NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|851329401|ref|NP_001297013|]
View 

dolichol-phosphate mannosyltransferase subunit 1 isoform 2 [Mus musculus]

Protein Classification

dolichol-phosphate mannosyltransferase subunit 1( domain architecture ID 1002602)

dolichol-phosphate mannosyltransferase subunit 1 (DPM1) transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02726 super family cl30529
dolichyl-phosphate beta-D-mannosyltransferase
21-237 3.80e-131

dolichyl-phosphate beta-D-mannosyltransferase


The actual alignment was detected with superfamily member PLN02726:

Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 369.41  E-value: 3.80e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  21 SSRQDKYSVLLPTYNERENLPLIVWLLVKSFsESAINYEIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPREKKLGLGT 100
Cdd:PLN02726   5 GEGAMKYSIIVPTYNERLNIALIVYLIFKAL-QDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 101 AYIHGIKHATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKI----------------- 163
Cdd:PLN02726  84 AYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLtsrganvlaqtllwpgv 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 164 ------IRLYRKEVLQKLIEKCVSKGYVFQMEMIVRARQMNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT 237
Cdd:PLN02726 164 sdltgsFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLLTT 243
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
21-237 3.80e-131

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 369.41  E-value: 3.80e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  21 SSRQDKYSVLLPTYNERENLPLIVWLLVKSFsESAINYEIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPREKKLGLGT 100
Cdd:PLN02726   5 GEGAMKYSIIVPTYNERLNIALIVYLIFKAL-QDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 101 AYIHGIKHATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKI----------------- 163
Cdd:PLN02726  84 AYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLtsrganvlaqtllwpgv 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 164 ------IRLYRKEVLQKLIEKCVSKGYVFQMEMIVRARQMNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT 237
Cdd:PLN02726 164 sdltgsFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLLTT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
29-233 7.35e-114

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: 324.87  E-value: 7.35e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  29 VLLPTYNERENLPLIVWLLVKSFSEsaINYEIIIIDDGSPDGTREVAEQLAEIYGPDRilLRPREKKLGLGTAYIHGIKH 108
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKG--IDYEIIVVDDNSPDGTAEIVRELAKEYPRVR--LIVRPGKRGLGSAYIEGFKA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 109 ATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKII-----------------------R 165
Cdd:cd06442   77 ARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLIsrganllarlllgrkvsdptsgfR 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 851329401 166 LYRKEVLQKLIEKCVSKGYVFQMEMIVRARQMNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTL 233
Cdd:cd06442  157 AYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
28-193 4.36e-38

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: 130.21  E-value: 4.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401   28 SVLLPTYNERENLPLIVWLLVKSFSEsaiNYEIIIIDDGSPDGTREVAEQLAEIYgpDRILLRPREKKLGLGTAYIHGIK 107
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  108 HATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIIRLYRKEVLQKLIEKCVSKGYVFQ 187
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGG 155

                  ....*.
gi 851329401  188 MEMIVR 193
Cdd:pfam00535 156 FALYRR 161
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
26-198 1.58e-22

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


Pssm-ID: 223539 [Multi-domain]  Cd Length: 291  Bit Score: 93.22  E-value: 1.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  26 KYSVLLPTYNERENLPLivwlLVKSFSE-SAINYEIIIIDDGSPDGTREVAEQLAEIYGpdRILLRPREKKLGLGTAYIH 104
Cdd:COG0463    4 KVSVVIPTYNEEEYLPE----ALESLLNqTYKDFEIIVVDDGSTDGTTEIAIEYGAKDV--RVIRLINERNGGLGAARNA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 105 GIKHATGNYVIIMDADLSHHPKFIPEFIRKQkegnfDIVSGTRYKGNGGVYGWD-LKRKIIRLYRKEVLQKLIEKCVSKG 183
Cdd:COG0463   78 GLEYARGDYIVFLDADDQHPPELIPLVAAGG-----DGDYIARLDDRDDIWLPRkLLSKLVKLLGNRLLGVLIPDGFGDL 152
                        170
                 ....*....|....*
gi 851329401 184 YVFQMEMIVRARQMN 198
Cdd:COG0463  153 RLLVRDAVDGLRAFL 167
 
Name Accession Description Interval E-value
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
21-237 3.80e-131

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 369.41  E-value: 3.80e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  21 SSRQDKYSVLLPTYNERENLPLIVWLLVKSFsESAINYEIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPREKKLGLGT 100
Cdd:PLN02726   5 GEGAMKYSIIVPTYNERLNIALIVYLIFKAL-QDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 101 AYIHGIKHATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKI----------------- 163
Cdd:PLN02726  84 AYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHGWDLRRKLtsrganvlaqtllwpgv 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 164 ------IRLYRKEVLQKLIEKCVSKGYVFQMEMIVRARQMNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT 237
Cdd:PLN02726 164 sdltgsFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEIVQYLKGLLYLLLTT 243
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
29-233 7.35e-114

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: 324.87  E-value: 7.35e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  29 VLLPTYNERENLPLIVWLLVKSFSEsaINYEIIIIDDGSPDGTREVAEQLAEIYGPDRilLRPREKKLGLGTAYIHGIKH 108
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKG--IDYEIIVVDDNSPDGTAEIVRELAKEYPRVR--LIVRPGKRGLGSAYIEGFKA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 109 ATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKII-----------------------R 165
Cdd:cd06442   77 ARGDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVEGWGLKRKLIsrganllarlllgrkvsdptsgfR 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 851329401 166 LYRKEVLQKLIEKCVSKGYVFQMEMIVRARQMNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTL 233
Cdd:cd06442  157 AYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLGGKEIVEYLKGLLRL 224
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
29-194 7.87e-62

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


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 191.63  E-value: 7.87e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  29 VLLPTYNERENLPLIVWLLVKSFSESaINYEIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPRekKLGLGTAYIHGIKH 108
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEG-YDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSR--NFGKGAAVRAGFKA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 109 ATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVyGWDLKRKII-----------------------R 165
Cdd:cd04179   78 ARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGA-GMPLLRRLGsrlfnflirlllgvrisdtqsgfR 156
                        170       180
                 ....*....|....*....|....*....
gi 851329401 166 LYRKEVLQKLIEKCVSKGYVFQMEMIVRA 194
Cdd:cd04179  157 LFRREVLEALLSLLESNGFEFGLELLVGA 185
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
28-193 4.36e-38

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: 130.21  E-value: 4.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401   28 SVLLPTYNERENLPLIVWLLVKSFSEsaiNYEIIIIDDGSPDGTREVAEQLAEIYgpDRILLRPREKKLGLGTAYIHGIK 107
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  108 HATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIIRLYRKEVLQKLIEKCVSKGYVFQ 187
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGG 155

                  ....*.
gi 851329401  188 MEMIVR 193
Cdd:pfam00535 156 FALYRR 161
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
29-177 9.97e-31

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: 111.80  E-value: 9.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  29 VLLPTYNERENLPLIVWLLVKSFSESAINYEIIIIDDGSPDGTREVAEQLAEIYGPDR-ILLRpreKKLGLGTAYIHGIK 107
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKvIRLS---RNFGQQAALLAGLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 108 HATGNYVIIMDADLSHHPKFIPEFIRKQKEGnFDIVSGTRYKGNGG------------VYGWDLKRKII------RLYRK 169
Cdd:cd04187   78 HARGDAVITMDADLQDPPELIPEMLAKWEEG-YDVVYGVRKNRKESwlkrltsklfyrLINKLSGVDIPdnggdfRLMDR 156

                 ....*...
gi 851329401 170 EVLQKLIE 177
Cdd:cd04187  157 KVVDALLL 164
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
29-217 6.30e-30

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: 110.73  E-value: 6.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  29 VLLPTYNERENLPLIVWLLVKSFSES-AINYEIIIIDDGSPDGTREVAEQLAEIYGPDRILLRpREKKLGLGTAYIHGIK 107
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYLEERpSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLT-LPKNRGKGGAVRAGML 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 108 HATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYK-GNGGVYGWDLKRKII---------------------- 164
Cdd:cd04188   80 AARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHlASAAVVKRSWLRNLLgrgfnflvrlllglgikdtqcg 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 851329401 165 -RLYRKEVLQKLIEKCVSKGYVFQMEMIVRARQMNYTIGEVPISFVDRvyGESK 217
Cdd:cd04188  160 fKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEI--PGSK 211
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
29-201 1.56e-25

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: 97.58  E-value: 1.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  29 VLLPTYNERENLPLIVWLLVKSFSEsaiNYEIIIIDDGSPDGTREVAEQLAEIygPDRILLRPREKKLGLGTAYIHGIKH 108
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYP---NFEVIVVDDGSTDGTLEILEEYAKK--DPRVIRVINEENQGLAAARNAGLKA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 109 ATGNYVIIMDADLSHHPKFIPEFIRK-QKEGNFDIVSGTrykgngGVYgwdlkrkiirLYRKEVLQKLIEKCVSKGYVFQ 187
Cdd:cd00761   76 ARGEYILFLDADDLLLPDWLERLVAElLADPEADAVGGP------GNL----------LFRRELLEEIGGFDEALLSGEE 139
                        170
                 ....*....|....
gi 851329401 188 MEMIVRARQMNYTI 201
Cdd:cd00761  140 DDDFLLRLLRGGKV 153
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
26-198 1.58e-22

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


Pssm-ID: 223539 [Multi-domain]  Cd Length: 291  Bit Score: 93.22  E-value: 1.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  26 KYSVLLPTYNERENLPLivwlLVKSFSE-SAINYEIIIIDDGSPDGTREVAEQLAEIYGpdRILLRPREKKLGLGTAYIH 104
Cdd:COG0463    4 KVSVVIPTYNEEEYLPE----ALESLLNqTYKDFEIIVVDDGSTDGTTEIAIEYGAKDV--RVIRLINERNGGLGAARNA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 105 GIKHATGNYVIIMDADLSHHPKFIPEFIRKQkegnfDIVSGTRYKGNGGVYGWD-LKRKIIRLYRKEVLQKLIEKCVSKG 183
Cdd:COG0463   78 GLEYARGDYIVFLDADDQHPPELIPLVAAGG-----DGDYIARLDDRDDIWLPRkLLSKLVKLLGNRLLGVLIPDGFGDL 152
                        170
                 ....*....|....*
gi 851329401 184 YVFQMEMIVRARQMN 198
Cdd:COG0463  153 RLLVRDAVDGLRAFL 167
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
25-237 1.22e-17

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 80.16  E-value: 1.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  25 DKYSVLLPTYNERENLPLIVWLLVKSFSESAINYEIIIIDDGSPDGTREVAEQLAEIygPDR----ILLrprEKKLGLGT 100
Cdd:PRK10714   6 KKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQA--PDShivaILL---NRNYGQHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 101 AYIHGIKHATGNYVIIMDADLSHHPKFIPEFIRKQKEGnFDIVsGTRYKGNGGVYGWDLKRKII---------------- 164
Cdd:PRK10714  81 AIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEG-YDVV-GTVRQNRQDSWFRKTASKMInrliqrttgkamgdyg 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 851329401 165 ---RLYRKEVLQKLIEkCVSKGYVFQMEMIVRARQmnyTIgEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT 237
Cdd:PRK10714 159 cmlRAYRRHIVDAMLH-CHERSTFIPILANTFARR---AI-EIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTT 229
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
29-120 1.04e-16

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: 74.96  E-value: 1.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  29 VLLPTYNERENLPLIVWLLVKSFSEsaiNYEIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPREKKlGLGTAYIHGIKH 108
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYP---KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENG-GKAGALNAGLRH 76
                         90
                 ....*....|..
gi 851329401 109 ATGNYVIIMDAD 120
Cdd:cd06423   77 AKGDIVVVLDAD 88
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
29-153 1.90e-14

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: 70.01  E-value: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  29 VLLPTYNERENLPLivwlLVKSFSesAINY-----EIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPREKKL-GLGTAY 102
Cdd:cd04192    1 VVIAARNEAENLPR----LLQSLS--ALDYpkekfEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNSRVSIsGKKNAL 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 851329401 103 IHGIKHATGNYVIIMDADLSHHPKFIPEFIRK-QKEGNFDIVSGTRYKGNGG 153
Cdd:cd04192   75 TTAIKAAKGDWIVTTDADCVVPSNWLLTFVAFiQKEQIGLVAGPVIYFKGKS 126
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
28-157 7.29e-13

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: 65.72  E-value: 7.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  28 SVLLPTYNERENLP-LIVWLLVKSFSESaiNYEIIIIDDGSPDGTREVAEQLAEIYgpDRILLRPREKKLgLGTAYIHGI 106
Cdd:cd02525    3 SIIIPVRNEEKYIEeLLESLLNQSYPKD--LIEIIVVDGGSTDGTREIVQEYAAKD--PRIRLIDNPKRI-QSAGLNIGI 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 851329401 107 KHATGNYVIIMDADlSHHPK-FIPEFIRKQKEGNFDIVSGTRYKGNGGVYGW 157
Cdd:cd02525   78 RNSRGDIIIRVDAH-AVYPKdYILELVEALKRTGADNVGGPMETIGESKFQK 128
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
26-120 1.65e-12

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


Pssm-ID: 224136 [Multi-domain]  Cd Length: 439  Bit Score: 66.11  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  26 KYSVLLPTYNERENLplivwllVKSFSESAIN-----YEIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPREKKLGLGT 100
Cdd:COG1215   55 KVSVIIPAYNEEPEV-------LEETLESLLSqdyprYEVIVVDDGSTDETYEILEELGAEYGPNFRVIYPEKKNGGKAG 127
                         90       100
                 ....*....|....*....|
gi 851329401 101 AYIHGIKHATGNYVIIMDAD 120
Cdd:COG1215  128 ALNNGLKRAKGDVVVILDAD 147
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
28-171 5.14e-12

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: 63.08  E-value: 5.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  28 SVLLPTYNERENLP--LivwllvksfsESAINY--EIIIIDDGSPDGTREVAEQL-AEIYgpdrillrpREKKLGLGTAY 102
Cdd:cd02511    3 SVVIITKNEERNIErcL----------ESVKWAvdEIIVVDSGSTDRTVEIAKEYgAKVY---------QRWWDGFGAQR 63
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 851329401 103 IHGIKHATGNYVIIMDAD--LShhPKFIPEFIRKQKEGNFDIVSGTR---YKGNGGVYGWDLKRKIIRLYRKEV 171
Cdd:cd02511   64 NFALELATNDWVLSLDADerLT--PELADEILALLATDDYDGYYVPRrnfFLGRWIRHGGWYPDRQLRLFRRGK 135
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
29-149 1.24e-11

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: 61.44  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  29 VLLPTYNERENLPLIVWLLVksfSESAINYEIIIIDDGSPDGTREVAEQLAE--------IYGPDrillrprekkLGLGT 100
Cdd:cd06420    1 LIITTYNRPEALELVLKSVL---NQSILPFEVIIADDGSTEETKELIEEFKSqfpipikhVWQED----------EGFRK 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 851329401 101 AYI--HGIKHATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFdiVSGTRYK 149
Cdd:cd06420   68 AKIrnKAIAAAKGDYLIFIDGDCIPHPDFIADHIELAEPGVF--LSGSRVL 116
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
28-122 5.54e-11

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 61.32  E-value: 5.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  28 SVLLPTYNERENLPL-----IVWLLVKSFSESAINYEIIIIDDGSPDGTREVAEQLAEIYGPDRILLR--PREKKLGLGT 100
Cdd:PTZ00260  73 SIVIPAYNEEDRLPKmlketIKYLESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINPNIDIRllSLLRNKGKGG 152
                         90       100
                 ....*....|....*....|..
gi 851329401 101 AYIHGIKHATGNYVIIMDADLS 122
Cdd:PTZ00260 153 AVRIGMLASRGKYILMVDADGA 174
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
28-120 2.48e-10

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: 58.03  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  28 SVLLPTYN-ERenlplivWLL--VKS-FSESAINYEIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPrEKKLGLGTAYI 103
Cdd:cd04196    1 AVLMATYNgEK-------YLReqLDSiLAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRN-GKNLGVARNFE 72
                         90
                 ....*....|....*..
gi 851329401 104 HGIKHATGNYVIIMDAD 120
Cdd:cd04196   73 SLLQAADGDYVFFCDQD 89
PRK10073 PRK10073
putative glycosyl transferase; Provisional
26-172 1.16e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 57.36  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  26 KYSVLLPTYNERENLPlivwllvkSFSESAI-----NYEIIIIDDGSPDGTREVAEQLAEIYGPDRILlrpREKKLGLGT 100
Cdd:PRK10073   7 KLSIIIPLYNAGKDFR--------AFMESLIaqtwtALEIIIVNDGSTDNSVEIAKHYAENYPHVRLL---HQANAGVSV 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 851329401 101 AYIHGIKHATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVS--GTRYKGNGGVygwdlKRKII---RLYRKEVL 172
Cdd:PRK10073  76 ARNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQcnADWCFRDTGE-----TWQSIpsdRLRSTGVL 147
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
24-130 3.65e-09

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: 55.07  E-value: 3.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401   24 QDKYSVLLPTYNERENL-PLIVWLLVKSFsesaINYEIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPREKKLGLG--- 99
Cdd:pfam13641   1 PPDVSVVVPAFNEDSVLgRVLEAILAQPY----PPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTgks 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 851329401  100 TAYIHGIKHATGNYVIIMDADLSHHPKFIPE 130
Cdd:pfam13641  77 RGLNHGFRAVKSDLVVLHDDDSVLHPGTLKK 107
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
29-205 1.45e-08

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: 52.56  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  29 VLLPTYNERENLPLivwlLVKSF-SESAINYEIIIIDDGSPDGTREVAEQlaeiYGPDRILLRPrEKKLGLGTAYIHGIK 107
Cdd:cd04186    1 IIIVNYNSLEYLKA----CLDSLlAQTYPDFEVIVVDNASTDGSVELLRE----LFPEVRLIRN-GENLGFGAGNNQGIR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 108 HATGNYVIIMDADLSHHPKFIPEFIRK-QKEGNFDIVSGtryKGNGGVYgwdlkrkiirLYRKEVLQKLiekcvskGY-- 184
Cdd:cd04186   72 EAKGDYVLLLNPDTVVEPGALLELLDAaEQDPDVGIVGP---KVSGAFL----------LVRREVFEEV-------GGfd 131
                        170       180
                 ....*....|....*....|....*..
gi 851329401 185 -VFQM-----EMIVRARQMNYTIGEVP 205
Cdd:cd04186  132 eDFFLyyedvDLCLRARLAGYRVLYVP 158
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
9-120 2.08e-08

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: 52.97  E-value: 2.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401   9 SLAASPRPPQGRSSRQDKYSVLLPTYNEREnlplivWLLVKSFSESAINY-----EIIIIDDGSPDGTREVAEQlaeiYG 83
Cdd:cd06439   13 ARLRPKPPSLPDPAYLPTVTIIIPAYNEEA------VIEAKLENLLALDYprdrlEIIVVSDGSTDGTAEIARE----YA 82
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 851329401  84 PDRILLRPREKKLGLGTAYIHGIKHATGNYVIIMDAD 120
Cdd:cd06439   83 DKGVKLLRFPERRGKAAALNRALALATGEIVVFTDAN 119
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
28-217 2.04e-07

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: 49.85  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  28 SVLLPTYNERENLPLivwlLVKS-FSESAINYEIIIIDDGSPDGTREVAEQlaeiYGPDRILLRpREKKLGLGTAYIHGI 106
Cdd:cd06433    1 SIITPTYNQAETLEE----TIDSvLSQTYPNIEYIVIDGGSTDGTVDIIKK----YEDKITYWI-SEPDKGIYDAMNKGI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401 107 KHATGNYVIIMDADLSHHPKFIPEFIRK-QKEGNFDIVSG--TRYKGNGGVYG------WDLKRKIIR--------LYRK 169
Cdd:cd06433   72 ALATGDIIGFLNSDDTLLPGALLAVVAAfAEHPEVDVVYGdvLLVDENGRVIGrrrpppFLDKFLLYGmpichqatFFRR 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 851329401 170 EVLQKLieKCVSKGYVFQM--EMIVRARQMNYTIGEVPISFVD-RVYGESK 217
Cdd:cd06433  152 SLFEKY--GGFDESYRIAAdyDLLLRLLLAGKIFKYLPEVLAAfRLGGVSS 200
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
28-129 4.48e-07

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 49.53  E-value: 4.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  28 SVLLPTYNERENLPLIVWLLVKSFSESAINyEIIIIDDGSPDGTREVAEQL-AEIYGPDRIL--LRPREKKlglGTAYIH 104
Cdd:PRK13915  34 SVVLPALNEEETVGKVVDSIRPLLMEPLVD-ELIVIDSGSTDATAERAAAAgARVVSREEILpeLPPRPGK---GEALWR 109
                         90       100
                 ....*....|....*....|....*.
gi 851329401 105 GIKHATGNYVIIMDADL-SHHPKFIP 129
Cdd:PRK13915 110 SLAATTGDIVVFVDADLiNFDPMFVP 135
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
28-146 5.64e-07

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 48.47  E-value: 5.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  28 SVLLPTYNeRENLPLIVWLLVKSFSESAINYEIIIIDDGS-PDGTREVAEQLAEIYGPDRILLrprEKKLGLGTAYIHGI 106
Cdd:cd04195    1 SVLMSVYI-KEKPEFLREALESILKQTLPPDEVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPL---EKNRGLGKALNEGL 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 851329401 107 KHATGNYVIIMDADLSHHP----KFIPEFirkQKEGNFDIVSGT 146
Cdd:cd04195   77 KHCTYDWVARMDTDDISLPdrfeKQLDFI---EKNPEIDIVGGG 117
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
27-120 6.70e-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: 48.34  E-value: 6.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  27 YSVLLPTYNERENLPLivwlLVKSFSESA-INYEIIIIDDGSPDGTREVAEQLAEiygpdrillRPREKKLGLGTAYIHG 105
Cdd:cd02522    1 LSIIIPTLNEAENLPR----LLASLRRLNpLPLEIIVVDGGSTDGTVAIARSAGV---------VVISSPKGRARQMNAG 67
                         90
                 ....*....|....*
gi 851329401 106 IKHATGNYVIIMDAD 120
Cdd:cd02522   68 AAAARGDWLLFLHAD 82
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
28-120 7.04e-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: 48.35  E-value: 7.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  28 SVLLPTYNerenlPLIVWL--LVKSF-SESAINYEIIIIDDGSPDgtREVAEQLAEIYGPD-RILLRPREKKLGLGTAYI 103
Cdd:cd04184    4 SIVMPVYN-----TPEKYLreAIESVrAQTYPNWELCIADDASTD--PEVKRVLKKYAAQDpRIKVVFREENGGISAATN 76
                         90
                 ....*....|....*..
gi 851329401 104 HGIKHATGNYVIIMDAD 120
Cdd:cd04184   77 SALELATGEFVALLDHD 93
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
59-165 1.33e-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: 47.24  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  59 EIIIIDDGSPDGTREVaeqLAEIYGPDRILLRPREKKLGlGTAYIH-GIKHA--TG-NYVIIMDADLSHHPKFIPEFIRK 134
Cdd:cd04185   28 HIIVIDNASTDGTAEW---LTSLGDLDNIVYLRLPENLG-GAGGFYeGVRRAyeLGyDWIWLMDDDAIPDPDALEKLLAY 103
                         90       100       110
                 ....*....|....*....|....*....|.
gi 851329401 135 QKEGNFDIVSGTRYKGNGGVYGWDLKRKIIR 165
Cdd:cd04185  104 ADKDNPQFLAPLVLDPDGSFVGVLISRRVVE 134
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
29-134 2.04e-06

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 47.18  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  29 VLLPTYNERENLPLIVWLLVKsfsesAINY-----EIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPREK-KLGlgtAY 102
Cdd:cd06421    5 VFIPTYNEPLEIVRKTLRAAL-----AIDYphdklRVYVLDDGRRPELRALAAELGVEYGYRYLTRPDNRHaKAG---NL 76
                         90       100       110
                 ....*....|....*....|....*....|..
gi 851329401 103 IHGIKHATGNYVIIMDADlsHHPKfiPEFIRK 134
Cdd:cd06421   77 NNALAHTTGDFVAILDAD--HVPT--PDFLRR 104
GT2 COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
28-137 2.89e-06

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 224137 [Multi-domain]  Cd Length: 305  Bit Score: 47.09  E-value: 2.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  28 SVLLPTYNERENLplivwllVKSFSE-SAINY---EIIIIDDGSPDGTREVaeqLAEIYGPDRILLRPREkKLGLGTAYI 103
Cdd:COG1216    6 SIIIVTYNRGEDL-------VECLASlAAQTYpddVIVVVDNGSTDGSLEA---LKARFFPNVRLIENGE-NLGFAGGFN 74
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 851329401 104 HGIKHATGN---YVIIMDADLSHHPKFIPEFIRKQKE 137
Cdd:COG1216   75 RGIKYALAKgddYVLLLNPDTVVEPDLLEELLKAAEE 111
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
28-134 1.18e-05

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


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 44.99  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  28 SVLLPTYNEREnlplIVWLLVKSfsESAINY-----EIIIIDDgSPDGTREVAEQLAEIY---GPDrILLRPREKKLGL- 98
Cdd:cd06437    4 TVQLPVFNEKY----VVERLIEA--ACALDYpkdrlEIQVLDD-STDETVRLAREIVEEYaaqGVN-IKHVRRADRTGYk 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 851329401  99 GTAYIHGIKHATGNYVIIMDADLShhPKfiPEFIRK 134
Cdd:cd06437   76 AGALAEGMKVAKGEYVAIFDADFV--PP--PDFLQK 107
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
28-120 1.21e-05

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 45.35  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401   28 SVLLPTYNERENLPLIVWLLVKSFSESAiNYEIIIIDDGSPDGTREVAEQLAE----IYGPDRillrpREKKLGLGTAYI 103
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQERILNQTFQYDP-EFELIIINDGSTDKTLEEVSSIKDhnlqVYYPNA-----PDTTYSLAASRN 74
                          90
                  ....*....|....*..
gi 851329401  104 HGIKHATGNYVIIMDAD 120
Cdd:pfam10111  75 RGTSHAIGEYISFIDGD 91
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
28-130 4.92e-04

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 39.93  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  28 SVLLPTYNERENLplivwllVKSFSESAIN---YEIIIIDDGSpdgTREVAEQLAEI--YGPDRILLRPREKKLGlgtAY 102
Cdd:cd06434    3 TVIIPVYDEDPDV-------FRECLRSILRqkpLEIIVVTDGD---DEPYLSILSQTvkYGGIFVITVPHPGKRR---AL 69
                         90       100
                 ....*....|....*....|....*...
gi 851329401 103 IHGIKHATGNYVIIMDADLSHHPKFIPE 130
Cdd:cd06434   70 AEGIRHVTTDIVVLLDSDTVWPPNALPE 97
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
59-119 4.95e-04

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


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 40.27  E-value: 4.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 851329401  59 EIIIIDDGSPDGtrEVAEQLAEIY--GPDRILLRPREKKLGLGTAYIHGIKHATGNYVIIMDA 119
Cdd:cd02510   32 EIILVDDFSDKP--ELKLLLEEYYkkYLPKVKVLRLKKREGLIRARIAGARAATGDVLVFLDS 92
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
59-142 2.65e-03

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


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 38.03  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851329401  59 EIIIIDDGSpdgtREVAEQLAEIYGPDRILLRPREKkLGLGTAYIHGIKHATGN---YVIIMDADLSHHPKFIPEFI--R 133
Cdd:cd02526   26 KVVVVDNSS----GNDIELRLRLNSEKIELIHLGEN-LGIAKALNIGIKAALENgadYVLLFDQDSVPPPDMVEKLLayK 100

                 ....*....
gi 851329401 134 KQKEGNFDI 142
Cdd:cd02526  101 ILSDKNSNI 109
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH