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Conserved domains on  [gi|2462537501|ref|XP_054230710|]
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UDP-glucose:glycoprotein glucosyltransferase 2 isoform X6 [Homo sapiens]

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 ...
1188-1454 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: 582.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1188 NIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTERQRIIW 1267
Cdd:pfam18404    2 NIFSVASGHLYERFLKIMMLSVRKNTKSPVKFWFIENFLSPSFKAFLPHLAKEYGFEYELVTYKWPSWLRKQTEKQRIIW 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1268 GYKILFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRFWKTGYWASHLLRRKYHISA 1347
Cdd:pfam18404   82 GYKILFLDVLFPLDLDKVIFVDADQVVRTDLKELVDMDLEGAPYGYTPMCDSRKEMEGFRFWKQGYWKDHLRGRPYHISA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1348 LYVVDLKKFRRIGAGDRLRSQYQALSQDPNSLSNLDQDLPNNMIYQVAIKSLPQDWLWCETWCDDESKQRAKTIDLCNNP 1427
Cdd:pfam18404  162 LYVVDLKRFRQMAAGDRLRSHYQQLSADPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESLKKAKTIDLCNNP 241
                          250       260
                   ....*....|....*....|....*..
gi 2462537501 1428 KTKESKLKAAARIVPEWVEYDAEIRQL 1454
Cdd:pfam18404  242 LTKEPKLDRAKRIIPEWTDYDEEVAAL 268
Thioredoxin_12 pfam18400
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in ...
45-226 3.13e-69

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: 230.59  E-value: 3.13e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501   45 ETPLLLEASEFMAEESNEKFWQFLETVQELAIY-KQTESDYSYYNLILKKAGQFLDNLHINLLKFAFSIRAYSPAIQMFQ 123
Cdd:pfam18400    1 ATPLLLEALETLAEENPDLFFPFLDALTNLDGEfADASTDEELYEAALKLASDHLSPLALSLFKLALSLRSASPRIEAFY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  124 QIAAD----EPPPDGCNAFVVIHKKHTCKINEIKKLLKKAA-SRTRPYLFKGDHKFPTNKEnLPVVILYAEMGTRTFSAF 198
Cdd:pfam18400   81 QIYAEsvsfEGAPPECDSWVDWGGEVYCDPEDLDALLKSEAsSRPQPELLPFDHVYPDSGS-SPVAILYADLGSPNFREF 159
                          170       180
                   ....*....|....*....|....*...
gi 2462537501  199 HKVLSEKAQNEEILYVLRHYIQKPSSRK 226
Cdd:pfam18400  160 HKYLSELAKDGKIRYVLRHVPPSGSESK 187
Thioredoxin_14 pfam18402
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in ...
437-686 2.64e-63

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: 215.99  E-value: 2.64e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  437 LDIRHS-----SIMWINDLENDDLYITWPTSCQKLLKPVFPGSVPSIRRNFHNLVLFIDPAQ-EYTLDFIKLADVFYSHE 510
Cdd:pfam18402    1 FDIRDRiegggVIIWLNDLEKDKRYSRWPSSLQELLRPTYPGQLPPIRKNLFNLVLVVDLSQpEDLLLLVETLQSFVQRG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  511 VPLRIGFVFILNTDDEvdgandaGVALWRAFNYIAEEFDISEAFISIVHMYQKVKKDQNILTVDNVKSVLQNTFPHANIW 590
Cdd:pfam18402   81 IPVRFGLVPLVNSTED-------GLAQAKLFYYLLENYGLKAALSFLTASLYALAKKVLSPTKAIFSSALKERTLRPQAL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  591 DILGI--HSKYDEERKAGASFYKMTGLGPL--PQALyNGEPFKHEEmNIKElkmAVLQRMMDASVYLQREVFLGTLNDRT 666
Cdd:pfam18402  154 SFDEVlkSEVYDERLKKAKEYLKRLGLDSLsgPVFV-NGVPLPRDE-NWLQ---ALSQRISEDLQLLQKAVYEGALTDDD 228
                          250       260
                   ....*....|....*....|
gi 2462537501  667 NAIDFLMDRNNVVPRINTLI 686
Cdd:pfam18402  229 DVPDFFYDLPNALPRRNPLI 248
UDP-g_GGTase pfam06427
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ...
1050-1155 4.95e-46

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: 160.73  E-value: 4.95e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1050 GQCFDKVTEQPPRGLQFTLGTKNKPAVVDTIVMAHHGYFQLKANPGAWILRLHQGKSEDIYQIVGHEGTD-SQADLEDII 1128
Cdd:pfam06427    2 GHARDVTTGSPPRGLQLVLGTEKNPHVADTIVMANLGYFQLKANPGVWKLELREGRSSDIYEIESVGAEGwPSPGDEGTE 81
                           90       100
                   ....*....|....*....|....*..
gi 2462537501 1129 VVLNSFKSKILKVKVKKETDKIKEDIL 1155
Cdd:pfam06427   82 VALTSFEGLTLYPRLSRKPGMENEDVL 108
Thioredoxin_13 pfam18401
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found ...
296-424 4.67e-45

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: 159.27  E-value: 4.67e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  296 ESNKQMMPLKVWELQDLSFQAASQIMSAPvyDAIKLMKDISQNFPIKARSLTRIAVNQHMREEIKENQKDLqvrfkIQPG 375
Cdd:pfam18401    1 EEVEDLKPLSVWELQDLGLQAAQFIMSSD--DPLDTLLKLSQDFPKYASSLARHNVSDELREEIEENQERL-----LPPG 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462537501  376 DARLFINGLRVDMDVYDAFSILDMLKLEGKMMNGLRNLGINGEDMSKFL 424
Cdd:pfam18401   74 DNALWLNGLQLDERDIDPFSLLDILRRERKLINGLRKLGLSGSEAVDLL 122
Thioredoxin_15 pfam18403
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose: ...
710-889 1.48e-42

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: 154.69  E-value: 1.48e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  710 TFFFLDSQdkSAVIAKNMYYLTqDDESIISAVTLWIIADFDKPSGRKLLFNALKHMKTSVHSRLGIIYNPTSKiNEENTA 789
Cdd:pfam18403    1 DLNKLYSE--HADLFDKMPYLE-ASSDKEDWATLWVVADLDSESGRKLLLSALEFRKSNPGVRLGIIHNPASP-SEASSL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  790 ISRGILAAFLTQKNMFLRSFLGQLAKEEIATAIYSGDKIKTFLIEF--------------------------LGPLDED- 842
Cdd:pfam18403   77 ISSALLAALLKLKNLDALEFLTKLLEEEEAAASESGKSSAEAAADYwkalqpflrvlglkpgqnalvlngrvVGPIPEDe 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462537501  843 -FYAEDFYLLEKITFSNLGEKIKGIVENMGINAN-NMSDFIMKVDALMS 889
Cdd:pfam18403  157 eFSADDFELLLSYERSKRIEPVYKAIEELGLEDKiSDPDAVAKLTSLVA 205
 
Name Accession Description Interval E-value
Glyco_transf_24 pfam18404
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ...
1188-1454 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: 582.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1188 NIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTERQRIIW 1267
Cdd:pfam18404    2 NIFSVASGHLYERFLKIMMLSVRKNTKSPVKFWFIENFLSPSFKAFLPHLAKEYGFEYELVTYKWPSWLRKQTEKQRIIW 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1268 GYKILFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRFWKTGYWASHLLRRKYHISA 1347
Cdd:pfam18404   82 GYKILFLDVLFPLDLDKVIFVDADQVVRTDLKELVDMDLEGAPYGYTPMCDSRKEMEGFRFWKQGYWKDHLRGRPYHISA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1348 LYVVDLKKFRRIGAGDRLRSQYQALSQDPNSLSNLDQDLPNNMIYQVAIKSLPQDWLWCETWCDDESKQRAKTIDLCNNP 1427
Cdd:pfam18404  162 LYVVDLKRFRQMAAGDRLRSHYQQLSADPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESLKKAKTIDLCNNP 241
                          250       260
                   ....*....|....*....|....*..
gi 2462537501 1428 KTKESKLKAAARIVPEWVEYDAEIRQL 1454
Cdd:pfam18404  242 LTKEPKLDRAKRIIPEWTDYDEEVAAL 268
GT8_HUGT1_C_like cd06432
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain ...
1187-1434 3.37e-180

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: 535.43  E-value: 3.37e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1187 LNIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTERQRII 1266
Cdd:cd06432      1 INIFSVASGHLYERFLRIMMLSVMKNTKSPVKFWFIKNFLSPQFKEFLPEMAKEYGFEYELVTYKWPRWLHKQTEKQRII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1267 WGYKILFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRFWKTGYWASHLLRRKYHIS 1346
Cdd:cd06432     81 WGYKILFLDVLFPLNVDKVIFVDADQIVRTDLKELMDMDLKGAPYGYTPFCDSRKEMDGFRFWKQGYWKSHLRGRPYHIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1347 ALYVVDLKKFRRIGAGDRLRSQYQALSQDPNSLSNLDQDLPNNMIYQVAIKSLPQDWLWCETWCDDESKQRAKTIDLCNN 1426
Cdd:cd06432    161 ALYVVDLKRFRRIAAGDRLRGQYQQLSQDPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESKKKAKTIDLCNN 240

                   ....*...
gi 2462537501 1427 PKTKESKL 1434
Cdd:cd06432    241 PLTKEPKL 248
Thioredoxin_12 pfam18400
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in ...
45-226 3.13e-69

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: 230.59  E-value: 3.13e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501   45 ETPLLLEASEFMAEESNEKFWQFLETVQELAIY-KQTESDYSYYNLILKKAGQFLDNLHINLLKFAFSIRAYSPAIQMFQ 123
Cdd:pfam18400    1 ATPLLLEALETLAEENPDLFFPFLDALTNLDGEfADASTDEELYEAALKLASDHLSPLALSLFKLALSLRSASPRIEAFY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  124 QIAAD----EPPPDGCNAFVVIHKKHTCKINEIKKLLKKAA-SRTRPYLFKGDHKFPTNKEnLPVVILYAEMGTRTFSAF 198
Cdd:pfam18400   81 QIYAEsvsfEGAPPECDSWVDWGGEVYCDPEDLDALLKSEAsSRPQPELLPFDHVYPDSGS-SPVAILYADLGSPNFREF 159
                          170       180
                   ....*....|....*....|....*...
gi 2462537501  199 HKVLSEKAQNEEILYVLRHYIQKPSSRK 226
Cdd:pfam18400  160 HKYLSELAKDGKIRYVLRHVPPSGSESK 187
Thioredoxin_14 pfam18402
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in ...
437-686 2.64e-63

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: 215.99  E-value: 2.64e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  437 LDIRHS-----SIMWINDLENDDLYITWPTSCQKLLKPVFPGSVPSIRRNFHNLVLFIDPAQ-EYTLDFIKLADVFYSHE 510
Cdd:pfam18402    1 FDIRDRiegggVIIWLNDLEKDKRYSRWPSSLQELLRPTYPGQLPPIRKNLFNLVLVVDLSQpEDLLLLVETLQSFVQRG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  511 VPLRIGFVFILNTDDEvdgandaGVALWRAFNYIAEEFDISEAFISIVHMYQKVKKDQNILTVDNVKSVLQNTFPHANIW 590
Cdd:pfam18402   81 IPVRFGLVPLVNSTED-------GLAQAKLFYYLLENYGLKAALSFLTASLYALAKKVLSPTKAIFSSALKERTLRPQAL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  591 DILGI--HSKYDEERKAGASFYKMTGLGPL--PQALyNGEPFKHEEmNIKElkmAVLQRMMDASVYLQREVFLGTLNDRT 666
Cdd:pfam18402  154 SFDEVlkSEVYDERLKKAKEYLKRLGLDSLsgPVFV-NGVPLPRDE-NWLQ---ALSQRISEDLQLLQKAVYEGALTDDD 228
                          250       260
                   ....*....|....*....|
gi 2462537501  667 NAIDFLMDRNNVVPRINTLI 686
Cdd:pfam18402  229 DVPDFFYDLPNALPRRNPLI 248
UDP-g_GGTase pfam06427
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ...
1050-1155 4.95e-46

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: 160.73  E-value: 4.95e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1050 GQCFDKVTEQPPRGLQFTLGTKNKPAVVDTIVMAHHGYFQLKANPGAWILRLHQGKSEDIYQIVGHEGTD-SQADLEDII 1128
Cdd:pfam06427    2 GHARDVTTGSPPRGLQLVLGTEKNPHVADTIVMANLGYFQLKANPGVWKLELREGRSSDIYEIESVGAEGwPSPGDEGTE 81
                           90       100
                   ....*....|....*....|....*..
gi 2462537501 1129 VVLNSFKSKILKVKVKKETDKIKEDIL 1155
Cdd:pfam06427   82 VALTSFEGLTLYPRLSRKPGMENEDVL 108
Thioredoxin_13 pfam18401
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found ...
296-424 4.67e-45

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: 159.27  E-value: 4.67e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  296 ESNKQMMPLKVWELQDLSFQAASQIMSAPvyDAIKLMKDISQNFPIKARSLTRIAVNQHMREEIKENQKDLqvrfkIQPG 375
Cdd:pfam18401    1 EEVEDLKPLSVWELQDLGLQAAQFIMSSD--DPLDTLLKLSQDFPKYASSLARHNVSDELREEIEENQERL-----LPPG 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462537501  376 DARLFINGLRVDMDVYDAFSILDMLKLEGKMMNGLRNLGINGEDMSKFL 424
Cdd:pfam18401   74 DNALWLNGLQLDERDIDPFSLLDILRRERKLINGLRKLGLSGSEAVDLL 122
Thioredoxin_15 pfam18403
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose: ...
710-889 1.48e-42

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: 154.69  E-value: 1.48e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  710 TFFFLDSQdkSAVIAKNMYYLTqDDESIISAVTLWIIADFDKPSGRKLLFNALKHMKTSVHSRLGIIYNPTSKiNEENTA 789
Cdd:pfam18403    1 DLNKLYSE--HADLFDKMPYLE-ASSDKEDWATLWVVADLDSESGRKLLLSALEFRKSNPGVRLGIIHNPASP-SEASSL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  790 ISRGILAAFLTQKNMFLRSFLGQLAKEEIATAIYSGDKIKTFLIEF--------------------------LGPLDED- 842
Cdd:pfam18403   77 ISSALLAALLKLKNLDALEFLTKLLEEEEAAASESGKSSAEAAADYwkalqpflrvlglkpgqnalvlngrvVGPIPEDe 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462537501  843 -FYAEDFYLLEKITFSNLGEKIKGIVENMGINAN-NMSDFIMKVDALMS 889
Cdd:pfam18403  157 eFSADDFELLLSYERSKRIEPVYKAIEELGLEDKiSDPDAVAKLTSLVA 205
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1184-1403 3.79e-14

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 75.01  E-value: 3.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1184 KDVLNIFSVASGHlYERFLRIMMLSVLRNTK-TPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQY------------ 1250
Cdd:COG1442      3 KNTINIVFAIDDN-YLPGLGVSIASLLENNPdRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVddellkdlpvsk 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1251 RWPR--WLRqqterqriiwgykiLFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGytpfcdSRREMDGYRF 1328
Cdd:COG1442     82 HISKatYYR--------------LLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLA------AVRDGTVTGS 141
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462537501 1329 WKtgYWASHL---LRRKYHISALYVVDLKKFRRIGAGDRLrsqYQALSQDPNSLSNLDQD-LpnNMIYQVAIKSLPQDW 1403
Cdd:COG1442    142 QK--KRAKRLglpDDDGYFNSGVLLINLKKWREENITEKA---LEFLKENPDKLKYPDQDiL--NIVLGGKVKFLPPRY 213
 
Name Accession Description Interval E-value
Glyco_transf_24 pfam18404
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ...
1188-1454 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: 582.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1188 NIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTERQRIIW 1267
Cdd:pfam18404    2 NIFSVASGHLYERFLKIMMLSVRKNTKSPVKFWFIENFLSPSFKAFLPHLAKEYGFEYELVTYKWPSWLRKQTEKQRIIW 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1268 GYKILFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRFWKTGYWASHLLRRKYHISA 1347
Cdd:pfam18404   82 GYKILFLDVLFPLDLDKVIFVDADQVVRTDLKELVDMDLEGAPYGYTPMCDSRKEMEGFRFWKQGYWKDHLRGRPYHISA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1348 LYVVDLKKFRRIGAGDRLRSQYQALSQDPNSLSNLDQDLPNNMIYQVAIKSLPQDWLWCETWCDDESKQRAKTIDLCNNP 1427
Cdd:pfam18404  162 LYVVDLKRFRQMAAGDRLRSHYQQLSADPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESLKKAKTIDLCNNP 241
                          250       260
                   ....*....|....*....|....*..
gi 2462537501 1428 KTKESKLKAAARIVPEWVEYDAEIRQL 1454
Cdd:pfam18404  242 LTKEPKLDRAKRIIPEWTDYDEEVAAL 268
GT8_HUGT1_C_like cd06432
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain ...
1187-1434 3.37e-180

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: 535.43  E-value: 3.37e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1187 LNIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTERQRII 1266
Cdd:cd06432      1 INIFSVASGHLYERFLRIMMLSVMKNTKSPVKFWFIKNFLSPQFKEFLPEMAKEYGFEYELVTYKWPRWLHKQTEKQRII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1267 WGYKILFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRFWKTGYWASHLLRRKYHIS 1346
Cdd:cd06432     81 WGYKILFLDVLFPLNVDKVIFVDADQIVRTDLKELMDMDLKGAPYGYTPFCDSRKEMDGFRFWKQGYWKSHLRGRPYHIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1347 ALYVVDLKKFRRIGAGDRLRSQYQALSQDPNSLSNLDQDLPNNMIYQVAIKSLPQDWLWCETWCDDESKQRAKTIDLCNN 1426
Cdd:cd06432    161 ALYVVDLKRFRRIAAGDRLRGQYQQLSQDPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESKKKAKTIDLCNN 240

                   ....*...
gi 2462537501 1427 PKTKESKL 1434
Cdd:cd06432    241 PLTKEPKL 248
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
1187-1428 3.63e-75

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: 250.05  E-value: 3.63e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1187 LNIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTE-RQRI 1265
Cdd:cd00505      1 IAIVIVATGDEYLRGAIVLMKSVLRHRTKPLRFHVLTNPLSDTFKAALDNLRKLYNFNYELIPVDILDSVDSEHLkRPIK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1266 IWGYKILFLDVLFPlAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRfwktgYWASHLLRRKYHI 1345
Cdd:cd00505     81 IVTLTKLHLPNLVP-DYDKILYVDADILVLTDIDELWDTPLGGQELAAAPDPGDRREGKYYR-----QKRSHLAGPDYFN 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1346 SALYVVDLKKFRR-IGAGDRLRSQYQALSqdpnSLSNLDQDLPNNMIYQVA--IKSLPQDWLWCETWCDD------ESKQ 1416
Cdd:cd00505    155 SGVFVVNLSKERRnQLLKVALEKWLQSLS----SLSGGDQDLLNTFFKQVPfiVKSLPCIWNVRLTGCYRslncfkAFVK 230
                          250
                   ....*....|..
gi 2462537501 1417 RAKTIDLCNNPK 1428
Cdd:cd00505    231 NAKVIHFNGPTK 242
Thioredoxin_12 pfam18400
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in ...
45-226 3.13e-69

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: 230.59  E-value: 3.13e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501   45 ETPLLLEASEFMAEESNEKFWQFLETVQELAIY-KQTESDYSYYNLILKKAGQFLDNLHINLLKFAFSIRAYSPAIQMFQ 123
Cdd:pfam18400    1 ATPLLLEALETLAEENPDLFFPFLDALTNLDGEfADASTDEELYEAALKLASDHLSPLALSLFKLALSLRSASPRIEAFY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  124 QIAAD----EPPPDGCNAFVVIHKKHTCKINEIKKLLKKAA-SRTRPYLFKGDHKFPTNKEnLPVVILYAEMGTRTFSAF 198
Cdd:pfam18400   81 QIYAEsvsfEGAPPECDSWVDWGGEVYCDPEDLDALLKSEAsSRPQPELLPFDHVYPDSGS-SPVAILYADLGSPNFREF 159
                          170       180
                   ....*....|....*....|....*...
gi 2462537501  199 HKVLSEKAQNEEILYVLRHYIQKPSSRK 226
Cdd:pfam18400  160 HKYLSELAKDGKIRYVLRHVPPSGSESK 187
Thioredoxin_14 pfam18402
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in ...
437-686 2.64e-63

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: 215.99  E-value: 2.64e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  437 LDIRHS-----SIMWINDLENDDLYITWPTSCQKLLKPVFPGSVPSIRRNFHNLVLFIDPAQ-EYTLDFIKLADVFYSHE 510
Cdd:pfam18402    1 FDIRDRiegggVIIWLNDLEKDKRYSRWPSSLQELLRPTYPGQLPPIRKNLFNLVLVVDLSQpEDLLLLVETLQSFVQRG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  511 VPLRIGFVFILNTDDEvdgandaGVALWRAFNYIAEEFDISEAFISIVHMYQKVKKDQNILTVDNVKSVLQNTFPHANIW 590
Cdd:pfam18402   81 IPVRFGLVPLVNSTED-------GLAQAKLFYYLLENYGLKAALSFLTASLYALAKKVLSPTKAIFSSALKERTLRPQAL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  591 DILGI--HSKYDEERKAGASFYKMTGLGPL--PQALyNGEPFKHEEmNIKElkmAVLQRMMDASVYLQREVFLGTLNDRT 666
Cdd:pfam18402  154 SFDEVlkSEVYDERLKKAKEYLKRLGLDSLsgPVFV-NGVPLPRDE-NWLQ---ALSQRISEDLQLLQKAVYEGALTDDD 228
                          250       260
                   ....*....|....*....|
gi 2462537501  667 NAIDFLMDRNNVVPRINTLI 686
Cdd:pfam18402  229 DVPDFFYDLPNALPRRNPLI 248
UDP-g_GGTase pfam06427
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ...
1050-1155 4.95e-46

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: 160.73  E-value: 4.95e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1050 GQCFDKVTEQPPRGLQFTLGTKNKPAVVDTIVMAHHGYFQLKANPGAWILRLHQGKSEDIYQIVGHEGTD-SQADLEDII 1128
Cdd:pfam06427    2 GHARDVTTGSPPRGLQLVLGTEKNPHVADTIVMANLGYFQLKANPGVWKLELREGRSSDIYEIESVGAEGwPSPGDEGTE 81
                           90       100
                   ....*....|....*....|....*..
gi 2462537501 1129 VVLNSFKSKILKVKVKKETDKIKEDIL 1155
Cdd:pfam06427   82 VALTSFEGLTLYPRLSRKPGMENEDVL 108
Thioredoxin_13 pfam18401
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found ...
296-424 4.67e-45

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: 159.27  E-value: 4.67e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  296 ESNKQMMPLKVWELQDLSFQAASQIMSAPvyDAIKLMKDISQNFPIKARSLTRIAVNQHMREEIKENQKDLqvrfkIQPG 375
Cdd:pfam18401    1 EEVEDLKPLSVWELQDLGLQAAQFIMSSD--DPLDTLLKLSQDFPKYASSLARHNVSDELREEIEENQERL-----LPPG 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462537501  376 DARLFINGLRVDMDVYDAFSILDMLKLEGKMMNGLRNLGINGEDMSKFL 424
Cdd:pfam18401   74 DNALWLNGLQLDERDIDPFSLLDILRRERKLINGLRKLGLSGSEAVDLL 122
Thioredoxin_15 pfam18403
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose: ...
710-889 1.48e-42

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: 154.69  E-value: 1.48e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  710 TFFFLDSQdkSAVIAKNMYYLTqDDESIISAVTLWIIADFDKPSGRKLLFNALKHMKTSVHSRLGIIYNPTSKiNEENTA 789
Cdd:pfam18403    1 DLNKLYSE--HADLFDKMPYLE-ASSDKEDWATLWVVADLDSESGRKLLLSALEFRKSNPGVRLGIIHNPASP-SEASSL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501  790 ISRGILAAFLTQKNMFLRSFLGQLAKEEIATAIYSGDKIKTFLIEF--------------------------LGPLDED- 842
Cdd:pfam18403   77 ISSALLAALLKLKNLDALEFLTKLLEEEEAAASESGKSSAEAAADYwkalqpflrvlglkpgqnalvlngrvVGPIPEDe 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462537501  843 -FYAEDFYLLEKITFSNLGEKIKGIVENMGINAN-NMSDFIMKVDALMS 889
Cdd:pfam18403  157 eFSADDFELLLSYERSKRIEPVYKAIEELGLEDKiSDPDAVAKLTSLVA 205
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1184-1403 3.79e-14

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 75.01  E-value: 3.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1184 KDVLNIFSVASGHlYERFLRIMMLSVLRNTK-TPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQY------------ 1250
Cdd:COG1442      3 KNTINIVFAIDDN-YLPGLGVSIASLLENNPdRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVddellkdlpvsk 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1251 RWPR--WLRqqterqriiwgykiLFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGytpfcdSRREMDGYRF 1328
Cdd:COG1442     82 HISKatYYR--------------LLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLA------AVRDGTVTGS 141
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462537501 1329 WKtgYWASHL---LRRKYHISALYVVDLKKFRRIGAGDRLrsqYQALSQDPNSLSNLDQD-LpnNMIYQVAIKSLPQDW 1403
Cdd:COG1442    142 QK--KRAKRLglpDDDGYFNSGVLLINLKKWREENITEKA---LEFLKENPDKLKYPDQDiL--NIVLGGKVKFLPPRY 213
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
1198-1403 1.24e-09

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: 60.31  E-value: 1.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1198 YERFLRIMMLSVLRNT-KTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRwLRQQTERQRIIWG---YKiLF 1273
Cdd:cd04194     11 YAPYLAVTIKSILANNsKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDD-FKFFPATTDHISYatyYR-LL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462537501 1274 LDVLFPlAVDKIIFVDADQIVRHDLKELRDFDLDGAPYG-----YTPFCDSRREMDGYRFWKTGYWASHLLrrkyhisal 1348
Cdd:cd04194     89 IPDLLP-DYDKVLYLDADIIVLGDLSELFDIDLGDNLLAavrdpFIEQEKKRKRRLGGYDDGSYFNSGVLL--------- 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462537501 1349 yvVDLKKFRRIGAGDRLrsqYQALSQDPNSLSNLDQD-LpnNMIYQVAIKSLPQDW 1403
Cdd:cd04194    159 --INLKKWREENITEKL---LELIKEYGGRLIYPDQDiL--NAVLKDKILYLPPRY 207
 
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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