NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|38197418|gb|AAH61762|]
View 

Glycosyltransferase-like 1B [Rattus norvegicus]

Protein Classification

LARGE family glycosyltransferase; glycosyltransferase family 8 protein( domain architecture ID 10157681)

LARGE family glycosyltransferase is a bifunctional glycosyltransferase containing N-terminal family 8 and C-terminal family 49 glycosyltransferase domains, similar to LARGE xylosyl- and glucuronyltransferase proteins, which exhibit both alpha-1,3-xylosyltransferase and beta-1,3-glucuronyltransferase activities and are involved in the maturation of alpha-dystroglycan| glycosyltransferase family 8 protein containing a class I SAM-dependent methyltransferase domain, catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds, and possibly the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
GT8_LARGE_C cd06431
LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in ...
67-346 2.44e-171

LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis; The catalytic domain of LARGE is a putative glycosyltransferase. Mutations of LARGE in mouse and human cause dystroglycanopathies, a disease associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. LARGE needs to both physically interact with alpha-dystroglycan and function as a glycosyltransferase in order to stimulate alpha-dystroglycan hyperglycosylation. LARGE localizes to the Golgi apparatus and contains three conserved DxD motifs. While two of the motifs are indispensible for glycosylation function, one is important for localization of th eenzyme. LARGE was originally named because it covers approximately large trunck of genomic DNA, more than 600bp long. The predicted protein structure contains an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif, and two putative catalytic domains. This catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis.


:

Pssm-ID: 133053  Cd Length: 280  Bit Score: 490.83  E-value: 2.44e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418  67 LHVAIVCAGYNSSREIITLMKSVLFYRKNPLHLHLITDAVARNILETLFRTWMVPAVVVSFYDAEELKPLVSWIPNKHYS 146
Cdd:cd06431   1 IHVAIVCAGYNASRDVVTLVKSVLFYRRNPLHFHLITDEIARRILATLFQTWMVPAVEVSFYNAEELKSRVSWIPNKHYS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 147 GLYGLMKLVLPSVLPLSLARVIVLDTDVTFSSDIMELWALFGHFSDKQVVGLVENQSDWYLGNLWKNHRPWPALGRGFNT 226
Cdd:cd06431  81 GIYGLMKLVLTEALPSDLEKVIVLDTDITFATDIAELWKIFHKFTGQQVLGLVENQSDWYLGNLWKNHRPWPALGRGFNT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 227 GVILLWLDRLQQIGWEQMWKLTAKRELLTLTATSLADQDIFNAVIKEHPELVHPLPCVWNVQLSDHTLAERCYLEAADLK 306
Cdd:cd06431 161 GVILLDLDKLRKMKWESMWRLTAERELMSMLSTSLADQDIFNAVIKQNPFLVYQLPCAWNVQLSDHTRSEQCYRDVSDLK 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 38197418 307 VIHWNSPKKLRVKNKHAEFFRDLHLTFLGFDGKLLCRELF 346
Cdd:cd06431 241 VIHWNSPKKLRVKNKHVEFFRNLYLTFLEYDGNLLRRELF 280
Glyco_transf_49 super family cl16461
Glycosyl-transferase for dystroglycan; This glycosyl-transferase brings about the ...
401-635 5.79e-51

Glycosyl-transferase for dystroglycan; This glycosyl-transferase brings about the glycosylation of the alpha-dystroglycan subunit. Dystroglycan is an integral member of the skeletal muscular dystrophin glycoprotein complex, which links dystrophin to proteins in the extracellular matrix.


The actual alignment was detected with superfamily member pfam13896:

Pssm-ID: 464027  Cd Length: 327  Bit Score: 180.14  E-value: 5.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418   401 DVTLVAQLSMDRLQMLEALCRHWRGPMSLALYLTDAEAQQFLRFVE------TSPVLSARkdVAYHVVYR---------- 464
Cdd:pfam13896   1 DVTLATHGTVDFLDNLEPLVERWRGPISVAVFAPGTDFSLALDYIAylrrcfPSELVREN--VTFHLVFPsehmppkqvt 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418   465 -------------------------------DGPLYPVNQLRNVALAQALTPYVFLSDIDFLPAYSLYDYLRASIEQLA- 512
Cdd:pfam13896  79 cpsallsssndcsellsplrklvppganyaaQNLLYPINLLRNVARKGAQTHFVLVIDIDLYPSPGLAEKFLEFLARNKk 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418   513 LGRRQRKAALVVPAFETLHYRfSFPNSKAELLTLLDAGSLHTFrYHEW-PQGHASTDYTRWREAQAP---------YRV- 581
Cdd:pfam13896 159 LLNRTSPCVFVVPAFEVDANA-TVPRTKAELLRLLKNGEARPF-HHKVcPKCHKPTNYDRWLNLSKNsdglnlfvaYKVt 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 38197418   582 QWSADYEPYVVVPRDCPRYDPRFVGFGWNKVAHIIELDAQEYEFLVLPEAFSIH 635
Cdd:pfam13896 237 YWQDPWEPFYIGTRNDPLYDERFTWYGFDRISQVYELCVAGYEFHVLDNAFLVH 290
 
Name Accession Description Interval E-value
GT8_LARGE_C cd06431
LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in ...
67-346 2.44e-171

LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis; The catalytic domain of LARGE is a putative glycosyltransferase. Mutations of LARGE in mouse and human cause dystroglycanopathies, a disease associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. LARGE needs to both physically interact with alpha-dystroglycan and function as a glycosyltransferase in order to stimulate alpha-dystroglycan hyperglycosylation. LARGE localizes to the Golgi apparatus and contains three conserved DxD motifs. While two of the motifs are indispensible for glycosylation function, one is important for localization of th eenzyme. LARGE was originally named because it covers approximately large trunck of genomic DNA, more than 600bp long. The predicted protein structure contains an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif, and two putative catalytic domains. This catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis.


Pssm-ID: 133053  Cd Length: 280  Bit Score: 490.83  E-value: 2.44e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418  67 LHVAIVCAGYNSSREIITLMKSVLFYRKNPLHLHLITDAVARNILETLFRTWMVPAVVVSFYDAEELKPLVSWIPNKHYS 146
Cdd:cd06431   1 IHVAIVCAGYNASRDVVTLVKSVLFYRRNPLHFHLITDEIARRILATLFQTWMVPAVEVSFYNAEELKSRVSWIPNKHYS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 147 GLYGLMKLVLPSVLPLSLARVIVLDTDVTFSSDIMELWALFGHFSDKQVVGLVENQSDWYLGNLWKNHRPWPALGRGFNT 226
Cdd:cd06431  81 GIYGLMKLVLTEALPSDLEKVIVLDTDITFATDIAELWKIFHKFTGQQVLGLVENQSDWYLGNLWKNHRPWPALGRGFNT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 227 GVILLWLDRLQQIGWEQMWKLTAKRELLTLTATSLADQDIFNAVIKEHPELVHPLPCVWNVQLSDHTLAERCYLEAADLK 306
Cdd:cd06431 161 GVILLDLDKLRKMKWESMWRLTAERELMSMLSTSLADQDIFNAVIKQNPFLVYQLPCAWNVQLSDHTRSEQCYRDVSDLK 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 38197418 307 VIHWNSPKKLRVKNKHAEFFRDLHLTFLGFDGKLLCRELF 346
Cdd:cd06431 241 VIHWNSPKKLRVKNKHVEFFRNLYLTFLEYDGNLLRRELF 280
Glyco_transf_49 pfam13896
Glycosyl-transferase for dystroglycan; This glycosyl-transferase brings about the ...
401-635 5.79e-51

Glycosyl-transferase for dystroglycan; This glycosyl-transferase brings about the glycosylation of the alpha-dystroglycan subunit. Dystroglycan is an integral member of the skeletal muscular dystrophin glycoprotein complex, which links dystrophin to proteins in the extracellular matrix.


Pssm-ID: 464027  Cd Length: 327  Bit Score: 180.14  E-value: 5.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418   401 DVTLVAQLSMDRLQMLEALCRHWRGPMSLALYLTDAEAQQFLRFVE------TSPVLSARkdVAYHVVYR---------- 464
Cdd:pfam13896   1 DVTLATHGTVDFLDNLEPLVERWRGPISVAVFAPGTDFSLALDYIAylrrcfPSELVREN--VTFHLVFPsehmppkqvt 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418   465 -------------------------------DGPLYPVNQLRNVALAQALTPYVFLSDIDFLPAYSLYDYLRASIEQLA- 512
Cdd:pfam13896  79 cpsallsssndcsellsplrklvppganyaaQNLLYPINLLRNVARKGAQTHFVLVIDIDLYPSPGLAEKFLEFLARNKk 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418   513 LGRRQRKAALVVPAFETLHYRfSFPNSKAELLTLLDAGSLHTFrYHEW-PQGHASTDYTRWREAQAP---------YRV- 581
Cdd:pfam13896 159 LLNRTSPCVFVVPAFEVDANA-TVPRTKAELLRLLKNGEARPF-HHKVcPKCHKPTNYDRWLNLSKNsdglnlfvaYKVt 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 38197418   582 QWSADYEPYVVVPRDCPRYDPRFVGFGWNKVAHIIELDAQEYEFLVLPEAFSIH 635
Cdd:pfam13896 237 YWQDPWEPFYIGTRNDPLYDERFTWYGFDRISQVYELCVAGYEFHVLDNAFLVH 290
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
84-315 2.52e-17

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 83.10  E-value: 2.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418  84 TLMKSVLFYRKN-PLHLHLITDAVARNILETLFRTWMVPAVVVSFY--DAEELKPLVSwipNKHYSgLYGLMKLVLPSVL 160
Cdd:COG1442  22 VSIASLLENNPDrPYDFHILTDGLSDENKERLEALAAKYNVSIEFIdvDDELLKDLPV---SKHIS-KATYYRLLIPELL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 161 PLSLARVIVLDTDVTFSSDIMELWALfgHFSDKqVVGLVENQSDWYLGNLWKNHRPWPALGRGFNTGVILLWLDRLQQIG 240
Cdd:COG1442  98 PDDYDKVLYLDADTLVLGDLSELWDI--DLGGN-LLAAVRDGTVTGSQKKRAKRLGLPDDDGYFNSGVLLINLKKWREEN 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 241 WEQ--MWKLTAKRELLTltatsLADQDIFNAVIKEHpelVHPLPCVWNVQ------LSDHTLAERCYLEAADLKVIHWNS 312
Cdd:COG1442 175 ITEkaLEFLKENPDKLK-----YPDQDILNIVLGGK---VKFLPPRYNYQyslyyeLKDKSNKKELLEARKNPVIIHYTG 246

                ...
gi 38197418 313 PKK 315
Cdd:COG1442 247 PTK 249
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
83-315 6.92e-16

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: 77.75  E-value: 6.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418    83 ITLMKSVLFYRKNP-LHLHLITDAV---ARNILETLFRTWMVPAVVVSFYDAEELKPLVSWIPNKHYSGLYGLMKLVLPS 158
Cdd:pfam01501  15 SVSIKSLLKNNSDFaLNFHIFTDDIpveNLDILNWLASSYKPVLPLLESDIKIFEYFSKLKLRSPKYWSLLNYLRLYLPD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418   159 VLPlSLARVIVLDTDVTFSSDIMELWALfgHFSDKqVVGLVENQSDWYlgNLWKNHRPWPALG----RGFNTGVILLWLD 234
Cdd:pfam01501  95 LFP-KLDKILYLDADIVVQGDLSPLWDI--DLGGK-VLAAVEDNYFQR--YPNFSEPIILENFgppaCYFNAGMLLFDLD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418   235 RlqqigWEQMwKLTAK-----RELLTLTATSLADQDIFNAVIKEHpelVHPLPCVWNVQLSDHTLAERCYLEA-ADLKVI 308
Cdd:pfam01501 169 A-----WRKE-NITERyikwlNLNENRTLWKLGDQDPLNIVFYGK---VKPLDPRWNVLGLGYYNKKKSLNEItENAAVI 239

                  ....*..
gi 38197418   309 HWNSPKK 315
Cdd:pfam01501 240 HYNGPTK 246
 
Name Accession Description Interval E-value
GT8_LARGE_C cd06431
LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in ...
67-346 2.44e-171

LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis; The catalytic domain of LARGE is a putative glycosyltransferase. Mutations of LARGE in mouse and human cause dystroglycanopathies, a disease associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. LARGE needs to both physically interact with alpha-dystroglycan and function as a glycosyltransferase in order to stimulate alpha-dystroglycan hyperglycosylation. LARGE localizes to the Golgi apparatus and contains three conserved DxD motifs. While two of the motifs are indispensible for glycosylation function, one is important for localization of th eenzyme. LARGE was originally named because it covers approximately large trunck of genomic DNA, more than 600bp long. The predicted protein structure contains an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif, and two putative catalytic domains. This catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis.


Pssm-ID: 133053  Cd Length: 280  Bit Score: 490.83  E-value: 2.44e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418  67 LHVAIVCAGYNSSREIITLMKSVLFYRKNPLHLHLITDAVARNILETLFRTWMVPAVVVSFYDAEELKPLVSWIPNKHYS 146
Cdd:cd06431   1 IHVAIVCAGYNASRDVVTLVKSVLFYRRNPLHFHLITDEIARRILATLFQTWMVPAVEVSFYNAEELKSRVSWIPNKHYS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 147 GLYGLMKLVLPSVLPLSLARVIVLDTDVTFSSDIMELWALFGHFSDKQVVGLVENQSDWYLGNLWKNHRPWPALGRGFNT 226
Cdd:cd06431  81 GIYGLMKLVLTEALPSDLEKVIVLDTDITFATDIAELWKIFHKFTGQQVLGLVENQSDWYLGNLWKNHRPWPALGRGFNT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 227 GVILLWLDRLQQIGWEQMWKLTAKRELLTLTATSLADQDIFNAVIKEHPELVHPLPCVWNVQLSDHTLAERCYLEAADLK 306
Cdd:cd06431 161 GVILLDLDKLRKMKWESMWRLTAERELMSMLSTSLADQDIFNAVIKQNPFLVYQLPCAWNVQLSDHTRSEQCYRDVSDLK 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 38197418 307 VIHWNSPKKLRVKNKHAEFFRDLHLTFLGFDGKLLCRELF 346
Cdd:cd06431 241 VIHWNSPKKLRVKNKHVEFFRNLYLTFLEYDGNLLRRELF 280
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
67-319 8.75e-70

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: 227.71  E-value: 8.75e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418  67 LHVAIVCAGYNSSREIITLMKSVLFYRKNPLHLHLITDAVARNILETLFRTWMVPAVVVSFYDAEELKPLVSWiPNKHYS 146
Cdd:cd00505   1 IAIVIVATGDEYLRGAIVLMKSVLRHRTKPLRFHVLTNPLSDTFKAALDNLRKLYNFNYELIPVDILDSVDSE-HLKRPI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 147 GLYGLMKLVLPSVLPlSLARVIVLDTDVTFSSDIMELWALfghFSDKQVVGLVENQSDWYLGNLWKNHRPWPALGRGFNT 226
Cdd:cd00505  80 KIVTLTKLHLPNLVP-DYDKILYVDADILVLTDIDELWDT---PLGGQELAAAPDPGDRREGKYYRQKRSHLAGPDYFNS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 227 GVILLWLDRLQqigWEQMWKLTAKRELLTLTATSLADQDIFNAVIKEHPELVHPLPCVWNVQLSDHTLAERC-YLEAADL 305
Cdd:cd00505 156 GVFVVNLSKER---RNQLLKVALEKWLQSLSSLSGGDQDLLNTFFKQVPFIVKSLPCIWNVRLTGCYRSLNCfKAFVKNA 232
                       250
                ....*....|....
gi 38197418 306 KVIHWNSPKKLRVK 319
Cdd:cd00505 233 KVIHFNGPTKPWNK 246
Glyco_transf_49 pfam13896
Glycosyl-transferase for dystroglycan; This glycosyl-transferase brings about the ...
401-635 5.79e-51

Glycosyl-transferase for dystroglycan; This glycosyl-transferase brings about the glycosylation of the alpha-dystroglycan subunit. Dystroglycan is an integral member of the skeletal muscular dystrophin glycoprotein complex, which links dystrophin to proteins in the extracellular matrix.


Pssm-ID: 464027  Cd Length: 327  Bit Score: 180.14  E-value: 5.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418   401 DVTLVAQLSMDRLQMLEALCRHWRGPMSLALYLTDAEAQQFLRFVE------TSPVLSARkdVAYHVVYR---------- 464
Cdd:pfam13896   1 DVTLATHGTVDFLDNLEPLVERWRGPISVAVFAPGTDFSLALDYIAylrrcfPSELVREN--VTFHLVFPsehmppkqvt 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418   465 -------------------------------DGPLYPVNQLRNVALAQALTPYVFLSDIDFLPAYSLYDYLRASIEQLA- 512
Cdd:pfam13896  79 cpsallsssndcsellsplrklvppganyaaQNLLYPINLLRNVARKGAQTHFVLVIDIDLYPSPGLAEKFLEFLARNKk 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418   513 LGRRQRKAALVVPAFETLHYRfSFPNSKAELLTLLDAGSLHTFrYHEW-PQGHASTDYTRWREAQAP---------YRV- 581
Cdd:pfam13896 159 LLNRTSPCVFVVPAFEVDANA-TVPRTKAELLRLLKNGEARPF-HHKVcPKCHKPTNYDRWLNLSKNsdglnlfvaYKVt 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 38197418   582 QWSADYEPYVVVPRDCPRYDPRFVGFGWNKVAHIIELDAQEYEFLVLPEAFSIH 635
Cdd:pfam13896 237 YWQDPWEPFYIGTRNDPLYDERFTWYGFDRISQVYELCVAGYEFHVLDNAFLVH 290
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
84-315 2.52e-17

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 83.10  E-value: 2.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418  84 TLMKSVLFYRKN-PLHLHLITDAVARNILETLFRTWMVPAVVVSFY--DAEELKPLVSwipNKHYSgLYGLMKLVLPSVL 160
Cdd:COG1442  22 VSIASLLENNPDrPYDFHILTDGLSDENKERLEALAAKYNVSIEFIdvDDELLKDLPV---SKHIS-KATYYRLLIPELL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 161 PLSLARVIVLDTDVTFSSDIMELWALfgHFSDKqVVGLVENQSDWYLGNLWKNHRPWPALGRGFNTGVILLWLDRLQQIG 240
Cdd:COG1442  98 PDDYDKVLYLDADTLVLGDLSELWDI--DLGGN-LLAAVRDGTVTGSQKKRAKRLGLPDDDGYFNSGVLLINLKKWREEN 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 241 WEQ--MWKLTAKRELLTltatsLADQDIFNAVIKEHpelVHPLPCVWNVQ------LSDHTLAERCYLEAADLKVIHWNS 312
Cdd:COG1442 175 ITEkaLEFLKENPDKLK-----YPDQDILNIVLGGK---VKFLPPRYNYQyslyyeLKDKSNKKELLEARKNPVIIHYTG 246

                ...
gi 38197418 313 PKK 315
Cdd:COG1442 247 PTK 249
GT8_like_2 cd06430
GT8_like_2 represents a subfamily of GT8 with unknown function; A subfamily of ...
67-311 2.53e-16

GT8_like_2 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: 133052  Cd Length: 304  Bit Score: 80.20  E-value: 2.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418  67 LHVAIVCAGyNSSREIITLMKSVLFYRKNPLHLHLIT-DAVARNILETLfRTWmvPAVVVSFYDAEeLKPLVswIPNKHY 145
Cdd:cd06430   1 MHLAVVACG-ERLEETLTMLKSAIVFSQKPLRFHIFAeDQLKQSFKEKL-DDW--PELIDRKFNYT-LHPIT--FPSGNA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 146 SGLYGLMK------LVLPSVLPlSLARVIVLDTDVTFSSDIMELWALFGHFSDKQVVGLVENQSDWYLGnlWKNHRPW-P 218
Cdd:cd06430  74 AEWKKLFKpcaaqrLFLPSLLP-DVDSLLYVDTDILFLRPVEEIWSFLKKFNSTQLAAMAPEHEEPNIG--WYNRFARhP 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 219 ALGR-GFNTGVILLWLDRLQQ-----------IGWEQMWKLTAKRELLTLTatsLADQDIFNAVIKEHPELVHPLPCVWN 286
Cdd:cd06430 151 YYGKtGVNSGVMLMNLTRMRRkyfkndmtpvgLRWEEILMPLYKKYKLKIT---WGDQDLINIIFHHNPEMLYVFPCHWN 227
                       250       260
                ....*....|....*....|....*..
gi 38197418 287 VQlSDHTLAERCYLEAAD--LKVIHWN 311
Cdd:cd06430 228 YR-PDHCMYGSNCKAAEEegVFILHGN 253
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
83-315 6.92e-16

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: 77.75  E-value: 6.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418    83 ITLMKSVLFYRKNP-LHLHLITDAV---ARNILETLFRTWMVPAVVVSFYDAEELKPLVSWIPNKHYSGLYGLMKLVLPS 158
Cdd:pfam01501  15 SVSIKSLLKNNSDFaLNFHIFTDDIpveNLDILNWLASSYKPVLPLLESDIKIFEYFSKLKLRSPKYWSLLNYLRLYLPD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418   159 VLPlSLARVIVLDTDVTFSSDIMELWALfgHFSDKqVVGLVENQSDWYlgNLWKNHRPWPALG----RGFNTGVILLWLD 234
Cdd:pfam01501  95 LFP-KLDKILYLDADIVVQGDLSPLWDI--DLGGK-VLAAVEDNYFQR--YPNFSEPIILENFgppaCYFNAGMLLFDLD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418   235 RlqqigWEQMwKLTAK-----RELLTLTATSLADQDIFNAVIKEHpelVHPLPCVWNVQLSDHTLAERCYLEA-ADLKVI 308
Cdd:pfam01501 169 A-----WRKE-NITERyikwlNLNENRTLWKLGDQDPLNIVFYGK---VKPLDPRWNVLGLGYYNKKKSLNEItENAAVI 239

                  ....*..
gi 38197418   309 HWNSPKK 315
Cdd:pfam01501 240 HYNGPTK 246
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
84-315 1.12e-14

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: 74.17  E-value: 1.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418  84 TLMKSVLFY-RKNPLHLHLITDAVA---RNILETLFRTWMVpAVVVSFYDAEELKPLvsWIPNKHYSgLYGLMKLVLPSV 159
Cdd:cd04194  17 VTIKSILANnSKRDYDFYILNDDISeenKKKLKELLKKYNS-SIEFIKIDNDDFKFF--PATTDHIS-YATYYRLLIPDL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 160 LPlSLARVIVLDTDVTFSSDIMELWALfgHFSDKQVVGLVENQSDWYLGNLWKNHRpwPALGRGFNTGVILLWLDRlqqi 239
Cdd:cd04194  93 LP-DYDKVLYLDADIIVLGDLSELFDI--DLGDNLLAAVRDPFIEQEKKRKRRLGG--YDDGSYFNSGVLLINLKK---- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 240 gWEQMwKLTAKreLLTLTAT-----SLADQDIFNAVIKEHpelVHPLPCVWNVQLSDHTL-----AERCYLEAA--DLKV 307
Cdd:cd04194 164 -WREE-NITEK--LLELIKEyggrlIYPDQDILNAVLKDK---ILYLPPRYNFQTGFYYLlkkksKEEQELEEArkNPVI 236

                ....*...
gi 38197418 308 IHWNSPKK 315
Cdd:cd04194 237 IHYTGSDK 244
GT8_like_1 cd06429
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ...
142-315 6.40e-05

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: 45.07  E-value: 6.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 142 NKHYSGLYGLMKLVLPSVLPlSLARVIVLDTDVTFSSDIMELWALfgHFSDKqVVGLVEnqSDWYLGNLWKNHRPWpalg 221
Cdd:cd06429  93 KPEYISLLNFARFYLPELFP-KLEKVIYLDDDVVVQKDLTELWNT--DLGGG-VAGAVE--TSWNPGVNVVNLTEW---- 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197418 222 RGFN-TGVILLWLDRLQQIGWEqMWKltakreLLTLTATSLADQDifnavikehpeLVHPLPCVWNVQ-LSDHTLAERCY 299
Cdd:cd06429 163 RRQNvTETYEKWMELNQEEEVT-LWK------LITLPPGLIVFYG-----------LTSPLDPSWHVRgLGYNYGIRPQD 224
                       170
                ....*....|....*.
gi 38197418 300 LEAAdlKVIHWNSPKK 315
Cdd:cd06429 225 IKAA--AVLHFNGNMK 238
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH