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Conserved domains on  [gi|147901175|ref|NP_795979|]
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glycosyltransferase 1 domain-containing protein 1 precursor [Mus musculus]

Protein Classification

Glyco4_Geo_Pelo superfamily-containing protein( domain architecture ID 1908431)

Glyco4_Geo_Pelo superfamily-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco4_Geo_Pelo super family cl45694
GPMC system family 4 glycosyltransferase; Members of this family are family 4 ...
 11-340 1.06e-66

GPMC system family 4 glycosyltransferase; Members of this family are family 4 glycosyltransferases of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family.


The actual alignment was detected with superfamily member NF038229:

Pssm-ID: 439530 [Multi-domain]  Cd Length: 338  Bit Score: 213.31  E-value: 1.06e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  11 PHTGNAVTAGRLRDHLEAAGHmCVLRDAFDFESPSEIANLIMDENLEAALALHLYRGGR----LLQGHSIPFGVIFGGTD 86
Cdd:NF038229  12 PVTGNAVTVRRIARHLEQLGH-EVRVLELDALDAAEILAALRQFRPDIIHAFHAYRSGRvwleLARALGIPYLVTLTGTD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  87 LNEDANhKEKKEVMGKVLEEARFAVAFTEAMKDTAQVQWPHATGKIFVQSQGIaTIPNANFNWntflqqSEIDQSADNLY 166
Cdd:NF038229  91 VNEALD-PDRRPETLRVLRGAAAIVAFNPLVRERLGQHLPPLAAKLVVIPQGV-ELGGEPFPL------RELGLFDSDEF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 167 IFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVGPEVDPVFTREVKERVRRAAGVRLIREMCQEDLHAVVKSCFALV 246
Cdd:NF038229 163 VFLLPAGLRPVKGVLFLLEMLAPLHAEDPRLRLAFAGPVLDEEYAAAFFAALARRPWARYLGEIPHDAMGALYRRADVVL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 247 NSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFSNPQEFIQLAKRLVSDPALEKEIVTNGREYVRTHHSW 326
Cdd:NF038229 243 NNSLFEGMANALLEAMALGRPVLARDIPGNRSVVRPGVTGLLYRDEAEFLRQARQLLQDPALRRRLGRPGRQLVRERYSP 322

                        330
                 ....*....|....
gi 147901175 327 QVERDTYQRLIRKL 340
Cdd:NF038229 323 EREAEAYLRLYRAV 336
 
Name Accession Description Interval E-value
Glyco4_Geo_Pelo NF038229
GPMC system family 4 glycosyltransferase; Members of this family are family 4 ...
 11-340 1.06e-66

GPMC system family 4 glycosyltransferase; Members of this family are family 4 glycosyltransferases of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family.


Pssm-ID: 439530 [Multi-domain]  Cd Length: 338  Bit Score: 213.31  E-value: 1.06e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  11 PHTGNAVTAGRLRDHLEAAGHmCVLRDAFDFESPSEIANLIMDENLEAALALHLYRGGR----LLQGHSIPFGVIFGGTD 86
Cdd:NF038229  12 PVTGNAVTVRRIARHLEQLGH-EVRVLELDALDAAEILAALRQFRPDIIHAFHAYRSGRvwleLARALGIPYLVTLTGTD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  87 LNEDANhKEKKEVMGKVLEEARFAVAFTEAMKDTAQVQWPHATGKIFVQSQGIaTIPNANFNWntflqqSEIDQSADNLY 166
Cdd:NF038229  91 VNEALD-PDRRPETLRVLRGAAAIVAFNPLVRERLGQHLPPLAAKLVVIPQGV-ELGGEPFPL------RELGLFDSDEF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 167 IFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVGPEVDPVFTREVKERVRRAAGVRLIREMCQEDLHAVVKSCFALV 246
Cdd:NF038229 163 VFLLPAGLRPVKGVLFLLEMLAPLHAEDPRLRLAFAGPVLDEEYAAAFFAALARRPWARYLGEIPHDAMGALYRRADVVL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 247 NSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFSNPQEFIQLAKRLVSDPALEKEIVTNGREYVRTHHSW 326
Cdd:NF038229 243 NNSLFEGMANALLEAMALGRPVLARDIPGNRSVVRPGVTGLLYRDEAEFLRQARQLLQDPALRRRLGRPGRQLVRERYSP 322

                        330
                 ....*....|....
gi 147901175 327 QVERDTYQRLIRKL 340
Cdd:NF038229 323 EREAEAYLRLYRAV 336
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-338 3.70e-29

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: 115.33  E-value: 3.70e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175   2 RLLFLA--VLRPHTGNAVTAGRLRDHLEAAGH--MCVLRDAFDFESPSEIANLIMDENLEAALALHLYR----------- 66
Cdd:cd03801    1 KILLLSpeLPPPVGGAERHVRELARALAARGHdvTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRllrelrpllrl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  67 -GGRLLQGHSIPFGVIF----------------GGTDLNEDANHKEKKEVMGKVLEEARFA---VAFTEAMKDTAQVQWP 126
Cdd:cd03801   81 rKFDVVHAHGLLAALLAallalllgaplvvtlhGAEPGRLLLLLAAERRLLARAEALLRRAdavIAVSEALRDELRALGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 127 HATGKIFVqsqgiatIPNA---NFNWNTFLQQSEIDQSAdnlYIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVG 203
Cdd:cd03801  161 IPPEKIVV-------IPNGvdlERFSPPLRRKLGIPPDR---PVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVG 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 204 PEvDPVFTREVKERVRRAAGVRLIREMCQEDLHAVVKSCFALVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHG 283
Cdd:cd03801  231 GD-GPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDG 309

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 147901175 284 VTGLLF--SNPQEFIQLAKRLVSDPALEKEIVTNGREYVRTHHSWQVERDTYQRLIR 338
Cdd:cd03801  310 EGGLVVppDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 235-340 4.31e-21

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 87.35  E-value: 4.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 235 LHAVVKSCFALVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLF--SNPQEFIQLAKRLVSDPALEKEI 312
Cdd:COG0438   14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVppGDPEALAEAILRLLEDPELRRRL 93

                         90       100
                 ....*....|....*....|....*...
gi 147901175 313 VTNGREYVRTHHSWQVERDTYQRLIRKL 340
Cdd:COG0438   94 GEAARERAEERFSWEAIAERLLALYEEL 121
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 166-318 2.42e-19

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: 83.48  E-value: 2.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  166 YIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVGPEvdpvftrEVKERVRRAAGVRLIREMCQ-------EDLHAV 238
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDG-------EEEKRLKKLAEKLGLGDNVIflgfvsdEDLPEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  239 VKSCFALVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLF--SNPQEFIQLAKRLVSDPALEKEIVTNG 316
Cdd:pfam00534  76 LKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVkpNNAEALAEAIDKLLEDEELRERLGENA 155


                  ..
gi 147901175  317 RE 318
Cdd:pfam00534 156 RK 157
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
176-327 9.79e-06

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 47.09  E-value: 9.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 176 PVKDPLYLVDAFSEWHQETPNVYMVIVGpevDPVFTR-----EVKERVRRAA---GVRLIREMCQ--EDLHAVVK-SCFA 244
Cdd:PRK15484 204 PDKGILLLMQAFEKLATAHSNLKLVVVG---DPTASSkgekaAYQKKVLEAAkriGDRCIMLGGQppEKMHNYYPlADLV 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 245 LVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFSNP---QEFIQLAKRLVSDPALEkEIVTNGREYVR 321
Cdd:PRK15484 281 VVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLAEPmtsDSIISDINRTLADPELT-QIAEQAKDFVF 359


                 ....*.
gi 147901175 322 THHSWQ 327
Cdd:PRK15484 360 SKYSWE 365
 
Name Accession Description Interval E-value
Glyco4_Geo_Pelo NF038229
GPMC system family 4 glycosyltransferase; Members of this family are family 4 ...
 11-340 1.06e-66

GPMC system family 4 glycosyltransferase; Members of this family are family 4 glycosyltransferases of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family.


Pssm-ID: 439530 [Multi-domain]  Cd Length: 338  Bit Score: 213.31  E-value: 1.06e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  11 PHTGNAVTAGRLRDHLEAAGHmCVLRDAFDFESPSEIANLIMDENLEAALALHLYRGGR----LLQGHSIPFGVIFGGTD 86
Cdd:NF038229  12 PVTGNAVTVRRIARHLEQLGH-EVRVLELDALDAAEILAALRQFRPDIIHAFHAYRSGRvwleLARALGIPYLVTLTGTD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  87 LNEDANhKEKKEVMGKVLEEARFAVAFTEAMKDTAQVQWPHATGKIFVQSQGIaTIPNANFNWntflqqSEIDQSADNLY 166
Cdd:NF038229  91 VNEALD-PDRRPETLRVLRGAAAIVAFNPLVRERLGQHLPPLAAKLVVIPQGV-ELGGEPFPL------RELGLFDSDEF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 167 IFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVGPEVDPVFTREVKERVRRAAGVRLIREMCQEDLHAVVKSCFALV 246
Cdd:NF038229 163 VFLLPAGLRPVKGVLFLLEMLAPLHAEDPRLRLAFAGPVLDEEYAAAFFAALARRPWARYLGEIPHDAMGALYRRADVVL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 247 NSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFSNPQEFIQLAKRLVSDPALEKEIVTNGREYVRTHHSW 326
Cdd:NF038229 243 NNSLFEGMANALLEAMALGRPVLARDIPGNRSVVRPGVTGLLYRDEAEFLRQARQLLQDPALRRRLGRPGRQLVRERYSP 322

