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Conserved domains on  [gi|1810224639|gb|QIB54489|]
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glycosyltransferase family 2 protein [Blautia producta ATCC 27340 = DSM 2950]

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 ...
 7-170 4.39e-44

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: 146.56  E-value: 4.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   7 LVIPAYNEQANIGNVLRKIQEI-NTDHWLDVVVIDDGSSDNTYGEALAC-----KVTVIRQVYNMGYGAALQTGYKYAVE 80
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVlEEGYDYEIIVVDDGSTDGTAEIARELaarvpRVRVIRLSRNFGKGAAVRAGFKAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  81 hgyEYLLQMDADGQHDVRNLERIYReltAIQERQPDIVIGSRFLSASQtYPVSKIRLVAIRMFRFVIRRLTGYTLTDPTS 160
Cdd:cd04179    81 ---DIVVTMDADLQHPPEDIPKLLE---KLLEGGADVVIGSRFVRGGG-AGMPLLRRLGSRLFNFLIRLLLGVRISDTQS 153

                         170
                  ....*....|
gi 1810224639 161 GLQGLNRRAF 170
Cdd:cd04179   154 GFRLFRREVL 163
 
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 ...
 7-170 4.39e-44

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: 146.56  E-value: 4.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   7 LVIPAYNEQANIGNVLRKIQEI-NTDHWLDVVVIDDGSSDNTYGEALAC-----KVTVIRQVYNMGYGAALQTGYKYAVE 80
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVlEEGYDYEIIVVDDGSTDGTAEIARELaarvpRVRVIRLSRNFGKGAAVRAGFKAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  81 hgyEYLLQMDADGQHDVRNLERIYReltAIQERQPDIVIGSRFLSASQtYPVSKIRLVAIRMFRFVIRRLTGYTLTDPTS 160
Cdd:cd04179    81 ---DIVVTMDADLQHPPEDIPKLLE---KLLEGGADVVIGSRFVRGGG-AGMPLLRRLGSRLFNFLIRLLLGVRISDTQS 153

                         170
                  ....*....|
gi 1810224639 161 GLQGLNRRAF 170
Cdd:cd04179   154 GFRLFRREVL 163
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 4-222 4.70e-34

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 121.35  E-value: 4.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   4 KVVLVIPAYNEQANIGNVLRKIQEINTDHWlDVVVIDDGSSDNTYG--EALACK---VTVIRQVYNMGYGAALQTGYKYA 78
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYPDF-EIIVVDDGSTDGTAEilRELAAKdprIRVIRLERNRGKGAARNAGLAAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  79 vehGYEYLLQMDADGQHDVRNLERIYReltAIQERQPDIVIGSRFLSASQtypvSKIRLVAIRMFRFvIRRLTGytLTDP 158
Cdd:COG0463    82 ---RGDYIAFLDADDQLDPEKLEELVA---ALEEGPADLVYGSRLIREGE----SDLRRLGSRLFNL-VRLLTN--LPDS 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1810224639 159 TSGLQGLNRRAFscyaSYSNFDIKYPDLNMILQMLLRGYHITEIPAIMHIRTEGIAMHSGAAHA 222
Cdd:COG0463   149 TSGFRLFRREVL----EELGFDEGFLEDTELLRALRHGFRIAEVPVRYRAGESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-172 8.68e-23

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: 90.92  E-value: 8.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   7 LVIPAYNEQANIGNVLRKIQEINTDHWlDVVVIDDGSSDNTYGEALA-----CKVTVIRQVYNMGYGAALQTGYKYAveh 81
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPNF-EIIVVDDGSTDGTVEIAEEyakkdPRVRVIRLPENRGKAGARNAGLRAA--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  82 GYEYLLQMDADGQHDVRNLERIYReltAIQERQPDIVIGSRFLSASQTYPVSK-IRLVAIRMFRFVIRRLTGYTLTDPTS 160
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVE---ALEEDGADVVVGSRYVIFGETGEYRRaSRITLSRLPFFLGLRLLGLNLPFLIG 154

                         170
                  ....*....|..
gi 1810224639 161 GLQGLNRRAFSC 172
Cdd:pfam00535 155 GFALYRREALEE 166
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 7-169 1.05e-12

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 66.33  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   7 LVIPAYNEQANIGNVL-------RKIQEINTDHWLDVVVIDDGSSDNTYGEALA---------CKVTVIRQVYNMGYGAA 70
Cdd:PTZ00260   74 IVIPAYNEEDRLPKMLketikylESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDfwrqninpnIDIRLLSLLRNKGKGGA 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  71 LQTGYKYAVEhgyEYLLQMDADGQHDVRNLERIYRELTAIQERQPDIVIGSRFLSAsQTYPVSK---IRLVAIRMFRFVI 147
Cdd:PTZ00260  154 VRIGMLASRG---KYILMVDADGATDIDDFDKLEDIMLKIEQNGLGIVFGSRNHLV-DSDVVAKrkwYRNILMYGFHFIV 229

                         170       180
                  ....*....|....*....|..
gi 1810224639 148 RRLTGYTLTDPTSGLQGLNRRA 169
Cdd:PTZ00260  230 NTICGTNLKDTQCGFKLFTRET 251
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 8-74 3.25e-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: 3.25e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1810224639   8 VIPAYNEQANIGNVLRKIQEINTDHwlDVVVIDDGSSDNTYGEALACKVTVI-------RQvynMGYGAALQTG 74
Cdd:TIGR04283   4 IIPVLNEAATLPELLADLQALRGDA--EVIVVDGGSTDGTVEIARSLGAKVIhspkgraRQ---MNAGAALAKG 72
 
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 ...
 7-170 4.39e-44

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: 146.56  E-value: 4.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   7 LVIPAYNEQANIGNVLRKIQEI-NTDHWLDVVVIDDGSSDNTYGEALAC-----KVTVIRQVYNMGYGAALQTGYKYAVE 80
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVlEEGYDYEIIVVDDGSTDGTAEIARELaarvpRVRVIRLSRNFGKGAAVRAGFKAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  81 hgyEYLLQMDADGQHDVRNLERIYReltAIQERQPDIVIGSRFLSASQtYPVSKIRLVAIRMFRFVIRRLTGYTLTDPTS 160
Cdd:cd04179    81 ---DIVVTMDADLQHPPEDIPKLLE---KLLEGGADVVIGSRFVRGGG-AGMPLLRRLGSRLFNFLIRLLLGVRISDTQS 153

                         170
                  ....*....|
gi 1810224639 161 GLQGLNRRAF 170
Cdd:cd04179   154 GFRLFRREVL 163
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 4-222 4.70e-34

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 121.35  E-value: 4.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   4 KVVLVIPAYNEQANIGNVLRKIQEINTDHWlDVVVIDDGSSDNTYG--EALACK---VTVIRQVYNMGYGAALQTGYKYA 78
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYPDF-EIIVVDDGSTDGTAEilRELAAKdprIRVIRLERNRGKGAARNAGLAAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  79 vehGYEYLLQMDADGQHDVRNLERIYReltAIQERQPDIVIGSRFLSASQtypvSKIRLVAIRMFRFvIRRLTGytLTDP 158
Cdd:COG0463    82 ---RGDYIAFLDADDQLDPEKLEELVA---ALEEGPADLVYGSRLIREGE----SDLRRLGSRLFNL-VRLLTN--LPDS 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1810224639 159 TSGLQGLNRRAFscyaSYSNFDIKYPDLNMILQMLLRGYHITEIPAIMHIRTEGIAMHSGAAHA 222
Cdd:COG0463   149 TSGFRLFRREVL----EELGFDEGFLEDTELLRALRHGFRIAEVPVRYRAGESKLNLRDLLRLL 208
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 7-212 3.89e-29

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: 109.16  E-value: 3.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   7 LVIPAYNEQANIGNVLRKIQEINTDHWLDVVVIDDGSSDNTYG--EALAC---KVTVIRQVYNMGYGAALQTGYKYAVEh 81
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGIDYEIIVVDDNSPDGTAEivRELAKeypRVRLIVRPGKRGLGSAYIEGFKAARG- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  82 gyEYLLQMDADGQHDVRNLERIYReltAIQERQPDIVIGSRFLSASQTYPVSKIRLVAIRMFRFVIRRLTGYTLTDPTSG 161
Cdd:cd06442    80 --DVIVVMDADLSHPPEYIPELLE---AQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1810224639 162 LQGLNRRAFScyASYSNFDIKYPD--LNMILQMLLRGYHITEIPAIMHIRTEG 212
Cdd:cd06442   155 FRAYRREVLE--KLIDSLVSKGYKfqLELLVRARRLGYRIVEVPITFVDREHG 205
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 7-203 4.02e-24

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: 95.71  E-value: 4.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   7 LVIPAYNEQANIGNVLRKI----QEINTDHWlDVVVIDDGSSDNT------YGEALACKVTVIRQVYNMGYGAALQTGYK 76
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAveylEERPSFSY-EIIVVDDGSKDGTaevarkLARKNPALIRVLTLPKNRGKGGAVRAGML 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  77 YAVEhgyEYLLQMDADGQHDVRNLERIyreLTAIQERQPDIVIGSRFLSASQTYPV-SKIRLVAIRMFRFVIRRLTGYTL 155
Cdd:cd04188    80 AARG---DYILFADADLATPFEELEKL---EEALKTSGYDIAIGSRAHLASAAVVKrSWLRNLLGRGFNFLVRLLLGLGI 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1810224639 156 TDPTSGLQGLNRRAFScyASYSN-------FDIkypDLNMILQMLlrGYHITEIP 203
Cdd:cd04188   154 KDTQCGFKLFTRDAAR--RLFPRlhlerwaFDV---ELLVLARRL--GYPIEEVP 201
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-172 8.68e-23

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: 90.92  E-value: 8.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   7 LVIPAYNEQANIGNVLRKIQEINTDHWlDVVVIDDGSSDNTYGEALA-----CKVTVIRQVYNMGYGAALQTGYKYAveh 81
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPNF-EIIVVDDGSTDGTVEIAEEyakkdPRVRVIRLPENRGKAGARNAGLRAA--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  82 GYEYLLQMDADGQHDVRNLERIYReltAIQERQPDIVIGSRFLSASQTYPVSK-IRLVAIRMFRFVIRRLTGYTLTDPTS 160
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVE---ALEEDGADVVVGSRYVIFGETGEYRRaSRITLSRLPFFLGLRLLGLNLPFLIG 154

                         170
                  ....*....|..
gi 1810224639 161 GLQGLNRRAFSC 172
Cdd:pfam00535 155 GFALYRREALEE 166
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 7-169 4.90e-20

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: 84.07  E-value: 4.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   7 LVIPAYNEQANIGNVLRKIQEI--NTDHWLDVVVIDDGSSDNTYGEALAC-----KVTVIRQVYNMGYGAALQTGYKYAV 79
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVleSLGYDYEIIFVDDGSTDRTLEILRELaardpRVKVIRLSRNFGQQAALLAGLDHAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  80 ehGyEYLLQMDADGQHDVRNLERIYRELtaiqERQPDIVIGSRflsasQTYPVSKIRLVAIRMFRFVIRRLTGYTLTDPT 159
Cdd:cd04187    81 --G-DAVITMDADLQDPPELIPEMLAKW----EEGYDVVYGVR-----KNRKESWLKRLTSKLFYRLINKLSGVDIPDNG 148

                         170
                  ....*....|
gi 1810224639 160 SGLQGLNRRA 169
Cdd:cd04187   149 GDFRLMDRKV 158
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 4-107 8.77e-15

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: 72.08  E-value: 8.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   4 KVVLVIPAYNEQANIGNVLRKIQEIN-TDHWLDVVVIDDGSSDNTYGEALA-----CKVTVIRQVYNMGYGAALQTGYKY 77
Cdd:COG1215    30 RVSVIIPAYNEEAVIEETLRSLLAQDyPKEKLEVIVVDDGSTDETAEIARElaaeyPRVRVIERPENGGKAAALNAGLKA 109

                          90       100       110
                  ....*....|....*....|....*....|
gi 1810224639  78 AvehGYEYLLQMDADGQHDVRNLERIYREL 107
Cdd:COG1215   110 A---RGDIVVFLDADTVLDPDWLRRLVAAF 136
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 8-120 1.97e-13

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: 65.99  E-value: 1.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   8 VIPAYNEQANIGNVLRKIQEiNTDHWLDVVVIDDGSSDNTYGEALACKVTVIRQVY-----NMGYGAALQTGYKYAvehG 82
Cdd:cd00761     2 IIPAYNEEPYLERCLESLLA-QTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRvineeNQGLAAARNAGLKAA---R 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1810224639  83 YEYLLQMDADGQHDVRNLERIYRELTaiQERQPDIVIG 120
Cdd:cd00761    78 GEYILFLDADDLLLPDWLERLVAELL--ADPEADAVGG 113
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 7-169 1.05e-12

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 66.33  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   7 LVIPAYNEQANIGNVL-------RKIQEINTDHWLDVVVIDDGSSDNTYGEALA---------CKVTVIRQVYNMGYGAA 70
Cdd:PTZ00260   74 IVIPAYNEEDRLPKMLketikylESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDfwrqninpnIDIRLLSLLRNKGKGGA 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  71 LQTGYKYAVEhgyEYLLQMDADGQHDVRNLERIYRELTAIQERQPDIVIGSRFLSAsQTYPVSK---IRLVAIRMFRFVI 147
Cdd:PTZ00260  154 VRIGMLASRG---KYILMVDADGATDIDDFDKLEDIMLKIEQNGLGIVFGSRNHLV-DSDVVAKrkwYRNILMYGFHFIV 229

                         170       180
                  ....*....|....*....|..
gi 1810224639 148 RRLTGYTLTDPTSGLQGLNRRA 169
Cdd:PTZ00260  230 NTICGTNLKDTQCGFKLFTRET 251
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 4-149 1.56e-11

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: 61.92  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   4 KVVLVIPAYNEQANIGNVLRKIQEInTDhwlDVVVIDDGSSDNTYGEALACKVTVIrQVYNMGYGAALQtgykYAVEH-G 82
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVKWA-VD---EIIVVDSGSTDRTVEIAKEYGAKVY-QRWWDGFGAQRN----FALELaT 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1810224639  83 YEYLLQMDAD---GQHDVRNLERIYRELT--AIQERQPDIVIGsRFLSASQTYPVSKIRLVAIRMFRFVIRR 149
Cdd:cd02511    72 NDWVLSLDADerlTPELADEILALLATDDydGYYVPRRNFFLG-RWIRHGGWYPDRQLRLFRRGKARFEDGR 142
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 7-92 1.91e-11

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: 60.70  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   7 LVIPAYNEQANIGNVLRKIQEINTDHwLDVVVIDDGSSDNT------YGEALACKVTVIRQVYNMGYGAALQTGYKYAVe 80
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPK-LEVIVVDDGSTDDTleileeLAALYIRRVLVVRDKENGGKAGALNAGLRHAK- 78

                          90
                  ....*....|..
gi 1810224639  81 hgYEYLLQMDAD 92
Cdd:cd06423    79 --GDIVVVLDAD 88
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 4-104 1.41e-10

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: 59.52  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   4 KVVLVIPAYNEQANIGnvlRKIQEINTDHW----LDVVVIDDGSSDNTY---GEALACKVTVIRQVYNMGYGAALQTGYK 76
Cdd:cd06439    30 TVTIIIPAYNEEAVIE---AKLENLLALDYprdrLEIIVVSDGSTDGTAeiaREYADKGVKLLRFPERRGKAAALNRALA 106

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1810224639  77 YAVEhgyEYLLQMDADGQHD---VRNLERIY 104
Cdd:cd06439   107 LATG---EIVVFTDANALLDpdaLRLLVRHF 134
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-92 3.02e-10

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 58.08  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   1 MDHKVVLVIPAYNEQANIGNVLRKIQEiNTDHWLDVVVIDDGSSDNTYGEALACK---VTVIRQVYNMGYGAALQTGYKY 77
Cdd:COG1216     1 MRPKVSVVIPTYNRPELLRRCLESLLA-QTYPPFEVIVVDNGSTDGTAELLAALAfprVRVIRNPENLGFAAARNLGLRA 79

                          90
                  ....*....|....*
gi 1810224639  78 AvehGYEYLLQMDAD 92
Cdd:COG1216    80 A---GGDYLLFLDDD 91
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 8-74 3.25e-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: 3.25e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1810224639   8 VIPAYNEQANIGNVLRKIQEINTDHwlDVVVIDDGSSDNTYGEALACKVTVI-------RQvynMGYGAALQTG 74
Cdd:TIGR04283   4 IIPVLNEAATLPELLADLQALRGDA--EVIVVDGGSTDGTVEIARSLGAKVIhspkgraRQ---MNAGAALAKG 72
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 1-61 5.09e-08

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 52.61  E-value: 5.09e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1810224639   1 MDHKVVLVIPAYNEQANIGNVLRKIQEINTDHWLD-VVVIDDGSSDNTYGEALACKVTVIRQ 61
Cdd:PRK13915   29 AGRTVSVVLPALNEEETVGKVVDSIRPLLMEPLVDeLIVIDSGSTDATAERAAAAGARVVSR 90
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-121 1.30e-07

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: 50.75  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   7 LVIPAYNEQANIGNVLRKIQEIN-TDHWLDVVVIDDGSSDNT--YGEALACKVTV------IRQVYNMGYGAALQTGYKY 77
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDyPKEKFEVILVDDHSTDGTvqILEFAAAKPNFqlkilnNSRVSISGKKNALTTAIKA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1810224639  78 AvehGYEYLLQMDADGQHDVRNLERIYReltAIQERQPDIVIGS 121
Cdd:cd04192    81 A---KGDWIVTTDADCVVPSNWLLTFVA---FIQKEQIGLVAGP 118
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 2-123 2.17e-07

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 50.08  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   2 DHKVVLVIPAYNEQANIGNVLRKIQEINTDHW-LDVVVIDDGSSDNT----------YGEAlacKVTVIRQVYNMGYGAA 70
Cdd:PLN02726    8 AMKYSIIVPTYNERLNIALIVYLIFKALQDVKdFEIIVVDDGSPDGTqdvvkqlqkvYGED---RILLRPRPGKLGLGTA 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1810224639  71 LQTGYKYAVEhgyEYLLQMDADGQHDVRNLeriyRELTAIQ-ERQPDIVIGSRF 123
Cdd:PLN02726   85 YIHGLKHASG---DFVVIMDADLSHHPKYL----PSFIKKQrETGADIVTGTRY 131
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 35-154 2.84e-07

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: 49.97  E-value: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  35 DVVVIDDGSSDNT---YGEALACKVTVIRQVYNMGYGAALQTGYKYAVEHGYEYLLQMDAD---GQHDVRNLERIYRELt 108
Cdd:cd02526    25 DKVVVVDNSSGNDielRLRLNSEKIELIHLGENLGIAKALNIGIKAALENGADYVLLFDQDsvpPPDMVEKLLAYKILS- 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1810224639 109 aiQERQPDIVIGSRFLSaSQTYPVSKIRLVAIRMFRFVIRRLTGYT 154
Cdd:cd02526   104 --DKNSNIGAVGPRIID-RRTGENSPGVRKSGYKLRIQKEGEEGLK 146
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 8-74 4.71e-07

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: 49.11  E-value: 4.71e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1810224639   8 VIPAYNEQANIGNVLRKIQEINTDHwLDVVVIDDGSSDNTygEALACK--VTVI-------RQvynMGYGAALQTG 74
Cdd:cd02522     4 IIPTLNEAENLPRLLASLRRLNPLP-LEIIVVDGGSTDGT--VAIARSagVVVIsspkgraRQ---MNAGAAAARG 73
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 8-92 9.15e-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: 47.60  E-value: 9.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   8 VIPAYNEQANIGNVLRKIQEINT-DHWLDVVVIDDGSSDNTYGEALACKVTVI-RQvynmgygAALQTGYKYAVEHGYEY 85
Cdd:cd06438     2 LIPAHNEEAVIGNTVRSLKAQDYpRELYRIFVVADNCTDDTAQVARAAGATVLeRH-------DPERRGKGYALDFGFRH 74


                  ....*..
gi 1810224639  86 LLQMDAD 92
Cdd:cd06438    75 LLNLADD 81
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 4-120 2.36e-06

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: 47.23  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   4 KVVLVIPAYNEQANIGNVLRKIqeINTDHWLD---VVVIDDGSSDNTYG--EALACKVTVIRQVYNMG--YGAALQTGYK 76
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESL--LNQSYPKDlieIIVVDGGSTDGTREivQEYAAKDPRIRLIDNPKriQSAGLNIGIR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1810224639  77 YAVehgYEYLLQMDADGQHDVRNLERIyreLTAIQERQPDIVIG 120
Cdd:cd02525    79 NSR---GDIIIRVDAHAVYPKDYILEL---VEALKRTGADNVGG 116
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 8-87 8.68e-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: 44.47  E-value: 8.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   8 VIPAYNEQANIGNVLRKIQEINTDHWlDVVVIDDGSSDNTYGEALAC--KVTVIRQVYNMGYGAALQTGYKYAvehGYEY 85
Cdd:cd04186     2 IIVNYNSLEYLKACLDSLLAQTYPDF-EVIVVDNASTDGSVELLRELfpEVRLIRNGENLGFGAGNNQGIREA---KGDY 77


                  ..
gi 1810224639  86 LL 87
Cdd:cd04186    78 VL 79
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 35-123 1.52e-05

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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 44.55  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  35 DVVVIDDGSSDNTyGEALA-----CKVTVIRQVYNMGyGAA-LQTGYKYAVEHGYEYLLQMDADGQHDVRNLERIyreLT 108
Cdd:cd04185    28 HIIVIDNASTDGT-AEWLTslgdlDNIVYLRLPENLG-GAGgFYEGVRRAYELGYDWIWLMDDDAIPDPDALEKL---LA 102

                          90
                  ....*....|....*
gi 1810224639 109 AIQERQPDIVIGSRF 123
Cdd:cd04185   103 YADKDNPQFLAPLVL 117
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 3-157 6.87e-05

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 43.19  E-value: 6.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   3 HKVVLVIPAYNEQANIGNVLRKI----QEINTDHwlDVVVIDDGSSDNT----YGEALACKVTVIRQVYNMGYG--AALQ 72
Cdd:PRK10714    6 KKVSVVIPVYNEQESLPELIRRTtaacESLGKEY--EILLIDDGSSDNSaemlVEAAQAPDSHIVAILLNRNYGqhSAIM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639  73 TGYKYAVEhgyEYLLQMDADGQHDVRNLERiyreLTAIQERQPDIVIGSRflsasQTYPVSKIRLVAIRMFRFVIRRLTG 152
Cdd:PRK10714   84 AGFSHVTG---DLIITLDADLQNPPEEIPR----LVAKADEGYDVVGTVR-----QNRQDSWFRKTASKMINRLIQRTTG 151


                  ....*
gi 1810224639 153 YTLTD 157
Cdd:PRK10714  152 KAMGD 156
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 7-103 2.09e-04

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: 40.83  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810224639   7 LVIPAYNEQANIGNVLRKIqeINTDHWLDVVVIDDGSSDNTYG----EALACKVTVIRQVY---NMGYGAALQTGYKYAV 79
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASL--LRNKPNFLVLVIDDASDDDTAGivrlAITDSRVHLLRRHLpnaRTGKGDALNAAYDQIR 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1810224639  80 EHGYE--------YLLQMDADGQHDVRNLERI 103
Cdd:cd06436    79 QILIEegadpervIIAVIDADGRLDPNALEAV 110
 
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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