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Conserved domains on  [gi|2310149060|ref|WP_261423826|]
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MULTISPECIES: glycosyltransferase family 1 protein [Serratia]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133545)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 1-346 3.16e-103

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: 308.14  E-value: 3.16e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060   1 MIYINARFLTQDVTGVQRFAEQICMELVELRSDIVLLAPRDIKRATLPASFN----------VRFIGKKSGHYWEQIELP 70
Cdd:cd03809     1 KILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREypelslgvikIKLWRELALLRWLQILLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  71 RYLKSlgsPLLLNLCSTAPAFYNN--QIVTHHDVTYKRYKKSFSLKFRALYSVLVPLMLRNSKALITVSNFSKSEILDYF 148
Cdd:cd03809    81 KKDKP---DLLHSPHNTAPLLLKGcpQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPISLRRADAIITVSEATRDDIIKFY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 149 SYVKENVYIVYNAVGQEFSP------GMLEENDKDKYILAVSSPNYHKNFHGMLESFSLVKRQhGGNVKLKVIGKSSASF 222
Cdd:cd03809   158 GVPPEKIVVIPLGVDPSFFPpesaavLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQ-GGDLKLVIVGGKGWED 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 223 SS--QDFSKNLVNDDVIFLGRIEDEKLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESVIYFD 300
Cdd:cd03809   237 EEllDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDAALYFD 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2310149060 301 PYNINEMADAMAKVISDEETRSKLISSGFDNVKKYSWKKSAQSVCD 346
Cdd:cd03809   317 PLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 1-346 3.16e-103

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: 308.14  E-value: 3.16e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060   1 MIYINARFLTQDVTGVQRFAEQICMELVELRSDIVLLAPRDIKRATLPASFN----------VRFIGKKSGHYWEQIELP 70
Cdd:cd03809     1 KILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREypelslgvikIKLWRELALLRWLQILLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  71 RYLKSlgsPLLLNLCSTAPAFYNN--QIVTHHDVTYKRYKKSFSLKFRALYSVLVPLMLRNSKALITVSNFSKSEILDYF 148
Cdd:cd03809    81 KKDKP---DLLHSPHNTAPLLLKGcpQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPISLRRADAIITVSEATRDDIIKFY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 149 SYVKENVYIVYNAVGQEFSP------GMLEENDKDKYILAVSSPNYHKNFHGMLESFSLVKRQhGGNVKLKVIGKSSASF 222
Cdd:cd03809   158 GVPPEKIVVIPLGVDPSFFPpesaavLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQ-GGDLKLVIVGGKGWED 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 223 SS--QDFSKNLVNDDVIFLGRIEDEKLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESVIYFD 300
Cdd:cd03809   237 EEllDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDAALYFD 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2310149060 301 PYNINEMADAMAKVISDEETRSKLISSGFDNVKKYSWKKSAQSVCD 346
Cdd:cd03809   317 PLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 176-328 1.58e-38

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: 134.71  E-value: 1.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 176 KDKYILAVSSPNYHKNFHGMLESFSLVKRQHGgNVKLKVIGKSSASFSSQDFSKNL-VNDDVIFLGRIEDEKLISLYQNA 254
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNP-NLKLVIAGDGEEEKRLKKLAEKLgLGDNVIFLGFVSDEDLPELLKIA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310149060 255 IAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVL--NESVIYFDPYNINEMADAMAKVISDEETRSKLISSG 328
Cdd:pfam00534  80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVkdGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENA 155
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 239-351 1.10e-27

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 105.07  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 239 LGRIEDEK-----LISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESV--IYFDPYNINEMADAM 311
Cdd:COG0438     1 MGRLVPRKgldllLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGEtgLLVPPGDPEALAEAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2310149060 312 AKVISDEETRSKLISSGFDNV-KKYSWKKSAQSVCDIINSI 351
Cdd:COG0438    81 LRLLEDPELRRRLGEAARERAeERFSWEAIAERLLALYEEL 121
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
 179-343 1.03e-21

glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 94.77  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 179 YILAVSSPNYHKNFHGMLESFSLVKRQHGGnVKLkVIGKSSASFSSQDFSKNLVN---------DDVIFLGRIEDEKLIS 249
Cdd:TIGR04047 195 YVLAVGGIEPRKNTIDLLEAFALLRARRPQ-AQL-VIAGGATLFDYDAYRREFRAraaelgvdpGPVVITGPVPDADLPA 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 250 LYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLN-ESVIYFDPYNINEMADAMAKVIsDEETRSKLISSG 328
Cdd:TIGR04047 273 LYRCADAFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYLGrFDAAWADPSDPDSIADALALAL-DPARRPALRAAG 351

                         170
                  ....*....|....*
gi 2310149060 329 FDNVKKYSWKKSAQS 343
Cdd:TIGR04047 352 PELAARYTWDASARA 366
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 236-340 7.51e-08

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 53.95  E-value: 7.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 236 VIFLGRIEDEKLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNE-----SVIYFDPYNINEMADA 310
Cdd:PLN02871  314 TVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPdqegkTGFLYTPGDVDDCVEK 393

                          90       100       110
                  ....*....|....*....|....*....|
gi 2310149060 311 MAKVISDEETRSKLISSGFDNVKKYSWKKS 340
Cdd:PLN02871  394 LETLLADPELRERMGAAAREEVEKWDWRAA 423
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 1-346 3.16e-103