                        330
                 ....*....|....
gi 147901175 327 QVERDTYQRLIRKL 340
Cdd:NF038229 323 EREAEAYLRLYRAV 336
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-338 3.70e-29

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: 115.33  E-value: 3.70e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175   2 RLLFLA--VLRPHTGNAVTAGRLRDHLEAAGH--MCVLRDAFDFESPSEIANLIMDENLEAALALHLYR----------- 66
Cdd:cd03801    1 KILLLSpeLPPPVGGAERHVRELARALAARGHdvTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRllrelrpllrl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  67 -GGRLLQGHSIPFGVIF----------------GGTDLNEDANHKEKKEVMGKVLEEARFA---VAFTEAMKDTAQVQWP 126
Cdd:cd03801   81 rKFDVVHAHGLLAALLAallalllgaplvvtlhGAEPGRLLLLLAAERRLLARAEALLRRAdavIAVSEALRDELRALGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 127 HATGKIFVqsqgiatIPNA---NFNWNTFLQQSEIDQSAdnlYIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVG 203
Cdd:cd03801  161 IPPEKIVV-------IPNGvdlERFSPPLRRKLGIPPDR---PVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVG 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 204 PEvDPVFTREVKERVRRAAGVRLIREMCQEDLHAVVKSCFALVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHG 283
Cdd:cd03801  231 GD-GPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDG 309

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 147901175 284 VTGLLF--SNPQEFIQLAKRLVSDPALEKEIVTNGREYVRTHHSWQVERDTYQRLIR 338
Cdd:cd03801  310 EGGLVVppDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 235-340 4.31e-21

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 87.35  E-value: 4.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 235 LHAVVKSCFALVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLF--SNPQEFIQLAKRLVSDPALEKEI 312
Cdd:COG0438   14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVppGDPEALAEAILRLLEDPELRRRL 93

                         90       100
                 ....*....|....*....|....*...
gi 147901175 313 VTNGREYVRTHHSWQVERDTYQRLIRKL 340
Cdd:COG0438   94 GEAARERAEERFSWEAIAERLLALYEEL 121
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 166-318 2.42e-19

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: 83.48  E-value: 2.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  166 YIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVGPEvdpvftrEVKERVRRAAGVRLIREMCQ-------EDLHAV 238
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDG-------EEEKRLKKLAEKLGLGDNVIflgfvsdEDLPEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  239 VKSCFALVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLF--SNPQEFIQLAKRLVSDPALEKEIVTNG 316
Cdd:pfam00534  76 LKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVkpNNAEALAEAIDKLLEDEELRERLGENA 155


                  ..
gi 147901175  317 RE 318
Cdd:pfam00534 156 RK 157
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 178-325 2.60e-17

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: 81.87  E-value: 2.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 178 KDPLYLVDAFSEWHQETPNVYMVIVGP-EVDPVFTREVKERVRRAA----GVRliremcqEDLHAVVKSCFALVNSSVSE 252
Cdd:cd03808  202 KGIDELIEAAKILKKKGPNVRFLLVGDgELENPSEILIEKLGLEGRieflGFR-------SDVPELLAESDVFVLPSYRE 274

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 147901175 253 GMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFsNPQEFIQLAK---RLVSDPALEKEIVTNGREYVRTHHS 325
Cdd:cd03808  275 GLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLV-PPGDVEALADaieKLIEDPELRKEMGEAARKRVEEKFD 349
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 133-336 2.74e-17

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: 81.59  E-value: 2.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 133 FVQSQGIA-----TIPNA----NFNwNTFLQQSEIDQS---ADNLYIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMV 200
Cdd:cd03807  147 FHQEQGYAknkivVIYNGidlfKLS-PDDASRARARRRlglAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLL 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 201 IVGPEVdpvfTREVKERVRRAAG----VRLIREmcQEDLHAVVKSCFALVNSSVSEGMSAAILEAMDLEVPVLARNIPGN 276
Cdd:cd03807  226 LVGRGP----ERPNLERLLLELGledrVHLLGE--RSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGA 299

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 147901175 277 SAVVEHGvTGLLFS--NPQEFIQLAKRLVSDPALEKEIVTNGREYVRTHHSWQVERDTYQRL 336
Cdd:cd03807  300 AELVDDG-TGFLVPagDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETL 360
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 76-331 3.36e-15

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: 75.88  E-value: 3.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  76 IPFGVIFGGTDLNEDANHKEKKEVMGKVLEEARFAVAFTEAMKDTAQVQWPHAtGKIFVqsqgiatIPNAnFNWNTFlqq 155
Cdd:cd03798  120 VPYVVTEHGSDINVFPPRSLLRKLLRWALRRAARVIAVSKALAEELVALGVPR-DRVDV-------IPNG-VDPARF--- 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 156 SEIDQSAD-NLYIFLIIC--GLRPVKDPLYLVDAFSEWHQETPNVYMVIVGPEVDPVFTREVKERVRRAAGVRLIREMCQ 232
Cdd:cd03798  188 QPEDRGLGlPLDAFVILFvgRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPH 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 233 EDLHAVVKSCFALVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFS--NPQEFIQLAKRLVSDPALEK 310
Cdd:cd03798  268 EQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPpgDADALAAALRRALAEPYLRE 347

                        250       260
                 ....*....|....*....|.
gi 147901175 311 EiVTNGREYVRTHHSWQVERD 331
Cdd:cd03798  348 L-GEAARARVAERFSWVKAAD 367
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
175-305 3.54e-15

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 71.39  E-value: 3.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  175 RPVKDPLYLVDAFSEWHQETPNVYMVIVGPEVDpvftREVKERVRR-AAGVRLIREMcqEDLHAVVKSCFALVNSSVSEG 253
Cdd:pfam13692  12 PNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPE----EELEELAAGlEDRVIFTGFV--EDLAELLAAADVFVLPSLYEG 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 147901175  254 MSAAILEAMDLEVPVLARNIPGNSAVVeHGVTGLLFS--NPQEFIQLAKRLVSD 305
Cdd:pfam13692  86 FGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPpgDPEALAEAILRLLED 138
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 131-310 2.61e-14

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: 72.78  E-value: 2.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 131 KIFVQSQGIA---------------TIPNAnFNWNTFLQQSEIDQSADNLYIFLIIC-G-LRPVKDPLYLVDAFSEWHQE 193
Cdd:cd03811  138 KIVCVSKGIKedlirlgpsppekieVIYNP-IDIDRIRALAKEPILNEPEDGPVILAvGrLDPQKGHDLLIEAFAKLRKK 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 194 TPNVYMVIVG--PEvdpvftREVKERVRRAAGvrlIREMC-----QEDLHAVVKSCFALVNSSVSEGMSAAILEAMDLEV 266
Cdd:cd03811  217 YPDVKLVILGdgPL------REELEKLAKELG---LAERViflgfQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGT 287

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 147901175 267 PVLARNIPGNSAVVEHGVTGLLF--SNPQEFIQLAKRLVSDPALEK 310
Cdd:cd03811  288 PVVSTDCPGPREILDDGENGLLVpdGDAAALAGILAALLQKKLDAA 333
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 134-327 1.29e-12

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: 67.77  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 134 VQSQGIATIPNANFNWNTFLQQSEIDQSADNL--YIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVG-------P 204
Cdd:cd03809  159 VPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLpePYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGgkgwedeE 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 205 EVDPVFTREVKERVRRAAGVRliremcQEDLHAVVKSCFALVNSSVSEGMSAAILEAMDLEVPVLARNIPgnsAVVEhgV 284
Cdd:cd03809  239 LLDLVKKLGLGGRVRFLGYVS------DEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNIS---VLPE--V 307

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 147901175 285 TG---LLFS--NPQEFIQLAKRLVSDPALEKEIVTNGREYVRtHHSWQ 327
Cdd:cd03809  308 AGdaaLYFDplDPESIADAILRLLEDPSLREELIRKGLERAK-KFSWE 354
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 174-327 5.17e-12

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: 66.11  E-value: 5.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 174 LRPVKDPLYLVDAFSEWHQETPNVYMVIVGPEVDPVFTREVKERVRRAAGVRLIRE------MCQEDLHAVVKSCFALVN 247
Cdd:cd03800  229 LDPRKGIDTLVRAFAQLPELRELANLVLVGGPSDDPLSMDREELAELAEELGLIDRvrfpgrVSRDDLPELYRAADVFVV 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 248 SSVSE--GMSAaiLEAMDLEVPVLARNIPGNSAVVEHGVTGLLFsNPQEFIQLA---KRLVSDPALEKEIVTNGREYVRT 322
Cdd:cd03800  309 PSLYEpfGLTA--IEAMACGTPVVATAVGGLQDIVRDGRTGLLV-DPHDPEALAaalRRLLDDPALWQRLSRAGLERARA 385


                 ....*
gi 147901175 323 HHSWQ 327
Cdd:cd03800  386 HYTWE 390
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 167-323 1.49e-11

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


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 64.65  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 167 IFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVG-PEVDPVFTREVKERVRRAAGV-RLIREMCQEDLHAVVkSCF- 243
Cdd:cd03792  199 YILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGhGAVDDPEGSVVYEEVMEYAGDdHDIHVLRLPPSDQEI-NALq 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 244 ----ALVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFSNPQEFIQLAKRLVSDPALEKEIVTNGREY 319
Cdd:cd03792  278 raatVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAVRILRLLTDPELRRKMGLAAREH 357


                 ....
gi 147901175 320 VRTH 323
Cdd:cd03792  358 VRDN 361
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 165-289 2.52e-11

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: 62.81  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 165 LYIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVGPEVDPVFTREVKERVRRAAGVRLIREMCQ-EDLHAVVKSCF 243
Cdd:cd01635  110 LADKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDdEVLELLLAAAD 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 147901175 244 ALVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLF 289
Cdd:cd01635  190 VFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 183-336 2.77e-11

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: 63.84  E-value: 2.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 183 LVDAFSEWHQEtPNVYMVIVG--PEvdpvfTREVKERVRR---AAGVRLIREMCQEDLHAVVKSCFALVNSSVSEGMSAA 257
Cdd:cd03817  219 LLRAFAELKKE-PNIKLVIVGdgPE-----REELKELARElglADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLV 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 258 ILEAMDLEVPVLARNIPGNSAVVEHGVTGLLF-SNPQEFIQLAKRLVSDPALEKEIVTNGREYVRTHHSWQVERDTYQRL 336
Cdd:cd03817  293 YLEAMAAGLPVVAAKDPAASELVEDGENGFLFePNDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAKSVEKLYEEV 372
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 139-318 4.28e-11

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: 63.14  E-value: 4.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 139 IATIPNA----NFNWNTFLQQSEIDQSADNLYIFLIICGLRPVKDPLYLVDAFSEWHQEtPNVYMVIVGPEvdpvftrEV 214
Cdd:cd03819  152 IRVIPNGvdtdRFPPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDE-PDFRLLVAGDG-------PE 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 215 KERVRRAAGVRLIREMCQ-----EDLHAVVKSCFALVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLF 289
Cdd:cd03819  224 RDEIRRLVERLGLRDRVTftgfrEDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLV 303

                        170       180       190
                 ....*....|....*....|....*....|.
gi 147901175 290 SNPQ--EFIQLAKRLVSDPALEKEIVTNGRE 318
Cdd:cd03819  304 PPGDaeALADAIRAAKLLPEAREKLQAAAAL 334
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 175-340 8.58e-10

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: 59.29  E-value: 8.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 175 RPVKDPLYLVDAFSEWHQETP-NVYMVIVGPEVDPVF--TRE--VKERVRRAAGVRLIREMCQedlhavVKSCFALVNSS 249
Cdd:cd04962  206 RPVKRIDDVVRVFARVRRKIPaKLLLVGDGPERVPAEelARElgVEDRVLFLGKQDDVEELLS------IADLFLLPSEK 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 250 VSEGMSAaiLEAMDLEVPVLARNIPGNSAVVEHGVTGLLFsNPQEFIQLAKRLVS---DPALEKEIVTNGREYVRTHHSW 326
Cdd:cd04962  280 ESFGLAA--LEAMACGVPVVSSNAGGIPEVVKHGETGFLS-DVGDVDAMAKSALSileDDELYNRMGRAARKRAAERFDP 356

                        170
                 ....*....|....
gi 147901175 327 QVERDTYQRLIRKL 340
Cdd:cd04962  357 ERIVPQYEAYYRRL 370
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 182-324 3.90e-09

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: 57.46  E-value: 3.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 182 YLVDAFSEWHQETPNVYMVIVGpevDPVFTREVKERVRRAAGVRLIREMCQEDLHAVVKSCFALVNSSV------SEGMS 255
Cdd:cd05844  206 VLIEAFRRLAARHPTARLVIAG---DGPLRPALQALAAALGRVRFLGALPHAEVQDWMRRAEIFCLPSVtaasgdSEGLG 282

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 147901175 256 AAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFSnPQEFIQLAKR---LVSDPALEKEIVTNGREYVRTHH 324
Cdd:cd05844  283 IVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVP-EGDVDALADAlqaLLADRALADRMGGAARAFVCEQF 353
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 166-323 4.16e-09

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: 57.28  E-value: 4.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 166 YIFLIICGLRPVKDPLYLVDAFsewhQETpNVYMVIVG--PEVDPVFTREVKERVRRaagVRLIREMCQEDLHAVVKSCF 243
Cdd:cd03795  192 KIFLFIGRLVYYKGLDYLIEAA----QYL-NYPIVIGGegPLKPDLEAQIELNLLDN---VKFLGRVDDEEKVIYLHLCD 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 244 ALVNSSV--SEGMSAAILEAMDLEVPVLARNIP-GNSAVVEHGVTGLLF--SNPQEFIQLAKRLVSDPALEKEIVTNGRE 318
Cdd:cd03795  264 VFVFPSVlrSEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVppKDPDALAEAIDKLLSDEELRESYGENAKK 343


                 ....*
gi 147901175 319 YVRTH 323
Cdd:cd03795  344 RFEEL 348
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 183-333 3.00e-08

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: 54.66  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 183 LVDAFSEwHQETPNVYMVIVGPEVDPvftREVKERVRRA--AGVRLIREMCQEDLHAVVKSC-FALVNSSVSEGMSAAI- 258
Cdd:cd03794  235 LLEAAER-LKRRPDIRFLFVGDGDEK---ERLKELAKARglDNVTFLGRVPKEEVPELLSAAdVGLVPLKDNPANRGSSp 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 259 ---LEAMDLEVPVLARNIPGNSAVVEHGVTGLLF--SNPQEFIQLAKRLVSDPALEKEIVTNGREYVRTHHSWQVERDTY 333
Cdd:cd03794  311 sklFEYMAAGKPILASDDGGSDLAVEINGCGLVVepGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRL 390
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 100-326 2.36e-07

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: 51.99  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 100 MGKVLEEArFAVAFTeAMKDTAQVQWPHATGKIFVqsqgiatIPNANF--NWNTFLQQSEIDQSADNLYIFLIICGLRPV 177
Cdd:cd03821  146 ERRNLNNA-ALVHFT-SEQEADELRRFGLEPPIAV-------IPNGVDipEFDPGLRDRRKHNGLEDRRIILFLGRIHPK 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 178 KDPLYLVDAFSEWHQETPNVYMVIVGPEvDPVFTREVKERVRRAAGVR-LIREMC-QEDLHAVVKS--CFALvnSSVSEG 253
Cdd:cd03821  217 KGLDLLIRAARKLAEQGRDWHLVIAGPD-DGAYPAFLQLQSSLGLGDRvTFTGPLyGEAKWALYASadLFVL--PSYSEN 293

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147901175 254 MSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFSNPQEFIQLAKRLVSDPALEKEIVTNGREYV--RTHHSW 326
Cdd:cd03821  294 FGNVVAEALACGLPVVITDKCGLSELVEAGCGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRARqvEENFSW 368
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 139-308 3.28e-07

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: 51.47  E-value: 3.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 139 IATIPNanfnWNTFLQQSEIDQSADNlyIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVG--PEvdpvftREVKE 216
Cdd:cd03820  161 VVVIPN----PLSFPSEEPSTNLKSK--RILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGdgPE------REELE 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 217 RvrraagvrLIREMCQED---LHAVVK---------SCFALvnSSVSEGMSAAILEAMDLEVPVLARNIP-GNSAVVEHG 283
Cdd:cd03820  229 K--------LIDKLGLEDrvkLLGPTKniaeeyansSIFVL--SSRYEGFPMVLLEAMAYGLPIISFDCPtGPSEIIEDG 298

                        170       180
                 ....*....|....*....|....*...
gi 147901175 284 VTGLLFsNPQEFIQLAK---RLVSDPAL 308
Cdd:cd03820  299 ENGLLV-PNGDVDALAEallRLMEDEEL 325
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
258-327 4.80e-07

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 47.21  E-value: 4.80e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175  258 ILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFSNPQEFIQLAKRLVSDPALEKEIVTNGREYVRTHHSWQ 327
Cdd:pfam13524  16 VFEAAACGAPLLTDRTPGLEELFEPGEEILLYRDPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHTYA 85
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 176-336 6.26e-07

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: 50.80  E-value: 6.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 176 PVKDPLYLVDAFSEWHQETPNVYMVIVGPEV-DPVFTREVKERVRRAAGVRLIREMCQEDLHAVVKSCFALVNSSVSEGM 254
Cdd:cd03813  304 PIKDVKTFIRAFKLVRRAMPDAEGWLIGPEDeDPEYAQECKRLVASLGLENKVKFLGFQNIKEYYPKLGLLVLTSISEGQ 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 255 SAAILEAMDLEVPVLARNIPGNSAVVE-----HGVTGLLF--SNPQEFIQLAKRLVSDPALEKEIVTNGREYVRTHHSWQ 327
Cdd:cd03813  384 PLVILEAMASGVPVVATDVGSCRELIYgaddaLGQAGLVVppADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLE 463


                 ....*....
gi 147901175 328 VERDTYQRL 336
Cdd:cd03813  464 GMIDSYRKL 472
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 163-320 7.67e-07

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: 50.14  E-value: 7.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 163 DNLYIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVGpevDPVFTREVKERVRRaagVRLIREMCQEDLHAVVKS- 241
Cdd:cd04951  186 NDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAG---DGPLRNELERLICN---LNLVDRVILLGQISNISEy 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 242 -----CFALvnSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFSNPQEFIQLAKRLVSDPALEKEIVTNG 316
Cdd:cd04951  260 ynaadLFVL--SSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHNYVVPVSDPQLLAEKIKEIFDMSDEERDILGNK 337


                 ....
gi 147901175 317 REYV 320
Cdd:cd04951  338 NEYI 341
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 233-326 1.00e-06

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: 49.99  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 233 EDLHAVVKSCFALVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFS--NPQEFIQLAKRLVSDPALEK 310
Cdd:cd03814  259 EELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEpgDAAAFAAALRALLEDPELRR 338

                         90
                 ....*....|....*.
gi 147901175 311 EIVTNGREYVRThHSW 326
Cdd:cd03814  339 RMAARARAEAER-YSW 353
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 139-340 1.08e-06

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: 50.02  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 139 IATIPNANfnwNTflqqsEIDQSADNLYI----------FLIICG----LRPVKDPLYLVDAFSEWHQEtPNVYMVIVGP 204
Cdd:cd03825  163 VVVIPNGI---DT-----EIFAPVDKAKArkrlgipqdkKVILFGaesvTKPRKGFDELIEALKLLATK-DDLLLVVFGK 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 205 evDPVFTREVKERVRraaGVRLIREmcQEDLHAVVKSCFALVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGV 284
Cdd:cd03825  234 --NDPQIVILPFDII---SLGYIDD--DEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGV 306

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 147901175 285 TGLLFSN--PQEFIQLAKRLVSDPALEKEIVTNGREYVRTHHSWQVERDTYQRLIRKL 340
Cdd:cd03825  307 TGYLVPPgdVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYKDL 364
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 246-299 3.00e-06

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


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 48.61  E-value: 3.00e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 147901175 246 VNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFSNPQEFIQLA 299
Cdd:cd04946  309 VNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLLLDKDPTPNEIV 362
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 215-340 3.19e-06

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: 48.44  E-value: 3.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 215 KERVRRAAGVRLIREMCQEDLHAVVKSCFALVNSSV-SEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFSNPQ 293
Cdd:cd03802  213 LQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDSVE 292

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 147901175 294 EFIQLAKRLvsdPALEKEIVtngREYVRTHHSWQVERDTYQRLIRKL 340
Cdd:cd03802  293 EMAEAIANI---DRIDRAAC---RRYAEDRFSAARMADRYEALYRKV 333
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
176-327 9.79e-06

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 47.09  E-value: 9.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 176 PVKDPLYLVDAFSEWHQETPNVYMVIVGpevDPVFTR-----EVKERVRRAA---GVRLIREMCQ--EDLHAVVK-SCFA 244
Cdd:PRK15484 204 PDKGILLLMQAFEKLATAHSNLKLVVVG---DPTASSkgekaAYQKKVLEAAkriGDRCIMLGGQppEKMHNYYPlADLV 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 245 LVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFSNP---QEFIQLAKRLVSDPALEkEIVTNGREYVR 321
Cdd:PRK15484 281 VVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLAEPmtsDSIISDINRTLADPELT-QIAEQAKDFVF 359


