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Conserved domains on  [gi|700302713|gb|AIU69532|]
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dolichol-P-glucose synthetase [Thermococcus eurythermalis]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135280)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  12691742|9445404|12200473|10508766
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 7-185 6.96e-60

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


:

Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 191.63  E-value: 6.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   7 VILPTMNEEKAVAKIISQIKETLEQmGISYEIIVV-DKSSDRTPEIARNLGAKV------VRQKRKGYGDAYLEGFAVAK 79
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEE-GYDYEIIVVdDGSTDGTAEIARELAARVprvrviRLSRNFGKGAAVRAGFKAAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  80 GKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVMGTRLKGEIKpGAMPWlHRYVGNPLLTKILNLFFKAGISDAHCGFRA 159
Cdd:cd04179   80 GDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGG-AGMPL-LRRLGSRLFNFLIRLLLGVRISDTQSGFRL 157

                        170       180
                 ....*....|....*....|....*...
gi 700302713 160 IKREALEKL--PLKCRGMEFASEMVIEA 185
Cdd:cd04179  158 FRREVLEALlsLLESNGFEFGLELLVGA 185
 
Name Accession Description Interval E-value
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 7-185 6.96e-60

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 191.63  E-value: 6.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   7 VILPTMNEEKAVAKIISQIKETLEQmGISYEIIVV-DKSSDRTPEIARNLGAKV------VRQKRKGYGDAYLEGFAVAK 79
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEE-GYDYEIIVVdDGSTDGTAEIARELAARVprvrviRLSRNFGKGAAVRAGFKAAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  80 GKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVMGTRLKGEIKpGAMPWlHRYVGNPLLTKILNLFFKAGISDAHCGFRA 159
Cdd:cd04179   80 GDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGG-AGMPL-LRRLGSRLFNFLIRLLLGVRISDTQSGFRL 157

                        170       180
                 ....*....|....*....|....*...
gi 700302713 160 IKREALEKL--PLKCRGMEFASEMVIEA 185
Cdd:cd04179  158 FRREVLEALlsLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 5-218 1.02e-47

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 161.02  E-value: 1.02e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   5 VSVILPTMNEEKAVAKIISQIketLEQMGISYEIIVVD-KSSDRTPEIARNLGAK------VVRQKRKGYGDAYLEGFAV 77
Cdd:COG0463    4 VSVVIPTYNEEEYLEEALESL---LAQTYPDFEIIVVDdGSTDGTAEILRELAAKdprirvIRLERNRGKGAARNAGLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  78 AKGKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVMGTRLKGEIKpgampWLHRYVGNPLLTkILNLFFKagISDAHCGF 157
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGE-----SDLRRLGSRLFN-LVRLLTN--LPDSTSGF 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 700302713 158 RAIKREALEKLPLKcRGMEFASEMvIEAAKAGLRIAEVPITYypRIGDSKLhSFRDGWRHL 218
Cdd:COG0463  153 RLFRREVLEELGFD-EGFLEDTEL-LRALRHGFRIAEVPVRY--RAGESKL-NLRDLLRLL 208
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 2-208 1.02e-37

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 135.98  E-value: 1.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   2 GVEVSVILPTMNEEKAVAKIISQIKETLEQMGiSYEIIVVDKSS-DRTPEIARNLGAK--------VVRQKRKGYGDAYL 72
Cdd:PLN02726   8 AMKYSIIVPTYNERLNIALIVYLIFKALQDVK-DFEIIVVDDGSpDGTQDVVKQLQKVygedrillRPRPGKLGLGTAYI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  73 EGFAVAKGKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVMGTR-LKGEikpGAMPW-----LHRYVGNPLLTKILNlff 146
Cdd:PLN02726  87 HGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRyVKGG---GVHGWdlrrkLTSRGANVLAQTLLW--- 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 700302713 147 kAGISDAHCGFRAIKREALEKLPLKC--RGMEFASEMVIEAAKAGLRIAEVPITYYPRI-GDSKL 208
Cdd:PLN02726 161 -PGVSDLTGSFRLYKRSALEDLVSSVvsKGYVFQMEIIVRASRKGYRIEEVPITFVDRVyGESKL 224
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-167 6.73e-33

