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Conserved domains on  [gi|1994078563|ref|WP_205163121|]
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glycosyltransferase [Arthrobacter roseus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
717-968 7.90e-59

Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 205.17  E-value: 7.90e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  717 ALLAHCRREGIPTIFWNKEDPVHFNRFRVTAKYFDHVFTTDDSCIPRYLEHPGKHlksVASLPFYAQPRLHNPLASEREY 796
Cdd:COG4641     60 ELVAALRARGIPTVFWDTDDPVTLDRFRELLPLYDLVFTFDGDCVEEYRALGARR---VFYLPFAADPELHRPVPPEARF 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  797 SHTISYAGSYYGdryaDRSRQLDRLLGAASPLGLTIYDRQhlnpdspyhFPEHLAR---HVAGGLDYAEMVQAYKAHPIH 873
Cdd:COG4641    137 RYDVAFVGNYYP----DRRARLEELLLAPAGLRLKIYGPG---------WPKLALPanvRRGGHLPGEEHPAAYASSKIT 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  874 INVNSVTESQTMFSRRVVEIAASGGAIISGPGRGAQRVL--GGTVPVLDNTDTAAALMELWMSDESVRNDDAWLAMRTVF 951
Cdd:COG4641    204 LNVNRMAASPDSPTRRTFEAAACGAFLLSDPWEGLEELFepGEEVLVFRDGEELAEKLRYLLADPEERRAIAEAGRRRVL 283

                          250
                   ....*....|....*..
gi 1994078563  952 RAHTGGHRLTYALRTAG 968
Cdd:COG4641    284 AEHTYAHRARELLAILE 300
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 235-630 2.14e-40

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: 153.85  E-value: 2.14e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  235 VHSAAPYNSNGYSTRSHGIVQGLRKQGADFVVAVRPGYPwdvktdrgtasrSSFEEEIDGVRHLFSAGPswtgqPLDSYV 314
Cdd:cd03801      5 LSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPG------------EPPEELEDGVIVPLLPSL-----AALLRA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  315 QYAADQYVQVAMQNRVSIIHAaSNHVTALPALIAARRLGLPFVYEVRGfweiTEQSSRPGWEHTDRFALALQLETLvaNE 394
Cdd:cd03801     68 RRLLRELRPLLRLRKFDVVHA-HGLLAALLAALLALLLGAPLVVTLHG----AEPGRLLLLLAAERRLLARAEALL--RR 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  395 ADQVLAITLQVADKLVSRGVAS-ERITLLPNSVDVHVFSPlpahqKTLAKLGIPDGIPVIGYAGSVVDYEGLDLLVRATG 473
Cdd:cd03801    141 ADAVIAVSEALRDELRALGGIPpEKIVVIPNGVDLERFSP-----PLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALA 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  474 EVLSRGLDVRTVIVG-DGPSLDGLRALtnELQLENHVTFTGRVPSSSVPLYLSCFDVVPSPRRRLPVtelvpPLKPLEAM 552
Cdd:cd03801    216 KLLRRGPDVRLVIVGgDGPLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGF-----GLVVLEAM 288

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1994078563  553 ASGKAVILTDLPPLRDLAGaDGERARLCDSESSKSLADAIEATLRDTSGTADMTRRARLWTVKDRTWVKAAATLKKVY 630
Cdd:cd03801    289 AAGLPVVATDVGGLPEVVE-DGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 1136-1389 4.47e-15

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.


The actual alignment was detected with superfamily member cd03801:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 366  Bit Score: 78.73  E-value: 4.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1136 VVVAGHDLKFATALIAELESTGHTVLVDKWTDHNKHDEAHSRNLLEQADVIFCEWTLGNAVWYSQNKLPHQRLVTRFHLQ 1215
Cdd:cd03801     36 VLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGA 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1216 ELYTPFPSRL-----------NMAAVDQLIFVGEHLRSIASRDYSIPEQQTRVIGNSVDIEGLDND-----KVSGARFNL 1279
Cdd:cd03801    116 EPGRLLLLLAaerrllaraeaLLRRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSPPlrrklGIPPDRPVL 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1280 GLVGIIPRRKRLDRALDLLSKLRREDDRFHLYIKGKRPEDYpwmakrteemdfysEQLRRIEADpfLNGAVTFDPH--GE 1357
Cdd:cd03801    196 LFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLR--------------AELEELELG--LGDRVRFLGFvpDE 259

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1994078563 1358 DMPGWYRKIGVVLSLSDFESFHLTLADGAASG 1389
Cdd:cd03801    260 ELPALYAAADVFVLPSRYEGFGLVVLEAMAAG 291
 
Name Accession Description Interval E-value
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
717-968 7.90e-59

Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 205.17  E-value: 7.90e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  717 ALLAHCRREGIPTIFWNKEDPVHFNRFRVTAKYFDHVFTTDDSCIPRYLEHPGKHlksVASLPFYAQPRLHNPLASEREY 796
Cdd:COG4641     60 ELVAALRARGIPTVFWDTDDPVTLDRFRELLPLYDLVFTFDGDCVEEYRALGARR---VFYLPFAADPELHRPVPPEARF 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  797 SHTISYAGSYYGdryaDRSRQLDRLLGAASPLGLTIYDRQhlnpdspyhFPEHLAR---HVAGGLDYAEMVQAYKAHPIH 873
Cdd:COG4641    137 RYDVAFVGNYYP----DRRARLEELLLAPAGLRLKIYGPG---------WPKLALPanvRRGGHLPGEEHPAAYASSKIT 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  874 INVNSVTESQTMFSRRVVEIAASGGAIISGPGRGAQRVL--GGTVPVLDNTDTAAALMELWMSDESVRNDDAWLAMRTVF 951
Cdd:COG4641    204 LNVNRMAASPDSPTRRTFEAAACGAFLLSDPWEGLEELFepGEEVLVFRDGEELAEKLRYLLADPEERRAIAEAGRRRVL 283

                          250
                   ....*....|....*..
gi 1994078563  952 RAHTGGHRLTYALRTAG 968
Cdd:COG4641    284 AEHTYAHRARELLAILE 300
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 235-630 2.14e-40

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: 153.85  E-value: 2.14e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  235 VHSAAPYNSNGYSTRSHGIVQGLRKQGADFVVAVRPGYPwdvktdrgtasrSSFEEEIDGVRHLFSAGPswtgqPLDSYV 314
Cdd:cd03801      5 LSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPG------------EPPEELEDGVIVPLLPSL-----AALLRA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  315 QYAADQYVQVAMQNRVSIIHAaSNHVTALPALIAARRLGLPFVYEVRGfweiTEQSSRPGWEHTDRFALALQLETLvaNE 394
Cdd:cd03801     68 RRLLRELRPLLRLRKFDVVHA-HGLLAALLAALLALLLGAPLVVTLHG----AEPGRLLLLLAAERRLLARAEALL--RR 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  395 ADQVLAITLQVADKLVSRGVAS-ERITLLPNSVDVHVFSPlpahqKTLAKLGIPDGIPVIGYAGSVVDYEGLDLLVRATG 473
Cdd:cd03801    141 ADAVIAVSEALRDELRALGGIPpEKIVVIPNGVDLERFSP-----PLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALA 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  474 EVLSRGLDVRTVIVG-DGPSLDGLRALtnELQLENHVTFTGRVPSSSVPLYLSCFDVVPSPRRRLPVtelvpPLKPLEAM 552
Cdd:cd03801    216 KLLRRGPDVRLVIVGgDGPLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGF-----GLVVLEAM 288

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1994078563  553 ASGKAVILTDLPPLRDLAGaDGERARLCDSESSKSLADAIEATLRDTSGTADMTRRARLWTVKDRTWVKAAATLKKVY 630
Cdd:cd03801    289 AAGLPVVATDVGGLPEVVE-DGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 451-612 1.20e-24

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: 101.58  E-value: 1.20e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  451 PVIGYAGSVVDYEGLDLLVRATGEVLSRGLDVRTVIVGDGPSLDGLRALTNELQLENHVTFTGRVPSSSVPLYLSCFDVV 530
Cdd:pfam00534    3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  531 PSPRRRLPVtelvpPLKPLEAMASGKAVILTDLPPLRDLAgADGERARLCDSESSKSLADAIEATLRDTSGTADMTRRAR 610
Cdd:pfam00534   83 VLPSRYEGF-----GIVLLEAMACGLPVIASDVGGPPEVV-KDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENAR 156


                   ..
gi 1994078563  611 LW 612
Cdd:pfam00534  157 KR 158
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
383-648 9.74e-23

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 102.75  E-value: 9.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  383 LALQLETLVANEADQVLAITLQVADKLVSRGVASERITLLPNSVDVHVFSPLPAHQKTL--AKLGIPDGIPVIGYAGSVV 460
Cdd:PRK10307   160 LATAFERSLLRRFDNVSTISRSMMNKAREKGVAAEKVIFFPNWSEVARFQPVADADVDAlrAQLGLPDGKKIVLYSGNIG 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  461 DYEGLDLLVRATGEVLSRGlDVRTVIVGDGPSLDGLRALTNELQLENhVTFTGRVPSSSVPLYLSCFDVVPSPRRRlPVT 540
Cdd:PRK10307   240 EKQGLELVIDAARRLRDRP-DLIFVICGQGGGKARLEKMAQCRGLPN-VHFLPLQPYDRLPALLKMADCHLLPQKA-GAA 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  541 ELVPPLKPLEAMASGKAVILTdlpplrdlAGADGERARLCDS-------ESSKSLADAIEATLRDTSGTADMTRRARLWt 613
Cdd:PRK10307   317 DLVLPSKLTNMLASGRNVVAT--------AEPGTELGQLVEGigvcvepESVEALVAAIAALARQALLRPKLGTVAREY- 387

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1994078563  614 vkdrtwvkAAATLkkvysqlgGRDAVMAQSLASLN 648
Cdd:PRK10307   388 --------AERTL--------DKENVLRQFIADIR 406
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 1136-1389 4.47e-15

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: 78.73  E-value: 4.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1136 VVVAGHDLKFATALIAELESTGHTVLVDKWTDHNKHDEAHSRNLLEQADVIFCEWTLGNAVWYSQNKLPHQRLVTRFHLQ 1215
Cdd:cd03801     36 VLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGA 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1216 ELYTPFPSRL-----------NMAAVDQLIFVGEHLRSIASRDYSIPEQQTRVIGNSVDIEGLDND-----KVSGARFNL 1279
Cdd:cd03801    116 EPGRLLLLLAaerrllaraeaLLRRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSPPlrrklGIPPDRPVL 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1280 GLVGIIPRRKRLDRALDLLSKLRREDDRFHLYIKGKRPEDYpwmakrteemdfysEQLRRIEADpfLNGAVTFDPH--GE 1357
Cdd:cd03801    196 LFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLR--------------AELEELELG--LGDRVRFLGFvpDE 259

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1994078563 1358 DMPGWYRKIGVVLSLSDFESFHLTLADGAASG 1389
Cdd:cd03801    260 ELPALYAAADVFVLPSRYEGFGLVVLEAMAAG 291
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 545-633 2.14e-14

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 71.17  E-value: 2.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  545 PLKPLEAMASGKAVILTDLPPLRDLAgADGERARLCDSESSKSLADAIEATLRDTSGTADMTRRARLWTVKDRTWVKAAA 624
Cdd:COG0438     34 GLVLLEAMAAGLPVIATDVGGLPEVI-EDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEAARERAEERFSWEAIAE 112


                   ....*....
gi 1994078563  625 TLKKVYSQL 633
Cdd:COG0438    113 RLLALYEEL 121
DUF3880 pfam12996
DUF based on E. rectale Gene description (DUF3880); Based on Eubacterium rectale gene ...
 732-807 4.80e-06

DUF based on E. rectale Gene description (DUF3880); Based on Eubacterium rectale gene EUBREC_3218. As seen in gene expression experiments (http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE14737), It appears to be upregulated in the presence of Bacteroides thetaiotaomicron vs when isolated in culture.


Pssm-ID: 463766  Cd Length: 77  Bit Score: 45.61  E-value: 4.80e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994078563  732 WNKEDPVHFNRFRVTAKYFDHVFTTDDSCIPRYLEHPGKHlksVASLPFYAQPRLHNPL---ASEREYSHTISYAGSYY 807
Cdd:pfam12996    1 WFVDDPYLTLYSKSIANPYNYIFTFDRDNVEELRELGAKN---VFYLPLAANPERFRPVrvdAEDDKYRSDISFVGSLY 76
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
1276-1393 7.34e-04

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 41.34  E-value: 7.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1276 RFNLGLVG-IIPRRKRLDRALDLLSKLRREDDRFHLYIKGKRPEdypwmakrteemdfysEQLRRIEADpfLNGAVTFdp 1354
Cdd:pfam13692    1 RPVILFVGrLHPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPE----------------EELEELAAG--LEDRVIF-- 60

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1994078563 1355 HG--EDMPGWYRKIGVVLSLSDFESFHLTLADGAASGaIPC 1393
Cdd:pfam13692   61 TGfvEDLAELLAAADVFVLPSLYEGFGLKLLEAMAAG-LPV 100
 
Name Accession Description Interval E-value
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
717-968 7.90e-59

Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 205.17  E-value: 7.90e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  717 ALLAHCRREGIPTIFWNKEDPVHFNRFRVTAKYFDHVFTTDDSCIPRYLEHPGKHlksVASLPFYAQPRLHNPLASEREY 796
Cdd:COG4641     60 ELVAALRARGIPTVFWDTDDPVTLDRFRELLPLYDLVFTFDGDCVEEYRALGARR---VFYLPFAADPELHRPVPPEARF 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  797 SHTISYAGSYYGdryaDRSRQLDRLLGAASPLGLTIYDRQhlnpdspyhFPEHLAR---HVAGGLDYAEMVQAYKAHPIH 873
Cdd:COG4641    137 RYDVAFVGNYYP----DRRARLEELLLAPAGLRLKIYGPG---------WPKLALPanvRRGGHLPGEEHPAAYASSKIT 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  874 INVNSVTESQTMFSRRVVEIAASGGAIISGPGRGAQRVL--GGTVPVLDNTDTAAALMELWMSDESVRNDDAWLAMRTVF 951
Cdd:COG4641    204 LNVNRMAASPDSPTRRTFEAAACGAFLLSDPWEGLEELFepGEEVLVFRDGEELAEKLRYLLADPEERRAIAEAGRRRVL 283

                          250
                   ....*....|....*..
gi 1994078563  952 RAHTGGHRLTYALRTAG 968
Cdd:COG4641    284 AEHTYAHRARELLAILE 300
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 235-630 2.14e-40

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: 153.85  E-value: 2.14e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  235 VHSAAPYNSNGYSTRSHGIVQGLRKQGADFVVAVRPGYPwdvktdrgtasrSSFEEEIDGVRHLFSAGPswtgqPLDSYV 314
Cdd:cd03801      5 LSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPG------------EPPEELEDGVIVPLLPSL-----AALLRA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  315 QYAADQYVQVAMQNRVSIIHAaSNHVTALPALIAARRLGLPFVYEVRGfweiTEQSSRPGWEHTDRFALALQLETLvaNE 394
Cdd:cd03801     68 RRLLRELRPLLRLRKFDVVHA-HGLLAALLAALLALLLGAPLVVTLHG----AEPGRLLLLLAAERRLLARAEALL--RR 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  395 ADQVLAITLQVADKLVSRGVAS-ERITLLPNSVDVHVFSPlpahqKTLAKLGIPDGIPVIGYAGSVVDYEGLDLLVRATG 473
Cdd:cd03801    141 ADAVIAVSEALRDELRALGGIPpEKIVVIPNGVDLERFSP-----PLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALA 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  474 EVLSRGLDVRTVIVG-DGPSLDGLRALtnELQLENHVTFTGRVPSSSVPLYLSCFDVVPSPRRRLPVtelvpPLKPLEAM 552
Cdd:cd03801    216 KLLRRGPDVRLVIVGgDGPLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGF-----GLVVLEAM 288

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1994078563  553 ASGKAVILTDLPPLRDLAGaDGERARLCDSESSKSLADAIEATLRDTSGTADMTRRARLWTVKDRTWVKAAATLKKVY 630
Cdd:cd03801    289 AAGLPVVATDVGGLPEVVE-DGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 248-623 8.93e-40

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: 152.88  E-value: 8.93e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  248 TRSHGIVQGLRKQGAD-FVVAVRPGYPwdvkTDRGTASRssfEEEIDGVR-HLFSAGPSWTGQPLD---SYV--QYAADQ 320
Cdd:cd03794     18 ARVYELAKELVRRGHEvTVLTPSPNYP----LGRIFAGA---TETKDGIRvIRVKLGPIKKNGLIRrllNYLsfALAALL 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  321 YVQVAmQNRVSIIHAASNHVT-ALPALIAARRLGLPFVYEVRGFWeiTEQSSRPGWEHTDRFALALQ-LETLVANEADQV 398
Cdd:cd03794     91 KLLVR-EERPDVIIAYSPPITlGLAALLLKKLRGAPFILDVRDLW--PESLIALGVLKKGSLLKLLKkLERKLYRLADAI 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  399 LAITLQVADKLVSRGVASERITLLPNSVDVHVFSPLPahQKTLAKLGIPDGIPVIGYAGSVVDYEGLDLLVRATgEVLSR 478
Cdd:cd03794    168 IVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPP--KDELRKKLGLDDKFVVVYAGNIGKAQGLETLLEAA-ERLKR 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  479 GLDVRTVIVGDGPSLDGLRALTNELQLENhVTFTGRVPSSSVPLYLSCFDVVPSPRRRLPVTELVPPLKPLEAMASGKAV 558
Cdd:cd03794    245 RPDIRFLFVGDGDEKERLKELAKARGLDN-VTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGSSPSKLFEYMAAGKPI 323

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994078563  559 ILTDLPPLrDLAGADGERARLCDSESSKSLADAIEATLRDTSGTADMTRRARLWTVKDRTWVKAA 623
Cdd:cd03794    324 LASDDGGS-DLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLA 387
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 242-633 1.32e-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: 143.29  E-value: 1.32e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  242 NSNGYSTRSHGIVQGLRKQGADF-VVAVRPGYPWDVKTDRGTASRSSFEEEIDGVRHLFSAGPSWtgqplDSYVQYAADQ 320
Cdd:cd03798     12 NSPGRGIFVRRQVRALSRRGVDVeVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLL-----APLRAPSLAK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  321 YVQVAMQNRVSIIHAasnHVtALPALIAA----RRLGLPFVyevrgfweITEQSSRPGWEHTDRFALALQLETLvaNEAD 396
Cdd:cd03798     87 LLKRRRRGPPDLIHA---HF-AYPAGFAAallaRLYGVPYV--------VTEHGSDINVFPPRSLLRKLLRWAL--RRAA 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  397 QVLAITLQVADKLVSRGVASERITLLPNSVDVHVFSPLPAhqktlaKLGIPDGIPVIGYAGSVVDYEGLDLLVRATGEVL 476
Cdd:cd03798    153 RVIAVSKALAEELVALGVPRDRVDVIPNGVDPARFQPEDR------GLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLA 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  477 SRGLDVRTVIVGDGPSLDGLRALTNELQLENHVTFTGRVPSSSVPLYLSCFD--VVPSPRRRLPVTElvpplkpLEAMAS 554
Cdd:cd03798    227 KARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDvfVLPSRHEGFGLVL-------LEAMAC 299

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994078563  555 GKAVILTDLPPLRDLAGaDGERARLCDSESSKSLADAIEATLRDTSGTADMtRRARLWTVKDRTWVKAAATLKKVYSQL 633
Cdd:cd03798    300 GLPVVATDVGGIPEVVG-DPETGLLVPPGDADALAAALRRALAEPYLRELG-EAARARVAERFSWVKAADRIAAAYRDV 376
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 328-611 4.17e-29

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: 120.15  E-value: 4.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  328 NRVSIIHAASNHVtALPALIAARRLGLPFVYevrgfweiTEQSSRPGWEHTDRFALALQLETlvaneaDQVLAITLQVAD 407
Cdd:cd03819     75 ERIDLIHAHSRAP-AWLGWLASRLTGVPLVT--------TVHGSYLATYHPKDFALAVRARG------DRVIAVSELVRD 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  408 KLVSR-GVASERITLLPNSVDVHVFSPLPAhQKTLAKLGIPDGIPVIGYAGSVVDYEGLDLLVRATGEvLSRGLDVRTVI 486
Cdd:cd03819    140 HLIEAlGVDPERIRVIPNGVDTDRFPPEAE-AEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAE-LKDEPDFRLLV 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  487 VGDGPSLDGLRALTNELQLENHVTFTGRVpsSSVPLYLSCFDVVPSPRRRLPVtelvpPLKPLEAMASGKAVILTDLPPL 566
Cdd:cd03819    218 AGDGPERDEIRRLVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSLHEEF-----GRVALEAMACGTPVVATDVGGA 290

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1994078563  567 RDL--AGADGERARLCDSEsskSLADAIEATLRDTSGTADMTRRARL 611
Cdd:cd03819    291 REIvvHGRTGLLVPPGDAE---ALADAIRAAKLLPEAREKLQAAAAL 334
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 242-630 1.22e-27

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: 116.61  E-value: 1.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  242 NSNGYSTRSHGIVQGLRKQGAD-FVVAVR-PGYpwdvktdrgtasrsSFEEEIDGVRHLFSAGPSWTGQPLDSYVQYAad 319
Cdd:cd03817     12 QVNGVATSVRNLARALEKRGHEvYVITPSdPGA--------------EDEEEVVRYRSFSIPIRKYHRQHIPFPFKKA-- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  320 qYVQVAMQNRVSIIHAASNHVTALPALIAARRLGLPFV------YEvrgfwEITEQ-SSRPGWEHTDRFALALQLetlvA 392
Cdd:cd03817     76 -VIDRIKELGPDIIHTHTPFSLGKLGLRIARKLKIPIVhtyhtmYE-----DYLHYiPKGKLLVKAVVRKLVRRF----Y 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  393 NEADQVLAITLQVADKLVSRGVaSERITLLPNSVDVHVFSPLPAHqKTLAKLGIPDGIPVIGYAGSVvDYE-GLDLLVRA 471
Cdd:cd03817    146 NHTDAVIAPSEKIKDTLREYGV-KGPIEVIPNGIDLDKFEKPLNT-EERRKLGLPPDEPILLYVGRL-AKEkNIDFLLRA 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  472 TGEVLSRgLDVRTVIVGDGPSLDGLRALTNELQLENHVTFTGRVPSSSVPLYLSCFD--VVPSPrrrlpvTElVPPLKPL 549
Cdd:cd03817    223 FAELKKE-PNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADlfVFAST------TE-TQGLVYL 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  550 EAMASGKAVILTDLPPLRDLAgADGERARLCDSESSKsLADAIEATLRDTSGTADMTRRARLwTVKDRTWVKAAATLKKV 629
Cdd:cd03817    295 EAMAAGLPVVAAKDPAASELV-EDGENGFLFEPNDET-LAEKLLHLRENLELLRKLSKNAEI-SAREFAFAKSVEKLYEE 371


                   .
gi 1994078563  630 Y 630
Cdd:cd03817    372 V 372
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 327-610 1.35e-26

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: 113.07  E-value: 1.35e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  327 QNRVSIIHAasnhVTALPAL---IAARRLGLP-FVYEVRGF-WEITEQS-SRPGWEHTDRFALALQLETLVANEADQVLA 400
Cdd:cd03808     79 KEKPDIVHC----HTPKPGIlgrLAARLAGVPkVIYTVHGLgFVFTEGKlLRLLYLLLEKLALLFTDKVIFVNEDDRDLA 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  401 ITLQVADKlvsrgvaSERITLLPNSVDVHVFSPLPAHqktlaklgIPDGIPVIGYAGSVVDYEGLDLLVRATGEVLSRGL 480
Cdd:cd03808    155 IKKGIIKK-------KKTVLIPGSGVDLDRFQYSPES--------LPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGP 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  481 DVRTVIVGDGPSLDGLRALTNELQLENHVTFTGRVpsSSVPLYLSCFDVV--PSPRRRLPVTeLvpplkpLEAMASGKAV 558
Cdd:cd03808    220 NVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFR--SDVPELLAESDVFvlPSYREGLPRS-L------LEAMAAGRPV 290

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1994078563  559 ILTDLPPLRDLAgADGERARLCDSESSKSLADAIEATLRDTSGTADMTRRAR 610
Cdd:cd03808    291 ITTDVPGCRELV-IDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAAR 341
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 271-626 1.86e-26

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: 113.49  E-value: 1.86e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  271 GYPWDVKTDRGTASRSSFEEEIDGVR--HLfSAGPSwTGQP-------LDSYVQYAADQYVqvAMQNRVSIIHA---ASN 338
Cdd:cd03800     38 GYQVDIFTRRISPADPEVVEIAPGARviRV-PAGPP-EYLPkeelwpyLEEFADGLLRFIA--REGGRYDLIHShywDSG 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  339 HVTALpaliAARRLGLPFV--YEVRGFWEITEQSSRPGWEHTDRFALalqlETLVANEADQVLAITLQVADKLVSR-GVA 415
Cdd:cd03800    114 LVGAL----LARRLGVPLVhtFHSLGRVKYRHLGAQDTYHPSLRITA----EEQILEAADRVIASTPQEADELISLyGAD 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  416 SERITLLPNSVDVHVFSPLPAHQKTLAKLGIPDGIPVIGYAGSVVDYEGLDLLVRATGEVLSRGLDVRTVIVGdGPSLDG 495
Cdd:cd03800    186 PSRINVVPPGVDLERFFPVDRAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVG-GPSDDP 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  496 -------LRALTNELQLENHVTFTGRVPSSSVPLYLSCFDVVPSPrrrlPVTElvpP--LKPLEAMASGKAVILTDLPPL 566
Cdd:cd03800    265 lsmdreeLAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVP----SLYE---PfgLTAIEAMACGTPVVATAVGGL 337

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  567 RDlAGADGERARLCDSESSKSLADAIEATLRDTSGTADMTRRARLWTVKDRTWVKAAATL 626
Cdd:cd03800    338 QD-IVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQL 396
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 329-610 4.71e-26

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: 111.64  E-value: 4.71e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  329 RVSIIHAASNHvTALPALIAAR-RLGLPFVYEVRGFWEiteqssrpgWEHTDRFALALqlETLVANEADQVLAITLQVAD 407
Cdd:cd03807     79 NPDVVHTWMYH-ADLIGGLAAKlAGGVKVIWSVRSSNI---------PQRLTRLVRKL--CLLLSKFSPATVANSSAVAE 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  408 KLVSRGVASERITLLPNSVDVHVFSPlPAHQKTLAK--LGIPDGIPVIGYAGSVVDYEGLDLLVRATGEVLSRGLDVRTV 485
Cdd:cd03807    147 FHQEQGYAKNKIVVIYNGIDLFKLSP-DDASRARARrrLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLL 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  486 IVGDGPSLDGLRALTNELQLENHVTFTGrvPSSSVPLYLSCFD--VVPSPRRRLPVTElvpplkpLEAMASGKAVILTDL 563
Cdd:cd03807    226 LVGRGPERPNLERLLLELGLEDRVHLLG--ERSDVPALLPAMDifVLSSRTEGFPNAL-------LEAMACGLPVVATDV 296

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1994078563  564 PPLRDLagADGERARLCDSESSKSLADAIEATLRDTSGTADMTRRAR 610
Cdd:cd03807    297 GGAAEL--VDDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAAR 341
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 240-630 1.20e-25

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: 110.46  E-value: 1.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  240 PYNSNGYSTRSHGIVQGLRKQGADFVVaVRPGypwdvktdrgtasrsSFEEEIDGVRHLFSAgPSWtgqPLDSYVQYAAD 319
Cdd:cd03814     10 HPQVNGVVRTLERLVDHLRRRGHEVRV-VAPG---------------PFDEAESAEGRVVSV-PSF---PLPFYPEYRLA 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  320 QYVQVAMQNRV-----SIIHAASNHVTALPALIAARRLGLPFV--Y--------EVRGFWEIteqsSRPGWEHTDRFala 384
Cdd:cd03814     70 LPLPRRVRRLIkefqpDIIHIATPGPLGLAALRAARRLGLPVVtsYhtdfpeylSYYTLGPL----SWLAWAYLRWF--- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  385 lqletlvANEADQVLAITLQVADKLVSRGVasERITLLPNSVDVHVFSPLPAHQKTLAKLGIPDGiPVIGYAGSVVDYEG 464
Cdd:cd03814    143 -------HNPFDTTLVPSPSIARELEGHGF--ERVRLWPRGVDTELFHPSRRDAALRRRLGPPGR-PLLLYVGRLAPEKN 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  465 LDLLVRATGEvLSRGLDVRTVIVGDGPSLDGLRALTnelqleNHVTFTGRVPSSSVPLYLSCFD--VVPSPrrrlpvTE- 541
Cdd:cd03814    213 LEALLDADLP-LAASPPVRLVVVGDGPARAELEARG------PDVIFTGFLTGEELARAYASADvfVFPSR------TEt 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  542 --LVpplkPLEAMASGKAVILTDLPPLRDLAGaDGERARLCDSESSKSLADAIEATLRDTSGTADMTRRARlWTVKDRTW 619
Cdd:cd03814    280 fgLV----VLEAMASGLPVVAADAGGPRDIVR-PGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARAR-AEAERYSW 353

                          410
                   ....*....|.
gi 1994078563  620 VKAAATLKKVY 630
Cdd:cd03814    354 EAFLDNLLDYY 364
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 451-612 1.20e-24

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: 101.58  E-value: 1.20e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  451 PVIGYAGSVVDYEGLDLLVRATGEVLSRGLDVRTVIVGDGPSLDGLRALTNELQLENHVTFTGRVPSSSVPLYLSCFDVV 530
Cdd:pfam00534    3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  531 PSPRRRLPVtelvpPLKPLEAMASGKAVILTDLPPLRDLAgADGERARLCDSESSKSLADAIEATLRDTSGTADMTRRAR 610
Cdd:pfam00534   83 VLPSRYEGF-----GIVLLEAMACGLPVIASDVGGPPEVV-KDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENAR 156


                   ..
gi 1994078563  611 LW 612
Cdd:pfam00534  157 KR 158
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 377-626 2.86e-24

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: 106.29  E-value: 2.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  377 HTDRFALALQLET-LVANEADQVLAITLQVADKLVSR-GVASERITLLPNSVDvHVFSPLPAHQKTLAKLGIPDgiPVIG 454
Cdd:cd03809    120 FPKRFRLYYRLLLpISLRRADAIITVSEATRDDIIKFyGVPPEKIVVIPLGVD-PSFFPPESAAVLIAKYLLPE--PYFL 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  455 YAGSVVDYEGLDLLVRATGEVLSRGLDVRTVIVG-DGPSLDGLRALTNELQLENHVTFTGRVPSSSVPLYLS---CFdVV 530
Cdd:cd03809    197 YVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGgKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRgarAF-VF 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  531 PSprRR----LPVtelvpplkpLEAMASGKAVILTDLPPLRDLAGADgerARLCDSESSKSLADAIEATLRDTSGTADMT 606
Cdd:cd03809    276 PS--LYegfgLPV---------LEAMACGTPVIASNISVLPEVAGDA---ALYFDPLDPESIADAILRLLEDPSLREELI 341

                          250       260
                   ....*....|....*....|
gi 1994078563  607 RRARLWtVKDRTWVKAAATL 626
Cdd:cd03809    342 RKGLER-AKKFSWEKTAEKT 360
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
451-598 5.91e-24

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 98.74  E-value: 5.91e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  451 PVIGYAGSVVDYE-GLDLLVRATGEVLSRGLDVRTVIVGDGPSLDgLRALTNELqlENHVTFTGRVPSssVPLYLSCFD- 528
Cdd:pfam13692    2 PVILFVGRLHPNVkGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEE-LEELAAGL--EDRVIFTGFVED--LAELLAAADv 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994078563  529 -VVPSPRRRLPvtelvppLKPLEAMASGKAVILTDLPPLRDLagADGERARLCDSESSKSLADAIEATLRD 598
Cdd:pfam13692   77 fVLPSLYEGFG-------LKLLEAMAAGLPVVATDVGGIPEL--VDGENGLLVPPGDPEALAEAILRLLED 138
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
383-648 9.74e-23

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 102.75  E-value: 9.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  383 LALQLETLVANEADQVLAITLQVADKLVSRGVASERITLLPNSVDVHVFSPLPAHQKTL--AKLGIPDGIPVIGYAGSVV 460
Cdd:PRK10307   160 LATAFERSLLRRFDNVSTISRSMMNKAREKGVAAEKVIFFPNWSEVARFQPVADADVDAlrAQLGLPDGKKIVLYSGNIG 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  461 DYEGLDLLVRATGEVLSRGlDVRTVIVGDGPSLDGLRALTNELQLENhVTFTGRVPSSSVPLYLSCFDVVPSPRRRlPVT 540
Cdd:PRK10307   240 EKQGLELVIDAARRLRDRP-DLIFVICGQGGGKARLEKMAQCRGLPN-VHFLPLQPYDRLPALLKMADCHLLPQKA-GAA 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  541 ELVPPLKPLEAMASGKAVILTdlpplrdlAGADGERARLCDS-------ESSKSLADAIEATLRDTSGTADMTRRARLWt 613
Cdd:PRK10307   317 DLVLPSKLTNMLASGRNVVAT--------AEPGTELGQLVEGigvcvepESVEALVAAIAALARQALLRPKLGTVAREY- 387

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1994078563  614 vkdrtwvkAAATLkkvysqlgGRDAVMAQSLASLN 648
Cdd:PRK10307   388 --------AERTL--------DKENVLRQFIADIR 406
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 341-610 4.46e-20

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: 93.97  E-value: 4.46e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  341 TALPALIAARRLGLPFVYEVRGF---WeiTEQSSRPGWehtdrfALALQL-ETLVANEADQVLAITLQVADKLVSRGVAs 416
Cdd:cd03821    103 TSLAACKLARRRGIPYVVSPHGMldpW--ALQQKHWKK------RIALHLiERRNLNNAALVHFTSEQEADELRRFGLE- 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  417 ERITLLPNSVDVHVFSPLPAHQKtlaKLGIPDGIPVIGYAGSVVDYEGLDLLVRATGEVLSRGLDVRTVIVG-DGPSLDG 495
Cdd:cd03821    174 PPIAVIPNGVDIPEFDPGLRDRR---KHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGpDDGAYPA 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  496 LRALTNELQLENHVTFTGRVPSSSVPLYLSCFD--VVPSPRRRLPVTelvpplkPLEAMASGKAVILTDLPPLRDLAGAD 573
Cdd:cd03821    251 FLQLQSSLGLGDRVTFTGPLYGEAKWALYASADlfVLPSYSENFGNV-------VAEALACGLPVVITDKCGLSELVEAG 323

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1994078563  574 GerARLCDSESSkSLADAIEATLRDTSGTADMTRRAR 610
Cdd:cd03821    324 C--GVVVDPNVS-SLAEALAEALRDPADRKRLGEMAR 357
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 253-598 4.97e-20

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: 93.58  E-value: 4.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  253 IVQGLRKQGADFVVAVRPGYPWDVKTDRGTASRSSFEEEIDGVRHLFSagpswtgqpLDSYVQYAAdqyvqVAMQNRVSI 332
Cdd:cd03811     21 LANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGL---------LKAILKLKR-----ILKRAKPDV 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  333 IHAASNHVTALPALIAARRLglPFVYEVRGFweiteqssrPGWEHTDRFALALQLetLVANEADQVLAITLQVADKLVSR 412
Cdd:cd03811     87 VISFLGFATYIVAKLAAARS--KVIAWIHSS---------LSKLYYLKKKLLLKL--KLYKKADKIVCVSKGIKEDLIRL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  413 G-VASERITLLPNSVDVHVFSPLPahqkTLAKLGIPDGIPVIGYAGSVVDYEGLDLLVRATGEVLSRGLDVRTVIVGDGP 491
Cdd:cd03811    154 GpSPPEKIEVIYNPIDIDRIRALA----KEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGP 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  492 SLDGLRALTNELQLENHVTFTGRVpsSSVPLYLSCFDVVPSPRRR--LPVTeLvpplkpLEAMASGKAVILTDLPPLRDL 569
Cdd:cd03811    230 LREELEKLAKELGLAERVIFLGFQ--SNPYPYLKKADLFVLSSRYegFPNV-L------LEAMALGTPVVSTDCPGPREI 300

                          330       340
                   ....*....|....*....|....*....
gi 1994078563  570 AGaDGERARLCDsESSKSLADAIEATLRD 598
Cdd:cd03811    301 LD-DGENGLLVP-DGDAAALAGILAALLQ 327
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 325-610 1.86e-17

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: 85.97  E-value: 1.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  325 AMQNRVSIIHA--ASNHVTALPAliaARRLGLPFVYEVRGFwEITEQ----SSRPGWehtdrFALALQLETLVANEADQV 398
Cdd:cd05844     77 AAGLAPALVHAhfGRDGVYALPL---ARALGVPLVVTFHGF-DITTSrawlAASPGW-----PSQFQRHRRALQRPAALF 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  399 LAITLQVADKLVSRGVASERITLLPNSVDVHVFSPLPAHQKTlaklgipdgiPVIGYAGSVVDYEGLDLLVRATGEVLSR 478
Cdd:cd05844    148 VAVSGFIRDRLLARGLPAERIHVHYIGIDPAKFAPRDPAERA----------PTILFVGRLVEKKGCDVLIEAFRRLAAR 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  479 GLDVRTVIVGDGPSLDGLRALTNELqleNHVTFTGRVPSSSVPLYLSCFDV--VPSPRRRLPVTELVpPLKPLEAMASGK 556
Cdd:cd05844    218 HPTARLVIAGDGPLRPALQALAAAL---GRVRFLGALPHAEVQDWMRRAEIfcLPSVTAASGDSEGL-GIVLLEAAACGV 293

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1994078563  557 AVILTDLPPLRDlAGADGERARLCDSESSKSLADAIEATLRDTSGTADMTRRAR 610
Cdd:cd05844    294 PVVSSRHGGIPE-AILDGETGFLVPEGDVDALADALQALLADRALADRMGGAAR 346
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 1136-1389 4.47e-15

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: 78.73  E-value: 4.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1136 VVVAGHDLKFATALIAELESTGHTVLVDKWTDHNKHDEAHSRNLLEQADVIFCEWTLGNAVWYSQNKLPHQRLVTRFHLQ 1215
Cdd:cd03801     36 VLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGA 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1216 ELYTPFPSRL-----------NMAAVDQLIFVGEHLRSIASRDYSIPEQQTRVIGNSVDIEGLDND-----KVSGARFNL 1279
Cdd:cd03801    116 EPGRLLLLLAaerrllaraeaLLRRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSPPlrrklGIPPDRPVL 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1280 GLVGIIPRRKRLDRALDLLSKLRREDDRFHLYIKGKRPEDYpwmakrteemdfysEQLRRIEADpfLNGAVTFDPH--GE 1357
Cdd:cd03801    196 LFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLR--------------AELEELELG--LGDRVRFLGFvpDE 259

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1994078563 1358 DMPGWYRKIGVVLSLSDFESFHLTLADGAASG 1389
Cdd:cd03801    260 ELPALYAAADVFVLPSRYEGFGLVVLEAMAAG 291
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 328-599 6.85e-15

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: 79.30  E-value: 6.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  328 NRVSIIHAASNHVTALPALIAARRLGLPFVYEVRGFW----EITEQSSRpgWEHTDrfalalqLETLVANEADQVLAITL 403
Cdd:cd03813    172 PEADLYHSVSTGYAGLLGALARHRRGIPFLLTEHGIYtrerKIEILQST--WIMGY-------IKKLWIRFFERLGKLAY 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  404 QVADKLVS-----------RGVASERITLLPNSVDVHVFSPLPAHQKTlaklgiPDGiPVIGYAGSVVDYEGLDLLVRAT 472
Cdd:cd03813    243 QQADKIISlyegnrrrqirLGADPDKTRVIPNGIDIQRFAPAREERPE------KEP-PVVGLVGRVVPIKDVKTFIRAF 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  473 GEVLSRGLDVRTVIVG---DGPS-LDGLRALTNELQLENHVTFTGRVpssSVPLYLSCFDVVPsprrrlpVTELVP--PL 546
Cdd:cd03813    316 KLVRRAMPDAEGWLIGpedEDPEyAQECKRLVASLGLENKVKFLGFQ---NIKEYYPKLGLLV-------LTSISEgqPL 385

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  547 KPLEAMASGKAVILTDLPPLRDL-------AGADGERARLCDSEsskSLADAIEATLRDT 599
Cdd:cd03813    386 VILEAMASGVPVVATDVGSCRELiygaddaLGQAGLVVPPADPE---ALAEALIKLLRDP 442
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 545-633 2.14e-14

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 71.17  E-value: 2.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  545 PLKPLEAMASGKAVILTDLPPLRDLAgADGERARLCDSESSKSLADAIEATLRDTSGTADMTRRARLWTVKDRTWVKAAA 624
Cdd:COG0438     34 GLVLLEAMAAGLPVIATDVGGLPEVI-EDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEAARERAEERFSWEAIAE 112


                   ....*....
gi 1994078563  625 TLKKVYSQL 633
Cdd:COG0438    113 RLLALYEEL 121
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
244-424 3.79e-14

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 71.66  E-value: 3.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  244 NGYSTRSHGIVQGLRKQGADFVVAVRPGYPWDvktdrgtasrssFEEEIDGVR-HLFSAGPSWTGQPLDSYVQYAAdqyv 322
Cdd:pfam13579    1 GGIGVYVLELARALAALGHEVRVVTPGGPPGR------------PELVGDGVRvHRLPVPPRPSPLADLAALRRLR---- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  323 QVAMQNRVSIIHAASNHvTALPALIAARRLGLPFVYEVRGFWeITEQSSRPGWehtdrfaLALQLETLVANEADQVLAIT 402
Cdd:pfam13579   65 RLLRAERPDVVHAHSPT-AGLAARLARRRRGVPLVVTVHGLA-LDYGSGWKRR-------LARALERRLLRRADAVVVVS 135

                          170       180
                   ....*....|....*....|..
gi 1994078563  403 LQVADKLVSRGVASERITLLPN 424
Cdd:pfam13579  136 EAEAELLRALGVPAARVVVVPN 157
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 309-616 2.95e-13

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: 73.15  E-value: 2.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  309 PLDSYVQY---AADQYVQVAMQNRVSIIHA--ASNHvtALPALIAARRLG--LPFVYEVRGFwEITEQSSRPGWEHTDRF 381
Cdd:cd04962     61 PLFEYPPYtlaLASKIVEVAKEHKLDVLHAhyAIPH--ASCAYLAREILGekIPIVTTLHGT-DITLVGYDPSLQPAVRF 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  382 ALalqletlvaNEADQVLAITLQVADKLVSRGVASERITLLPNSVDVHVFSPLPAhQKTLAKLGIPDGIPVIGYAGSVVD 461
Cdd:cd04962    138 SI---------NKSDRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKPA-GALKRRLLAPPDEKVVIHVSNFRP 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  462 YEGLDLLVRATGEVlSRGLDVRTVIVGDGPSLDGLRALTNELQLENHVTFTGRVPssSVPLYLSCFDVV--PSPRRRLpv 539
Cdd:cd04962    208 VKRIDDVVRVFARV-RRKIPAKLLLVGDGPERVPAEELARELGVEDRVLFLGKQD--DVEELLSIADLFllPSEKESF-- 282

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1994078563  540 telvpPLKPLEAMASGKAVILTDLPPLRDLAgADGERARLCDSESSKSLADAIEATLRDTSGTADMTRRARLWTVKD 616
Cdd:cd04962    283 -----GLAALEAMACGVPVVSSNAGGIPEVV-KHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAER 353
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 342-630 6.23e-13

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: 72.03  E-value: 6.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  342 ALPALIAARRLGLPFVyevrgfweIT----EQSSRPGWEHTDRFALALQLETLVAneADQVLAITLQVADKLVSRgvasE 417
Cdd:cd03822     93 GLYALGLLLHLRIPVI--------TTlhtvLDLSDPGKQALKVLFRIATLSERVV--VMAPISRFLLVRIKLIPA----V 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  418 RITLLPnsvdvH-VFSPLPAHQKTLAKLGIPDGIPVIGYAGSVVDYEGLDLLVRATGEVLSRGLDVRTVIVG-DGPSLDG 495
Cdd:cd03822    159 NIEVIP-----HgVPEVPQDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGeLHPSLAR 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  496 LR------ALTNELQLENHVTF-TGRVPSSSVPLYLSCFDVVPSP-RRRLPVTELVPPLkpleAMASGKAVILTDLPPLR 567
Cdd:cd03822    234 YEgeryrkAAIEELGLQDHVDFhNNFLPEEEVPRYISAADVVVLPyLNTEQSSSGTLSY----AIACGKPVISTPLRHAE 309

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1994078563  568 DLagADGERARLCDSESSKSLADAIEATLRDTSGTADMTRRARLWTvKDRTWVKAAATLKKVY 630
Cdd:cd03822    310 EL--LADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYA-RAMTWESIADRYLRLF 369
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 418-611 1.03e-12

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: 71.63  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  418 RITLLPNSVDVHVFSPLPAHQKTLAKLG-IPDGIPVIGYAGSVVD-YEGLDLLVRATGEVLSRGLDVRTVIVGDG----- 490
Cdd:cd03818    180 RISVIHDGVDTDRLAPDPAARLRLLNGTeLKAGDPVITYVARNLEpYRGFHVFMRALPRIQARRPDARVVVVGGDgvsyg 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  491 ---PSLDGLRA-LTNELQLE-NHVTFTGRVPSSSVPLYLSCFDVVPSPRRrlpvtELVPPLKPLEAMASGKAVILTDLPP 565
Cdd:cd03818    260 sppPDGGSWKQkMLAELGVDlERVHFVGKVPYDQYVRLLQLSDAHVYLTY-----PFVLSWSLLEAMACGCPVIGSDTAP 334

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1994078563  566 LRDLAgADGERARLCDSESSKSLADAIEATLRDTSGTADMTRRARL 611
Cdd:cd03818    335 VREVI-RDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARR 379
GT4_TuaH-like cd04950
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this ...
 415-627 2.14e-12

teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. 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.


Pssm-ID: 340856 [Multi-domain]  Cd Length: 373  Bit Score: 70.48  E-value: 2.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  415 ASERITLLPNSVDVHVFSPLPAHQKTLAKL-GIPDgiPVIGYAGsVVDyEGLDL-LVratGEVLSRGLDVRTVIVGDGPS 492
Cdd:cd04950    171 LHENVHPIPNGVDVEHFAAARQPLDDPIDLrEIPG--PVLGFFG-AID-EKLDFdLI---EELAKARPQWNFVFIGPVVK 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  493 LDGlraltNELQLENHVTFTGRVPSSSVPLYLSCFDVVPSPRRRLPVTELVPPLKPLEAMASGKAVILTDLPPLRDLAGA 572
Cdd:cd04950    244 IDP-----SSLPRAPNIHWLGPKPYKELPAYLAGFDVALLPFALNEYTRFISPLKLFEYLAAGKPVVATSIPSVVRFYGE 318

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1994078563  573 dgerARLCDSEsSKSLADAIEATLrDTSGTADMTRRARLWtVKDRTWVKAAATLK 627
Cdd:cd04950    319 ----AVLCGDD-PDEFSAAIEKAL-ALKGDARDKRLARAL-ARQESWDERARAME 366
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 235-631 9.98e-12

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: 68.12  E-value: 9.98e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  235 VHSAAPYNSNGYSTRSHGIVQGLRKQGAD-FVVAVRPGYPWDVKTDRGTASRSSFEeeiDGVRHLFSAGPSWtgQPLDSY 313
Cdd:cd03823      6 NSLYPPQRVGGAEISVHDLAEALVAEGHEvAVLTAGVGPPGQATVARSVVRYRRAP---DETLPLALKRRGY--ELFETY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  314 VQYAADQYVQVAMQNRVSIIHaaSNHVTALPALI--AARRLGLPFVYEVRGFWeiteqssrpgWEHTDRFalalqletLV 391
Cdd:cd03823     81 NPGLRRLLARLLEDFRPDVVH--THNLSGLGASLldAARDLGIPVVHTLHDYW----------LLCPRQF--------LF 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  392 ANEADQVLAITLQVADKLVSRGVASERITLLPNSVdvhvfSPLPAHQKTLAKlgiPDGIPVIGYAGSVVDYEGLDLLVRA 471
Cdd:cd03823    141 KKGGDAVLAPSRFTANLHEANGLFSARISVIPNAV-----EPDLAPPPRRRP---GTERLRFGYIGRLTEEKGIDLLVEA 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  472 TGEVLSrgLDVRTVIVGDGPSLDgLRALTNELQLENHvtftGRVPSSSVPLYLSCFDVVpsprrrlpvteLVP------- 544
Cdd:cd03823    213 FKRLPR--EDIELVIAGHGPLSD-ERQIEGGRRIAFL----GRVPTDDIKDFYEKIDVL-----------VVPsiwpepf 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  545 PLKPLEAMASGKAVILTDLPPLRDLAGaDGERARLCDSESSKSLADAIEATLRDtsgtADMTRRARLWTVKDRTWVKAAA 624
Cdd:cd03823    275 GLVVREAIAAGLPVIASDLGGIAELIQ-PGVNGLLFAPGDAEDLAAAMRRLLTD----PALLERLRAGAEPPRSTESQAE 349


                   ....*..
gi 1994078563  625 TLKKVYS 631
Cdd:cd03823    350 EYLKLYR 356
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 328-562 3.11e-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: 66.93  E-value: 3.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  328 NRVSIIHAASNHVTALPALIAARRlGLPfvyeVRgfweIT-EQSSRPGWEHTDR---FALALQLETLvaneADQVLAITL 403
Cdd:cd03812     79 EKYDIVHVHGSSSNGIILLLAAKA-GVP----VR----IAhSHNTKDSSIKLRKirkNVLKKLIERL----STKYLACSE 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  404 QVADKLVSRgVASERITLLPNSVDVHVFSPLPAHQKTLAKLGIPDGIPVIGYAGSVVDYEGLDLLVRATGEVLSRGLDVR 483
Cdd:cd03812    146 DAGEWLFGE-VENGKFKVIPNGIDIEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVK 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  484 TVIVGDGPSLDGLRALTNELQLENHVTFTGRVpsSSVPLYLSCFDV--VPSPRRRLPVTElvpplkpLEAMASGKAVILT 561
Cdd:cd03812    225 LVLVGEGELKEKIKEKVKELGLEDKVIFLGFR--NDVSEILSAMDVflFPSLYEGLPLVA-------VEAQASGLPCLLS 295


                   .
gi 1994078563  562 D 562
Cdd:cd03812    296 D 296
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 448-610 6.58e-11

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: 65.76  E-value: 6.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  448 DGIPVIGYAGSVVDYEGLDLLVRAtgevlSRGLDVRTVIVGDGPSLDGLRALTNELQLENhVTFTGRVPSSSVPLYLSCF 527
Cdd:cd03795    189 KGKKIFLFIGRLVYYKGLDYLIEA-----AQYLNYPIVIGGEGPLKPDLEAQIELNLLDN-VKFLGRVDDEEKVIYLHLC 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  528 DVV--PSPRRrlpvTE---LVPplkpLEAMASGKAVILTDLPPLRDLAGADGERARLCDSESSKSLADAIEATLRDTSGT 602
Cdd:cd03795    263 DVFvfPSVLR----SEafgIVL----LEAMMCGKPVISTNIGTGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELR 334


                   ....*...
gi 1994078563  603 ADMTRRAR 610
Cdd:cd03795    335 ESYGENAK 342
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 455-569 1.00e-10

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: 63.58  E-value: 1.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  455 YAGSVVDYEGLDLLVRATGEVLSRGLDVRTVIVGDGPSLDGLRALTNELQLENHVTFTGRVPSSSV-PLYLSCFDVVPSP 533
Cdd:cd01635    115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVlELLLAAADVFVLP 194

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1994078563  534 RRRLPVtelvpPLKPLEAMASGKAVILTDLPPLRDL 569
Cdd:cd01635    195 SRSEGF-----GLVLLEAMAAGKPVIATDVGGIPEF 225
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 374-610 1.53e-10

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: 64.57  E-value: 1.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  374 GWEHTDRFA-----LALQLETLVANEADQVlaITLQVADKLVSRGVASERITLLPNSVDVHVFSPL-PAHQKTLAklgip 447
Cdd:cd03820    113 VWEHNNYEAynkglRRLLLRRLLYKRADKI--VVLTEADKLKKYKQPNSNVVVIPNPLSFPSEEPStNLKSKRIL----- 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  448 dgipvigYAGSVVDYEGLDLLVRATGEVLSRGLDVRTVIVGDGPSLDGLRALTNELQLENHVTFTGRV-------PSSSV 520
Cdd:cd03820    186 -------AVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLGPTkniaeeyANSSI 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  521 plylscFdVVPSprrR---LPVTeLvpplkpLEAMASGKAVILTDLPP-LRDLaGADGERARLCDSESSKSLADAIEATL 596
Cdd:cd03820    259 ------F-VLSS---RyegFPMV-L------LEAMAYGLPIISFDCPTgPSEI-IEDGENGLLVPNGDVDALAEALLRLM 320

                          250
                   ....*....|....
gi 1994078563  597 RDTSGTADMTRRAR 610
Cdd:cd03820    321 EDEELRKKMGKNAR 334
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
253-428 1.22e-09