                 ....*.
gi 147901175 322 THHSWQ 327
Cdd:PRK15484 360 SKYSWE 365
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 131-304 1.74e-05

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: 46.14  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 131 KIFVQSQGIATIPNANFNWNTFlqqSEIDQSADNlYIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVGpevdpvf 210
Cdd:cd04949  130 ERFNKYPPIFTIPVGYVDQLDT---AESNHERKS-NKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYG------- 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 211 trEVKERvrraagvRLIREMcQEDLHA--VVK---------SCFA----LVNSSVSEGMSAAILEAMDLEVPVLARNIP- 274
Cdd:cd04949  199 --YGEER-------EKLKKL-IEELHLedNVFlkgyhsnldQEYQdaylSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKy 268

                        170       180       190
                 ....*....|....*....|....*....|.
gi 147901175 275 GNSAVVEHGVTGLLFsnPQEFIQ-LAKRLVS 304
Cdd:cd04949  269 GPSELIEDGENGYLI--EKNNIDaLADKIIE 297
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
287-346 1.20e-04

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


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 43.38  E-value: 1.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 287 LLFSNPQEFIQLAKRLVSDPALEKEIVTNGREYVRTHHswqverdTYQRLIRKLETNLED 346
Cdd:COG4641  249 LVFRDGEELAEKLRYLLADPEERRAIAEAGRRRVLAEH-------TYAHRARELLAILEE 301
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 163-338 3.23e-04

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: 41.99  E-value: 3.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 163 DNLYIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVGpEVDPVFTREVKERVRRAAGVRLIREM---------CQE 233
Cdd:cd03822  185 EGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAG-ELHPSLARYEGERYRKAAIEELGLQDhvdfhnnflPEE 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 234 DLHAVVKSC--FALVNSSVSEGMSAAILEAMDLEVPVLARNIPGNSAVVeHGVTGLL--FSNPQEFIQLAKRLVSDPALE 309
Cdd:cd03822  264 EVPRYISAAdvVVLPYLNTEQSSSGTLSYAIACGKPVISTPLRHAEELL-ADGRGVLvpFDDPSAIAEAILRLLEDDERR 342

                        170       180
                 ....*....|....*....|....*....
gi 147901175 310 KEIVTNGREYVRThHSWQVERDTYQRLIR 338
Cdd:cd03822  343 QAIAERAYAYARA-MTWESIADRYLRLFN 370
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 224-324 5.70e-04

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: 41.28  E-value: 5.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147901175 224 VRLIREMCQEDLHAVVKSCFALVNSSVS------EGMSAAILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFsnPQEFIQ 297
Cdd:cd03799  233 VKLLGWKPQEEIIEILDEADIFIAPSVTaadgdqDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLV--PERDAE 310

                         90       100       110
                 ....*....|....*....|....*....|.
gi 147901175 298 -LAKR---LVSDPALEKEIVTNGREYVRTHH 324
Cdd:cd03799  311 aIAEKltyLIEHPAIWPEMGKAGRARVEEEY 341
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 259-320 8.05e-04

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: 41.04  E-value: 8.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 147901175 259 LEAMDLEVPVLARNIPGNSAVVEHGVTGLLF-SNPQEFIQLAKRLVSDPALEKEIVTNGREYV 320
Cdd:cd03805  317 LEAMYAGKPVIACNSGGPLETVVEGVTGFLCePTPEAFAEAMLKLANDPDLADRMGAAGRKRV 379
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 258-329 7.70e-03

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: 37.69  E-value: 7.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147901175 258 ILEAMDLEVPVLARNIPGNSAVVEHGVTGLLFS--NPQEFIQLAKRLVSDPALEKEIVTNGREyvRTHHSWQVE 329
Cdd:cd03823  278 VREAIAAGLPVIASDLGGIAELIQPGVNGLLFApgDAEDLAAAMRRLLTDPALLERLRAGAEP--PRSTESQAE 349
DUF2007 pfam09413
Putative prokaryotic signal transducing protein; This is a family of putative prokaryotic ...
 13-62 8.81e-03

Putative prokaryotic signal transducing protein; This is a family of putative prokaryotic signal transducing proteins of Pii-type.


Pssm-ID: 430595  Cd Length: 66  Bit Score: 34.50  E-value: 8.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 147901175   13 TGNAVTAGRLRDHLEAAGHMCVLRDAFD-------FESPSEIanLIMDENLEAALAL 62
Cdd:pfam09413   7 TNDPVLASMIKALLEEAGIPCVIKDEFMsilegslGELPVRI--LVAEDDLERARRI 61
 
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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