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 120.58  E-value: 6.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713    6 SVILPTMNEEKAVAKIISQIketLEQMGISYEIIVVD-KSSDRTPEIARNL-----GAKVVRQ-KRKGYGDAYLEGFAVA 78
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESL---LNQTYPNFEIIVVDdGSTDGTVEIAEEYakkdpRVRVIRLpENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   79 KGKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVMGTRLKGEIKPGAMPWLHRYVGNPLLTKILNLFFKAGISDAHCGFR 158
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFA 157


                  ....*....
gi 700302713  159 AIKREALEK 167
Cdd:pfam00535 158 LYRREALEE 166
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 5-61 7.78e-08

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 52.51  E-value: 7.78e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 700302713    5 VSVILPTMNEEKavakiisQIKETLEQMGISY---EIIVVD-KSSDRTPEIARNLGAKVVR 61
Cdd:TIGR04283   1 LSIIIPVLNEAA-------TLPELLADLQALRgdaEVIVVDgGSTDGTVEIARSLGAKVIH 54
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
3-89 9.97e-03

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 37.47  E-value: 9.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   3 VEVSVILPTMNEEKAVAKIISQIKETLEQMGISYEIIVVDK-SSDRTpeiarnlgAKVVRQKRKGYGDAY-----LE--- 73
Cdd:NF038302   1 LDFTVAIPTYNGANRLPEVLERLRSQIGTESLSWEIIVVDNnSTDNT--------AQVVQEYQKNWPSPYplrycFEpqq 72

                         90       100
                 ....*....|....*....|....
gi 700302713  74 --GFA------VAKGKYIVMMDAD 89
Cdd:NF038302  73 gaAFArqraiqEAKGELIGFLDDD 96
 
Name Accession Description Interval E-value
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 7-185 6.96e-60

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 191.63  E-value: 6.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   7 VILPTMNEEKAVAKIISQIKETLEQmGISYEIIVV-DKSSDRTPEIARNLGAKV------VRQKRKGYGDAYLEGFAVAK 79
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEE-GYDYEIIVVdDGSTDGTAEIARELAARVprvrviRLSRNFGKGAAVRAGFKAAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  80 GKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVMGTRLKGEIKpGAMPWlHRYVGNPLLTKILNLFFKAGISDAHCGFRA 159
Cdd:cd04179   80 GDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGG-AGMPL-LRRLGSRLFNFLIRLLLGVRISDTQSGFRL 157

                        170       180
                 ....*....|....*....|....*...
gi 700302713 160 IKREALEKL--PLKCRGMEFASEMVIEA 185
Cdd:cd04179  158 FRREVLEALlsLLESNGFEFGLELLVGA 185
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 7-219 5.29e-51

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 170.02  E-value: 5.29e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   7 VILPTMNEEKAVAKIISQIKETLEqmGISYEIIVVDKSS-DRTPEIARNLGAK------VVRQKRKGYGDAYLEGFAVAK 79
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALK--GIDYEIIVVDDNSpDGTAEIVRELAKEyprvrlIVRPGKRGLGSAYIEGFKAAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  80 GKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVMGTRLKGEIKPGAMPWLHRyvgnpLLTKILNLFFK----AGISDAHC 155
Cdd:cd06442   79 GDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRK-----LISRGANLLARlllgRKVSDPTS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 700302713 156 GFRAIKREALEKLPLKCR--GMEFASEMVIEAAKAGLRIAEVPITYYPRI-GDSKLhSFRDGWRHLR 219
Cdd:cd06442  154 GFRAYRREVLEKLIDSLVskGYKFQLELLVRARRLGYRIVEVPITFVDREhGESKL-GGKEIVEYLK 219
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 5-218 1.02e-47

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 161.02  E-value: 1.02e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   5 VSVILPTMNEEKAVAKIISQIketLEQMGISYEIIVVD-KSSDRTPEIARNLGAK------VVRQKRKGYGDAYLEGFAV 77
Cdd:COG0463    4 VSVVIPTYNEEEYLEEALESL---LAQTYPDFEIIVVDdGSTDGTAEILRELAAKdprirvIRLERNRGKGAARNAGLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  78 AKGKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVMGTRLKGEIKpgampWLHRYVGNPLLTkILNLFFKagISDAHCGF 157
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGE-----SDLRRLGSRLFN-LVRLLTN--LPDSTSGF 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 700302713 158 RAIKREALEKLPLKcRGMEFASEMvIEAAKAGLRIAEVPITYypRIGDSKLhSFRDGWRHL 218
Cdd:COG0463  153 RLFRREVLEELGFD-EGFLEDTEL-LRALRHGFRIAEVPVRY--RAGESKL-NLRDLLRLL 208
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 2-208 1.02e-37

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 135.98  E-value: 1.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   2 GVEVSVILPTMNEEKAVAKIISQIKETLEQMGiSYEIIVVDKSS-DRTPEIARNLGAK--------VVRQKRKGYGDAYL 72
Cdd:PLN02726   8 AMKYSIIVPTYNERLNIALIVYLIFKALQDVK-DFEIIVVDDGSpDGTQDVVKQLQKVygedrillRPRPGKLGLGTAYI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  73 EGFAVAKGKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVMGTR-LKGEikpGAMPW-----LHRYVGNPLLTKILNlff 146
Cdd:PLN02726  87 HGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRyVKGG---GVHGWdlrrkLTSRGANVLAQTLLW--- 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 700302713 147 kAGISDAHCGFRAIKREALEKLPLKC--RGMEFASEMVIEAAKAGLRIAEVPITYYPRI-GDSKL 208
Cdd:PLN02726 161 -PGVSDLTGSFRLYKRSALEDLVSSVvsKGYVFQMEIIVRASRKGYRIEEVPITFVDRVyGESKL 224
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 7-207 2.34e-35

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 128.45  E-value: 2.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   7 VILPTMNEEKAVAKIISQIKETLEQM-GISYEIIVV-DKSSDRTPEIARNLGAK-------VVRQKRKGYGDAYLEGFAV 77
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYLEERpSFSYEIIVVdDGSKDGTAEVARKLARKnpalirvLTLPKNRGKGGAVRAGMLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  78 AKGKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVMGTRlkgeIKPGAMPWLHRYVGNPLLTKILNLF----FKAGISDA 153
Cdd:cd04188   81 ARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSR----AHLASAAVVKRSWLRNLLGRGFNFLvrllLGLGIKDT 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 700302713 154 HCGFRAIKREALEKLPLKCR--GMEFASEMVIEAAKAGLRIAEVPITYYPrIGDSK 207
Cdd:cd04188  157 QCGFKLFTRDAARRLFPRLHleRWAFDVELLVLARRLGYPIEEVPVRWVE-IPGSK 211
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-167 6.73e-33

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 120.58  E-value: 6.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713    6 SVILPTMNEEKAVAKIISQIketLEQMGISYEIIVVD-KSSDRTPEIARNL-----GAKVVRQ-KRKGYGDAYLEGFAVA 78
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESL---LNQTYPNFEIIVVDdGSTDGTVEIAEEYakkdpRVRVIRLpENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   79 KGKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVMGTRLKGEIKPGAMPWLHRYVGNPLLTKILNLFFKAGISDAHCGFR 158
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFA 157


                  ....*....
gi 700302713  159 AIKREALEK 167
Cdd:pfam00535 158 LYRREALEE 166
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 7-175 2.14e-24

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 98.32  E-value: 2.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   7 VILPTMNEEKAVAKIISQIKETLEQMGISYEIIVV-DKSSDRTPEIARNLGA-----KVVR-QKRKGYGDAYLEGFAVAK 79
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVdDGSTDRTLEILRELAArdprvKVIRlSRNFGQQAALLAGLDHAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  80 GKYIVMMDADGSYDPRDIPKFLEMLkNEDVDFVMGTRLKGEikpgaMPWLhRYVGNPLLTKILNLFFKAGISDAHCGFRA 159
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKW-EEGYDVVYGVRKNRK-----ESWL-KRLTSKLFYRLINKLSGVDIPDNGGDFRL 153

                        170
                 ....*....|....*.
gi 700302713 160 IKREALEKLpLKCRGM 175
Cdd:cd04187  154 MDRKVVDAL-LLLPER 168
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 1-195 4.59e-21

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 92.29  E-value: 4.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   1 MGVEVSVILPTMNEEKAVAKIISQIKETLEQmGISYEIIVVDK-SSDRTPEIARNLGAKVVRQK--------RKGYGDAY 71
Cdd:PRK13915  29 AGRTVSVVLPALNEEETVGKVVDSIRPLLME-PLVDELIVIDSgSTDATAERAAAAGARVVSREeilpelppRPGKGEAL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  72 LEGFAVAKGKYIVMMDAD-GSYDPRDIPKFLE-MLKNEDVDFVMG-----TRLKGEIKPGAMPWLHRYVGNPLltkiLNL 144
Cdd:PRK13915 108 WRSLAATTGDIVVFVDADlINFDPMFVPGLLGpLLTDPGVHLVKAfyrrpLRVSGGVDATGGGRVTELVARPL----LNL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 700302713 145 FFK--AGISDAHCGFRAIKREALEKLPLKC-RGMEFAseMVIEAA-KAGL-RIAEV 195
Cdd:PRK13915 184 LRPelAGFVQPLGGEYAGRRELLESLPFVPgYGVEIG--LLIDTLdRLGLdAIAQV 237
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 3-229 4.92e-19

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 86.74  E-value: 4.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   3 VEVSVILPTMNEEKAVAKIISQIKETLE-----QMGISYEIIVV-DKSSDRTPEIAR---------NLGAKVVR-QKRKG 66
Cdd:PTZ00260  70 VDLSIVIPAYNEEDRLPKMLKETIKYLEsrsrkDPKFKYEIIIVnDGSKDKTLKVAKdfwrqninpNIDIRLLSlLRNKG 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  67 YGDAYLEGFAVAKGKYIVMMDADGSYDPRDIPKFLE-MLKNEDVD--FVMGTR---LKGEIKPGAMPWlhRYVGNPLLTK 140
Cdd:PTZ00260 150 KGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDiMLKIEQNGlgIVFGSRnhlVDSDVVAKRKWY--RNILMYGFHF 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713 141 ILNLFFKAGISDAHCGFRAIKREALEKL--PLKCRGMEFASEMVIEAAKAGLRIAEVPITyYPRIGDSKLHSFRDGWRHL 218
Cdd:PTZ00260 228 IVNTICGTNLKDTQCGFKLFTRETARIIfpSLHLERWAFDIEIVMIAQKLNLPIAEVPVN-WTEVEGSKLNVISASIQMA 306

                        250
                 ....*....|.
gi 700302713 219 RLMLLYSPSYL 229
Cdd:PTZ00260 307 RDILLVRSFYL 317
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 7-115 7.73e-15

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 71.38  E-value: 7.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   7 VILPTMNEEKAVAKIISQIketLEQMGISYEIIVVD-KSSDRTPEIARNLGAK------VVRQKRKGYGDAYLEGFAVAK 79
Cdd:cd00761    1 VIIPAYNEEPYLERCLESL---LAQTYPNFEVIVVDdGSTDGTLEILEEYAKKdprvirVINEENQGLAAARNAGLKAAR 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 700302713  80 GKYIVMMDADGSYDPRDIPKFL-EMLKNEDVDFVMGT 115
Cdd:cd00761   78 GEYILFLDADDLLLPDWLERLVaELLADPEADAVGGP 114
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 5-237 1.03e-14

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 73.03  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   5 VSVILPTMNEEKAVAKIISQIKETLEQMGiSYEIIVVDK-SSDRTPEIARNLGA-----KVVRQKRKGYGDAYLEGFAVA 78
Cdd:cd02525    2 VSIIIPVRNEEKYIEELLESLLNQSYPKD-LIEIIVVDGgSTDGTREIVQEYAAkdpriRLIDNPKRIQSAGLNIGIRNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  79 KGKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVMgtrlkgeikpGAMPWLHRYVGNPLLTKILNLFFKAGISDAHCG-- 156
Cdd:cd02525   81 RGDIIIRVDAHAVYPKDYILELVEALKRTGADNVG----------GPMETIGESKFQKAIAVAQSSPLGSGGSAYRGGav 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713 157 ---------FRAIKREALEKLPLKC----RGMEfaSEMVIEAAKAGLRIAEVP---ITYYPRIGDSKL--HSFRDG-WRh 217
Cdd:cd02525  151 kigyvdtvhHGAYRREVFEKVGGFDeslvRNED--AELNYRLRKAGYKIWLSPdirVYYYPRSTLKKLarQYFRYGkWR- 227

                        250       260
                 ....*....|....*....|..
gi 700302713 218 LRLMLLY--SPSYLFLLPGLFL 237
Cdd:cd02525  228 ARTLRKHrkSLSLRHLLPLAFV 249
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 5-284 1.08e-14

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 74.01  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   5 VSVILPTMNEEKAVAKIISQIKEtLEQMGISYEIIVV-DKSSDRTPEIARNLGAK------VVRQKRKGYGDAYLEGFAV 77
Cdd:COG1215   31 VSVIIPAYNEEAVIEETLRSLLA-QDYPKEKLEVIVVdDGSTDETAEIARELAAEyprvrvIERPENGGKAAALNAGLKA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  78 AKGKYIVMMDADGSYDPRDIPKFLEMLKNEDVdfvmgtrlkgeikpgampwlhryvgnplltkilnlffkagisDAHCGF 157
Cdd:COG1215  110 ARGDIVVFLDADTVLDPDWLRRLVAAFADPGV------------------------------------------GASGAN 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713 158 RAIKREALEKLPLkcrgmeFASEMVIE-------AAKAGLRIAEVPityYPRIGDSKLHSFRDGWR--------HLRLML 222
Cdd:COG1215  148 LAFRREALEEVGG------FDEDTLGEdldlslrLLRAGYRIVYVP---DAVVYEEAPETLRALFRqrrrwargGLQLLL 218

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 700302713 223 LY----SPSYLFLLPGLFLVIIGFGLIAYAYNTDPLRMHTMILGSLLTIVGFQVINFGISGKVYAV 284
Cdd:COG1215  219 KHrpllRPRRLLLFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGL 284
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 5-110 1.22e-14

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 72.32  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   5 VSVILPTMNEEKavakiisQIKETLEQ-MGISYEIIVVDK-SSDRTPEIARNLGAKVVRQKRKGYGDAYLEGFAVAKGKY 82
Cdd:cd02511    2 LSVVIITKNEER-------NIERCLESvKWAVDEIIVVDSgSTDRTVEIAKEYGAKVYQRWWDGFGAQRNFALELATNDW 74

                         90       100
                 ....*....|....*....|....*...
gi 700302713  83 IVMMDADGSYDPRDIPKFLEMLKNEDVD 110
Cdd:cd02511   75 VLSLDADERLTPELADEILALLATDDYD 102
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 7-184 9.63e-14

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 68.79  E-value: 9.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   7 VILPTMNEEKAVAKIISQIketLEQMGISYEIIVV-DKSSDRTPEIARNLGAK-------VVRQKRKGYGDAYLEGFAVA 78
Cdd:cd06423    1 IIVPAYNEEAVIERTIESL---LALDYPKLEVIVVdDGSTDDTLEILEELAALyirrvlvVRDKENGGKAGALNAGLRHA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  79 KGKYIVMMDADGSYDPrDIPKFL--EMLKNEDVDFVMGtrlkgeikpgampwlHRYVGNP---LLTKILNLFFKAGISDA 153
Cdd:cd06423   78 KGDIVVVLDADTILEP-DALKRLvvPFFADPKVGAVQG---------------RVRVRNGsenLLTRLQAIEYLSIFRLG 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 700302713 154 HCGFR-------------AIKREALEKLplkcrgMEFASEMVIE 184
Cdd:cd06423  142 RRAQSalggvlvlsgafgAFRREALREV------GGWDEDTLTE 179
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 5-115 1.16e-11

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 64.14  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   5 VSVILPTMNEEKAVAKiisQIKETLEQmgiSY-----EIIVV-DKSSDRTPEIARNLGA---KVVRQK-RKGYGDAYLEG 74
Cdd:cd06439   31 VTIIIPAYNEEAVIEA---KLENLLAL---DYprdrlEIIVVsDGSTDGTAEIAREYADkgvKLLRFPeRRGKAAALNRA 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 700302713  75 FAVAKGKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVMGT 115
Cdd:cd06439  105 LALATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSGE 145
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 4-110 4.50e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 63.14  E-value: 4.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   4 EVSVILPTMNEEKAVAKII-SQIKETLEqmgiSYEIIVV-DKSSDRTPEIARNLGAK-----VVRQKRKGYGDAYLEGFA 76
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAFMeSLIAQTWT----ALEIIIVnDGSTDNSVEIAKHYAENyphvrLLHQANAGVSVARNTGLA 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 700302713  77 VAKGKYIVMMDADGSYDPRDIPKFLEMLKNEDVD 110
Cdd:PRK10073  83 VATGKYVAFPDADDVVYPTMYETLMTMALEDDLD 116
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-102 7.71e-11

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 60.78  E-value: 7.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   1 MGVEVSVILPTMNEEKAVAKIISQIketLEQMGISYEIIVVD-KSSDRTPEIARNL---GAKVVRQKR-KGYGDAYLEGF 75
Cdd:COG1216    1 MRPKVSVVIPTYNRPELLRRCLESL---LAQTYPPFEVIVVDnGSTDGTAELLAALafpRVRVIRNPEnLGFAAARNLGL 77

                         90       100
                 ....*....|....*....|....*..
gi 700302713  76 AVAKGKYIVMMDADGSYDPRDIPKFLE 102
Cdd:COG1216   78 RAAGGDYLLFLDDDTVVEPDWLERLLA 104
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 5-202 6.16e-10

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 58.92  E-value: 6.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713    5 VSVILPTMNEEKAVAKIISQIketLEQMGISYEIIV-VDKSSDRTPEIARNLGA-------KVVRQKRK----GYGDAYL 72
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAI---LAQPYPPVEVVVvVNPSDAETLDVAEEIAArfpdvrlRVIRNARLlgptGKSRGLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   73 EGFAVAKGKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVmgtrlkgeikpGAMPWLHRyvGNPLLTKILNLFFK-AGIS 151
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAV-----------GTPVFSLN--RSTMLSALGALEFAlRHLR 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 700302713  152 daHCGFRAIKRealeKLPLKCRGMEFASEMVIEAAKAG--------------LRIAEVPITYYPR 202
Cdd:pfam13641 148 --MMSLRLALG----VLPLSGAGSAIRREVLKELGLFDpffllgddkslgrrLRRHGWRVAYAPD 206
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 4-270 2.45e-09

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 57.82  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   4 EVSVILPTMNEEKAVAKIISQIKETLEQMGISYEIIVVDK-SSDRTPEI----ARNLGAKVVR---QKRKGYGDAYLEGF 75
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDgSSDNSAEMlveaAQAPDSHIVAillNRNYGQHSAIMAGF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  76 AVAKGKYIVMMDADGSYDPRDIPKFLEMlKNEDVDfVMGTRlkgeiKPGAMPWLHRYVGNPLLTKILNLFFKAGISDAHC 155
Cdd:PRK10714  87 SHVTGDLIITLDADLQNPPEEIPRLVAK-ADEGYD-VVGTV-----RQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGC 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713 156 GFRAIKREALEKLpLKCRgmEFASEMVIEAAKAGLRIAEVPITYYPR-IGDSKlHSFrdgwrhLRLM-LLYSpsylfLLP 233
Cdd:PRK10714 160 MLRAYRRHIVDAM-LHCH--ERSTFIPILANTFARRAIEIPVHHAEReFGDSK-YSF------MRLInLMYD-----LVT 224

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 700302713 234 GLflviigfgliayayNTDPLRMHTmILGSLLTIVGF 270
Cdd:PRK10714 225 CL--------------TTTPLRLLS-LLGSIIAIGGF 246
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 5-64 4.95e-09

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 56.04  E-value: 4.95e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 700302713   5 VSVILPTMNEEKAVAKIISQIketLEQMGISYEIIVVD-KSSDRTPEIARNLGAKVVRQKR 64
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASL---RRLNPLPLEIIVVDgGSTDGTVAIARSAGVVVISSPK 58
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 6-170 5.85e-09

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 55.24  E-value: 5.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   6 SVILPTMNEEKavakiisQIKET----LEQMGISYEIIVVD-KSSDRTPEIARNLG---AKVVRQKRKGYGDAYLEGFAV 77
Cdd:cd06433    1 SIITPTYNQAE-------TLEETidsvLSQTYPNIEYIVIDgGSTDGTVDIIKKYEdkiTYWISEPDKGIYDAMNKGIAL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  78 AKGKYIVMMDADGSYDPRDIPKFLEML-KNEDVDFVMG-TRLKGEIKPGAMPWLHRYvgnplltkILNLFFKAGISDAHC 155
Cdd:cd06433   74 ATGDIIGFLNSDDTLLPGALLAVVAAFaEHPEVDVVYGdVLLVDENGRVIGRRRPPP--------FLDKFLLYGMPICHQ 145

                        170
                 ....*....|....*
gi 700302713 156 GFrAIKREALEKLPL 170
Cdd:cd06433  146 AT-FFRRSLFEKYGG 159
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 5-61 7.78e-08

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 52.51  E-value: 7.78e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 700302713    5 VSVILPTMNEEKavakiisQIKETLEQMGISY---EIIVVD-KSSDRTPEIARNLGAKVVR 61
Cdd:TIGR04283   1 LSIIIPVLNEAA-------TLPELLADLQALRgdaEVIVVDgGSTDGTVEIARSLGAKVIH 54
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 5-112 4.83e-07

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 50.39  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   5 VSVILPTMNEEKAVAKIISQIKEtleqmgISY-----EIIVVDKSSDRTPEIARNLGAK----------VVRQKRKGY-G 68
Cdd:cd06437    3 VTVQLPVFNEKYVVERLIEAACA------LDYpkdrlEIQVLDDSTDETVRLAREIVEEyaaqgvnikhVRRADRTGYkA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 700302713  69 DAYLEGFAVAKGKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFV 112
Cdd:cd06437   77 GALAEGMKVAKGEYVAIFDADFVPPPDFLQKTPPYFADPKLGFV 120
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 7-172 4.92e-07

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 49.52  E-value: 4.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   7 VILPTMNEEKAVAKIISQIKEtLEQMGISYEIIVV-DKSSDRTPEIARNLGAKVVR---QKRKGYGDAYLEGF---AVAK 79
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKA-QDYPRELYRIFVVaDNCTDDTAQVARAAGATVLErhdPERRGKGYALDFGFrhlLNLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  80 GKY--IVMMDADGSYDprdiPKFLEMLkneDVDFVMGTR-LKGE--IKPGAMPWLHRYVGNPLLtkILNLFFKAGISDAH 154
Cdd:cd06438   80 DDPdaVVVFDADNLVD----PNALEEL---NARFAAGARvVQAYynSKNPDDSWITRLYAFAFL--VFNRLRPLGRSNLG 150

                        170       180
                 ....*....|....*....|....*
gi 700302713 155 C-------GFrAIKREALEKLPLKC 172
Cdd:cd06438  151 LscqlggtGM-CFPWAVLRQAPWAA 174
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-114 3.13e-06

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 46.78  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   7 VILPTMNEEkavakiiSQIKETLE----QMGISYEIIVVD-KSSDRTPEIARNLGAKVVR---QKRKGYGDAYLEGFAVA 78
Cdd:cd04186    1 IIIVNYNSL-------EYLKACLDsllaQTYPDFEVIVVDnASTDGSVELLRELFPEVRLirnGENLGFGAGNNQGIREA 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 700302713  79 KGKYIVMMDADGSYDPRDIPKFLE-MLKNEDVDFVMG 114
Cdd:cd04186   74 KGDYVLLLNPDTVVEPGALLELLDaAEQDPDVGIVGP 110
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 7-129 8.10e-05

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 43.14  E-value: 8.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   7 VILPTMNEEKAVAKIISQIKETLEQMGIsyeIIVVDKSSDRTPEIAR----NLGAKVVRQK----RKGYGDA------YL 72
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRNKPNFLV---LVIDDASDDDTAGIVRlaitDSRVHLLRRHlpnaRTGKGDAlnaaydQI 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 700302713  73 EGFAVAKG----KYIVM-MDADGSYDPRdipkFLEMLK--NEDVDfVMGTRLKGEIKPGAMPWL 129
Cdd:cd06436   78 RQILIEEGadpeRVIIAvIDADGRLDPN----ALEAVApyFSDPR-VAGTQSRVRMYNRHKNLL 136
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 4-116 5.68e-04

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 41.09  E-value: 5.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   4 EVSVILPTMNE-----EKAVAKIISQIKetleqmgisYEIIVVDKSSDRTP-----EIARNLGAKVVRQKRKGYGDAYLE 73
Cdd:cd06434    1 DVTVIIPVYDEdpdvfRECLRSILRQKP---------LEIIVVTDGDDEPYlsilsQTVKYGGIFVITVPHPGKRRALAE 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 700302713  74 GFAVAKGKYIVMMDADGSYDPRDIPKFLEMLKNEDVDFVmGTR 116
Cdd:cd06434   72 GIRHVTTDIVVLLDSDTVWPPNALPEMLKPFEDPKVGGV-GTN 113
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 6-88 7.31e-04

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 41.04  E-value: 7.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   6 SVILPTMNEEKAVakIISQIKETLEQMGISY--EIIVVDKSSDRtPEIARNL---------GAKVVR-QKRKGYGDAYLE 73
Cdd:cd02510    1 SVIIIFHNEALST--LLRTVHSVINRTPPELlkEIILVDDFSDK-PELKLLLeeyykkylpKVKVLRlKKREGLIRARIA 77

                         90
                 ....*....|....*
gi 700302713  74 GFAVAKGKYIVMMDA 88
Cdd:cd02510   78 GARAATGDVLVFLDS 92
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-89 1.17e-03

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 39.92  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   6 SVILPTMNEEKavaKIISQIKETLEQMGISYEIIVV-DKSSDRTPEIARNLGAK-------VVRQKRKGYGDAYLEGFAV 77
Cdd:cd04196    1 AVLMATYNGEK---YLREQLDSILAQTYKNDELIISdDGSTDGTVEIIKEYIDKdpfiiilIRNGKNLGVARNFESLLQA 77

                         90
                 ....*....|..
gi 700302713  78 AKGKYIVMMDAD 89
Cdd:cd04196   78 ADGDYVFFCDQD 89
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-89 3.65e-03

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 38.42  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   7 VILPTMNEEKAVAKIISQIkETLEQMGISYEIIVV-DKSSDRTPEIA------RNLGAKVVRQKR---KGYGDAYLEGFA 76
Cdd:cd04192    1 VVIAARNEAENLPRLLQSL-SALDYPKEKFEVILVdDHSTDGTVQILefaaakPNFQLKILNNSRvsiSGKKNALTTAIK 79

                         90
                 ....*....|...
gi 700302713  77 VAKGKYIVMMDAD 89
Cdd:cd04192   80 AAKGDWIVTTDAD 92
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 18-110 5.15e-03

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 38.03  E-value: 5.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713  18 VAKIISQIKETLEQmgiSYEIIVVDKSSDRTPEIA---RNLGAKVVRQKR-KGYGDAYLEGFAVAKGK---YIVMMDADG 90
Cdd:cd02526   10 LSKLKELLAALAEQ---VDKVVVVDNSSGNDIELRlrlNSEKIELIHLGEnLGIAKALNIGIKAALENgadYVLLFDQDS 86

                         90       100
                 ....*....|....*....|
gi 700302713  91 SYDPRDIPKFLEMLKNEDVD 110
Cdd:cd02526   87 VPPPDMVEKLLAYKILSDKN 106
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
3-89 9.97e-03

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 37.47  E-value: 9.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700302713   3 VEVSVILPTMNEEKAVAKIISQIKETLEQMGISYEIIVVDK-SSDRTpeiarnlgAKVVRQKRKGYGDAY-----LE--- 73
Cdd:NF038302   1 LDFTVAIPTYNGANRLPEVLERLRSQIGTESLSWEIIVVDNnSTDNT--------AQVVQEYQKNWPSPYplrycFEpqq 72

                         90       100
                 ....*....|....*....|....
gi 700302713  74 --GFA------VAKGKYIVMMDAD 89
Cdd:NF038302  73 gaAFArqraiqEAKGELIGFLDDD 96
 
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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