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 58.70  E-value: 1.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  253 IVQGLRKQGADFVVAVRpgypwdvktdrgtASRSSFEEEIDGVRHLFSAGPSWTGQPLDSYvqYAADQYVQVAMQNRVSI 332
Cdd:pfam13439   10 LARALARRGHEVTVVTP-------------GGPGPLAEEVVRVVRVPRVPLPLPPRLLRSL--AFLRRLRRLLRRERPDV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  333 IHAASNHVTALPALIAARRLGLPFVYEVRGFWeitEQSSRPGWEHTDRFALALQLETLVANEADQVLAITLQVADKLVSR 412
Cdd:pfam13439   75 VHAHSPFPLGLAALAARLRLGIPLVVTYHGLF---PDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRL 151

                          170
                   ....*....|....*..
gi 1994078563  413 -GVASERITLLPNSVDV 428
Cdd:pfam13439  152 yGVPPEKIRVIPNGVDL 168
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 1146-1389 1.31e-09

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: 61.60  E-value: 1.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1146 ATALIAELESTGHTVLV--------DKWTDHNKHDEAHSRNLL---------------EQADVIFCEwtLGNAVWYSQ-- 1200
Cdd:cd03819     17 ILDLARALAERGHRVLVvtaggpllPRLRQIGIGLPGLKVPLLrallgnvrlarlirrERIDLIHAH--SRAPAWLGWla 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1201 NKLPHQRLVTRFHLQELYTPFPSR---LNMAAVDQLIFVGEHLRSIASRDYSIPEQQTRVIGNSVDI---------EGLD 1268
Cdd:cd03819     95 SRLTGVPLVTTVHGSYLATYHPKDfalAVRARGDRVIAVSELVRDHLIEALGVDPERIRVIPNGVDTdrfppeaeaEERA 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1269 NDKVSGARFNLGLVGIIPRRKRLDRALDLLSKLRREDDrFHLYIKGKRPEDypwmakrteemdfysEQLRRIEADPFLNG 1348
Cdd:cd03819    175 QLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPD-FRLLVAGDGPER---------------DEIRRLVERLGLRD 238

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1994078563 1349 AVTFDPHGEDMPGWYRKIGVVLSLSDFESFHLTLADGAASG 1389
Cdd:cd03819    239 RVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACG 279
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 189-610 1.21e-08

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 59.34  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  189 AEAAVQQRRTMDTILGGARVLAEGIFLPERQPNPGyvAEPRRTMYCVH-SAAPYNSnGYSTRSHGIVQGLRKQGADFVVa 267
Cdd:PLN02871    21 FSARSSSYRNAAVLVSVRRVASSEAPPPLLDTDSR--SRPRRIALFVEpSPFSYVS-GYKNRFQNFIRYLREMGDEVLV- 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  268 vrpgypwdVKTDRGTAsrssfeEEIDG--VRHLFSAGPSWTGQPLDSYvqyAADQYV--QVAmQNRVSIIHAASNHVTAL 343
Cdd:PLN02871    97 --------VTTDEGVP------QEFHGakVIGSWSFPCPFYQKVPLSL---ALSPRIisEVA-RFKPDLIHASSPGIMVF 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  344 PALIAARRLGLP-----------------FVYEVRGFWEITeqssrpgwehtdRFAlalqletlvANEADQVLAITLQVA 406
Cdd:PLN02871   159 GALFYAKLLCVPlvmsyhthvpvyiprytFSWLVKPMWDII------------RFL---------HRAADLTLVTSPALG 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  407 DKLVSRGVAS-ERITLLPNSVDVHVFSPLPAHQKTLAKL--GIPDGiPVIGYAGSVVDYEGLDLLVRatgeVLSRGLDVR 483
Cdd:PLN02871   218 KELEAAGVTAaNRIRVWNKGVDSESFHPRFRSEEMRARLsgGEPEK-PLIVYVGRLGAEKNLDFLKR----VMERLPGAR 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  484 TVIVGDGPSldglraltnELQLENH-----VTFTGRVPS---SSVPLYLSCFdVVPSPRRRLpvtelvpPLKPLEAMASG 555
Cdd:PLN02871   293 LAFVGDGPY---------REELEKMfagtpTVFTGMLQGdelSQAYASGDVF-VMPSESETL-------GFVVLEAMASG 355

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994078563  556 KAVI------LTDLPPlRDLAGADGERARLCDSESSKSLadaIEATLRDTSGTADMTRRAR 610
Cdd:PLN02871   356 VPVVaaraggIPDIIP-PDQEGKTGFLYTPGDVDDCVEK---LETLLADPELRERMGAAAR 412
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 329-520 6.35e-08

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: 56.86  E-value: 6.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  329 RVSIIHAASNHVT-ALPALIAARRLGLPFVYevrgfweiTEQSsrpgwehtdRFALAlQLETLVANEA--------DQVL 399
Cdd:cd03796     88 RIQIVHGHQAFSSlAHEALFHARTLGLKTVF--------TDHS---------LFGFA-DASSILTNKLlrfsladiDHVI 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  400 AITLQVADKLVSR-GVASERITLLPNSVDVHVFSPLPAHQKtlaklgiPDGIpVIGYAGSVVDYEGLDLLVRATGEVLSR 478
Cdd:cd03796    150 CVSHTSKENTVLRaSLDPRIVSVIPNAVDSSDFTPDPSKPD-------PNKI-TIVVISRLVYRKGIDLLVGIIPRICKK 221

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1994078563  479 GLDVRTVIVGDGPSLDGLRALTNELQLENHVTFTGRVPSSSV 520
Cdd:cd03796    222 HPNVRFIIGGDGPKRIELEEMREKYQLQDRVELLGAVPHEEV 263
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 1184-1393 1.32e-07

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: 55.44  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1184 DVIFCeWTLGNAVWYSQNKLPHQRLVTRFH--LQELYTPFPSRLNMAAV----DQLIFVGEHLRSIASRDYSIPEQQTRV 1257
Cdd:cd03811     85 DVVIS-FLGFATYIVAKLAAARSKVIAWIHssLSKLYYLKKKLLLKLKLykkaDKIVCVSKGIKEDLIRLGPSPPEKIEV 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1258 IGNSVDIEGL------DNDKVSGARFNLGLVGIIPRRKRLDRALDLLSKLRREDDRFHLYIKGKRPEDypwmakrteemd 1331
Cdd:cd03811    164 IYNPIDIDRIralakePILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLR------------ 231

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994078563 1332 fysEQLRRIEADPFLNGAVTFdpHG--EDMPGWYRK-IGVVLSlSDFESFHLTLADGAASGaIPC 1393
Cdd:cd03811    232 ---EELEKLAKELGLAERVIF--LGfqSNPYPYLKKaDLFVLS-SRYEGFPNVLLEAMALG-TPV 289
DUF3880 pfam12996
DUF based on E. rectale Gene description (DUF3880); Based on Eubacterium rectale gene ...
 732-807 4.80e-06

DUF based on E. rectale Gene description (DUF3880); Based on Eubacterium rectale gene EUBREC_3218. As seen in gene expression experiments (http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE14737), It appears to be upregulated in the presence of Bacteroides thetaiotaomicron vs when isolated in culture.


Pssm-ID: 463766  Cd Length: 77  Bit Score: 45.61  E-value: 4.80e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994078563  732 WNKEDPVHFNRFRVTAKYFDHVFTTDDSCIPRYLEHPGKHlksVASLPFYAQPRLHNPL---ASEREYSHTISYAGSYY 807
Cdd:pfam12996    1 WFVDDPYLTLYSKSIANPYNYIFTFDRDNVEELRELGAKN---VFYLPLAANPERFRPVrvdAEDDKYRSDISFVGSLY 76
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 389-615 1.38e-05

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: 48.98  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  389 TLVANEADQVLaitlqVADKLVSRgvasERITLLPNSVDVHVFSPLP-AHQKTLAKLGIPDGIPVIGYAGSVVDYEGLDL 467
Cdd:cd04951    135 TNVSREALDEF-----IAKKAFSK----NKSVPVYNGIDLNKFKKDInVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPN 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  468 LVRATGEVLSRGLDVRTVIVGDGPSLDGLRALTNELQLENHVTFTGRVpsSSVPLYLSCFDVVPSPRRRLPVTELVPplk 547
Cdd:cd04951    206 LLLAISELILSKNDFKLLIAGDGPLRNELERLICNLNLVDRVILLGQI--SNISEYYNAADLFVLSSEWEGFGLVVA--- 280

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994078563  548 plEAMASGKAVILTDlpplrdlagADGERARLCDSE------SSKSLADAIEATLRDTSGTADMTRRARLWTVK 615
Cdd:cd04951    281 --EAMACERPVVATD---------AGGVAEVVGDHNyvvpvsDPQLLAEKIKEIFDMSDEERDILGNKNEYIAK 343
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 455-559 1.74e-05

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: 48.82  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  455 YAGSVVDYEGLDLLVRATGEvlsrgLDVRTVIVGDGPSLDGLRALTnelqlENHVTFTGRVPSSSVPLYLScfdvvpspR 534
Cdd:cd03804    204 TASRLVPYKRIDLAVEAFNE-----LPKRLVVIGDGPDLDRLRAMA-----SPNVEFLGYQPDEVLKELLS--------K 265

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1994078563  535 RR---LPVTE---LVpplkPLEAMASGKAVI 559
Cdd:cd03804    266 ARafvFAAEEdfgIV----PVEAQACGTPVI 292
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
395-513 3.84e-05

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 47.78  E-value: 3.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  395 ADQVLAITLQVADKLVSRGVASERITLLPNSVDVHVFS-PLPAHQKTLAKLgipdgipvigYAGSVVDY------EGLDL 467
Cdd:PRK09922   134 ADYHLAISSGIKEQMMARGISAQRISVIYNPVEIKTIIiPPPERDKPAVFL----------YVGRLKFEgqknvkELFDG 203

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1994078563  468 LVRATGEVLsrgLDVrtviVGDGPSLDGLRALTNELQLENHVTFTG 513
Cdd:PRK09922   204 LSQTTGEWQ---LHI----IGDGSDFEKCKAYSRELGIEQRIIWHG 242
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 394-561 8.08e-05

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: 46.67  E-value: 8.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  394 EADQVLAITLQVADKLVSRGVASERITLLPNSVDVHVF--SP--LPAHQKTLaklgipdgipvIGYAGSVVDYEGLDLLV 469
Cdd:cd03799    125 QGDLFLPNCELFKHRLIALGCDEKKIIVHRSGIDCNKFrfKPryLPLDGKIR-----------ILTVGRLTEKKGLEYAI 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  470 RATGEVLSRGLDVRTVIVGDGPSLDGLRALTNELQLENHVTFTGRVPSSSVPLYLSCFDVVPSPRrrlpVT-----ELVP 544
Cdd:cd03799    194 EAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPS----VTaadgdQDGP 269

                          170
                   ....*....|....*..
gi 1994078563  545 PLKPLEAMASGKAVILT 561
Cdd:cd03799    270 PNTLKEAMAMGLPVIST 286
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 418-633 1.17e-04

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: 46.17  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  418 RITLLPNSVDVHVFSPLPAhQKTLAKLGIPDGIPVIGYAGSVVD--YEGLDLLVRATgEVLSRGLDVRTVIVGDGPSLD- 494
Cdd:cd03825    162 PVVVIPNGIDTEIFAPVDK-AKARKRLGIPQDKKVILFGAESVTkpRKGFDELIEAL-KLLATKDDLLLVVFGKNDPQIv 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  495 -------GLRALTNELQLenhvtftgrvpsssVPLYLSC-FDVVPSPRRRLPVTELvpplkplEAMASGKAVILTDLPPL 566
Cdd:cd03825    240 ilpfdiiSLGYIDDDEQL--------------VDIYSAAdLFVHPSLADNLPNTLL-------EAMACGTPVVAFDTGGS 298

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1994078563  567 RDLAgADGERARLCDSESSKSLADAIEATLRDTSGTADMTRRARLWTVKDRTWVKAAATLKKVYSQL 633
Cdd:cd03825    299 PEIV-QHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYKDL 364
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 1246-1393 2.89e-04

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: 45.00  E-value: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1246 RDYSIPEQQTRVIGNSVDIEGLDNDK-----------VSGARFNLGLVGIIPRRKRLDRALDLLSKLRREDDRFHLYIKG 1314
Cdd:cd03807    149 QEQGYAKNKIVVIYNGIDLFKLSPDDasrararrrlgLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVG 228

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994078563 1315 KRPEdypwmakrteemdfySEQLRRIEADPFLNGAVTFDPHGEDMPGWYRKIGVVLSLSDFESFHLTLADGAASGaIPC 1393
Cdd:cd03807    229 RGPE---------------RPNLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACG-LPV 291
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
1276-1393 7.34e-04

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 41.34  E-value: 7.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1276 RFNLGLVG-IIPRRKRLDRALDLLSKLRREDDRFHLYIKGKRPEdypwmakrteemdfysEQLRRIEADpfLNGAVTFdp 1354
Cdd:pfam13692    1 RPVILFVGrLHPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPE----------------EELEELAAG--LEDRVIF-- 60

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1994078563 1355 HG--EDMPGWYRKIGVVLSLSDFESFHLTLADGAASGaIPC 1393
Cdd:pfam13692   61 TGfvEDLAELLAAADVFVLPSLYEGFGLKLLEAMAAG-LPV 100
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 1209-1389 1.25e-03

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: 43.00  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1209 VTRFHLQELYTPFPSRLNMAavdQLIFVGEHLRSIAS---------RDYSIPEQQTRVIGNSVDIE---GLDNDKVSGAR 1276
Cdd:cd03800    137 VKYRHLGAQDTYHPSLRITA---EEQILEAADRVIAStpqeadeliSLYGADPSRINVVPPGVDLErffPVDRAEARRAR 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1277 FNLGL-------VGIIPRRKRLDRALDLLSKLRREDDRFHLYI-KGKRPEDypwmakrtEEMDfySEQLRRIEADPFLNG 1348
Cdd:cd03800    214 LLLPPdkpvvlaLGRLDPRKGIDTLVRAFAQLPELRELANLVLvGGPSDDP--------LSMD--REELAELAEELGLID 283

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1994078563 1349 AVTFDPH--GEDMPGWYRKIGVVLSLSDFESFHLTLADGAASG 1389
Cdd:cd03800    284 RVRFPGRvsRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACG 326
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
872-965 1.69e-03

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 39.12  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  872 IHINVNSVTESQTMfsrRVVEIAASGGAIISGPGRGAQRVL--GGTVPVLDNTDTAAALMELWMSDESVRNDDAWLAMRT 949
Cdd:pfam13524    1 IVLNPSRRPDSPNM---RVFEAAACGAPLLTDRTPGLEELFepGEEILLYRDPEELAEKIRYLLEHPEERRAIAAAGRER 77

                           90
                   ....*....|....*.
gi 1994078563  950 VFRAHTGGHRLTYALR 965
Cdd:pfam13524   78 VLAEHTYAHRAEQLLD 93
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 1282-1389 2.64e-03

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: 41.24  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1282 VGIIPRRKRLDRALDLLSKLRREDDRFHLYIKGKRPEDYPWMAKRTEEmdfyseqlrRIEADPFLngaVTFDPHGEDMPG 1361
Cdd:cd01635    116 VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAAL---------GLLERVVI---IGGLVDDEVLEL 183

                           90       100
                   ....*....|....*....|....*...
gi 1994078563 1362 WYRKIGVVLSLSDFESFHLTLADGAASG 1389
Cdd:cd01635    184 LLAAADVFVLPSRSEGFGLVLLEAMAAG 211
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 1224-1325 6.21e-03

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: 40.79  E-value: 6.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563 1224 RLNMAAVDQLIFVGEHLRSIASRDYsIPEQQTRVIGNSVDIEGLDNDKVS--------GARFNLGLVGIIPRRKRLDRAL 1295
Cdd:cd03794    158 RKLYRLADAIIVLSPGLKEYLLRKG-VPKEKIIVIPNWADLEEFKPPPKDelrkklglDDKFVVVYAGNIGKAQGLETLL 236

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1994078563 1296 DLLSKLRREDD-RFHLYIKGKRPEDYPWMAK 1325
Cdd:cd03794    237 EAAERLKRRPDiRFLFVGDGDEKERLKELAK 267
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 259-575 7.15e-03

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 40.79  E-value: 7.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  259 KQGADFVVAV--RPGYPWDVKTDRGTASRSSFEEEIDGVRHLFsagpswtgQPLDSYVQYAADQYVQVAMQNRVSIIHA- 335
Cdd:PRK15179   336 REGADFFAATlaDAGIPVSVYSDMQAWGGCEFSSLLAPYREYL--------RFLPKQIIEGTTKLTDVMRSSVPSVVHIw 407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  336 --ASNHVTALPALIAarrlGLP-FVYEVRGFWEItEQSSRPGWEHTDRFALALQLETlVANEADQVLAITlQVADKLvsr 412
Cdd:PRK15179   408 qdGSIFACALAALLA----GVPrIVLSVRTMPPV-DRPDRYRVEYDIIYSELLKMRG-VALSSNSQFAAH-RYADWL--- 477

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  413 GVASERITLLPNSVDVHVFSPLPAHQKTLAKL--GIPDGIPVIGYAGSVVDYEGLDLLVRATGEVLSRGLDVRTVIVGDG 490
Cdd:PRK15179   478 GVDERRIPVVYNGLAPLKSVQDDACTAMMAQFdaRTSDARFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGG 557

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994078563  491 PSLDGLRALTNELQLENHVTFTGRvpSSSVPLYLSCFD--VVPSPRRRLPVTelvpplkPLEAMASGKAVILTdlpplrd 568
Cdd:PRK15179   558 PLLESVREFAQRLGMGERILFTGL--SRRVGYWLTQFNafLLLSRFEGLPNV-------LIEAQFSGVPVVTT------- 621


                   ....*..
gi 1994078563  569 LAGADGE 575
Cdd:PRK15179   622 LAGGAGE 628
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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