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: 308.14  E-value: 3.16e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060   1 MIYINARFLTQDVTGVQRFAEQICMELVELRSDIVLLAPRDIKRATLPASFN----------VRFIGKKSGHYWEQIELP 70
Cdd:cd03809     1 KILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREypelslgvikIKLWRELALLRWLQILLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  71 RYLKSlgsPLLLNLCSTAPAFYNN--QIVTHHDVTYKRYKKSFSLKFRALYSVLVPLMLRNSKALITVSNFSKSEILDYF 148
Cdd:cd03809    81 KKDKP---DLLHSPHNTAPLLLKGcpQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPISLRRADAIITVSEATRDDIIKFY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 149 SYVKENVYIVYNAVGQEFSP------GMLEENDKDKYILAVSSPNYHKNFHGMLESFSLVKRQhGGNVKLKVIGKSSASF 222
Cdd:cd03809   158 GVPPEKIVVIPLGVDPSFFPpesaavLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQ-GGDLKLVIVGGKGWED 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 223 SS--QDFSKNLVNDDVIFLGRIEDEKLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESVIYFD 300
Cdd:cd03809   237 EEllDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDAALYFD 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2310149060 301 PYNINEMADAMAKVISDEETRSKLISSGFDNVKKYSWKKSAQSVCD 346
Cdd:cd03809   317 PLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-349 5.83e-47

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: 163.09  E-value: 5.83e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060   2 IYINARFLTQDVTGVQRFAEQICMELVELRSDIVLLAPRDIKRATLPASFNVRFIGKKS----GHYWEQIELPRYLKSLG 77
Cdd:cd03801     2 ILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSlaalLRARRLLRELRPLLRLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  78 SPLLLNLCSTAPAFYNN---------QIVTHHDVTYKRYKKSFSLKFRALYSVLVplMLRNSKALITVSNFSKSEILDYF 148
Cdd:cd03801    82 KFDVVHAHGLLAALLAAllalllgapLVVTLHGAEPGRLLLLLAAERRLLARAEA--LLRRADAVIAVSEALRDELRALG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 149 SYVKENVYIVYNAV-GQEFSPGMLEEN---DKDKYILAVSSPNYHKNFHGMLESFSLVKRQHGgNVKLKVIGKSSASFSS 224
Cdd:cd03801   160 GIPPEKIVVIPNGVdLERFSPPLRRKLgipPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGP-DVRLVIVGGDGPLRAE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 225 QDFSKNLVNDDVIFLGRIEDEKLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVL--NESVIYFDPY 302
Cdd:cd03801   239 LEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVedGEGGLVVPPD 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2310149060 303 NINEMADAMAKVISDEETRSKLISSGFDNV-KKYSWKKSAQSVCDIIN 349
Cdd:cd03801   319 DVEALADALLRLLADPELRARLGRAARERVaERFSWERVAERLLDLYR 366
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 176-328 1.58e-38

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: 134.71  E-value: 1.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 176 KDKYILAVSSPNYHKNFHGMLESFSLVKRQHGgNVKLKVIGKSSASFSSQDFSKNL-VNDDVIFLGRIEDEKLISLYQNA 254
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNP-NLKLVIAGDGEEEKRLKKLAEKLgLGDNVIFLGFVSDEDLPELLKIA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310149060 255 IAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVL--NESVIYFDPYNINEMADAMAKVISDEETRSKLISSG 328
Cdd:pfam00534  80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVkdGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENA 155
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 15-339 1.32e-30

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: 119.26  E-value: 1.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  15 GVQRFAEQICMELVELRSDIVLLAPRDIKRAT---LPASFNVRFIGKKSGH--------YWEQIELPRYLK--------S 75
Cdd:cd03820    14 GAERVAINLANHLAKKGYDVTIISLDSAEKPPfyeLDDNIKIKNLGDRKYShfklllkyFKKVRRLRKYLKnnkpdvviS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  76 LGSPLLLNLCS-TAPAFYnnqIVTHHdVTYKRYKKSFSLKFRALYSVlvplmlRNSKALITVSnfsKSEILDYFSYVKEN 154
Cdd:cd03820    94 FRTSLLTFLALiGLKSKL---IVWEH-NNYEAYNKGLRRLLLRRLLY------KRADKIVVLT---EADKLKKYKQPNSN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 155 VYIVYNAVgqEFSPGMLEENDKDKYILAVSSPNYHKNFHGMLESFSLVKRQHGGnVKLKVIGKSSASFSSQDF-SKNLVN 233
Cdd:cd03820   161 VVVIPNPL--SFPSEEPSTNLKSKRILAVGRLTYQKGFDLLIEAWALIAKKHPD-WKLRIYGDGPEREELEKLiDKLGLE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 234 DDVIFLGRIEDekLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMP-EVL--NESVIYFDPYNINEMADA 310
Cdd:cd03820   238 DRVKLLGPTKN--IAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCPTGPsEIIedGENGLLVPNGDVDALAEA 315

                         330       340
                  ....*....|....*....|....*....
gi 2310149060 311 MAKVISDEETRSKLISSGFDNVKKYSWKK 339
Cdd:cd03820   316 LLRLMEDEELRKKMGKNARKNAERFSIEK 344
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
178-317 6.49e-28

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 106.06  E-value: 6.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 178 KYILAVSS--PNYhKNFHGMLESFSLVKRQHGgNVKLKVIGKSSASfSSQDFSKNLvNDDVIFLGRIEDekLISLYQNAI 255
Cdd:pfam13692   2 PVILFVGRlhPNV-KGVDYLLEAVPLLRKRDN-DVRLVIVGDGPEE-ELEELAAGL-EDRVIFTGFVED--LAELLAAAD 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310149060 256 AFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLN-ESVIYFDPYNINEMADAMAKVISD 317
Cdd:pfam13692  76 VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDgENGLLVPPGDPEALAEAILRLLED 138
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 239-351 1.10e-27

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 105.07  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 239 LGRIEDEK-----LISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESV--IYFDPYNINEMADAM 311
Cdd:COG0438     1 MGRLVPRKgldllLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGEtgLLVPPGDPEALAEAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2310149060 312 AKVISDEETRSKLISSGFDNV-KKYSWKKSAQSVCDIINSI 351
Cdd:COG0438    81 LRLLEDPELRRRLGEAARERAeERFSWEAIAERLLALYEEL 121
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 15-324 6.21e-27

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: 108.98  E-value: 6.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  15 GVQRFAEQICMELVELRSDIVLLAPRD-------IKRATLPASFNVRFIGKKSGHYWEQIE-LPRYLKSLGSPLLLNLCS 86
Cdd:cd03811    13 GAERVLLNLANALDKRGYDVTLVLLRDegdldkqLNGDVKLIRLLIRVLKLIKLGLLKAILkLKRILKRAKPDVVISFLG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  87 TAPAFYNNQ-------IVTHH-DVTYKRYKKSFSLKFRALYsvlvplmlRNSKALITVSNFSKSEILDYFSYVKENVYIV 158
Cdd:cd03811    93 FATYIVAKLaaarskvIAWIHsSLSKLYYLKKKLLLKLKLY--------KKADKIVCVSKGIKEDLIRLGPSPPEKIEVI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 159 YNAVGQEFSPGMLEEN-----DKDKYILAVSSPNYHKNFHGMLESFSLVKRqHGGNVKLKVIGKSSASFSSQDFSKNL-V 232
Cdd:cd03811   165 YNPIDIDRIRALAKEPilnepEDGPVILAVGRLDPQKGHDLLIEAFAKLRK-KYPDVKLVILGDGPLREELEKLAKELgL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 233 NDDVIFLGRIEDekLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVL-NESVIYFDPYNINEMADAM 311
Cdd:cd03811   244 AERVIFLGFQSN--PYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILdDGENGLLVPDGDAAALAGI 321

                         330
                  ....*....|...
gi 2310149060 312 AKVISDEETRSKL 324
Cdd:cd03811   322 LAALLQKKLDAAL 334
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 15-336 3.52e-24

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: 101.52  E-value: 3.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  15 GVQRFAEQICMELVELRSDIVLLAPRDIKRATLPASFNVRFIG---KKSG--HYWE---QIELPRYLKSLgSPLLLNLCS 86
Cdd:cd03808    11 GFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKELGVKVIDipiLRRGinPLKDlkaLFKLYKLLKKE-KPDIVHCHT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  87 TAPAFY-------NNQIVTHHDVTYKRYKKSFSLKFRALYSVLVPLMLRNSKALITVSNFSKSEILDYFSYVKENVYIVY 159
Cdd:cd03808    90 PKPGILgrlaarlAGVPKVIYTVHGLGFVFTEGKLLRLLYLLLEKLALLFTDKVIFVNEDDRDLAIKKGIIKKKKTVLIP 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 160 -NAVGQEFSPGMLEENDKDKYILA-VSSPNYHKNFHGMLESFSLVKRQHGgNVKLKVIGKSSASFSSQDFSKNLVNDDVI 237
Cdd:cd03808   170 gSGVDLDRFQYSPESLPSEKVVFLfVARLLKDKGIDELIEAAKILKKKGP-NVRFLLVGDGELENPSEILIEKLGLEGRI 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 238 -FLGRIEDekLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVL--NESVIYFDPYNINEMADAMAKV 314
Cdd:cd03808   249 eFLGFRSD--VPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVidGVNGFLVPPGDVEALADAIEKL 326

                         330       340
                  ....*....|....*....|...
gi 2310149060 315 ISDEETRSKLISSGFDNV-KKYS 336
Cdd:cd03808   327 IEDPELRKEMGEAARKRVeEKFD 349
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 96-344 2.02e-22

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


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 96.96  E-value: 2.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  96 IVTHH----DVTYkrYKKSFSLKFRALYSVLVPLMLRNSKALITVSNFSKSEILDYfsYVKENVYIVYNAVGQEFSPGML 171
Cdd:cd03817   112 VHTYHtmyeDYLH--YIPKGKLLVKAVVRKLVRRFYNHTDAVIAPSEKIKDTLREY--GVKGPIEVIPNGIDLDKFEKPL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 172 EENDKDKY--------ILAVSSPNYHKNFHGMLESFSLVKRQHggNVKLKVIGKSSASFSSQDFSKNL-VNDDVIFLGRI 242
Cdd:cd03817   188 NTEERRKLglppdepiLLYVGRLAKEKNIDFLLRAFAELKKEP--NIKLVIVGDGPEREELKELARELgLADKVIFTGFV 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 243 EDEKLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESV--IYFDPYNInEMADAMAKVISDEET 320
Cdd:cd03817   266 PREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGEngFLFEPNDE-TLAEKLLHLRENLEL 344

                         250       260
                  ....*....|....*....|....
gi 2310149060 321 RSKLISSGFDNVKKYSWKKSAQSV 344
Cdd:cd03817   345 LRKLSKNAEISAREFAFAKSVEKL 368
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
 179-343 1.03e-21

glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 94.77  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 179 YILAVSSPNYHKNFHGMLESFSLVKRQHGGnVKLkVIGKSSASFSSQDFSKNLVN---------DDVIFLGRIEDEKLIS 249
Cdd:TIGR04047 195 YVLAVGGIEPRKNTIDLLEAFALLRARRPQ-AQL-VIAGGATLFDYDAYRREFRAraaelgvdpGPVVITGPVPDADLPA 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 250 LYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLN-ESVIYFDPYNINEMADAMAKVIsDEETRSKLISSG 328
Cdd:TIGR04047 273 LYRCADAFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYLGrFDAAWADPSDPDSIADALALAL-DPARRPALRAAG 351

                         170
                  ....*....|....*
gi 2310149060 329 FDNVKKYSWKKSAQS 343
Cdd:TIGR04047 352 PELAARYTWDASARA 366
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 178-342 6.24e-21

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: 92.69  E-value: 6.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 178 KYILAVSSPNYHKNFHGMLESFSLVKRqHGGNVKLKVIGKSSASFSSQD------FSKNL-VNDDVIFLGRIEDEKLISL 250
Cdd:cd03800   221 PVVLALGRLDPRKGIDTLVRAFAQLPE-LRELANLVLVGGPSDDPLSMDreelaeLAEELgLIDRVRFPGRVSRDDLPEL 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 251 YQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESV--IYFDPYNINEMADAMAKVISDEETRSKLISSG 328
Cdd:cd03800   300 YRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRtgLLVDPHDPEALAAALRRLLDDPALWQRLSRAG 379

                         170
                  ....*....|....*
gi 2310149060 329 FDNVK-KYSWKKSAQ 342
Cdd:cd03800   380 LERARaHYTWESVAD 394
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 127-344 8.69e-21

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: 92.06  E-value: 8.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 127 LRNSKALITVSNFSKSEILDYFSYvKENVYIVYNAVGQ-EFSPG--MLEENDKDKYILAVSSPNYHKNFHGMLESFSLVK 203
Cdd:cd03798   148 LRRAARVIAVSKALAEELVALGVP-RDRVDVIPNGVDPaRFQPEdrGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLA 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 204 RQHGgNVKLKVIGKSSASFSSQDFSKNLVN-DDVIFLGRIEDEKlISLYQNAI-AFVFPSFYEGFGIPPLEAQACGCPVI 281
Cdd:cd03798   227 KARP-DVVLLIVGDGPLREALRALAEDLGLgDRVTFTGRLPHEQ-VPAYYRACdVFVLPSRHEGFGLVLLEAMACGLPVV 304

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310149060 282 SSNKASMPEVLN--ESVIYFDPYNINEMADAMAKVI-------SDEETRSKLissgfdnVKKYSWKKSAQSV 344
Cdd:cd03798   305 ATDVGGIPEVVGdpETGLLVPPGDADALAAALRRALaepylreLGEAARARV-------AERFSWVKAADRI 369
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 96-335 2.38e-20

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: 90.84  E-value: 2.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  96 IVTHHDVTYKRYKKSFSLKFRALYSvlvplmlRNSKALITVSNFSKSEILDYfSYVKENVYIVYNAVG-QEFSPG----- 169
Cdd:cd03807   107 IWSVRSSNIPQRLTRLVRKLCLLLS-------KFSPATVANSSAVAEFHQEQ-GYAKNKIVVIYNGIDlFKLSPDdasra 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 170 ----MLEENDKDKYILAVSspNYH--KNFHGMLESFSLVKRQHGgNVKLKVIGKSSASFSSQDFSKNL-VNDDVIFLGRI 242
Cdd:cd03807   179 rarrRLGLAEDRRVIGIVG--RLHpvKDHSDLLRAAALLVETHP-DLRLLLVGRGPERPNLERLLLELgLEDRVHLLGER 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 243 EDekLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESV-IYFDPYNINEMADAMAKVISDEETR 321
Cdd:cd03807   256 SD--VPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDGTgFLVPAGDPQALADAIRALLEDPEKR 333

                         250
                  ....*....|....
gi 2310149060 322 SKLISSGFDNVKKY 335
Cdd:cd03807   334 ARLGRAARERIANE 347
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 225-343 5.50e-19

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: 87.04  E-value: 5.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 225 QDFSKNLVNDDVIFLGRIEDEKLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNE-SVIYFDPyN 303
Cdd:cd03821   253 QLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAgCGVVVDP-N 331

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2310149060 304 INEMADAMAKVISDEETRSKL---ISSGFDNVKKYSWKKSAQS 343
Cdd:cd03821   332 VSSLAEALAEALRDPADRKRLgemARRARQVEENFSWEAVAGQ 374
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 181-296 8.38e-18

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


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 81.30  E-value: 8.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 181 LAVSSPNYHKNFHGMLESFSLVKRQHGGNVKLKVIGKSSASFSSQDFSKNLVNDDVIFLG-RIEDEKLISLYQNAIAFVF 259
Cdd:cd01635   114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGgLVDDEVLELLLAAADVFVL 193

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2310149060 260 PSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESV 296
Cdd:cd01635   194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGE 230
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 101-324 1.90e-17

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: 82.40  E-value: 1.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 101 DVTYKRYKKSFSlkfralysVLVPLMLRNSKALITVSNFSKSEILDYFSyVKENVYIVYNAVGQ-EFSPgmlEENDKD-- 177
Cdd:cd04962   121 DITLVGYDPSLQ--------PAVRFSINKSDRVTAVSSSLRQETYELFD-VDKDIEVIHNFIDEdVFKR---KPAGALkr 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 178 --------KYILAVSSPNYHKNFHGMLESFSLVKRQHggNVKLKVIGKSSASFSSQDFSKNL-VNDDVIFLGRIEDekLI 248
Cdd:cd04962   189 rllappdeKVVIHVSNFRPVKRIDDVVRVFARVRRKI--PAKLLLVGDGPERVPAEELARELgVEDRVLFLGKQDD--VE 264

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310149060 249 SLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESVIYF--DPYNINEMADAMAKVISDEETRSKL 324
Cdd:cd04962   265 ELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFlsDVGDVDAMAKSALSILEDDELYNRM 342
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 80-342 1.45e-16

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: 79.64  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  80 LLLNLCSTAPAFYNNQIVTHHDVTYKRYKKsfslkFRALYSVLVPLMLRNSKALITVSNFSKSEILDYFSYvkENVYIVY 159
Cdd:cd03812    92 NGIILLLAAKAGVPVRIAHSHNTKDSSIKL-----RKIRKNVLKKLIERLSTKYLACSEDAGEWLFGEVEN--GKFKVIP 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 160 NAVGQE---FSPGMlEENDKDKYILA-------VSSPNYHKNFHGMLESFSLVKRQhGGNVKLKVIGKSSASFSSQDFSK 229
Cdd:cd03812   165 NGIDIEkykFNKEK-RRKRRKLLILEdklvlghVGRFNEQKNHSFLIDIFEELKKK-NPNVKLVLVGEGELKEKIKEKVK 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 230 NL-VNDDVIFLGRIEDekLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESVIYFDPYNINEM- 307
Cdd:cd03812   243 ELgLEDKVIFLGFRND--VSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITNNVEFLPLNETPSTw 320

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2310149060 308 ADAMAKVISDEETRSKLISSGFDNVKKYSWKKSAQ 342
Cdd:cd03812   321 AEKILKLIKRKRRINKEINKEKKELGYDDESLELT 355
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 125-337 3.80e-16

