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Conserved domains on  [gi|2124654928|ref|XP_044680481|]
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hypothetical protein J7337_007169 [Fusarium musae]

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 ...
1167-1434 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: 630.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1167 INIFSVASGHLYERMLNIMMVSVMRNTKHTVKFWFIEQFLSPSFKEFIPHMAAEYGFKYEMVTYKWPHWLRQQKEKQREI 1246
Cdd:pfam18404    1 INIFSVASGHLYERFLKIMMLSVRKNTKSPVKFWFIENFLSPSFKAFLPHLAKEYGFEYELVTYKWPSWLRKQTEKQRII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1247 WGYKILFLDVLFPLSLDKVIFVDADQIVRTDMIDLVNHDLEGAPYGFTPMCDSRTEMEGFRFWKQGYWANYLRGLPYHIS 1326
Cdd:pfam18404   81 WGYKILFLDVLFPLDLDKVIFVDADQVVRTDLKELVDMDLEGAPYGYTPMCDSRKEMEGFRFWKQGYWKDHLRGRPYHIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1327 ALYVVDLNRFRQLAAGDRLRQQYHALSADPNSLSNLDQDLPNNMQFTIPIHSLPQEWLWCETWCSDESLAQARTIDLCNN 1406
Cdd:pfam18404  161 ALYVVDLKRFRQMAAGDRLRSHYQQLSADPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESLKKAKTIDLCNN 240
                          250       260
                   ....*....|....*....|....*...
gi 2124654928 1407 PQTKEPKLDRARRQVPEWTLYDEEIAAL 1434
Cdd:pfam18404  241 PLTKEPKLDRAKRIIPEWTDYDEEVAAL 268
Thioredoxin_14 pfam18402
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in ...
402-644 1.35e-89

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: 291.10  E-value: 1.35e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  402 FDWTDRLEEGKALLWLNDLEKDARYQKLPSDLTALLQRTYPGQLPQVALNLFHIVAPVDFTNIEDGR-AFGQLAQFMQRG 480
Cdd:pfam18402    1 FDIRDRIEGGGVIIWLNDLEKDKRYSRWPSSLQELLRPTYPGQLPPIRKNLFNLVLVVDLSQPEDLLlLVETLQSFVQRG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  481 VTLRFGILPLV-TTPASAAQAKVVYHLMETYGFESLITYLQESEE---GPEGAANKKAFTRAIDGRETLPgaNKMTLAEI 556
Cdd:pfam18402   81 IPVRFGLVPLVnSTEDGLAQAKLFYYLLENYGLKAALSFLTASLYalaKKVLSPTKAIFSSALKERTLRP--QALSFDEV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  557 LEADTYKQRVEASKAWANRLNADTTVRPVFVNGLAIPREKSWVQAMGQRLTEDQQAIQKAVYFGQIEEGTPVSDLF--LR 634
Cdd:pfam18402  159 LKSEVYDERLKKAKEYLKRLGLDSLSGPVFVNGVPLPRDENWLQALSQRISEDLQLLQKAVYEGALTDDDDVPDFFydLP 238
                          250
                   ....*....|
gi 2124654928  635 DAISKRNTYI 644
Cdd:pfam18402  239 NALPRRNPLI 248
Thioredoxin_15 pfam18403
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose: ...
656-851 3.69e-64

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: 216.71  E-value: 3.69e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  656 DINKLHKDFVGLFGNIAVLPSDSkaPKESWAVLTAVADLATDDGQDLLLAALEFKRKNPGVRLDLVHNPPSSAEAH-VIN 734
Cdd:pfam18403    1 DLNKLYSEHADLFDKMPYLEASS--DKEDWATLWVVADLDSESGRKLLLSALEFRKSNPGVRLGIIHNPASPSEASsLIS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  735 GAFKLNEGKLAEMKNKDDLKAILEA----------SWTAEDDGLGTALADFLSASNILPGTKGLLLNGRVVGPLPSDVSF 804
Cdd:pfam18403   79 SALLAALLKLKNLDALEFLTKLLEEeeaaasesgkSSAEAAADYWKALQPFLRVLGLKPGQNALVLNGRVVGPIPEDEEF 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2124654928  805 NEDDLQQLLEFERRNRILPVYAAIKDLGFEDKLSDPIAAAKLTSITA 851
Cdd:pfam18403  159 SADDFELLLSYERSKRIEPVYKAIEELGLEDKISDPDAVAKLTSLVA 205
Thioredoxin_12 pfam18400
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in ...
36-215 7.47e-61

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: 206.32  E-value: 7.47e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928   36 PYLLELLETAAGENSTAYFPLLDKIAG--GHFQSTNSDAELYDRFLEVLQQdgHITkPEALSTYKLALSLRVAAPRIEAH 113
Cdd:pfam18400    3 PLLLEALETLAEENPDLFFPFLDALTNldGEFADASTDEELYEAALKLASD--HLS-PLALSLFKLALSLRSASPRIEAF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  114 YQYYTtavDSVSKGDTNDDCSTWALIDNKKYCS-ETLGKAVEGDFSAR-QVNLLPFDRVLGFGKD---AILYADPTSASF 188
Cdd:pfam18400   80 YQIYA---ESVSFEGAPPECDSWVDWGGEVYCDpEDLDALLKSEASSRpQPELLPFDHVYPDSGSspvAILYADLGSPNF 156
                          170       180
                   ....*....|....*....|....*..
gi 2124654928  189 GPFHIALSKAAKQGDVSYRLRYRRSAG 215
Cdd:pfam18400  157 REFHKYLSELAKDGKIRYVLRHVPPSG 183
UDP-g_GGTase pfam06427
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ...
1021-1129 1.58e-60

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: 202.33  E-value: 1.58e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1021 EGHSRDGKRGA-PRGAQLSLATEKEPLITDTIVMANLGYFQFKANPGFYNIQLKQGRTSKIFTIESVGAHGYaPVPGDEG 1099
Cdd:pfam06427    1 EGHARDVTTGSpPRGLQLVLGTEKNPHVADTIVMANLGYFQLKANPGVWKLELREGRSSDIYEIESVGAEGW-PSPGDEG 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 2124654928 1100 TEIALMDFKGTTLYPRLNRKPGMEEVDVLE 1129
Cdd:pfam06427   80 TEVALTSFEGLTLYPRLSRKPGMENEDVLE 109
Thioredoxin_13 pfam18401
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found ...
264-397 2.37e-56

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: 191.63  E-value: 2.37e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  264 EEVADLKPLSTSELASLGLKTASFILNSENPLDALVKSTQDFPKFSASIATHEVAKEFAAEQEKNVAAGIPSGINFLWMN 343
Cdd:pfam18401    1 EEVEDLKPLSVWELQDLGLQAAQFIMSSDDPLDTLLKLSQDFPKYASSLARHNVSDELREEIEENQERLLPPGDNALWLN 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2124654928  344 GVQLIERQIEPFTLIEMIRRERKLIDGVRDLGFNGQQANSLLGHSEVASSKAED 397
Cdd:pfam18401   81 GLQLDERDIDPFSLLDILRRERKLINGLRKLGLSGSEAVDLLSHPALAAAQADS 134
 
Name Accession Description Interval E-value
Glyco_transf_24 pfam18404
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ...
1167-1434 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: 630.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1167 INIFSVASGHLYERMLNIMMVSVMRNTKHTVKFWFIEQFLSPSFKEFIPHMAAEYGFKYEMVTYKWPHWLRQQKEKQREI 1246
Cdd:pfam18404    1 INIFSVASGHLYERFLKIMMLSVRKNTKSPVKFWFIENFLSPSFKAFLPHLAKEYGFEYELVTYKWPSWLRKQTEKQRII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1247 WGYKILFLDVLFPLSLDKVIFVDADQIVRTDMIDLVNHDLEGAPYGFTPMCDSRTEMEGFRFWKQGYWANYLRGLPYHIS 1326
Cdd:pfam18404   81 WGYKILFLDVLFPLDLDKVIFVDADQVVRTDLKELVDMDLEGAPYGYTPMCDSRKEMEGFRFWKQGYWKDHLRGRPYHIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1327 ALYVVDLNRFRQLAAGDRLRQQYHALSADPNSLSNLDQDLPNNMQFTIPIHSLPQEWLWCETWCSDESLAQARTIDLCNN 1406
Cdd:pfam18404  161 ALYVVDLKRFRQMAAGDRLRSHYQQLSADPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESLKKAKTIDLCNN 240
                          250       260
                   ....*....|....*....|....*...
gi 2124654928 1407 PQTKEPKLDRARRQVPEWTLYDEEIAAL 1434
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 ...
1167-1414 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: 549.68  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1167 INIFSVASGHLYERMLNIMMVSVMRNTKHTVKFWFIEQFLSPSFKEFIPHMAAEYGFKYEMVTYKWPHWLRQQKEKQREI 1246
Cdd:cd06432      1 INIFSVASGHLYERFLRIMMLSVMKNTKSPVKFWFIKNFLSPQFKEFLPEMAKEYGFEYELVTYKWPRWLHKQTEKQRII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1247 WGYKILFLDVLFPLSLDKVIFVDADQIVRTDMIDLVNHDLEGAPYGFTPMCDSRTEMEGFRFWKQGYWANYLRGLPYHIS 1326
Cdd:cd06432     81 WGYKILFLDVLFPLNVDKVIFVDADQIVRTDLKELMDMDLKGAPYGYTPFCDSRKEMDGFRFWKQGYWKSHLRGRPYHIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1327 ALYVVDLNRFRQLAAGDRLRQQYHALSADPNSLSNLDQDLPNNMQFTIPIHSLPQEWLWCETWCSDESLAQARTIDLCNN 1406
Cdd:cd06432    161 ALYVVDLKRFRRIAAGDRLRGQYQQLSQDPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESKKKAKTIDLCNN 240

                   ....*...
gi 2124654928 1407 PQTKEPKL 1414
Cdd:cd06432    241 PLTKEPKL 248
Thioredoxin_14 pfam18402
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in ...
402-644 1.35e-89

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: 291.10  E-value: 1.35e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  402 FDWTDRLEEGKALLWLNDLEKDARYQKLPSDLTALLQRTYPGQLPQVALNLFHIVAPVDFTNIEDGR-AFGQLAQFMQRG 480
Cdd:pfam18402    1 FDIRDRIEGGGVIIWLNDLEKDKRYSRWPSSLQELLRPTYPGQLPPIRKNLFNLVLVVDLSQPEDLLlLVETLQSFVQRG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  481 VTLRFGILPLV-TTPASAAQAKVVYHLMETYGFESLITYLQESEE---GPEGAANKKAFTRAIDGRETLPgaNKMTLAEI 556
Cdd:pfam18402   81 IPVRFGLVPLVnSTEDGLAQAKLFYYLLENYGLKAALSFLTASLYalaKKVLSPTKAIFSSALKERTLRP--QALSFDEV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  557 LEADTYKQRVEASKAWANRLNADTTVRPVFVNGLAIPREKSWVQAMGQRLTEDQQAIQKAVYFGQIEEGTPVSDLF--LR 634
Cdd:pfam18402  159 LKSEVYDERLKKAKEYLKRLGLDSLSGPVFVNGVPLPRDENWLQALSQRISEDLQLLQKAVYEGALTDDDDVPDFFydLP 238
                          250
                   ....*....|
gi 2124654928  635 DAISKRNTYI 644
Cdd:pfam18402  239 NALPRRNPLI 248
Thioredoxin_15 pfam18403
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose: ...
656-851 3.69e-64

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: 216.71  E-value: 3.69e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  656 DINKLHKDFVGLFGNIAVLPSDSkaPKESWAVLTAVADLATDDGQDLLLAALEFKRKNPGVRLDLVHNPPSSAEAH-VIN 734
Cdd:pfam18403    1 DLNKLYSEHADLFDKMPYLEASS--DKEDWATLWVVADLDSESGRKLLLSALEFRKSNPGVRLGIIHNPASPSEASsLIS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  735 GAFKLNEGKLAEMKNKDDLKAILEA----------SWTAEDDGLGTALADFLSASNILPGTKGLLLNGRVVGPLPSDVSF 804
Cdd:pfam18403   79 SALLAALLKLKNLDALEFLTKLLEEeeaaasesgkSSAEAAADYWKALQPFLRVLGLKPGQNALVLNGRVVGPIPEDEEF 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2124654928  805 NEDDLQQLLEFERRNRILPVYAAIKDLGFEDKLSDPIAAAKLTSITA 851
Cdd:pfam18403  159 SADDFELLLSYERSKRIEPVYKAIEELGLEDKISDPDAVAKLTSLVA 205
Thioredoxin_12 pfam18400
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in ...
36-215 7.47e-61

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: 206.32  E-value: 7.47e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928   36 PYLLELLETAAGENSTAYFPLLDKIAG--GHFQSTNSDAELYDRFLEVLQQdgHITkPEALSTYKLALSLRVAAPRIEAH 113
Cdd:pfam18400    3 PLLLEALETLAEENPDLFFPFLDALTNldGEFADASTDEELYEAALKLASD--HLS-PLALSLFKLALSLRSASPRIEAF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  114 YQYYTtavDSVSKGDTNDDCSTWALIDNKKYCS-ETLGKAVEGDFSAR-QVNLLPFDRVLGFGKD---AILYADPTSASF 188
Cdd:pfam18400   80 YQIYA---ESVSFEGAPPECDSWVDWGGEVYCDpEDLDALLKSEASSRpQPELLPFDHVYPDSGSspvAILYADLGSPNF 156
                          170       180
                   ....*....|....*....|....*..
gi 2124654928  189 GPFHIALSKAAKQGDVSYRLRYRRSAG 215
Cdd:pfam18400  157 REFHKYLSELAKDGKIRYVLRHVPPSG 183
UDP-g_GGTase pfam06427
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ...
1021-1129 1.58e-60

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: 202.33  E-value: 1.58e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1021 EGHSRDGKRGA-PRGAQLSLATEKEPLITDTIVMANLGYFQFKANPGFYNIQLKQGRTSKIFTIESVGAHGYaPVPGDEG 1099
Cdd:pfam06427    1 EGHARDVTTGSpPRGLQLVLGTEKNPHVADTIVMANLGYFQLKANPGVWKLELREGRSSDIYEIESVGAEGW-PSPGDEG 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 2124654928 1100 TEIALMDFKGTTLYPRLNRKPGMEEVDVLE 1129
Cdd:pfam06427   80 TEVALTSFEGLTLYPRLSRKPGMENEDVLE 109
Thioredoxin_13 pfam18401
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found ...
264-397 2.37e-56

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: 191.63  E-value: 2.37e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  264 EEVADLKPLSTSELASLGLKTASFILNSENPLDALVKSTQDFPKFSASIATHEVAKEFAAEQEKNVAAGIPSGINFLWMN 343
Cdd:pfam18401    1 EEVEDLKPLSVWELQDLGLQAAQFIMSSDDPLDTLLKLSQDFPKYASSLARHNVSDELREEIEENQERLLPPGDNALWLN 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2124654928  344 GVQLIERQIEPFTLIEMIRRERKLIDGVRDLGFNGQQANSLLGHSEVASSKAED 397
Cdd:pfam18401   81 GLQLDERDIDPFSLLDILRRERKLINGLRKLGLSGSEAVDLLSHPALAAAQADS 134
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1167-1383 1.07e-12

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 70.39  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1167 INIFSVASGHlYERMLNIMMVSVMRNTKHT-VKFWFIEQFLSPSFKEFIPHMAAEYGFKYEMVTYKwPHWLRQQKEKQR- 1244
Cdd:COG1442      6 INIVFAIDDN-YLPGLGVSIASLLENNPDRpYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVD-DELLKDLPVSKHi 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1245 --EIWgYKiLFLDVLFPLSLDKVIFVDADQIVRTDMIDLVNHDLEGAPYGFTPMCDSRTEMEgfrfwkqgYWANYLrGLP 1322
Cdd:COG1442     84 skATY-YR-LLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTGSQK--------KRAKRL-GLP 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1323 ----YHISALYVVDLNRFRQLAAGDRLRQqyhALSADPNSLSNLDQD-----LPNNmqftipIHSLPQEW 1383
Cdd:COG1442    153 dddgYFNSGVLLINLKKWREENITEKALE---FLKENPDKLKYPDQDilnivLGGK------VKFLPPRY 213
 
Name Accession Description Interval E-value
Glyco_transf_24 pfam18404
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ...
1167-1434 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: 630.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1167 INIFSVASGHLYERMLNIMMVSVMRNTKHTVKFWFIEQFLSPSFKEFIPHMAAEYGFKYEMVTYKWPHWLRQQKEKQREI 1246
Cdd:pfam18404    1 INIFSVASGHLYERFLKIMMLSVRKNTKSPVKFWFIENFLSPSFKAFLPHLAKEYGFEYELVTYKWPSWLRKQTEKQRII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1247 WGYKILFLDVLFPLSLDKVIFVDADQIVRTDMIDLVNHDLEGAPYGFTPMCDSRTEMEGFRFWKQGYWANYLRGLPYHIS 1326
Cdd:pfam18404   81 WGYKILFLDVLFPLDLDKVIFVDADQVVRTDLKELVDMDLEGAPYGYTPMCDSRKEMEGFRFWKQGYWKDHLRGRPYHIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1327 ALYVVDLNRFRQLAAGDRLRQQYHALSADPNSLSNLDQDLPNNMQFTIPIHSLPQEWLWCETWCSDESLAQARTIDLCNN 1406
Cdd:pfam18404  161 ALYVVDLKRFRQMAAGDRLRSHYQQLSADPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESLKKAKTIDLCNN 240
                          250       260
                   ....*....|....*....|....*...
gi 2124654928 1407 PQTKEPKLDRARRQVPEWTLYDEEIAAL 1434
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 ...
1167-1414 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: 549.68  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1167 INIFSVASGHLYERMLNIMMVSVMRNTKHTVKFWFIEQFLSPSFKEFIPHMAAEYGFKYEMVTYKWPHWLRQQKEKQREI 1246
Cdd:cd06432      1 INIFSVASGHLYERFLRIMMLSVMKNTKSPVKFWFIKNFLSPQFKEFLPEMAKEYGFEYELVTYKWPRWLHKQTEKQRII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1247 WGYKILFLDVLFPLSLDKVIFVDADQIVRTDMIDLVNHDLEGAPYGFTPMCDSRTEMEGFRFWKQGYWANYLRGLPYHIS 1326
Cdd:cd06432     81 WGYKILFLDVLFPLNVDKVIFVDADQIVRTDLKELMDMDLKGAPYGYTPFCDSRKEMDGFRFWKQGYWKSHLRGRPYHIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1327 ALYVVDLNRFRQLAAGDRLRQQYHALSADPNSLSNLDQDLPNNMQFTIPIHSLPQEWLWCETWCSDESLAQARTIDLCNN 1406
Cdd:cd06432    161 ALYVVDLKRFRRIAAGDRLRGQYQQLSQDPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESKKKAKTIDLCNN 240

                   ....*...
gi 2124654928 1407 PQTKEPKL 1414
Cdd:cd06432    241 PLTKEPKL 248
Thioredoxin_14 pfam18402
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in ...
402-644 1.35e-89

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: 291.10  E-value: 1.35e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  402 FDWTDRLEEGKALLWLNDLEKDARYQKLPSDLTALLQRTYPGQLPQVALNLFHIVAPVDFTNIEDGR-AFGQLAQFMQRG 480
Cdd:pfam18402    1 FDIRDRIEGGGVIIWLNDLEKDKRYSRWPSSLQELLRPTYPGQLPPIRKNLFNLVLVVDLSQPEDLLlLVETLQSFVQRG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  481 VTLRFGILPLV-TTPASAAQAKVVYHLMETYGFESLITYLQESEE---GPEGAANKKAFTRAIDGRETLPgaNKMTLAEI 556
Cdd:pfam18402   81 IPVRFGLVPLVnSTEDGLAQAKLFYYLLENYGLKAALSFLTASLYalaKKVLSPTKAIFSSALKERTLRP--QALSFDEV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  557 LEADTYKQRVEASKAWANRLNADTTVRPVFVNGLAIPREKSWVQAMGQRLTEDQQAIQKAVYFGQIEEGTPVSDLF--LR 634
Cdd:pfam18402  159 LKSEVYDERLKKAKEYLKRLGLDSLSGPVFVNGVPLPRDENWLQALSQRISEDLQLLQKAVYEGALTDDDDVPDFFydLP 238
                          250
                   ....*....|
gi 2124654928  635 DAISKRNTYI 644
Cdd:pfam18402  239 NALPRRNPLI 248
Thioredoxin_15 pfam18403
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose: ...
656-851 3.69e-64

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: 216.71  E-value: 3.69e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  656 DINKLHKDFVGLFGNIAVLPSDSkaPKESWAVLTAVADLATDDGQDLLLAALEFKRKNPGVRLDLVHNPPSSAEAH-VIN 734
Cdd:pfam18403    1 DLNKLYSEHADLFDKMPYLEASS--DKEDWATLWVVADLDSESGRKLLLSALEFRKSNPGVRLGIIHNPASPSEASsLIS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  735 GAFKLNEGKLAEMKNKDDLKAILEA----------SWTAEDDGLGTALADFLSASNILPGTKGLLLNGRVVGPLPSDVSF 804
Cdd:pfam18403   79 SALLAALLKLKNLDALEFLTKLLEEeeaaasesgkSSAEAAADYWKALQPFLRVLGLKPGQNALVLNGRVVGPIPEDEEF 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2124654928  805 NEDDLQQLLEFERRNRILPVYAAIKDLGFEDKLSDPIAAAKLTSITA 851
Cdd:pfam18403  159 SADDFELLLSYERSKRIEPVYKAIEELGLEDKISDPDAVAKLTSLVA 205
Thioredoxin_12 pfam18400
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in ...
36-215 7.47e-61

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: 206.32  E-value: 7.47e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928   36 PYLLELLETAAGENSTAYFPLLDKIAG--GHFQSTNSDAELYDRFLEVLQQdgHITkPEALSTYKLALSLRVAAPRIEAH 113
Cdd:pfam18400    3 PLLLEALETLAEENPDLFFPFLDALTNldGEFADASTDEELYEAALKLASD--HLS-PLALSLFKLALSLRSASPRIEAF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  114 YQYYTtavDSVSKGDTNDDCSTWALIDNKKYCS-ETLGKAVEGDFSAR-QVNLLPFDRVLGFGKD---AILYADPTSASF 188
Cdd:pfam18400   80 YQIYA---ESVSFEGAPPECDSWVDWGGEVYCDpEDLDALLKSEASSRpQPELLPFDHVYPDSGSspvAILYADLGSPNF 156
                          170       180
                   ....*....|....*....|....*..
gi 2124654928  189 GPFHIALSKAAKQGDVSYRLRYRRSAG 215
Cdd:pfam18400  157 REFHKYLSELAKDGKIRYVLRHVPPSG 183
UDP-g_GGTase pfam06427
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ...
1021-1129 1.58e-60

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: 202.33  E-value: 1.58e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1021 EGHSRDGKRGA-PRGAQLSLATEKEPLITDTIVMANLGYFQFKANPGFYNIQLKQGRTSKIFTIESVGAHGYaPVPGDEG 1099
Cdd:pfam06427    1 EGHARDVTTGSpPRGLQLVLGTEKNPHVADTIVMANLGYFQLKANPGVWKLELREGRSSDIYEIESVGAEGW-PSPGDEG 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 2124654928 1100 TEIALMDFKGTTLYPRLNRKPGMEEVDVLE 1129
Cdd:pfam06427   80 TEVALTSFEGLTLYPRLSRKPGMENEDVLE 109
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
1167-1414 4.14e-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: 203.83  E-value: 4.14e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1167 INIFSVASGHLYERMLNIMMVSVMRNTKHTVKFWFIEQFLSPSFKEFIPHMAAEYGFKYEMVTYKWPHWLRQQ-KEKQRE 1245
Cdd:cd00505      1 IAIVIVATGDEYLRGAIVLMKSVLRHRTKPLRFHVLTNPLSDTFKAALDNLRKLYNFNYELIPVDILDSVDSEhLKRPIK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1246 IWGYKILFLDVLFPlSLDKVIFVDADQIVRTDMIDLVNHDLEGAPYGFTPMCDSRTEMEGFRFWKQGYWANYlrglpYHI 1325
Cdd:cd00505     81 IVTLTKLHLPNLVP-DYDKILYVDADILVLTDIDELWDTPLGGQELAAAPDPGDRREGKYYRQKRSHLAGPD-----YFN 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1326 SALYVVDLNRFRQL-AAGDRLRQQYHALSadpnSLSNLDQDLPNNM--QFTIPIHSLPQEWLWCETWCSDESLAQ----- 1397
Cdd:cd00505    155 SGVFVVNLSKERRNqLLKVALEKWLQSLS----SLSGGDQDLLNTFfkQVPFIVKSLPCIWNVRLTGCYRSLNCFkafvk 230
                          250
                   ....*....|....*...
gi 2124654928 1398 -ARTIDLCNNpqTKEPKL 1414
Cdd:cd00505    231 nAKVIHFNGP--TKPWNK 246
Thioredoxin_13 pfam18401
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found ...
264-397 2.37e-56

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: 191.63  E-value: 2.37e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928  264 EEVADLKPLSTSELASLGLKTASFILNSENPLDALVKSTQDFPKFSASIATHEVAKEFAAEQEKNVAAGIPSGINFLWMN 343
Cdd:pfam18401    1 EEVEDLKPLSVWELQDLGLQAAQFIMSSDDPLDTLLKLSQDFPKYASSLARHNVSDELREEIEENQERLLPPGDNALWLN 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2124654928  344 GVQLIERQIEPFTLIEMIRRERKLIDGVRDLGFNGQQANSLLGHSEVASSKAED 397
Cdd:pfam18401   81 GLQLDERDIDPFSLLDILRRERKLINGLRKLGLSGSEAVDLLSHPALAAAQADS 134
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1167-1383 1.07e-12

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 70.39  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1167 INIFSVASGHlYERMLNIMMVSVMRNTKHT-VKFWFIEQFLSPSFKEFIPHMAAEYGFKYEMVTYKwPHWLRQQKEKQR- 1244
Cdd:COG1442      6 INIVFAIDDN-YLPGLGVSIASLLENNPDRpYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVD-DELLKDLPVSKHi 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1245 --EIWgYKiLFLDVLFPLSLDKVIFVDADQIVRTDMIDLVNHDLEGAPYGFTPMCDSRTEMEgfrfwkqgYWANYLrGLP 1322
Cdd:COG1442     84 skATY-YR-LLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTGSQK--------KRAKRL-GLP 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1323 ----YHISALYVVDLNRFRQLAAGDRLRQqyhALSADPNSLSNLDQD-----LPNNmqftipIHSLPQEW 1383
Cdd:COG1442    153 dddgYFNSGVLLINLKKWREENITEKALE---FLKENPDKLKYPDQDilnivLGGK------VKFLPPRY 213
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
1167-1383 2.17e-08

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: 56.84  E-value: 2.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1167 INIFSVASGHlYERMLNIMMVSVMRNTKHT-VKFWFIEQFLSPSFKEFIPHMAAEYGFKYEMVTYKwphwLRQQKEKQRE 1245
Cdd:cd04194      1 MNIVFAIDDN-YAPYLAVTIKSILANNSKRdYDFYILNDDISEENKKKLKELLKKYNSSIEFIKID----NDDFKFFPAT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124654928 1246 IWGYKI-----LFLDVLFPlSLDKVIFVDADQIVRTDMIDLVNHDLEGAPYGftpMCdsrTEMEGFRFWKQGYWANYLRG 1320
Cdd:cd04194     76 TDHISYatyyrLLIPDLLP-DYDKVLYLDADIIVLGDLSELFDIDLGDNLLA---AV---RDPFIEQEKKRKRRLGGYDD 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124654928 1321 LPYHISALYVVDLNRFRQLAAGDRLRQqyhALSADPNSLSNLDQD-LpnNMQFTIPIHSLPQEW 1383
Cdd:cd04194    149 GSYFNSGVLLINLKKWREENITEKLLE---LIKEYGGRLIYPDQDiL--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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