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Conserved domains on  [gi|446626294|ref|WP_000703640|]
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MULTISPECIES: glycosyltransferase family 2 protein [Salmonella]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135621)

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

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  12691742|9445404|16037492|10521532
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 5-185 3.73e-85

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: 253.55  E-value: 3.73e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   5 LVVPVFNEEDTIPIFYKTVREFNELKEYEIEIVFINDGSKDATESIINKIAASDPLVIPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294  85 GDAVIPIDVDLQDPIEVIPHLIEKWQAGADMVLAKRSDRStDGRMKRKTAEWFYKLHNKISNPKIEENVGDFRLMSRAVV 164
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159

                        170       180
                 ....*....|....*....|.
gi 446626294 165 ENIKQMPERNLFMKGVLSWVG 185
Cdd:cd04187  160 DALLLLPERHRFLRGLIAWVG 180
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 5-185 3.73e-85

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: 253.55  E-value: 3.73e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   5 LVVPVFNEEDTIPIFYKTVREFNELKEYEIEIVFINDGSKDATESIINKIAASDPLVIPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294  85 GDAVIPIDVDLQDPIEVIPHLIEKWQAGADMVLAKRSDRStDGRMKRKTAEWFYKLHNKISNPKIEENVGDFRLMSRAVV 164
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159

                        170       180
                 ....*....|....*....|.
gi 446626294 165 ENIKQMPERNLFMKGVLSWVG 185
Cdd:cd04187  160 DALLLLPERHRFLRGLIAWVG 180
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 2-303 1.19e-55

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 183.01  E-value: 1.19e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   2 KISLVVPVFNEEDTIPIFYKTVREFNELKEYEIEIVFINDGSKDATESIINKIA-ASDPLVIPLSFTRNFGKEPALFAGL 80
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAqAPDSHIVAILLNRNYGQHSAIMAGF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294  81 DHATGDAVIPIDVDLQDPIEVIPHLIEKWQAGADMVLAKRSDRSTdgrmkrktaEWFYKLHNKISNPKIE----ENVGDF 156
Cdd:PRK10714  87 SHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQD---------SWFRKTASKMINRLIQrttgKAMGDY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294 157 RLMSRA----VVENIKQMPERNLFMKGVLSWVGGKTDVVKYARAERVAGDSKFNGWKLWNLALEGITSFSTFPLRIWTYI 232
Cdd:PRK10714 158 GCMLRAyrrhIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLL 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446626294 233 GLFIAGMSFLYGAWMIIDKLIFGNNVPGYPS-LLVSVLFLG-GVQLIGIGILGEYIGRIYIETKQRPKYILKR 303
Cdd:PRK10714 238 GSIIAIGGFSLAVLLVVLRLTFGPQWAAEGVfMLFAVLFTFiGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQ 310
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-214 5.78e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 141.38  E-value: 5.78e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   1 MKISLVVPVFNEEDTIPifyKTVREFNELKEYEIEIVFINDGSKDATESIINKIAASDPLVIPLSFTRNFGKEPALFAGL 80
Cdd:COG0463    2 PLVSVVIPTYNEEEYLE---EALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294  81 DHATGDAVIPIDVDLQDPIEVIPHLIEKWQA-GADMVLAKRSDRSTDGRMKRKTAEWFYkLHNKISNpkIEENVGDFRLM 159
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLTN--LPDSTSGFRLF 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446626294 160 SRAVVENIKqMPERNLFMKGVL--SWVGGKTDVVKYARAErvaGDSKFNGWKLWNLA 214
Cdd:COG0463  156 RREVLEELG-FDEGFLEDTELLraLRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-165 4.72e-30

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: 111.72  E-value: 4.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294    4 SLVVPVFNEEDTIPIFYKTVREfneLKEYEIEIVFINDGSKDATESIINKIAASDPLVIPLSFTRNFGKEPALFAGLDHA 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN---QTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   84 TGDAVIPIDVDLQDPIEVIPHLIEKWQA-GADMVLAKR--SDRSTDGRMKRKTAEW---FYKLHNKISNPKIEENVGDFR 157
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRyvIFGETGEYRRASRITLsrlPFFLGLRLLGLNLPFLIGGFA 157


                  ....*...
gi 446626294  158 LMSRAVVE 165
Cdd:pfam00535 158 LYRREALE 165
 
Name Accession Description Interval E-value
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 5-185 3.73e-85

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: 253.55  E-value: 3.73e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   5 LVVPVFNEEDTIPIFYKTVREFNELKEYEIEIVFINDGSKDATESIINKIAASDPLVIPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294  85 GDAVIPIDVDLQDPIEVIPHLIEKWQAGADMVLAKRSDRStDGRMKRKTAEWFYKLHNKISNPKIEENVGDFRLMSRAVV 164
Cdd:cd04187   81 GDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRK-ESWLKRLTSKLFYRLINKLSGVDIPDNGGDFRLMDRKVV 159

                        170       180
                 ....*....|....*....|.
gi 446626294 165 ENIKQMPERNLFMKGVLSWVG 185
Cdd:cd04187  160 DALLLLPERHRFLRGLIAWVG 180
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 5-185 2.25e-58

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: 2.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   5 LVVPVFNEEDTIPIFYKTVREFNElKEYEIEIVFINDGSKDATESIINKIAASDPLVIPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLE-EGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294  85 GDAVIPIDVDLQDPIEVIPHLIEK-WQAGADMVLAKRSDRSTDGRM---KRKTAEWFYKLHNKISNPKIEENVGDFRLMS 160
Cdd:cd04179   80 GDIVVTMDADLQHPPEDIPKLLEKlLEGGADVVIGSRFVRGGGAGMpllRRLGSRLFNFLIRLLLGVRISDTQSGFRLFR 159

                        170       180
                 ....*....|....*....|....*
gi 446626294 161 RAVVENIKQMPERNLFMKGVLSWVG 185
Cdd:cd04179  160 REVLEALLSLLESNGFEFGLELLVG 184
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 2-303 1.19e-55

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 183.01  E-value: 1.19e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   2 KISLVVPVFNEEDTIPIFYKTVREFNELKEYEIEIVFINDGSKDATESIINKIA-ASDPLVIPLSFTRNFGKEPALFAGL 80
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAqAPDSHIVAILLNRNYGQHSAIMAGF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294  81 DHATGDAVIPIDVDLQDPIEVIPHLIEKWQAGADMVLAKRSDRSTdgrmkrktaEWFYKLHNKISNPKIE----ENVGDF 156
Cdd:PRK10714  87 SHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQD---------SWFRKTASKMINRLIQrttgKAMGDY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294 157 RLMSRA----VVENIKQMPERNLFMKGVLSWVGGKTDVVKYARAERVAGDSKFNGWKLWNLALEGITSFSTFPLRIWTYI 232
Cdd:PRK10714 158 GCMLRAyrrhIVDAMLHCHERSTFIPILANTFARRAIEIPVHHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSLL 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446626294 233 GLFIAGMSFLYGAWMIIDKLIFGNNVPGYPS-LLVSVLFLG-GVQLIGIGILGEYIGRIYIETKQRPKYILKR 303
Cdd:PRK10714 238 GSIIAIGGFSLAVLLVVLRLTFGPQWAAEGVfMLFAVLFTFiGAQFIGMGLLGEYIGRIYNDVRARPRYFVQQ 310
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-214 5.78e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 141.38  E-value: 5.78e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   1 MKISLVVPVFNEEDTIPifyKTVREFNELKEYEIEIVFINDGSKDATESIINKIAASDPLVIPLSFTRNFGKEPALFAGL 80
Cdd:COG0463    2 PLVSVVIPTYNEEEYLE---EALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294  81 DHATGDAVIPIDVDLQDPIEVIPHLIEKWQA-GADMVLAKRSDRSTDGRMKRKTAEWFYkLHNKISNpkIEENVGDFRLM 159
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALEEgPADLVYGSRLIREGESDLRRLGSRLFN-LVRLLTN--LPDSTSGFRLF 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446626294 160 SRAVVENIKqMPERNLFMKGVL--SWVGGKTDVVKYARAErvaGDSKFNGWKLWNLA 214
Cdd:COG0463  156 RREVLEELG-FDEGFLEDTELLraLRHGFRIAEVPVRYRA---GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-165 4.72e-30

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: 111.72  E-value: 4.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294    4 SLVVPVFNEEDTIPIFYKTVREfneLKEYEIEIVFINDGSKDATESIINKIAASDPLVIPLSFTRNFGKEPALFAGLDHA 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN---QTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   84 TGDAVIPIDVDLQDPIEVIPHLIEKWQA-GADMVLAKR--SDRSTDGRMKRKTAEW---FYKLHNKISNPKIEENVGDFR 157
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEdGADVVVGSRyvIFGETGEYRRASRITLsrlPFFLGLRLLGLNLPFLIGGFA 157


                  ....*...
gi 446626294  158 LMSRAVVE 165
Cdd:pfam00535 158 LYRREALE 165
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 5-132 3.10e-20

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: 86.85  E-value: 3.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   5 LVVPVFNEEDTIPIFYKTVREF-NELKEYEIEIVFINDGSKDATESIINKIAASDPLVIP-LSFTRNFGKEPALFAGLDH 82
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYlEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRvLTLPKNRGKGGAVRAGMLA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446626294  83 ATGDAVIPIDVDLQDPIEVIPHLIE-KWQAGADMVLAKRSDRSTDGRMKRK 132
Cdd:cd04188   81 ARGDYILFADADLATPFEELEKLEEaLKTSGYDIAIGSRAHLASAAVVKRS 131
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 5-212 2.49e-19

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: 84.51  E-value: 2.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   5 LVVPVFNEEDTIPIFykTVREFNELKEYEIEIVFINDGSKDATESIINKIAASDPLVIPLSFTRNFGKEPALFAGLDHAT 84
Cdd:cd06442    1 IIIPTYNERENIPEL--IERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294  85 GDAVIPIDVDLQDPIEVIPHLIEK-WQAGADMVLAKR--SDRSTDGR-MKRK----TAEWFYKLhnkISNPKIEENVGDF 156
Cdd:cd06442   79 GDVIVVMDADLSHPPEYIPELLEAqLEGGADLVIGSRyvEGGGVEGWgLKRKlisrGANLLARL---LLGRKVSDPTSGF 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446626294 157 RLMSRAVVENIKQmperNLFMKG--------VLSWVGGKTDV-VKYARAERVAGDSKFNGWKLWN 212
Cdd:cd06442  156 RAYRREVLEKLID----SLVSKGykfqlellVRARRLGYRIVeVPITFVDREHGESKLGGKEIVE 216
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-109 2.35e-15

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


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 72.15  E-value: 2.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   6 VVPVFNEEDTIPIFYKTVREfneLKEYEIEIVFINDGSKDATESIINKIAASDPLVIPLSFTRNFGKEPALFAGLDHATG 85
Cdd:cd00761    2 IIPAYNEEPYLERCLESLLA---QTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARG 78

                         90       100
                 ....*....|....*....|....
gi 446626294  86 DAVIPIDVDlqdpIEVIPHLIEKW 109
Cdd:cd00761   79 EYILFLDAD----DLLLPDWLERL 98
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 1-94 8.33e-15

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 73.24  E-value: 8.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   1 MKISLVVPVFNEEDTIPifyKTVREFNELK--EYEIEIVFINDGSKDATESIINKIAASDPLVIPLSFTRNFGKEPALFA 78
Cdd:COG1215   29 PRVSVIIPAYNEEAVIE---ETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNA 105

                         90
                 ....*....|....*.
gi 446626294  79 GLDHATGDAVIPIDVD 94
Cdd:COG1215  106 GLKAARGDIVVFLDAD 121
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-167 1.12e-14

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 72.04  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   1 MKISLVVPVFNEEDTIPIFYKTVRE-FNELKEYEIeiVFINDGSKDATESIINKIAAS--DPLVIPLSFTRNFGKEPALF 77
Cdd:PLN02726   9 MKYSIIVPTYNERLNIALIVYLIFKaLQDVKDFEI--IVVDDGSPDGTQDVVKQLQKVygEDRILLRPRPGKLGLGTAYI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294  78 AGLDHATGDAVIPIDVDLQDPIEVIPHLIEKWQA-GADMVLAKRSdRSTDG----RMKRK-TAEWFYKLHNKISNPKIEE 151
Cdd:PLN02726  87 HGLKHASGDFVVIMDADLSHHPKYLPSFIKKQREtGADIVTGTRY-VKGGGvhgwDLRRKlTSRGANVLAQTLLWPGVSD 165

                        170
                 ....*....|....*.
gi 446626294 152 NVGDFRLMSRAVVENI 167
Cdd:PLN02726 166 LTGSFRLYKRSALEDL 181
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 5-94 1.25e-10

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: 59.55  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   5 LVVPVFNEEDTIPifyKTVREFNELKEYEIEIVFINDGSKDATESIINKIAASDP---LVIPLSftRNFGKEPALFAGLD 81
Cdd:cd06423    1 IIVPAYNEEAVIE---RTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIrrvLVVRDK--ENGGKAGALNAGLR 75

                         90
                 ....*....|...
gi 446626294  82 HATGDAVIPIDVD 94
Cdd:cd06423   76 HAKGDIVVVLDAD 88
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 3-167 1.95e-10

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 60.94  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   3 ISLVVPVFNEEDTIPIFYK-TVREFNELKE----YEIEIVFINDGSKDATESI-----INKIAASDPLVIpLSFTRNFGK 72
Cdd:PTZ00260  72 LSIVIPAYNEEDRLPKMLKeTIKYLESRSRkdpkFKYEIIIVNDGSKDKTLKVakdfwRQNINPNIDIRL-LSLLRNKGK 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294  73 EPALFAGLDHATGDAVIPIDVDLQDPIE----VIPHLIEKWQAGADMVLAKRSD-RSTDGRMKRK-----TAEWFYKLHN 142
Cdd:PTZ00260 151 GGAVRIGMLASRGKYILMVDADGATDIDdfdkLEDIMLKIEQNGLGIVFGSRNHlVDSDVVAKRKwyrniLMYGFHFIVN 230

                        170       180
                 ....*....|....*....|....*
gi 446626294 143 KISNPKIEENVGDFRLMSRAVVENI 167
Cdd:PTZ00260 231 TICGTNLKDTQCGFKLFTRETARII 255
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 2-94 3.36e-10

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


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 59.52  E-value: 3.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   2 KISLVVPVFNEEDTIPifyKTVREFNELkEY---EIEIVFINDGSKDATESIINKIAASDPLVIplSFTRNFGKEPALFA 78
Cdd:cd06439   30 TVTIIIPAYNEEAVIE---AKLENLLAL-DYprdRLEIIVVSDGSTDGTAEIAREYADKGVKLL--RFPERRGKAAALNR 103

                         90
                 ....*....|....*.
gi 446626294  79 GLDHATGDAVIPIDVD 94
Cdd:cd06439  104 ALALATGEIVVFTDAN 119
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-117 6.20e-09

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 55.00  E-value: 6.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   1 MKISLVVPVFNEEDTIPifyKTVREFNELKEYEIEIVFINDGSKDATESIINKIAASDPLVIPLSFTRNFGKepALFAGL 80
Cdd:COG1216    3 PKVSVVIPTYNRPELLR---RCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRVRVIRNPENLGFAA--ARNLGL 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446626294  81 DHATGDAVIPIDVDlqdpIEVIPHLIEKWQAGADMVL 117
Cdd:COG1216   78 RAAGGDYLLFLDDD----TVVEPDWLERLLAAACLLI 110
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 2-116 3.36e-07

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: 50.31  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   2 KISLVVPVFNEEDTIPifyKTVREFNElKEYE---IEIVFINDGSKDATESIINKIAASDPLVIPLSftrNFGK--EPAL 76
Cdd:cd02525    1 FVSIIIPVRNEEKYIE---ELLESLLN-QSYPkdlIEIIVVDGGSTDGTREIVQEYAAKDPRIRLID---NPKRiqSAGL 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446626294  77 FAGLDHATGDAVIPIDVDLQDPIEVIPHLIEKWQA-GADMV 116
Cdd:cd02525   74 NIGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRtGADNV 114
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 3-86 6.55e-07

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


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 49.11  E-value: 6.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   3 ISLVVPVFNEEDTIPifyKTVREFNELKEYEIEIVFINDGSKDATESIinkiaASDPLVIPLSFTRNFGKEpaLFAGLDH 82
Cdd:cd02522    1 LSIIIPTLNEAENLP---RLLASLRRLNPLPLEIIVVDGGSTDGTVAI-----ARSAGVVVISSPKGRARQ--MNAGAAA 70


                 ....
gi 446626294  83 ATGD 86
Cdd:cd02522   71 ARGD 74
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 1-98 2.26e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 48.38  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   1 MKISLVVPVFNEEDTIPIFYKTVREfnELKEYEI-EIVFINDGSKDATESIINK-----IAASD--PLVIPLSftrnfGK 72
Cdd:PRK13915  31 RTVSVVLPALNEEETVGKVVDSIRP--LLMEPLVdELIVIDSGSTDATAERAAAagarvVSREEilPELPPRP-----GK 103

                         90       100
                 ....*....|....*....|....*.
gi 446626294  73 EPALFAGLDHATGDAVIPIDVDLQDP 98
Cdd:PRK13915 104 GEALWRSLAATTGDIVVFVDADLINF 129
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-98 3.75e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 44.20  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   5 LVVPVFNEEDTIPIFYKTVREFNELKEyEIEIVFINDGSKDATESIINKIAA-SDPLVIPLSFTR--NFGKEPALFAGLD 81
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYPKE-KFEVILVDDHSTDGTVQILEFAAAkPNFQLKILNNSRvsISGKKNALTTAIK 79

                         90
                 ....*....|....*..
gi 446626294  82 HATGDAVIPIDVDLQDP 98
Cdd:cd04192   80 AAKGDWIVTTDADCVVP 96
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-107 4.01e-05

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 44.65  E-value: 4.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   2 KISLVVPVFNEEDTIPIFyktvreFNELKEYEI---EIVFINDGSKDATESIINKIAASDPLVIPLSfTRNFGKEPALFA 78
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAF------MESLIAQTWtalEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNT 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 446626294  79 GLDHATGDAVIPIDV-DLQDPiEVIPHLIE 107
Cdd:PRK10073  80 GLAVATGKYVAFPDAdDVVYP-TMYETLMT 108
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 2-110 9.34e-05

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: 43.05  E-value: 9.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294   2 KISLVVPVFNEEDTIPIFYKTVREFNElkeyeiEIVFINDGSKDATESIINKIAASdplVIPLSFtRNFGkePALFAGLD 81
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVD------EIIVVDSGSTDRTVEIAKEYGAK---VYQRWW-DGFG--AQRNFALE 68

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446626294  82 HATGDAVIPIDVD---LQDPIEVIPHLIEKWQ 110
Cdd:cd02511   69 LATNDWVLSLDADerlTPELADEILALLATDD 100
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-94 3.30e-04

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: 41.49  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626294    4 SLVVPVFNEEDTiPIFYKTVREFNELKEYEIEIVFINDGSKDATESIINKIAASDPLV-IPLSFTRNFGKEPALFAGLDH 82
Cdd:pfam10111   1 SVVIPVYNGEKT-HWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVyYPNAPDTTYSLAASRNRGTSH 79

                          90
                  ....*....|..
gi 446626294   83 ATGDAVIPIDVD 94
Cdd:pfam10111  80 AIGEYISFIDGD 91
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 41-88 2.51e-03

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 38.38  E-value: 2.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446626294  41 DGSKDATESIINKIAASDPLVI-------PLSFTRNFgkepalFAGLDHATGDAV 88
Cdd:cd04196   35 DGSTDGTVEIIKEYIDKDPFIIilirngkNLGVARNF------ESLLQAADGDYV 83
 
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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