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


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 78.52  E-value: 3.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 125 LMLRNSKALITVSNFskseILDYFS---YVKENVYIVYNAVgqEFSPGMLE---ENDKDKYILAVSSPNYHKNFHGMLES 198
Cdd:cd03823   139 LFKKGGDAVLAPSRF----TANLHEangLFSARISVIPNAV--EPDLAPPPrrrPGTERLRFGYIGRLTEEKGIDLLVEA 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 199 FSLVKRqhgGNVKLKVIGkssaSFSSQDFSKNLVNDDVIFLGRIEDEKLISLYQNAIAFVFPS-FYEGFGIPPLEAQACG 277
Cdd:cd03823   213 FKRLPR---EDIELVIAG----HGPLSDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSiWPEPFGLVVREAIAAG 285

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310149060 278 CPVISSNKASMPEVLNESV--IYFDPYNINEMADAMAKVISDEEtRSKLISSGFDNVKKYSW 337
Cdd:cd03823   286 LPVIASDLGGIAELIQPGVngLLFAPGDAEDLAAAMRRLLTDPA-LLERLRAGAEPPRSTES 346
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 113-324 6.65e-16

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: 77.70  E-value: 6.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 113 LKFRALYSVLVPLM---LRNSKALITVSN--FSKSEILDYFsyvKENVYIV--------YNaVGQEFSPGMLEENDKDKY 179
Cdd:cd03795   118 VKQKKLLKLYKPLMtrfLRRADRIIATSPnyVETSPTLREF---KNKVRVIplgidknvYN-IPRVDFENIKREKKGKKI 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 180 ILAVSSPNYHKNFHGMLESfslVKRQhggNVKLKVIGKSSASFSSQDFSKNLVNDDVIFLGRIEDEKLISLYQNAIAFVF 259
Cdd:cd03795   194 FLFIGRLVYYKGLDYLIEA---AQYL---NYPIVIGGEGPLKPDLEAQIELNLLDNVKFLGRVDDEEKVIYLHLCDVFVF 267

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 260 PSFY--EGFGIPPLEAQACGCPVISSNKA-SMPEVLN--ESVIYFDPYNINEMADAMAKVISDEETRSKL 324
Cdd:cd03795   268 PSVLrsEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNngETGLVVPPKDPDALAEAIDKLLSDEELRESY 337
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 3-342 6.10e-14

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: 72.37  E-value: 6.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060   3 YINARFLTQDVTGVQRFAEqICMELVELRSDIVLLAPR-------------------DIKRATLPASFNVRFIGKKSGHY 63
Cdd:cd03794     4 LISQYYPPPKGAAAARVYE-LAKELVRRGHEVTVLTPSpnyplgrifagatetkdgiRVIRVKLGPIKKNGLIRRLLNYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  64 WEQIELPRYLKSLGSPLLLNLCSTAPAF-----------YNNQIVTH-HDVTYKRYKKSFSLKFRALYSVLVPL---MLR 128
Cdd:cd03794    83 SFALAALLKLLVREERPDVIIAYSPPITlglaalllkklRGAPFILDvRDLWPESLIALGVLKKGSLLKLLKKLerkLYR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 129 NSKALITVSNfsksEILDYFSY---VKENVYIVYN-AVGQEFSPGMLEE-----NDKDKYILAVSSPNYHK-NFHGMLES 198
Cdd:cd03794   163 LADAIIVLSP----GLKEYLLRkgvPKEKIIVIPNwADLEEFKPPPKDElrkklGLDDKFVVVYAGNIGKAqGLETLLEA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 199 FSLVKRQHggNVKLKVIGKSSASFSSQDFSKNLVNDDVIFLGRIEDEKLISLYQNA-IAFVF--PSFYEGFGIP--PLEA 273
Cdd:cd03794   239 AERLKRRP--DIRFLFVGDGDEKERLKELAKARGLDNVTFLGRVPKEEVPELLSAAdVGLVPlkDNPANRGSSPskLFEY 316

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310149060 274 QACGCPVISSNKASMPEV--LNESVIYFDPYNINEMADAMAKVISDEETRSKLISSGFDNVK-KYSWKKSAQ 342
Cdd:cd03794   317 MAAGKPILASDDGGSDLAveINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEeKFSREKLAD 388
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 134-324 6.61e-14

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: 71.62  E-value: 6.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 134 ITVSNFSKSEILDYFSYVKENVYIVYNAVG-QEFSPGMLEEN------DKDKYILA----VSSPNYHKNFHGMLESFslv 202
Cdd:cd03819   131 IAVSELVRDHLIEALGVDPERIRVIPNGVDtDRFPPEAEAEEraqlglPEGKPVVGyvgrLSPEKGWLLLVDAAAEL--- 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 203 krQHGGNVKLKVIGKSSASfssqDFSKNLVN-----DDVIFLGRIEDekLISLYQNAIAFVFPSFYEGFGIPPLEAQACG 277
Cdd:cd03819   208 --KDEPDFRLLVAGDGPER----DEIRRLVErlglrDRVTFTGFRED--VPAALAASDVVVLPSLHEEFGRVALEAMACG 279

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2310149060 278 CPVISSNKASMPEVLN--ESVIYFDPYNINEMADAMAKVISDEETRSKL 324
Cdd:cd03819   280 TPVVATDVGGAREIVVhgRTGLLVPPGDAEALADAIRAAKLLPEAREKL 328
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 103-312 9.37e-13

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: 68.47  E-value: 9.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 103 TYKRYKKSFSLKFRALySVLVPLMLRNSK-----------ALITVSNFSKSEILDYfsYVKENVyIVYNAVG-QEFSPgm 170
Cdd:cd03804   121 LYHQYLAESGLGKGIK-SLLASLFLHYLRlwdvrtaqrvdLFIANSQFVARRIKKF--YGREST-VIYPPVDtDAFAP-- 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 171 leENDKDKYILAVSSPNYHKNFHGMLESFSLVKRqhggnvKLKVIGkssasfSSQDFS--KNLVNDDVIFLGRIEDEKLI 248
Cdd:cd03804   195 --AADKEDYYLTASRLVPYKRIDLAVEAFNELPK------RLVVIG------DGPDLDrlRAMASPNVEFLGYQPDEVLK 260

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310149060 249 SLYQNAIAFVFPSfYEGFGIPPLEAQACGCPVISSNKASMPEVL--NESVIYFDPYNINEMADAMA 312
Cdd:cd03804   261 ELLSKARAFVFAA-EEDFGIVPVEAQACGTPVIAFGKGGALETVrpGPTGILFGEQTVESLKAAVE 325
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 133-324 1.18e-12

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: 68.13  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 133 LITVSNFSKSEILDYFSYVKENVYIVYNAVG-QEFSPGMLEEN------DKDKYIL---AVSSPNYHKNFHGMLESFS-L 201
Cdd:cd03825   141 IVAPSRWLADMVRRSPLLKGLPVVVIPNGIDtEIFAPVDKAKArkrlgiPQDKKVIlfgAESVTKPRKGFDELIEALKlL 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 202 VKRQhggNVKLKVIGKSSASFSSQDFsknlvndDVIFLGRIEDE-KLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPV 280
Cdd:cd03825   221 ATKD---DLLLVVFGKNDPQIVILPF-------DIISLGYIDDDeQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPV 290

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2310149060 281 ISSNKASMPEVLNESV--IYFDPYNINEMADAMAKVISDEETRSKL 324
Cdd:cd03825   291 VAFDTGGSPEIVQHGVtgYLVPPGDVQALAEAIEWLLANPKERESL 336
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 175-314 2.50e-12

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


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 66.93  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 175 DKDKYILAVSSPNY---------HKNFHGMLEsfslVKRQHGgnVKLKVIGKSSasfsSQDFSKNLVN----DDVIFLGR 241
Cdd:cd03802   158 DPADYRFQPDPEDYlaflgriapEKGLEDAIR----VARRAG--LPLKIAGKVR----DEDYFYYLQEplpgPRIEFIGE 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310149060 242 IEDEKLISLYQNAIAFVFPS-FYEGFGIPPLEAQACGCPVISSNKASMPEVLNESVIYFDPYNINEMADAMAKV 314
Cdd:cd03802   228 VGHDEKQELLGGARALLFPInWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDSVEEMAEAIANI 301
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 137-335 3.96e-12

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


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 66.84  E-value: 3.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 137 SNFSKSEILDYFSYVKEN-VYIVYNAVGQEFSPGMLEENDKDKYILAVSSPNY--------HKNFHGMLESFSLVKRQH- 206
Cdd:cd03805   162 SNFTAGVFKKTFPSLAKNpPEVLYPCVDTDSFDSTSEDPDPGDLIAKSNKKFFlsinrferKKNIALAIEAFAKLKQKLp 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 207 -GGNVKLKVIGkssasfsSQDF-----------------SKNLVNDDVIFLGRIEDEKLISLYQNAIAFVF-PSfYEGFG 267
Cdd:cd03805   242 eFENVRLVIAG-------GYDPrvaenveyleelqrlaeELLNVEDQVLFLRSISDSQKEQLLSSALALLYtPS-NEHFG 313

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310149060 268 IPPLEAQACGCPVISSNKASMPE-VLNESVIYFDPYNINEMADAMAKVISDEETRSKLISSGFDNVKKY 335
Cdd:cd03805   314 IVPLEAMYAGKPVIACNSGGPLEtVVEGVTGFLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEK 382
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 235-337 9.21e-12

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: 65.39  E-value: 9.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 235 DVIFLGRIEDEKLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESV--IYFDPYNINEMADAMA 312
Cdd:cd03814   249 DVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGtgALVEPGDAAAFAAALR 328

                          90       100
                  ....*....|....*....|....*
gi 2310149060 313 KVISDEETRSKLISSGFDNVKKYSW 337
Cdd:cd03814   329 ALLEDPELRRRMAARARAEAERYSW 353
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 96-324 1.29e-11

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: 65.17  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  96 IVTHH--DVTYKRYKKSFSLKFRALYSVLVPLMLRNSKALITVSNFSKSEILDyFSYVKENVYIVYnaVGQE---FSPGm 170
Cdd:cd05844   108 VVTFHgfDITTSRAWLAASPGWPSQFQRHRRALQRPAALFVAVSGFIRDRLLA-RGLPAERIHVHY--IGIDpakFAPR- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 171 lEENDKDKYILAVSSPNYHKNFHGMLESFSLVKRQHGgNVKLKVIGKSSASFSSQDFSKNLVNddVIFLGRIEDEKLISL 250
Cdd:cd05844   184 -DPAERAPTILFVGRLVEKKGCDVLIEAFRRLAARHP-TARLVIAGDGPLRPALQALAAALGR--VRFLGALPHAEVQDW 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 251 YQNAIAFVFPSFY------EGFGIPPLEAQACGCPVISSNKASMPEVL--NESVIYFDPYNINEMADAMAKVISDEETRS 322
Cdd:cd05844   260 MRRAEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAIldGETGFLVPEGDVDALADALQALLADRALAD 339


                  ..
gi 2310149060 323 KL 324
Cdd:cd05844   340 RM 341
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 174-336 2.77e-09

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: 57.84  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 174 NDKDKYILAVSSPNYHKNFHGMLESFSLVKrQHGGNVKLKVIGKSSASFSSQDFSKNL-VNDDVIFLGRIEDeklISLYQ 252
Cdd:cd04951   185 KNDEFVILNVGRLTEAKDYPNLLLAISELI-LSKNDFKLLIAGDGPLRNELERLICNLnLVDRVILLGQISN---ISEYY 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 253 NAI-AFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESVIYFDPYNINEMADAMAKVISDE-ETRSKLISSGFD 330
Cdd:cd04951   261 NAAdLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHNYVVPVSDPQLLAEKIKEIFDMSdEERDILGNKNEY 340


                  ....*.
gi 2310149060 331 NVKKYS 336
Cdd:cd04951   341 IAKNFS 346
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 192-324 1.23e-08

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: 56.22  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 192 FHGMLESFSLVKRQHGgNVKLKVIGKSSASFSS---------QDFSKNLVNDD--VIFLGRIEDEKLISLYQNAIAFVFP 260
Cdd:cd03818   229 FHVFMRALPRIQARRP-DARVVVVGGDGVSYGSpppdggswkQKMLAELGVDLerVHFVGKVPYDQYVRLLQLSDAHVYL 307

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310149060 261 S--FYEGFGIppLEAQACGCPVISSNKASMPEVLNES-----VIYFDPyniNEMADAMAKVISDEETRSKL 324
Cdd:cd03818   308 TypFVLSWSL--LEAMACGCPVIGSDTAPVREVIRDGrngllVDFFDP---DALAAAVLELLEDPDRAAAL 373
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 127-350 3.59e-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: 54.55  E-value: 3.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 127 LRNSKALITVSNFSKsEILDYFSYV-KENVYIVYNAV-GQEFSPGMLEENDKDKYILAVSSPNYHKNFHGMLESFSLVKR 204
Cdd:cd03796   142 LADIDHVICVSHTSK-ENTVLRASLdPRIVSVIPNAVdSSDFTPDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICK 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 205 QHGgNVKLkVIGKSSASFSS--QDFSKNLVNDDVIFLGRIEDEKLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVIS 282
Cdd:cd03796   221 KHP-NVRF-IIGGDGPKRIEleEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVS 298

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310149060 283 SNKASMPEVLNESVIYFDPYNINEMADAMAKVISDEETRSKLISSGFDNVKK-YSWKKSA---QSVCDIINS 350
Cdd:cd03796   299 TRVGGIPEVLPPDMILLAEPDPEDIVRKLEEAISILRTGKHDPWSFHNRVKKmYSWEDVArrtEKVYDRILS 370
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 236-340 7.51e-08

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 53.95  E-value: 7.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 236 VIFLGRIEDEKLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNE-----SVIYFDPYNINEMADA 310
Cdd:PLN02871  314 TVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPdqegkTGFLYTPGDVDDCVEK 393

                          90       100       110
                  ....*....|....*....|....*....|
gi 2310149060 311 MAKVISDEETRSKLISSGFDNVKKYSWKKS 340
Cdd:PLN02871  394 LETLLADPELRERMGAAAREEVEKWDWRAA 423
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 75-339 7.61e-08

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


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 53.46  E-value: 7.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  75 SLGSPLLLNLCSTAPAF---YNNQIVTHHDVTYKRYKKSFSLKFRALYSVlvplmlrnsKALITVSNFSKSEILDYFSYV 151
Cdd:cd04949    65 TLTGQVILNTKGPAKKGavlHNEHVKNNDDPEHSLIKNFYKYVFENLNKY---------DAIIVSTEQQKQDLSERFNKY 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 152 KENVYIVYNAVGQEFSPGMLEENDKDKyILAVSSPNYHKNFHGMLESFSLVKRQhGGNVKLKVIGKSSASFSSQDFSKNL 231
Cdd:cd04949   136 PPIFTIPVGYVDQLDTAESNHERKSNK-IITISRLAPEKQLDHLIEAVAKAVKK-VPEITLDIYGYGEEREKLKKLIEEL 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 232 VNDDVIFLgRIEDEKLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPevlNESVI-----YFDPY-NIN 305
Cdd:cd04949   214 HLEDNVFL-KGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKYGP---SELIEdgengYLIEKnNID 289

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2310149060 306 EMADAMAKVISDEETRSKLISSGFDNVKKYSWKK 339
Cdd:cd04949   290 ALADKIIELLNDPEKLQQFSEESYKIAEKYSTEN 323
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
195-343 2.67e-07

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 51.71  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 195 MLESFSLVKRQHGgNVKLKVIGKSSASFSS---------QDFSKNLvNDDVIFLGRIEDEKLISLYQNAIAFVFPS-FYE 264
Cdd:PRK15484  211 LMQAFEKLATAHS-NLKLVVVGDPTASSKGekaayqkkvLEAAKRI-GDRCIMLGGQPPEKMHNYYPLADLVVVPSqVEE 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 265 GFGIPPLEAQACGCPVISSNKASMPEVLNESVIYF---DPYNINEMADAMAKVISDEEtRSKLISSGFDNV-KKYSWKKS 340
Cdd:PRK15484  289 AFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYhlaEPMTSDSIISDINRTLADPE-LTQIAEQAKDFVfSKYSWEGV 367


                  ...
gi 2310149060 341 AQS 343
Cdd:PRK15484  368 TQR 370
PLN00142 PLN00142
sucrose synthase
 256-344 2.96e-07

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 52.29  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 256 AFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVLNESVIYF--DPYNINEMADAMA----KVISDEETRSKLISSGF 329
Cdd:PLN00142  669 AFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFhiDPYHGDEAANKIAdffeKCKEDPSYWNKISDAGL 748

                          90
                  ....*....|....*.
gi 2310149060 330 DNV-KKYSWKKSAQSV 344
Cdd:PLN00142  749 QRIyECYTWKIYAERL 764
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
15-162 6.90e-07

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 48.68  E-value: 6.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  15 GVQRFAEQICMELVELRSDIVLLAPRD-------IKRATLPASFNVRFIGKKSGHYWEQIELPRYLKSLG-------SPL 80
Cdd:pfam13439   2 GVERYVLELARALARRGHEVTVVTPGGpgplaeeVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERpdvvhahSPF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  81 LLNLCSTAPAFYNNQ--IVTHHDVTYKRYKKSFSLK-FRALYSVLVPLMLRNSKALITVSNFSKSEILDYFSYVKENVYI 157
Cdd:pfam13439  82 PLGLAALAARLRLGIplVVTYHGLFPDYKRLGARLSpLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVPPEKIRV 161


                  ....*
gi 2310149060 158 VYNAV 162
Cdd:pfam13439 162 IPNGV 166
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
190-323 8.48e-07

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 50.09  E-value: 8.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 190 KNFHGMLESFSLVKrqhgGNVKLKVIGKSSASFSSQDFSKNL-VNDDVIFLGRIED--EKLISLYQNAIAFVFPSFYEGF 266
Cdd:PRK09922  195 KNVKELFDGLSQTT----GEWQLHIIGDGSDFEKCKAYSRELgIEQRIIWHGWQSQpwEVVQQKIKNVSALLLTSKFEGF 270

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310149060 267 GIPPLEAQACGCPVISSNKASMPE-VLNESV---IYfDPYNINEMADAMAKVISDEETRSK 323
Cdd:PRK09922  271 PMTLLEAMSYGIPCISSDCMSGPRdIIKPGLngeLY-TPGNIDEFVGKLNKVISGEVKYQH 330
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 256-337 1.62e-06

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 50.16  E-value: 1.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060  256 AFVFPSFYEGFGIPPLEAQACGCPVISSnKASMP----EVLNESVIyFDPYNINEMADAMAKVISDEETRSKLISSGFDN 331
Cdd:TIGR02468  574 VFINPAFIEPFGLTLIEAAAHGLPMVAT-KNGGPvdihRVLDNGLL-VDPHDQQAIADALLKLVADKQLWAECRQNGLKN 651


                   ....*.
gi 2310149060  332 VKKYSW 337
Cdd:TIGR02468  652 IHLFSW 657
PHA01633 PHA01633
putative glycosyl transferase group 1
 154-281 5.75e-06

putative glycosyl transferase group 1


Pssm-ID: 107050 [Multi-domain]  Cd Length: 335  Bit Score: 47.67  E-value: 5.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 154 NVYIVYNAvgQEFSPGMLEENDKD-----KYILaVSSPNYHKNFHGMLESFSLVkrqhggNVKLKVIGKSSASF--SSQD 226
Cdd:PHA01633  123 NFKIVENA--EKLVPQLKQKLDKDfpdtiKFGI-VSGLTKRKNMDLMLQVFNEL------NTKYPDIAKKIHFFviSHKQ 193

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2310149060 227 FSKNLVNDDVIFL---GRIEDEKLISLYqNAIAFVF-PSFYEGFGIPPLEAQACGCPVI 281
Cdd:PHA01633  194 FTQLEVPANVHFVaefGHNSREYIFAFY-GAMDFTIvPSGTEGFGMPVLESMAMGTPVI 251
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
255-346 1.16e-05

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 43.36  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 255 IAFVFPSFYEGFGIPPLEAQACGCPVISSNKASMPEVL--NESVIYFDpyNINEMADAMAKVISDEETRSKLISSGFDNV 332
Cdd:pfam13524   1 IVLNPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFepGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERV 78

                          90
                  ....*....|....*
gi 2310149060 333 -KKYSWKKSAQSVCD 346
Cdd:pfam13524  79 lAEHTYAHRAEQLLD 93
PLN02949 PLN02949
transferase, transferring glycosyl groups
 171-320 9.57e-05

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 43.96  E-value: 9.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 171 LEENDKDKYILAVSSPNYHKNFHGMLESFSLVKRQ---HGGNVKLKVIGKSSASF------SSQDFSKNL-VNDDVIFLG 240
Cdd:PLN02949  262 LERSEDPPYIISVAQFRPEKAHALQLEAFALALEKldaDVPRPKLQFVGSCRNKEdeerlqKLKDRAKELgLDGDVEFHK 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 241 RIEDEKLISLYQNAIAFVFPSFYEGFGIPPLEAQACGCPVISSNKAS--MPEVLNES--VIYFDPYNINEMADAMAKVIS 316
Cdd:PLN02949  342 NVSYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGpkMDIVLDEDgqQTGFLATTVEEYADAILEVLR 421


                  ....
gi 2310149060 317 DEET 320
Cdd:PLN02949  422 MRET 425
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 195-335 5.45e-04

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: 41.55  E-value: 5.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 195 MLESFSLVKRQhGGNVKLKVIGkssASFSSQDFS---KNLVN-----DDVIFLGR--IEDekliSLYQNAIaFVFPSFYE 264
Cdd:cd03813   311 FIRAFKLVRRA-MPDAEGWLIG---PEDEDPEYAqecKRLVAslgleNKVKFLGFqnIKE----YYPKLGL-LVLTSISE 381

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310149060 265 GFGIPPLEAQACGCPVISSNKASMPEVLNESVIYFD-------PYNINEMADAMAKVISDEETRSKLISSGFDNVKKY 335
Cdd:cd03813   382 GQPLVILEAMASGVPVVATDVGSCRELIYGADDALGqaglvvpPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKY 459
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 226-324 1.91e-03

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


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 39.75  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310149060 226 DFSKNLVNDDVIFLGRIEDEKLISLYQNAIAFVFPSFYEGFGIPP--LEAQACGCPVISSNKASMPEVL-NESVIYF--- 299
Cdd:cd04946   275 LAENKLENVKVNFTGEVSNKEVKQLYKENDVDVFVNVSESEGIPVsiMEAISFGIPVIATNVGGTREIVeNETNGLLldk 354

                          90       100
                  ....*....|....*....|....*
gi 2310149060 300 DPYNiNEMADAMAKVISDEETRSKL 324
Cdd:cd04946   355 DPTP-NEIVSSIMKFYLDGGDYKTM 378
GT3_GSY2-like cd03793
glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related ...
 258-284 2.96e-03

glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related to the GT3 family of glycosyltransferases, catalyzes the transfer of a glucose molecule from UDP-glucose to a terminal branch of a glycogen molecule, a rate-limit step of glycogen biosynthesis. GSY2, the member of this family in S. cerevisiae, has been shown to possess glycogen synthase activity.


Pssm-ID: 340824 [Multi-domain]  Cd Length: 590  Bit Score: 39.66  E-value: 2.96e-03
                          10        20
                  ....*....|....*....|....*..
gi 2310149060 258 VFPSFYEGFGIPPLEAQACGCPVISSN 284
Cdd:cd03793   479 VFPSYYEPWGYTPAECTVMGIPSITTN 505
 
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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