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Conserved domains on  [gi|334183827|ref|NP_001185370|]
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EMS-MUTAGENIZED BRI1 SUPPRESSOR 1 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_transf_24 pfam18404
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ...
1302-1569 0e+00

Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT). This domain belongs to glucosyltransferase 24 family (GT24) A-type domain. The GT domain displays the expected glycosyltransferase type A (GT-A) fold.


:

Pssm-ID: 436473  Cd Length: 268  Bit Score: 600.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1302 INIFSIASGHLYERFLKIMILSVLKNTNRPVKFWFIKNYLSPQFKDVIPHMAQEYNFEYELITYKWPSWLHKQKEKQRII 1381
Cdd:pfam18404    1 INIFSVASGHLYERFLKIMMLSVRKNTKSPVKFWFIENFLSPSFKAFLPHLAKEYGFEYELVTYKWPSWLRKQTEKQRII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1382 WAYKILFLDVIFPLSLEKVIFVDADQIIRTDMGELYDMDIKGRPLAYTPFCDNNREMDGYKFWKQGFWKEHLRGRPYHIS 1461
Cdd:pfam18404   81 WGYKILFLDVLFPLDLDKVIFVDADQVVRTDLKELVDMDLEGAPYGYTPMCDSRKEMEGFRFWKQGYWKDHLRGRPYHIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1462 ALYVVDLVKFRETAAGDNLRVFYETLSKDPNSLSNLDQDLPNYAQHTVPIFSLPQEWLWCESWCGNATKAKARTIDLCNN 1541
Cdd:pfam18404  161 ALYVVDLKRFRQMAAGDRLRSHYQQLSADPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESLKKAKTIDLCNN 240
                          250       260
                   ....*....|....*....|....*...
gi 334183827  1542 PMTKEPKLQGARRIVTEWPDLDLEARKF 1569
Cdd:pfam18404  241 PLTKEPKLDRAKRIIPEWTDYDEEVAAL 268
Thioredoxin_14 pfam18402
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in ...
452-722 9.22e-61

Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).


:

Pssm-ID: 465750  Cd Length: 248  Bit Score: 208.67  E-value: 9.22e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   452 VDFRS-----VHVTYLNNLEEDDMYKRWRSNINEILMPAFPGQLRYIRKNLFHAVYVIDPAT-ACGLESIETLRSLYENQ 525
Cdd:pfam18402    1 FDIRDrieggGVIIWLNDLEKDKRYSRWPSSLQELLRPTYPGQLPPIRKNLFNLVLVVDLSQpEDLLLLVETLQSFVQRG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   526 LPVRFGVILYSTqliktiennggqipssdavtnaqvKEDLSTMVIRLFLYIKEHHGIQTAFQFLGNLntLRTESADSSEA 605
Cdd:pfam18402   81 IPVRFGLVPLVN------------------------STEDGLAQAKLFYYLLENYGLKAALSFLTAS--LYALAKKVLSP 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   606 DieQEHVDGAFVETILPkvktLPQDILLKLRQEHTLKEASEASSMFVFKLGLAKLKCSFLMNGLVFDSVE--EETLLNAM 683
Cdd:pfam18402  135 T--KAIFSSALKERTLR----PQALSFDEVLKSEVYDERLKKAKEYLKRLGLDSLSGPVFVNGVPLPRDEnwLQALSQRI 208
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 334183827   684 NEELPKIQEQVYYGQIESHTKVLDKLLSESG-LSRYNPQI 722
Cdd:pfam18402  209 SEDLQLLQKAVYEGALTDDDDVPDFFYDLPNaLPRRNPLI 248
Thioredoxin_12 pfam18400
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in ...
43-237 9.14e-59

Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).


:

Pssm-ID: 465748  Cd Length: 187  Bit Score: 200.54  E-value: 9.14e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827    43 GTPLLLEAGELISKESKQLFWEFTDAWLGSDGDDSDCKSARDCLLKISKQASTLLAQPVASLFHFSLTLRSASPRLVLYR 122
Cdd:pfam18400    1 ATPLLLEALETLAEENPDLFFPFLDALTNLDGEFADASTDEELYEAALKLASDHLSPLALSLFKLALSLRSASPRIEAFY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   123 QLADESLSSFPHGDDpsatgC-CWVDTGSSLFYDVADLQSWLASApavGDAVQGPELFDFDHVHFDSrAGSPVAVLYGAV 201
Cdd:pfam18400   81 QIYAESVSFEGAPPE-----CdSWVDWGGEVYCDPEDLDALLKSE---ASSRPQPELLPFDHVYPDS-GSSPVAILYADL 151
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 334183827   202 GTDCFRKFHLSLAKAAKEGKVTYVVRPVLPLGCEGK 237
Cdd:pfam18400  152 GSPNFREFHKYLSELAKDGKIRYVLRHVPPSGSESK 187
Thioredoxin_15 pfam18403
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose: ...
734-983 2.98e-38

Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).


:

Pssm-ID: 465751  Cd Length: 205  Bit Score: 142.36  E-value: 2.98e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   734 SLASSTRKGESMLNDVNYLHSPETSEDvkYVTHLLAADVATKKGMKLLHEGVRYLIGgSKSARLGVLFSSSQNADPHSLl 813
Cdd:pfam18403    1 DLNKLYSEHADLFDKMPYLEASSDKED--WATLWVVADLDSESGRKLLLSALEFRKS-NPGVRLGIIHNPASPSEASSL- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   814 fikfFEKTASSFSHKEKVLYFLDKLCLFYEREYllktsvesassqmfidkvleladeyglsskAYRSCLVESVDEELLKR 893
Cdd:pfam18403   77 ----ISSALLAALLKLKNLDALEFLTKLLEEEE------------------------------AAASESGKSSAEAAADY 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   894 LTKVAQFLSwELGLESDANAIISNGRVIFPVDE-RTFLGQDLHLLESMEFNQRVKPVQEIIEGIEWQDvdpdlltSKYFS 972
Cdd:pfam18403  123 WKALQPFLR-VLGLKPGQNALVLNGRVVGPIPEdEEFSADDFELLLSYERSKRIEPVYKAIEELGLED-------KISDP 194
                          250
                   ....*....|.
gi 334183827   973 DVFMFVSSAMA 983
Cdd:pfam18403  195 DAVAKLTSLVA 205
UDP-g_GGTase pfam06427
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ...
1144-1247 1.99e-35

UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded beta-sandwiches found in UDP-glucose-glycoprotein glucosyltransferase-like proteins. UDP-g_GGTase is an important, central component of the QC system in the ER for checking that glycoproteins are folded correctly. This QC prevents incorrectly folded glycoproteins from leaving the ER.


:

Pssm-ID: 461910  Cd Length: 109  Bit Score: 130.69  E-value: 1.99e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1144 GHCAEKDHEA-PRGLQLILGTKNRPHLVDTLVMANLGYWQMKVSPGVWYLQLAPGRSSELYALK--GGNDGSQDQSSLKR 1220
Cdd:pfam06427    2 GHARDVTTGSpPRGLQLVLGTEKNPHVADTIVMANLGYFQLKANPGVWKLELREGRSSDIYEIEsvGAEGWPSPGDEGTE 81
                           90       100
                   ....*....|....*....|....*..
gi 334183827  1221 ITIDDLRGKVVHLEVVKRKGKEHEKLL 1247
Cdd:pfam06427   82 VALTSFEGLTLYPRLSRKPGMENEDVL 108
Thioredoxin_13 pfam18401
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found ...
320-453 1.32e-29

Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).


:

Pssm-ID: 465749  Cd Length: 136  Bit Score: 114.97  E-value: 1.32e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   320 SSTVSDTLDVWELKDLGHQTAQRIVHASDPLQSMQEINQNFPSVVSSLSRMKLNESIKDEILSNQ-RMVPPGKALLALNG 398
Cdd:pfam18401    2 EVEDLKPLSVWELQDLGLQAAQFIMSSDDPLDTLLKLSQDFPKYASSLARHNVSDELREEIEENQeRLLPPGDNALWLNG 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 334183827   399 ALLNIEDIDLYMLMDLAHQELSLANHFSKLKIPDGAIRKLLLTTPLPEPDSYRVD 453
Cdd:pfam18401   82 LQLDERDIDPFSLLDILRRERKLINGLRKLGLSGSEAVDLLSHPALAAAQADSYD 136
 
Name Accession Description Interval E-value
Glyco_transf_24 pfam18404
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ...
1302-1569 0e+00

Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT). This domain belongs to glucosyltransferase 24 family (GT24) A-type domain. The GT domain displays the expected glycosyltransferase type A (GT-A) fold.


Pssm-ID: 436473  Cd Length: 268  Bit Score: 600.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1302 INIFSIASGHLYERFLKIMILSVLKNTNRPVKFWFIKNYLSPQFKDVIPHMAQEYNFEYELITYKWPSWLHKQKEKQRII 1381
Cdd:pfam18404    1 INIFSVASGHLYERFLKIMMLSVRKNTKSPVKFWFIENFLSPSFKAFLPHLAKEYGFEYELVTYKWPSWLRKQTEKQRII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1382 WAYKILFLDVIFPLSLEKVIFVDADQIIRTDMGELYDMDIKGRPLAYTPFCDNNREMDGYKFWKQGFWKEHLRGRPYHIS 1461
Cdd:pfam18404   81 WGYKILFLDVLFPLDLDKVIFVDADQVVRTDLKELVDMDLEGAPYGYTPMCDSRKEMEGFRFWKQGYWKDHLRGRPYHIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1462 ALYVVDLVKFRETAAGDNLRVFYETLSKDPNSLSNLDQDLPNYAQHTVPIFSLPQEWLWCESWCGNATKAKARTIDLCNN 1541
Cdd:pfam18404  161 ALYVVDLKRFRQMAAGDRLRSHYQQLSADPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESLKKAKTIDLCNN 240
                          250       260
                   ....*....|....*....|....*...
gi 334183827  1542 PMTKEPKLQGARRIVTEWPDLDLEARKF 1569
Cdd:pfam18404  241 PLTKEPKLDRAKRIIPEWTDYDEEVAAL 268
GT8_HUGT1_C_like cd06432
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain ...
1302-1549 0e+00

The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain of glycoprotein glucosyltransferase (UGT). UGT is a large glycoprotein whose C-terminus contains the catalytic activity. This catalytic C-terminal domain is highly homologous to Glycosyltransferase Family 8 (GT 8) and contains the DXD motif that coordinates donor sugar binding, characteristic for Family 8 glycosyltransferases. GT 8 proteins are retaining enzymes based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. The non-catalytic N-terminal portion of the human UTG1 (HUGT1) has been shown to monitor the protein folding status and activate its glucosyltransferase activity.


Pssm-ID: 133054  Cd Length: 248  Bit Score: 541.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1302 INIFSIASGHLYERFLKIMILSVLKNTNRPVKFWFIKNYLSPQFKDVIPHMAQEYNFEYELITYKWPSWLHKQKEKQRII 1381
Cdd:cd06432     1 INIFSVASGHLYERFLRIMMLSVMKNTKSPVKFWFIKNFLSPQFKEFLPEMAKEYGFEYELVTYKWPRWLHKQTEKQRII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1382 WAYKILFLDVIFPLSLEKVIFVDADQIIRTDMGELYDMDIKGRPLAYTPFCDNNREMDGYKFWKQGFWKEHLRGRPYHIS 1461
Cdd:cd06432    81 WGYKILFLDVLFPLNVDKVIFVDADQIVRTDLKELMDMDLKGAPYGYTPFCDSRKEMDGFRFWKQGYWKSHLRGRPYHIS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1462 ALYVVDLVKFRETAAGDNLRVFYETLSKDPNSLSNLDQDLPNYAQHTVPIFSLPQEWLWCESWCGNATKAKARTIDLCNN 1541
Cdd:cd06432   161 ALYVVDLKRFRRIAAGDRLRGQYQQLSQDPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESKKKAKTIDLCNN 240

                  ....*...
gi 334183827 1542 PMTKEPKL 1549
Cdd:cd06432   241 PLTKEPKL 248
Thioredoxin_14 pfam18402
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in ...
452-722 9.22e-61

Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).


Pssm-ID: 465750  Cd Length: 248  Bit Score: 208.67  E-value: 9.22e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   452 VDFRS-----VHVTYLNNLEEDDMYKRWRSNINEILMPAFPGQLRYIRKNLFHAVYVIDPAT-ACGLESIETLRSLYENQ 525
Cdd:pfam18402    1 FDIRDrieggGVIIWLNDLEKDKRYSRWPSSLQELLRPTYPGQLPPIRKNLFNLVLVVDLSQpEDLLLLVETLQSFVQRG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   526 LPVRFGVILYSTqliktiennggqipssdavtnaqvKEDLSTMVIRLFLYIKEHHGIQTAFQFLGNLntLRTESADSSEA 605
Cdd:pfam18402   81 IPVRFGLVPLVN------------------------STEDGLAQAKLFYYLLENYGLKAALSFLTAS--LYALAKKVLSP 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   606 DieQEHVDGAFVETILPkvktLPQDILLKLRQEHTLKEASEASSMFVFKLGLAKLKCSFLMNGLVFDSVE--EETLLNAM 683
Cdd:pfam18402  135 T--KAIFSSALKERTLR----PQALSFDEVLKSEVYDERLKKAKEYLKRLGLDSLSGPVFVNGVPLPRDEnwLQALSQRI 208
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 334183827   684 NEELPKIQEQVYYGQIESHTKVLDKLLSESG-LSRYNPQI 722
Cdd:pfam18402  209 SEDLQLLQKAVYEGALTDDDDVPDFFYDLPNaLPRRNPLI 248
Thioredoxin_12 pfam18400
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in ...
43-237 9.14e-59

Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).


Pssm-ID: 465748  Cd Length: 187  Bit Score: 200.54  E-value: 9.14e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827    43 GTPLLLEAGELISKESKQLFWEFTDAWLGSDGDDSDCKSARDCLLKISKQASTLLAQPVASLFHFSLTLRSASPRLVLYR 122
Cdd:pfam18400    1 ATPLLLEALETLAEENPDLFFPFLDALTNLDGEFADASTDEELYEAALKLASDHLSPLALSLFKLALSLRSASPRIEAFY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   123 QLADESLSSFPHGDDpsatgC-CWVDTGSSLFYDVADLQSWLASApavGDAVQGPELFDFDHVHFDSrAGSPVAVLYGAV 201
Cdd:pfam18400   81 QIYAESVSFEGAPPE-----CdSWVDWGGEVYCDPEDLDALLKSE---ASSRPQPELLPFDHVYPDS-GSSPVAILYADL 151
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 334183827   202 GTDCFRKFHLSLAKAAKEGKVTYVVRPVLPLGCEGK 237
Cdd:pfam18400  152 GSPNFREFHKYLSELAKDGKIRYVLRHVPPSGSESK 187
Thioredoxin_15 pfam18403
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose: ...
734-983 2.98e-38

Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).


Pssm-ID: 465751  Cd Length: 205  Bit Score: 142.36  E-value: 2.98e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   734 SLASSTRKGESMLNDVNYLHSPETSEDvkYVTHLLAADVATKKGMKLLHEGVRYLIGgSKSARLGVLFSSSQNADPHSLl 813
Cdd:pfam18403    1 DLNKLYSEHADLFDKMPYLEASSDKED--WATLWVVADLDSESGRKLLLSALEFRKS-NPGVRLGIIHNPASPSEASSL- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   814 fikfFEKTASSFSHKEKVLYFLDKLCLFYEREYllktsvesassqmfidkvleladeyglsskAYRSCLVESVDEELLKR 893
Cdd:pfam18403   77 ----ISSALLAALLKLKNLDALEFLTKLLEEEE------------------------------AAASESGKSSAEAAADY 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   894 LTKVAQFLSwELGLESDANAIISNGRVIFPVDE-RTFLGQDLHLLESMEFNQRVKPVQEIIEGIEWQDvdpdlltSKYFS 972
Cdd:pfam18403  123 WKALQPFLR-VLGLKPGQNALVLNGRVVGPIPEdEEFSADDFELLLSYERSKRIEPVYKAIEELGLED-------KISDP 194
                          250
                   ....*....|.
gi 334183827   973 DVFMFVSSAMA 983
Cdd:pfam18403  195 DAVAKLTSLVA 205
UDP-g_GGTase pfam06427
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ...
1144-1247 1.99e-35

UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded beta-sandwiches found in UDP-glucose-glycoprotein glucosyltransferase-like proteins. UDP-g_GGTase is an important, central component of the QC system in the ER for checking that glycoproteins are folded correctly. This QC prevents incorrectly folded glycoproteins from leaving the ER.


Pssm-ID: 461910  Cd Length: 109  Bit Score: 130.69  E-value: 1.99e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1144 GHCAEKDHEA-PRGLQLILGTKNRPHLVDTLVMANLGYWQMKVSPGVWYLQLAPGRSSELYALK--GGNDGSQDQSSLKR 1220
Cdd:pfam06427    2 GHARDVTTGSpPRGLQLVLGTEKNPHVADTIVMANLGYFQLKANPGVWKLELREGRSSDIYEIEsvGAEGWPSPGDEGTE 81
                           90       100
                   ....*....|....*....|....*..
gi 334183827  1221 ITIDDLRGKVVHLEVVKRKGKEHEKLL 1247
Cdd:pfam06427   82 VALTSFEGLTLYPRLSRKPGMENEDVL 108
Thioredoxin_13 pfam18401
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found ...
320-453 1.32e-29

Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).


Pssm-ID: 465749  Cd Length: 136  Bit Score: 114.97  E-value: 1.32e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   320 SSTVSDTLDVWELKDLGHQTAQRIVHASDPLQSMQEINQNFPSVVSSLSRMKLNESIKDEILSNQ-RMVPPGKALLALNG 398
Cdd:pfam18401    2 EVEDLKPLSVWELQDLGLQAAQFIMSSDDPLDTLLKLSQDFPKYASSLARHNVSDELREEIEENQeRLLPPGDNALWLNG 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 334183827   399 ALLNIEDIDLYMLMDLAHQELSLANHFSKLKIPDGAIRKLLLTTPLPEPDSYRVD 453
Cdd:pfam18401   82 LQLDERDIDPFSLLDILRRERKLINGLRKLGLSGSEAVDLLSHPALAAAQADSYD 136
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1300-1518 4.34e-18

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 86.95  E-value: 4.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1300 KTINIFSIASGHlYERFLKIMILSVLKNT-NRPVKFWFIKNYLSPQFKDVIPHMAQEYNFEYELITYKwPSWLHKQKEKQ 1378
Cdd:COG1442     4 NTINIVFAIDDN-YLPGLGVSIASLLENNpDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVD-DELLKDLPVSK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1379 RIIWA--YKiLFLDVIFPLSLEKVIFVDADQIIRTDMGELYDMDIKGRPLAYTPfcdnnremDGYKFWKQGFWKEHLR-- 1454
Cdd:COG1442    82 HISKAtyYR-LLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVR--------DGTVTGSQKKRAKRLGlp 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334183827 1455 -GRPYHISALYVVDLVKFRETaagDNLRVFYETLSKDPNSLSNLDQDLPN--YAQHtvpIFSLPQEW 1518
Cdd:COG1442   153 dDDGYFNSGVLLINLKKWREE---NITEKALEFLKENPDKLKYPDQDILNivLGGK---VKFLPPRY 213
 
Name Accession Description Interval E-value
Glyco_transf_24 pfam18404
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ...
1302-1569 0e+00

Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT). This domain belongs to glucosyltransferase 24 family (GT24) A-type domain. The GT domain displays the expected glycosyltransferase type A (GT-A) fold.


Pssm-ID: 436473  Cd Length: 268  Bit Score: 600.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1302 INIFSIASGHLYERFLKIMILSVLKNTNRPVKFWFIKNYLSPQFKDVIPHMAQEYNFEYELITYKWPSWLHKQKEKQRII 1381
Cdd:pfam18404    1 INIFSVASGHLYERFLKIMMLSVRKNTKSPVKFWFIENFLSPSFKAFLPHLAKEYGFEYELVTYKWPSWLRKQTEKQRII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1382 WAYKILFLDVIFPLSLEKVIFVDADQIIRTDMGELYDMDIKGRPLAYTPFCDNNREMDGYKFWKQGFWKEHLRGRPYHIS 1461
Cdd:pfam18404   81 WGYKILFLDVLFPLDLDKVIFVDADQVVRTDLKELVDMDLEGAPYGYTPMCDSRKEMEGFRFWKQGYWKDHLRGRPYHIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1462 ALYVVDLVKFRETAAGDNLRVFYETLSKDPNSLSNLDQDLPNYAQHTVPIFSLPQEWLWCESWCGNATKAKARTIDLCNN 1541
Cdd:pfam18404  161 ALYVVDLKRFRQMAAGDRLRSHYQQLSADPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESLKKAKTIDLCNN 240
                          250       260
                   ....*....|....*....|....*...
gi 334183827  1542 PMTKEPKLQGARRIVTEWPDLDLEARKF 1569
Cdd:pfam18404  241 PLTKEPKLDRAKRIIPEWTDYDEEVAAL 268
GT8_HUGT1_C_like cd06432
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain ...
1302-1549 0e+00

The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain of glycoprotein glucosyltransferase (UGT). UGT is a large glycoprotein whose C-terminus contains the catalytic activity. This catalytic C-terminal domain is highly homologous to Glycosyltransferase Family 8 (GT 8) and contains the DXD motif that coordinates donor sugar binding, characteristic for Family 8 glycosyltransferases. GT 8 proteins are retaining enzymes based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. The non-catalytic N-terminal portion of the human UTG1 (HUGT1) has been shown to monitor the protein folding status and activate its glucosyltransferase activity.


Pssm-ID: 133054  Cd Length: 248  Bit Score: 541.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1302 INIFSIASGHLYERFLKIMILSVLKNTNRPVKFWFIKNYLSPQFKDVIPHMAQEYNFEYELITYKWPSWLHKQKEKQRII 1381
Cdd:cd06432     1 INIFSVASGHLYERFLRIMMLSVMKNTKSPVKFWFIKNFLSPQFKEFLPEMAKEYGFEYELVTYKWPRWLHKQTEKQRII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1382 WAYKILFLDVIFPLSLEKVIFVDADQIIRTDMGELYDMDIKGRPLAYTPFCDNNREMDGYKFWKQGFWKEHLRGRPYHIS 1461
Cdd:cd06432    81 WGYKILFLDVLFPLNVDKVIFVDADQIVRTDLKELMDMDLKGAPYGYTPFCDSRKEMDGFRFWKQGYWKSHLRGRPYHIS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1462 ALYVVDLVKFRETAAGDNLRVFYETLSKDPNSLSNLDQDLPNYAQHTVPIFSLPQEWLWCESWCGNATKAKARTIDLCNN 1541
Cdd:cd06432   161 ALYVVDLKRFRRIAAGDRLRGQYQQLSQDPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESKKKAKTIDLCNN 240

                  ....*...
gi 334183827 1542 PMTKEPKL 1549
Cdd:cd06432   241 PLTKEPKL 248
Thioredoxin_14 pfam18402
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in ...
452-722 9.22e-61

Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).


Pssm-ID: 465750  Cd Length: 248  Bit Score: 208.67  E-value: 9.22e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   452 VDFRS-----VHVTYLNNLEEDDMYKRWRSNINEILMPAFPGQLRYIRKNLFHAVYVIDPAT-ACGLESIETLRSLYENQ 525
Cdd:pfam18402    1 FDIRDrieggGVIIWLNDLEKDKRYSRWPSSLQELLRPTYPGQLPPIRKNLFNLVLVVDLSQpEDLLLLVETLQSFVQRG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   526 LPVRFGVILYSTqliktiennggqipssdavtnaqvKEDLSTMVIRLFLYIKEHHGIQTAFQFLGNLntLRTESADSSEA 605
Cdd:pfam18402   81 IPVRFGLVPLVN------------------------STEDGLAQAKLFYYLLENYGLKAALSFLTAS--LYALAKKVLSP 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   606 DieQEHVDGAFVETILPkvktLPQDILLKLRQEHTLKEASEASSMFVFKLGLAKLKCSFLMNGLVFDSVE--EETLLNAM 683
Cdd:pfam18402  135 T--KAIFSSALKERTLR----PQALSFDEVLKSEVYDERLKKAKEYLKRLGLDSLSGPVFVNGVPLPRDEnwLQALSQRI 208
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 334183827   684 NEELPKIQEQVYYGQIESHTKVLDKLLSESG-LSRYNPQI 722
Cdd:pfam18402  209 SEDLQLLQKAVYEGALTDDDDVPDFFYDLPNaLPRRNPLI 248
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
1302-1549 3.15e-59

Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis; Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.


Pssm-ID: 132996 [Multi-domain]  Cd Length: 246  Bit Score: 204.21  E-value: 3.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1302 INIFSIASGHLYERFLKIMILSVLKNTNRPVKFWFIKNYLSPQFKDVIPHMAQEYNFEYELITYKWPSWLHKQ-KEKQRI 1380
Cdd:cd00505     1 IAIVIVATGDEYLRGAIVLMKSVLRHRTKPLRFHVLTNPLSDTFKAALDNLRKLYNFNYELIPVDILDSVDSEhLKRPIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1381 IWAYKILFLDVIFPlSLEKVIFVDADQIIRTDMGELYDMDIKGRPLAYTPFCDNNREMDGYKFWKQgfwkeHLRGRPYHI 1460
Cdd:cd00505    81 IVTLTKLHLPNLVP-DYDKILYVDADILVLTDIDELWDTPLGGQELAAAPDPGDRREGKYYRQKRS-----HLAGPDYFN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1461 SALYVVDLVKFREtaaGDNLRVFYETLSKDPNSLSNLDQDLPN--YAQHTVPIFSLPQEWLWCESWC------GNATKAK 1532
Cdd:cd00505   155 SGVFVVNLSKERR---NQLLKVALEKWLQSLSSLSGGDQDLLNtfFKQVPFIVKSLPCIWNVRLTGCyrslncFKAFVKN 231
                         250
                  ....*....|....*..
gi 334183827 1533 ARTIDLCNNpmTKEPKL 1549
Cdd:cd00505   232 AKVIHFNGP--TKPWNK 246
Thioredoxin_12 pfam18400
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in ...
43-237 9.14e-59

Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).


Pssm-ID: 465748  Cd Length: 187  Bit Score: 200.54  E-value: 9.14e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827    43 GTPLLLEAGELISKESKQLFWEFTDAWLGSDGDDSDCKSARDCLLKISKQASTLLAQPVASLFHFSLTLRSASPRLVLYR 122
Cdd:pfam18400    1 ATPLLLEALETLAEENPDLFFPFLDALTNLDGEFADASTDEELYEAALKLASDHLSPLALSLFKLALSLRSASPRIEAFY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   123 QLADESLSSFPHGDDpsatgC-CWVDTGSSLFYDVADLQSWLASApavGDAVQGPELFDFDHVHFDSrAGSPVAVLYGAV 201
Cdd:pfam18400   81 QIYAESVSFEGAPPE-----CdSWVDWGGEVYCDPEDLDALLKSE---ASSRPQPELLPFDHVYPDS-GSSPVAILYADL 151
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 334183827   202 GTDCFRKFHLSLAKAAKEGKVTYVVRPVLPLGCEGK 237
Cdd:pfam18400  152 GSPNFREFHKYLSELAKDGKIRYVLRHVPPSGSESK 187
Thioredoxin_15 pfam18403
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose: ...
734-983 2.98e-38

Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).


Pssm-ID: 465751  Cd Length: 205  Bit Score: 142.36  E-value: 2.98e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   734 SLASSTRKGESMLNDVNYLHSPETSEDvkYVTHLLAADVATKKGMKLLHEGVRYLIGgSKSARLGVLFSSSQNADPHSLl 813
Cdd:pfam18403    1 DLNKLYSEHADLFDKMPYLEASSDKED--WATLWVVADLDSESGRKLLLSALEFRKS-NPGVRLGIIHNPASPSEASSL- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   814 fikfFEKTASSFSHKEKVLYFLDKLCLFYEREYllktsvesassqmfidkvleladeyglsskAYRSCLVESVDEELLKR 893
Cdd:pfam18403   77 ----ISSALLAALLKLKNLDALEFLTKLLEEEE------------------------------AAASESGKSSAEAAADY 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   894 LTKVAQFLSwELGLESDANAIISNGRVIFPVDE-RTFLGQDLHLLESMEFNQRVKPVQEIIEGIEWQDvdpdlltSKYFS 972
Cdd:pfam18403  123 WKALQPFLR-VLGLKPGQNALVLNGRVVGPIPEdEEFSADDFELLLSYERSKRIEPVYKAIEELGLED-------KISDP 194
                          250
                   ....*....|.
gi 334183827   973 DVFMFVSSAMA 983
Cdd:pfam18403  195 DAVAKLTSLVA 205
UDP-g_GGTase pfam06427
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ...
1144-1247 1.99e-35

UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded beta-sandwiches found in UDP-glucose-glycoprotein glucosyltransferase-like proteins. UDP-g_GGTase is an important, central component of the QC system in the ER for checking that glycoproteins are folded correctly. This QC prevents incorrectly folded glycoproteins from leaving the ER.


Pssm-ID: 461910  Cd Length: 109  Bit Score: 130.69  E-value: 1.99e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1144 GHCAEKDHEA-PRGLQLILGTKNRPHLVDTLVMANLGYWQMKVSPGVWYLQLAPGRSSELYALK--GGNDGSQDQSSLKR 1220
Cdd:pfam06427    2 GHARDVTTGSpPRGLQLVLGTEKNPHVADTIVMANLGYFQLKANPGVWKLELREGRSSDIYEIEsvGAEGWPSPGDEGTE 81
                           90       100
                   ....*....|....*....|....*..
gi 334183827  1221 ITIDDLRGKVVHLEVVKRKGKEHEKLL 1247
Cdd:pfam06427   82 VALTSFEGLTLYPRLSRKPGMENEDVL 108
Thioredoxin_13 pfam18401
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found ...
320-453 1.32e-29

Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).


Pssm-ID: 465749  Cd Length: 136  Bit Score: 114.97  E-value: 1.32e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827   320 SSTVSDTLDVWELKDLGHQTAQRIVHASDPLQSMQEINQNFPSVVSSLSRMKLNESIKDEILSNQ-RMVPPGKALLALNG 398
Cdd:pfam18401    2 EVEDLKPLSVWELQDLGLQAAQFIMSSDDPLDTLLKLSQDFPKYASSLARHNVSDELREEIEENQeRLLPPGDNALWLNG 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 334183827   399 ALLNIEDIDLYMLMDLAHQELSLANHFSKLKIPDGAIRKLLLTTPLPEPDSYRVD 453
Cdd:pfam18401   82 LQLDERDIDPFSLLDILRRERKLINGLRKLGLSGSEAVDLLSHPALAAAQADSYD 136
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1300-1518 4.34e-18

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 86.95  E-value: 4.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1300 KTINIFSIASGHlYERFLKIMILSVLKNT-NRPVKFWFIKNYLSPQFKDVIPHMAQEYNFEYELITYKwPSWLHKQKEKQ 1378
Cdd:COG1442     4 NTINIVFAIDDN-YLPGLGVSIASLLENNpDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVD-DELLKDLPVSK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1379 RIIWA--YKiLFLDVIFPLSLEKVIFVDADQIIRTDMGELYDMDIKGRPLAYTPfcdnnremDGYKFWKQGFWKEHLR-- 1454
Cdd:COG1442    82 HISKAtyYR-LLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVR--------DGTVTGSQKKRAKRLGlp 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334183827 1455 -GRPYHISALYVVDLVKFRETaagDNLRVFYETLSKDPNSLSNLDQDLPN--YAQHtvpIFSLPQEW 1518
Cdd:COG1442   153 dDDGYFNSGVLLINLKKWREE---NITEKALEFLKENPDKLKYPDQDILNivLGGK---VKFLPPRY 213
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
1302-1518 1.45e-15

A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.


Pssm-ID: 133037 [Multi-domain]  Cd Length: 248  Bit Score: 78.03  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1302 INIFsIASGHLYERFLKIMILSVLKNTN-RPVKFWFIKNYLSPQFKDVIPHMAQEYNFEYELITYKWPSWLHKQKEKQRI 1380
Cdd:cd04194     1 MNIV-FAIDDNYAPYLAVTIKSILANNSkRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFPATTDHI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1381 -IWAYKILFLDVIFPlSLEKVIFVDADQIIRTDMGELYDMDIKGRPLA-----YTPFCDNNREMDGYKFWKQGFWkehlr 1454
Cdd:cd04194    80 sYATYYRLLIPDLLP-DYDKVLYLDADIIVLGDLSELFDIDLGDNLLAavrdpFIEQEKKRKRRLGGYDDGSYFN----- 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334183827 1455 grpyhiSALYVVDLVKFREtaagDNLRV-FYETLSKDPNSLSNLDQDLPN--YAQHtvpIFSLPQEW 1518
Cdd:cd04194   154 ------SGVLLINLKKWRE----ENITEkLLELIKEYGGRLIYPDQDILNavLKDK---ILYLPPRY 207
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
1313-1502 2.39e-04

Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.


Pssm-ID: 279798 [Multi-domain]  Cd Length: 252  Bit Score: 44.62  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1313 YERFLKIMILSVLKNTNRP-VKFWFIKNYLSPQFKDVIPHMAQEYNFEYELITYKWPSWLHKQKEKQRIIWAYKIL---- 1387
Cdd:pfam01501   10 YLLGASVSIKSLLKNNSDFaLNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDIKIFEYFSKLKLRSPKYWSLLnylr 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827  1388 -FLDVIFPlSLEKVIFVDADQIIRTDMGELYDMDIKGRPLA--YTPFCDNNremdgykFWKQGFWKEHLRGRPYHI--SA 1462
Cdd:pfam01501   90 lYLPDLFP-KLDKILYLDADIVVQGDLSPLWDIDLGGKVLAavEDNYFQRY-------PNFSEPIILENFGPPACYfnAG 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 334183827  1463 LYVVDLVKFRETaagdNLRVFY-ETLSKDPNSLSNLDQDLP 1502
Cdd:pfam01501  162 MLLFDLDAWRKE----NITERYiKWLNLNENRTLWKLGDQD 198
GT8_like_1 cd06429
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ...
1325-1424 4.65e-03

GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of glycosyltransferase family 8 with unknown function: Glycosyltransferase family 8 comprises enzymes with a number of known activities; lipopolysaccharide galactosyltransferase lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase and inositol 1-alpha-galactosyltransferase. It is classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed.


Pssm-ID: 133051 [Multi-domain]  Cd Length: 257  Bit Score: 40.84  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183827 1325 LKNTNRPVKFWFIKNYLSP-----QFKDVIPHMAQEYNFEY-ELITYKWPSWLHKQKEKQRIIWAYKILFLDVIFPlSLE 1398
Cdd:cd06429    37 DNQNYGAMRSWFDLNPLKIatvkvLNFDDFKLLGKVKVDSLmQLESEADTSNLKQRKPEYISLLNFARFYLPELFP-KLE 115
                          90       100
                  ....*....|....*....|....*.
gi 334183827 1399 KVIFVDADQIIRTDMGELYDMDIKGR 1424
Cdd:cd06429   116 KVIYLDDDVVVQKDLTELWNTDLGGG 141
 
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.
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