKLGTVAREY 387
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 227-326 1.94e-04

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: 43.05  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 227 NLHLVVVGDGQPVM--DRLQALRdehgLQQQVHLLGYRDGA--CRLMAGfdifALA-----SHKEAAGTVFLEAAYVGVP 297
Cdd:cd03802   195 GLPLKIAGKVRDEDyfYYLQEPL----PGPRIEFIGEVGHDekQELLGG----ARAllfpiNWDEPFGLVMIEAMACGTP 266

                          90       100
                  ....*....|....*....|....*....
gi 1539789114 298 IVATRVGGVPEMVVDGSNAILTRLGDNAA 326
Cdd:cd03802   267 VIAYRRGGLPEVIQHGETGFLVDSVEEMA 295
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 230-344 4.86e-04

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: 41.89  E-value: 4.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 230 LVVVGDGqPVMDRLQALrdehgLQQQVHLLGYRDGA--------CRLMagfdIFAlasHKEAAGTVFLEAAYVGVPIVAT 301
Cdd:cd03804   228 LVVIGDG-PDLDRLRAM-----ASPNVEFLGYQPDEvlkellskARAF----VFA---AEEDFGIVPVEAQACGTPVIAF 294

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1539789114 302 RVGGVPEMVVDGSNAILTRLGDNAALTGAlrllVDDPERRRQM 344
Cdd:cd03804   295 GKGGALETVRPGPTGILFGEQTVESLKAA----VEEFEQNFDR 333
PRK14098 PRK14098
starch synthase;
188-358 1.29e-03

starch synthase;


Pssm-ID: 172588 [Multi-domain]  Cd Length: 489  Bit Score: 40.87  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 188 AELGFGEQDIVVGCVAVLREPKGhADLLQA----MVPLckthpNLHLVVVGDGQPVMD-RLQALRDEHGLQQQVHLlGYR 262
Cdd:PRK14098  299 VGLPFDEETPLVGVIINFDDFQG-AELLAEslekLVEL-----DIQLVICGSGDKEYEkRFQDFAEEHPEQVSVQT-EFT 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 263 DGACRL-MAGFDIFALASHKEAAGTVFLEA-AYVGVPIVATRvGGVPEMVVD-----GSNAILTRLGDnAALTG----AL 331
Cdd:PRK14098  372 DAFFHLaIAGLDMLLMPGKIESCGMLQMFAmSYGTIPVAYAG-GGIVETIEEvsedkGSGFIFHDYTP-EALVAklgeAL 449

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1539789114 332 RLLvDDPER-----RRQMGRaGWDWMRSAHRF 358
Cdd:PRK14098  450 ALY-HDEERweelvLEAMER-DFSWKNSAEEY 479
SpsG COG3980
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall ...
 214-349 1.63e-03

Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443179 [Multi-domain]  Cd Length: 342  Bit Score: 39.91  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 214 LLQAmvpLCKTHPNLHL-VVVGDGQPVMDRLQALRDEHGLQqqVHLLGYRDGACRLMAGFDIfALAshkeAAGTVFLEAA 292
Cdd:COG3980   189 VLRA---LLQLDPDLKItVVVGPGYPHLDELRALAAERPLN--IELHRNVKDMAELMAQADL-AIS----AAGTTTYELA 258

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1539789114 293 YVGVP----IVATR-VGGVPEMVVDGS--NAILTRLGDNAALTGALRLLVDDPERRRQMGRAGW 349
Cdd:COG3980   259 ALGLPtivvAVADNqRAIAEALEENGAaiNLGLGEELTDEELANALDELLLDPERRARMSRKAR 322
KdtA COG1519
3-deoxy-D-manno-octulosonic-acid transferase [Cell wall/membrane/envelope biogenesis]; ...
 289-354 1.66e-03

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: 40.12  E-value: 1.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1539789114 289 LEAAYVGVPIVatrVGgvPEM--------VVDGSNAILtRLGDNAALTGALRLLVDDPERRRQMGRAGWDWMRS 354
Cdd:COG1519   338 LEPAALGKPVL---FG--PHTfnfaeaaeLLIAAGAAI-QVADAEELAAAVLALLADPELRAAMGAAARAVVEA 405
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
213-336 2.00e-03

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 39.69  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 213 DLLQAmvpLCKTHPNLHLVVVGDGQPVmDRLQALRDEHGLQQQVHLLGY--------RDGACRLMAgfdiFALASHKEAA 284
Cdd:PRK09922  199 ELFDG---LSQTTGEWQLHIIGDGSDF-EKCKAYSRELGIEQRIIWHGWqsqpwevvQQKIKNVSA----LLLTSKFEGF 270

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1539789114 285 GTVFLEAAYVGVP-IVATRVGGVPEMVVDGSNAILTRLGDNAALTGALRLLVD 336
Cdd:PRK09922  271 PMTLLEAMSYGIPcISSDCMSGPRDIIKPGLNGELYTPGNIDEFVGKLNKVIS 323
GT28_Beta-DGS-like cd17507
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ...
 133-347 3.33e-03

beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). 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: 340861 [Multi-domain]  Cd Length: 364  Bit Score: 39.22  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 133 RVLTVSSFVKQLLAERGIPAEYI---GIvpPIAvpPRWSEIRKDDPWqglqevraevRAELGFGEQDIVVGCVAVLREPk 209
Cdd:cd17507   145 RYFVASEEVKRELVERGVTPSQIkvtGI--PVR--PSFAEVRDKDEA----------RNELNLSPDKPTVLLMGGGGGM- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114 210 GHADLLQAMvpLCKTHPNLHLVVV-GDGQPVMDRLQALRDehgLQQQVHLLGYRDGACRLMAGFDifaLASHKEAAGTVF 288
Cdd:cd17507   210 GPVKETVEA--LLDSLRAGQVLVVcGKNKKLYEKLSGLEE---DYINVRVLGYVDDMNELMAASD---LVITKPGGLTIS 281

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1539789114 289 lEAAYVGVPIVATR------VGGVPEMVvdgSNAILTRLGDNAALTGALRLLVDDPERRRQMGRA 347
Cdd:cd17507   282 -EALARGLPVIIYDpipgqeEENADFLE---NNGAGIIARDPEELLEIVARLIDPPSLLRMMSEA 342
Glyco_trans_4_2 pfam13477
Glycosyl transferase 4-like;
20-116 6.01e-03

Glycosyl transferase 4-like;


Pssm-ID: 433241 [Multi-domain]  Cd Length: 139  Bit Score: 36.92  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539789114  20 EIYIFRHMQVMRARGHEVALLCQPEARlAQLARDDGFTVH-TLRMGGLLRLLRGIWSVSRLVRRERYDVVNT-TSRRDAL 97
Cdd:pfam13477  10 SIHTLRWADALADRGYDVHVISSKGPA-KDELIAEGIHVHrLKVPRKGPLGYLKAFRLKKLIKKIKPDVVHVhYAKPYGL 88

                          90
                  ....*....|....*....
gi 1539789114  98 IAAAGARLGGTPLVVRSRH 116
Cdd:pfam13477  89 LAGLAARLSGFPPVVLSAW 107
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH