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Conserved domains on  [gi|2410729449|ref|WP_268541850|]
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glycosyltransferase family 2 protein [Candidatus Nitrosotenuis cloacae]

Protein Classification

DPM1_like and GtrA domain-containing protein( domain architecture ID 10157757)

DPM1_like and GtrA domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 12-237 6.09e-93

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: 277.88  E-value: 6.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  12 IIIPTYNESQNILQMLKSIEEHLPENTtAQTIVVDDNSPDGTGRLVDDYLKnvkkiANHTIDVIHRKTKEGLSSAILKGI 91
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGID-YEIIVVDDNSPDGTAEIVRELAK-----EYPRVRLIVRPGKRGLGSAYIEGF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  92 QYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIVIASRYVQGGSIRGWTLKRKLMSKIATLIAKRGLSVDAKDPMSG 171
Cdd:cd06442    75 KAARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSG 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449 172 FFAFKRQVIQGL--KFDAIGYKMLLEILVK--KKNANVLEIPYTFTNRKFGSSKLDAKTVTDYFRAVWKL 237
Cdd:cd06442   155 FRAYRREVLEKLidSLVSKGYKFQLELLVRarRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
GtrA COG2246
Putative flippase GtrA (transmembrane translocase of bactoprenol-linked glucose) [Lipid ...
 255-381 1.85e-27

Putative flippase GtrA (transmembrane translocase of bactoprenol-linked glucose) [Lipid transport and metabolism];


:

Pssm-ID: 441847  Cd Length: 133  Bit Score: 105.29  E-value: 1.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449 255 FFSKAGRFYSIGAVGLLVNYLVSSMFV-VSNLWYIYATLIGIAVSMSSNFVLNKLWTFEDRNfePRHTMTQYVKFIGFSS 333
Cdd:COG2246     6 LLRQLLRFGLVGGLGTLVDLGVFYLLVeLLGLPPLLANVIAFVVAVIVNFLLNRRWTFRSRG--GRSRLREFLRFLLVSL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2410729449 334 LGALTQIAMVYVLVDQYDVQYPIALVAAVSCAAISNFILNKKWTFKEK 381
Cdd:COG2246    84 VGLALNLGLLALLVYVLGLPYLLAKLIGIVVGTVFNFLLSRRWVFRKK 131
 
Name Accession Description Interval E-value
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 12-237 6.09e-93

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: 277.88  E-value: 6.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  12 IIIPTYNESQNILQMLKSIEEHLPENTtAQTIVVDDNSPDGTGRLVDDYLKnvkkiANHTIDVIHRKTKEGLSSAILKGI 91
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGID-YEIIVVDDNSPDGTAEIVRELAK-----EYPRVRLIVRPGKRGLGSAYIEGF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  92 QYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIVIASRYVQGGSIRGWTLKRKLMSKIATLIAKRGLSVDAKDPMSG 171
Cdd:cd06442    75 KAARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSG 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449 172 FFAFKRQVIQGL--KFDAIGYKMLLEILVK--KKNANVLEIPYTFTNRKFGSSKLDAKTVTDYFRAVWKL 237
Cdd:cd06442   155 FRAYRREVLEKLidSLVSKGYKFQLELLVRarRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-238 8.12e-54

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 178.35  E-value: 8.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449   1 MKHEGGGTQVSIIIPTYNESQNILQMLKSIEEHLPENTTAQTIVVDDNSPDGTgrlvDDYLKNVKKI-ANHTIDVIHRKT 79
Cdd:PLN02726    2 EAPGEGAMKYSIIVPTYNERLNIALIVYLIFKALQDVKDFEIIVVDDGSPDGT----QDVVKQLQKVyGEDRILLRPRPG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  80 KEGLSSAILKGIQYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIVIASRYVQGGSIRGWTLKRKLMSKIATLIAKR 159
Cdd:PLN02726   78 KLGLGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449 160 GLSVDAKDPMSGFFAFKRQVIQGL--KFDAIGYKMLLEILV--KKKNANVLEIPYTFTNRKFGSSKLDAKTVTDYFRAVW 235
Cdd:PLN02726  158 LLWPGVSDLTGSFRLYKRSALEDLvsSVVSKGYVFQMEIIVraSRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLL 237


                  ...
gi 2410729449 236 KLY 238
Cdd:PLN02726  238 YLL 240
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 10-216 1.75e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 144.84  E-value: 1.75e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  10 VSIIIPTYNESQNILQMLKSIEEHLPENttAQTIVVDDNSPDGTGRLVDDYLKNvkkiaNHTIDVIHRKTKEGLSSAILK 89
Cdd:COG0463     4 VSVVIPTYNEEEYLEEALESLLAQTYPD--FEIIVVDDGSTDGTAEILRELAAK-----DPRIRVIRLERNRGKGAARNA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  90 GIQYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIVIASRYVQGGSIRgwtlKRKLMSKIATLIAkrgLSVDAKDPM 169
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESD----LRRLGSRLFNLVR---LLTNLPDST 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2410729449 170 SGFFAFKRQVIQGLKFDAiGYKMLLEIL-VKKKNANVLEIPYTFTNRK 216
Cdd:COG0463   150 SGFRLFRREVLEELGFDE-GFLEDTELLrALRHGFRIAEVPVRYRAGE 196
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 11-181 8.00e-34

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: 123.27  E-value: 8.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  11 SIIIPTYNESQNILQMLKSIEEHLPENTtaQTIVVDDNSPDGTGRLVDDYLKNVKKIAnhtidVIHRKTKEGLSSAILKG 90
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNF--EIIVVDDGSTDGTVEIAEEYAKKDPRVR-----VIRLPENRGKAGARNAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  91 IQYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIVIASRYVQGGSIRGWTL-KRKLMSKIATLIAKRGLSVDAKDPM 169
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRaSRITLSRLPFFLGLRLLGLNLPFLI 153

                         170
                  ....*....|..
gi 2410729449 170 SGFFAFKRQVIQ 181
Cdd:pfam00535 154 GGFALYRREALE 165
GtrA COG2246
Putative flippase GtrA (transmembrane translocase of bactoprenol-linked glucose) [Lipid ...
 255-381 1.85e-27

Putative flippase GtrA (transmembrane translocase of bactoprenol-linked glucose) [Lipid transport and metabolism];


Pssm-ID: 441847  Cd Length: 133  Bit Score: 105.29  E-value: 1.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449 255 FFSKAGRFYSIGAVGLLVNYLVSSMFV-VSNLWYIYATLIGIAVSMSSNFVLNKLWTFEDRNfePRHTMTQYVKFIGFSS 333
Cdd:COG2246     6 LLRQLLRFGLVGGLGTLVDLGVFYLLVeLLGLPPLLANVIAFVVAVIVNFLLNRRWTFRSRG--GRSRLREFLRFLLVSL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2410729449 334 LGALTQIAMVYVLVDQYDVQYPIALVAAVSCAAISNFILNKKWTFKEK 381
Cdd:COG2246    84 VGLALNLGLLALLVYVLGLPYLLAKLIGIVVGTVFNFLLSRRWVFRKK 131
GtrA pfam04138
GtrA-like protein; Members of this family are predicted to be integral membrane proteins with ...
 261-378 1.79e-24

GtrA-like protein; Members of this family are predicted to be integral membrane proteins with three or four transmembrane spans. They are involved in the synthesis of cell surface polysaccharides. The GtrA family are a subset of this family. GtrA is predicted to be an integral membrane protein with 4 transmembrane spans. It is involved is in O antigen modification by Shigella flexneri bacteriophage X (SfX), but does not determine the specificity of glucosylation. Its function remains unknown, but it may play a role in translocation of undecaprenyl phosphate linked glucose (UndP-Glc) across the cytoplasmic membrane. Another member of this family is a DTDP-glucose-4-keto-6-deoxy-D-glucose reductase, which catalyzes the conversion of dTDP-4-keto-6-deoxy-D-glucose to dTDP-D-fucose, which is involved in the biosynthesis of the serotype-specific polysaccharide antigen of Actinobacillus actinomycetemcomitans Y4 (serotype b). This family also includes the teichoic acid glycosylation protein, GtcA, which is a serotype-specific protein in some Listeria innocua and monocytogenes strains. Its exact function is not known, but it is essential for decoration of cell wall teichoic acids with glucose and galactose.


Pssm-ID: 427738  Cd Length: 116  Bit Score: 96.85  E-value: 1.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449 261 RFYSIGAVGLLVNYLVSSMFV-VSNLWYIYATLIGIAVSMSSNFVLNKLWTFEDRnfePRHTMTQYVKFIGFSSLGALTQ 339
Cdd:pfam04138   1 RFLLVGVLGTLVDLAVFLLLLeLFGLSYLLANAIAFVVAILVNFLLNRRWTFRDR---RSGSLRELLRFFLVSLAGLLLN 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2410729449 340 IAMVYVLVDQYDVQYPIALVAAVSCAAISNFILNKKWTF 378
Cdd:pfam04138  78 LLLLWLLVDGLGLPPLLAKLVGIAVGTVVNFLLSRFFVF 116
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 10-137 1.41e-07

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: 51.74  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  10 VSIIIPTYNESQNILQMLKSIeEHLPEntTAQTIVVDDNSPDGTgrlvddylknVKKIANHTIDVIHrkTKEGLSSAILK 89
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADL-QALRG--DAEVIVVDGGSTDGT----------VEIARSLGAKVIH--SPKGRARQMNA 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2410729449  90 GIQYATGNTIVVMDSDlshpaSLLPKmldALKHQKCDIVIASRYVQGG 137
Cdd:TIGR04283  66 GAALAKGDILLFLHAD-----TRLPK---DFLEAIRRALAKPGYVAGA 105
 
Name Accession Description Interval E-value
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 12-237 6.09e-93

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: 277.88  E-value: 6.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  12 IIIPTYNESQNILQMLKSIEEHLPENTtAQTIVVDDNSPDGTGRLVDDYLKnvkkiANHTIDVIHRKTKEGLSSAILKGI 91
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGID-YEIIVVDDNSPDGTAEIVRELAK-----EYPRVRLIVRPGKRGLGSAYIEGF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  92 QYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIVIASRYVQGGSIRGWTLKRKLMSKIATLIAKRGLSVDAKDPMSG 171
Cdd:cd06442    75 KAARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSG 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449 172 FFAFKRQVIQGL--KFDAIGYKMLLEILVK--KKNANVLEIPYTFTNRKFGSSKLDAKTVTDYFRAVWKL 237
Cdd:cd06442   155 FRAYRREVLEKLidSLVSKGYKFQLELLVRarRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 12-199 1.97e-57

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: 185.47  E-value: 1.97e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  12 IIIPTYNESQNILQMLKSIEEHLPENTTAQTIVVDDNSPDGTGRLVDDYLKNVKKIAnhtidVIHRKTKEGLSSAILKGI 91
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVR-----VIRLSRNFGKGAAVRAGF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  92 QYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIVIASRYVQGGSiRGWTLKRKLMSKIATLIAKRGLSVDAKDPMSG 171
Cdd:cd04179    76 KAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGG-AGMPLLRRLGSRLFNFLIRLLLGVRISDTQSG 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 2410729449 172 FFAFKRQVIQGLK--FDAIGYKMLLEILVK 199
Cdd:cd04179   155 FRLFRREVLEALLslLESNGFEFGLELLVG 184
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-238 8.12e-54

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 178.35  E-value: 8.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449   1 MKHEGGGTQVSIIIPTYNESQNILQMLKSIEEHLPENTTAQTIVVDDNSPDGTgrlvDDYLKNVKKI-ANHTIDVIHRKT 79
Cdd:PLN02726    2 EAPGEGAMKYSIIVPTYNERLNIALIVYLIFKALQDVKDFEIIVVDDGSPDGT----QDVVKQLQKVyGEDRILLRPRPG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  80 KEGLSSAILKGIQYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIVIASRYVQGGSIRGWTLKRKLMSKIATLIAKR 159
Cdd:PLN02726   78 KLGLGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449 160 GLSVDAKDPMSGFFAFKRQVIQGL--KFDAIGYKMLLEILV--KKKNANVLEIPYTFTNRKFGSSKLDAKTVTDYFRAVW 235
Cdd:PLN02726  158 LLWPGVSDLTGSFRLYKRSALEDLvsSVVSKGYVFQMEIIVraSRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLL 237


                  ...
gi 2410729449 236 KLY 238
Cdd:PLN02726  238 YLL 240
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 10-216 1.75e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 144.84  E-value: 1.75e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  10 VSIIIPTYNESQNILQMLKSIEEHLPENttAQTIVVDDNSPDGTGRLVDDYLKNvkkiaNHTIDVIHRKTKEGLSSAILK 89
Cdd:COG0463     4 VSVVIPTYNEEEYLEEALESLLAQTYPD--FEIIVVDDGSTDGTAEILRELAAK-----DPRIRVIRLERNRGKGAARNA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  90 GIQYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIVIASRYVQGGSIRgwtlKRKLMSKIATLIAkrgLSVDAKDPM 169
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESD----LRRLGSRLFNLVR---LLTNLPDST 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2410729449 170 SGFFAFKRQVIQGLKFDAiGYKMLLEIL-VKKKNANVLEIPYTFTNRK 216
Cdd:COG0463   150 SGFRLFRREVLEELGFDE-GFLEDTELLrALRHGFRIAEVPVRYRAGE 196
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 11-181 8.00e-34

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: 123.27  E-value: 8.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  11 SIIIPTYNESQNILQMLKSIEEHLPENTtaQTIVVDDNSPDGTGRLVDDYLKNVKKIAnhtidVIHRKTKEGLSSAILKG 90
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNF--EIIVVDDGSTDGTVEIAEEYAKKDPRVR-----VIRLPENRGKAGARNAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  91 IQYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIVIASRYVQGGSIRGWTL-KRKLMSKIATLIAKRGLSVDAKDPM 169
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRaSRITLSRLPFFLGLRLLGLNLPFLI 153

                         170
                  ....*....|..
gi 2410729449 170 SGFFAFKRQVIQ 181
Cdd:pfam00535 154 GGFALYRREALE 165
GtrA COG2246
Putative flippase GtrA (transmembrane translocase of bactoprenol-linked glucose) [Lipid ...
 255-381 1.85e-27

Putative flippase GtrA (transmembrane translocase of bactoprenol-linked glucose) [Lipid transport and metabolism];


Pssm-ID: 441847  Cd Length: 133  Bit Score: 105.29  E-value: 1.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449 255 FFSKAGRFYSIGAVGLLVNYLVSSMFV-VSNLWYIYATLIGIAVSMSSNFVLNKLWTFEDRNfePRHTMTQYVKFIGFSS 333
Cdd:COG2246     6 LLRQLLRFGLVGGLGTLVDLGVFYLLVeLLGLPPLLANVIAFVVAVIVNFLLNRRWTFRSRG--GRSRLREFLRFLLVSL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2410729449 334 LGALTQIAMVYVLVDQYDVQYPIALVAAVSCAAISNFILNKKWTFKEK 381
Cdd:COG2246    84 VGLALNLGLLALLVYVLGLPYLLAKLIGIVVGTVFNFLLSRRWVFRKK 131
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 12-209 4.03e-27

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: 106.88  E-value: 4.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  12 IIIPTYNESQNILQMLKSIEEHLPENT--TAQTIVVDDNSPDGTGRLVDDYLKNVKKIanhtIDVIHRKTKEGLSSAILK 89
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPsfSYEIIVVDDGSKDGTAEVARKLARKNPAL----IRVLTLPKNRGKGGAVRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  90 GIQYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIVIASRYVQGGSI---RGWtlKRKLMSKIATLIAKRGLSVDAK 166
Cdd:cd04188    77 GMLAARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHLASAAvvkRSW--LRNLLGRGFNFLVRLLLGLGIK 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2410729449 167 DPMSGFFAFKRQV---------IQGLKFDaigykmlLEILV--KKKNANVLEIP 209
Cdd:cd04188   155 DTQCGFKLFTRDAarrlfprlhLERWAFD-------VELLVlaRRLGYPIEEVP 201
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 12-184 4.75e-25

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: 100.24  E-value: 4.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  12 IIIPTYNESQNILQMLKSIEEHLPENTTA-QTIVVDDNSPDGTGRLVDDYLKnvkkiANHTIDVIHrktkegLS------ 84
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDyEIIFVDDGSTDRTLEILRELAA-----RDPRVKVIR------LSrnfgqq 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  85 SAILKGIQYATGNTIVVMDSDLSHPASLLPKMLDALKhQKCDIVIASRyvqggSIRGWTLKRKLMSKIATLIAKRGLSVD 164
Cdd:cd04187    70 AALLAGLDHARGDAVITMDADLQDPPELIPEMLAKWE-EGYDVVYGVR-----KNRKESWLKRLTSKLFYRLINKLSGVD 143

                         170       180
                  ....*....|....*....|
gi 2410729449 165 AKDPMSGFFAFKRQVIQGLK 184
Cdd:cd04187   144 IPDNGGDFRLMDRKVVDALL 163
GtrA pfam04138
GtrA-like protein; Members of this family are predicted to be integral membrane proteins with ...
 261-378 1.79e-24

GtrA-like protein; Members of this family are predicted to be integral membrane proteins with three or four transmembrane spans. They are involved in the synthesis of cell surface polysaccharides. The GtrA family are a subset of this family. GtrA is predicted to be an integral membrane protein with 4 transmembrane spans. It is involved is in O antigen modification by Shigella flexneri bacteriophage X (SfX), but does not determine the specificity of glucosylation. Its function remains unknown, but it may play a role in translocation of undecaprenyl phosphate linked glucose (UndP-Glc) across the cytoplasmic membrane. Another member of this family is a DTDP-glucose-4-keto-6-deoxy-D-glucose reductase, which catalyzes the conversion of dTDP-4-keto-6-deoxy-D-glucose to dTDP-D-fucose, which is involved in the biosynthesis of the serotype-specific polysaccharide antigen of Actinobacillus actinomycetemcomitans Y4 (serotype b). This family also includes the teichoic acid glycosylation protein, GtcA, which is a serotype-specific protein in some Listeria innocua and monocytogenes strains. Its exact function is not known, but it is essential for decoration of cell wall teichoic acids with glucose and galactose.


Pssm-ID: 427738  Cd Length: 116  Bit Score: 96.85  E-value: 1.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449 261 RFYSIGAVGLLVNYLVSSMFV-VSNLWYIYATLIGIAVSMSSNFVLNKLWTFEDRnfePRHTMTQYVKFIGFSSLGALTQ 339
Cdd:pfam04138   1 RFLLVGVLGTLVDLAVFLLLLeLFGLSYLLANAIAFVVAILVNFLLNRRWTFRDR---RSGSLRELLRFFLVSLAGLLLN 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2410729449 340 IAMVYVLVDQYDVQYPIALVAAVSCAAISNFILNKKWTF 378
Cdd:pfam04138  78 LLLLWLLVDGLGLPPLLAKLVGIAVGTVVNFLLSRFFVF 116
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 12-130 4.67e-19

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: 83.32  E-value: 4.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  12 IIIPTYNESQNILQMLKSIEEHLPENTtaQTIVVDDNSPDGTGRLVDDYLKNvkkiaNHTIDVIHRKTKEGLSSAILKGI 91
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNF--EVIVVDDGSTDGTLEILEEYAKK-----DPRVIRVINEENQGLAAARNAGL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2410729449  92 QYATGNTIVVMDSDLSHPASLLPKMLDAL-KHQKCDIVIA 130
Cdd:cd00761    74 KAARGEYILFLDADDLLLPDWLERLVAELlADPEADAVGG 113
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 10-128 4.33e-18

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: 84.02  E-value: 4.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  10 VSIIIPTYNESQNILQMLKSIEEHLPENTTAQTIVVDDNSPDGTGRLVDDYLKNVKKIanhtiDVIHRKTKEGLSSAILK 89
Cdd:COG1215    31 VSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIARELAAEYPRV-----RVIERPENGGKAAALNA 105

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2410729449  90 GIQYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIV 128
Cdd:COG1215   106 GLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS 144
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 10-190 1.57e-15

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: 75.35  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  10 VSIIIPTYNESQNILQMLKSIEEHLPENTTAQTIVVDDNSPDGTGRLVDDYLKNVKKIAnhtidVIHRKtKEGLSSAILK 89
Cdd:cd02525     2 VSIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIR-----LIDNP-KRIQSAGLNI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  90 GIQYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIVIASRYVQGGSIRGWTLKRKLMSKIATLIAK-RGLSVDAKDP 168
Cdd:cd02525    76 GIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIAVAQSSPLGSGGSAyRGGAVKIGYV 155

                         170       180
                  ....*....|....*....|...
gi 2410729449 169 MSGFF-AFKRQViqglkFDAIGY 190
Cdd:cd02525   156 DTVHHgAYRREV-----FEKVGG 173
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
10-119 1.15e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 71.95  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  10 VSIIIPTYNESQNILQMLKSIEEHLPENttAQTIVVDDNSPDGTGRLVddylknvKKIANHTIDVIHRKTKEGLSSAILK 89
Cdd:COG1216     5 VSVVIPTYNRPELLRRCLESLLAQTYPP--FEVIVVDNGSTDGTAELL-------AALAFPRVRVIRNPENLGFAAARNL 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 2410729449  90 GIQYATGNTIVVMDSDLSHPASLLPKMLDA 119
Cdd:COG1216    76 GLRAAGGDYLLFLDDDTVVEPDWLERLLAA 105
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 12-180 3.24e-13

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: 67.25  E-value: 3.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  12 IIIPTYNESQNILQMLKSIEehlpenttAQT------IVVDDNSPDGTGRLVDDYLKNVKKIANhtidVIHRKTKEGLSS 85
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLL--------ALDypklevIVVDDGSTDDTLEILEELAALYIRRVL----VVRDKENGGKAG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  86 AILKGIQYATGNTIVVMDSDlSHPASLLPKMLDALKHQKCDIVIASRYVQG--GSIRGWTLKRKLMSKIATLIAKRGLSV 163
Cdd:cd06423    69 ALNAGLRHAKGDIVVVLDAD-TILEPDALKRLVVPFFADPKVGAVQGRVRVrnGSENLLTRLQAIEYLSIFRLGRRAQSA 147

                         170
                  ....*....|....*....
gi 2410729449 164 DAKDP-MSG-FFAFKRQVI 180
Cdd:cd06423   148 LGGVLvLSGaFGAFRREAL 166
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 10-188 2.12e-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: 60.67  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  10 VSIIIPTYNESQNILQMLksieehlpENTTAQT--------IVVDDNSPDGTGRLVDDYLKNVkkianhtIDVIHRKTKE 81
Cdd:cd06439    31 VTIIIPAYNEEAVIEAKL--------ENLLALDyprdrleiIVVSDGSTDGTAEIAREYADKG-------VKLLRFPERR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  82 GLSSAILKGIQYATGNTIVVMDSDlshpaSLLPKmlDALKHQK------------CDIVIASRYVQGGSIRG-WTLK--- 145
Cdd:cd06439    96 GKAAALNRALALATGEIVVFTDAN-----ALLDP--DALRLLVrhfadpsvgavsGELVIVDGGGSGSGEGLyWKYEnwl 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2410729449 146 RKLMSKIATLIAKRGlsvdakdpmsGFFAFKRQVIQGLKFDAI 188
Cdd:cd06439   169 KRAESRLGSTVGANG----------AIYAIRRELFRPLPADTI 201
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 9-221 6.13e-10

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 59.75  E-value: 6.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449   9 QVSIIIPTYNESQNILQMLksieehlpENTTA---------QTIVVDDNSPDGTGRLVddyLKNVKKIANHTIDVIHRKT 79
Cdd:PRK10714    7 KVSVVIPVYNEQESLPELI--------RRTTAaceslgkeyEILLIDDGSSDNSAEML---VEAAQAPDSHIVAILLNRN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  80 KeGLSSAILKGIQYATGNTIVVMDSDLSHPASLLPKMLdALKHQKCDIVIASRyvqggSIRGWTLKRKLMSKIATLIAKR 159
Cdd:PRK10714   76 Y-GQHSAIMAGFSHVTGDLIITLDADLQNPPEEIPRLV-AKADEGYDVVGTVR-----QNRQDSWFRKTASKMINRLIQR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449 160 GLSVDAKDPMSGFFAFKRQVIqglkfDAigykML--------LEILVKKKNANVLEIPYTFTNRKFGSSK 221
Cdd:PRK10714  149 TTGKAMGDYGCMLRAYRRHIV-----DA----MLhcherstfIPILANTFARRAIEIPVHHAEREFGDSK 209
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 9-209 6.86e-10

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 59.78  E-value: 6.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449   9 QVSIIIPTYNESQNILQMLKSIEEHLPE------NTTAQTIVVDDNSPDGTGRLVDDYLKNvKKIANHTIDVIHRKTKEG 82
Cdd:PTZ00260   71 DLSIVIPAYNEEDRLPKMLKETIKYLESrsrkdpKFKYEIIIVNDGSKDKTLKVAKDFWRQ-NINPNIDIRLLSLLRNKG 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  83 LSSAILKGIQYATGNTIVVMDSDLSHPASLLPKMLDAL---KHQKCDIVIASR--YVQGGSIRGWTLKRKLMSKIATLIA 157
Cdd:PTZ00260  150 KGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMlkiEQNGLGIVFGSRnhLVDSDVVAKRKWYRNILMYGFHFIV 229

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2410729449 158 KRGLSVDAKDPMSGFFAFKR----QVIQGLKFDAIGYKMLLEILVKKKNANVLEIP 209
Cdd:PTZ00260  230 NTICGTNLKDTQCGFKLFTRetarIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVP 285
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 11-104 9.38e-10

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: 59.14  E-value: 9.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  11 SIIIPTYNESQN-ILQMLKSIEEHLPENTTAQTIVVDDNSPDGTgrlVDDYLKNVKKIANHTIDVIHRKTKEGLSSAILK 89
Cdd:cd02510     1 SVIIIFHNEALStLLRTVHSVINRTPPELLKEIILVDDFSDKPE---LKLLLEEYYKKYLPKVKVLRLKKREGLIRARIA 77

                          90
                  ....*....|....*
gi 2410729449  90 GIQYATGNTIVVMDS 104
Cdd:cd02510    78 GARAATGDVLVFLDS 92
GtrA COG2246
Putative flippase GtrA (transmembrane translocase of bactoprenol-linked glucose) [Lipid ...
 250-314 1.43e-09

Putative flippase GtrA (transmembrane translocase of bactoprenol-linked glucose) [Lipid transport and metabolism];


Pssm-ID: 441847  Cd Length: 133  Bit Score: 55.60  E-value: 1.43e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2410729449 250 RTSVSFFSKAGRFYSIGAVGLLVNYLVSSMFV-VSNLWYIYATLIGIAVSMSSNFVLNKLWTFEDR 314
Cdd:COG2246    66 RGGRSRLREFLRFLLVSLVGLALNLGLLALLVyVLGLPYLLAKLIGIVVGTVFNFLLSRRWVFRKK 131
GtrA COG2246
Putative flippase GtrA (transmembrane translocase of bactoprenol-linked glucose) [Lipid ...
 317-381 3.73e-09

Putative flippase GtrA (transmembrane translocase of bactoprenol-linked glucose) [Lipid transport and metabolism];


Pssm-ID: 441847  Cd Length: 133  Bit Score: 54.44  E-value: 3.73e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2410729449 317 EPRHTMTQYVKFIGFSSLGALTQIAMVYVLVDQYDVQYPIALVAAVSCAAISNFILNKKWTFKEK 381
Cdd:COG2246     2 ALRRLLRQLLRFGLVGGLGTLVDLGVFYLLVELLGLPPLLANVIAFVVAVIVNFLLNRRWTFRSR 66
GtrA pfam04138
GtrA-like protein; Members of this family are predicted to be integral membrane proteins with ...
 327-379 4.71e-09

GtrA-like protein; Members of this family are predicted to be integral membrane proteins with three or four transmembrane spans. They are involved in the synthesis of cell surface polysaccharides. The GtrA family are a subset of this family. GtrA is predicted to be an integral membrane protein with 4 transmembrane spans. It is involved is in O antigen modification by Shigella flexneri bacteriophage X (SfX), but does not determine the specificity of glucosylation. Its function remains unknown, but it may play a role in translocation of undecaprenyl phosphate linked glucose (UndP-Glc) across the cytoplasmic membrane. Another member of this family is a DTDP-glucose-4-keto-6-deoxy-D-glucose reductase, which catalyzes the conversion of dTDP-4-keto-6-deoxy-D-glucose to dTDP-D-fucose, which is involved in the biosynthesis of the serotype-specific polysaccharide antigen of Actinobacillus actinomycetemcomitans Y4 (serotype b). This family also includes the teichoic acid glycosylation protein, GtcA, which is a serotype-specific protein in some Listeria innocua and monocytogenes strains. Its exact function is not known, but it is essential for decoration of cell wall teichoic acids with glucose and galactose.


Pssm-ID: 427738  Cd Length: 116  Bit Score: 53.71  E-value: 4.71e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2410729449 327 KFIGFSSLGALTQIAMVYVLVDQYDVQYPIALVAAVSCAAISNFILNKKWTFK 379
Cdd:pfam04138   1 RFLLVGVLGTLVDLAVFLLLLELFGLSYLLANAIAFVVAILVNFLLNRRWTFR 53
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 11-128 1.34e-08

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: 54.47  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  11 SIIIPTYNESQNILQMLKSIEEhlpenttaQT------IVVDDNSPDGTgrlVDdYLKNvkkiANHTIDVIHRKTKEGLS 84
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLS--------QTypnieyIVIDGGSTDGT---VD-IIKK----YEDKITYWISEPDKGIY 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2410729449  85 SAILKGIQYATGNTIVVMDS-DLSHPASLLPKMLDALKHQKCDIV 128
Cdd:cd06433    65 DAMNKGIALATGDIIGFLNSdDTLLPGALLAVVAAFAEHPEVDVV 109
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 10-137 1.41e-07

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: 51.74  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  10 VSIIIPTYNESQNILQMLKSIeEHLPEntTAQTIVVDDNSPDGTgrlvddylknVKKIANHTIDVIHrkTKEGLSSAILK 89
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADL-QALRG--DAEVIVVDGGSTDGT----------VEIARSLGAKVIH--SPKGRARQMNA 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2410729449  90 GIQYATGNTIVVMDSDlshpaSLLPKmldALKHQKCDIVIASRYVQGG 137
Cdd:TIGR04283  66 GAALAKGDILLFLHAD-----TRLPK---DFLEAIRRALAKPGYVAGA 105
GtrA pfam04138
GtrA-like protein; Members of this family are predicted to be integral membrane proteins with ...
 249-311 4.69e-07

GtrA-like protein; Members of this family are predicted to be integral membrane proteins with three or four transmembrane spans. They are involved in the synthesis of cell surface polysaccharides. The GtrA family are a subset of this family. GtrA is predicted to be an integral membrane protein with 4 transmembrane spans. It is involved is in O antigen modification by Shigella flexneri bacteriophage X (SfX), but does not determine the specificity of glucosylation. Its function remains unknown, but it may play a role in translocation of undecaprenyl phosphate linked glucose (UndP-Glc) across the cytoplasmic membrane. Another member of this family is a DTDP-glucose-4-keto-6-deoxy-D-glucose reductase, which catalyzes the conversion of dTDP-4-keto-6-deoxy-D-glucose to dTDP-D-fucose, which is involved in the biosynthesis of the serotype-specific polysaccharide antigen of Actinobacillus actinomycetemcomitans Y4 (serotype b). This family also includes the teichoic acid glycosylation protein, GtcA, which is a serotype-specific protein in some Listeria innocua and monocytogenes strains. Its exact function is not known, but it is essential for decoration of cell wall teichoic acids with glucose and galactose.


Pssm-ID: 427738  Cd Length: 116  Bit Score: 47.93  E-value: 4.69e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2410729449 249 RRTSVSFFSKAGRFYSIGAVGLLVNYLVSSMFV-VSNLWYIYATLIGIAVSMSSNFVLNKLWTF 311
Cdd:pfam04138  53 RDRRSGSLRELLRFFLVSLAGLLLNLLLLWLLVdGLGLPPLLAKLVGIAVGTVVNFLLSRFFVF 116
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 10-128 5.19e-07

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 49.89  E-value: 5.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  10 VSIIIPTYNESQNIL-QMLKSIEEHLPENTtaQTIVVDDNSPDgtgRLVDDYLKNVKKIaNHTIDVIHRKTKEGLSSAIL 88
Cdd:cd04184     3 ISIVMPVYNTPEKYLrEAIESVRAQTYPNW--ELCIADDASTD---PEVKRVLKKYAAQ-DPRIKVVFREENGGISAATN 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2410729449  89 KGIQYATGNTIVVMDS-DLSHPASLLpKMLDAL-KHQKCDIV 128
Cdd:cd04184    77 SALELATGEFVALLDHdDELAPHALY-EVVKALnEHPDADLI 117
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 12-139 8.60e-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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 48.32  E-value: 8.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  12 IIIPTYNESQNILQMLKSIEEHLPENTTaqTIVVDDNSPDGTGRLVDDYLKNVKKIANHtidvihrkTKEGLSSAILKGI 91
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFE--VIVVDNASTDGSVELLRELFPEVRLIRNG--------ENLGFGAGNNQGI 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2410729449  92 QYATGNTIVVMDSD--LSHPAslLPKMLDALKHQKcDIVIASRYVQGGSI 139
Cdd:cd04186    71 REAKGDYVLLLNPDtvVEPGA--LLELLDAAEQDP-DVGIVGPKVSGAFL 117
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 10-137 1.05e-06

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: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  10 VSIIIPTYNESQNILQMLKSIEEHLPENttAQTIVVDDNSPDGTGRLVDDYlknvkkianhtiDVIHRKTKEGLSSAILK 89
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLP--LEIIVVDGGSTDGTVAIARSA------------GVVVISSPKGRARQMNA 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2410729449  90 GIQYATGNTIVVMDSDlshpaSLLPKMLDALKHQKCdivIASRYVQGG 137
Cdd:cd02522    67 GAAAARGDWLLFLHAD-----TRLPPDWDAAIIETL---RADGAVAGA 106
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 12-138 1.59e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 48.82  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  12 IIIPTYNESQNILQMLKSIE------EHLpenttaQTIVVDDNSPDGTGRLVDDYL----KNVKKIANhtidviHRKTKE 81
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSaldypkEKF------EVILVDDHSTDGTVQILEFAAakpnFQLKILNN------SRVSIS 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2410729449  82 GLSSAILKGIQYATGNTIVVMDSDLSHPASLLPKMLDAL-KHQKCDIVIASRYVQGGS 138
Cdd:cd04192    69 GKKNALTTAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIqKEQIGLVAGPVIYFKGKS 126
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 10-157 1.68e-06

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: 48.79  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  10 VSIIIPTYNESQNIL-QMLKSIEEHLPenttAQTIVV-DDNSpdgtgrlvDDYLKNVKKIANHTIDVIHRKTKEGLSSAI 87
Cdd:cd06434     2 VTVIIPVYDEDPDVFrECLRSILRQKP----LEIIVVtDGDD--------EPYLSILSQTVKYGGIFVITVPHPGKRRAL 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  88 LKGIQYATGNTIVVMDSDLSHPASLLPKMLDALKHQKCDIViasryvqGGSIRgwtLKRKLMSKIATLIA 157
Cdd:cd06434    70 AEGIRHVTTDIVVLLDSDTVWPPNALPEMLKPFEDPKVGGV-------GTNQR---ILRPRDSKWSFLAA 129
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 10-191 1.94e-06

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: 48.52  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  10 VSIIIPTYNESQNILQMLksiEEHL-PENTTAQTIVVDDNSPDGTGRLVDDYLKNVKKIANHTIDVIHRKTKEGLSSAIL 88
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVL---EAILaQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTGKSRGLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  89 KGIQYATGNTIVVMDSD-LSHPaSLLPKMLDALKHQKCDIVIASRYVQGGSiRGWT------LKRKLMSKIATLIAKRGL 161
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDsVLHP-GTLKKYVQYFDSPKVGAVGTPVFSLNRS-TMLSalgaleFALRHLRMMSLRLALGVL 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2410729449 162 svdakdPMSG-FFAFKRQVIQGL-KFDAIGYK 191
Cdd:pfam13641 159 ------PLSGaGSAIRREVLKELgLFDPFFLL 184
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 13-173 2.42e-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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 47.63  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  13 IIPTYNESQNILQMLKSIEehlpenttAQT------IVVDDNSPDGTGRLVDDyLKNVKKianhtIDVIHRKTKEGLSSA 86
Cdd:cd04185     2 VVVTYNRLDLLKECLDALL--------AQTrppdhiIVIDNASTDGTAEWLTS-LGDLDN-----IVYLRLPENLGGAGG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  87 ILKGIQYATGNT---IVVMDSDLSHPASLLPKMLDALKHQKCDIVIASRYVQGGSIRGWTLKRKLMSKIatliakrGLsv 163
Cdd:cd04185    68 FYEGVRRAYELGydwIWLMDDDAIPDPDALEKLLAYADKDNPQFLAPLVLDPDGSFVGVLISRRVVEKI-------GL-- 138

                         170
                  ....*....|
gi 2410729449 164 dakdPMSGFF 173
Cdd:cd04185   139 ----PDKEFF 144
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 10-105 6.05e-06

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: 46.90  E-value: 6.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  10 VSIIIPTYNESQNILQMLKSIEEHlpentTAQTIVVDDNSPDGTgrlvddylknvKKIA-NHTIDVIHRKtKEGLSSAIL 88
Cdd:cd02511     2 LSVVIITKNEERNIERCLESVKWA-----VDEIIVVDSGSTDRT-----------VEIAkEYGAKVYQRW-WDGFGAQRN 64

                          90
                  ....*....|....*..
gi 2410729449  89 KGIQYATGNTIVVMDSD 105
Cdd:cd02511    65 FALELATNDWVLSLDAD 81
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 11-96 7.75e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 43.39  E-value: 7.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  11 SIIIPTYNESQNILQMLKSIEehlpenttAQT------IVVDDNSPDGTGRLVDDYlknvkkIANHTIDVIHRKTKEGLS 84
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSIL--------AQTykndelIISDDGSTDGTVEIIKEY------IDKDPFIIILIRNGKNLG 66

                          90
                  ....*....|....
gi 2410729449  85 SA--ILKGIQYATG 96
Cdd:cd04196    67 VArnFESLLQAADG 80
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 8-105 1.23e-04

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 43.50  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449   8 TQVSIIIPTYNESQNILQMLKSIEehlpenttAQT------IVVDDNSPDGTGRLVDDYLKNVKKianhtIDVIHRKTkE 81
Cdd:PRK10073    6 PKLSIIIPLYNAGKDFRAFMESLI--------AQTwtaleiIIVNDGSTDNSVEIAKHYAENYPH-----VRLLHQAN-A 71

                          90       100
                  ....*....|....*....|....
gi 2410729449  82 GLSSAILKGIQYATGNTIVVMDSD 105
Cdd:PRK10073   72 GVSVARNTGLAVATGKYVAFPDAD 95
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 6-120 3.84e-04

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 41.83  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449   6 GGTQVSIIIPTYNESQNILQMLKSIEEHLPENTTAQTIVVDDNSPDGTGRLVddylknvkkiANHTIDVIHRKT------ 79
Cdd:PRK13915   29 AGRTVSVVLPALNEEETVGKVVDSIRPLLMEPLVDELIVIDSGSTDATAERA----------AAAGARVVSREEilpelp 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2410729449  80 -KEGLSSAILKGIQYATGNTIVVMDSDLSHPAS-LLPKMLDAL 120
Cdd:PRK13915   99 pRPGKGEALWRSLAATTGDIVVFVDADLINFDPmFVPGLLGPL 141
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 12-122 7.19e-04

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 40.52  E-value: 7.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  12 IIIPTYNESQNILQMLKSIEEHLPENTTaQTIVVDDNSPDGTGRLVDDYLKNVKKIANHTIDVIHRK-TKEGLSSAILKG 90
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTL-ELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSpSPKGVGYAKNQA 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2410729449  91 IQYATGNTIVVMDS-DLSHPASLLPKMLDALKH 122
Cdd:cd06913    80 IAQSSGRYLCFLDSdDVMMPQRIRLQYEAALQH 112
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 12-105 2.28e-03

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 38.71  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729449  12 IIIPTYNESQNILQMLKSIeehlpentTAQT------IVVDDNSPDGTGRLVDDYlknvKKIANhtIDVIH--------R 77
Cdd:cd06420     1 LIITTYNRPEALELVLKSV--------LNQSilpfevIIADDGSTEETKELIEEF----KSQFP--IPIKHvwqedegfR 66

                          90       100
                  ....*....|....*....|....*....
gi 2410729449  78 KTKeglssaIL-KGIQYATGNTIVVMDSD 105
Cdd:cd06420    67 KAK------IRnKAIAAAKGDYLIFIDGD 89
 
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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